Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
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|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O14733
|
MP2K7_HUMAN
|
MAASSLEQKLSRLEAKLKQENREARRRIDLNLDISPQRPRPTLQLPLANDGGSRSPSSESSPQHPTPPARPRHMLGLPSTLFTPRSMESIEIDQKLQEIMKQTGYLTIGGQRYQAEINDLENLGEMGSGTCGQVWKMRFRKTGHVIAVKQMRRSGNKEENKRILMDLDVVLKSHDCPYIVQCFGTFITNTDVFIAMELMGTCAEKLKKRMQGPIPERILGKMTVAIVKALYYLKEKHGVIHRDVKPSNILLDERGQIKLCDFGISGRLVDSKAKTRSAGCAAYMAPERIDPPDPTKPDYDIRADVWSLGISLVELATGQFPYKNCKTDFEVLTKVLQEEPPLLPGHMGFSGDFQSFVKDCLTKDHRKRPKYNKLLEHSFIKRYETLEVDVASWFKDVMAKTESPRTSGVLSQPHLPFFR
|
2.7.12.2
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
|
apoptotic process [GO:0006915]; cellular response to interleukin-1 [GO:0071347]; cellular response to lipopolysaccharide [GO:0071222]; cellular senescence [GO:0090398]; Fc-epsilon receptor signaling pathway [GO:0038095]; JNK cascade [GO:0007254]; phosphorylation [GO:0016310]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of JNK cascade [GO:0046330]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of telomerase activity [GO:0051973]; positive regulation of telomere capping [GO:1904355]; positive regulation of telomere maintenance via telomerase [GO:0032212]; regulation of motor neuron apoptotic process [GO:2000671]; response to heat [GO:0009408]; response to osmotic stress [GO:0006970]; response to tumor necrosis factor [GO:0034612]; response to UV [GO:0009411]; response to wounding [GO:0009611]; signal transduction [GO:0007165]; stress-activated MAPK cascade [GO:0051403]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; enzyme binding [GO:0019899]; JUN kinase kinase activity [GO:0008545]; magnesium ion binding [GO:0000287]; MAP kinase activity [GO:0004707]; MAP kinase kinase activity [GO:0004708]; molecular function activator activity [GO:0140677]; protein kinase binding [GO:0019901]; protein phosphatase binding [GO:0019903]; protein serine kinase activity [GO:0106310]; protein tyrosine kinase activity [GO:0004713]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase subfamily
|
PTM: Activated by phosphorylation on Ser-271 and Thr-275 by MAP kinase kinase kinases (MAP3Ks). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.2; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.12.2; CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2;
| null | null | null | null |
FUNCTION: Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Essential component of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. With MAP2K4/MKK4, is the one of the only known kinase to directly activate the stress-activated protein kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation, but they differ in their preference for the phosphorylation site in the Thr-Pro-Tyr motif. MAP2K4/MKK4 shows preference for phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr residue. The monophosphorylation of JNKs on the Thr residue is sufficient to increase JNK activity indicating that MAP2K7/MKK7 is important to trigger JNK activity, while the additional phosphorylation of the Tyr residue by MAP2K4/MKK4 ensures optimal JNK activation. Has a specific role in JNK signal transduction pathway activated by pro-inflammatory cytokines. The MKK/JNK signaling pathway is also involved in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis. Part of a non-canonical MAPK signaling pathway, composed of the upstream MAP3K12 kinase and downstream MAP kinases MAPK1/ERK2 and MAPK3/ERK1, that enhances the AP-1-mediated transcription of APP in response to APOE (PubMed:28111074). {ECO:0000269|PubMed:28111074, ECO:0000269|PubMed:9312068, ECO:0000269|PubMed:9372971, ECO:0000269|PubMed:9535930, ECO:0000269|Ref.5}.
|
Homo sapiens (Human)
|
O14734
|
ACOT8_HUMAN
|
MSSPQAPEDGQGCGDRGDPPGDLRSVLVTTVLNLEPLDEDLFRGRHYWVPAKRLFGGQIVGQALVAAAKSVSEDVHVHSLHCYFVRAGDPKLPVLYQVERTRTGSSFSVRSVKAVQHGKPIFICQASFQQAQPSPMQHQFSMPTVPPPEELLDCETLIDQYLRDPNLQKRYPLALNRIAAQEVPIEIKPVNPSPLSQLQRMEPKQMFWVRARGYIGEGDMKMHCCVAAYISDYAFLGTALLPHQWQHKVHFMVSLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAVTCAQEGVIRVKPQVSESKL
|
3.1.2.1; 3.1.2.11; 3.1.2.2; 3.1.2.27; 3.1.2.3; 3.1.2.5
| null |
acyl-CoA metabolic process [GO:0006637]; alpha-linolenic acid metabolic process [GO:0036109]; bile acid biosynthetic process [GO:0006699]; dicarboxylic acid catabolic process [GO:0043649]; fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; fatty acid catabolic process [GO:0009062]; negative regulation of CD4 production [GO:0045225]; peroxisome fission [GO:0016559]
|
cytosol [GO:0005829]; peroxisomal matrix [GO:0005782]
|
acetoacetyl-CoA hydrolase activity [GO:0047603]; acetyl-CoA hydrolase activity [GO:0003986]; acyl-CoA hydrolase activity [GO:0016289]; carboxylic ester hydrolase activity [GO:0052689]; choloyl-CoA hydrolase activity [GO:0033882]; fatty acyl-CoA hydrolase activity [GO:0047617]; hydroxymethylglutaryl-CoA hydrolase activity [GO:0047994]; long-chain fatty acyl-CoA hydrolase activity [GO:0052816]; medium-chain fatty acyl-CoA hydrolase activity [GO:0052815]; succinyl-CoA hydrolase activity [GO:0004778]
|
PF13622;PF02551;
|
2.40.160.210;
|
C/M/P thioester hydrolase family
| null |
SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:10092594, ECO:0000269|PubMed:15194431}. Note=Predominantly localized in the peroxisome but a localization to the cytosol cannot be excluded. {ECO:0000269|PubMed:10092594, ECO:0000269|PubMed:15194431}.
|
CATALYTIC ACTIVITY: Reaction=choloyl-CoA + H2O = cholate + CoA + H(+); Xref=Rhea:RHEA:14541, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29747, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373; EC=3.1.2.27; Evidence={ECO:0000250|UniProtKB:P58137}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14542; Evidence={ECO:0000250|UniProtKB:P58137}; CATALYTIC ACTIVITY: Reaction=chenodeoxycholoyl-CoA + H2O = chenodeoxycholate + CoA + H(+); Xref=Rhea:RHEA:31511, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:36234, ChEBI:CHEBI:57287, ChEBI:CHEBI:62989; EC=3.1.2.27; Evidence={ECO:0000250|UniProtKB:P58137}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31512; Evidence={ECO:0000250|UniProtKB:P58137}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O = acetate + CoA + H(+); Xref=Rhea:RHEA:20289, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=3.1.2.1; Evidence={ECO:0000269|PubMed:10944470, ECO:0000269|PubMed:9299485}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20290; Evidence={ECO:0000305|PubMed:9299485}; CATALYTIC ACTIVITY: Reaction=butanoyl-CoA + H2O = butanoate + CoA + H(+); Xref=Rhea:RHEA:40111, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371; Evidence={ECO:0000269|PubMed:10944470, ECO:0000269|PubMed:9299485}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40112; Evidence={ECO:0000305|PubMed:9299485}; CATALYTIC ACTIVITY: Reaction=2-methylpropanoyl-CoA + H2O = 2-methylpropanoate + CoA + H(+); Xref=Rhea:RHEA:40799, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:48944, ChEBI:CHEBI:57287, ChEBI:CHEBI:57338; Evidence={ECO:0000269|PubMed:10944470}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40800; Evidence={ECO:0000305|PubMed:10944470}; CATALYTIC ACTIVITY: Reaction=H2O + hexanoyl-CoA = CoA + H(+) + hexanoate; Xref=Rhea:RHEA:40115, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620; Evidence={ECO:0000269|PubMed:9153233}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40116; Evidence={ECO:0000305|PubMed:9153233}; CATALYTIC ACTIVITY: Reaction=H2O + octanoyl-CoA = CoA + H(+) + octanoate; Xref=Rhea:RHEA:30143, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386; Evidence={ECO:0000269|PubMed:10944470, ECO:0000269|PubMed:9153233, ECO:0000269|PubMed:9299485}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30144; Evidence={ECO:0000305|PubMed:9299485}; CATALYTIC ACTIVITY: Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+); Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430; Evidence={ECO:0000269|PubMed:10944470, ECO:0000269|PubMed:9153233, ECO:0000269|PubMed:9299485}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060; Evidence={ECO:0000305|PubMed:9299485}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+); Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375; Evidence={ECO:0000269|PubMed:9153233}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136; Evidence={ECO:0000305|PubMed:9153233}; CATALYTIC ACTIVITY: Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate; Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385; Evidence={ECO:0000269|PubMed:10944470, ECO:0000269|PubMed:9153233, ECO:0000269|PubMed:9299485}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120; Evidence={ECO:0000305|PubMed:9299485}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2; Evidence={ECO:0000269|PubMed:9153233, ECO:0000269|PubMed:9299485}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence={ECO:0000305|PubMed:9299485}; CATALYTIC ACTIVITY: Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate; Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394; Evidence={ECO:0000269|PubMed:9299485}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140; Evidence={ECO:0000305|PubMed:9299485}; CATALYTIC ACTIVITY: Reaction=H2O + malonyl-CoA = CoA + H(+) + malonate; Xref=Rhea:RHEA:40219, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15792, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384; Evidence={ECO:0000250|UniProtKB:P58137}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40220; Evidence={ECO:0000250|UniProtKB:P58137}; CATALYTIC ACTIVITY: Reaction=acetoacetyl-CoA + H2O = acetoacetate + CoA + H(+); Xref=Rhea:RHEA:15673, ChEBI:CHEBI:13705, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57286, ChEBI:CHEBI:57287; EC=3.1.2.11; Evidence={ECO:0000250|UniProtKB:P58137}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15674; Evidence={ECO:0000250|UniProtKB:P58137}; CATALYTIC ACTIVITY: Reaction=H2O + propanoyl-CoA = CoA + H(+) + propanoate; Xref=Rhea:RHEA:40103, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17272, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392; Evidence={ECO:0000250|UniProtKB:P58137}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40104; Evidence={ECO:0000250|UniProtKB:P58137}; CATALYTIC ACTIVITY: Reaction=H2O + succinyl-CoA = CoA + H(+) + succinate; Xref=Rhea:RHEA:11516, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=3.1.2.3; Evidence={ECO:0000250|UniProtKB:P58137}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11517; Evidence={ECO:0000250|UniProtKB:P58137}; CATALYTIC ACTIVITY: Reaction=glutaryl-CoA + H2O = CoA + glutarate + H(+); Xref=Rhea:RHEA:40575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30921, ChEBI:CHEBI:57287, ChEBI:CHEBI:57378; Evidence={ECO:0000250|UniProtKB:P58137}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40576; Evidence={ECO:0000250|UniProtKB:P58137}; CATALYTIC ACTIVITY: Reaction=H2O + hexanedioyl-CoA = CoA + H(+) + hexanedioate; Xref=Rhea:RHEA:40583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17128, ChEBI:CHEBI:57287, ChEBI:CHEBI:76327; Evidence={ECO:0000250|UniProtKB:P58137}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40584; Evidence={ECO:0000250|UniProtKB:P58137}; CATALYTIC ACTIVITY: Reaction=H2O + octanedioyl-CoA = CoA + H(+) + octanedioate; Xref=Rhea:RHEA:40587, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:76282, ChEBI:CHEBI:76317; Evidence={ECO:0000250|UniProtKB:P58137}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40588; Evidence={ECO:0000250|UniProtKB:P58137}; CATALYTIC ACTIVITY: Reaction=decanedioyl-CoA + H2O = CoA + decanedioate + H(+); Xref=Rhea:RHEA:40591, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:76283, ChEBI:CHEBI:76316; Evidence={ECO:0000250|UniProtKB:P58137}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40592; Evidence={ECO:0000250|UniProtKB:P58137}; CATALYTIC ACTIVITY: Reaction=dodecanedioyl-CoA + H2O = CoA + dodecanedioate + H(+); Xref=Rhea:RHEA:40595, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:76273, ChEBI:CHEBI:76315; Evidence={ECO:0000250|UniProtKB:P58137}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40596; Evidence={ECO:0000250|UniProtKB:P58137}; CATALYTIC ACTIVITY: Reaction=(9Z)-tetradecenoyl-CoA + H2O = (9Z)-tetradecenoate + CoA + H(+); Xref=Rhea:RHEA:40135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32370, ChEBI:CHEBI:57287, ChEBI:CHEBI:65060; Evidence={ECO:0000250|UniProtKB:P58137}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40136; Evidence={ECO:0000250|UniProtKB:P58137}; CATALYTIC ACTIVITY: Reaction=(9Z)-hexadecenoyl-CoA + H2O = (9Z)-hexadecenoate + CoA + H(+); Xref=Rhea:RHEA:40131, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372, ChEBI:CHEBI:57287, ChEBI:CHEBI:61540; Evidence={ECO:0000250|UniProtKB:P58137}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40132; Evidence={ECO:0000250|UniProtKB:P58137}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+); Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence={ECO:0000250|UniProtKB:P58137}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140; Evidence={ECO:0000250|UniProtKB:P58137}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoyl-CoA + H2O = (9Z,12Z)-octadecadienoate + CoA + H(+); Xref=Rhea:RHEA:40143, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383; Evidence={ECO:0000250|UniProtKB:P58137}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40144; Evidence={ECO:0000250|UniProtKB:P58137}; CATALYTIC ACTIVITY: Reaction=eicosanoyl-CoA + H2O = CoA + eicosanoate + H(+); Xref=Rhea:RHEA:40147, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32360, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380; Evidence={ECO:0000250|UniProtKB:P58137}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148; Evidence={ECO:0000250|UniProtKB:P58137}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + CoA + H(+); Xref=Rhea:RHEA:40151, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368; Evidence={ECO:0000250|UniProtKB:P58137}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40152; Evidence={ECO:0000250|UniProtKB:P58137}; CATALYTIC ACTIVITY: Reaction=4,8-dimethylnonanoyl-CoA + H2O = 4,8-dimethylnonanoate + CoA + H(+); Xref=Rhea:RHEA:40223, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:77061, ChEBI:CHEBI:77063; Evidence={ECO:0000250|UniProtKB:P58137}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40224; Evidence={ECO:0000250|UniProtKB:P58137}; CATALYTIC ACTIVITY: Reaction=2,6-dimethylheptanoyl-CoA + H2O = 2,6-dimethylheptanoate + CoA + H(+); Xref=Rhea:RHEA:59952, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:84847, ChEBI:CHEBI:143533; Evidence={ECO:0000250|UniProtKB:Q8VHK0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59953; Evidence={ECO:0000250|UniProtKB:Q8VHK0}; CATALYTIC ACTIVITY: Reaction=(3S)-hydroxy-3-methylglutaryl-CoA + H2O = 3-hydroxy-3-methylglutarate + CoA + H(+); Xref=Rhea:RHEA:16305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17325, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287; EC=3.1.2.5; Evidence={ECO:0000250|UniProtKB:P58137}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16306; Evidence={ECO:0000250|UniProtKB:P58137}; CATALYTIC ACTIVITY: Reaction=3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + H2O = 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + CoA + H(+); Xref=Rhea:RHEA:59936, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:63001, ChEBI:CHEBI:85674; Evidence={ECO:0000250|UniProtKB:P58137}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59937; Evidence={ECO:0000250|UniProtKB:P58137}; CATALYTIC ACTIVITY: Reaction=2-methyloctadecanoyl-CoA + H2O = 2-methyloctadecanoate + CoA + H(+); Xref=Rhea:RHEA:59940, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:143530, ChEBI:CHEBI:143531; Evidence={ECO:0000250|UniProtKB:P58137}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59941; Evidence={ECO:0000250|UniProtKB:P58137}; CATALYTIC ACTIVITY: Reaction=H2O + prostaglandin F2alpha-CoA = CoA + H(+) + prostaglandin F2alpha; Xref=Rhea:RHEA:59948, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57404, ChEBI:CHEBI:143532; Evidence={ECO:0000250|UniProtKB:P58137}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59949; Evidence={ECO:0000250|UniProtKB:P58137};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.1 uM for decanoyl-CoA {ECO:0000269|PubMed:9153233}; Vmax=7.1 umol/min/mg enzyme {ECO:0000269|PubMed:9153233};
|
PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:10944470, ECO:0000305|PubMed:9299485}.
| null | null |
FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels (PubMed:15194431, PubMed:9153233, PubMed:9299485). Displays no strong substrate specificity with respect to the carboxylic acid moiety of Acyl-CoAs (By similarity). Hydrolyzes medium length (C2 to C20) straight-chain, saturated and unsaturated acyl-CoAS but is inactive towards substrates with longer aliphatic chains (PubMed:9153233, PubMed:9299485). Moreover, it catalyzes the hydrolysis of CoA esters of bile acids, such as choloyl-CoA and chenodeoxycholoyl-CoA and competes with bile acid CoA:amino acid N-acyltransferase (BAAT) (By similarity). Is also able to hydrolyze CoA esters of dicarboxylic acids (By similarity). It is involved in the metabolic regulation of peroxisome proliferation (PubMed:15194431). {ECO:0000250|UniProtKB:P58137, ECO:0000269|PubMed:15194431, ECO:0000269|PubMed:9153233, ECO:0000269|PubMed:9299485}.; FUNCTION: (Microbial infection) May mediate Nef-induced down-regulation of CD4 cell-surface expression (PubMed:9153233). {ECO:0000269|PubMed:9153233}.
|
Homo sapiens (Human)
|
O14735
|
CDIPT_HUMAN
|
MPDENIFLFVPNLIGYARIVFAIISFYFMPCCPLTASSFYLLSGLLDAFDGHAARALNQGTRFGAMLDMLTDRCSTMCLLVNLALLYPGATLFFQISMSLDVASHWLHLHSSVVRGSESHKMIDLSGNPVLRIYYTSRPALFTLCAGNELFYCLLYLFHFSEGPLVGSVGLFRMGLWVTAPIALLKSLISVIHLITAARNMAALDAADRAKKK
|
2.7.8.11
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:8110188}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:8110188}; Note=Catalytic activity is higher with Mg(2+). {ECO:0000269|PubMed:8110188};
|
phosphatidylinositol biosynthetic process [GO:0006661]
|
endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
CDP-diacylglycerol-inositol 3-phosphatidyltransferase activity [GO:0003881]; metal ion binding [GO:0046872]
|
PF01066;
|
1.20.120.1760;
|
CDP-alcohol phosphatidyltransferase class-I family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:8110188}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000305|PubMed:8110188}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a CDP-1,2-diacyl-sn-glycerol + myo-inositol = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + CMP + H(+); Xref=Rhea:RHEA:11580, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268, ChEBI:CHEBI:57880, ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.11; Evidence={ECO:0000269|PubMed:8110188, ECO:0000269|PubMed:9407135}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11581; Evidence={ECO:0000305|PubMed:9407135}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11582; Evidence={ECO:0000305|PubMed:9407135};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:8110188};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:8110188};
|
FUNCTION: Catalyzes the biosynthesis of phosphatidylinositol (PtdIns) as well as PtdIns:inositol exchange reaction. May thus act to reduce an excessive cellular PtdIns content. The exchange activity is due to the reverse reaction of PtdIns synthase and is dependent on CMP, which is tightly bound to the enzyme. {ECO:0000269|PubMed:8110188, ECO:0000269|PubMed:9407135}.
|
Homo sapiens (Human)
|
O14737
|
PDCD5_HUMAN
|
MADEELEALRRQRLAELQAKHGDPGDAAQQEAKHREAEMRNSILAQVLDQSARARLSNLALVKPEKTKAVENYLIQMARYGQLSEKVSEQGLIEILKKVSQQTEKTTTVKFNRRKVMDSDEDDDY
| null | null |
apoptotic process [GO:0006915]; cellular response to transforming growth factor beta stimulus [GO:0071560]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of chaperone-mediated protein folding [GO:1903645]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of gene expression [GO:0010628]; positive regulation of protein insertion into mitochondrial outer membrane [GO:1903638]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]
|
acetyltransferase activator activity [GO:0010698]; beta-tubulin binding [GO:0048487]; DNA binding [GO:0003677]; heparin binding [GO:0008201]
|
PF01984;
|
1.10.8.140;
|
PDCD5 family
| null | null | null | null | null | null | null |
FUNCTION: May function in the process of apoptosis.
|
Homo sapiens (Human)
|
O14744
|
ANM5_HUMAN
|
MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAKNRPGPQTRSDLLLSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPEDLRDDIIENAPTTHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKMHQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNVQVLMVLGAGRGPLVNASLRAAKQADRRIKLYAVEKNPNAVVTLENWQFEEWGSQVTVVSSDMREWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFLAPISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFAGYFETVLYQDITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICVRFWRCSNSKKVWYEWAVTAPVCSAIHNPTGRSYTIGL
|
2.1.1.320
| null |
chromatin remodeling [GO:0006338]; circadian regulation of gene expression [GO:0032922]; DNA-templated transcription termination [GO:0006353]; endothelial cell activation [GO:0042118]; Golgi ribbon formation [GO:0090161]; liver regeneration [GO:0097421]; negative regulation of cell differentiation [GO:0045596]; negative regulation of gene expression via chromosomal CpG dinucleotide methylation [GO:0044027]; peptidyl-arginine methylation [GO:0018216]; peptidyl-arginine N-methylation [GO:0035246]; positive regulation of adenylate cyclase-inhibiting dopamine receptor signaling pathway [GO:1904992]; positive regulation of mRNA splicing, via spliceosome [GO:0048026]; positive regulation of oligodendrocyte differentiation [GO:0048714]; regulation of DNA-templated transcription [GO:0006355]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of mitotic nuclear division [GO:0007088]; regulation of signal transduction by p53 class mediator [GO:1901796]; spliceosomal snRNP assembly [GO:0000387]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; histone methyltransferase complex [GO:0035097]; methylosome [GO:0034709]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
E-box binding [GO:0070888]; histone arginine N-methyltransferase activity [GO:0008469]; histone H3 methyltransferase activity [GO:0140938]; histone H4R3 methyltransferase activity [GO:0044020]; histone methyltransferase activity [GO:0042054]; identical protein binding [GO:0042802]; methyl-CpG binding [GO:0008327]; methyltransferase activity [GO:0008168]; p53 binding [GO:0002039]; protein heterodimerization activity [GO:0046982]; protein-arginine N-methyltransferase activity [GO:0016274]; protein-arginine omega-N symmetric methyltransferase activity [GO:0035243]; ribonucleoprotein complex binding [GO:0043021]; transcription corepressor activity [GO:0003714]
|
PF05185;PF17286;PF17285;
|
3.20.20.150;2.70.160.11;3.40.50.150;
|
Class I-like SAM-binding methyltransferase superfamily, Protein arginine N-methyltransferase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21081503, ECO:0000269|PubMed:21917714, ECO:0000269|PubMed:22269951}. Nucleus {ECO:0000269|PubMed:18404153, ECO:0000269|PubMed:21081503, ECO:0000269|PubMed:21917714, ECO:0000269|PubMed:22269951}. Chromosome {ECO:0000269|PubMed:16428440, ECO:0000269|PubMed:33376131}. Golgi apparatus {ECO:0000269|PubMed:20421892}. Note=Localizes to promoter regions of target genes on chromosomes (PubMed:33376131). Localizes to methylated chromatin (PubMed:16428440). {ECO:0000269|PubMed:16428440, ECO:0000269|PubMed:33376131}.
|
CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48108, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:11992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:88221; EC=2.1.1.320; Evidence={ECO:0000269|PubMed:19011621, ECO:0000269|PubMed:21081503, ECO:0000269|PubMed:23071334};
| null | null | null | null |
FUNCTION: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA (PubMed:10531356, PubMed:11152681, PubMed:11747828, PubMed:12411503, PubMed:15737618, PubMed:17709427, PubMed:20159986, PubMed:20810653, PubMed:21081503, PubMed:21258366, PubMed:21917714, PubMed:22269951). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles (PubMed:11747828, PubMed:12411503, PubMed:17709427). Methylates SUPT5H and may regulate its transcriptional elongation properties (PubMed:12718890). May methylate the N-terminal region of MBD2 (PubMed:16428440). Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. Methylates histone H2A and H4 'Arg-3' during germ cell development (By similarity). Methylates histone H3 'Arg-8', which may repress transcription (By similarity). Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (By similarity). Methylates RPS10. Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation (PubMed:21258366, PubMed:21917714). Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity (PubMed:21917714). Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9 (PubMed:22269951). Methylates and regulates SRGAP2 which is involved in cell migration and differentiation (PubMed:20810653). Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter (By similarity). Methylates GM130/GOLGA2, regulating Golgi ribbon formation (PubMed:20421892). Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (PubMed:25284789). Symmetrically methylates POLR2A, a modification that allows the recruitment to POLR2A of proteins including SMN1/SMN2 and SETX. This is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination (PubMed:26700805). Along with LYAR, binds the promoter of gamma-globin HBG1/HBG2 and represses its expression (PubMed:25092918). Symmetrically methylates NCL (PubMed:21081503). Methylates p53/TP53; methylation might possibly affect p53/TP53 target gene specificity (PubMed:19011621). Involved in spliceosome maturation and mRNA splicing in prophase I spermatocytes through the catalysis of the symmetrical arginine dimethylation of SNRPB (small nuclear ribonucleoprotein-associated protein) and the interaction with tudor domain-containing protein TDRD6 (By similarity). {ECO:0000250|UniProtKB:Q8CIG8, ECO:0000269|PubMed:10531356, ECO:0000269|PubMed:11152681, ECO:0000269|PubMed:11747828, ECO:0000269|PubMed:12411503, ECO:0000269|PubMed:12718890, ECO:0000269|PubMed:15737618, ECO:0000269|PubMed:16428440, ECO:0000269|PubMed:17709427, ECO:0000269|PubMed:19011621, ECO:0000269|PubMed:20159986, ECO:0000269|PubMed:20421892, ECO:0000269|PubMed:20810653, ECO:0000269|PubMed:21081503, ECO:0000269|PubMed:21258366, ECO:0000269|PubMed:21917714, ECO:0000269|PubMed:22269951, ECO:0000269|PubMed:25092918, ECO:0000269|PubMed:25284789, ECO:0000269|PubMed:26700805}.
|
Homo sapiens (Human)
|
O14745
|
NHRF1_HUMAN
|
MSADAAAGAPLPRLCCLEKGPNGYGFHLHGEKGKLGQYIRLVEPGSPAEKAGLLAGDRLVEVNGENVEKETHQQVVSRIRAALNAVRLLVVDPETDEQLQKLGVQVREELLRAQEAPGQAEPPAAAEVQGAGNENEPREADKSHPEQRELRPRLCTMKKGPSGYGFNLHSDKSKPGQFIRSVDPDSPAEASGLRAQDRIVEVNGVCMEGKQHGDVVSAIRAGGDETKLLVVDRETDEFFKKCRVIPSQEHLNGPLPVPFTNGEIQKENSREALAEAALESPRPALVRSASSDTSEELNSQDSPPKQDSTAPSSTSSSDPILDFNISLAMAKERAHQKRSSKRAPQMDWSKKNELFSNL
| null | null |
actin cytoskeleton organization [GO:0030036]; adenylate cyclase-activating dopamine receptor signaling pathway [GO:0007191]; auditory receptor cell stereocilium organization [GO:0060088]; bile acid secretion [GO:0032782]; cerebrospinal fluid circulation [GO:0090660]; cilium organization [GO:0044782]; establishment of epithelial cell apical/basal polarity [GO:0045198]; establishment of Golgi localization [GO:0051683]; fibroblast migration [GO:0010761]; gamma-aminobutyric acid import [GO:0051939]; gland morphogenesis [GO:0022612]; glutathione transport [GO:0034635]; import across plasma membrane [GO:0098739]; intracellular phosphate ion homeostasis [GO:0030643]; maintenance of epithelial cell apical/basal polarity [GO:0045199]; microvillus assembly [GO:0030033]; morphogenesis of an epithelium [GO:0002009]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of fibroblast migration [GO:0010764]; negative regulation of mitotic cell cycle [GO:0045930]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative regulation of platelet-derived growth factor receptor signaling pathway [GO:0010642]; negative regulation of sodium ion transport [GO:0010766]; nuclear migration [GO:0007097]; phospholipase C-activating dopamine receptor signaling pathway [GO:0060158]; plasma membrane organization [GO:0007009]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of monoatomic ion transmembrane transport [GO:0034767]; protein localization to plasma membrane [GO:0072659]; protein-containing complex assembly [GO:0065003]; regulation of cell shape [GO:0008360]; regulation of cell size [GO:0008361]; regulation of protein kinase activity [GO:0045859]; regulation of renal phosphate excretion [GO:1903402]; renal absorption [GO:0070293]; renal phosphate ion absorption [GO:0097291]; renal sodium ion transport [GO:0003096]; sensory perception of sound [GO:0007605]; transport across blood-brain barrier [GO:0150104]; Wnt signaling pathway [GO:0016055]
|
actin cytoskeleton [GO:0015629]; apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]; cell periphery [GO:0071944]; cytoplasm [GO:0005737]; endomembrane system [GO:0012505]; extracellular exosome [GO:0070062]; filopodium [GO:0030175]; membrane [GO:0016020]; microvillus [GO:0005902]; microvillus membrane [GO:0031528]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane protein complex [GO:0098797]; ruffle [GO:0001726]; sperm midpiece [GO:0097225]; stereocilium tip [GO:0032426]; vesicle [GO:0031982]
|
beta-2 adrenergic receptor binding [GO:0031698]; beta-catenin binding [GO:0008013]; channel activator activity [GO:0099103]; chloride channel regulator activity [GO:0017081]; dopamine receptor binding [GO:0050780]; gamma-aminobutyric acid transmembrane transporter activity [GO:0015185]; growth factor receptor binding [GO:0070851]; identical protein binding [GO:0042802]; myosin II binding [GO:0045159]; PDZ domain binding [GO:0030165]; phosphatase binding [GO:0019902]; protein self-association [GO:0043621]; protein-containing complex binding [GO:0044877]; protein-membrane adaptor activity [GO:0043495]; signaling receptor binding [GO:0005102]; transmembrane transporter binding [GO:0044325]; type 2 metabotropic glutamate receptor binding [GO:0031799]; type 3 metabotropic glutamate receptor binding [GO:0031800]
|
PF09007;PF00595;
|
2.30.42.10;
| null |
PTM: Phosphorylated on serine residues. {ECO:0000269|PubMed:9314537}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Apical cell membrane {ECO:0000250}. Endomembrane system; Peripheral membrane protein. Cell projection, filopodium. Cell projection, ruffle. Cell projection, microvillus. Note=Translocates from the cytoplasm to the apical cell membrane in a PODXL-dependent manner. Colocalizes with CFTR at the midpiece of sperm tail (By similarity). Colocalizes with actin in microvilli-rich apical regions of the syncytiotrophoblast. Found in microvilli, ruffling membrane and filopodia of HeLa cells. Present in lipid rafts of T-cells. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Scaffold protein that connects plasma membrane proteins with members of the ezrin/moesin/radixin family and thereby helps to link them to the actin cytoskeleton and to regulate their surface expression. Necessary for recycling of internalized ADRB2. Was first known to play a role in the regulation of the activity and subcellular location of SLC9A3. Necessary for cAMP-mediated phosphorylation and inhibition of SLC9A3. May enhance Wnt signaling. May participate in HTR4 targeting to microvilli (By similarity). Involved in the regulation of phosphate reabsorption in the renal proximal tubules. Involved in sperm capacitation. May participate in the regulation of the chloride and bicarbonate homeostasis in spermatozoa. {ECO:0000250, ECO:0000269|PubMed:10499588, ECO:0000269|PubMed:18784102, ECO:0000269|PubMed:9096337, ECO:0000269|PubMed:9430655}.
|
Homo sapiens (Human)
|
O14746
|
TERT_HUMAN
|
MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQVWKNPTFFLRVISDTASLCYSILKAKNAGMSLGAKGAAGPLPSEAVQWLCHQAFLLKLTRHRVTYVPLLGSLRTAQTQLSRKLPGTTLTALEAAANPALPSDFKTILD
|
2.7.7.49
| null |
cellular response to hypoxia [GO:0071456]; DNA biosynthetic process [GO:0071897]; DNA strand elongation [GO:0022616]; establishment of protein localization to telomere [GO:0070200]; mitochondrion organization [GO:0007005]; negative regulation of cellular senescence [GO:2000773]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; negative regulation of gene expression [GO:0010629]; negative regulation of neuron apoptotic process [GO:0043524]; positive regulation of angiogenesis [GO:0045766]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of glucose import [GO:0046326]; positive regulation of hair cycle [GO:0042635]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of nitric-oxide synthase activity [GO:0051000]; positive regulation of protein binding [GO:0032092]; positive regulation of protein localization to nucleolus [GO:1904751]; positive regulation of stem cell proliferation [GO:2000648]; positive regulation of transdifferentiation [GO:1903620]; positive regulation of vascular associated smooth muscle cell migration [GO:1904754]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; positive regulation of Wnt signaling pathway [GO:0030177]; regulation of protein stability [GO:0031647]; replicative senescence [GO:0090399]; response to cadmium ion [GO:0046686]; RNA-templated DNA biosynthetic process [GO:0006278]; RNA-templated transcription [GO:0001172]; siRNA processing [GO:0030422]; siRNA transcription [GO:0140745]; telomere maintenance [GO:0000723]; telomere maintenance via telomerase [GO:0007004]
|
chromosome, telomeric region [GO:0000781]; cytosol [GO:0005829]; mitochondrial nucleoid [GO:0042645]; nuclear speck [GO:0016607]; nuclear telomere cap complex [GO:0000783]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; PML body [GO:0016605]; RNA-directed RNA polymerase complex [GO:0031379]; telomerase catalytic core complex [GO:0000333]; telomerase holoenzyme complex [GO:0005697]; TERT-RMRP complex [GO:1990572]
|
DNA binding [GO:0003677]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein-folding chaperone binding [GO:0051087]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968]; RNA-directed DNA polymerase activity [GO:0003964]; telomerase activity [GO:0003720]; telomerase RNA binding [GO:0070034]; telomerase RNA reverse transcriptase activity [GO:0003721]; telomeric DNA binding [GO:0042162]; template-free RNA nucleotidyltransferase [GO:0098680]; transcription coactivator binding [GO:0001223]; tRNA binding [GO:0000049]
|
PF00078;PF12009;PF21399;
|
1.10.132.70;1.10.357.90;3.30.70.2630;
|
Reverse transcriptase family, Telomerase subfamily
|
PTM: Phosphorylation at Tyr-707 under oxidative stress leads to translocation of TERT to the cytoplasm and reduces its antiapoptotic activity. Dephosphorylated by SHP2/PTPN11 leading to nuclear retention. Phosphorylation at Ser-227 by the AKT pathway promotes nuclear location. Phosphorylation at the G2/M phase at Ser-457 by DYRK2 promotes ubiquitination by the EDVP complex and degradation. {ECO:0000269|PubMed:12808100, ECO:0000269|PubMed:18829466, ECO:0000269|PubMed:22366458, ECO:0000269|PubMed:23362280}.; PTM: Ubiquitinated by the EDVP complex, a E3 ligase complex following phosphorylation at Ser-457 by DYRK2. Ubiquitinated leads to proteasomal degradation. {ECO:0000269|PubMed:23362280}.; PTM: (Microbial infection) In case of infection by HIV-1, the EDVP complex is hijacked by HIV-1 via interaction between HIV-1 Vpr and DCAF1/VPRBP, leading to ubiquitination and degradation. {ECO:0000269|PubMed:23362280}.
|
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:22226966}. Nucleus, nucleoplasm. Nucleus. Chromosome, telomere. Cytoplasm. Nucleus, PML body. Note=Shuttling between nuclear and cytoplasm depends on cell cycle, phosphorylation states, transformation and DNA damage. Diffuse localization in the nucleoplasm. Enriched in nucleoli of certain cell types. Translocated to the cytoplasm via nuclear pores in a CRM1/RAN-dependent manner involving oxidative stress-mediated phosphorylation at Tyr-707. Dephosphorylation at this site by SHP2 retains TERT in the nucleus. Translocated to the nucleus by phosphorylation by AKT.
|
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000269|PubMed:21602826, ECO:0000269|PubMed:29695869};
| null | null | null | null |
FUNCTION: Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis. {ECO:0000269|PubMed:14963003, ECO:0000269|PubMed:15082768, ECO:0000269|PubMed:15857955, ECO:0000269|PubMed:17026956, ECO:0000269|PubMed:17264120, ECO:0000269|PubMed:17296728, ECO:0000269|PubMed:17548608, ECO:0000269|PubMed:19188162, ECO:0000269|PubMed:19567472, ECO:0000269|PubMed:19571879, ECO:0000269|PubMed:19777057, ECO:0000269|PubMed:9389643}.
|
Homo sapiens (Human)
|
O14756
|
H17B6_HUMAN
|
MWLYLAAFVGLYYLLHWYRERQVVSHLQDKYVFITGCDSGFGNLLARQLDARGLRVLAACLTEKGAEQLRGQTSDRLETVTLDVTKMESIAAATQWVKEHVGDRGLWGLVNNAGILTPITLCEWLNTEDSMNMLKVNLIGVIQVTLSMLPLVRRARGRIVNVSSILGRVAFFVGGYCVSKYGVEAFSDILRREIQHFGVKISIVEPGYFRTGMTNMTQSLERMKQSWKEAPKHIKETYGQQYFDALYNIMKEGLLNCSTNLNLVTDCMEHALTSVHPRTRYSAGWDAKFFFIPLSYLPTSLADYILTRSWPKPAQAV
|
1.1.1.105; 1.1.1.209; 1.1.1.239; 1.1.1.53; 1.1.1.62
| null |
androgen biosynthetic process [GO:0006702]; androgen catabolic process [GO:0006710]; brexanolone catabolic process [GO:0062175]; retinol metabolic process [GO:0042572]; steroid metabolic process [GO:0008202]
|
early endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; intracellular membrane-bounded organelle [GO:0043231]
|
5alpha-androstane-3beta,17beta-diol dehydrogenase activity [GO:0047024]; androstan-3-alpha,17-beta-diol dehydrogenase activity [GO:0047044]; androsterone dehydrogenase activity [GO:0047023]; catalytic activity [GO:0003824]; electron transfer activity [GO:0009055]; estradiol 17-beta-dehydrogenase [NAD(P)] activity [GO:0004303]; NAD-retinol dehydrogenase activity [GO:0004745]; oxidoreductase activity [GO:0016491]; testosterone 17-beta-dehydrogenase (NADP+) activity [GO:0047045]; testosterone dehydrogenase (NAD+) activity [GO:0047035]
|
PF00106;
|
3.40.50.720;
|
Short-chain dehydrogenases/reductases (SDR) family
| null |
SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:11360992}; Peripheral membrane protein {ECO:0000269|PubMed:11360992}; Lumenal side {ECO:0000269|PubMed:11360992}. Early endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Lumenal side {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=all-trans-retinol--[retinol-binding protein] + NAD(+) = all-trans-retinal--[retinol-binding protein] + H(+) + NADH; Xref=Rhea:RHEA:48488, Rhea:RHEA-COMP:14428, Rhea:RHEA-COMP:14430, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83228; EC=1.1.1.105; Evidence={ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992}; CATALYTIC ACTIVITY: Reaction=all-trans-retinol + NAD(+) = all-trans-retinal + H(+) + NADH; Xref=Rhea:RHEA:21284, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.105; Evidence={ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21285; Evidence={ECO:0000305|PubMed:11360992}; CATALYTIC ACTIVITY: Reaction=androsterone + NAD(+) = 5alpha-androstan-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:20381, ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16032, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.209; Evidence={ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20382; Evidence={ECO:0000269|PubMed:11360992}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20383; Evidence={ECO:0000269|PubMed:11360992}; CATALYTIC ACTIVITY: Reaction=NAD(+) + testosterone = androst-4-ene-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:14929, ChEBI:CHEBI:15378, ChEBI:CHEBI:16422, ChEBI:CHEBI:17347, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.239; Evidence={ECO:0000250|UniProtKB:Q9R092}; CATALYTIC ACTIVITY: Reaction=5alpha-androstane-3alpha,17beta-diol + NAD(+) = 17beta-hydroxy-5alpha-androstan-3-one + H(+) + NADH; Xref=Rhea:RHEA:42004, ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:36713, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.53; Evidence={ECO:0000269|PubMed:11360992}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42006; Evidence={ECO:0000305|PubMed:11360992}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + NAD(+) = estrone + H(+) + NADH; Xref=Rhea:RHEA:24612, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:17263, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.62; Evidence={ECO:0000250|UniProtKB:Q9R092}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + NADP(+) = estrone + H(+) + NADPH; Xref=Rhea:RHEA:24616, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:17263, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.62; Evidence={ECO:0000250|UniProtKB:Q9R092}; CATALYTIC ACTIVITY: Reaction=3alpha-hydroxy-5alpha-pregnan-20-one + NAD(+) = 5alpha-pregnane-3,20-dione + H(+) + NADH; Xref=Rhea:RHEA:41980, ChEBI:CHEBI:15378, ChEBI:CHEBI:28952, ChEBI:CHEBI:50169, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41981; Evidence={ECO:0000305|PubMed:11360992}; CATALYTIC ACTIVITY: Reaction=5alpha-androstane-3beta,17beta-diol + NAD(+) = 17beta-hydroxy-5alpha-androstan-3-one + H(+) + NADH; Xref=Rhea:RHEA:42184, ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:18329, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:11360992}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42186; Evidence={ECO:0000305|PubMed:11360992}; CATALYTIC ACTIVITY: Reaction=3beta-hydroxy-5alpha-androstan-17-one + NAD(+) = 5alpha-androstan-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:42188, ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:541975; Evidence={ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992, ECO:0000269|PubMed:11513953}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42190; Evidence={ECO:0000305|PubMed:11360992};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.19 uM for NAD {ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992}; KM=0.18 uM for NADH {ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992}; KM=54 uM for NADPH {ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992}; KM=940 uM for NADP {ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992}; KM=3.2 uM for all-trans-retinol {ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992}; KM=0.24 uM for allopregnanolone {ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992}; KM=0.13 uM for 3-alpha-androstanediol {ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992}; KM=0.23 uM for androsterone {ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992}; KM=0.13 uM for dehydroepiandrosterone {ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992}; Vmax=1.2 nmol/min/mg enzyme with all-trans-retinol {ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992}; Vmax=14.7 nmol/min/mg enzyme with allopregnanolone {ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992}; Vmax=16.5 nmol/min/mg enzyme with 3-alpha-androstanediol {ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992}; Vmax=35 nmol/min/mg enzyme with androsterone {ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992}; Vmax=0.9 nmol/min/mg enzyme with dehydroepiandrosterone {ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992}; Note=The kinetic parameters were determined using microsomes from transfected cells.;
| null | null | null |
FUNCTION: NAD-dependent oxidoreductase with broad substrate specificity that shows both oxidative and reductive activity (in vitro). Has 17-beta-hydroxysteroid dehydrogenase activity towards various steroids (in vitro). Converts 5-alpha-androstan-3-alpha,17-beta-diol to androsterone and estradiol to estrone (in vitro). Has 3-alpha-hydroxysteroid dehydrogenase activity towards androsterone (in vitro). Has retinol dehydrogenase activity towards all-trans-retinol (in vitro). Can convert androsterone to epi-androsterone. Androsterone is first oxidized to 5-alpha-androstane-3,17-dione and then reduced to epi-andosterone. Can act on both C-19 and C-21 3-alpha-hydroxysteroids. {ECO:0000269|PubMed:10896656, ECO:0000269|PubMed:11360992, ECO:0000269|PubMed:11513953}.
|
Homo sapiens (Human)
|
O14757
|
CHK1_HUMAN
|
MAVPFVEDWDLVQTLGEGAYGEVQLAVNRVTEEAVAVKIVDMKRAVDCPENIKKEICINKMLNHENVVKFYGHRREGNIQYLFLEYCSGGELFDRIEPDIGMPEPDAQRFFHQLMAGVVYLHGIGITHRDIKPENLLLDERDNLKISDFGLATVFRYNNRERLLNKMCGTLPYVAPELLKRREFHAEPVDVWSCGIVLTAMLAGELPWDQPSDSCQEYSDWKEKKTYLNPWKKIDSAPLALLHKILVENPSARITIPDIKKDRWYNKPLKKGAKRPRVTSGGVSESPSGFSKHIQSNLDFSPVNSASSEENVKYSSSQPEPRTGLSLWDTSPSYIDKLVQGISFSQPTCPDHMLLNSQLLGTPGSSQNPWQRLVKRMTRFFTKLDADKSYQCLKETCEKLGYQWKKSCMNQVTISTTDRRNNKLIFKVNLLEMDDKILVDFRLSKGDGLEFKRHFLKIKGKLIDIVSSQKIWLPAT
|
2.7.11.1
| null |
apoptotic process [GO:0006915]; apoptotic process involved in development [GO:1902742]; cellular response to caffeine [GO:0071313]; cellular response to mechanical stimulus [GO:0071260]; chromatin remodeling [GO:0006338]; DNA damage checkpoint signaling [GO:0000077]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; G2/M transition of mitotic cell cycle [GO:0000086]; inner cell mass cell proliferation [GO:0001833]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; mitotic G2/M transition checkpoint [GO:0044818]; negative regulation of DNA biosynthetic process [GO:2000279]; negative regulation of G0 to G1 transition [GO:0070317]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of mitotic nuclear division [GO:0045839]; nucleus organization [GO:0006997]; peptidyl-threonine phosphorylation [GO:0018107]; positive regulation of cell cycle [GO:0045787]; protein phosphorylation [GO:0006468]; regulation of cell population proliferation [GO:0042127]; regulation of double-strand break repair via homologous recombination [GO:0010569]; regulation of mitotic centrosome separation [GO:0046602]; regulation of signal transduction by p53 class mediator [GO:1901796]; replicative senescence [GO:0090399]; signal transduction in response to DNA damage [GO:0042770]
|
centrosome [GO:0005813]; chromatin [GO:0000785]; condensed nuclear chromosome [GO:0000794]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; replication fork [GO:0005657]
|
ATP binding [GO:0005524]; histone H3T11 kinase activity [GO:0035402]; protein domain specific binding [GO:0019904]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
3.30.310.80;1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, NIM1 subfamily
|
PTM: Phosphorylated by ATR in a RAD17-dependent manner in response to ultraviolet irradiation and inhibition of DNA replication (PubMed:10859164, PubMed:11390642, PubMed:12446774, PubMed:12588868, PubMed:12676583, PubMed:12676925, PubMed:12676962, PubMed:14681223, PubMed:14988723, PubMed:15650047, PubMed:15707391, PubMed:15870257, PubMed:25083873, PubMed:31316063). Phosphorylated by ATM in response to ionizing irradiation (PubMed:12588868, PubMed:12676583). ATM and ATR can both phosphorylate Ser-317 and Ser-345 and this results in enhanced kinase activity (PubMed:11390642, PubMed:12446774, PubMed:12588868, PubMed:12660173, PubMed:12676583, PubMed:12676962, PubMed:14657349, PubMed:15665856, PubMed:15707391, PubMed:15870257, PubMed:25083873). Phosphorylation at Ser-345 induces a change in the conformation of the protein, activates the kinase activity and is a prerequisite for interaction with FBXO6 and subsequent ubiquitination at Lys-436 (PubMed:19716789). Phosphorylation at Ser-345 also increases binding to 14-3-3 proteins and promotes nuclear retention (PubMed:12676962). Conversely, dephosphorylation at Ser-345 by PPM1D may contribute to exit from checkpoint mediated cell cycle arrest (PubMed:15870257). Phosphorylation at Ser-280 by AKT1/PKB, may promote mono and/or diubiquitination. Also phosphorylated at undefined residues during mitotic arrest, resulting in decreased activity (By similarity). {ECO:0000250|UniProtKB:O35280, ECO:0000269|PubMed:10859164, ECO:0000269|PubMed:11390642, ECO:0000269|PubMed:12446774, ECO:0000269|PubMed:12588868, ECO:0000269|PubMed:12660173, ECO:0000269|PubMed:12676583, ECO:0000269|PubMed:12676925, ECO:0000269|PubMed:12676962, ECO:0000269|PubMed:14657349, ECO:0000269|PubMed:14681223, ECO:0000269|PubMed:14988723, ECO:0000269|PubMed:15650047, ECO:0000269|PubMed:15665856, ECO:0000269|PubMed:15707391, ECO:0000269|PubMed:15870257, ECO:0000269|PubMed:19716789, ECO:0000269|PubMed:25083873, ECO:0000269|PubMed:31316063}.; PTM: Ubiquitinated. Mono or diubiquitination promotes nuclear exclusion (By similarity). The activated form (phosphorylated on Ser-345) is polyubiquitinated at Lys-436 by some SCF-type E3 ubiquitin ligase complex containing FBXO6 promoting its degradation. Ubiquitination and degradation are required to terminate the checkpoint and ensure that activated CHEK1 does not accumulate as cells progress through S phase, when replication forks encounter transient impediments during normal DNA replication. 'Lys-63'-mediated ubiquitination by TRAF4 at Lys-132 activates cell cycle arrest and activation of DNA repair (PubMed:32357935). {ECO:0000250, ECO:0000269|PubMed:10859164, ECO:0000269|PubMed:11390642, ECO:0000269|PubMed:12446774, ECO:0000269|PubMed:12676583, ECO:0000269|PubMed:12676925, ECO:0000269|PubMed:12676962, ECO:0000269|PubMed:14681223, ECO:0000269|PubMed:14988723, ECO:0000269|PubMed:15650047, ECO:0000269|PubMed:15707391, ECO:0000269|PubMed:15870257, ECO:0000269|PubMed:19716789}.; PTM: Proteolytically cleaved at the C-terminus by SPRTN during normal DNA replication, thereby promoting CHEK1 removal from chromatin and activating the protein kinase activity. {ECO:0000269|PubMed:31316063}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11836499, ECO:0000269|PubMed:12676962, ECO:0000269|PubMed:15311285, ECO:0000269|PubMed:15710331, ECO:0000269|PubMed:9278511}. Chromosome {ECO:0000269|PubMed:12676962, ECO:0000269|PubMed:31316063, ECO:0000269|PubMed:9382850}. Cytoplasm {ECO:0000269|PubMed:12676962}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15311285}. Note=Nuclear export is mediated at least in part by XPO1/CRM1 (PubMed:12676962). Also localizes to the centrosome specifically during interphase, where it may protect centrosomal CDC2 kinase from inappropriate activation by cytoplasmic CDC25B (PubMed:15311285). Proteolytic cleavage at the C-terminus by SPRTN promotes removal from chromatin (PubMed:31316063). {ECO:0000269|PubMed:12676962, ECO:0000269|PubMed:15311285, ECO:0000269|PubMed:31316063}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:10673501, ECO:0000269|PubMed:12660173, ECO:0000269|PubMed:14559997, ECO:0000269|PubMed:15659650, ECO:0000269|PubMed:15665856, ECO:0000269|PubMed:16511572, ECO:0000269|PubMed:16963448, ECO:0000269|PubMed:17296736, ECO:0000269|PubMed:17380128, ECO:0000269|PubMed:18317453, ECO:0000269|PubMed:18728393, ECO:0000269|PubMed:31316063, ECO:0000269|PubMed:9278511}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:10673501, ECO:0000269|PubMed:12660173, ECO:0000269|PubMed:14559997, ECO:0000269|PubMed:15659650, ECO:0000269|PubMed:15665856, ECO:0000269|PubMed:16511572, ECO:0000269|PubMed:16963448, ECO:0000269|PubMed:17296736, ECO:0000269|PubMed:17380128, ECO:0000269|PubMed:18317453, ECO:0000269|PubMed:18728393, ECO:0000269|PubMed:31316063, ECO:0000269|PubMed:9278511};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA (PubMed:11535615, PubMed:12399544, PubMed:12446774, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15650047, PubMed:15665856, PubMed:32357935). May also negatively regulate cell cycle progression during unperturbed cell cycles (PubMed:11535615, PubMed:12399544, PubMed:12446774, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15650047, PubMed:15665856). This regulation is achieved by a number of mechanisms that together help to preserve the integrity of the genome (PubMed:11535615, PubMed:12399544, PubMed:12446774, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15650047, PubMed:15665856). Recognizes the substrate consensus sequence [R-X-X-S/T] (PubMed:11535615, PubMed:12399544, PubMed:12446774, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15650047, PubMed:15665856). Binds to and phosphorylates CDC25A, CDC25B and CDC25C (PubMed:12676583, PubMed:12676925, PubMed:12759351, PubMed:14559997, PubMed:14681206, PubMed:19734889, PubMed:9278511). Phosphorylation of CDC25A at 'Ser-178' and 'Thr-507' and phosphorylation of CDC25C at 'Ser-216' creates binding sites for 14-3-3 proteins which inhibit CDC25A and CDC25C (PubMed:9278511). Phosphorylation of CDC25A at 'Ser-76', 'Ser-124', 'Ser-178', 'Ser-279' and 'Ser-293' promotes proteolysis of CDC25A (PubMed:12676583, PubMed:12676925, PubMed:12759351, PubMed:14681206, PubMed:19734889, PubMed:9278511). Phosphorylation of CDC25A at 'Ser-76' primes the protein for subsequent phosphorylation at 'Ser-79', 'Ser-82' and 'Ser-88' by NEK11, which is required for polyubiquitination and degradation of CDCD25A (PubMed:19734889, PubMed:20090422, PubMed:9278511). Inhibition of CDC25 leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression (PubMed:9278511). Also phosphorylates NEK6 (PubMed:18728393). Binds to and phosphorylates RAD51 at 'Thr-309', which promotes the release of RAD51 from BRCA2 and enhances the association of RAD51 with chromatin, thereby promoting DNA repair by homologous recombination (PubMed:15665856). Phosphorylates multiple sites within the C-terminus of TP53, which promotes activation of TP53 by acetylation and promotes cell cycle arrest and suppression of cellular proliferation (PubMed:10673501, PubMed:15659650, PubMed:16511572). Also promotes repair of DNA cross-links through phosphorylation of FANCE (PubMed:17296736). Binds to and phosphorylates TLK1 at 'Ser-743', which prevents the TLK1-dependent phosphorylation of the chromatin assembly factor ASF1A (PubMed:12660173, PubMed:12955071). This may enhance chromatin assembly both in the presence or absence of DNA damage (PubMed:12660173, PubMed:12955071). May also play a role in replication fork maintenance through regulation of PCNA (PubMed:18451105). May regulate the transcription of genes that regulate cell-cycle progression through the phosphorylation of histones (By similarity). Phosphorylates histone H3.1 (to form H3T11ph), which leads to epigenetic inhibition of a subset of genes (By similarity). May also phosphorylate RB1 to promote its interaction with the E2F family of transcription factors and subsequent cell cycle arrest (PubMed:17380128). Phosphorylates SPRTN, promoting SPRTN recruitment to chromatin (PubMed:31316063). Reduces replication stress and activates the G2/M checkpoint, by phosphorylating and inactivating PABIR1/FAM122A and promoting the serine/threonine-protein phosphatase 2A-mediated dephosphorylation and stabilization of WEE1 levels and activity (PubMed:33108758). {ECO:0000250|UniProtKB:O35280, ECO:0000269|PubMed:10673501, ECO:0000269|PubMed:11535615, ECO:0000269|PubMed:12399544, ECO:0000269|PubMed:12446774, ECO:0000269|PubMed:12660173, ECO:0000269|PubMed:12676583, ECO:0000269|PubMed:12676925, ECO:0000269|PubMed:12759351, ECO:0000269|PubMed:12955071, ECO:0000269|PubMed:14559997, ECO:0000269|PubMed:14681206, ECO:0000269|PubMed:14988723, ECO:0000269|PubMed:15311285, ECO:0000269|PubMed:15650047, ECO:0000269|PubMed:15659650, ECO:0000269|PubMed:15665856, ECO:0000269|PubMed:16511572, ECO:0000269|PubMed:17296736, ECO:0000269|PubMed:17380128, ECO:0000269|PubMed:18451105, ECO:0000269|PubMed:18728393, ECO:0000269|PubMed:19734889, ECO:0000269|PubMed:20090422, ECO:0000269|PubMed:31316063, ECO:0000269|PubMed:32357935, ECO:0000269|PubMed:33108758, ECO:0000269|PubMed:9278511}.; FUNCTION: [Isoform 2]: Endogenous repressor of isoform 1, interacts with, and antagonizes CHK1 to promote the S to G2/M phase transition. {ECO:0000269|PubMed:22184239}.
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Homo sapiens (Human)
|
O14763
|
TR10B_HUMAN
|
MEQRGQNAPAASGARKRHGPGPREARGARPGPRVPKTLVLVVAAVLLLVSAESALITQQDLAPQQRAAPQQKRSSPSEGLCPPGHHISEDGRDCISCKYGQDYSTHWNDLLFCLRCTRCDSGEVELSPCTTTRNTVCQCEEGTFREEDSPEMCRKCRTGCPRGMVKVGDCTPWSDIECVHKESGTKHSGEVPAVEETVTSSPGTPASPCSLSGIIIGVTVAAVVLIVAVFVCKSLLWKKVLPYLKGICSGGGGDPERVDRSSQRPGAEDNVLNEIVSILQPTQVPEQEMEVQEPAEPTGVNMLSPGESEHLLEPAEAERSQRRRLLVPANEGDPTETLRQCFDDFADLVPFDSWEPLMRKLGLMDNEIKVAKAEAAGHRDTLYTMLIKWVNKTGRDASVHTLLDALETLGERLAKQKIEDHLLSSGKFMYLEGNADSAMS
| null | null |
activation of NF-kappaB-inducing kinase activity [GO:0007250]; apoptotic process [GO:0006915]; cell surface receptor signaling pathway [GO:0007166]; cellular response to mechanical stimulus [GO:0071260]; defense response to tumor cell [GO:0002357]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; positive regulation of apoptotic process [GO:0043065]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; regulation of apoptotic process [GO:0042981]; response to endoplasmic reticulum stress [GO:0034976]; TRAIL-activated apoptotic signaling pathway [GO:0036462]
|
cell surface [GO:0009986]; plasma membrane [GO:0005886]
|
signaling receptor activity [GO:0038023]; TRAIL binding [GO:0045569]; TRAIL receptor activity [GO:0036463]
|
PF00531;PF00020;
|
1.10.533.10;2.10.50.10;
| null |
PTM: (Microbial infection) Glycosylated on Arg residue by S.typhimurium protein Ssek3. {ECO:0000269|PubMed:30902834}.
|
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Receptor for the cytotoxic ligand TNFSF10/TRAIL (PubMed:10549288). The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF-kappa-B. Essential for ER stress-induced apoptosis. {ECO:0000269|PubMed:10542098, ECO:0000269|PubMed:10549288, ECO:0000269|PubMed:15322075}.
|
Homo sapiens (Human)
|
O14764
|
GBRD_HUMAN
|
MDAPARLLAPLLLLCAQQLRGTRAMNDIGDYVGSNLEISWLPNLDGLIAGYARNFRPGIGGPPVNVALALEVASIDHISEANMEYTMTVFLHQSWRDSRLSYNHTNETLGLDSRFVDKLWLPDTFIVNAKSAWFHDVTVENKLIRLQPDGVILYSIRITSTVACDMDLAKYPMDEQECMLDLESYGYSSEDIVYYWSESQEHIHGLDKLQLAQFTITSYRFTTELMNFKSAGQFPRLSLHFHLRRNRGVYIIQSYMPSVLLVAMSWVSFWISQAAVPARVSLGITTVLTMTTLMVSARSSLPRASAIKALDVYFWICYVFVFAALVEYAFAHFNADYRKKQKAKVKVSRPRAEMDVRNAIVLFSLSAAGVTQELAISRRQRRVPGNLMGSYRSVGVETGETKKEGAARSGGQGGIRARLRPIDADTIDIYARAVFPAAFAAVNVIYWAAYAM
| null | null |
chloride transmembrane transport [GO:1902476]; gamma-aminobutyric acid signaling pathway [GO:0007214]; signal transduction [GO:0007165]; synaptic transmission, GABAergic [GO:0051932]
|
axon [GO:0030424]; chloride channel complex [GO:0034707]; dendrite [GO:0030425]; GABA-A receptor complex [GO:1902711]; GABA-ergic synapse [GO:0098982]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]; transmembrane transporter complex [GO:1902495]
|
chloride channel activity [GO:0005254]; GABA-A receptor activity [GO:0004890]; neurotransmitter receptor activity [GO:0030594]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315]
|
PF02931;PF02932;
|
2.70.170.10;1.20.58.390;
|
Ligand-gated ion channel (TC 1.A.9) family, Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily, GABRD sub-subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P18506}; Multi-pass membrane protein {ECO:0000269|PubMed:35355020}.
|
CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:35355020};
| null | null | null | null |
FUNCTION: Delta subunit of the heteropentameric ligand-gated chloride channel gated by gamma-aminobutyric acid (GABA), a major inhibitory neurotransmitter in the brain (PubMed:35355020). GABA-gated chloride channels, also named GABA(A) receptors (GABAAR), consist of five subunits arranged around a central pore and contain GABA active binding site(s) located at the alpha and beta subunit interface(s) (PubMed:35355020). When activated by GABA, GABAARs selectively allow the flow of chloride anions across the cell membrane down their electrochemical gradient (PubMed:35355020). GABAARs containing delta/GABRD subunits are predominantly located in extrasynaptic or perisynaptic positions on hippocampus and cerebellar granule cells, and contribute to the tonic GABAergic inhibition (By similarity). GABAAR containing alpha-4-beta-3-delta subunits can simultaneously bind GABA and histamine where histamine binds at the interface of two neighboring beta subunits, which may be involved in the regulation of sleep and wakefulness (PubMed:35355020). {ECO:0000250|UniProtKB:P18506, ECO:0000269|PubMed:35355020}.
|
Homo sapiens (Human)
|
O14770
|
MEIS2_HUMAN
|
MAQRYDELPHYGGMDGVGVPASMYGDPHAPRPIPPVHHLNHGPPLHATQHYGAHAPHPNVMPASMGSAVNDALKRDKDAIYGHPLFPLLALVFEKCELATCTPREPGVAGGDVCSSDSFNEDIAVFAKQVRAEKPLFSSNPELDNLMIQAIQVLRFHLLELEKVHELCDNFCHRYISCLKGKMPIDLVIDERDGSSKSDHEELSGSSTNLADHNPSSWRDHDDATSTHSAGTPGPSSGGHASQSGDNSSEQGDGLDNSVASPGTGDDDDPDKDKKRQKKRGIFPKVATNIMRAWLFQHLTHPYPSEEQKKQLAQDTGLTILQVNNWFINARRRIVQPMIDQSNRAGFLLDPSVSQGAAYSPEGQPMGSFVLDGQQHMGIRPAGLQSMPGDYVSQGGPMGMSMAQPSYTPPQMTPHPTQLRHGPPMHSYLPSHPHHPAMMMHGGPPTHPGMTMSAQSPTMLNSVDPNVGGQVMDIHAQ
| null | null |
animal organ morphogenesis [GO:0009887]; brain development [GO:0007420]; embryonic pattern specification [GO:0009880]; eye development [GO:0001654]; negative regulation of myeloid cell differentiation [GO:0045638]; negative regulation of transcription by RNA polymerase II [GO:0000122]; pancreas development [GO:0031016]; positive regulation of cardiac muscle myoblast proliferation [GO:0110024]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of transcription by RNA polymerase II [GO:0045944]; response to growth factor [GO:0070848]; response to mechanical stimulus [GO:0009612]; visual learning [GO:0008542]
|
chromatin [GO:0000785]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
|
DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]; transcription factor binding [GO:0008134]
|
PF05920;PF16493;
|
1.10.10.60;
|
TALE/MEIS homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P97367}.
| null | null | null | null | null |
FUNCTION: Involved in transcriptional regulation. Binds to HOX or PBX proteins to form dimers, or to a DNA-bound dimer of PBX and HOX proteins and thought to have a role in stabilization of the homeoprotein-DNA complex. Isoform 3 is required for the activity of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element; MEIS2 is not involved in complex DNA-binding. Probably in complex with PBX1, is involved in transcriptional regulation by KLF4. Isoform 3 and isoform 4 can bind to a EPHA8 promoter sequence containing the DNA motif 5'-CGGTCA-3'; in cooperation with a PBX protein (such as PBX2) is proposed to be involved in the transcriptional activation of EPHA8 in the developing midbrain. May be involved in regulation of myeloid differentiation. Can bind to the DNA sequence 5'-TGACAG-3'in the activator ACT sequence of the D(1A) dopamine receptor (DRD1) promoter and activate DRD1 transcription; isoform 5 cannot activate DRD1 transcription. {ECO:0000269|PubMed:10764806, ECO:0000269|PubMed:11279116, ECO:0000269|PubMed:21746878}.
|
Homo sapiens (Human)
|
O14771
|
ZN213_HUMAN
|
MAAPLEAQDQAPGEGEGLLIVKVEDSSWEQESAQHEDGRDSEACRQRFRQFCYGDVHGPHEAFSQLWELCCRWLRPELRTKEQILELLVLEQFLTVLPGEIQGWVREQHPGSGEEAVALVEDLQKQPVKAWRQDVPSEEAEPEAAGRGSQATGPPPTVGARRRPSVPQEQHSHSAQPPALLKEGRPGETTDTCFVSGVHGPVALGDIPFYFSREEWGTLDPAQRDLFWDIKRENSRNTTLGFGLKGQSEKSLLQEMVPVVPGQTGSDVTVSWSPEEAEAWESENRPRAALGPVVGARRGRPPTRRRQFRDLAAEKPHSCGQCGKRFRWGSDLARHQRTHTGEKPHKCPECDKSFRSSSDLVRHQGVHTGEKPFSCSECGKSFSRSAYLADHQRIHTGEKPFGCSDCGKSFSLRSYLLDHRRVHTGERPFGCGECDKSFKQRAHLIAHQSLHAKMAQPVG
| null | null |
regulation of transcription by RNA polymerase II [GO:0006357]
|
PcG protein complex [GO:0031519]; transcription regulator complex [GO:0005667]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF01352;PF02023;PF00096;PF13465;
|
6.10.140.140;3.30.160.60;1.10.4020.10;
|
Krueppel C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
| null | null | null | null | null |
FUNCTION: May be involved in transcriptional regulation.
|
Homo sapiens (Human)
|
O14772
|
FPGT_HUMAN
|
MRAVRRGLREGGAMAAARDPPEVSLREATQRKLRRFSELRGKLVARGEFWDIVAITAADEKQELAYNQQLSEKLKRKELPLGVQYHVFVDPAGAKIGNGGSTLCALQCLEKLYGDKWNSFTILLIHSGGYSQRLPNASALGKIFTALPLGNPIYQMLELKLAMYIDFPLNMNPGILVTCADDIELYSIGEFEFIRFDKPGFTALAHPSSLTIGTTHGVFVLDPFDDLKHRDLEYRSCHRFLHKPSIEKMYQFNAVCRPGNFCQQDFAGGDIADLKLDSDYVYTDSLFYMDHKSAKMLLAFYEKIGTLSCEIDAYGDFLQALGPGATVEYTRNTSNVIKEESELVEMRQRIFHLLKGTSLNVVVLNNSKFYHIGTTEEYLFYFTSDNSLKSELGLQSITFSIFPDIPECSGKTSCIIQSILDSRCSVAPGSVVEYSRLGPDVSVGENCIISGSYILTKAALPAHSFVCSLSLKMNRCLKYATMAFGVQDNLKKSVKTLSDIKLLQFFGVCFLSCLDVWNLKVTEELFSGNKTCLSLWTARIFPVCSSLSDSVITSLKMLNAVKNKSAFSLNSYKLLSIEEMLIYKDVEDMITYREQIFLEISLKSSLM
|
2.7.7.30
| null |
fucose metabolic process [GO:0006004]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
catalytic activity [GO:0003824]; fucose-1-phosphate guanylyltransferase activity [GO:0047341]; GTP binding [GO:0005525]
|
PF07959;
|
2.160.10.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=beta-L-fucose 1-phosphate + GTP + H(+) = diphosphate + GDP-beta-L-fucose; Xref=Rhea:RHEA:13549, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57268, ChEBI:CHEBI:57273; EC=2.7.7.30; Evidence={ECO:0000269|PubMed:9804772}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13550; Evidence={ECO:0000305|PubMed:9804772};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8 to 7.8. {ECO:0000305|PubMed:9804772};
| null |
FUNCTION: Catalyzes the formation of GDP-L-fucose from GTP and L-fucose-1-phosphate (PubMed:9804772). Functions as a salvage pathway to reutilize L-fucose arising from the turnover of glycoproteins and glycolipids (PubMed:9804772). {ECO:0000269|PubMed:9804772}.
|
Homo sapiens (Human)
|
O14773
|
TPP1_HUMAN
|
MGLQACLLGLFALILSGKCSYSPEPDQRRTLPPGWVSLGRADPEEELSLTFALRQQNVERLSELVQAVSDPSSPQYGKYLTLENVADLVRPSPLTLHTVQKWLLAAGAQKCHSVITQDFLTCWLSIRQAELLLPGAEFHHYVGGPTETHVVRSPHPYQLPQALAPHVDFVGGLHRFPPTSSLRQRPEPQVTGTVGLHLGVTPSVIRKRYNLTSQDVGSGTSNNSQACAQFLEQYFHDSDLAQFMRLFGGNFAHQASVARVVGQQGRGRAGIEASLDVQYLMSAGANISTWVYSSPGRHEGQEPFLQWLMLLSNESALPHVHTVSYGDDEDSLSSAYIQRVNTELMKAAARGLTLLFASGDSGAGCWSVSGRHQFRPTFPASSPYVTTVGGTSFQEPFLITNEIVDYISGGGFSNVFPRPSYQEEAVTKFLSSSPHLPPSSYFNASGRAYPDVAALSDGYWVVSNRVPIPWVSGTSASTPVFGGILSLINEHRILSGRPPLGFLNPRLYQQHGAGLFDVTRGCHESCLDEEVEGQGFCSGPGWDPVTGWGTPNFPALLKTLLNP
|
3.4.14.9
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967};
|
bone resorption [GO:0045453]; central nervous system development [GO:0007417]; epithelial cell differentiation [GO:0030855]; lipid metabolic process [GO:0006629]; lysosomal protein catabolic process [GO:1905146]; lysosome organization [GO:0007040]; nervous system development [GO:0007399]; neuromuscular process controlling balance [GO:0050885]; peptide catabolic process [GO:0043171]; protein catabolic process [GO:0030163]; protein localization to chromosome, telomeric region [GO:0070198]; proteolysis [GO:0006508]
|
extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]; melanosome [GO:0042470]; membrane raft [GO:0045121]; recycling endosome [GO:0055037]
|
endopeptidase activity [GO:0004175]; lysophosphatidic acid binding [GO:0035727]; metal ion binding [GO:0046872]; peptidase activity [GO:0008233]; peptide binding [GO:0042277]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]; sulfatide binding [GO:0120146]; tripeptidyl-peptidase activity [GO:0008240]
|
PF00082;PF09286;
|
3.40.50.200;
| null |
PTM: Activated by autocatalytic proteolytical processing upon acidification (PubMed:11054422, PubMed:19038966, PubMed:19038967). N-glycosylation is required for processing and activity (PubMed:19038966, PubMed:19038967). {ECO:0000269|PubMed:11054422, ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967}.
|
SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:19941651}. Melanosome {ECO:0000269|PubMed:12643545}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000269|PubMed:12643545}.
|
CATALYTIC ACTIVITY: Reaction=Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity.; EC=3.4.14.9; Evidence={ECO:0000269|PubMed:11054422, ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967};
| null | null | null | null |
FUNCTION: Lysosomal serine protease with tripeptidyl-peptidase I activity (PubMed:11054422, PubMed:19038966, PubMed:19038967). May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases (PubMed:11054422, PubMed:19038966, PubMed:19038967). Requires substrates with an unsubstituted N-terminus (PubMed:19038966). {ECO:0000269|PubMed:11054422, ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967}.
|
Homo sapiens (Human)
|
O14775
|
GNB5_HUMAN
|
MCDQTFLVNVFGSCDKCFKQRALRPVFKKSQQLSYCSTCAEIMATEGLHENETLASLKSEAESLKGKLEEERAKLHDVELHQVAERVEALGQFVMKTRRTLKGHGNKVLCMDWCKDKRRIVSSSQDGKVIVWDSFTTNKEHAVTMPCTWVMACAYAPSGCAIACGGLDNKCSVYPLTFDKNENMAAKKKSVAMHTNYLSACSFTNSDMQILTASGDGTCALWDVESGQLLQSFHGHGADVLCLDLAPSETGNTFVSGGCDKKAMVWDMRSGQCVQAFETHESDINSVRYYPSGDAFASGSDDATCRLYDLRADREVAIYSKESIIFGASSVDFSLSGRLLFAGYNDYTINVWDVLKGSRVSILFGHENRVSTLRVSPDGTAFCSGSWDHTLRVWA
| null | null |
dark adaptation [GO:1990603]; dopamine receptor signaling pathway [GO:0007212]; G protein-coupled receptor signaling pathway [GO:0007186]; light adaption [GO:0036367]; negative regulation of voltage-gated calcium channel activity [GO:1901386]; positive regulation of GTPase activity [GO:0043547]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; GTPase activator complex [GO:1902773]; heterotrimeric G-protein complex [GO:0005834]; nucleus [GO:0005634]; presynapse [GO:0098793]
|
G-protein gamma-subunit binding [GO:0031682]; GTPase activator activity [GO:0005096]; GTPase activity [GO:0003924]; protein-folding chaperone binding [GO:0051087]; signaling receptor complex adaptor activity [GO:0030159]
|
PF00400;
|
2.130.10.10;
|
WD repeat G protein beta family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P62881}.
| null | null | null | null | null |
FUNCTION: Enhances GTPase-activating protein (GAP) activity of regulator of G protein signaling (RGS) proteins, such as RGS7 and RGS9, hence involved in the termination of the signaling initiated by the G protein coupled receptors (GPCRs) by accelerating the GTP hydrolysis on the G-alpha subunits, thereby promoting their inactivation (PubMed:27677260). Increases RGS7 GTPase-activating protein (GAP) activity, thereby regulating mood and cognition (By similarity). Increases RGS9 GTPase-activating protein (GAP) activity, hence contributes to the deactivation of G protein signaling initiated by D(2) dopamine receptors (PubMed:27677260). May play an important role in neuronal signaling, including in the parasympathetic, but not sympathetic, control of heart rate (By similarity). {ECO:0000250|UniProtKB:A1L271, ECO:0000250|UniProtKB:P62881, ECO:0000269|PubMed:27677260}.
|
Homo sapiens (Human)
|
O14776
|
TCRG1_HUMAN
|
MAERGGDGGESERFNPGELRMAQQQALRFRGPAPPPNAVMRGPPPLMRPPPPFGMMRGPPPPPRPPFGRPPFDPNMPPMPPPGGIPPPMGPPHLQRPPFMPPPMSSMPPPPGMMFPPGMPPVTAPGTPALPPTEEIWVENKTPDGKVYYYNARTRESAWTKPDGVKVIQQSELTPMLAAQAQVQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQVQAQVQAQVQAQAVGASTPTTSSPAPAVSTSTSSSTPSSTTSTTTTATSVAQTVSTPTTQDQTPSSAVSVATPTVSVSTPAPTATPVQTVPQPHPQTLPPAVPHSVPQPTTAIPAFPPVMVPPFRVPLPGMPIPLPGVAMMQIVSCPYVKTVATTKTGVLPGMAPPIVPMIHPQVAIAASPATLAGATAVSEWTEYKTADGKTYYYNNRTLESTWEKPQELKEKEKLEEKIKEPIKEPSEEPLPMETEEEDPKEEPIKEIKEEPKEEEMTEEEKAAQKAKPVATAPIPGTPWCVVWTGDERVFFYNPTTRLSMWDRPDDLIGRADVDKIIQEPPHKKGMEELKKLRHPTPTMLSIQKWQFSMSAIKEEQELMEEINEDEPVKAKKRKRDDNKDIDSEKEAAMEAEIKAARERAIVPLEARMKQFKDMLLERGVSAFSTWEKELHKIVFDPRYLLLNPKERKQVFDQYVKTRAEEERREKKNKIMQAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAAARKKEKEDSKTRGEKIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYIEKIAKNLDSEKEKELERQARIEASLREREREVQKARSEQTKEIDREREQHKREEAIQNFKALLSDMVRSSDVSWSDTRRTLRKDHRWESGSLLEREEKEKLFNEHIEALTKKKREHFRQLLDETSAITLTSTWKEVKKIIKEDPRCIKFSSSDRKKQREFEEYIRDKYITAKADFRTLLKETKFITYRSKKLIQESDQHLKDVEKILQNDKRYLVLDCVPEERRKLIVAYVDDLDRRGPPPPPTASEPTRRSTK
| null | null |
mRNA processing [GO:0006397]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transcription elongation by RNA polymerase II [GO:0034244]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; RNA splicing [GO:0008380]
|
nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
identical protein binding [GO:0042802]; RNA binding [GO:0003723]; RNA polymerase binding [GO:0070063]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription coactivator activity [GO:0003713]; transcription coregulator activity [GO:0003712]; transcription corepressor activity [GO:0003714]; transcription elongation factor activity [GO:0003711]; ubiquitin-like protein conjugating enzyme binding [GO:0044390]
|
PF01846;PF00397;
|
2.20.70.10;1.10.10.440;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10908677, ECO:0000269|PubMed:15485897, ECO:0000269|PubMed:9315662}.
| null | null | null | null | null |
FUNCTION: Transcription factor that binds RNA polymerase II and inhibits the elongation of transcripts from target promoters. Regulates transcription elongation in a TATA box-dependent manner. Necessary for TAT-dependent activation of the human immunodeficiency virus type 1 (HIV-1) promoter. {ECO:0000269|PubMed:11604498, ECO:0000269|PubMed:9315662}.
|
Homo sapiens (Human)
|
O14777
|
NDC80_HUMAN
|
MKRSSVSSGGAGRLSMQELRSQDVNKQGLYTPQTKEKPTFGKLSINKPTSERKVSLFGKRTSGHGSRNSQLGIFSSSEKIKDPRPLNDKAFIQQCIRQLCEFLTENGYAHNVSMKSLQAPSVKDFLKIFTFLYGFLCPSYELPDTKFEEEVPRIFKDLGYPFALSKSSMYTVGAPHTWPHIVAALVWLIDCIKIHTAMKESSPLFDDGQPWGEETEDGIMHNKLFLDYTIKCYESFMSGADSFDEMNAELQSKLKDLFNVDAFKLESLEAKNRALNEQIARLEQEREKEPNRLESLRKLKASLQGDVQKYQAYMSNLESHSAILDQKLNGLNEEIARVELECETIKQENTRLQNIIDNQKYSVADIERINHERNELQQTINKLTKDLEAEQQKLWNEELKYARGKEAIETQLAEYHKLARKLKLIPKGAENSKGYDFEIKFNPEAGANCLVKYRAQVYVPLKELLNETEEEINKALNKKMGLEDTLEQLNAMITESKRSVRTLKEEVQKLDDLYQQKIKEAEEEDEKCASELESLEKHKHLLESTVNQGLSEAMNELDAVQREYQLVVQTTTEERRKVGNNLQRLLEMVATHVGSVEKHLEEQIAKVDREYEECMSEDLSENIKEIRDKYEKKATLIKSSEE
| null | null |
attachment of mitotic spindle microtubules to kinetochore [GO:0051315]; attachment of spindle microtubules to kinetochore [GO:0008608]; cell division [GO:0051301]; centrosome duplication [GO:0051298]; chromosome segregation [GO:0007059]; establishment of mitotic spindle orientation [GO:0000132]; G2/MI transition of meiotic cell cycle [GO:0008315]; kinetochore organization [GO:0051383]; metaphase chromosome alignment [GO:0051310]; mitotic cell cycle [GO:0000278]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle assembly checkpoint signaling [GO:0007094]; mitotic spindle organization [GO:0007052]; positive regulation of mitotic cell cycle spindle assembly checkpoint [GO:0090267]; regulation of protein stability [GO:0031647]; skeletal muscle satellite cell proliferation [GO:0014841]; spindle assembly involved in female meiosis I [GO:0007057]
|
centrosome [GO:0005813]; chromosome, centromeric region [GO:0000775]; cytosol [GO:0005829]; kinetochore [GO:0000776]; membrane [GO:0016020]; Ndc80 complex [GO:0031262]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; outer kinetochore [GO:0000940]
|
cyclin binding [GO:0030332]; identical protein binding [GO:0042802]; kinetochore adaptor activity [GO:0140483]; microtubule binding [GO:0008017]
|
PF18077;PF03801;
|
6.10.250.1950;1.10.418.30;
|
NDC80/HEC1 family
|
PTM: Phosphorylation begins in S phase of the cell cycle and peaks in mitosis. Phosphorylated by NEK2. Also phosphorylated by AURKA and AURKB. {ECO:0000269|PubMed:12386167, ECO:0000269|PubMed:14602875, ECO:0000269|PubMed:30409912}.; PTM: Acetylated at Lys-53 and Lys-59 by KAT5 during mitosis, promoting robust kinetochore-microtubule attachment (PubMed:30409912). Deacetylated by SIRT1 (PubMed:30409912). {ECO:0000269|PubMed:30409912}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9315664}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:14699129}. Note=Localizes to kinetochores from late prophase to anaphase (PubMed:14699129). Localizes specifically to the outer plate of the kinetochore (PubMed:14699129). {ECO:0000269|PubMed:14699129}.
| null | null | null | null | null |
FUNCTION: Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity (PubMed:12351790, PubMed:14654001, PubMed:14699129, PubMed:15062103, PubMed:15235793, PubMed:15239953, PubMed:15548592, PubMed:16732327, PubMed:30409912, PubMed:9315664). Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore (PubMed:15548592, PubMed:30409912). The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules (PubMed:23085020). Plays a role in chromosome congression and is essential for the end-on attachment of the kinetochores to spindle microtubules (PubMed:23891108, PubMed:25743205). {ECO:0000269|PubMed:12351790, ECO:0000269|PubMed:14654001, ECO:0000269|PubMed:14699129, ECO:0000269|PubMed:15062103, ECO:0000269|PubMed:15235793, ECO:0000269|PubMed:15239953, ECO:0000269|PubMed:15548592, ECO:0000269|PubMed:16732327, ECO:0000269|PubMed:23085020, ECO:0000269|PubMed:23891108, ECO:0000269|PubMed:25743205, ECO:0000269|PubMed:30409912, ECO:0000269|PubMed:9315664}.
|
Homo sapiens (Human)
|
O14782
|
KIF3C_HUMAN
|
MASKTKASEALKVVARCRPLSRKEEAAGHEQILTMDVKLGQVTLRNPRAAPGELPKTFTFDAVYDASSKQADLYDETVRPLIDSVLQGFNGTVFAYGQTGTGKTYTMQGTWVEPELRGVIPNAFEHIFTHISRSQNQQYLVRASYLEIYQEEIRDLLSKEPGKRLELKENPETGVYIKDLSSFVTKNVKEIEHVMNLGNQTRAVGSTHMNEVSSRSHAIFIITVECSERGSDGQDHIRVGKLNLVDLAGSERQNKAGPNTAGGAATPSSGGGGGGGGSGGGAGGERPKEASKINLSLSALGNVIAALAGNRSTHIPYRDSKLTRLLQDSLGGNAKTIMVATLGPASHSYDESLSTLRFANRAKNIKNKPRVNEDPKDTLLREFQEEIARLKAQLEKRGMLGKRPRRKSSRRKKAVSAPPGYPEGPVIEAWVAEEEDDNNNNHRPPQPILESALEKNMENYLQEQKERLEEEKAAIQDDRSLVSEEKQKLLEEKEKMLEDLRREQQATELLAAKYKAMESKLLIGGRNIMDHTNEQQKMLELKRQEIAEQKRREREMQQEMMLRDEETMELRGTYTSLQQEVEVKTKKLKKLYAKLQAVKAEIQDQHDEYIRVRQDLEEAQNEQTRELKLKYLIIENFIPPEEKNKIMNRLFLDCEEEQWKFQPLVPAGVSSSQMKKRPTSAVGYKRPISQYARVAMAMGSHPRYRAENIMFLELDVSPPAVFEMEFSHDQEQDPRALHMERLMRLDSFLERPSTSKVRKSRSWCQSPQRPPPSTTHASLASASLRPATVADHE
| null | null |
microtubule-based movement [GO:0007018]; mitotic cell cycle [GO:0000278]
|
ciliary tip [GO:0097542]; cilium [GO:0005929]; cytosol [GO:0005829]; kinesin complex [GO:0005871]; microtubule [GO:0005874]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cytoskeletal motor activity [GO:0003774]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]
|
PF00225;
|
3.40.850.10;
|
TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, Kinesin II subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Microtubule-based anterograde translocator for membranous organelles. {ECO:0000250}.
|
Homo sapiens (Human)
|
O14786
|
NRP1_HUMAN
|
MERGLPLLCAVLALVLAPAGAFRNDKCGDTIKIESPGYLTSPGYPHSYHPSEKCEWLIQAPDPYQRIMINFNPHFDLEDRDCKYDYVEVFDGENENGHFRGKFCGKIAPPPVVSSGPFLFIKFVSDYETHGAGFSIRYEIFKRGPECSQNYTTPSGVIKSPGFPEKYPNSLECTYIVFVPKMSEIILEFESFDLEPDSNPPGGMFCRYDRLEIWDGFPDVGPHIGRYCGQKTPGRIRSSSGILSMVFYTDSAIAKEGFSANYSVLQSSVSEDFKCMEALGMESGEIHSDQITASSQYSTNWSAERSRLNYPENGWTPGEDSYREWIQVDLGLLRFVTAVGTQGAISKETKKKYYVKTYKIDVSSNGEDWITIKEGNKPVLFQGNTNPTDVVVAVFPKPLITRFVRIKPATWETGISMRFEVYGCKITDYPCSGMLGMVSGLISDSQITSSNQGDRNWMPENIRLVTSRSGWALPPAPHSYINEWLQIDLGEEKIVRGIIIQGGKHRENKVFMRKFKIGYSNNGSDWKMIMDDSKRKAKSFEGNNNYDTPELRTFPALSTRFIRIYPERATHGGLGLRMELLGCEVEAPTAGPTTPNGNLVDECDDDQANCHSGTGDDFQLTGGTTVLATEKPTVIDSTIQSEFPTYGFNCEFGWGSHKTFCHWEHDNHVQLKWSVLTSKTGPIQDHTGDGNFIYSQADENQKGKVARLVSPVVYSQNSAHCMTFWYHMSGSHVGTLRVKLRYQKPEEYDQLVWMAIGHQGDHWKEGRVLLHKSLKLYQVIFEGEIGKGNLGGIAVDDISINNHISQEDCAKPADLDKKNPEIKIDETGSTPGYEGEGEGDKNISRKPGNVLKTLDPILITIIAMSALGVLLGAVCGVVLYCACWHNGMSERNLSALENYNFELVDGVKLKKDKLNTQSTYSEA
| null | null |
angiogenesis [GO:0001525]; angiogenesis involved in coronary vascular morphogenesis [GO:0060978]; animal organ morphogenesis [GO:0009887]; artery morphogenesis [GO:0048844]; axon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; axonal fasciculation [GO:0007413]; axonogenesis involved in innervation [GO:0060385]; basal dendrite arborization [GO:0150020]; basal dendrite development [GO:0150018]; branching involved in blood vessel morphogenesis [GO:0001569]; branchiomotor neuron axon guidance [GO:0021785]; cell migration involved in sprouting angiogenesis [GO:0002042]; cell-cell signaling [GO:0007267]; cellular response to hepatocyte growth factor stimulus [GO:0035729]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; commissural neuron axon guidance [GO:0071679]; coronary artery morphogenesis [GO:0060982]; dichotomous subdivision of terminal units involved in salivary gland branching [GO:0060666]; dorsal root ganglion morphogenesis [GO:1904835]; endothelial cell chemotaxis [GO:0035767]; endothelial tip cell fate specification [GO:0097102]; facial nerve structural organization [GO:0021612]; facioacoustic ganglion development [GO:1903375]; gonadotrophin-releasing hormone neuronal migration to the hypothalamus [GO:0021828]; hepatocyte growth factor receptor signaling pathway [GO:0048012]; integrin-mediated signaling pathway [GO:0007229]; motor neuron axon guidance [GO:0008045]; motor neuron migration [GO:0097475]; negative regulation of axon extension involved in axon guidance [GO:0048843]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of neuron apoptotic process [GO:0043524]; neural crest cell migration [GO:0001755]; neural crest cell migration involved in autonomic nervous system development [GO:1901166]; neuron migration [GO:0001764]; neuropilin signaling pathway [GO:0038189]; otic placode development [GO:1905040]; outflow tract septum morphogenesis [GO:0003148]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive chemotaxis [GO:0050918]; positive regulation of angiogenesis [GO:0045766]; positive regulation of axon extension involved in axon guidance [GO:0048842]; positive regulation of cell migration involved in sprouting angiogenesis [GO:0090050]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of filopodium assembly [GO:0051491]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of smooth muscle cell migration [GO:0014911]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; postsynapse organization [GO:0099173]; protein localization to early endosome [GO:1902946]; regulation of Cdc42 protein signal transduction [GO:0032489]; regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030947]; regulation of vesicle-mediated transport [GO:0060627]; renal artery morphogenesis [GO:0061441]; response to wounding [GO:0009611]; retina vasculature morphogenesis in camera-type eye [GO:0061299]; retinal ganglion cell axon guidance [GO:0031290]; semaphorin-plexin signaling pathway [GO:0071526]; sensory neuron axon guidance [GO:0097374]; signal transduction [GO:0007165]; sprouting angiogenesis [GO:0002040]; substrate-dependent cell migration, cell extension [GO:0006930]; symbiont entry into host cell [GO:0046718]; sympathetic ganglion development [GO:0061549]; sympathetic neuron projection extension [GO:0097490]; sympathetic neuron projection guidance [GO:0097491]; trigeminal ganglion development [GO:0061551]; trigeminal nerve structural organization [GO:0021637]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; vasculogenesis [GO:0001570]; VEGF-activated neuropilin signaling pathway [GO:0038190]; ventral trunk neural crest cell migration [GO:0036486]; vestibulocochlear nerve structural organization [GO:0021649]
|
axon [GO:0030424]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; early endosome [GO:0005769]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; glutamatergic synapse [GO:0098978]; mitochondrial membrane [GO:0031966]; neurofilament [GO:0005883]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; receptor complex [GO:0043235]; semaphorin receptor complex [GO:0002116]; sorting endosome [GO:0097443]
|
coreceptor activity [GO:0015026]; cytokine binding [GO:0019955]; growth factor binding [GO:0019838]; GTPase activator activity [GO:0005096]; heparin binding [GO:0008201]; metal ion binding [GO:0046872]; protein kinase binding [GO:0019901]; semaphorin receptor activity [GO:0017154]; vascular endothelial growth factor binding [GO:0038085]; vascular endothelial growth factor receptor activity [GO:0005021]
|
PF00431;PF11980;PF00754;PF00629;
|
2.60.120.200;2.60.120.260;2.60.120.290;
|
Neuropilin family
| null |
SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:10688880}.; SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305|PubMed:30623799}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:30623799}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:30623799}.
| null | null | null | null | null |
FUNCTION: Cell-surface receptor involved in the development of the cardiovascular system, in angiogenesis, in the formation of certain neuronal circuits and in organogenesis outside the nervous system. Mediates the chemorepulsant activity of semaphorins (PubMed:10688880, PubMed:9288753, PubMed:9529250). Recognizes a C-end rule (CendR) motif R/KXXR/K on its ligands which causes cellular internalization and vascular leakage (PubMed:19805273). It binds to semaphorin 3A, the PLGF-2 isoform of PGF, the VEGF165 isoform of VEGFA and VEGFB (PubMed:10688880, PubMed:19805273, PubMed:9288753, PubMed:9529250). Coexpression with KDR results in increased VEGF165 binding to KDR as well as increased chemotaxis. Regulates VEGF-induced angiogenesis. Binding to VEGFA initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development (By similarity). Regulates mitochondrial iron transport via interaction with ABCB8/MITOSUR (PubMed:30623799). {ECO:0000250|UniProtKB:P97333, ECO:0000269|PubMed:10688880, ECO:0000269|PubMed:19805273, ECO:0000269|PubMed:30623799, ECO:0000269|PubMed:9288753, ECO:0000269|PubMed:9529250}.; FUNCTION: (Microbial infection) Acts as a host factor for human coronavirus SARS-CoV-2 infection. Recognizes and binds to CendR motif RRAR on SARS-CoV-2 spike protein S1 which enhances SARS-CoV-2 infection. {ECO:0000269|PubMed:33082293, ECO:0000269|PubMed:33082294}.; FUNCTION: [Isoform 2]: Binds VEGF-165 and may inhibit its binding to cells (PubMed:10748121, PubMed:26503042). May induce apoptosis by sequestering VEGF-165 (PubMed:10748121). May bind as well various members of the semaphorin family. Its expression has an averse effect on blood vessel number and integrity. {ECO:0000269|PubMed:10748121, ECO:0000269|PubMed:26503042}.
|
Homo sapiens (Human)
|
O14787
|
TNPO2_HUMAN
|
MDWQPDEQGLQQVLQLLKDSQSPNTATQRIVQDKLKQLNQFPDFNNYLIFVLTRLKSEDEPTRSLSGLILKNNVKAHYQSFPPPVADFIKQECLNNIGDASSLIRATIGILITTIASKGELQMWPELLPQLCNLLNSEDYNTCEGAFGALQKICEDSSELLDSDALNRPLNIMIPKFLQFFKHCSPKIRSHAIACVNQFIMDRAQALMDNIDTFIEHLFALAVDDDPEVRKNVCRALVMLLEVRIDRLIPHMHSIIQYMLQRTQDHDENVALEACEFWLTLAEQPICKEVLASHLVQLIPILVNGMKYSEIDIILLKGDVEEDEAVPDSEQDIKPRFHKSRTVTLPHEAERPDGSEDAEDDDDDDALSDWNLRKCSAAALDVLANVFREELLPHLLPLLKGLLFHPEWVVKESGILVLGAIAEGCMQGMVPYLPELIPHLIQCLSDKKALVRSIACWTLSRYAHWVVSQPPDMHLKPLMTELLKRILDGNKRVQEAACSAFATLEEEACTELVPYLSYILDTLVFAFGKYQHKNLLILYDAIGTLADSVGHHLNQPEYIQKLMPPLIQKWNELKDEDKDLFPLLECLSSVATALQSGFLPYCEPVYQRCVTLVQKTLAQAMMYTQHPEQYEAPDKDFMIVALDLLSGLAEGLGGHVEQLVARSNIMTLLFQCMQDSMPEVRQSSFALLGDLTKACFIHVKPCIAEFMPILGTNLNPEFISVCNNATWAIGEICMQMGAEMQPYVQMVLNNLVEIINRPNTPKTLLENTGRLTSPSAIPAITIGRLGYVCPQEVAPMLQQFIRPWCTSLRNIRDNEEKDSAFRGICMMIGVNPGGVVQDFIFFCDAVASWVSPKDDLRDMFYKILHGFKDQVGEDNWQQFSEQFPPLLKERLAAFYGV
| null | null |
protein import into nucleus [GO:0006606]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139]; small GTPase binding [GO:0031267]
|
PF02985;PF13513;PF03810;
|
1.25.10.10;
|
Importin beta family, Importin beta-2 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Probably functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O14788
|
TNF11_HUMAN
|
MRRASRDYTKYLRGSEEMGGGPGAPHEGPLHAPPPPAPHQPPAASRSMFVALLGLGLGQVVCSVALFFYFRAQMDPNRISEDGTHCIYRILRLHENADFQDTTLESQDTKLIPDSCRRIKQAFQGAVQKELQHIVGSQHIRAEKAMVDGSWLDLAKRSKLEAQPFAHLTINATDIPSGSHKVSLSSWYHDRGWAKISNMTFSNGKLIVNQDGFYYLYANICFRHHETSGDLATEYLQLMVYVTKTSIKIPSSHTLMKGGSTKYWSGNSEFHFYSINVGGFFKLRSGEEISIEVSNPSLLDPDQDATYFGAFKVRDID
| null | null |
bone resorption [GO:0045453]; calcium ion homeostasis [GO:0055074]; calcium-mediated signaling [GO:0019722]; cellular response to leukemia inhibitory factor [GO:1990830]; cytokine-mediated signaling pathway [GO:0019221]; ERK1 and ERK2 cascade [GO:0070371]; immune response [GO:0006955]; JNK cascade [GO:0007254]; mammary gland alveolus development [GO:0060749]; mammary gland epithelial cell proliferation [GO:0033598]; monocyte chemotaxis [GO:0002548]; negative regulation of transcription by RNA polymerase II [GO:0000122]; ossification [GO:0001503]; osteoclast development [GO:0036035]; osteoclast differentiation [GO:0030316]; osteoclast proliferation [GO:0002158]; paracrine signaling [GO:0038001]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; positive regulation of bone resorption [GO:0045780]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of corticotropin-releasing hormone secretion [GO:0051466]; positive regulation of DNA-binding transcription factor activity [GO:0051091]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of fever generation by positive regulation of prostaglandin secretion [GO:0071812]; positive regulation of gene expression [GO:0010628]; positive regulation of homotypic cell-cell adhesion [GO:0034112]; positive regulation of intracellular signal transduction [GO:1902533]; positive regulation of JNK cascade [GO:0046330]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of osteoclast development [GO:2001206]; positive regulation of osteoclast differentiation [GO:0045672]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of T cell activation [GO:0050870]; positive regulation of transcription by RNA polymerase II [GO:0045944]; tooth eruption [GO:0044691]; tumor necrosis factor-mediated signaling pathway [GO:0033209]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
cytokine activity [GO:0005125]; identical protein binding [GO:0042802]; tumor necrosis factor receptor binding [GO:0005164]; tumor necrosis factor receptor superfamily binding [GO:0032813]
|
PF00229;
|
2.60.120.40;
|
Tumor necrosis factor family
|
PTM: The soluble form of isoform 1 derives from the membrane form by proteolytic processing (By similarity). The cleavage may be catalyzed by ADAM17. {ECO:0000250}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member 11, soluble form]: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Cytokine that binds to TNFRSF11B/OPG and to TNFRSF11A/RANK. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive T-cell proliferation. May be an important regulator of interactions between T-cells and dendritic cells and may play a role in the regulation of the T-cell-dependent immune response. May also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy (PubMed:22664871). Induces osteoclastogenesis by activating multiple signaling pathways in osteoclast precursor cells, chief among which is induction of long lasting oscillations in the intracellular concentration of Ca (2+) resulting in the activation of NFATC1, which translocates to the nucleus and induces osteoclast-specific gene transcription to allow differentiation of osteoclasts. During osteoclast differentiation, in a TMEM64 and ATP2A2-dependent manner induces activation of CREB1 and mitochondrial ROS generation necessary for proper osteoclast generation (By similarity). {ECO:0000250|UniProtKB:O35235, ECO:0000269|PubMed:22664871}.
|
Homo sapiens (Human)
|
O14791
|
APOL1_HUMAN
|
MEGAALLRVSVLCIWMSALFLGVGVRAEEAGARVQQNVPSGTDTGDPQSKPLGDWAAGTMDPESSIFIEDAIKYFKEKVSTQNLLLLLTDNEAWNGFVAAAELPRNEADELRKALDNLARQMIMKDKNWHDKGQQYRNWFLKEFPRLKSELEDNIRRLRALADGVQKVHKGTTIANVVSGSLSISSGILTLVGMGLAPFTEGGSLVLLEPGMELGITAALTGITSSTMDYGKKWWTQAQAHDLVIKSLDKLKEVREFLGENISNFLSLAGNTYQLTRGIGKDIRALRRARANLQSVPHASASRPRVTEPISAESGEQVERVNEPSILEMSRGVKLTDVAPVSFFLVLDVVYLVYESKHLHEGAKSETAEELKKVAQELEEKLNILNNNYKILQADQEL
| null | null |
chloride transmembrane transport [GO:1902476]; cholesterol metabolic process [GO:0008203]; cytolysis by host of symbiont cells [GO:0051838]; innate immune response [GO:0045087]; lipid transport [GO:0006869]; lipoprotein metabolic process [GO:0042157]
|
blood microparticle [GO:0072562]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; membrane [GO:0016020]; very-low-density lipoprotein particle [GO:0034361]
|
chloride channel activity [GO:0005254]; lipid binding [GO:0008289]
|
PF05461;
| null |
Apolipoprotein L family
|
PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000269|PubMed:26091039}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: May play a role in lipid exchange and transport throughout the body. May participate in reverse cholesterol transport from peripheral cells to the liver.
|
Homo sapiens (Human)
|
O14792
|
HS3S1_HUMAN
|
MAALLLGAVLLVAQPQLVPSRPAELGQQELLRKAGTLQDDVRDGVAPNGSAQQLPQTIIIGVRKGGTRALLEMLSLHPDVAAAENEVHFFDWEEHYSHGLGWYLSQMPFSWPHQLTVEKTPAYFTSPKVPERVYSMNPSIRLLLILRDPSERVLSDYTQVFYNHMQKHKPYPSIEEFLVRDGRLNVDYKALNRSLYHVHMQNWLRFFPLRHIHIVDGDRLIRDPFPEIQKVERFLKLSPQINASNFYFNKTKGFYCLRDSGRDRCLHESKGRAHPQVDPKLLNKLHEYFHEPNKKFFELVGRTFDWH
|
2.8.2.23
| null |
glycosaminoglycan biosynthetic process [GO:0006024]; heparan sulfate proteoglycan biosynthetic process, enzymatic modification [GO:0015015]
|
Golgi lumen [GO:0005796]
|
[heparan sulfate]-glucosamine 3-sulfotransferase 1 activity [GO:0008467]; sulfotransferase activity [GO:0008146]
|
PF00685;
|
3.40.50.300;
|
Sulfotransferase 1 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus lumen {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan sulfate](n) = 3-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:15461, Rhea:RHEA-COMP:9830, Rhea:RHEA-COMP:9831, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:58388, ChEBI:CHEBI:70975; EC=2.8.2.23; Evidence={ECO:0000269|PubMed:8900198, ECO:0000269|PubMed:9988768};
| null | null | null | null |
FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to position 3 of glucosamine residues in heparan (PubMed:8900198, PubMed:9346953, PubMed:9988768). Catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact) (PubMed:8900198, PubMed:9988768). This modification is a crucial step in the biosynthesis of anticoagulant heparan sulfate as it completes the structure of the antithrombin pentasaccharide binding site (PubMed:8900198, PubMed:9988768). {ECO:0000269|PubMed:8900198, ECO:0000269|PubMed:9346953, ECO:0000269|PubMed:9988768}.
|
Homo sapiens (Human)
|
O14793
|
GDF8_HUMAN
|
MQKLQLCVYIYLFMLIVAGPVDLNENSEQKENVEKEGLCNACTWRQNTKSSRIEAIKIQILSKLRLETAPNISKDVIRQLLPKAPPLRELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDFLMQVDGKPKCCFFKFSSKIQYNKVVKAQLWIYLRPVETPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPGPGEDGLNPFLEVKVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS
| null | null |
cellular response to dexamethasone stimulus [GO:0071549]; cellular response to hypoxia [GO:0071456]; muscle cell cellular homeostasis [GO:0046716]; muscle organ development [GO:0007517]; myoblast migration involved in skeletal muscle regeneration [GO:0014839]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of muscle hypertrophy [GO:0014741]; negative regulation of myoblast differentiation [GO:0045662]; negative regulation of myoblast proliferation [GO:2000818]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative regulation of satellite cell differentiation [GO:1902725]; negative regulation of skeletal muscle satellite cell proliferation [GO:1902723]; negative regulation of skeletal muscle tissue growth [GO:0048632]; ovulation cycle process [GO:0022602]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of lamellipodium assembly [GO:0010592]; positive regulation of macrophage chemotaxis [GO:0010759]; response to electrical stimulus [GO:0051602]; response to estrogen [GO:0043627]; response to ethanol [GO:0045471]; response to gravity [GO:0009629]; response to muscle activity [GO:0014850]; response to testosterone [GO:0033574]; skeletal muscle atrophy [GO:0014732]; skeletal muscle satellite cell differentiation [GO:0014816]; transforming growth factor beta receptor signaling pathway [GO:0007179]
|
extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; signaling receptor binding [GO:0005102]
|
PF00019;PF00688;
|
2.60.120.970;2.10.90.10;
|
TGF-beta family
|
PTM: Synthesized as large precursor molecule that undergoes proteolytic cleavage to generate an N-terminal propeptide and a disulfide linked C-terminal dimer, which is the biologically active molecule. The circulating form consists of a latent complex of the C-terminal dimer and other proteins, including its propeptide, which maintain the C-terminal dimer in a latent, inactive state. Ligand activation requires additional cleavage of the prodomain by a tolloid-like metalloproteinase. {ECO:0000250|UniProtKB:O08689}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O08689}.
| null | null | null | null | null |
FUNCTION: Acts specifically as a negative regulator of skeletal muscle growth. {ECO:0000250|UniProtKB:O08689}.
|
Homo sapiens (Human)
|
O14795
|
UN13B_HUMAN
|
MSLLCVRVKRAKFQGSPDKFNTYVTLKVQNVKSTTVAVRGDQPSWEQDFMFEISRLDLGLSVEVWNKGLIWDTMVGTVWIALKTIRQSDEEGPGEWSTLEAETLMKDDEICGTRNPTPHKILLDTRFELPFDIPEEEARYWTYKWEQINALGADNEYSSQEESQRKPLPTAAAQCSFEDPDSAVDDRDSDYRSETSNSFPPPYHTASQPNASVHQFPVPVRSPQQLLLQGSSRDSCNDSMQSYDLDYPERRAISPTSSSRYGSSCNVSQGSSQLSELDQYHEQDDDHRETDSIHSCHSSHSLSRDGQAGFGEQEKPLEVTGQAEKEAACEPKEMKEDATTHPPPDLVLQKDHFLGPQESFPEENASSPFTQARAHWIRAVTKVRLQLQEIPDDGDPSLPQWLPEGPAGGLYGIDSMPDLRRKKPLPLVSDLSLVQSRKAGITSAMATRTSLKDEELKSHVYKKTLQALIYPISCTTPHNFEVWTATTPTYCYECEGLLWGIARQGMRCSECGVKCHEKCQDLLNADCLQRAAEKSCKHGAEDRTQNIIMAMKDRMKIRERNKPEIFEVIRDVFTVNKAAHVQQMKTVKQSVLDGTSKWSAKITITVVCAQGLQAKDKTGSSDPYVTVQVSKTKKRTKTIFGNLNPVWEEKFHFECHNSSDRIKVRVWDEDDDIKSRVKQRLKRESDDFLGQTIIEVRTLSGEMDVWYNLEKRTDKSAVSGAIRLQISVEIKGEEKVAPYHVQYTCLHENLFHYLTDIQGSGGVRIPEARGDDAWKVYFDETAQEIVDEFAMRYGIESIYQAMTHFACLSSKYMCPGVPAVMSTLLANINAYYAHTTASTNVSASDRFAASNFGKERFVKLLDQLHNSLRIDLSTYRNNFPAGSPERLQDLKSTVDLLTSITFFRMKVQELQSPPRASQVVKDCVKACLNSTYEYIFNNCHDLYSRQYQLKQELPPEEQGPSIRNLDFWPKLITLIVSIIEEDKNSYTPVLNQFPQELNVGKVSAEVMWHLFAQDMKYALEEHEKDHLCKSADYMNLHFKVKWLHNEYVRDLPVLQGQVPEYPAWFEQFVLQWLDENEDVSLEFLRGALERDKKDGFQQTSEHALFSCSVVDVFTQLNQSFEIIRKLECPDPSILAHYMRRFAKTIGKVLMQYADILSKDFPAYCTKEKLPCILMNNVQQLRVQLEKMFEAMGGKELDLEAADSLKELQVKLNTVLDELSMVFGNSFQVRIDECVRQMADILGQVRGTGNASPDARASAAQDADSVLRPLMDFLDGNLTLFATVCEKTVLKRVLKELWRVVMNTMERMIVLPPLTDQTGTQLIFTAAKELSHLSKLKDHMVREETRNLTPKQCAVLDLALDTIKQYFHAGGNGLKKTFLEKSPDLQSLRYALSLYTQTTDTLIKTFVRSQTTQGSGVDDPVGEVSIQVDLFTHPGTGEHKVTVKVVAANDLKWQTAGMFRPFVEVTMVGPHQSDKKRKFTTKSKSNNWAPKYNETFHFLLGNEEGPESYELQICVKDYCFAREDRVLGLAVMPLRDVTAKGSCACWCPLGRKIHMDETGLTILRILSQRSNDEVAREFVKLKSESRSTEEGS
| null |
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
|
acrosomal vesicle exocytosis [GO:0060478]; cellular response to glucose stimulus [GO:0071333]; chemical synaptic transmission [GO:0007268]; dense core granule priming [GO:0061789]; neuromuscular junction development [GO:0007528]; neuronal dense core vesicle exocytosis [GO:0099011]; positive regulation of apoptotic process [GO:0043065]; positive regulation of inhibitory postsynaptic potential [GO:0097151]; positive regulation of protein secretion [GO:0050714]; positive regulation of synaptic vesicle priming [GO:0010808]; presynaptic dense core vesicle exocytosis [GO:0099525]; synaptic transmission, glutamatergic [GO:0035249]; synaptic vesicle docking [GO:0016081]; synaptic vesicle maturation [GO:0016188]; synaptic vesicle priming [GO:0016082]
|
cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; presynaptic active zone [GO:0048786]; presynaptic active zone cytoplasmic component [GO:0098831]; presynaptic membrane [GO:0042734]; synaptic vesicle membrane [GO:0030672]; terminal bouton [GO:0043195]
|
calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; diacylglycerol binding [GO:0019992]; GTP-dependent protein binding [GO:0030742]; phospholipid binding [GO:0005543]; small GTPase binding [GO:0031267]; syntaxin-1 binding [GO:0017075]
|
PF00130;PF00168;PF06292;
|
1.10.357.50;1.20.58.1100;3.30.60.20;2.60.40.150;
|
Unc-13 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}. Synapse {ECO:0000250}. Note=Localized to synapses. Translocated to the plasma membrane in response to phorbol ester binding (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-depending refilling of readily releasable vesicle pool (RRP) (By similarity). Essential for synaptic vesicle maturation in a subset of excitatory/glutamatergic but not inhibitory/GABA-mediated synapses (By similarity). In collaboration with UNC13A, facilitates neuronal dense core vesicles fusion as well as controls the location and efficiency of their synaptic release (By similarity). {ECO:0000250|UniProtKB:Q9Z1N9}.
|
Homo sapiens (Human)
|
O14796
|
SH21B_HUMAN
|
MDLPYYHGRLTKQDCETLLLKEGVDGNFLLRDSESIPGVLCLCVSFKNIVYTYRIFREKHGYYRIQTAEGSPKQVFPSLKELISKFEKPNQGMVVHLLKPIKRTSPSLRWRGLKLELETFVNSNSDYVDVLP
| null | null |
adaptive immune response [GO:0002250]; innate immune response [GO:0045087]; leukocyte activation involved in immune response [GO:0002366]; negative regulation of bone resorption [GO:0045779]; negative regulation of neutrophil differentiation [GO:0045659]; negative regulation of signal transduction [GO:0009968]; positive regulation of B cell differentiation [GO:0045579]; positive regulation of innate immune response [GO:0045089]; positive regulation of natural killer cell mediated immunity [GO:0002717]
|
cytosol [GO:0005829]
|
protein-macromolecule adaptor activity [GO:0030674]
|
PF00017;
|
3.30.505.10;
| null | null | null | null | null | null | null | null |
FUNCTION: Cytoplasmic adapter regulating receptors of the signaling lymphocytic activation molecule (SLAM) family such as CD84, SLAMF1, LY9 and CD244 (PubMed:11689425). In SLAM signaling seems to cooperate with SH2D1A/SAP. Plays a role in regulation of effector functions of natural killer (NK) cells by controlling signal transduction through CD244/2B4 without effecting its tyrosine phosphorylation; downstream signaling involves PLCG1 and ERK activation (PubMed:24687958). Activation of SLAMF7-mediated NK cell function does not effect receptor tyrosine phosphorylation but distal signaling (By similarity). In the context of NK cell-mediated cytotoxicity does not enhance conjugate formation with target cells but stimulates polarization of the microtubule-organizing center and cytotoxic granules toward the NK cell synapse (PubMed:24687958). Negatively regulates CD40-induced cytokine production in dendritic cells downstream of SLAM family receptors probably by inducing activation of the PI3K pathway to inhibit p38 MAPK and JNK activation (By similarity). {ECO:0000250|UniProtKB:O35324, ECO:0000269|PubMed:11689425, ECO:0000269|PubMed:24687958, ECO:0000305|PubMed:21219180}.
|
Homo sapiens (Human)
|
O14798
|
TR10C_HUMAN
|
MARIPKTLKFVVVIVAVLLPVLAYSATTARQEEVPQQTVAPQQQRHSFKGEECPAGSHRSEHTGACNPCTEGVDYTNASNNEPSCFPCTVCKSDQKHKSSCTMTRDTVCQCKEGTFRNENSPEMCRKCSRCPSGEVQVSNCTSWDDIQCVEEFGANATVETPAAEETMNTSPGTPAPAAEETMNTSPGTPAPAAEETMTTSPGTPAPAAEETMTTSPGTPAPAAEETMITSPGTPASSHYLSCTIVGIIVLIVLLIVFV
| null | null |
positive regulation of apoptotic process [GO:0043065]; TRAIL-activated apoptotic signaling pathway [GO:0036462]
|
cell surface [GO:0009986]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
|
TRAIL binding [GO:0045569]; transmembrane signaling receptor activity [GO:0004888]
|
PF00020;
|
2.10.50.10;
| null |
PTM: N-glycosylated and O-glycosylated.
|
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
| null | null | null | null | null |
FUNCTION: Receptor for the cytotoxic ligand TRAIL. Lacks a cytoplasmic death domain and hence is not capable of inducing apoptosis. May protect cells against TRAIL mediated apoptosis by competing with TRAIL-R1 and R2 for binding to the ligand.
|
Homo sapiens (Human)
|
O14802
|
RPC1_HUMAN
|
MVKEQFRETDVAKKISHICFGMKSPEEMRQQAHIQVVSKNLYSQDNQHAPLLYGVLDHRMGTSEKDRPCETCGKNLADCLGHYGYIDLELPCFHVGYFRAVIGILQMICKTCCHIMLSQEEKKQFLDYLKRPGLTYLQKRGLKKKISDKCRKKNICHHCGAFNGTVKKCGLLKIIHEKYKTNKKVVDPIVSNFLQSFETAIEHNKEVEPLLGRAQENLNPLVVLNLFKRIPAEDVPLLLMNPEAGKPSDLILTRLLVPPLCIRPSVVSDLKSGTNEDDLTMKLTEIIFLNDVIKKHRISGAKTQMIMEDWDFLQLQCALYINSELSGIPLNMAPKKWTRGFVQRLKGKQGRFRGNLSGKRVDFSGRTVISPDPNLRIDEVAVPVHVAKILTFPEKVNKANINFLRKLVQNGPEVHPGANFIQQRHTQMKRFLKYGNREKMAQELKYGDIVERHLIDGDVVLFNRQPSLHKLSIMAHLARVKPHRTFRFNECVCTPYNADFDGDEMNLHLPQTEEAKAEALVLMGTKANLVTPRNGEPLIAAIQDFLTGAYLLTLKDTFFDRAKACQIIASILVGKDEKIKVRLPPPTILKPVTLWTGKQIFSVILRPSDDNPVRANLRTKGKQYCGKGEDLCANDSYVTIQNSELMSGSMDKGTLGSGSKNNIFYILLRDWGQNEAADAMSRLARLAPVYLSNRGFSIGIGDVTPGQGLLKAKYELLNAGYKKCDEYIEALNTGKLQQQPGCTAEETLEALILKELSVIRDHAGSACLRELDKSNSPLTMALCGSKGSFINISQMIACVGQQAISGSRVPDGFENRSLPHFEKHSKLPAAKGFVANSFYSGLTPTEFFFHTMAGREGLVDTAVKTAETGYMQRRLVKSLEDLCSQYDLTVRSSTGDIIQFIYGGDGLDPAAMEGKDEPLEFKRVLDNIKAVFPCPSEPALSKNELILTTESIMKKSEFLCCQDSFLQEIKKFIKGVSEKIKKTRDKYGINDNGTTEPRVLYQLDRITPTQVEKFLETCRDKYMRAQMEPGSAVGALCAQSIGEPGTQMTLKTFHFAGVASMNITLGVPRIKEIINASKAISTPIITAQLDKDDDADYARLVKGRIEKTLLGEISEYIEEVFLPDDCFILVKLSLERIRLLRLEVNAETVRYSICTSKLRVKPGDVAVHGEAVVCVTPRENSKSSMYYVLQFLKEDLPKVVVQGIPEVSRAVIHIDEQSGKEKYKLLVEGDNLRAVMATHGVKGTRTTSNNTYEVEKTLGIEAARTTIINEIQYTMVNHGMSIDRRHVMLLSDLMTYKGEVLGITRFGLAKMKESVLMLASFEKTADHLFDAAYFGQKDSVCGVSECIIMGIPMNIGTGLFKLLHKADRDPNPPKRPLIFDTNEFHIPLVT
|
2.7.7.6
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:34675218}; Note=Two Mg(2+) ions are coordinated by both the catalytic residues and the nucleic acid substrate to enhance substrate recognition and catalytic efficiency. {ECO:0000250|UniProtKB:P24928, ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:34675218};
|
defense response to virus [GO:0051607]; DNA-templated transcription [GO:0006351]; innate immune response [GO:0045087]; positive regulation of interferon-beta production [GO:0032728]; tRNA transcription by RNA polymerase III [GO:0042797]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase III complex [GO:0005666]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; DNA/RNA hybrid binding [GO:0071667]; magnesium ion binding [GO:0000287]; RNA polymerase III activity [GO:0001056]; zinc ion binding [GO:0008270]
|
PF04997;PF00623;PF04983;PF05000;PF04998;
|
1.10.132.30;1.10.150.390;2.40.40.20;6.10.250.2940;6.20.50.80;3.30.1490.180;4.10.860.120;1.10.274.100;
|
RNA polymerase beta' chain family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11416169, ECO:0000269|PubMed:33335104}. Cytoplasm, cytosol {ECO:0000269|PubMed:33335104}.
|
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; Evidence={ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370, ECO:0000269|PubMed:33335104, ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:34675218, ECO:0000269|PubMed:9331371}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249; Evidence={ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370, ECO:0000269|PubMed:33335104, ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:34675218, ECO:0000269|PubMed:9331371};
| null | null | null | null |
FUNCTION: Catalytic core component of RNA polymerase III (Pol III), a DNA-dependent RNA polymerase which synthesizes small non-coding RNAs using the four ribonucleoside triphosphates as substrates. Synthesizes 5S rRNA, snRNAs, tRNAs and miRNAs from at least 500 distinct genomic loci (PubMed:19609254, PubMed:19631370, PubMed:20413673, PubMed:33335104, PubMed:33558764, PubMed:33558766, PubMed:34675218, PubMed:35637192, PubMed:9331371). Pol III-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol III is recruited to DNA promoters type I, II or III with the help of general transcription factors and other specific initiation factors. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA (PubMed:20413673, PubMed:33335104, PubMed:33558764, PubMed:33558766, PubMed:33674783, PubMed:34675218). Forms Pol III active center together with the second largest subunit POLR3B/RPC2. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR3A/RPC1 contributing a Mg(2+)-coordinating DxDGD motif, and POLR3B/RPC2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate (PubMed:19609254, PubMed:20413673, PubMed:33335104, PubMed:33558764, PubMed:33674783, PubMed:34675218, PubMed:9331371). Pol III plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as a nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF-kappa-B through the RIG-I pathway. {ECO:0000250, ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370, ECO:0000269|PubMed:20413673, ECO:0000269|PubMed:33335104, ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:33558766, ECO:0000269|PubMed:33674783, ECO:0000269|PubMed:34675218, ECO:0000269|PubMed:35637192, ECO:0000269|PubMed:9331371}.
|
Homo sapiens (Human)
|
O14804
|
TAAR5_HUMAN
|
MRAVFIQGAEEHPAAFCYQVNGSCPRTVHTLGIQLVIYLACAAGMLIIVLGNVFVAFAVSYFKALHTPTNFLLLSLALADMFLGLLVLPLSTIRSVESCWFFGDFLCRLHTYLDTLFCLTSIFHLCFISIDRHCAICDPLLYPSKFTVRVALRYILAGWGVPAAYTSLFLYTDVVETRLSQWLEEMPCVGSCQLLLNKFWGWLNFPLFFVPCLIMISLYVKIFVVATRQAQQITTLSKSLAGAAKHERKAAKTLGIAVGIYLLCWLPFTIDTMVDSLLHFITPPLVFDIFIWFAYFNSACNPIIYVFSYQWFRKALKLTLSQKVFSPQTRTVDLYQE
| null | null |
G protein-coupled receptor signaling pathway [GO:0007186]; sensory perception of chemical stimulus [GO:0007606]; signal transduction [GO:0007165]
|
plasma membrane [GO:0005886]
|
G protein-coupled receptor activity [GO:0004930]; trace-amine receptor activity [GO:0001594]; trimethylamine receptor activity [GO:1990081]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23393561}; Multi-pass membrane protein {ECO:0000269|PubMed:23393561}.
| null | null | null | null | null |
FUNCTION: Olfactory receptor specific for trimethylamine, a trace amine. Also activated at lower level by dimethylethylamine. Trimethylamine is a bacterial metabolite found in some animal odors, and to humans it is a repulsive odor associated with bad breath and spoiled food. This receptor is probably mediated by the G(s)-class of G-proteins which activate adenylate cyclase. {ECO:0000269|PubMed:23393561}.
|
Homo sapiens (Human)
|
O14807
|
RASM_HUMAN
|
MATSAVPSDNLPTYKLVVVGDGGVGKSALTIQFFQKIFVPDYDPTIEDSYLKHTEIDNQWAILDVLDTAGQEEFSAMREQYMRTGDGFLIVYSVTDKASFEHVDRFHQLILRVKDRESFPMILVANKVDLMHLRKITREQGKEMATKHNIPYIETSAKDPPLNVDKAFHDLVRVIRQQIPEKSQKKKKKTKWRGDRATGTHKLQCVIL
|
3.6.5.2
| null |
actin cytoskeleton organization [GO:0030036]; cellular response to leukemia inhibitory factor [GO:1990830]; Ras protein signal transduction [GO:0007265]
|
plasma membrane [GO:0005886]
|
G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTP-dependent protein binding [GO:0030742]; GTPase activity [GO:0003924]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Ras family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P01116};
| null | null | null | null |
FUNCTION: Serves as an important signal transducer for a novel upstream stimuli in controlling cell proliferation. Activates the MAP kinase pathway. {ECO:0000269|PubMed:16630891, ECO:0000269|PubMed:28289718}.
|
Homo sapiens (Human)
|
O14810
|
CPLX1_HUMAN
|
MEFVMKQALGGATKDMGKMLGGDEEKDPDAAKKEEERQEALRQAEEERKAKYAKMEAEREAVRQGIRDKYGIKKKEEREAEAQAAMEANSEGSLTRPKKAIPPGCGDEVEEEDESILDTVIKYLPGPLQDMLKK
| null | null |
chemical synaptic transmission [GO:0007268]; exocytosis [GO:0006887]; insulin secretion [GO:0030073]; regulation of exocytic insertion of neurotransmitter receptor to postsynaptic membrane [GO:0099145]; regulation of exocytosis [GO:0017157]; regulation of neurotransmitter secretion [GO:0046928]; regulation of synaptic vesicle fusion to presynaptic active zone membrane [GO:0031630]; synaptic vesicle exocytosis [GO:0016079]
|
calyx of Held [GO:0044305]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; perikaryon [GO:0043204]; postsynapse [GO:0098794]; Schaffer collateral - CA1 synapse [GO:0098685]; SNARE complex [GO:0031201]; synaptobrevin 2-SNAP-25-syntaxin-3-complexin complex [GO:0070554]; terminal bouton [GO:0043195]
|
neurotransmitter transmembrane transporter activity [GO:0005326]; SNARE binding [GO:0000149]; syntaxin binding [GO:0019905]
|
PF05835;
|
1.20.5.580;
|
Complexin/synaphin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P63040}. Perikaryon {ECO:0000250|UniProtKB:P63040}. Presynapse {ECO:0000250|UniProtKB:P63040}. Note=Enriched at synaptic-releasing sites in mature neurons. {ECO:0000250|UniProtKB:P63040}.
| null | null | null | null | null |
FUNCTION: Positively regulates a late step in exocytosis of various cytoplasmic vesicles, such as synaptic vesicles and other secretory vesicles (PubMed:21785414). Organizes the SNAREs into a cross-linked zigzag topology that, when interposed between the vesicle and plasma membranes, is incompatible with fusion, thereby preventing SNAREs from releasing neurotransmitters until an action potential arrives at the synapse (PubMed:21785414). Also involved in glucose-induced secretion of insulin by pancreatic beta-cells. Essential for motor behavior. {ECO:0000250|UniProtKB:P63040, ECO:0000269|PubMed:21785414}.
|
Homo sapiens (Human)
|
O14813
|
PHX2A_HUMAN
|
MDYSYLNSYDSCVAAMEASAYGDFGACSQPGGFQYSPLRPAFPAAGPPCPALGSSNCALGALRDHQPAPYSAVPYKFFPEPSGLHEKRKQRRIRTTFTSAQLKELERVFAETHYPDIYTREELALKIDLTEARVQVWFQNRRAKFRKQERAASAKGAAGAAGAKKGEARCSSEDDDSKESTCSPTPDSTASLPPPPAPGLASPRLSPSPLPVALGSGPGPGPGPQPLKGALWAGVAGGGGGGPGAGAAELLKAWQPAESGPGPFSGVLSSFHRKPGPALKTNLF
| null | null |
dopaminergic neuron differentiation [GO:0071542]; locus ceruleus development [GO:0021703]; midbrain development [GO:0030901]; noradrenergic neuron differentiation [GO:0003357]; oculomotor nerve formation [GO:0021623]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of respiratory gaseous exchange [GO:0043576]; regulation of transcription by RNA polymerase II [GO:0006357]; somatic motor neuron differentiation [GO:0021523]; sympathetic nervous system development [GO:0048485]; trochlear nerve formation [GO:0021642]
|
chromatin [GO:0000785]; nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00046;
|
1.10.10.60;
|
Paired homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
| null | null | null | null | null |
FUNCTION: May be involved in regulating the specificity of expression of the catecholamine biosynthetic genes. Acts as a transcription activator/factor. Could maintain the noradrenergic phenotype.
|
Homo sapiens (Human)
|
O14815
|
CAN9_HUMAN
|
MPYLYRAPGPQAHPVPKDARITHSSGQSFEQMRQECLQRGTLFEDADFPASNSSLFYSERPQIPFVWKRPGEIVKNPEFILGGATRTDICQGELGDCWLLAAIASLTLNQKALARVIPQDQSFGPGYAGIFHFQFWQHSEWLDVVIDDRLPTFRDRLVFLHSADHNEFWSALLEKAYAKLNGSYEALKGGSAIEAMEDFTGGVAETFQTKEAPENFYEILEKALKRGSLLGCFIDTRSAAESEARTPFGLIKGHAYSVTGIDQVSFRGQRIELIRIRNPWGQVEWNGSWSDSSPEWRSVGPAEQKRLCHTALDDGEFWMAFKDFKAHFDKVEICNLTPDALEEDAIHKWEVTVHQGSWVRGSTAGGCRNFLDTFWTNPQIKLSLTEKDEGQEECSFLVALMQKDRRKLKRFGANVLTIGYAIYECPDKDEHLNKDFFRYHASRARSKTFINLREVSDRFKLPPGEYILIPSTFEPHQEADFCLRIFSEKKAITRDMDGNVDIDLPEPPKPTPPDQETEEEQRFRALFEQVAGEDMEVTAEELEYVLNAVLQKKKDIKFKKLSLISCKNIISLMDTSGNGKLEFDEFKVFWDKLKQWINLFLRFDADKSGTMSTYELRTALKAAGFQLSSHLLQLIVLRYADEELQLDFDDFLNCLVRLENASRVFQALSTKNKEFIHLNINEFIHLTMNI
|
3.4.22.-
| null |
digestion [GO:0007586]; proteolysis [GO:0006508]
|
cytoplasm [GO:0005737]
|
calcium ion binding [GO:0005509]; calcium-dependent cysteine-type endopeptidase activity [GO:0004198]
|
PF01067;PF13833;PF00648;
|
2.60.120.380;3.90.70.10;1.10.238.10;
|
Peptidase C2 family
| null | null | null | null | null | null | null |
FUNCTION: Calcium-regulated non-lysosomal thiol-protease.
|
Homo sapiens (Human)
|
O14817
|
TSN4_HUMAN
|
MARACLQAVKYLMFAFNLLFWLGGCGVLGVGIWLAATQGSFATLSSSFPSLSAANLLIITGAFVMAIGFVGCLGAIKENKCLLLTFFLLLLLVFLLEATIAILFFAYTDKIDRYAQQDLKKGLHLYGTQGNVGLTNAWSIIQTDFRCCGVSNYTDWFEVYNATRVPDSCCLEFSESCGLHAPGTWWKAPCYETVKVWLQENLLAVGIFGLCTALVQILGLTFAMTMYCQVVKADTYCA
| null | null |
protein-containing complex assembly [GO:0065003]
|
focal adhesion [GO:0005925]; plasma membrane [GO:0005886]; vesicle [GO:0031982]
|
antigen binding [GO:0003823]; integrin binding [GO:0005178]
|
PF00335;
|
1.10.1450.10;
|
Tetraspanin (TM4SF) family
| null |
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
| null | null | null | null | null | null |
Homo sapiens (Human)
|
O14818
|
PSA7_HUMAN
|
MSYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGVRGRDIVVLGVEKKSVAKLQDERTVRKICALDDNVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIASLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRGAKSVREFLEKNYTDEAIETDDLTIKLVIKALLEVVQSGGKNIELAVMRRDQSLKILNPEEIEKYVAEIEKEKEENEKKKQKKAS
| null | null |
proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; postsynapse [GO:0098794]; proteasome complex [GO:0000502]; proteasome core complex [GO:0005839]; proteasome core complex, alpha-subunit complex [GO:0019773]
|
identical protein binding [GO:0042802]
|
PF00227;PF10584;
|
3.60.20.10;
|
Peptidase T1A family
|
PTM: Phosphorylation by ABL1 or ABL2 leads to an inhibition of proteasomal activity and cell cycle transition blocks. {ECO:0000269|PubMed:16678104}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345, ECO:0000269|PubMed:34711951}. Nucleus {ECO:0000269|PubMed:12181345, ECO:0000269|PubMed:34711951}. Note=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9. {ECO:0000269|PubMed:34711951}.
| null | null | null | null | null |
FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Inhibits the transactivation function of HIF-1A under both normoxic and hypoxia-mimicking conditions. The interaction with EMAP2 increases the proteasome-mediated HIF-1A degradation under the hypoxic conditions. Plays a role in hepatitis C virus internal ribosome entry site-mediated translation. Mediates nuclear translocation of the androgen receptor (AR) and thereby enhances androgen-mediated transactivation. Promotes MAVS degradation and thereby negatively regulates MAVS-mediated innate immune response. {ECO:0000269|PubMed:11389899, ECO:0000269|PubMed:11713272, ECO:0000269|PubMed:12119296, ECO:0000269|PubMed:15244466, ECO:0000269|PubMed:19442227, ECO:0000269|PubMed:19734229, ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}.
|
Homo sapiens (Human)
|
O14827
|
RGRF2_HUMAN
|
MQKSVRYNEGHALYLAFLARKEGTKRGFLSKKTAEASRWHEKWFALYQNVLFYFEGEQSCRPAGMYLLEGCSCERTPAPPRAGAGQGGVRDALDKQYYFTVLFGHEGQKPLELRCEEEQDGKEWMEAIHQASYADILIEREVLMQKYIHLVQIVETEKIAANQLRHQLEDQDTEIERLKSEIIALNKTKERMRPYQSNQEDEDPDIKKIKKVQSFMRGWLCRRKWKTIVQDYICSPHAESMRKRNQIVFTMVEAESEYVHQLYILVNGFLRPLRMAASSKKPPISHDDVSSIFLNSETIMFLHEIFHQGLKARIANWPTLILADLFDILLPMLNIYQEFVRNHQYSLQVLANCKQNRDFDKLLKQYEANPACEGRMLETFLTYPMFQIPRYIITLHELLAHTPHEHVERKSLEFAKSKLEELSRVMHDEVSDTENIRKNLAIERMIVEGCDILLDTSQTFIRQGSLIQVPSVERGKLSKVRLGSLSLKKEGERQCFLFTKHFLICTRSSGGKLHLLKTGGVLSLIDCTLIEEPDASDDDSKGSGQVFGHLDFKIVVEPPDAAAFTVVLLAPSRQEKAAWMSDISQCVDNIRCNGLMTIVFEENSKVTVPHMIKSDARLHKDDTDICFSKTLNSCKVPQIRYASVERLLERLTDLRFLSIDFLNTFLHTYRIFTTAAVVLGKLSDIYKRPFTSIPVRSLELFFATSQNNRGEHLVDGKSPRLCRKFSSPPPLAVSRTSSPVRARKLSLTSPLNSKIGALDLTTSSSPTTTTQSPAASPPPHTGQIPLDLSRGLSSPEQSPGTVEENVDNPRVDLCNKLKRSIQKAVLESAPADRAGVESSPAADTTELSPCRSPSTPRHLRYRQPGGQTADNAHCSVSPASAFAIATAAAGHGSPPGFNNTERTCDKEFIIRRTATNRVLNVLRHWVSKHAQDFELNNELKMNVLNLLEEVLRDPDLLPQERKAAANILRALSQDDQDDIHLKLEDIIQMTDCMKAECFESLSAMELAEQITLLDHVIFRSIPYEEFLGQGWMKLDKNERTPYIMKTSQHFNDMSNLVASQIMNYADVSSRANAIEKWVAVADICRCLHNYNGVLEITSALNRSAIYRLKKTWAKVSKQTKALMDKLQKTVSSEGRFKNLRETLKNCNPPAVPYLGMYLTDLAFIEEGTPNFTEEGLVNFSKMRMISHIIREIRQFQQTSYRIDHQPKVAQYLLDKDLIIDEDTLYELSLKIEPRLPA
| null | null |
long-term synaptic potentiation [GO:0060291]; Ras protein signal transduction [GO:0007265]; regulation of small GTPase mediated signal transduction [GO:0051056]; response to endoplasmic reticulum stress [GO:0034976]
|
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]
|
calmodulin binding [GO:0005516]; guanyl-nucleotide exchange factor activity [GO:0005085]
|
PF00169;PF00617;PF00618;PF00621;
|
1.20.900.10;2.30.29.30;1.10.840.10;1.20.870.10;
| null |
PTM: Phosphorylated by CDK5; down-regulates RASGRF2-mediated RAC1 activation. {ECO:0000269|PubMed:15128856}.; PTM: Ubiquitinated upon interaction with Ras. Ubiquitination leads to degradation through the 26S proteasome (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Note=Translocates to membranes when activated. Found both at cell periphery and along the axon of neurons (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Functions as a calcium-regulated nucleotide exchange factor activating both Ras and RAC1 through the exchange of bound GDP for GTP. Preferentially activates HRAS in vivo compared to RRAS based on their different types of prenylation. Functions in synaptic plasticity by contributing to the induction of long term potentiation. {ECO:0000269|PubMed:15128856}.
|
Homo sapiens (Human)
|
O14828
|
SCAM3_HUMAN
|
MAQSRDGGNPFAEPSELDNPFQDPAVIQHRPSRQYATLDVYNPFETREPPPAYEPPAPAPLPPPSAPSLQPSRKLSPTEPKNYGSYSTQASAAAATAELLKKQEELNRKAEELDRRERELQHAALGGTATRQNNWPPLPSFCPVQPCFFQDISMEIPQEFQKTVSTMYYLWMCSTLALLLNFLACLASFCVETNNGAGFGLSILWVLLFTPCSFVCWYRPMYKAFRSDSSFNFFVFFFIFFVQDVLFVLQAIGIPGWGFSGWISALVVPKGNTAVSVLMLLVALLFTGIAVLGIVMLKRIHSLYRRTGASFQKAQQEFAAGVFSNPAVRTAAANAAAGAAENAFRAP
| null | null |
post-Golgi vesicle-mediated transport [GO:0006892]; protein transport [GO:0015031]
|
extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; recycling endosome membrane [GO:0055038]; trans-Golgi network membrane [GO:0032588]
|
ubiquitin protein ligase binding [GO:0031625]
|
PF04144;
| null |
SCAMP family
|
PTM: Monoubiquitinated.
|
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface.
|
Homo sapiens (Human)
|
O14829
|
PPE1_HUMAN
|
MGCSSSSTKTRRSDTSLRAALIIQNWYRGYKARLKARQHYALTIFQSIEYADEQGQMQLSTFFSFMLENYTHIHKEELELRNQSLESEQDMRDRWDYVDSIDVPDSYNGPRLQFPLTCTDIDLLLEAFKEQQILHAHYVLEVLFETKKVLKQMPNFTHIQTSPSKEVTICGDLHGKLDDLFLIFYKNGLPSERNPYVFNGDFVDRGKNSIEILMILCVSFLVYPNDLHLNRGNHEDFMMNLRYGFTKEILHKYKLHGKRILQILEEFYAWLPIGTIVDNEILVIHGGISETTDLNLLHRVERNKMKSVLIPPTETNRDHDTDSKHNKVGVTFNAHGRIKTNGSPTEHLTEHEWEQIIDILWSDPRGKNGCFPNTCRGGGCYFGPDVTSKILNKYQLKMLIRSHECKPEGYEICHDGKVVTIFSASNYYEEGSNRGAYIKLCSGTTPRFFQYQVTKATCFQPLRQRVDTMENSAIKILRERVISRKSDLTRAFQLQDHRKSGKLSVSQWAFCMENILGLNLPWRSLSSNLVNIDQNGNVEYMSSFQNIRIEKPVQEAHSTLVETLYRYRSDLEIIFNAIDTDHSGLISVEEFRAMWKLFSSHYNVHIDDSQVNKLANIMDLNKDGSIDFNEFLKAFYVVHRYEDLMKPDVTNLG
|
3.1.3.16
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
detection of stimulus involved in sensory perception [GO:0050906]; protein dephosphorylation [GO:0006470]
|
cytosol [GO:0005829]; nucleus [GO:0005634]
|
calcium ion binding [GO:0005509]; iron ion binding [GO:0005506]; manganese ion binding [GO:0030145]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]
|
PF13499;PF00612;PF00149;PF08321;
|
3.60.21.10;1.10.238.10;
|
PPP phosphatase family
| null | null |
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16;
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0.;
| null |
FUNCTION: May have a role in the recovery or adaptation response of photoreceptors. May have a role in development.
|
Homo sapiens (Human)
|
O14830
|
PPE2_HUMAN
|
MGSGTSTQHHFAFQNAERAFKAAALIQRWYRRYVARLEMRRRCTWSIFQSIEYAGQQDQVKLHDFFSYLMDHFIPSSHNDRDFLTRIFTEDRFAQDSEMKKCSDYESIEVPDSYTGPRLSFPLLPDHATALVEAFRLKQQLHARYVLNLLYETKKHLVQLPNINRVSTCYSEEITVCGDLHGQLDDLIFIFYKNGLPSPERSYVFNGDFVDRGKDSVEILMILFAFMLVYPKEFHLNRGNHEDHMVNLRYGFTKEVMNKYKVHGKEILRTLQDVFCWLPLATLIDEKVLILHGGVSDITDLELLDKIERSKIVSTMRCKTRQKSEKQMEEKRRANQKSSAQGPIPWFLPESRSLPSSPLRLGSYKAQKTSRSSSIPCSGSLDGRELSRQVRSSVELELERCRQQAGLLVTGEKEEPSRSASEADSEAGELRKPTQEEWRQVVDILWSDPMAQEGCKANTIRGGGCYFGPDVTQQLLQKYNMQFLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGAYVKLGPALTPHIVQYQANKVTHTLTMRQRISRVEESALRALREKLFAHSSDLLSEFKKHDADKVGLITLSDWAAAVESVLHLGLPWRMLRPQLVNSSADNMLEYKSWLKNLAKEQLSRENIQSSLLETLYRNRSNLETIFRIIDSDHSGFISLDEFRQTWKLFSSHMNIDITDDCICDLARSIDFNKDGHIDINEFLEAFRLVEKSCPEGDASECPQATNAKDSGCSSPGAH
|
3.1.3.16
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250};
|
detection of stimulus involved in sensory perception [GO:0050906]; negative regulation of MAPK cascade [GO:0043409]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; protein dephosphorylation [GO:0006470]; regulation of JUN kinase activity [GO:0043506]; regulation of MAP kinase activity [GO:0043405]; visual perception [GO:0007601]
|
cytosol [GO:0005829]; nucleus [GO:0005634]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750]
|
calcium ion binding [GO:0005509]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; iron ion binding [GO:0005506]; manganese ion binding [GO:0030145]; mitogen-activated protein kinase kinase kinase binding [GO:0031435]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]
|
PF13499;PF00149;PF08321;
|
3.60.21.10;1.10.238.10;
|
PPP phosphatase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cell projection, cilium, photoreceptor outer segment. Photoreceptor inner segment. Note=Localized to photoreceptors, PPEF-2(L) is at least 2 fold more abundant in rod inner segments than in the outer segments.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16;
| null | null | null | null |
FUNCTION: May play a role in phototransduction. May dephosphorylate photoactivated rhodopsin. May function as a calcium sensing regulator of ionic currents, energy production or synaptic transmission.
|
Homo sapiens (Human)
|
O14832
|
PAHX_HUMAN
|
MEQLRAAARLQIVLGHLGRPSAGAVVAHPTSGTISSASFHPQQFQYTLDNNVLTLEQRKFYEENGFLVIKNLVPDADIQRFRNEFEKICRKEVKPLGLTVMRDVTISKSEYAPSEKMITKVQDFQEDKELFRYCTLPEILKYVECFTGPNIMAMHTMLINKPPDSGKKTSRHPLHQDLHYFPFRPSDLIVCAWTAMEHISRNNGCLVVLPGTHKGSLKPHDYPKWEGGVNKMFHGIQDYEENKARVHLVMEKGDTVFFHPLLIHGSGQNKTQGFRKAISCHFASADCHYIDVKGTSQENIEKEVVGIAHKFFGAENSVNLKDIWMFRARLVKGERTNL
|
1.14.11.18
|
COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269|PubMed:10744784, ECO:0000269|PubMed:16186124, ECO:0000269|PubMed:9326939}; COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000269|PubMed:10744784, ECO:0000269|PubMed:16186124}; COFACTOR: Name=ATP; Xref=ChEBI:CHEBI:30616; Evidence={ECO:0000269|PubMed:10744784}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10744784};
|
2-oxobutyrate catabolic process [GO:0019606]; 2-oxoglutarate metabolic process [GO:0006103]; fatty acid alpha-oxidation [GO:0001561]; isoprenoid metabolic process [GO:0006720]; methyl-branched fatty acid metabolic process [GO:0097089]
|
9+0 non-motile cilium [GO:0097731]; cytosol [GO:0005829]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]
|
carboxylic acid binding [GO:0031406]; ferrous iron binding [GO:0008198]; L-ascorbic acid binding [GO:0031418]; phytanoyl-CoA dioxygenase activity [GO:0048244]
|
PF05721;
|
2.60.120.620;
|
PhyH family
| null |
SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:9326939}.
|
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + phytanoyl-CoA = 2-hydroxyphytanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:16065, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57334, ChEBI:CHEBI:57391; EC=1.14.11.18; Evidence={ECO:0000269|PubMed:10767344, ECO:0000269|PubMed:12031666, ECO:0000269|PubMed:9326939}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16066; Evidence={ECO:0000305|PubMed:12031666, ECO:0000305|PubMed:9326939}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 3-methylhexadecanoyl-CoA + O2 = 2-hydroxy-3-methylhexadecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:44000, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:58784, ChEBI:CHEBI:83969; Evidence={ECO:0000269|PubMed:10744784, ECO:0000269|PubMed:12923223}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44001; Evidence={ECO:0000305|PubMed:10744784, ECO:0000305|PubMed:12923223}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + hexadecanoyl-CoA + O2 = 2-hydroxyhexadecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54596, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57379, ChEBI:CHEBI:74115; Evidence={ECO:0000269|PubMed:12031666}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54597; Evidence={ECO:0000305|PubMed:12031666}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + octanoyl-CoA = 2-hydroxyoctanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54600, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57386, ChEBI:CHEBI:138290; Evidence={ECO:0000269|PubMed:12031666}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54601; Evidence={ECO:0000305|PubMed:12031666}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + decanoyl-CoA + O2 = 2-hydroxydecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54604, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:61430, ChEBI:CHEBI:138292; Evidence={ECO:0000269|PubMed:12031666}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54605; Evidence={ECO:0000305|PubMed:12031666}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 3-methylbutanoyl-CoA + O2 = 2-hydroxy-3-methylbutanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54612, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57345, ChEBI:CHEBI:138296; Evidence={ECO:0000269|PubMed:12031666}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54613; Evidence={ECO:0000305|PubMed:12031666}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + heptadecanoyl-CoA + O2 = 2-hydroxyheptadecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54616, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:74307, ChEBI:CHEBI:138297; Evidence={ECO:0000269|PubMed:12031666}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54617; Evidence={ECO:0000305|PubMed:12031666}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + eicosanoyl-CoA + O2 = 2-hydroxyeicosanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54620, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57380, ChEBI:CHEBI:138298; Evidence={ECO:0000269|PubMed:12031666}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54621; Evidence={ECO:0000305|PubMed:12031666}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + octadecanoyl-CoA = 2-hydroxyoctadecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54624, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57394, ChEBI:CHEBI:74116; Evidence={ECO:0000269|PubMed:12031666}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54625; Evidence={ECO:0000305|PubMed:12031666}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + dodecanoyl-CoA + O2 = 2-hydroxydodecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54628, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57375, ChEBI:CHEBI:138299; Evidence={ECO:0000269|PubMed:12031666}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54629; Evidence={ECO:0000305|PubMed:12031666}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + tetradecanoyl-CoA = 2-hydroxytetradecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54632, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57385, ChEBI:CHEBI:138300; Evidence={ECO:0000269|PubMed:12031666}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54633; Evidence={ECO:0000305|PubMed:12031666}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + hexanoyl-CoA + O2 = 2-hydroxyhexanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:55172, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:62620, ChEBI:CHEBI:138630; Evidence={ECO:0000269|PubMed:12031666}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55173; Evidence={ECO:0000305|PubMed:12031666}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + butanoyl-CoA + O2 = 2-hydroxybutanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:55176, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57371, ChEBI:CHEBI:138628; Evidence={ECO:0000269|PubMed:12031666}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55177; Evidence={ECO:0000305|PubMed:12031666}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 3-methylnonanoyl-CoA + O2 = 2-hydroxy-3-methylnonanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:55180, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:138633, ChEBI:CHEBI:138634; Evidence={ECO:0000269|PubMed:12923223}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55181; Evidence={ECO:0000305|PubMed:12923223}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 3-methylundecanoyl-CoA + O2 = 2-hydroxy-3-methylundecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:55184, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:84183, ChEBI:CHEBI:138632; Evidence={ECO:0000269|PubMed:12923223}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55185; Evidence={ECO:0000305|PubMed:12923223}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 3-methyldodecanoyl-CoA + O2 = 2-hydroxy-3-methyldodecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:55192, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:138636, ChEBI:CHEBI:138637; Evidence={ECO:0000269|PubMed:12923223}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55193; Evidence={ECO:0000305|PubMed:12923223};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=40.8 uM for 3-methylhexadecanoyl-CoA {ECO:0000269|PubMed:12923223}; KM=29.5 uM for phytanoyl-CoA (in presence of SCP2) {ECO:0000269|PubMed:12031666}; KM=29.1 uM for hexadecanoyl-CoA (in presence of SCP2) {ECO:0000269|PubMed:12031666};
|
PATHWAY: Lipid metabolism; fatty acid metabolism.
| null | null |
FUNCTION: Catalyzes the 2-hydroxylation of not only racemic phytanoyl-CoA and the isomers of 3-methylhexadecanoyl-CoA, but also a variety of other mono-branched 3-methylacyl-CoA esters (with a chain length of at least seven carbon atoms) and straight-chain acyl-CoA esters (with a chain length longer than four carbon atoms) (PubMed:10744784, PubMed:12031666, PubMed:12923223, PubMed:9326939). Does not hydroxylate long and very long straight chain acyl-CoAs or 2-methyl- and 4-methyl-branched acyl-CoAs (PubMed:10744784, PubMed:12923223). {ECO:0000269|PubMed:10744784, ECO:0000269|PubMed:12031666, ECO:0000269|PubMed:12923223, ECO:0000269|PubMed:9326939}.
|
Homo sapiens (Human)
|
O14836
|
TR13B_HUMAN
|
MSGLGRSRRGGRSRVDQEERFPQGLWTGVAMRSCPEEQYWDPLLGTCMSCKTICNHQSQRTCAAFCRSLSCRKEQGKFYDHLLRDCISCASICGQHPKQCAYFCENKLRSPVNLPPELRRQRSGEVENNSDNSGRYQGLEHRGSEASPALPGLKLSADQVALVYSTLGLCLCAVLCCFLVAVACFLKKRGDPCSCQPRSRPRQSPAKSSQDHAMEAGSPVSTSPEPVETCSFCFPECRAPTQESAVTPGTPDPTCAGRWGCHTRTTVLQPCPHIPDSGLGIVCVPAQEGGPGA
| null | null |
adaptive immune response [GO:0002250]; B cell homeostasis [GO:0001782]; cell surface receptor signaling pathway [GO:0007166]; hematopoietic progenitor cell differentiation [GO:0002244]; negative regulation of B cell proliferation [GO:0030889]
|
plasma membrane [GO:0005886]
|
signaling receptor activity [GO:0038023]
|
PF09305;
|
4.10.1290.10;
| null | null |
SUBCELLULAR LOCATION: Membrane; Single-pass type III membrane protein.
| null | null | null | null | null |
FUNCTION: Receptor for TNFSF13/APRIL and TNFSF13B/TALL1/BAFF/BLYS that binds both ligands with similar high affinity. Mediates calcineurin-dependent activation of NF-AT, as well as activation of NF-kappa-B and AP-1. Involved in the stimulation of B- and T-cell function and the regulation of humoral immunity. {ECO:0000269|PubMed:10956646, ECO:0000269|PubMed:10973284}.
|
Homo sapiens (Human)
|
O14841
|
OPLA_HUMAN
|
MGSPEGRFHFAIDRGGTFTDVFAQCPGGHVRVLKLLSEDPANYADAPTEGIRRILEQEAGMLLPRDQPLDSSHIASIRMGTTVATNALLERKGERVALLVTRGFRDLLHIGTQARGDLFDLAVPMPEVLYEEVLEVDERVVLHRGEAGTGTPVKGRTGDLLEVQQPVDLGALRGKLEGLLSRGIRSLAVVLMHSYTWAQHEQQVGVLARELGFTHVSLSSEAMPMVRIVPRGHTACADAYLTPAIQRYVQGFCRGFQGQLKDVQVLFMRSDGGLAPMDTFSGSSAVLSGPAGGVVGYSATTYQQEGGQPVIGFDMGGTSTDVSRYAGEFEHVFEASTAGVTLQAPQLDINTVAAGGGSRLFFRSGLFVVGPESAGAHPGPACYRKGGPVTVTDANLVLGRLLPASFPCIFGPGENQPLSPEASRKALEAVATEVNSFLTNGPCPASPLSLEEVAMGFVRVANEAMCRPIRALTQARGHDPSAHVLACFGGAGGQHACAIARALGMDTVHIHRHSGLLSALGLALADVVHEAQEPCSLLYAPETFVQLDQRLSRLEEQCVDALQAQGFPRSQISTESFLHLRYQGTDCALMVSAHQHPATARSPRAGDFGAAFVERYMREFGFVIPERPVVVDDVRVRGTGRSGLRLEDAPKAQTGPPRVDKMTQCYFEGGYQETPVYLLAELGYGHKLHGPCLIIDSNSTILVEPGCQAEVTKTGDICISVGAEVPGTVGPQLDPIQLSIFSHRFMSIAEQMGRILQRTAISTNIKERLDFSCALFGPDGGLVSNAPHIPVHLGAMQETVQFQIQHLGADLHPGDVLLSNHPSAGGSHLPDLTVITPVFWPGQTRPVFYVASRGHHADIGGITPGSMPPHSTMLQQEGAVFLSFKLVQGGVFQEEAVTEALRAPGKVPNCSGTRNLHDNLSDLRAQVAANQKGIQLVGELIGQYGLDVVQAYMGHIQANAELAVRDMLRAFGTSRQARGLPLEVSSEDHMDDGSPIRLRVQISLSQGSAVFDFSGTGPEVFGNLNAPRAVTLSALIYCLRCLVGRDIPLNQGCLAPVRVVIPRGSILDPSPEAAVVGGNVLTSQRVVDVILGAFGACAASQGCMNNVTLGNAHMGYYETVAGGAGAGPSWHGRSGVHSHMTNTRITDPEILESRYPVILRRFELRRGSGGRGRFRGGDGVTRELLFREEALLSVLTERRAFRPYGLHGGEPGARGLNLLIRKNGRTVNLGGKTSVTVYPGDVFCLHTPGGGGYGDPEDPAPPPGSPPQALAFPEHGSVYEYRRAQEAV
|
3.5.2.9
| null |
glutathione metabolic process [GO:0006749]
|
cytosol [GO:0005829]
|
5-oxoprolinase (ATP-hydrolyzing) activity [GO:0017168]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]
|
PF19278;PF05378;PF01968;PF02538;
| null |
Oxoprolinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q75WB5}.
|
CATALYTIC ACTIVITY: Reaction=5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:10348, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58402, ChEBI:CHEBI:456216; EC=3.5.2.9; Evidence={ECO:0000250|UniProtKB:Q75WB5};
| null | null | null | null |
FUNCTION: Catalyzes the cleavage of 5-oxo-L-proline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate. {ECO:0000250|UniProtKB:Q75WB5}.
|
Homo sapiens (Human)
|
O14842
|
FFAR1_HUMAN
|
MDLPPQLSFGLYVAAFALGFPLNVLAIRGATAHARLRLTPSLVYALNLGCSDLLLTVSLPLKAVEALASGAWPLPASLCPVFAVAHFFPLYAGGGFLAALSAGRYLGAAFPLGYQAFRRPCYSWGVCAAIWALVLCHLGLVFGLEAPGGWLDHSNTSLGINTPVNGSPVCLEAWDPASAGPARFSLSLLLFFLPLAITAFCYVGCLRALARSGLTHRRKLRAAWVAGGALLTLLLCVGPYNASNVASFLYPNLGGSWRKLGLITGAWSVVLNPLVTGYLGRGPGLKTVCAARTQGGKSQK
| null | null |
G protein-coupled receptor signaling pathway [GO:0007186]; glucose homeostasis [GO:0042593]; insulin secretion [GO:0030073]; ion channel modulating, G protein-coupled receptor signaling pathway [GO:0099105]; ligand-gated ion channel signaling pathway [GO:1990806]; negative regulation of interleukin-1 beta production [GO:0032691]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of calcium ion transport [GO:0051928]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of insulin secretion [GO:0032024]; response to fatty acid [GO:0070542]
|
plasma membrane [GO:0005886]
|
bioactive lipid receptor activity [GO:0045125]; G protein-coupled receptor activity [GO:0004930]; lipid binding [GO:0008289]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17699519, ECO:0000269|PubMed:25043059}; Multi-pass membrane protein {ECO:0000269|PubMed:25043059}.
| null | null | null | null | null |
FUNCTION: G-protein coupled receptor for medium and long chain saturated and unsaturated fatty acids that plays an important role in glucose homeostasis. Fatty acid binding increases glucose-stimulated insulin secretion, and may also enhance the secretion of glucagon-like peptide 1 (GLP-1). May also play a role in bone homeostasis; receptor signaling activates pathways that inhibit osteoclast differentiation (By similarity). Ligand binding leads to a conformation change that triggers signaling via G-proteins that activate phospholipase C, leading to an increase of the intracellular calcium concentration. Seems to act through a G(q) and G(i)-mediated pathway. Mediates the anti-inflammatory effects of omega-3 polyunsaturated fatty acids (PUFAs) via inhibition of NLRP3 inflammasome activation. {ECO:0000250|UniProtKB:Q76JU9, ECO:0000269|PubMed:12496284, ECO:0000269|PubMed:17699519, ECO:0000269|PubMed:23809162, ECO:0000269|PubMed:24130766, ECO:0000269|PubMed:24742677}.
|
Homo sapiens (Human)
|
O14843
|
FFAR3_HUMAN
|
MDTGPDQSYFSGNHWFVFSVYLLTFLVGLPLNLLALVVFVGKLQRRPVAVDVLLLNLTASDLLLLLFLPFRMVEAANGMHWPLPFILCPLSGFIFFTTIYLTALFLAAVSIERFLSVAHPLWYKTRPRLGQAGLVSVACWLLASAHCSVVYVIEFSGDISHSQGTNGTCYLEFRKDQLAILLPVRLEMAVVLFVVPLIITSYCYSRLVWILGRGGSHRRQRRVAGLLAATLLNFLVCFGPYNVSHVVGYICGESPAWRIYVTLLSTLNSCVDPFVYYFSSSGFQADFHELLRRLCGLWGQWQQESSMELKEQKGGEEQRADRPAERKTSEHSQGCGTGGQVACAES
| null | null |
adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; cellular response to fatty acid [GO:0071398]; G protein-coupled receptor signaling pathway [GO:0007186]; inflammatory response [GO:0006954]; mucosal immune response [GO:0002385]; negative regulation of blood pressure [GO:0045776]; positive regulation of acute inflammatory response to non-antigenic stimulus [GO:0002879]; positive regulation of chemokine production [GO:0032722]; positive regulation of cytokine production involved in immune response [GO:0002720]; regulation of hormone biosynthetic process [GO:0046885]; regulation of insulin receptor signaling pathway [GO:0046626]; regulation of norepinephrine secretion [GO:0014061]; regulation of peptide hormone secretion [GO:0090276]
|
plasma membrane [GO:0005886]
|
G protein-coupled receptor activity [GO:0004930]; lipid binding [GO:0008289]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18801738}; Multi-pass membrane protein {ECO:0000269|PubMed:18801738}.
| null | null | null | null | null |
FUNCTION: G protein-coupled receptor that is activated by a major product of dietary fiber digestion, the short chain fatty acids (SCFAs), and that plays a role in the regulation of whole-body energy homeostasis and in intestinal immunity. In omnivorous mammals, the short chain fatty acids acetate, propionate and butyrate are produced primarily by the gut microbiome that metabolizes dietary fibers. SCFAs serve as a source of energy but also act as signaling molecules. That G protein-coupled receptor is probably coupled to the pertussis toxin-sensitive, G(i/o)-alpha family of G proteins. Its activation results in the formation of inositol 1,4,5-trisphosphate, the mobilization of intracellular calcium, the phosphorylation of the MAPK3/ERK1 and MAPK1/ERK2 kinases and the inhibition of intracellular cAMP accumulation (PubMed:12711604). Activated by SCFAs and by beta-hydroxybutyrate, a ketone body produced by the liver upon starvation, it inhibits N-type calcium channels and modulates the activity of sympathetic neurons through a signaling cascade involving the beta and gamma subunits of its coupled G protein, phospholipase C and MAP kinases. Thereby, it may regulate energy expenditure through the control of the sympathetic nervous system that controls for instance heart rate. Upon activation by SCFAs accumulating in the intestine, it may also signal to the brain via neural circuits which in turn would regulate intestinal gluconeogenesis. May also control the production of hormones involved in whole-body energy homeostasis. May for instance, regulate blood pressure through renin secretion. May also regulate secretion of the PYY peptide by enteroendocrine cells and control gut motility, intestinal transit rate, and the harvesting of energy from SCFAs produced by gut microbiota. May also indirectly regulate the production of LEP/Leptin, a hormone acting on the CNS to inhibit food intake, in response to the presence of short-chain fatty acids in the intestine. Finally, may also play a role in glucose homeostasis. Besides its role in energy homeostasis, may play a role in intestinal immunity. May mediate the activation of the inflammatory and immune response by SCFAs in the gut, regulating the rapid production of chemokines and cytokines by intestinal epithelial cells. Among SCFAs, the fatty acids containing less than 6 carbons, the most potent activators are probably propionate, butyrate and pentanoate while acetate is a poor activator (PubMed:12496283, PubMed:12711604). {ECO:0000269|PubMed:12496283, ECO:0000269|PubMed:12711604, ECO:0000269|PubMed:18801738, ECO:0000269|PubMed:23066016}.
|
Homo sapiens (Human)
|
O14862
|
AIM2_HUMAN
|
MESKYKEILLLTGLDNITDEELDRFKFFLSDEFNIATGKLHTANRIQVATLMIQNAGAVSAVMKTIRIFQKLNYMLLAKRLQEEKEKVDKQYKSVTKPKPLSQAEMSPAASAAIRNDVAKQRAAPKVSPHVKPEQKQMVAQQESIREGFQKRCLPVMVLKAKKPFTFETQEGKQEMFHATVATEKEFFFVKVFNTLLKDKFIPKRIIIIARYYRHSGFLEVNSASRVLDAESDQKVNVPLNIIRKAGETPKINTLQTQPLGTIVNGLFVVQKVTEKKKNILFDLSDNTGKMEVLGVRNEDTMKCKEGDKVRLTFFTLSKNGEKLQLTSGVHSTIKVIKAKKKT
| null | null |
activation of innate immune response [GO:0002218]; AIM2 inflammasome complex assembly [GO:0140970]; brain development [GO:0007420]; cellular response to interferon-beta [GO:0035458]; cellular response to xenobiotic stimulus [GO:0071466]; defense response to virus [GO:0051607]; DNA damage response [GO:0006974]; immune response [GO:0006955]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; neuron cellular homeostasis [GO:0070050]; pattern recognition receptor signaling pathway [GO:0002221]; positive regulation of cysteine-type endopeptidase activity [GO:2001056]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; pyroptosis [GO:0070269]; pyroptosome complex assembly [GO:1904270]; regulation of behavior [GO:0050795]; T cell homeostasis [GO:0043029]; tumor necrosis factor-mediated signaling pathway [GO:0033209]
|
AIM2 inflammasome complex [GO:0097169]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; site of double-strand break [GO:0035861]
|
cysteine-type endopeptidase activator activity [GO:0140608]; double-stranded DNA binding [GO:0003690]; identical protein binding [GO:0042802]; pattern recognition receptor activity [GO:0038187]; signaling adaptor activity [GO:0035591]
|
PF02760;PF02758;
|
1.10.533.10;2.40.50.140;
|
HIN-200 family
|
PTM: Degraded via selective autophagy following interaction with TRIM11. {ECO:0000269|PubMed:27498865}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19158675, ECO:0000269|PubMed:19158676, ECO:0000269|PubMed:19158679, ECO:0000269|PubMed:24531343, ECO:0000269|PubMed:8454910}. Inflammasome {ECO:0000269|PubMed:19158676, ECO:0000269|PubMed:19158679}. Nucleus {ECO:0000269|PubMed:15582594}. Note=Activated inflammasomes can aggregate in the cytosol as speck-like particles (PubMed:19158675, PubMed:19158676, PubMed:19158679). Activated inflammasomes can also aggregate in the nucleus in response to DNA damage: AIM2 is recruited to double-strand DNA breaks and mediates activation of the AIM2 inflammasome (By similarity). {ECO:0000250|UniProtKB:Q91VJ1, ECO:0000269|PubMed:19158675, ECO:0000269|PubMed:19158676, ECO:0000269|PubMed:19158679}.
| null | null | null | null | null |
FUNCTION: Sensor component of the AIM2 inflammasome, which mediates inflammasome activation in response to the presence of double-stranded DNA (dsDNA) in the cytosol, leading to subsequent pyroptosis (PubMed:17726700, PubMed:19158675, PubMed:19158676, PubMed:19158679, PubMed:20566831, PubMed:23530044, PubMed:26197926, PubMed:26583071, PubMed:29440442, PubMed:33980849, PubMed:37364111). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (PubMed:17726700, PubMed:19158675, PubMed:19158676, PubMed:19158679, PubMed:20566831, PubMed:26197926, PubMed:29440442, PubMed:33980849). Acts as a recognition receptor (PRR): specifically recognizes and binds dsDNA in the cytosol, and mediates the formation of the inflammasome polymeric complex composed of AIM2, CASP1 and PYCARD/ASC (PubMed:17726700, PubMed:19158675, PubMed:19158676, PubMed:19158679, PubMed:20566831, PubMed:26197926, PubMed:29440442, PubMed:33980849). Recruitment of pro-caspase-1 (proCASP1) to the AIM2 inflammasome promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), promoting cytokine secretion (PubMed:17726700, PubMed:19158675, PubMed:19158676, PubMed:19158679, PubMed:20566831). In some cells, CASP1 activation mediates cleavage and activation of GSDMD, triggering pyroptosis without promoting cytokine secretion (PubMed:19158675, PubMed:19158676). Detects cytosolic dsDNA of viral and bacterial origin in a non-sequence-specific manner (PubMed:17726700, PubMed:19158675, PubMed:19158676, PubMed:19158679, PubMed:20566831, PubMed:26197926, PubMed:26583071, PubMed:29440442, PubMed:33980849). Involved in the DNA damage response caused by acute ionizing radiation by mediating pyroptosis of intestinal epithelial cells and bone marrow cells in response to double-strand DNA breaks (By similarity). Mechanistically, AIM2 senses DNA damage in the nucleus to mediate inflammasome assembly and inflammatory cell death (By similarity). Also acts as a regulator of neurodevelopment via its role in the DNA damage response: acts by promoting neural cell death in response to DNA damage in the developing brain, thereby purging genetically compromised cells of the central nervous system (By similarity). Pyroptosis mediated by the AIM2 inflammasome in response to DNA damage is dependent on GSDMD without involving IL1B and IL18 cytokine secretion (By similarity). Also acts as a mediator of pyroptosis, necroptosis and apoptosis (PANoptosis), an integral part of host defense against pathogens, in response to bacterial infection (By similarity). Can also trigger PYCARD/ASC-dependent, caspase-1-independent cell death that involves caspase-8 (CASP8) (By similarity). {ECO:0000250|UniProtKB:Q91VJ1, ECO:0000269|PubMed:17726700, ECO:0000269|PubMed:19158675, ECO:0000269|PubMed:19158676, ECO:0000269|PubMed:19158679, ECO:0000269|PubMed:20566831, ECO:0000269|PubMed:23530044, ECO:0000269|PubMed:26197926, ECO:0000269|PubMed:26583071, ECO:0000269|PubMed:29440442, ECO:0000269|PubMed:33980849, ECO:0000269|PubMed:37364111}.; FUNCTION: Also acts as a tumor suppressor independently of its role in inflammatory response (PubMed:16432157). Able to suppress overt cell proliferation in enterocytes: restricts stem cell proliferation in the intestinal mucosa in an inflammasome-independent manner, contributing to a decrease in the likelihood of colorectal cancer development (By similarity). AIM2 suppresses cell proliferation by inhibiting phosphorylation of AKT1 at 'Ser-473', preventing AKT1 activation and AKT-mTOR signaling pathway (By similarity). Inhibits AKT1 phosphorylation both by inhibiting the activity of PRKDC/DNA-PK kinase and promoting dephosphorylation by PP2A phosphatase (By similarity). Also acts as a key regulator of regulatory T-cells (Treg) homeostasis by promoting their stability: acts by preventing AKT1 activation (By similarity). Its role in Treg homeostasis is important to restain autoimmune diseases (By similarity). {ECO:0000250|UniProtKB:Q91VJ1, ECO:0000269|PubMed:16432157}.
|
Homo sapiens (Human)
|
O14863
|
ZNT4_HUMAN
|
MAGSGAWKRLKSMLRKDDAPLFLNDTSAFDFSDEAGDEGLSRFNKLRVVVADDGSEAPERPVNGAHPTLQADDDSLLDQDLPLTNSQLSLKVDSCDNCSKQREILKQRKVKARLTIAAVLYLLFMIGELVGGYIANSLAIMTDALHMLTDLSAIILTLLALWLSSKSPTKRFTFGFHRLEVLSAMISVLLVYILMGFLLYEAVQRTIHMNYEINGDIMLITAAVGVAVNVIMGFLLNQSGHRHSHSHSLPSNSPTRGSGCERNHGQDSLAVRAAFVHALGDLVQSVGVLIAAYIIRFKPEYKIADPICTYVFSLLVAFTTFRIIWDTVVIILEGVPSHLNVDYIKEALMKIEDVYSVEDLNIWSLTSGKSTAIVHIQLIPGSSSKWEEVQSKANHLLLNTFGMYRCTIQLQSYRQEVDRTCANCQSSSP
| null | null |
response to toxic substance [GO:0009636]; response to zinc ion [GO:0010043]; zinc export across plasma membrane [GO:0140882]; zinc ion import into lysosome [GO:0140916]; zinc ion transmembrane transport [GO:0071577]
|
cytoplasm [GO:0005737]; endosome membrane [GO:0010008]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]
|
antiporter activity [GO:0015297]; metal ion binding [GO:0046872]; zinc ion transmembrane transporter activity [GO:0005385]
|
PF01545;
|
1.20.1510.10;
|
Cation diffusion facilitator (CDF) transporter (TC 2.A.4) family, SLC30A subfamily
|
PTM: Homodimerization through dityrosine bonds is stimulated by oxidative stress. {ECO:0000269|PubMed:19521526}.
|
SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:O55174}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:17349999}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:17349999}; Multi-pass membrane protein {ECO:0000255}. Note=Enriched in vesicles within the basal region of epithelial cells. {ECO:0000250|UniProtKB:O55174}.
|
CATALYTIC ACTIVITY: Reaction=2 H(+)(out) + Zn(2+)(in) = 2 H(+)(in) + Zn(2+)(out); Xref=Rhea:RHEA:72627, ChEBI:CHEBI:15378, ChEBI:CHEBI:29105; Evidence={ECO:0000305|PubMed:19521526};
| null | null | null | null |
FUNCTION: Probable proton-coupled zinc ion antiporter mediating zinc import from cytoplasm potentially into the endocytic compartment (PubMed:19521526). Controls zinc deposition in milk (By similarity). {ECO:0000250|UniProtKB:O35149, ECO:0000305|PubMed:19521526}.
|
Homo sapiens (Human)
|
O14867
|
BACH1_HUMAN
|
MSLSENSVFAYESSVHSTNVLLSLNDQRKKDVLCDVTIFVEGQRFRAHRSVLAACSSYFHSRIVGQADGELNITLPEEVTVKGFEPLIQFAYTAKLILSKENVDEVCKCVEFLSVHNIEESCFQFLKFKFLDSTADQQECPRKKCFSSHCQKTDLKLSLLDQRDLETDEVEEFLENKNVQTPQCKLRRYQGNAKASPPLQDSASQTYESMCLEKDAALALPSLCPKYRKFQKAFGTDRVRTGESSVKDIHASVQPNERSENECLGGVPECRDLQVMLKCDESKLAMEPEETKKDPASQCPTEKSEVTPFPHNSSIDPHGLYSLSLLHTYDQYGDLNFAGMQNTTVLTEKPLSGTDVQEKTFGESQDLPLKSDLGTREDSSVASSDRSSVEREVAEHLAKGFWSDICSTDTPCQMQLSPAVAKDGSEQISQKRSECPWLGIRISESPEPGQRTFTTLSSVNCPFISTLSTEGCSSNLEIGNDDYVSEPQQEPCPYACVISLGDDSETDTEGDSESCSAREQECEVKLPFNAQRIISLSRNDFQSLLKMHKLTPEQLDCIHDIRRRSKNRIAAQRCRKRKLDCIQNLESEIEKLQSEKESLLKERDHILSTLGETKQNLTGLCQKVCKEAALSQEQIQILAKYSAADCPLSFLISEKDKSTPDGELALPSIFSLSDRPPAVLPPCARGNSEPGYARGQESQQMSTATSEQAGPAEQCRQSGGISDFCQQMTDKCTTDE
| null | null |
DNA repair [GO:0006281]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of DNA-templated transcription [GO:0006355]; regulation of metabolic process [GO:0019222]; regulation of transcription by RNA polymerase II [GO:0006357]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; heme binding [GO:0020037]; ligand-activated transcription factor activity [GO:0098531]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00651;PF03131;
|
1.10.880.10;
|
BZIP family, CNC subfamily
|
PTM: Ubiquitinated by the SCF(FBXL17) complex, leading to its degradation by the proteasome. {ECO:0000269|PubMed:24035498}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:24035498}.
| null | null | null | null | null |
FUNCTION: Transcriptional regulator that acts as a repressor or activator, depending on the context. Binds to NF-E2 DNA binding sites. Plays important roles in coordinating transcription activation and repression by MAFK (By similarity). Together with MAF, represses the transcription of genes under the control of the NFE2L2 oxidative stress pathway (PubMed:24035498). {ECO:0000250|UniProtKB:P97302, ECO:0000269|PubMed:24035498}.
|
Homo sapiens (Human)
|
O14874
|
BCKD_HUMAN
|
MILASVLRSGPGGGLPLRPLLGPALALRARSTSATDTHHVEMARERSKTVTSFYNQSAIDAAAEKPSVRLTPTMMLYAGRSQDGSHLLKSARYLQQELPVRIAHRIKGFRCLPFIIGCNPTILHVHELYIRAFQKLTDFPPIKDQADEAQYCQLVRQLLDDHKDVVTLLAEGLRESRKHIEDEKLVRYFLDKTLTSRLGIRMLATHHLALHEDKPDFVGIICTRLSPKKIIEKWVDFARRLCEHKYGNAPRVRINGHVAARFPFIPMPLDYILPELLKNAMRATMESHLDTPYNVPDVVITIANNDVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQDPRISPLFGHLDMHSGAQSGPMHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLRHIDGREESFRI
|
2.7.11.1; 2.7.11.4
| null |
amino acid catabolic process [GO:0009063]; branched-chain amino acid catabolic process [GO:0009083]; lipid biosynthetic process [GO:0008610]; negative regulation of cellular amino acid metabolic process [GO:0045763]; phosphorylation [GO:0016310]; regulation of glucose metabolic process [GO:0010906]
|
mitochondrial matrix [GO:0005759]; mitochondrial oxoglutarate dehydrogenase complex [GO:0009353]; mitochondrion [GO:0005739]
|
[3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase activity [GO:0047323]; ATP binding [GO:0005524]; kinase activity [GO:0016301]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine phosphatase activity [GO:0004722]; pyruvate dehydrogenase (acetyl-transferring) kinase activity [GO:0004740]
|
PF10436;PF02518;
|
1.20.140.20;3.30.565.10;
|
PDK/BCKDK protein kinase family
|
PTM: Autophosphorylated. {ECO:0000269|PubMed:24449431}.
|
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q00972, ECO:0000305|PubMed:24449431}. Note=Detected in the cytosolic compartment of liver cells. {ECO:0000250|UniProtKB:Q00972}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[3-methyl-2-oxobutanoate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[3-methyl-2-oxobutanoate dehydrogenase]; Xref=Rhea:RHEA:17301, Rhea:RHEA-COMP:13695, Rhea:RHEA-COMP:13696, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.4; Evidence={ECO:0000269|PubMed:24449431, ECO:0000269|PubMed:29779826, ECO:0000269|PubMed:37558654}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17302; Evidence={ECO:0000269|PubMed:24449431, ECO:0000269|PubMed:29779826, ECO:0000269|PubMed:37558654}; CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:24449431, ECO:0000269|PubMed:29779826}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000269|PubMed:24449431, ECO:0000269|PubMed:29779826};
| null |
PATHWAY: Protein modification. {ECO:0000269|PubMed:24449431, ECO:0000269|PubMed:29779826}.
| null | null |
FUNCTION: Serine/threonine-protein kinase component of macronutrients metabolism. Forms a functional kinase and phosphatase pair with PPM1K, serving as a metabolic regulatory node that coordinates branched-chain amino acids (BCAAs) with glucose and lipid metabolism via two distinct phosphoprotein targets: mitochondrial BCKDHA subunit of the branched-chain alpha-ketoacid dehydrogenase (BCKDH) complex and cytosolic ACLY, a lipogenic enzyme of Krebs cycle (PubMed:24449431, PubMed:29779826, PubMed:37558654). Phosphorylates and inactivates mitochondrial BCKDH complex a multisubunit complex consisting of three multimeric components each involved in different steps of BCAA catabolism: E1 composed of BCKDHA and BCKDHB, E2 core composed of DBT monomers, and E3 composed of DLD monomers. Associates with the E2 component of BCKDH complex and phosphorylates BCKDHA on Ser-337, leading to conformational changes that interrupt substrate channeling between E1 and E2 and inactivates the BCKDH complex (PubMed:29779826, PubMed:37558654). Phosphorylates ACLY on Ser-455 in response to changes in cellular carbohydrate abundance such as occurs during fasting to feeding metabolic transition. Refeeding stimulates MLXIPL/ChREBP transcription factor, leading to increased BCKDK to PPM1K expression ratio, phosphorylation and activation of ACLY that ultimately results in the generation of malonyl-CoA and oxaloacetate immediate substrates of de novo lipogenesis and glucogenesis, respectively (PubMed:29779826). Recognizes phosphosites having SxxE/D canonical motif (PubMed:29779826). {ECO:0000269|PubMed:24449431, ECO:0000269|PubMed:29779826, ECO:0000269|PubMed:37558654}.
|
Homo sapiens (Human)
|
O14879
|
IFIT3_HUMAN
|
MSEVTKNSLEKILPQLKCHFTWNLFKEDSVSRDLEDRVCNQIEFLNTEFKATMYNLLAYIKHLDGNNEAALECLRQAEELIQQEHADQAEIRSLVTWGNYAWVYYHLGRLSDAQIYVDKVKQTCKKFSNPYSIEYSELDCEEGWTQLKCGRNERAKVCFEKALEEKPNNPEFSSGLAIAMYHLDNHPEKQFSTDVLKQAIELSPDNQYVKVLLGLKLQKMNKEAEGEQFVEEALEKSPCQTDVLRSAAKFYRRKGDLDKAIELFQRVLESTPNNGYLYHQIGCCYKAKVRQMQNTGESEASGNKEMIEALKQYAMDYSNKALEKGLNPLNAYSDLAEFLETECYQTPFNKEVPDAEKQQSHQRYCNLQKYNGKSEDTAVQHGLEGLSISKKSTDKEEIKDQPQNVSENLLPQNAPNYWYLQGLIHKQNGDLLQAAKCYEKELGRLLRDAPSGIGSIFLSASELEDGSEEMGQGAVSSSPRELLSNSEQLN
| null | null |
antiviral innate immune response [GO:0140374]; defense response to virus [GO:0051607]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell population proliferation [GO:0008285]; response to virus [GO:0009615]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]
|
identical protein binding [GO:0042802]
|
PF13424;PF13176;PF13181;
|
1.25.40.10;
|
IFIT family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17050680, ECO:0000269|PubMed:18706081}. Mitochondrion {ECO:0000269|PubMed:21813773}.
| null | null | null | null | null |
FUNCTION: IFN-induced antiviral protein which acts as an inhibitor of cellular as well as viral processes, cell migration, proliferation, signaling, and viral replication. Enhances MAVS-mediated host antiviral responses by serving as an adapter bridging TBK1 to MAVS which leads to the activation of TBK1 and phosphorylation of IRF3 and phosphorylated IRF3 translocates into nucleus to promote antiviral gene transcription. Exhibits an antiproliferative activity via the up-regulation of cell cycle negative regulators CDKN1A/p21 and CDKN1B/p27. Normally, CDKN1B/p27 turnover is regulated by COPS5, which binds CDKN1B/p27 in the nucleus and exports it to the cytoplasm for ubiquitin-dependent degradation. IFIT3 sequesters COPS5 in the cytoplasm, thereby increasing nuclear CDKN1B/p27 protein levels. Up-regulates CDKN1A/p21 by down-regulating MYC, a repressor of CDKN1A/p21. Can negatively regulate the apoptotic effects of IFIT2. {ECO:0000269|PubMed:17050680, ECO:0000269|PubMed:20686046, ECO:0000269|PubMed:21190939, ECO:0000269|PubMed:21642987, ECO:0000269|PubMed:21813773}.
|
Homo sapiens (Human)
|
O14880
|
MGST3_HUMAN
|
MAVLSKEYGFVLLTGAASFIMVAHLAINVSKARKKYKVEYPIMYSTDPENGHIFNCIQRAHQNTLEVYPPFLFFLAVGGVYHPRIASGLGLAWIVGRVLYAYGYYTGEPSKRSRGALGSIALLGLVGTTVCSAFQHLGWVKSGLGSGPKCCH
|
1.11.1.-; 2.5.1.-; 4.4.1.20
| null |
arachidonic acid metabolic process [GO:0019369]; leukotriene biosynthetic process [GO:0019370]; lipid metabolic process [GO:0006629]; prostanoid metabolic process [GO:0006692]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; nuclear envelope [GO:0005635]
|
glutathione peroxidase activity [GO:0004602]; glutathione transferase activity [GO:0004364]; identical protein binding [GO:0042802]; leukotriene-C4 synthase activity [GO:0004464]
|
PF01124;
|
1.20.120.550;
|
MAPEG family
| null |
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:27184847}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=leukotriene C4 = glutathione + leukotriene A4; Xref=Rhea:RHEA:17617, ChEBI:CHEBI:57463, ChEBI:CHEBI:57925, ChEBI:CHEBI:57973; EC=4.4.1.20; Evidence={ECO:0000269|PubMed:9278457}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17619; Evidence={ECO:0000305|PubMed:9278457}; CATALYTIC ACTIVITY: Reaction=15-deoxy-Delta(12,14)-prostaglandin J2 + glutathione = 15-deoxy-Delta(12,14)-prostaglandin J2-S-(R)-glutathione; Xref=Rhea:RHEA:75963, ChEBI:CHEBI:57925, ChEBI:CHEBI:85236, ChEBI:CHEBI:194498; Evidence={ECO:0000269|PubMed:36370807}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75964; Evidence={ECO:0000305|PubMed:36370807}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + 2 glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:48620, ChEBI:CHEBI:15377, ChEBI:CHEBI:57450, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90632; Evidence={ECO:0000269|PubMed:9278457}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48621; Evidence={ECO:0000305|PubMed:9278457};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=21 uM for (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate {ECO:0000269|PubMed:9278457}; KM=9.2 uM for 15-deoxy-Delta12,14-prostaglandin J2 {ECO:0000269|PubMed:36370807};
|
PATHWAY: Lipid metabolism; leukotriene C4 biosynthesis. {ECO:0000305|PubMed:9278457}.; PATHWAY: Lipid metabolism; arachidonate metabolism. {ECO:0000305|PubMed:9278457}.
| null | null |
FUNCTION: Displays both glutathione S-transferase and glutathione peroxidase activities toward oxyeicosanoids, as part of cellular detoxification as well as synthesis of bioactive metabolites (PubMed:36370807, PubMed:9278457). Catalyzes conjugate addition of reduced glutathione to the alpha, beta-unsaturated C=C carbonyl group of eisosanoids such as leukotriene A4 and 15-deoxy-Delta12,14-prostaglandin J2 to form GSH adducts relevant to the inflammatory response (PubMed:36370807, PubMed:9278457). Catalyzes glutathione-dependent reduction of eicosanoid peroxides to yield the corresponding eicosanoid hydroxides (PubMed:9278457). {ECO:0000269|PubMed:36370807, ECO:0000269|PubMed:9278457}.
|
Homo sapiens (Human)
|
O14893
|
GEMI2_HUMAN
|
MRRAELAGLKTMAWVPAESAVEELMPRLLPVEPCDLTEGFDPSVPPRTPQEYLRRVQIEAAQCPDVVVAQIDPKKLKRKQSVNISLSGCQPAPEGYSPTLQWQQQQVAQFSTVRQNVNKHRSHWKSQQLDSNVTMPKSEDEEGWKKFCLGEKLCADGAVGPATNESPGIDYVQIGFPPLLSIVSRMNQATVTSVLEYLSNWFGERDFTPELGRWLYALLACLEKPLLPEAHSLIRQLARRCSEVRLLVDSKDDERVPALNLLICLVSRYFDQRDLADEPS
| null | null |
mRNA processing [GO:0006397]; negative regulation of RNA binding [GO:1905215]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]; spliceosomal complex assembly [GO:0000245]; spliceosomal snRNP assembly [GO:0000387]
|
cytosol [GO:0005829]; Gemini of coiled bodies [GO:0097504]; nuclear body [GO:0016604]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SMN complex [GO:0032797]; SMN-Sm protein complex [GO:0034719]; spliceosomal complex [GO:0005681]
| null |
PF04938;
|
1.20.5.220;1.20.58.1070;
|
Gemin-2 family
| null |
SUBCELLULAR LOCATION: Nucleus, gem. Cytoplasm. Note=Localized in subnuclear structures next to coiled bodies, called gems, which are highly enriched in spliceosomal snRNPs. Also found in the cytoplasm.
| null | null | null | null | null |
FUNCTION: The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs (PubMed:18984161, PubMed:9323129). Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core) (PubMed:18984161). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG (5Sm) are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP (PubMed:18984161). To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A (PubMed:18984161, PubMed:9323129). Binding of snRNA inside 5Sm ultimately triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP (PubMed:31799625). Within the SMN complex, GEMIN2 constrains the conformation of 5Sm, thereby promoting 5Sm binding to snRNA containing the snRNP code (a nonameric Sm site and a 3'-adjacent stem-loop), thus preventing progression of assembly until a cognate substrate is bound (PubMed:16314521, PubMed:21816274, PubMed:31799625). {ECO:0000269|PubMed:16314521, ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:21816274, ECO:0000269|PubMed:31799625, ECO:0000269|PubMed:9323129}.
|
Homo sapiens (Human)
|
O14894
|
T4S5_HUMAN
|
MCTGKCARCVGLSLITLCLVCIVANALLLVPNGETSWTNTNHLSLQVWLMGGFIGGGLMVLCPGIAAVRAGGKGCCGAGCCGNRCRMLRSVFSSAFGVLGAIYCLSVSGAGLRNGPRCLMNGEWGYHFEDTAGAYLLNRTLWDRCEAPPRVVPWNVTLFSLLVAASCLEIVLCGIQLVNATIGVFCGDCRKKQDTPH
| null | null |
cell cycle [GO:0007049]; regulation of G1/S transition of mitotic cell cycle [GO:2000045]
|
lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]
|
arginine binding [GO:0034618]
|
PF05805;
| null |
L6 tetraspanin family
| null |
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:30956113}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:30956113}; Multi-pass membrane protein {ECO:0000255}. Note=Localization to cell membrane increases during conditions of arginine depletion and translocation to lysosome membrane seen upon arginine repletion. {ECO:0000269|PubMed:30956113}.
| null | null | null | null | null |
FUNCTION: Acts as a lysosomal membrane arginine sensor (PubMed:30956113). Forms a complex with MTOR and SLC38A9 on lysosomal membranes in an arginine-regulated manner, leading to arginine efflux which enables the activation of mTORC1 which subsequently leads to RPS6KB1 and EIF4EBP1 phosphorylations (PubMed:30956113). Facilitates cell cycle G1/S phase progression and the translocation of the CDK4-CCND1 complex into the nucleus (PubMed:20399237). CDKN1B and RHOA/ROCK signaling activity are involved in TM4SF5-mediated acceleration of G1/S phase progression (PubMed:20399237). {ECO:0000269|PubMed:20399237, ECO:0000269|PubMed:30956113}.
|
Homo sapiens (Human)
|
O14896
|
IRF6_HUMAN
|
MALHPRRVRLKPWLVAQVDSGLYPGLIWLHRDSKRFQIPWKHATRHSPQQEEENTIFKAWAVETGKYQEGVDDPDPAKWKAQLRCALNKSREFNLMYDGTKEVPMNPVKIYQVCDIPQPQGSIINPGSTGSAPWDEKDNDVDEEDEEDELDQSQHHVPIQDTFPFLNINGSPMAPASVGNCSVGNCSPEAVWPKTEPLEMEVPQAPIQPFYSSPELWISSLPMTDLDIKFQYRGKEYGQTMTVSNPQGCRLFYGDLGPMPDQEELFGPVSLEQVKFPGPEHITNEKQKLFTSKLLDVMDRGLILEVSGHAIYAIRLCQCKVYWSGPCAPSLVAPNLIERQKKVKLFCLETFLSDLIAHQKGQIEKQPPFEIYLCFGEEWPDGKPLERKLILVQVIPVVARMIYEMFSGDFTRSFDSGSVRLQISTPDIKDNIVAQLKQLYRILQTQESWQPMQPTPSMQLPPALPPQ
| null | null |
cell development [GO:0048468]; cranial skeletal system development [GO:1904888]; immune system process [GO:0002376]; keratinocyte differentiation [GO:0030216]; keratinocyte proliferation [GO:0043616]; limb development [GO:0060173]; mammary gland epithelial cell differentiation [GO:0060644]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of keratinocyte proliferation [GO:0010839]; negative regulation of stem cell proliferation [GO:2000647]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; roof of mouth development [GO:0060021]; stem cell proliferation [GO:0072089]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00605;PF10401;
|
2.60.200.10;1.10.10.10;
|
IRF family
|
PTM: Phosphorylated. Phosphorylation status depends on the cell cycle and is a signal for ubiquitination and proteasome-mediated degradation. {ECO:0000269|PubMed:16049006, ECO:0000269|PubMed:18212048}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:16049006, ECO:0000269|PubMed:18212048}. Note=Translocates to nucleus in response to an activating signal. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Probable DNA-binding transcriptional activator. Key determinant of the keratinocyte proliferation-differentiation switch involved in appropriate epidermal development (By similarity). Plays a role in regulating mammary epithelial cell proliferation (By similarity). May regulate WDR65 transcription (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O14901
|
KLF11_HUMAN
|
MHTPDFAGPDDARAVDIMDICESILERKRHDSERSTCSILEQTDMEAVEALVCMSSWGQRSQKGDLLRIRPLTPVSDSGDVTTTVHMDAATPELPKDFHSLSTLCITPPQSPDLVEPSTRTPVSPQVTDSKACTATDVLQSSAVVARALSGGAERGLLGLEPVPSSPCRAKGTSVIRHTGESPAACFPTIQTPDCRLSDSREGEEQLLGHFETLQDTHLTDSLLSTNLVSCQPCLHKSGGLLLTDKGQQAGWPGAVQTCSPKNYENDLPRKTTPLISVSVPAPPVLCQMIPVTGQSSMLPAFLKPPPQLSVGTVRPILAQAAPAPQPVFVGPAVPQGAVMLVLPQGALPPPAPCAANVMAAGNTKLLPLAPAPVFITSSQNCVPQVDFSRRRNYVCSFPGCRKTYFKSSHLKAHLRTHTGEKPFNCSWDGCDKKFARSDELSRHRRTHTGEKKFVCPVCDRRFMRSDHLTKHARRHMTTKKIPGWQAEVGKLNRIASAESPGSPLVSMPASA
| null | null |
apoptotic process [GO:0006915]; cellular response to peptide [GO:1901653]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of apoptotic process [GO:0043065]; regulation of G1/S transition of mitotic cell cycle [GO:2000045]; regulation of transcription by RNA polymerase II [GO:0006357]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]; transcription cis-regulatory region binding [GO:0000976]
|
PF00096;
|
3.30.160.60;
|
Sp1 C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9748269}.
| null | null | null | null | null |
FUNCTION: Transcription factor (PubMed:10207080, PubMed:9748269). Activates the epsilon- and gamma-globin gene promoters and, to a much lower degree, the beta-globin gene and represses promoters containing SP1-like binding inhibiting cell growth (PubMed:10207080, PubMed:16131492, PubMed:9748269). Represses transcription of SMAD7 which enhances TGF-beta signaling (By similarity). Induces apoptosis (By similarity). {ECO:0000250|UniProtKB:Q8K1S5, ECO:0000269|PubMed:10207080, ECO:0000269|PubMed:16131492}.
|
Homo sapiens (Human)
|
O14904
|
WNT9A_HUMAN
|
MLDGSPLARWLAAAFGLTLLLAALRPSAAYFGLTGSEPLTILPLTLEPEAAAQAHYKACDRLKLERKQRRMCRRDPGVAETLVEAVSMSALECQFQFRFERWNCTLEGRYRASLLKRGFKETAFLYAISSAGLTHALAKACSAGRMERCTCDEAPDLENREAWQWGGCGDNLKYSSKFVKEFLGRRSSKDLRARVDFHNNLVGVKVIKAGVETTCKCHGVSGSCTVRTCWRQLAPFHEVGKHLKHKYETALKVGSTTNEAAGEAGAISPPRGRASGAGGSDPLPRTPELVHLDDSPSFCLAGRFSPGTAGRRCHREKNCESICCGRGHNTQSRVVTRPCQCQVRWCCYVECRQCTQREEVYTCKG
| null | null |
canonical Wnt signaling pathway [GO:0060070]; cell fate commitment [GO:0045165]; cellular response to retinoic acid [GO:0071300]; cornea development in camera-type eye [GO:0061303]; embryonic skeletal joint development [GO:0072498]; iris morphogenesis [GO:0061072]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of chondrocyte differentiation [GO:0032331]; neuron differentiation [GO:0030182]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; frizzled binding [GO:0005109]; receptor ligand activity [GO:0048018]
|
PF00110;
|
3.30.2460.20;
|
Wnt family
|
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:26902720}.
| null | null | null | null | null |
FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Functions in the canonical Wnt/beta-catenin signaling pathway. Required for normal timing of IHH expression during embryonic bone development, normal chondrocyte maturation and for normal bone mineralization during embryonic bone development. Plays a redundant role in maintaining joint integrity. {ECO:0000250|UniProtKB:O42280, ECO:0000250|UniProtKB:Q8R5M2}.
|
Homo sapiens (Human)
|
O14905
|
WNT9B_HUMAN
|
MRPPPALALAGLCLLALPAAAASYFGLTGREVLTPFPGLGTAAAPAQGGAHLKQCDLLKLSRRQKQLCRREPGLAETLRDAAHLGLLECQFQFRHERWNCSLEGRMGLLKRGFKETAFLYAVSSAALTHTLARACSAGRMERCTCDDSPGLESRQAWQWGVCGDNLKYSTKFLSNFLGSKRGNKDLRARADAHNTHVGIKAVKSGLRTTCKCHGVSGSCAVRTCWKQLSPFRETGQVLKLRYDSAVKVSSATNEALGRLELWAPARQGSLTKGLAPRSGDLVYMEDSPSFCRPSKYSPGTAGRVCSREASCSSLCCGRGYDTQSRLVAFSCHCQVQWCCYVECQQCVQEELVYTCKH
| null | null |
branching involved in ureteric bud morphogenesis [GO:0001658]; canonical Wnt signaling pathway [GO:0060070]; cell fate commitment [GO:0045165]; cellular response to retinoic acid [GO:0071300]; cellular response to starvation [GO:0009267]; collecting duct development [GO:0072044]; cornea development in camera-type eye [GO:0061303]; embryonic cranial skeleton morphogenesis [GO:0048701]; establishment of planar polarity involved in nephron morphogenesis [GO:0072046]; in utero embryonic development [GO:0001701]; kidney rudiment formation [GO:0072003]; male genitalia development [GO:0030539]; mesenchymal stem cell maintenance involved in nephron morphogenesis [GO:0072038]; mesonephric duct formation [GO:0072181]; metanephric tubule formation [GO:0072174]; midbrain dopaminergic neuron differentiation [GO:1904948]; negative regulation of stem cell population maintenance [GO:1902455]; neuron differentiation [GO:0030182]; non-canonical Wnt signaling pathway [GO:0035567]; regulation of asymmetric cell division [GO:0009786]; regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis [GO:0003339]; regulation of protein phosphorylation [GO:0001932]; regulation of tube size [GO:0035150]; response to retinoic acid [GO:0032526]; roof of mouth development [GO:0060021]; uterus morphogenesis [GO:0061038]; Wnt signaling pathway, planar cell polarity pathway [GO:0060071]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
co-receptor binding [GO:0039706]; cytokine activity [GO:0005125]; frizzled binding [GO:0005109]; receptor ligand activity [GO:0048018]
|
PF00110;
|
3.30.2460.20;
|
Wnt family
|
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:26902720}.
| null | null | null | null | null |
FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt/beta-catenin signaling pathway. Required for normal embryonic kidney development, and for normal development of the urogenital tract, including uterus and part of the oviduct and the upper vagina in females, and epididymis and vas deferens in males. Activates a signaling cascade in the metanephric mesenchyme that induces tubulogenesis. Acts upstream of WNT4 in the signaling pathways that mediate development of kidney tubules and the Muellerian ducts. Plays a role in cranofacial development and is required for normal fusion of the palate during embryonic development (By similarity). {ECO:0000250|UniProtKB:O35468, ECO:0000305|PubMed:20093360}.
|
Homo sapiens (Human)
|
O14907
|
TX1B3_HUMAN
|
MSYIPGQPVTAVVQRVEIHKLRQGENLILGFSIGGGIDQDPSQNPFSEDKTDKGIYVTRVSEGGPAEIAGLQIGDKIMQVNGWDMTMVTHDQARKRLTKRSEEVVRLLVTRQSLQKAVQQSMLS
| null | null |
activation of GTPase activity [GO:0090630]; cell-cell adhesion [GO:0098609]; chemical synaptic transmission [GO:0007268]; embryo development [GO:0009790]; establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of protein localization to cell surface [GO:2000009]; negative regulation of Wnt signaling pathway [GO:0030178]; receptor clustering [GO:0043113]; receptor localization to synapse [GO:0097120]; Rho protein signal transduction [GO:0007266]; Wnt signaling pathway [GO:0016055]
|
actin cytoskeleton [GO:0015629]; basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; fibrillar center [GO:0001650]; intracellular membrane-bounded organelle [GO:0043231]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; postsynaptic density membrane [GO:0098839]
|
beta-catenin binding [GO:0008013]
|
PF00595;
|
2.30.42.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Recruited to the cell membrane by interaction with membrane proteins.
| null | null | null | null | null |
FUNCTION: May regulate a number of protein-protein interactions by competing for PDZ domain binding sites. Binds CTNNB1 and may thereby act as an inhibitor of the Wnt signaling pathway. Competes with LIN7A for KCNJ4 binding, and thereby promotes KCNJ4 internalization. May play a role in the Rho signaling pathway. May play a role in activation of CDC42 by the viral protein HPV16 E6. {ECO:0000269|PubMed:10940294, ECO:0000269|PubMed:16855024, ECO:0000269|PubMed:21139582}.
|
Homo sapiens (Human)
|
O14908
|
GIPC1_HUMAN
|
MPLGLGRRKKAPPLVENEEAEPGRGGLGVGEPGPLGGGGSGGPQMGLPPPPPALRPRLVFHTQLAHGSPTGRIEGFTNVKELYGKIAEAFRLPTAEVMFCTLNTHKVDMDKLLGGQIGLEDFIFAHVKGQRKEVEVFKSEDALGLTITDNGAGYAFIKRIKEGSVIDHIHLISVGDMIEAINGQSLLGCRHYEVARLLKELPRGRTFTLKLTEPRKAFDMISQRSAGGRPGSGPQLGTGRGTLRLRSRGPATVEDLPSAFEEKAIEKVDDLLESYMGIRDTELAATMVELGKDKRNPDELAEALDERLGDFAFPDEFVFDVWGAIGDAKVGRY
| null | null |
cellular response to interleukin-7 [GO:0098761]; chemical synaptic transmission [GO:0007268]; endothelial cell migration [GO:0043542]; G protein-coupled receptor signaling pathway [GO:0007186]; glutamate secretion [GO:0014047]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; positive regulation of cytokinesis [GO:0032467]; positive regulation of melanin biosynthetic process [GO:0048023]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; presynaptic modulation of chemical synaptic transmission [GO:0099171]; protein targeting [GO:0006605]; regulation of protein stability [GO:0031647]; regulation of synaptic plasticity [GO:0048167]
|
cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; dendritic shaft [GO:0043198]; dendritic spine [GO:0043197]; extracellular exosome [GO:0070062]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; Schaffer collateral - CA1 synapse [GO:0098685]; synaptic vesicle [GO:0008021]; vesicle membrane [GO:0012506]
|
actin binding [GO:0003779]; cadherin binding [GO:0045296]; identical protein binding [GO:0042802]; myosin binding [GO:0017022]; signaling receptor binding [GO:0005102]
|
PF00595;
|
2.30.42.10;
|
GIPC family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32413282, ECO:0000269|PubMed:9770488}. Membrane {ECO:0000269|PubMed:9770488}; Peripheral membrane protein.
| null | null | null | null | null |
FUNCTION: May be involved in G protein-linked signaling.
|
Homo sapiens (Human)
|
O14910
|
LIN7A_HUMAN
|
MLKPSVTSAPTADMATLTVVQPLTLDRDVARAIELLEKLQESGEVPVHKLQSLKKVLQSEFCTAIREVYQYMHETITVNGCPEFRARATAKATVAAFAASEGHSHPRVVELPKTDEGLGFNVMGGKEQNSPIYISRIIPGGVAERHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAKDSVKLVVRYTPKVLEEMEARFEKLRTARRRQQQQLLIQQQQQQQQQQTQQNHMS
| null | null |
exocytosis [GO:0006887]; inner ear development [GO:0048839]; maintenance of epithelial cell apical/basal polarity [GO:0045199]; neurotransmitter secretion [GO:0007269]; protein localization to basolateral plasma membrane [GO:1903361]; protein transport [GO:0015031]; protein-containing complex assembly [GO:0065003]; synaptic vesicle transport [GO:0048489]
|
basolateral plasma membrane [GO:0016323]; bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; extracellular exosome [GO:0070062]; MPP7-DLG1-LIN7 complex [GO:0097025]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; presynapse [GO:0098793]; synapse [GO:0045202]
|
L27 domain binding [GO:0097016]
|
PF02828;PF00595;
|
2.30.42.10;1.10.287.650;
|
Lin-7 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8JZS0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8JZS0}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q8JZS0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8JZS0}. Cell junction {ECO:0000250|UniProtKB:Q8JZS0}. Postsynaptic density membrane {ECO:0000250|UniProtKB:Q8JZS0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8JZS0}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q8JZS0}. Note=Mainly basolateral in renal epithelial cells. {ECO:0000250|UniProtKB:Q8JZS0}.
| null | null | null | null | null |
FUNCTION: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules (By similarity). This complex may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells. {ECO:0000250|UniProtKB:Q8JZS0, ECO:0000269|PubMed:12967566}.
|
Homo sapiens (Human)
|
O14917
|
PCD17_HUMAN
|
MYLSICCCFLLWAPALTLKNLNYSVPEEQGAGTVIGNIGRDARLQPGLPPAERGGGGRSKSGSYRVLENSAPHLLDVDADSGLLYTKQRIDRESLCRHNAKCQLSLEVFANDKEICMIKVEIQDINDNAPSFSSDQIEMDISENAAPGTRFPLTSAHDPDAGENGLRTYLLTRDDHGLFGLDVKSRGDGTKFPELVIQKALDREQQNHHTLVLTALDGGEPPRSATVQINVKVIDSNDNSPVFEAPSYLVELPENAPLGTVVIDLNATDADEGPNGEVLYSFSSYVPDRVRELFSIDPKTGLIRVKGNLDYEENGMLEIDVQARDLGPNPIPAHCKVTVKLIDRNDNAPSIGFVSVRQGALSEAAPPGTVIALVRVTDRDSGKNGQLQCRVLGGGGTGGGGGLGGPGGSVPFKLEENYDNFYTVVTDRPLDRETQDEYNVTIVARDGGSPPLNSTKSFAIKILDENDNPPRFTKGLYVLQVHENNIPGEYLGSVLAQDPDLGQNGTVSYSILPSHIGDVSIYTYVSVNPTNGAIYALRSFNFEQTKAFEFKVLAKDSGAPAHLESNATVRVTVLDVNDNAPVIVLPTLQNDTAELQVPRNAGLGYLVSTVRALDSDFGESGRLTYEIVDGNDDHLFEIDPSSGEIRTLHPFWEDVTPVVELVVKVTDHGKPTLSAVAKLIIRSVSGSLPEGVPRVNGEQHHWDMSLPLIVTLSTISIILLAAMITIAVKCKRENKEIRTYNCRIAEYSHPQLGGGKGKKKKINKNDIMLVQSEVEERNAMNVMNVVSSPSLATSPMYFDYQTRLPLSSPRSEVMYLKPASNNLTVPQGHAGCHTSFTGQGTNASETPATRMSIIQTDNFPAEPNYMGSRQQFVQSSSTFKDPERASLRDSGHGDSDQADSDQDTNKGSCCDMSVREALKMKTTSTKSQPLEQEPEECVNCTDECRVLGHSDRCWMPQFPAANQAENADYRTNLFVPTVEANVETETYETVNPTGKKTFCTFGKDKREHTILIANVKPYLKAKRALSPLLQEVPSASSSPTKACIEPCTSTKGSLDGCEAKPGALAEASSQYLPTDSQYLSPSKQPRDPPFMASDQMARVFADVHSRASRDSSEMGAVLEQLDHPNRDLGRESVDAEEVVREIDKLLQDCRGNDPVAVRK
| null | null |
adult behavior [GO:0030534]; cell adhesion [GO:0007155]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; negative regulation of synaptic transmission [GO:0050805]; presynaptic active zone assembly [GO:1904071]; regulation of synaptic vesicle clustering [GO:2000807]; synaptic membrane adhesion [GO:0099560]
|
GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]
|
calcium ion binding [GO:0005509]
|
PF00028;PF08266;
|
2.60.40.60;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Potential calcium-dependent cell-adhesion protein.
|
Homo sapiens (Human)
|
O14920
|
IKKB_HUMAN
|
MSWSPSLTTQTCGAWEMKERLGTGGFGNVIRWHNQETGEQIAIKQCRQELSPRNRERWCLEIQIMRRLTHPNVVAARDVPEGMQNLAPNDLPLLAMEYCQGGDLRKYLNQFENCCGLREGAILTLLSDIASALRYLHENRIIHRDLKPENIVLQQGEQRLIHKIIDLGYAKELDQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFLPNWQPVQWHSKVRQKSEVDIVVSEDLNGTVKFSSSLPYPNNLNSVLAERLEKWLQLMLMWHPRQRGTDPTYGPNGCFKALDDILNLKLVHILNMVTGTIHTYPVTEDESLQSLKARIQQDTGIPEEDQELLQEAGLALIPDKPATQCISDGKLNEGHTLDMDLVFLFDNSKITYETQISPRPQPESVSCILQEPKRNLAFFQLRKVWGQVWHSIQTLKEDCNRLQQGQRAAMMNLLRNNSCLSKMKNSMASMSQQLKAKLDFFKTSIQIDLEKYSEQTEFGITSDKLLLAWREMEQAVELCGRENEVKLLVERMMALQTDIVDLQRSPMGRKQGGTLDDLEEQARELYRRLREKPRDQRTEGDSQEMVRLLLQAIQSFEKKVRVIYTQLSKTVVCKQKALELLPKVEEVVSLMNEDEKTVVRLQEKRQKELWNLLKIACSKVRGPVSGSPDSMNASRLSQPGQLMSQPSTASNSLPEPAKKSEELVAEAHNLCTLLENAIQDTVREQDQSFTALDWSWLQTEEEEHSCLEQAS
|
2.7.11.1; 2.7.11.10
| null |
antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent [GO:0002479]; canonical NF-kappaB signal transduction [GO:0007249]; cellular response to tumor necrosis factor [GO:0071356]; cortical actin cytoskeleton organization [GO:0030866]; Fc-epsilon receptor signaling pathway [GO:0038095]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; interleukin-1-mediated signaling pathway [GO:0070498]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; negative regulation of bicellular tight junction assembly [GO:1903347]; negative regulation of myosin-light-chain-phosphatase activity [GO:0035509]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein localization to plasma membrane [GO:0072659]; protein maturation [GO:0051604]; protein phosphorylation [GO:0006468]; regulation of establishment of endothelial barrier [GO:1903140]; regulation of phosphorylation [GO:0042325]; regulation of tumor necrosis factor-mediated signaling pathway [GO:0010803]; response to virus [GO:0009615]; stimulatory C-type lectin receptor signaling pathway [GO:0002223]; stress-activated MAPK cascade [GO:0051403]; T cell receptor signaling pathway [GO:0050852]; toll-like receptor 3 signaling pathway [GO:0034138]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]; tumor necrosis factor-mediated signaling pathway [GO:0033209]
|
CD40 receptor complex [GO:0035631]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; IkappaB kinase complex [GO:0008385]; membrane raft [GO:0045121]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; IkappaB kinase activity [GO:0008384]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; scaffold protein binding [GO:0097110]; transferrin receptor binding [GO:1990459]
|
PF18397;PF12179;PF00069;
|
1.20.1270.250;6.10.250.2110;1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, I-kappa-B kinase subfamily
|
PTM: Upon cytokine stimulation, phosphorylated on Ser-177 and Ser-181 by MEKK1 and/or MAP3K14/NIK as well as TBK1 and PRKCZ; which enhances activity (PubMed:10022904, PubMed:16207722). Phosphorylated by MAP3K7/TAK1 in response to NOD1 and NOD2 signaling, promoting activation and phosphorylation of NF-kappa-B inhibitors, leading to NF-kappa-B activation (PubMed:11460167). Once activated, autophosphorylates on the C-terminal serine cluster; which decreases activity and prevents prolonged activation of the inflammatory response (PubMed:10195894). Phosphorylated by the IKK-related kinases TBK1 and IKBKE, which is associated with reduced CHUK/IKKA and IKBKB activity and NF-kappa-B-dependent gene transcription (PubMed:10783893). Dephosphorylated at Ser-177 and Ser-181 by PPM1A and PPM1B (PubMed:18930133). {ECO:0000269|PubMed:10022904, ECO:0000269|PubMed:10195894, ECO:0000269|PubMed:10783893, ECO:0000269|PubMed:11460167, ECO:0000269|PubMed:16207722, ECO:0000269|PubMed:18930133}.; PTM: (Microbial infection) Acetylation of Thr-180 by Yersinia YopJ prevents phosphorylation and activation, thus blocking the I-kappa-B pathway. {ECO:0000269|PubMed:16728640, ECO:0000269|PubMed:17116858}.; PTM: Ubiquitinated. Monoubiquitination involves TRIM21 that leads to inhibition of Tax-induced NF-kappa-B signaling. According to PubMed:19675099, 'Ser-163' does not serve as a monoubiquitination site. According to PubMed:16267042, ubiquitination on 'Ser-163' modulates phosphorylation on C-terminal serine residues. {ECO:0000269|PubMed:16267042, ECO:0000269|PubMed:19675099}.; PTM: (Microbial infection) Monoubiquitination by TRIM21 is disrupted by Yersinia YopJ. {ECO:0000269|PubMed:19675099}.; PTM: Hydroxylated by PHD1/EGLN2, loss of hydroxylation under hypoxic conditions results in activation of NF-kappa-B. {ECO:0000269|PubMed:17114296}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20797629}. Nucleus {ECO:0000269|PubMed:20797629}. Membrane raft {ECO:0000269|PubMed:17287217}. Note=Colocalized with DPP4 in membrane rafts. {ECO:0000269|PubMed:17287217}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[I-kappa-B protein] = ADP + H(+) + O-phospho-L-seryl-[I-kappa-B protein]; Xref=Rhea:RHEA:19073, Rhea:RHEA-COMP:13698, Rhea:RHEA-COMP:13699, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.10; Evidence={ECO:0000269|PubMed:9346484}; CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:25326418}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000305};
| null | null | null | null |
FUNCTION: Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:30337470, PubMed:9346484). Acts as a part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation (PubMed:9346484). Phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:9346484). These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:9346484). In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:9346484). In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE (PubMed:11297557, PubMed:14673179, PubMed:20410276, PubMed:21138416). IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs (PubMed:11297557, PubMed:20410276, PubMed:21138416). Phosphorylates FOXO3, mediating the TNF-dependent inactivation of this pro-apoptotic transcription factor (PubMed:15084260). Also phosphorylates other substrates including NAA10, NCOA3, BCL10 and IRS1 (PubMed:17213322, PubMed:19716809). Phosphorylates RIPK1 at 'Ser-25' which represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death (By similarity). Phosphorylates the C-terminus of IRF5, stimulating IRF5 homodimerization and translocation into the nucleus (PubMed:25326418). {ECO:0000250|UniProtKB:O88351, ECO:0000269|PubMed:11297557, ECO:0000269|PubMed:14673179, ECO:0000269|PubMed:15084260, ECO:0000269|PubMed:17213322, ECO:0000269|PubMed:19716809, ECO:0000269|PubMed:20410276, ECO:0000269|PubMed:20434986, ECO:0000269|PubMed:20797629, ECO:0000269|PubMed:21138416, ECO:0000269|PubMed:25326418, ECO:0000269|PubMed:30337470, ECO:0000269|PubMed:9346484}.
|
Homo sapiens (Human)
|
O14924
|
RGS12_HUMAN
|
MFRAGEASKRPLPGPSPPRVRSVEVARGRAGYGFTLSGQAPCVLSCVMRGSPADFVGLRAGDQILAVNEINVKKASHEDVVKLIGKCSGVLHMVIAEGVGRFESCSSDEEGGLYEGKGWLKPKLDSKALGINRAERVVEEMQSGGIFNMIFENPSLCASNSEPLKLKQRSLSESAATRFDVGHESINNPNPNMLSKEEISKVIHDDSVFSIGLESHDDFALDASILNVAMIVGYLGSIELPSTSSNLESDSLQAIRGCMRRLRAEQKIHSLVTMKIMHDCVQLSTDKAGVVAEYPAEKLAFSAVCPDDRRFFGLVTMQTNDDGSLAQEEEGALRTSCHVFMVDPDLFNHKIHQGIARRFGFECTADPDTNGCLEFPASSLPVLQFISVLYRDMGELIEGMRARAFLDGDADAHQNNSTSSNSDSGIGNFHQEEKSNRVLVVDLGGSSSRHGPGGSAWDGVGGRGAQPWGAPWTGPFCPDPEGSPPFEAAHQTDRFWDLNKHLGPASPVEVPPASLRSSVPPSKRGTVGAGCGFNQRWLPVHVLREWQCGHTSDQDSYTDSTDGWSSINCGTLPPPMSKIPADRYRVEGSFAQPPLNAPKREWSRKAFGMQSIFGPHRNVRKTKEDKKGSKFGRGTGLTQPSQRTSARRSFGRSKRFSITRSLDDLESATVSDGELTGADLKDCVSNNSLSSNASLPSVQSCRRLRERRVASWAVSFERLLQDPVGVRYFSDFLRKEFSEENILFWQACEYFNHVPAHDKKELSYRAREIFSKFLCSKATTPVNIDSQAQLADDVLRAPHPDMFKEQQLQIFNLMKFDSYTRFLKSPLYQECILAEVEGRALPDSQQVPSSPASKHSLGSDHSSVSTPKKLSGKSKSGRSLNEELGDEDSEKKRKGAFFSWSRTRSTGRSQKKREHGDHADDALHANGGLCRRESQGSVSSAGSLDLSEACRTLAPEKDKATKHCCIHLPDGTSCVVAVKAGFSIKDILSGLCERHGINGAAADLFLVGGDKPLVLHQDSSILESRDLRLEKRTLFRLDLVPINRSVGLKAKPTKPVTEVLRPVVARYGLDLSGLLVRLSGEKEPLDLGAPISSLDGQRVVLEEKDPSRGKASADKQKGVPVKQNTAVNSSSRNHSATGEERTLGKSNSIKIKGENGKNARDPRLSKREESIAKIGKKKYQKINLDEAEEFFELISKAQSNRADDQRGLLRKEDLVLPEFLRLPPGSTELTLPTPAAVAKGFSKRSATGNGRESASQPGEQWEPVQESSDSPSTSPGSASSPPGPPGTTPPGQKSPSGPFCTPQSPVSLAQEGTAQIWKRQSQEVEAGGIQTVEDEHVAELTLMGEGDISSPNSTLLPPPSTPQEVPGPSRPGSGTHGSRDLPVNRIIDVDLVTGSAPGRDGGIAGAQAGPGRSQASGGPPTSDLPGLGPVPGEPAKPKTSAHHATFV
| null | null |
G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of signal transduction [GO:0009968]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]
|
condensed nuclear chromosome [GO:0000794]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; nuclear matrix [GO:0016363]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; synapse [GO:0045202]
|
GTPase activator activity [GO:0005096]; GTPase activity [GO:0003924]; GTPase regulator activity [GO:0030695]
|
PF02188;PF00595;PF02196;PF00615;PF16613;PF16611;PF16612;
|
1.10.196.10;2.30.42.10;2.30.29.30;1.10.167.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10869340}. Cytoplasm {ECO:0000250|UniProtKB:O08774}. Cell projection, dendrite {ECO:0000250|UniProtKB:O08774}. Synapse {ECO:0000250|UniProtKB:O08774}.; SUBCELLULAR LOCATION: [Isoform 5]: Nucleus matrix {ECO:0000269|PubMed:12024043}. Note=Also localized to discrete nuclear foci that are distinct from sites of RNA processing, PML nuclear bodies, and PcG domains. {ECO:0000269|PubMed:12024043}.
| null | null | null | null | null |
FUNCTION: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. {ECO:0000250|UniProtKB:O08774}.; FUNCTION: [Isoform 5]: Behaves as a cell cycle-dependent transcriptional repressor, promoting inhibition of S-phase DNA synthesis. {ECO:0000269|PubMed:12024043}.
|
Homo sapiens (Human)
|
O14925
|
TIM23_HUMAN
|
MEGGGGSGNKTTGGLAGFFGAGGAGYSHADLAGVPLTGMNPLSPYLNVDPRYLVQDTDEFILPTGANKTRGRFELAFFTIGGCCMTGAAFGAMNGLRLGLKETQNMAWSKPRNVQILNMVTRQGALWANTLGSLALLYSAFGVIIEKTRGAEDDLNTVAAGTMTGMLYKCTGGLRGIARGGLTGLTLTSLYALYNNWEHMKGSLLQQSL
| null | null |
intracellular protein transport [GO:0006886]; protein import into mitochondrial matrix [GO:0030150]; protein targeting to mitochondrion [GO:0006626]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; TIM23 mitochondrial import inner membrane translocase complex [GO:0005744]
|
protein transmembrane transporter activity [GO:0008320]
|
PF02466;
| null |
Tim17/Tim22/Tim23 family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:25997101}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. {ECO:0000305|PubMed:10339406}.
|
Homo sapiens (Human)
|
O14926
|
FSCN2_HUMAN
|
MPTNGLHQVLKIQFGLVNDTDRYLTAESFGFKVNASAPSLKRKQTWVLEPDPGQGTAVLLRSSHLGRYLSAEEDGRVACEAEQPGRDCRFLVLPQPDGRWVLRSEPHGRFFGGTEDQLSCFATAVSPAELWTVHLAIHPQAHLLSVSRRRYVHLCPREDEMAADGDKPWGVDALLTLIFRSRRYCLKSCDSRYLRSDGRLVWEPEPRACYTLEFKAGKLAFKDCDGHYLAPVGPAGTLKAGRNTRPGKDELFDLEESHPQVVLVAANHRYVSVRQGVNVSANQDDELDHETFLMQIDQETKKCTFYSSTGGYWTLVTHGGIHATATQVSANTMFEMEWRGRRVALKASNGRYVCMKKNGQLAAISDFVGKDEEFTLKLINRPILVLRGLDGFVCHHRGSNQLDTNRSVYDVFHLSFSDGAYRIRGRDGGFWYTGSHGSVCSDGERAEDFVFEFRERGRLAIRARSGKYLRGGASGLLRADADAPAGTALWEY
| null | null |
actin cytoskeleton organization [GO:0030036]; actin filament bundle assembly [GO:0051017]; anatomical structure morphogenesis [GO:0009653]; cell migration [GO:0016477]; establishment or maintenance of cell polarity [GO:0007163]; eye photoreceptor cell development [GO:0042462]; visual perception [GO:0007601]
|
actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; stereocilium [GO:0032420]
|
actin binding [GO:0003779]; actin filament binding [GO:0051015]; protein-macromolecule adaptor activity [GO:0030674]
|
PF06268;
|
2.80.10.50;
|
Fascin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, stereocilium {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Acts as an actin bundling protein. May play a pivotal role in photoreceptor cell-specific events, such as disk morphogenesis.
|
Homo sapiens (Human)
|
O14929
|
HAT1_HUMAN
|
MAGFGAMEKFLVEYKSAVEKKLAEYKCNTNTAIELKLVRFPEDLENDIRTFFPEYTHQLFGDDETAFGYKGLKILLYYIAGSLSTMFRVEYASKVDENFDCVEADDVEGKIRQIIPPGFCTNTNDFLSLLEKEVDFKPFGTLLHTYSVLSPTGGENFTFQIYKADMTCRGFREYHERLQTFLMWFIETASFIDVDDERWHYFLVFEKYNKDGATLFATVGYMTVYNYYVYPDKTRPRVSQMLILTPFQGQGHGAQLLETVHRYYTEFPTVLDITAEDPSKSYVKLRDFVLVKLCQDLPCFSREKLMQGFNEDMVIEAQQKFKINKQHARRVYEILRLLVTDMSDAEQYRSYRLDIKRRLISPYKKKQRDLAKMRKCLRPEELTNQMNQIEISMQHEQLEESFQELVEDYRRVIERLAQE
|
2.3.1.48
| null |
chromosome organization [GO:0051276]; internal protein amino acid acetylation [GO:0006475]; nucleosome assembly [GO:0006334]; subtelomeric heterochromatin formation [GO:0031509]
|
chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; mitochondrion [GO:0005739]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
|
histone acetyltransferase activity [GO:0004402]; histone binding [GO:0042393]; histone H4 acetyltransferase activity [GO:0010485]; histone H4K12 acetyltransferase activity [GO:0043997]
|
PF21183;PF10394;
|
1.10.10.390;3.40.630.30;3.90.360.10;
|
HAT1 family
|
PTM: Phosphorylated by AMPK at Ser-190; phosphorylation increases HAT1 activity. {ECO:0000269|PubMed:28143904}.
|
SUBCELLULAR LOCATION: [Isoform A]: Nucleus matrix {ECO:0000269|PubMed:20148353, ECO:0000269|PubMed:23653357}. Mitochondrion {ECO:0000269|PubMed:32081014}.; SUBCELLULAR LOCATION: [Isoform B]: Cytoplasm {ECO:0000269|PubMed:20148353}. Nucleus {ECO:0000269|PubMed:20148353}. Nucleus matrix {ECO:0000269|PubMed:20148353}. Nucleus, nucleoplasm {ECO:0000269|PubMed:20148353}. Note=Localization is predominantly nuclear in normal cells. Treatment with hydrogen peroxide or ionizing radiation enhances nuclear localization through redistribution of existing protein. {ECO:0000269|PubMed:20148353}.
|
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000269|PubMed:11585814, ECO:0000269|PubMed:22615379, ECO:0000269|PubMed:9427644};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.68 uM for acetyl-CoA {ECO:0000269|PubMed:22615379}; Note=kcat is 4.14 sec(-1) for acetyl-CoA. {ECO:0000269|PubMed:22615379};
| null | null | null |
FUNCTION: Histone acetyltransferase that plays a role in different biological processes including cell cycle progression, glucose metabolism, histone production or DNA damage repair (PubMed:20953179, PubMed:23653357, PubMed:31278053, PubMed:32081014). Coordinates histone production and acetylation via H4 promoter binding (PubMed:31278053). Acetylates histone H4 at 'Lys-5' (H4K5ac) and 'Lys-12' (H4K12ac) and, to a lesser extent, histone H2A at 'Lys-5' (H2AK5ac) (PubMed:11585814, PubMed:22615379). Drives H4 production by chromatin binding to support chromatin replication and acetylation. Since transcription of H4 genes is tightly coupled to S-phase, plays an important role in S-phase entry and progression (PubMed:31278053). Promotes homologous recombination in DNA repair by facilitating histone turnover and incorporation of acetylated H3.3 at sites of double-strand breaks (PubMed:23653357). In addition, acetylates other substrates such as chromatin-related proteins (PubMed:32081014). Acetylates also RSAD2 which mediates the interaction of ubiquitin ligase UBE4A with RSAD2 leading to RSAD2 ubiquitination and subsequent degradation (PubMed:31812350). {ECO:0000269|PubMed:11585814, ECO:0000269|PubMed:20953179, ECO:0000269|PubMed:22615379, ECO:0000269|PubMed:23653357, ECO:0000269|PubMed:31278053, ECO:0000269|PubMed:31812350, ECO:0000269|PubMed:32081014}.; FUNCTION: (Microbial infection) Contributes to hepatitis B virus (HBV) replication by acetylating histone H4 at the sites of 'Lys-5' and 'Lys-12' on the covalently closed circular DNA (cccDNA) minichromosome leading to its accumulation within the host cell. {ECO:0000269|PubMed:31695772}.
|
Homo sapiens (Human)
|
O14931
|
NCTR3_HUMAN
|
MAWMLLLILIMVHPGSCALWVSQPPEIRTLEGSSAFLPCSFNASQGRLAIGSVTWFRDEVVPGKEVRNGTPEFRGRLAPLASSRFLHDHQAELHIRDVRGHDASIYVCRVEVLGLGVGTGNGTRLVVEKEHPQLGAGTVLLLRAGFYAVSFLSVAVGSTVYYQGKCLTWKGPRRQLPAVVPAPLPPPCGSSAHLLPPVPGG
| null | null |
cell recognition [GO:0008037]; immune response [GO:0006955]; immune response-activating cell surface receptor signaling pathway [GO:0002429]; inflammatory response [GO:0006954]; natural killer cell activation [GO:0030101]; positive regulation of natural killer cell mediated cytotoxicity [GO:0045954]
|
plasma membrane [GO:0005886]
|
identical protein binding [GO:0042802]
|
PF07686;
|
2.60.40.10;
|
Natural cytotoxicity receptor (NCR) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10562324}; Single-pass type I membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Cell membrane receptor of natural killer/NK cells that is activated by binding of extracellular ligands including BAG6 and NCR3LG1. Stimulates NK cells cytotoxicity toward neighboring cells producing these ligands. It controls, for instance, NK cells cytotoxicity against tumor cells. Engagement of NCR3 by BAG6 also promotes myeloid dendritic cells (DC) maturation, both through killing DCs that did not acquire a mature phenotype, and inducing the release by NK cells of TNFA and IFNG which promote DC maturation. {ECO:0000269|PubMed:10562324, ECO:0000269|PubMed:15784725, ECO:0000269|PubMed:18055229, ECO:0000269|PubMed:18852879}.
|
Homo sapiens (Human)
|
O14933
|
UB2L6_HUMAN
|
MMASMRVVKELEDLQKKPPPYLRNLSSDDANVLVWHALLLPDQPPYHLKAFNLRISFPPEYPFKPPMIKFTTKIYHPNVDENGQICLPIISSENWKPCTKTCQVLEALNVLVNRPNIREPLRMDLADLLTQNPELFRKNAEEFTLRFGVDRPS
|
2.3.2.23
| null |
innate immune response [GO:0045087]; ISG15-protein conjugation [GO:0032020]; protein modification process [GO:0036211]; protein polyubiquitination [GO:0000209]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]
|
ISG15 transferase activity [GO:0042296]; ubiquitin binding [GO:0043130]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842]
|
PF00179;
|
3.10.110.10;
|
Ubiquitin-conjugating enzyme family
|
PTM: ISGylated. {ECO:0000269|PubMed:16428300}.
| null |
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133};
| null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000255|PROSITE-ProRule:PRU00388}.
| null | null |
FUNCTION: Catalyzes the covalent attachment of ubiquitin or ISG15 to other proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Promotes ubiquitination and subsequent proteasomal degradation of FLT3. {ECO:0000269|PubMed:15131269, ECO:0000269|PubMed:16428300, ECO:0000269|PubMed:20508617}.
|
Homo sapiens (Human)
|
O14936
|
CSKP_HUMAN
|
MADDDVLFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQLRKFNARRKLKGAVLAAVSSHKFNSFYGDPPEELPDFSEDPTSSGLLAAERAVSQVLDSLEEIHALTDCSEKDLDFLHSVFQDQHLHTLLDLYDKINTKSSPQIRNPPSDAVQRAKEVLEEISCYPENNDAKELKRILTQPHFMALLQTHDVVAHEVYSDEALRVTPPPTSPYLNGDSPESANGDMDMENVTRVRLVQFQKNTDEPMGITLKMNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIVPSYRTQSSSCERDSPSTSRQSPANGHSSTNNSVSDLPSTTQPKGRQIYVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPELQEWRVACIAMEKTKQEQQASCTWFGKKKKQYKDKYLAKHNAVFDQLDLVTYEEVVKLPAFKRKTLVLLGAHGVGRRHIKNTLITKHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLETIRKIHEQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPTITPGLNEDESLQRLQKESDILQRTYAHYFDLTIINNEIDETIRHLEEAVELVCTAPQWVPVSWVY
|
2.7.11.1
|
COFACTOR: Note=Unlike other protein kinases, does not require a divalent cation such as magnesium for catalytic activity. {ECO:0000269|PubMed:18423203};
|
calcium ion import [GO:0070509]; cell adhesion [GO:0007155]; establishment of localization in cell [GO:0051649]; negative regulation of cell-matrix adhesion [GO:0001953]; negative regulation of cellular response to growth factor stimulus [GO:0090288]; negative regulation of keratinocyte proliferation [GO:0010839]; negative regulation of wound healing [GO:0061045]; phosphorylation [GO:0016310]; positive regulation of calcium ion import [GO:0090280]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of neurotransmitter secretion [GO:0046928]; regulation of synaptic vesicle exocytosis [GO:2000300]
|
actin cytoskeleton [GO:0015629]; basement membrane [GO:0005604]; basolateral plasma membrane [GO:0016323]; cell-cell junction [GO:0005911]; ciliary membrane [GO:0060170]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; nuclear lamina [GO:0005652]; nuclear matrix [GO:0016363]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]; Schaffer collateral - CA1 synapse [GO:0098685]; vesicle [GO:0031982]
|
ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; guanylate kinase activity [GO:0004385]; neurexin family protein binding [GO:0042043]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; signaling receptor binding [GO:0005102]
|
PF00625;PF02828;PF00595;PF00069;PF07653;
|
2.30.42.10;6.10.140.620;3.30.63.10;1.10.287.650;3.40.50.300;2.30.30.40;1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, CaMK subfamily; MAGUK family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q62915}. Cytoplasm {ECO:0000250|UniProtKB:Q62915}. Cell membrane {ECO:0000250|UniProtKB:Q62915}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q62915}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:18423203}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000269|PubMed:18423203}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=563 uM for ATP {ECO:0000269|PubMed:18423203}; KM=748.7 uM for ATP (when NRXN1 is phosphorylated) {ECO:0000269|PubMed:18423203}; Vmax=4.9 nmol/min/mmol enzyme {ECO:0000269|PubMed:18423203}; Note=Kinetics of autophosphorylation assay were measured, rather than phosphorylation of an exogenous substrate.;
| null | null | null |
FUNCTION: Multidomain scaffolding Mg(2+)-independent protein kinase that catalyzes the phosphotransfer from ATP to proteins such as NRXN1, and plays a role in synaptic transmembrane protein anchoring and ion channel trafficking (PubMed:18423203). Contributes to neural development and regulation of gene expression via interaction with the transcription factor TBR1. Binds to cell-surface proteins, including amyloid precursor protein, neurexins and syndecans. May mediate a link between the extracellular matrix and the actin cytoskeleton via its interaction with syndecan and with the actin/spectrin-binding protein 4.1. Component of the LIN-10-LIN-2-LIN-7 complex, which associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules (By similarity). {ECO:0000250|UniProtKB:O70589, ECO:0000269|PubMed:18423203}.
|
Homo sapiens (Human)
|
O14939
|
PLD2_HUMAN
|
MTATPESLFPTGDELDSSQLQMESDEVDTLKEGEDPADRMHPFLAIYELQSLKVHPLVFAPGVPVTAQVVGTERYTSGSKVGTCTLYSVRLTHGDFSWTTKKKYRHFQELHRDLLRHKVLMSLLPLARFAVAYSPARDAGNREMPSLPRAGPEGSTRHAASKQKYLENYLNRLLTMSFYRNYHAMTEFLEVSQLSFIPDLGRKGLEGMIRKRSGGHRVPGLTCCGRDQVCYRWSKRWLVVKDSFLLYMCLETGAISFVQLFDPGFEVQVGKRSTEARHGVRIDTSHRSLILKCSSYRQARWWAQEITELAQGPGRDFLQLHRHDSYAPPRPGTLARWFVNGAGYFAAVADAILRAQEEIFITDWWLSPEVYLKRPAHSDDWRLDIMLKRKAEEGVRVSILLFKEVELALGINSGYSKRALMLLHPNIKVMRHPDQVTLWAHHEKLLVVDQVVAFLGGLDLAYGRWDDLHYRLTDLGDSSESAASQPPTPRPDSPATPDLSHNQFFWLGKDYSNLITKDWVQLDRPFEDFIDRETTPRMPWRDVGVVVHGLPARDLARHFIQRWNFTKTTKAKYKTPTYPYLLPKSTSTANQLPFTLPGGQCTTVQVLRSVDRWSAGTLENSILNAYLHTIRESQHFLYIENQFFISCSDGRTVLNKVGDEIVDRILKAHKQGWCYRVYVLLPLLPGFEGDISTGGGNSIQAILHFTYRTLCRGEYSILHRLKAAMGTAWRDYISICGLRTHGELGGHPVSELIYIHSKVLIADDRTVIIGSANINDRSLLGKRDSELAVLIEDTETEPSLMNGAEYQAGRFALSLRKHCFGVILGANTRPDLDLRDPICDDFFQLWQDMAESNANIYEQIFRCLPSNATRSLRTLREYVAVEPLATVSPPLARSELTQVQGHLVHFPLKFLEDESLLPPLGSKEGMIPLEVWT
|
3.1.4.4
| null |
cytoskeleton organization [GO:0007010]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; phosphatidic acid biosynthetic process [GO:0006654]; phospholipid catabolic process [GO:0009395]; regulation of vesicle-mediated transport [GO:0060627]; small GTPase-mediated signal transduction [GO:0007264]; synaptic vesicle recycling [GO:0036465]
|
endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]; plasma membrane region [GO:0098590]; presynapse [GO:0098793]
|
N-acylphosphatidylethanolamine-specific phospholipase D activity [GO:0070290]; phosphatidylinositol binding [GO:0035091]; phospholipase D activity [GO:0004630]
|
PF00614;PF13091;PF00787;
|
3.30.870.10;3.30.1520.10;2.30.29.30;
|
Phospholipase D family
|
PTM: Phosphorylated by FGR. {ECO:0000250|UniProtKB:P70498}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P97813}; Lipid-anchor {ECO:0000250|UniProtKB:P97813}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4; Evidence={ECO:0000269|PubMed:9582313}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14446; Evidence={ECO:0000305|PubMed:9582313}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:44872, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72859, ChEBI:CHEBI:72999; Evidence={ECO:0000269|PubMed:9582313}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44873; Evidence={ECO:0000305|PubMed:9582313};
| null | null | null | null |
FUNCTION: Function as phospholipase selective for phosphatidylcholine (PubMed:9582313). May have a role in signal-induced cytoskeletal regulation and/or endocytosis (By similarity). {ECO:0000250|UniProtKB:P97813, ECO:0000269|PubMed:9582313}.
|
Homo sapiens (Human)
|
O14944
|
EREG_HUMAN
|
MTAGRRMEMLCAGRVPALLLCLGFHLLQAVLSTTVIPSCIPGESSDNCTALVQTEDNPRVAQVSITKCSSDMNGYCLHGQCIYLVDMSQNYCRCEVGYTGVRCEHFFLTVHQPLSKEYVALTVILIILFLITVVGSTYYFCRWYRNRKSKEPKKEYERVTSGDPELPQV
| null | null |
anatomical structure morphogenesis [GO:0009653]; angiogenesis [GO:0001525]; animal organ morphogenesis [GO:0009887]; cell-cell signaling [GO:0007267]; cytokine-mediated signaling pathway [GO:0019221]; epidermal growth factor receptor signaling pathway [GO:0007173]; ERBB2-EGFR signaling pathway [GO:0038134]; ERBB2-ERBB4 signaling pathway [GO:0038135]; ERBB4-ERBB4 signaling pathway [GO:0038138]; female meiotic nuclear division [GO:0007143]; keratinocyte differentiation [GO:0030216]; keratinocyte proliferation [GO:0043616]; luteinizing hormone signaling pathway [GO:0042700]; mRNA transcription [GO:0009299]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of smooth muscle cell differentiation [GO:0051151]; oocyte maturation [GO:0001556]; ovarian cumulus expansion [GO:0001550]; ovulation [GO:0030728]; positive regulation of cell division [GO:0051781]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cytokine production [GO:0001819]; positive regulation of DNA replication [GO:0045740]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of innate immune response [GO:0045089]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of phosphorylation [GO:0042327]; positive regulation of protein kinase activity [GO:0045860]; positive regulation of smooth muscle cell proliferation [GO:0048661]; primary follicle stage [GO:0048160]; response to peptide hormone [GO:0043434]; wound healing [GO:0042060]
|
clathrin-coated endocytic vesicle membrane [GO:0030669]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
epidermal growth factor receptor binding [GO:0005154]; growth factor activity [GO:0008083]; receptor ligand activity [GO:0048018]; transmembrane receptor protein tyrosine kinase activator activity [GO:0030297]
| null |
2.10.25.10;
| null | null |
SUBCELLULAR LOCATION: [Epiregulin]: Secreted, extracellular space {ECO:0000269|PubMed:9337852}.; SUBCELLULAR LOCATION: [Proepiregulin]: Cell membrane {ECO:0000269|PubMed:9337852}; Single-pass type I membrane protein {ECO:0000269|PubMed:9337852}.
| null | null | null | null | null |
FUNCTION: Ligand of the EGF receptor/EGFR and ERBB4. Stimulates EGFR and ERBB4 tyrosine phosphorylation (PubMed:9419975). Contributes to inflammation, wound healing, tissue repair, and oocyte maturation by regulating angiogenesis and vascular remodeling and by stimulating cell proliferation (PubMed:24631357). {ECO:0000269|PubMed:9419975, ECO:0000303|PubMed:24631357}.
|
Homo sapiens (Human)
|
O14948
|
TFEC_HUMAN
|
MTLDHQIINPTLKWSQPAVPSGGPLVQHAHTTLDSDAGLTENPLTKLLAIGKEDDNAQWHMEDVIEDIIGMESSFKEEGADSPLLMQRTLSGSILDVYSGEQGISPINMGLTSASCPSSLPMKREITETDTRALAKERQKKDNHNLIERRRRYNINYRIKELGTLIPKSNDPDMRWNKGTILKASVEYIKWLQKEQQRARELEHRQKKLEQANRRLLLRIQELEIQARTHGLPTLASLGTVDLGAHVTKQQSHPEQNSVDYCQQLTVSQGPSPELCDQAIAFSDPLSYFTDLSFSAALKEEQRLDGMLLDDTISPFGTDPLLSATSPAVSKESSRRSSFSSDDGDEL
| null | null |
cellular response to heat [GO:0034605]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF11851;PF00010;
|
4.10.280.10;
|
MiT/TFE family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:11467950}.
| null | null | null | null | null |
FUNCTION: Transcriptional regulator that acts as a repressor or an activator. Acts as a transcriptional repressor on minimal promoter containing element F (that includes an E-box sequence). Binds to element F in an E-box sequence-specific manner. Acts as a transcriptional transactivator on the proximal promoter region of the tartrate-resistant acid phosphatase (TRAP) E-box containing promoter (By similarity). Collaborates with MITF in target gene activation (By similarity). Acts as a transcriptional repressor on minimal promoter containing mu E3 enhancer sequence (By similarity). Binds to mu E3 DNA sequence of the immunoglobulin heavy-chain gene enhancer (By similarity). Binds DNA in a homo- or heterodimeric form. {ECO:0000250, ECO:0000269|PubMed:11467950, ECO:0000269|PubMed:9256061}.
|
Homo sapiens (Human)
|
O14949
|
QCR8_HUMAN
|
MGREFGNLTRMRHVISYSLSPFEQRAYPHVFTKGIPNVLRRIRESFFRVVPQFVVFYLIYTWGTEEFERSKRKNPAAYENDK
| null | null |
cellular respiration [GO:0045333]; cerebellar Purkinje cell layer development [GO:0021680]; hippocampus development [GO:0021766]; hypothalamus development [GO:0021854]; midbrain development [GO:0030901]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; pons development [GO:0021548]; pyramidal neuron development [GO:0021860]; subthalamus development [GO:0021539]; thalamus development [GO:0021794]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739]
| null |
PF02939;
|
1.20.5.210;
|
UQCRQ/QCR8 family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P08525}; Single-pass membrane protein {ECO:0000250|UniProtKB:P08525}.
| null | null | null | null | null |
FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. {ECO:0000250|UniProtKB:P08525}.
|
Homo sapiens (Human)
|
O14950
|
ML12B_HUMAN
|
MSSKKAKTKTTKKRPQRATSNVFAMFDQSQIQEFKEAFNMIDQNRDGFIDKEDLHDMLASLGKNPTDAYLDAMMNEAPGPINFTMFLTMFGEKLNGTDPEDVIRNAFACFDEEATGTIQEDYLRELLTTMGDRFTDEEVDELYREAPIDKKGNFNYIEFTRILKHGAKDKDD
| null | null |
platelet aggregation [GO:0070527]; regulation of cell shape [GO:0008360]
|
apical part of cell [GO:0045177]; brush border [GO:0005903]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; myofibril [GO:0030016]; myosin II complex [GO:0016460]; stress fiber [GO:0001725]; Z disc [GO:0030018]
|
calcium ion binding [GO:0005509]; myosin heavy chain binding [GO:0032036]
|
PF08976;PF13499;
|
1.10.238.10;
| null |
PTM: Phosphorylation increases the actin-activated myosin ATPase activity and thereby regulates the contractile activity. It is required to generate the driving force in the migration of the cells but not necessary for localization of myosin-2 at the leading edge. Phosphorylation is reduced following epigallocatechin-3-O-gallate treatment. {ECO:0000269|PubMed:11942626, ECO:0000269|PubMed:12429016, ECO:0000269|PubMed:15946647, ECO:0000269|PubMed:17126281}.
| null | null | null | null | null | null |
FUNCTION: Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Phosphorylation triggers actin polymerization in vascular smooth muscle. Implicated in cytokinesis, receptor capping, and cell locomotion. {ECO:0000269|PubMed:10965042}.
|
Homo sapiens (Human)
|
O14958
|
CASQ2_HUMAN
|
MKRTHLFIVGIYFLSSCRAEEGLNFPTYDGKDRVVSLSEKNFKQVLKKYDLLCLYYHEPVSSDKVTQKQFQLKEIVLELVAQVLEHKAIGFVMVDAKKEAKLAKKLGFDEEGSLYILKGDRTIEFDGEFAADVLVEFLLDLIEDPVEIISSKLEVQAFERIEDYIKLIGFFKSEDSEYYKAFEEAAEHFQPYIKFFATFDKGVAKKLSLKMNEVDFYEPFMDEPIAIPNKPYTEEELVEFVKEHQRPTLRRLRPEEMFETWEDDLNGIHIVAFAEKSDPDGYEFLEILKQVARDNTDNPDLSILWIDPDDFPLLVAYWEKTFKIDLFRPQIGVVNVTDADSVWMEIPDDDDLPTAEELEDWIEDVLSGKINTEDDDEDDDDDDNSDEEDNDDSDDDDDE
| null | null |
cardiac muscle contraction [GO:0060048]; cellular response to caffeine [GO:0071313]; detection of calcium ion [GO:0005513]; intracellular calcium ion homeostasis [GO:0006874]; negative regulation of potassium ion transmembrane transporter activity [GO:1901017]; negative regulation of potassium ion transport [GO:0043267]; negative regulation of ryanodine-sensitive calcium-release channel activity [GO:0060315]; protein polymerization [GO:0051258]; Purkinje myocyte to ventricular cardiac muscle cell signaling [GO:0086029]; regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion [GO:0010881]; regulation of cell communication by electrical coupling [GO:0010649]; regulation of heart rate [GO:0002027]; regulation of membrane repolarization [GO:0060306]; regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0010880]; sequestering of calcium ion [GO:0051208]; striated muscle contraction [GO:0006941]
|
calcium channel complex [GO:0034704]; cytoplasm [GO:0005737]; junctional sarcoplasmic reticulum membrane [GO:0014701]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum lumen [GO:0033018]; sarcoplasmic reticulum membrane [GO:0033017]; Z disc [GO:0030018]
|
calcium ion binding [GO:0005509]; calcium ion sequestering activity [GO:0140314]; calcium-dependent protein binding [GO:0048306]; ion binding [GO:0043167]; protein homodimerization activity [GO:0042803]
|
PF01216;
|
3.40.30.10;
|
Calsequestrin family
|
PTM: Phosphorylation in the C-terminus, probably by CK2, moderately increases calcium buffering capacity. {ECO:0000269|PubMed:21416293}.; PTM: N-glycosylated. {ECO:0000269|PubMed:15485681}.
|
SUBCELLULAR LOCATION: Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:O09161}. Note=This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of cardiac and slow skeletal muscle cells. {ECO:0000250|UniProtKB:O09161}.
| null | null | null | null | null |
FUNCTION: Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, especially at the interface between subunits. Can bind around 60 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR2; this plays an important role in triggering muscle contraction. Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats. {ECO:0000269|PubMed:16908766, ECO:0000269|PubMed:17881003, ECO:0000269|PubMed:18399795, ECO:0000269|PubMed:21416293}.
|
Homo sapiens (Human)
|
O14960
|
LECT2_HUMAN
|
MFSTKALLLAGLISTALAGPWANICAGKSSNEIRTCDRHGCGQYSAQRSQRPHQGVDILCSAGSTVYAPFTGMIVGQEKPYQNKNAINNGVRISGRGFCVKMFYIKPIKYKGPIKKGEKLGTLLPLQKVYPGIQSHVHIENCDSSDPTAYL
| null | null |
chemotaxis [GO:0006935]; skeletal system development [GO:0001501]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]
|
identical protein binding [GO:0042802]; metal ion binding [GO:0046872]
|
PF01551;
|
2.70.70.10;
|
LECT2/MIM-1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8877413}. Secreted {ECO:0000269|PubMed:8877413}.
| null | null | null | null | null |
FUNCTION: Has a neutrophil chemotactic activity. Also a positive regulator of chondrocyte proliferation (PubMed:9524238). Does not show metalloendopeptidase activity (PubMed:27334921). {ECO:0000269|PubMed:27334921, ECO:0000269|PubMed:9524238}.
|
Homo sapiens (Human)
|
O14964
|
HGS_HUMAN
|
MGRGSGTFERLLDKATSQLLLETDWESILQICDLIRQGDTQAKYAVNSIKKKVNDKNPHVALYALEVMESVVKNCGQTVHDEVANKQTMEELKDLLKRQVEVNVRNKILYLIQAWAHAFRNEPKYKVVQDTYQIMKVEGHVFPEFKESDAMFAAERAPDWVDAEECHRCRVQFGVMTRKHHCRACGQIFCGKCSSKYSTIPKFGIEKEVRVCEPCYEQLNRKAEGKATSTTELPPEYLTSPLSQQSQLPPKRDETALQEEEELQLALALSQSEAEEKERLRQKSTYTSYPKAEPMPSASSAPPASSLYSSPVNSSAPLAEDIDPELARYLNRNYWEKKQEEARKSPTPSAPVPLTEPAAQPGEGHAAPTNVVENPLPETDSQPIPPSGGPFSEPQFHNGESEESHEQFLKALQNAVTTFVNRMKSNHMRGRSITNDSAVLSLFQSINGMHPQLLELLNQLDERRLYYEGLQDKLAQIRDARGALSALREEHREKLRRAAEEAERQRQIQLAQKLEIMRQKKQEYLEVQRQLAIQRLQEQEKERQMRLEQQKQTVQMRAQMPAFPLPYAQLQAMPAAGGVLYQPSGPASFPSTFSPAGSVEGSPMHGVYMSQPAPAAGPYPSMPSTAADPSMVSAYMYPAGATGAQAAPQAQAGPTASPAYSSYQPTPTAGYQNVASQAPQSLPAISQPPQSSTMGYMGSQSVSMGYQPYNMQNLMTTLPSQDASLPPQQPYIAGQQPMYQQMAPSGGPPQQQPPVAQQPQAQGPPAQGSEAQLISFD
| null | null |
endocytic recycling [GO:0032456]; endosomal transport [GO:0016197]; macroautophagy [GO:0016236]; membrane fission [GO:0090148]; membrane invagination [GO:0010324]; multivesicular body assembly [GO:0036258]; negative regulation of angiogenesis [GO:0016525]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of platelet-derived growth factor receptor signaling pathway [GO:0010642]; negative regulation of receptor signaling pathway via JAK-STAT [GO:0046426]; negative regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030948]; positive regulation of exosomal secretion [GO:1903543]; positive regulation of gene expression [GO:0010628]; protein localization to membrane [GO:0072657]; protein targeting to lysosome [GO:0006622]; protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043328]; receptor internalization [GO:0031623]; regulation of MAP kinase activity [GO:0043405]; regulation of protein catabolic process [GO:0042176]; signal transduction [GO:0007165]
|
cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; ESCRT-0 complex [GO:0033565]; extracellular exosome [GO:0070062]; lysosome [GO:0005764]; multivesicular body membrane [GO:0032585]; phagocytic vesicle lumen [GO:0097013]
|
metal ion binding [GO:0046872]; phosphatidylinositol binding [GO:0035091]; protein domain specific binding [GO:0019904]; ubiquitin binding [GO:0043130]; ubiquitin-like protein ligase binding [GO:0044389]
|
PF01363;PF12210;PF00790;
|
1.20.5.1940;1.25.40.90;3.30.40.10;
| null |
PTM: Phosphorylated on Tyr-334. A minor site of phosphorylation on Tyr-329 is detected (By similarity). Phosphorylation occurs in response to EGF, IL-2, GM-CSF and HGF. {ECO:0000250|UniProtKB:Q99LI8}.; PTM: Ubiquitinated (PubMed:25588945). Ubiquitinated by ITCH (PubMed:14602072, PubMed:24790097). {ECO:0000269|PubMed:14602072, ECO:0000269|PubMed:24790097, ECO:0000269|PubMed:25588945}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9JJ50}. Early endosome membrane {ECO:0000269|PubMed:23166352, ECO:0000269|PubMed:24790097}; Peripheral membrane protein {ECO:0000305|PubMed:23166352, ECO:0000305|PubMed:24790097}; Cytoplasmic side {ECO:0000305|PubMed:23166352, ECO:0000305|PubMed:24790097}. Endosome, multivesicular body membrane {ECO:0000250|UniProtKB:Q9JJ50}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JJ50}. Note=Colocalizes with UBQLN1 in ubiquitin-rich cytoplasmic aggregates that are not endocytic compartments. {ECO:0000269|PubMed:16159959}.
| null | null | null | null | null |
FUNCTION: Involved in intracellular signal transduction mediated by cytokines and growth factors. When associated with STAM, it suppresses DNA signaling upon stimulation by IL-2 and GM-CSF. Could be a direct effector of PI3-kinase in vesicular pathway via early endosomes and may regulate trafficking to early and late endosomes by recruiting clathrin. May concentrate ubiquitinated receptors within clathrin-coated regions. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with STAM (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as a sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes. May contribute to the efficient recruitment of SMADs to the activin receptor complex. Involved in receptor recycling via its association with the CART complex, a multiprotein complex required for efficient transferrin receptor recycling but not for EGFR degradation.
|
Homo sapiens (Human)
|
O14965
|
AURKA_HUMAN
|
MDRSKENCISGPVKATAPVGGPKRVLVTQQFPCQNPLPVNSGQAQRVLCPSNSSQRIPLQAQKLVSSHKPVQNQKQKQLQATSVPHPVSRPLNNTQKSKQPLPSAPENNPEEELASKQKNEESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPWITANSSKPSNCQNKESASKQS
|
2.7.11.1
| null |
anterior/posterior axis specification [GO:0009948]; apoptotic process [GO:0006915]; cell division [GO:0051301]; centrosome localization [GO:0051642]; cilium disassembly [GO:0061523]; G2/M transition of mitotic cell cycle [GO:0000086]; liver regeneration [GO:0097421]; mitotic cell cycle [GO:0000278]; mitotic centrosome separation [GO:0007100]; mitotic spindle organization [GO:0007052]; negative regulation of apoptotic process [GO:0043066]; negative regulation of gene expression [GO:0010629]; negative regulation of protein binding [GO:0032091]; neuron projection extension [GO:1990138]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of mitochondrial fission [GO:0090141]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of mitotic nuclear division [GO:0045840]; positive regulation of oocyte maturation [GO:1900195]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein autophosphorylation [GO:0046777]; protein localization to centrosome [GO:0071539]; protein phosphorylation [GO:0006468]; regulation of centrosome cycle [GO:0046605]; regulation of cytokinesis [GO:0032465]; regulation of G2/M transition of mitotic cell cycle [GO:0010389]; regulation of protein stability [GO:0031647]; regulation of signal transduction by p53 class mediator [GO:1901796]; response to wounding [GO:0009611]; spindle assembly involved in female meiosis I [GO:0007057]; spindle organization [GO:0007051]
|
axon hillock [GO:0043203]; basolateral plasma membrane [GO:0016323]; centriole [GO:0005814]; centrosome [GO:0005813]; chromosome passenger complex [GO:0032133]; ciliary basal body [GO:0036064]; cytosol [GO:0005829]; germinal vesicle [GO:0042585]; glutamatergic synapse [GO:0098978]; kinetochore [GO:0000776]; meiotic spindle [GO:0072687]; microtubule cytoskeleton [GO:0015630]; midbody [GO:0030496]; mitotic spindle [GO:0072686]; mitotic spindle pole [GO:0097431]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; postsynaptic density [GO:0014069]; pronucleus [GO:0045120]; spindle [GO:0005819]; spindle microtubule [GO:0005876]; spindle midzone [GO:0051233]; spindle pole centrosome [GO:0031616]
|
ATP binding [GO:0005524]; histone H3S10 kinase activity [GO:0035175]; molecular function activator activity [GO:0140677]; protein heterodimerization activity [GO:0046982]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; ubiquitin protein ligase binding [GO:0031625]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, Aurora subfamily
|
PTM: Activated by phosphorylation at Thr-288; this brings about a change in the conformation of the activation segment. Phosphorylation at Thr-288 varies during the cell cycle and is highest during M phase. Autophosphorylated at Thr-288 upon TPX2 binding. Thr-288 can be phosphorylated by several kinases, including PAK and PKA. Protein phosphatase type 1 (PP1) binds AURKA and inhibits its activity by dephosphorylating Thr-288 during mitosis. Phosphorylation at Ser-342 decreases the kinase activity. PPP2CA controls degradation by dephosphorylating Ser-51 at the end of mitosis. {ECO:0000269|PubMed:11039908, ECO:0000269|PubMed:11551964, ECO:0000269|PubMed:12390251, ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:16246726, ECO:0000269|PubMed:17229885, ECO:0000269|PubMed:18662907, ECO:0000269|PubMed:19668197}.; PTM: Ubiquitinated by the E3 ubiquitin-protein ligase complex SCF(FBXL7) during mitosis, leading to its degradation by the proteasome (By similarity). Ubiquitinated by CHFR, leading to its degradation by the proteasome (By similarity). Ubiquitinated by the anaphase-promoting complex (APC), leading to its degradation by the proteasome (PubMed:10851084, PubMed:11039908). Ubiquitinated by the CUL3-KLHL18 ligase leading to its activation at the centrosome which is required for initiating mitotic entry (PubMed:23213400). Ubiquitination mediated by CUL3-KLHL18 ligase does not lead to its degradation by the proteasome (PubMed:23213400). {ECO:0000250|UniProtKB:P97477, ECO:0000269|PubMed:10851084, ECO:0000269|PubMed:11039908, ECO:0000269|PubMed:23213400}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:12576638, ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:17229885, ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:19357306, ECO:0000269|PubMed:21225229, ECO:0000269|PubMed:22014574, ECO:0000269|PubMed:23213400, ECO:0000269|PubMed:25657325, ECO:0000269|PubMed:30538148, ECO:0000269|PubMed:9153231}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:12576638, ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:19351716, ECO:0000269|PubMed:25657325, ECO:0000269|PubMed:26246606, ECO:0000269|PubMed:9153231, ECO:0000269|PubMed:9606188}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:P97477}. Cell projection, neuron projection {ECO:0000250|UniProtKB:P97477}. Cell projection, cilium {ECO:0000269|PubMed:17604723}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17604723}. Basolateral cell membrane {ECO:0000250|UniProtKB:F1PNY0}. Note=Detected at the neurite hillock in developing neurons (By similarity). Localizes at the centrosome in mitotic cells from early prophase until telophase, but also localizes to the spindle pole MTs from prophase to anaphase (PubMed:17229885, PubMed:21225229, PubMed:9606188). Colocalized with SIRT2 at centrosome (PubMed:22014574). Moves to the midbody during both telophase and cytokinesis (PubMed:17726514). Associates with both the pericentriolar material (PCM) and centrioles (PubMed:22014574). The localization to the spindle poles is regulated by AAAS (PubMed:26246606). {ECO:0000250|UniProtKB:P97477, ECO:0000269|PubMed:17229885, ECO:0000269|PubMed:17726514, ECO:0000269|PubMed:21225229, ECO:0000269|PubMed:22014574, ECO:0000269|PubMed:26246606, ECO:0000269|PubMed:9606188}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:12237287, ECO:0000269|PubMed:16337122, ECO:0000269|PubMed:19140666, ECO:0000269|PubMed:19402633, ECO:0000269|PubMed:27837025, ECO:0000269|PubMed:28218735}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:12237287, ECO:0000269|PubMed:16337122, ECO:0000269|PubMed:19140666, ECO:0000269|PubMed:19402633, ECO:0000269|PubMed:27837025, ECO:0000269|PubMed:28218735};
| null | null | null | null |
FUNCTION: Mitotic serine/threonine kinase that contributes to the regulation of cell cycle progression (PubMed:11039908, PubMed:12390251, PubMed:17125279, PubMed:17360485, PubMed:18615013, PubMed:26246606). Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis (PubMed:14523000, PubMed:26246606). Required for normal spindle positioning during mitosis and for the localization of NUMA1 and DCTN1 to the cell cortex during metaphase (PubMed:27335426). Required for initial activation of CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2 (PubMed:11551964, PubMed:14702041, PubMed:15128871, PubMed:15147269, PubMed:15987997, PubMed:17604723, PubMed:18056443, PubMed:18615013). Regulates KIF2A tubulin depolymerase activity (PubMed:19351716). Important for microtubule formation and/or stabilization (PubMed:18056443). Required for normal axon formation (PubMed:19812038). Plays a role in microtubule remodeling during neurite extension (PubMed:19668197). Also acts as a key regulatory component of the p53/TP53 pathway, and particularly the checkpoint-response pathways critical for oncogenic transformation of cells, by phosphorylating and destabilizing p53/TP53 (PubMed:14702041). Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity (PubMed:11551964). Inhibits cilia outgrowth (By similarity). Required for cilia disassembly via phosphorylation of HDAC6 and subsequent deacetylation of alpha-tubulin (PubMed:17604723, PubMed:20643351). Regulates protein levels of the anti-apoptosis protein BIRC5 by suppressing the expression of the SCF(FBXL7) E3 ubiquitin-protein ligase substrate adapter FBXL7 through the phosphorylation of the transcription factor FOXP1 (PubMed:28218735). {ECO:0000250|UniProtKB:A0A8I3S724, ECO:0000269|PubMed:11039908, ECO:0000269|PubMed:11551964, ECO:0000269|PubMed:12390251, ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:14523000, ECO:0000269|PubMed:14702041, ECO:0000269|PubMed:15128871, ECO:0000269|PubMed:15147269, ECO:0000269|PubMed:15987997, ECO:0000269|PubMed:17125279, ECO:0000269|PubMed:17360485, ECO:0000269|PubMed:17604723, ECO:0000269|PubMed:18056443, ECO:0000269|PubMed:18615013, ECO:0000269|PubMed:19351716, ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:19812038, ECO:0000269|PubMed:20643351, ECO:0000269|PubMed:26246606, ECO:0000269|PubMed:27335426, ECO:0000269|PubMed:28218735}.
|
Homo sapiens (Human)
|
O14966
|
RAB7L_HUMAN
|
MGSRDHLFKVLVVGDAAVGKTSLVQRYSQDSFSKHYKSTVGVDFALKVLQWSDYEIVRLQLWDIAGQERFTSMTRLYYRDASACVIMFDVTNATTFSNSQRWKQDLDSKLTLPNGEPVPCLLLANKCDLSPWAVSRDQIDRFSKENGFTGWTETSVKENKNINEAMRVLIEKMMRNSTEDIMSLSTQGDYINLQTKSSSWSCC
| null | null |
cell differentiation [GO:0030154]; cellular detoxification [GO:1990748]; endosome to lysosome transport [GO:0008333]; Golgi organization [GO:0007030]; intracellular protein transport [GO:0006886]; melanosome organization [GO:0032438]; mitochondrion organization [GO:0007005]; modulation by host of viral process [GO:0044788]; negative regulation of neuron projection development [GO:0010977]; phagosome-lysosome fusion [GO:0090385]; positive regulation of intracellular protein transport [GO:0090316]; positive regulation of receptor recycling [GO:0001921]; positive regulation of T cell receptor signaling pathway [GO:0050862]; protein localization to ciliary membrane [GO:1903441]; protein localization to membrane [GO:0072657]; regulation of retrograde transport, endosome to Golgi [GO:1905279]; response to bacterium [GO:0009617]; retrograde transport, endosome to Golgi [GO:0042147]; synapse assembly [GO:0007416]; T cell activation [GO:0042110]
|
cis-Golgi network [GO:0005801]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; early endosome [GO:0005769]; endomembrane system [GO:0012505]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; intracellular vesicle [GO:0097708]; late endosome [GO:0005770]; lysosome [GO:0005764]; melanosome [GO:0042470]; mitochondrion [GO:0005739]; perinuclear region of cytoplasm [GO:0048471]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; trans-Golgi network [GO:0005802]; vacuole [GO:0005773]
|
dynein complex binding [GO:0070840]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; kinesin binding [GO:0019894]; small GTPase binding [GO:0031267]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Rab family
|
PTM: In case of Salmonella enterica serovar Typhimurium (S.Typhimurium) infection, is proteolytically cleaved between Gly-41 and Val-42 by the GtgE viral protease encoded on the Gifsy-2 lysogen bacteriophage, which therefore prevents the recruitment of RAB29 to S.Typhimurium-containing vacuoles. In contrast, no proteolytically cleavage is detected in S.Typhi-infected cells (PubMed:22042847). {ECO:0000269|PubMed:22042847}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:24788816, ECO:0000269|PubMed:29212815}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:24788816}. Golgi apparatus {ECO:0000269|PubMed:22042847}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:24788816, ECO:0000269|PubMed:29212815}. Vacuole {ECO:0000269|PubMed:22042847}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22042847}. Note=Colocalizes with LRRK2 along tubular structures emerging from Golgi apparatus (PubMed:29212815). Colocalizes with GM130 at the Golgi apparatus (PubMed:22042847). Colocalizes with dynamic tubules emerging from and retracting to the Golgi apparatus (PubMed:22042847). Colocalizes with TGN46 at the trans-Golgi network (TGN) (PubMed:24788816). In Salmonella enterica serovar Typhi (S.Typhi) infected epithelial cells, is recruited and colocalized with both S.Typhi-containing vacuoles and dynamic tubules as well as those emerging from the vacuole toward the cell periphery (PubMed:22042847). {ECO:0000269|PubMed:22042847, ECO:0000269|PubMed:24788816, ECO:0000269|PubMed:29212815}.
| null | null | null | null | null |
FUNCTION: The small GTPases Rab are key regulators in vesicle trafficking (PubMed:24788816). Essential for maintaining the integrity of the endosome-trans-Golgi network structure (By similarity). Together with LRRK2, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner (PubMed:24788816). Recruits LRRK2 to the Golgi complex and stimulates LRRK2 kinase activity (PubMed:29212815). Regulates neuronal process morphology in the intact central nervous system (CNS) (By similarity). May play a role in the formation of typhoid toxin transport intermediates during Salmonella enterica serovar Typhi (S.Typhi) epithelial cell infection (PubMed:22042847). {ECO:0000250|UniProtKB:Q63481, ECO:0000269|PubMed:22042847, ECO:0000269|PubMed:24788816, ECO:0000269|PubMed:29212815}.
|
Homo sapiens (Human)
|
O14967
|
CLGN_HUMAN
|
MHFQAFWLCLGLLFISINAEFMDDDVETEDFEENSEEIDVNESELSSEIKYKTPQPIGEVYFAETFDSGRLAGWVLSKAKKDDMDEEISIYDGRWEIEELKENQVPGDRGLVLKSRAKHHAISAVLAKPFIFADKPLIVQYEVNFQDGIDCGGAYIKLLADTDDLILENFYDKTSYIIMFGPDKCGEDYKLHFIFRHKHPKTGVFEEKHAKPPDVDLKKFFTDRKTHLYTLVMNPDDTFEVLVDQTVVNKGSLLEDVVPPIKPPKEIEDPNDKKPEEWDERAKIPDPSAVKPEDWDESEPAQIEDSSVVKPAGWLDDEPKFIPDPNAEKPDDWNEDTDGEWEAPQILNPACRIGCGEWKPPMIDNPKYKGVWRPPLVDNPNYQGIWSPRKIPNPDYFEDDHPFLLTSFSALGLELWSMTSDIYFDNFIICSEKEVADHWAADGWRWKIMIANANKPGVLKQLMAAAEGHPWLWLIYLVTAGVPIALITSFCWPRKVKKKHKDTEYKKTDICIPQTKGVLEQEEKEEKAALEKPMDLEEEKKQNDGEMLEKEEESEPEEKSEEEIEIIEGQEESNQSNKSGSEDEMKEADESTGSGDGPIKSVRKRRVRKD
| null | null |
binding of sperm to zona pellucida [GO:0007339]; ERAD pathway [GO:0036503]; protein folding [GO:0006457]; protein-containing complex assembly [GO:0065003]; single fertilization [GO:0007338]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]
|
calcium ion binding [GO:0005509]; protein folding chaperone [GO:0044183]; unfolded protein binding [GO:0051082]
|
PF00262;
|
2.60.120.200;2.10.250.10;
|
Calreticulin family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Functions during spermatogenesis as a chaperone for a range of client proteins that are important for sperm adhesion onto the egg zona pellucida and for subsequent penetration of the zona pellucida. Required for normal sperm migration from the uterus into the oviduct. Required for normal male fertility. Binds calcium ions (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O14972
|
VP26C_HUMAN
|
MGTALDIKIKRANKVYHAGEVLSGVVVISSKDSVQHQGVSLTMEGTVNLQLSAKSVGVFEAFYNSVKPIQIINSTIEMVKPGKFPSGKTEIPFEFPLHLKGNKVLYETYHGVFVNIQYTLRCDMKRSLLAKDLTKTCEFIVHSAPQKGKFTPSPVDFTITPETLQNVKERALLPKFLLRGHLNSTNCVITQPLTGELVVESSEAAIRSVELQLVRVETCGCAEGYARDATEIQNIQIADGDVCRGLSVPIYMVFPRLFTCPTLETTNFKVEFEVNIVVLLHPDHLITENFPLKLCRI
| null | null |
endocytic recycling [GO:0032456]; intracellular protein transport [GO:0006886]
|
endosome [GO:0005768]; nucleus [GO:0005634]
| null |
PF03643;
|
2.60.40.640;
|
VPS26 family
| null |
SUBCELLULAR LOCATION: Endosome {ECO:0000305|PubMed:28892079}.
| null | null | null | null | null |
FUNCTION: Acts as a component of the retriever complex. The retriever complex is a heterotrimeric complex related to retromer cargo-selective complex (CSC) and essential for retromer-independent retrieval and recycling of numerous cargos such as integrin alpha-5/beta-1 (ITGA5:ITGB1) (PubMed:28892079). The recruitment of the retriever complex to the endosomal membrane involves CCC and WASH complexes (PubMed:28892079). In the endosomes, drives the retriever and recycling of NxxY-motif-containing cargo proteins by coupling to SNX17, a cargo essential for the homeostatic maintenance of numerous cell surface proteins associated with processes that include cell migration, cell adhesion, nutrient supply and cell signaling (PubMed:28892079). {ECO:0000269|PubMed:28892079}.; FUNCTION: (Microbial infection) The heterotrimeric retriever complex, in collaboration with the CCC complex, mediates the exit of human papillomavirus to the cell surface. {ECO:0000269|PubMed:28892079}.
|
Homo sapiens (Human)
|
O14974
|
MYPT1_HUMAN
|
MKMADAKQKRNEQLKRWIGSETDLEPPVVKRQKTKVKFDDGAVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIEAARKEEERIMLRDARQWLNSGHINDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVADEDILGYLEELQKKQNLLHSEKRDKKSPLIESTANMDNNQSQKTFKNKETLIIEPEKNASRIESLEQEKVDEEEEGKKDESSCSSEEDEEDDSESEAETDKTKPLASVTNANTSSTQAAPVAVTTPTVSSGQATPTSPIKKFPTTATKISPKEEERKDESPATWRLGLRKTGSYGALAEITASKEGQKEKDTAGVTRSASSPRLSSSLDNKEKEKDSKGTRLAYVAPTIPRRLASTSDIEEKENRDSSSLRTSSSYTRRKWEDDLKKNSSVNEGSTYHKSCSFGRRQDDLISSSVPSTTSTPTVTSAAGLQKSLLSSTSTTTKITTGSSSAGTQSSTSNRLWAEDSTEKEKDSVPTAVTIPVAPTVVNAAASTTTLTTTTAGTVSSTTEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRSRSTRTREQENEEKEKEEKEKQDKEKQEEKKESETSREDEYKQKYSRTYDETYQRYRPVSTSSSTTPSSSLSTMSSSLYASSQLNRPNSLVGITSAYSRGITKENEREGEKREEEKEGEDKSQPKSIRERRRPREKRRSTGVSFWTQDSDENEQEQQSDTEEGSNKKETQTDSISRYETSSTSAGDRYDSLLGRSGSYSYLEERKPYSSRLEKDDSTDFKKLYEQILAENEKLKAQLHDTNMELTDLKLQLEKATQRQERFADRSLLEMEKRERRALERRISEMEEELKMLPDLKADNQRLKDENGALIRVISKLSK
| null | null |
cellular response to xenobiotic stimulus [GO:0071466]; centrosome cycle [GO:0007098]; mitotic cell cycle [GO:0000278]; negative regulation of catalytic activity [GO:0043086]; positive regulation of myosin-light-chain-phosphatase activity [GO:0035508]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein dephosphorylation [GO:0006470]; regulation of cell adhesion [GO:0030155]; regulation of myosin-light-chain-phosphatase activity [GO:0035507]; regulation of nucleocytoplasmic transport [GO:0046822]; signal transduction [GO:0007165]
|
A band [GO:0031672]; actin cytoskeleton [GO:0015629]; centrosome [GO:0005813]; contractile fiber [GO:0043292]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; kinetochore [GO:0000776]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; PTW/PP1 phosphatase complex [GO:0072357]; stress fiber [GO:0001725]; Z disc [GO:0030018]
|
14-3-3 protein binding [GO:0071889]; enzyme inhibitor activity [GO:0004857]; phosphatase regulator activity [GO:0019208]; protein kinase binding [GO:0019901]
|
PF12796;PF15898;
|
6.10.140.390;6.10.250.1820;1.25.40.20;
| null |
PTM: Phosphorylated by CIT (Rho-associated kinase) (By similarity). Phosphorylated cooperatively by ROCK1 and CDC42BP on Thr-696. Phosphorylated on upon DNA damage, probably by ATM or ATR. In vitro, phosphorylation of Ser-695 by PKA and PKG appears to prevent phosphorylation of the inhibitory site Thr-696, probably mediated by PRKG1. Phosphorylation at Ser-445, Ser-472 and Ser-910 by NUAK1 promotes interaction with 14-3-3, leading to inhibit interaction with myosin light chain MLC2, preventing dephosphorylation of MLC2. May be phosphorylated at Thr-696 by DMPK; may inhibit the myosin phosphatase activity. Phosphorylated at Ser-473 by CDK1 during mitosis, creating docking sites for the POLO box domains of PLK1. Subsequently, PLK1 binds and phosphorylates PPP1R12A. {ECO:0000250, ECO:0000269|PubMed:10567269, ECO:0000269|PubMed:11283607, ECO:0000269|PubMed:11287000, ECO:0000269|PubMed:11331307, ECO:0000269|PubMed:11719507, ECO:0000269|PubMed:12773565, ECO:0000269|PubMed:15194681, ECO:0000269|PubMed:15723050, ECO:0000269|PubMed:17126281, ECO:0000269|PubMed:18477460, ECO:0000269|PubMed:19131646, ECO:0000269|PubMed:19701943, ECO:0000269|PubMed:19997641, ECO:0000269|PubMed:20354225, ECO:0000269|PubMed:21457715}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12923170, ECO:0000269|PubMed:18477460}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:12923170}. Note=Also along actomyosin filaments. {ECO:0000269|PubMed:12923170}.
| null | null | null | null | null |
FUNCTION: Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent suppression of HIF1A activity. {ECO:0000269|PubMed:18477460, ECO:0000269|PubMed:19245366, ECO:0000269|PubMed:20354225}.
|
Homo sapiens (Human)
|
O14975
|
S27A2_HUMAN
|
MLSAIYTVLAGLLFLPLLVNLCCPYFFQDIGYFLKVAAVGRRVRSYGKRRPARTILRAFLEKARQTPHKPFLLFRDETLTYAQVDRRSNQVARALHDHLGLRQGDCVALLMGNEPAYVWLWLGLVKLGCAMACLNYNIRAKSLLHCFQCCGAKVLLVSPELQAAVEEILPSLKKDDVSIYYVSRTSNTDGIDSFLDKVDEVSTEPIPESWRSEVTFSTPALYIYTSGTTGLPKAAMITHQRIWYGTGLTFVSGLKADDVIYITLPFYHSAALLIGIHGCIVAGATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGDICIYEFYAATEGNIGFMNYARKVGAVGRVNYLQKKIITYDLIKYDVEKDEPVRDENGYCVRVPKGEVGLLVCKITQLTPFNGYAGAKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHEGRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVEEGFNPAVIKDALYFLDDTAKMYVPMTEDIYNAISAKTLKL
|
6.2.1.-; 6.2.1.15; 6.2.1.24; 6.2.1.3; 6.2.1.7
| null |
bile acid biosynthetic process [GO:0006699]; bile acid metabolic process [GO:0008206]; fatty acid alpha-oxidation [GO:0001561]; fatty acid beta-oxidation [GO:0006635]; fatty-acyl-CoA biosynthetic process [GO:0046949]; long-chain fatty acid import into cell [GO:0044539]; long-chain fatty acid metabolic process [GO:0001676]; methyl-branched fatty acid metabolic process [GO:0097089]; very long-chain fatty acid catabolic process [GO:0042760]
|
cytosol [GO:0005829]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; peroxisomal membrane [GO:0005778]; plasma membrane [GO:0005886]; specific granule membrane [GO:0035579]
|
arachidonate-CoA ligase activity [GO:0047676]; ATP binding [GO:0005524]; cholate-CoA ligase activity [GO:0047747]; enzyme binding [GO:0019899]; fatty acid transmembrane transporter activity [GO:0015245]; long-chain fatty acid transporter activity [GO:0005324]; long-chain fatty acid-CoA ligase activity [GO:0004467]; oleate transmembrane transporter activity [GO:1901480]; phytanate-CoA ligase activity [GO:0050197]; pristanate-CoA ligase activity [GO:0070251]; very long-chain fatty acid-CoA ligase activity [GO:0031957]
|
PF00501;PF13193;
|
3.30.300.30;3.40.50.12780;
|
ATP-dependent AMP-binding enzyme family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11980911, ECO:0000269|PubMed:22022213, ECO:0000269|PubMed:24269233}; Multi-pass membrane protein {ECO:0000255}. Peroxisome membrane {ECO:0000269|PubMed:10198260, ECO:0000269|PubMed:10640429}; Peripheral membrane protein {ECO:0000269|PubMed:10640429}. Cell membrane {ECO:0000269|PubMed:20530735}; Multi-pass membrane protein {ECO:0000255}. Microsome {ECO:0000269|PubMed:10640429}.
|
CATALYTIC ACTIVITY: [Isoform 1]: Reaction=a fatty acid(in) = a fatty acid(out); Xref=Rhea:RHEA:38879, ChEBI:CHEBI:28868; Evidence={ECO:0000269|PubMed:20530735, ECO:0000269|PubMed:21768100, ECO:0000269|PubMed:22022213}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38881; Evidence={ECO:0000305|PubMed:20530735, ECO:0000305|PubMed:21768100}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=(9Z)-octadecenoate(out) = (9Z)-octadecenoate(in); Xref=Rhea:RHEA:33655, ChEBI:CHEBI:30823; Evidence={ECO:0000269|PubMed:22022213}; CATALYTIC ACTIVITY: [Isoform 2]: Reaction=a fatty acid(in) = a fatty acid(out); Xref=Rhea:RHEA:38879, ChEBI:CHEBI:28868; Evidence={ECO:0000269|PubMed:21768100}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38881; Evidence={ECO:0000305|PubMed:21768100}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560, ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3; Evidence={ECO:0000269|PubMed:10198260, ECO:0000269|PubMed:10749848, ECO:0000269|PubMed:11980911, ECO:0000269|PubMed:22022213, ECO:0000305|PubMed:20530735}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422; Evidence={ECO:0000305|PubMed:10198260, ECO:0000305|PubMed:10749848, ECO:0000305|PubMed:11980911, ECO:0000305|PubMed:20530735, ECO:0000305|PubMed:22022213}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:19713, ChEBI:CHEBI:30616, ChEBI:CHEBI:32395, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:456215; EC=6.2.1.15; Evidence={ECO:0000250|UniProtKB:O35488}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714; Evidence={ECO:0000250|UniProtKB:O35488}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:10198260, ECO:0000269|PubMed:10749848, ECO:0000269|PubMed:11980911, ECO:0000305|PubMed:20530735}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752; Evidence={ECO:0000305|PubMed:10198260, ECO:0000305|PubMed:10749848, ECO:0000305|PubMed:11980911, ECO:0000305|PubMed:20530735}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=(9Z)-octadecenoate + ATP + CoA = (9Z)-octadecenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:33607, ChEBI:CHEBI:30616, ChEBI:CHEBI:30823, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:22022213}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608; Evidence={ECO:0000305|PubMed:22022213}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=3,7,11,15-tetramethylhexadecanoate + ATP + CoA = AMP + diphosphate + phytanoyl-CoA; Xref=Rhea:RHEA:21380, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37257, ChEBI:CHEBI:57287, ChEBI:CHEBI:57391, ChEBI:CHEBI:456215; EC=6.2.1.24; Evidence={ECO:0000269|PubMed:10198260}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21381; Evidence={ECO:0000305|PubMed:10198260}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=(9Z,12Z,15Z)-octadecatrienoate + ATP + CoA = (9Z,12Z,15Z)-octadecatrienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:44936, ChEBI:CHEBI:30616, ChEBI:CHEBI:32387, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:74034, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:21768100}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44937; Evidence={ECO:0000305|PubMed:21768100}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=2,6,10,14-tetramethylpentadecanoate + ATP + CoA = AMP + diphosphate + pristanoyl-CoA; Xref=Rhea:RHEA:47264, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:77250, ChEBI:CHEBI:77268, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:10198260}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47265; Evidence={ECO:0000305|PubMed:10198260}; CATALYTIC ACTIVITY: Reaction=(E)-hexadec-2-enoate + ATP + CoA = (2E)-hexadecenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:36139, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61526, ChEBI:CHEBI:72745, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:24269233}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36140; Evidence={ECO:0000305|PubMed:24269233}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=a very long-chain fatty acid + ATP + CoA = a very long-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:54536, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:58950, ChEBI:CHEBI:138261, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:10198260, ECO:0000269|PubMed:10749848, ECO:0000269|PubMed:11980911, ECO:0000269|PubMed:21768100, ECO:0000305|PubMed:20530735}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54537; Evidence={ECO:0000305|PubMed:10198260, ECO:0000305|PubMed:10749848, ECO:0000305|PubMed:11980911, ECO:0000305|PubMed:20530735}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=ATP + CoA + tetracosanoate = AMP + diphosphate + tetracosanoyl-CoA; Xref=Rhea:RHEA:33639, ChEBI:CHEBI:30616, ChEBI:CHEBI:31014, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:65052, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:10198260, ECO:0000269|PubMed:10749848, ECO:0000269|PubMed:21768100, ECO:0000305|PubMed:20530735}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640; Evidence={ECO:0000305|PubMed:10198260, ECO:0000305|PubMed:10749848, ECO:0000305|PubMed:20530735, ECO:0000305|PubMed:21768100}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + ATP + CoA = (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:44932, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:74298, ChEBI:CHEBI:77016, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:21768100}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44933; Evidence={ECO:0000305|PubMed:21768100}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate + ATP + CoA = (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:22976, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:58677, ChEBI:CHEBI:58734, ChEBI:CHEBI:456215; EC=6.2.1.7; Evidence={ECO:0000269|PubMed:11980911}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22977; Evidence={ECO:0000305|PubMed:11980911};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12 uM for hexadecanoate (palmitate) {ECO:0000269|PubMed:11980911}; Vmax=1.4 nmol/min/mg enzyme for hexadecanoyl-CoA (palmitoyl-CoA) synthesis {ECO:0000269|PubMed:11980911};
| null | null | null |
FUNCTION: Mediates the import of long-chain fatty acids (LCFA) into the cell by facilitating their transport across cell membranes, playing an important role in hepatic fatty acid uptake (PubMed:10198260, PubMed:10749848, PubMed:11980911, PubMed:20530735, PubMed:22022213, PubMed:24269233). Also functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates, which prevents fatty acid efflux from cells and might drive more fatty acid uptake (PubMed:10198260, PubMed:10749848, PubMed:11980911, PubMed:20530735, PubMed:22022213, PubMed:24269233). Plays a pivotal role in regulating available LCFA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation or triglyceride synthesis (PubMed:20530735). Can also activate branched-chain fatty acids such as phytanic acid and pristanic acid (PubMed:10198260). May contribute to the synthesis of sphingosine-1-phosphate (PubMed:24269233). Does not activate C24 bile acids, cholate and chenodeoxycholate (PubMed:11980911). In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol (PubMed:11980911). However, it is not critical for THCA activation and bile synthesis in vivo (PubMed:20530735). {ECO:0000269|PubMed:10198260, ECO:0000269|PubMed:10749848, ECO:0000269|PubMed:11980911, ECO:0000269|PubMed:20530735, ECO:0000269|PubMed:22022213, ECO:0000269|PubMed:24269233}.; FUNCTION: [Isoform 1]: Exhibits both long-chain fatty acids (LCFA) transport activity and acyl CoA synthetase towards very long-chain fatty acids (PubMed:10198260, PubMed:21768100). Shows a preference for generating CoA derivatives of n-3 fatty acids, which are preferentially trafficked into phosphatidylinositol (PubMed:21768100). {ECO:0000269|PubMed:10198260, ECO:0000269|PubMed:21768100}.; FUNCTION: [Isoform 2]: Exhibits long-chain fatty acids (LCFA) transport activity but lacks acyl CoA synthetase towards very long-chain fatty acids. {ECO:0000269|PubMed:21768100}.
|
Homo sapiens (Human)
|
O14976
|
GAK_HUMAN
|
MSLLQSALDFLAGPGSLGGASGRDQSDFVGQTVELGELRLRVRRVLAEGGFAFVYEAQDVGSGREYALKRLLSNEEEKNRAIIQEVCFMKKLSGHPNIVQFCSAASIGKEESDTGQAEFLLLTELCKGQLVEFLKKMESRGPLSCDTVLKIFYQTCRAVQHMHRQKPPIIHRDLKVENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQRRALVEEEITRNTTPMYRTPEIIDLYSNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKYSIPPHDTQYTVFHSLIRAMLQVNPEERLSIAEVVHQLQEIAAARNVNPKSPITELLEQNGGYGSATLSRGPPPPVGPAGSGYSGGLALAEYDQPYGGFLDILRGGTERLFTNLKDTSSKVIQSVANYAKGDLDISYITSRIAVMSFPAEGVESALKNNIEDVRLFLDSKHPGHYAVYNLSPRTYRPSRFHNRVSECGWAARRAPHLHTLYNICRNMHAWLRQDHKNVCVVHCMDGRAASAVAVCSFLCFCRLFSTAEAAVYMFSMKRCPPGIWPSHKRYIEYMCDMVAEEPITPHSKPILVRAVVMTPVPLFSKQRSGCRPFCEVYVGDERVASTSQEYDKMRDFKIEDGKAVIPLGVTVQGDVLIVIYHARSTLGGRLQAKMASMKMFQIQFHTGFVPRNATTVKFAKYDLDACDIQEKYPDLFQVNLEVEVEPRDRPSREAPPWENSSMRGLNPKILFSSREEQQDILSKFGKPELPRQPGSTAQYDAGAGSPEAEPTDSDSPPSSSADASRFLHTLDWQEEKEAETGAENASSKESESALMEDRDESEVSDEGGSPISSEGQEPRADPEPPGLAAGLVQQDLVFEVETPAVLPEPVPQEDGVDLLGLHSEVGAGPAVPPQACKAPSSNTDLLSCLLGPPEAASQGPPEDLLSEDPLLLASPAPPLSVQSTPRGGPPAAADPFGPLLPSSGNNSQPCSNPDLFGEFLNSDSVTVPPSFPSAHSAPPPSCSADFLHLGDLPGEPSKMTASSSNPDLLGGWAAWTETAASAVAPTPATEGPLFSPGGQPAPCGSQASWTKSQNPDPFADLGDLSSGLQGSPAGFPPGGFIPKTATTPKGSSSWQTSRPPAQGASWPPQAKPPPKACTQPRPNYASNFSVIGAREERGVRAPSFAQKPKVSENDFEDLLSNQGFSSRSDKKGPKTIAEMRKQDLAKDTDPLKLKLLDWIEGKERNIRALLSTLHTVLWDGESRWTPVGMADLVAPEQVKKHYRRAVLAVHPDKAAGQPYEQHAKMIFMELNDAWSEFENQGSRPLF
|
2.7.11.1
| null |
cell cycle [GO:0007049]; chaperone cofactor-dependent protein refolding [GO:0051085]; clathrin coat assembly [GO:0048268]; clathrin coat disassembly [GO:0072318]; clathrin-dependent endocytosis [GO:0072583]; endoplasmic reticulum organization [GO:0007029]; Golgi organization [GO:0007030]; Golgi to lysosome transport [GO:0090160]; intracellular transport [GO:0046907]; negative regulation of neuron projection development [GO:0010977]; phosphorylation [GO:0016310]; protein localization to Golgi apparatus [GO:0034067]; protein localization to plasma membrane [GO:0072659]; receptor-mediated endocytosis [GO:0006898]; regulation of clathrin coat assembly [GO:1905443]; synaptic vesicle uncoating [GO:0016191]
|
clathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; presynapse [GO:0098793]; vesicle [GO:0031982]
|
ATP binding [GO:0005524]; clathrin binding [GO:0030276]; cyclin binding [GO:0030332]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein-folding chaperone binding [GO:0051087]
|
PF00069;PF10409;
|
2.60.40.1110;1.10.287.110;3.90.190.10;1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10625686}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:10625686}. Cell junction, focal adhesion {ECO:0000305|PubMed:10625686}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:31962345}. Note=Localizes to the perinuclear area and to the trans-Golgi network. Also seen on the plasma membrane, probably at focal adhesions. Recruitment to clathrin-coated vesicles depends on temporal variations in phosphoinositide composition of clathrin-coated vesicles (PubMed:31962345). {ECO:0000269|PubMed:31962345}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Associates with cyclin G and CDK5. Seems to act as an auxilin homolog that is involved in the uncoating of clathrin-coated vesicles by Hsc70 in non-neuronal cells. Expression oscillates slightly during the cell cycle, peaking at G1 (PubMed:10625686). May play a role in clathrin-mediated endocytosis and intracellular trafficking, and in the dynamics of clathrin assembly/disassembly (PubMed:18489706). {ECO:0000269|PubMed:10625686, ECO:0000269|PubMed:18489706}.
|
Homo sapiens (Human)
|
O14977
|
AZIN1_HUMAN
|
MKGFIDDANYSVGLLDEGTNLGNVIDNYVYEHTLTGKNAFFVGDLGKIVKKHSQWQNVVAQIKPFYTVKCNSAPAVLEILAALGTGFACSSKNEMALVQELGVPPENIIYISPCKQVSQIKYAAKVGVNILTCDNEIELKKIARNHPNAKVLLHIATEDNIGGEEGNMKFGTTLKNCRHLLECAKELDVQIIGVKFHVSSACKESQVYVHALSDARCVFDMAGEIGFTMNMLDIGGGFTGTEFQLEEVNHVISPLLDIYFPEGSGVKIISEPGSYYVSSAFTLAVNIIAKKVVENDKFPSGVEKTGSDEPAFMYYMNDGVYGSFASKLSEDLNTIPEVHKKYKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSFHEPSAFNDFQRPAIYYMMSFSDWYEMQDAGITSDSMMKNFFFVPSCIQLSQEDSFSAEA
| null | null |
negative regulation of protein catabolic process [GO:0042177]; positive regulation of polyamine transmembrane transport [GO:1902269]; putrescine biosynthetic process from ornithine [GO:0033387]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
ornithine decarboxylase activator activity [GO:0042978]; ornithine decarboxylase activity [GO:0004586]
|
PF02784;PF00278;
|
3.20.20.10;
|
Orn/Lys/Arg decarboxylase class-II family, ODC antizyme inhibitor subfamily
|
PTM: Ubiquitinated, leading to its proteasomal degradation; a process that is reduced in presence of antizyme OAZ1. {ECO:0000269|PubMed:17900240}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O35484}.
| null | null | null | null | null |
FUNCTION: Antizyme inhibitor (AZI) protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake. AZI is an enzymatically inactive ODC homolog that counteracts the negative effect of ODC antizymes (AZs) OAZ1, OAZ2 and OAZ3 on ODC activity by competing with ODC for antizyme-binding (PubMed:17900240, PubMed:26305948). Inhibits antizyme-dependent ODC degradation and releases ODC monomers from their inactive complex with antizymes, leading to formation of the catalytically active ODC homodimer and restoring polyamine production (PubMed:17900240). {ECO:0000269|PubMed:17900240, ECO:0000269|PubMed:26305948}.
|
Homo sapiens (Human)
|
O14978
|
ZN263_HUMAN
|
MASGPGSQEREGLLIVKLEEDCAWSQELPPPDPGPSPEASHLRFRRFRFQEAAGPREALSRLQELCHGWLRPEMRTKEQILELLVLEQFLTILPQEIQSRVQELHPESGEEAVTLVEDMQRELGRLRQQVTNHGRGTEVLLEEPLPLETARESPSFKLEPMETERSPGPRLQELLGPSPQRDPQAVKERALSAPWLSLFPPEGNMEDKEMTGPQLPESLEDVAMYISQEEWGHQDPSKRALSRDTVQESYENVDSLESHIPSQEVPGTQVGQGGKLWDPSVQSCKEGLSPRGPAPGEEKFENLEGVPSVCSENIHPQVLLPDQARGEVPWSPELGRPHDRSQGDWAPPPEGGMEQALAGASSGRELGRPKELQPKKLHLCPLCGKNFSNNSNLIRHQRIHAAERLCMGVDCTEIFGGNPRFLSLHRAHLGEEAHKCLECGKCFSQNTHLTRHQRTHTGEKPYQCNICGKCFSCNSNLHRHQRTHTGEKPYKCPECGEIFAHSSNLLRHQRIHTGERPYKCPECGKSFSRSSHLVIHERTHERERLYPFSECGEAVSDSTPFLTNHGAHKAEKKLFECLTCGKSFRQGMHLTRHQRTHTGEKPYKCTLCGENFSHRSNLIRHQRIHTGEKPYTCHECGDSFSHSSNRIRHLRTHTGERPYKCSECGESFSRSSRLMSHQRTHTG
| null | null |
negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]; transcription cis-regulatory region binding [GO:0000976]
|
PF01352;PF02023;PF00096;
|
6.10.140.140;3.30.160.60;1.10.4020.10;
|
Krueppel C2H2-type zinc-finger protein family
|
PTM: Ubiquitinated, leading to proteasomal degradation. {ECO:0000269|PubMed:32051553}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32051553}.
| null | null | null | null | null |
FUNCTION: Transcription factor that binds to the consensus sequence 5'-TCCTCCC-3' and acts as a transcriptional repressor (PubMed:32051553). Binds to the promoter region of SIX3 and recruits other proteins involved in chromatin modification and transcriptional corepression, resulting in methylation of the promoter and transcriptional repression (PubMed:32051553). Acts as a transcriptional repressor of HS3ST1 and HS3ST3A1 via binding to gene promoter regions (PubMed:32277030). {ECO:0000269|PubMed:32051553, ECO:0000269|PubMed:32277030}.
|
Homo sapiens (Human)
|
O14979
|
HNRDL_HUMAN
|
MEVPPRLSHVPPPLFPSAPATLASRSLSHWRPRPPRQLAPLLPSLAPSSARQGARRAQRHVTAQQPSRLAGGAAIKGGRRRRPDLFRRHFKSSSIQRSAAAAAATRTARQHPPADSSVTMEDMNEYSNIEEFAEGSKINASKNQQDDGKMFIGGLSWDTSKKDLTEYLSRFGEVVDCTIKTDPVTGRSRGFGFVLFKDAASVDKVLELKEHKLDGKLIDPKRAKALKGKEPPKKVFVGGLSPDTSEEQIKEYFGAFGEIENIELPMDTKTNERRGFCFITYTDEEPVKKLLESRYHQIGSGKCEIKVAQPKEVYRQQQQQQKGGRGAAAGGRGGTRGRGRGQGQNWNQGFNNYYDQGYGNYNSAYGGDQNYSGYGGYDYTGYNYGNYGYGQGYADYSGQQSTYGKASRGGGNHQNNYQPY
| null | null |
regulation of gene expression [GO:0010468]; RNA processing [GO:0006396]
|
cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]
|
DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; poly(A) binding [GO:0008143]; poly(G) binding [GO:0034046]; RNA binding [GO:0003723]; single-stranded DNA binding [GO:0003697]
|
PF00076;
|
3.30.70.330;
| null |
PTM: Dimethylation of Arg-408 is probably of the asymmetric type.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11705999, ECO:0000269|PubMed:12406575}. Cytoplasm {ECO:0000269|PubMed:11705999, ECO:0000269|PubMed:12406575}. Note=Shuttles between the nucleus and the cytoplasm in a TNPO1-dependent manner. {ECO:0000269|PubMed:11705999, ECO:0000269|PubMed:12406575}.
| null | null | null | null | null |
FUNCTION: Acts as a transcriptional regulator. Promotes transcription repression. Promotes transcription activation in differentiated myotubes (By similarity). Binds to double- and single-stranded DNA sequences. Binds to the transcription suppressor CATR sequence of the COX5B promoter (By similarity). Binds with high affinity to RNA molecules that contain AU-rich elements (AREs) found within the 3'-UTR of many proto-oncogenes and cytokine mRNAs. Binds both to nuclear and cytoplasmic poly(A) mRNAs. Binds to poly(G) and poly(A), but not to poly(U) or poly(C) RNA homopolymers. Binds to the 5'-ACUAGC-3' RNA consensus sequence. {ECO:0000250, ECO:0000269|PubMed:9538234}.
|
Homo sapiens (Human)
|
O14980
|
XPO1_HUMAN
|
MPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLKEHPDAWTRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDPTCVEKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLLSEEVFDFSSGQITQVKSKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPLGYIFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFVTLFTLTMMQLKQMLPLNTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHDQLIEKRLNLRETLMEALHYMLLVSEVEETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDVPPRRQLYLPMLFKVRLLMVSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTERIMTEKLHNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKAIIASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRHFVQVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLIEKYMLLPNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIYLDMLNVYKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAENFVPPLLDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDFEEYPEHRTNFFLLLQAVNSHCFPAFLAIPPTQFKLVLDSIIWAFKHTMRNVADTGLQILFTLLQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKISTSLNPGNPVNNQIFLQEYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEHLRDFLVQIKEFAGEDTSDLFLEEREIALRQADEEKHKRQMSVPGIFNPHEIPEEMCD
| null | null |
mRNA export from nucleus [GO:0006406]; nucleocytoplasmic transport [GO:0006913]; protein export from nucleus [GO:0006611]; protein localization to nucleus [GO:0034504]; regulation of centrosome duplication [GO:0010824]; regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032434]; regulation of protein export from nucleus [GO:0046825]; ribosomal large subunit export from nucleus [GO:0000055]; ribosomal small subunit export from nucleus [GO:0000056]; ribosomal subunit export from nucleus [GO:0000054]; ribosome biogenesis [GO:0042254]
|
annulate lamellae [GO:0005642]; Cajal body [GO:0015030]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; kinetochore [GO:0000776]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; ribonucleoprotein complex [GO:1990904]
|
nuclear export signal receptor activity [GO:0005049]; RNA binding [GO:0003723]; small GTPase binding [GO:0031267]
|
PF08767;PF18777;PF18784;PF18787;PF03810;PF08389;
|
1.25.10.10;
|
Exportin family
| null |
SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleoplasm. Nucleus, Cajal body. Nucleus, nucleolus. Note=Located in the nucleoplasm, Cajal bodies and nucleoli. Shuttles between the nucleus/nucleolus and the cytoplasm.
| null | null | null | null | null |
FUNCTION: Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus, in association with RANBP3, binds cooperatively to the NES on its target protein and to the GTPase RAN in its active GTP-bound form (Ran-GTP). Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap. {ECO:0000269|PubMed:15574332, ECO:0000269|PubMed:20921223, ECO:0000269|PubMed:9311922, ECO:0000269|PubMed:9323133}.; FUNCTION: (Microbial infection) Mediates the export of unspliced or incompletely spliced RNAs out of the nucleus from different viruses including HIV-1, HTLV-1 and influenza A. Interacts with, and mediates the nuclear export of HIV-1 Rev and HTLV-1 Rex proteins. Involved in HTLV-1 Rex multimerization. {ECO:0000269|PubMed:14612415, ECO:0000269|PubMed:9837918}.
|
Homo sapiens (Human)
|
O14981
|
BTAF1_HUMAN
|
MAVSRLDRLFILLDTGTTPVTRKAAAQQLGEVVKLHPHELNNLLSKVLIYLRSANWDTRIAAGQAVEAIVKNVPEWNPVPRTRQEPTSESSMEDSPTTERLNFDRFDICRLLQHGASLLGSAGAEFEVQDEKSGEVDPKERIARQRKLLQKKLGLNMGEAIGMSTEELFNDEDLDYTPTSASFVNKQPTLQAAELIDSEFRAGMSNRQKNKAKRMAKLFAKQRSRDAVETNEKSNDSTDGEPEEKRRKIANVVINQSANDSKVLIDNIPDSSSLIEETNEWPLESFCEELCNDLFNPSWEVRHGAGTGLREILKAHGKSGGKMGDSTLEEMIQQHQEWLEDLVIRLLCVFALDRFGDFVSDEVVAPVRETCAQTLGVVLKHMNETGVHKTVDVLLKLLTQEQWEVRHGGLLGIKYALAVRQDVINTLLPKVLTRIIEGLQDLDDDVRAVAAASLVPVVESLVYLQTQKVPFIINTLWDALLELDDLTASTNSIMTLLSSLLTYPQVQQCSIQQSLTVLVPRVWPFLHHTISSVRRAALETLFTLLSTQDQNSSSWLIPILPDMLRHIFQFCVLESSQEILDLIHKVWMELLSKASVQYVVAAACPWMGAWLCLMMQPSHLPIDLNMLLEVKARAKEKTGGKVRQGQSQNKEVLQEYIAGADTIMEDPATRDFVVMRARMMAAKLLGALCCCICDPGVNVVTQEIKPAESLGQLLLFHLNSKSALQRISVALVICEWAALQKECKAVTLAVQPRLLDILSEHLYYDEIAVPFTRMQNECKQLISSLADVHIEVGNRVNNNVLTIDQASDLVTTVFNEATSSFDLNPQVLQQLDSKRQQVQMTVTETNQEWQVLQLRVHTFAACAVVSLQQLPEKLNPIIKPLMETIKKEENTLVQNYAAQCIAKLLQQCTTRTPCPNSKIIKNLCSSLCVDPYLTPCVTCPVPTQSGQENSKGSTSEKDGMHHTVTKHRGIITLYRHQKAAFAITSRRGPTPKAVKAQIADLPAGSSGNILVELDEAQKPYLVQRRGAEFALTTIVKHFGGEMAVKLPHLWDAMVGPLRNTIDINNFDGKSLLDKGDSPAQELVNSLQVFETAAASMDSELHPLLVQHLPHLYMCLQYPSTAVRHMAARCVGVMSKIATMETMNIFLEKVLPWLGAIDDSVKQEGAIEALACVMEQLDVGIVPYIVLLVVPVLGRMSDQTDSVRFMATQCFATLIRLMPLEAGIPDPPNMSAELIQLKAKERHFLEQLLDGKKLENYKIPVPINAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCHRAQEYARSKLAECMPLPSLVVCPPTLTGHWVDEVGKFCSREYLNPLHYTGPPTERIRLQHQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGVLAMDALHRQVLPFLLRRMKEDVLQDLPPKIIQDYYCTLSPLQVQLYEDFAKSRAKCDVDETVSSATLSEETEKPKLKATGHVFQALQYLRKLCNHPALVLTPQHPEFKTTAEKLAVQNSSLHDIQHAPKLSALKQLLLDCGLGNGSTSESGTESVVAQHRILIFCQLKSMLDIVEHDLLKPHLPSVTYLRLDGSIPPGQRHSIVSRFNNDPSIDVLLLTTHVGGLGLNLTGADTVVFVEHDWNPMRDLQAMDRAHRIGQKRVVNVYRLITRGTLEEKIMGLQKFKMNIANTVISQENSSLQSMGTDQLLDLFTLDKDGKAEKADTSTSGKASMKSILENLSDLWDQEQYDSEYSLENFMHSLK
|
3.6.4.-
| null |
negative regulation of chromatin binding [GO:0035562]; negative regulation of DNA-templated transcription [GO:0045892]
|
intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent chromatin remodeler activity [GO:0140658]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; TBP-class protein binding [GO:0017025]; transcription coregulator activity [GO:0003712]
|
PF12054;PF00271;PF00176;
|
1.25.10.10;3.40.50.300;3.40.50.10810;
|
SNF2/RAD54 helicase family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Regulates transcription in association with TATA binding protein (TBP). Removes TBP from the TATA box in an ATP-dependent manner.
|
Homo sapiens (Human)
|
O14983
|
AT2A1_HUMAN
|
MEAAHAKTTEECLAYFGVSETTGLTPDQVKRNLEKYGLNELPAEEGKTLWELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILIANAIVGVWQERNAENAIEALKEYEPEMGKVYRADRKSVQRIKARDIVPGDIVEVAVGDKVPADIRILAIKSTTLRVDQSILTGESVSVIKHTEPVPDPRAVNQDKKNMLFSGTNIAAGKALGIVATTGVGTEIGKIRDQMAATEQDKTPLQQKLDEFGEQLSKVISLICVAVWLINIGHFNDPVHGGSWFRGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCKMFIIDKVDGDICLLNEFSITGSTYAPEGEVLKNDKPVRPGQYDGLVELATICALCNDSSLDFNEAKGVYEKVGEATETALTTLVEKMNVFNTDVRSLSKVERANACNSVIRQLMKKEFTLEFSRDRKSMSVYCSPAKSSRAAVGNKMFVKGAPEGVIDRCNYVRVGTTRVPLTGPVKEKIMAVIKEWGTGRDTLRCLALATRDTPPKREEMVLDDSARFLEYETDLTFVGVVGMLDPPRKEVTGSIQLCRDAGIRVIMITGDNKGTAIAICRRIGIFGENEEVADRAYTGREFDDLPLAEQREACRRACCFARVEPSHKSKIVEYLQSYDEITAMTGDGVNDAPALKKAEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAALGLPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMDRPPRSPKEPLISGWLFFRYMAIGGYVGAATVGAAAWWFLYAEDGPHVNYSQLTHFMQCTEDNTHFEGIDCEVFEAPEPMTMALSVLVTIEMCNALNSLSENQSLLRMPPWVNIWLLGSICLSMSLHFLILYVDPLPMIFKLRALDLTQWLMVLKISLPVIGLDEILKFVARNYLEDPEDERRK
|
7.2.2.10
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P04191};
|
apoptotic mitochondrial changes [GO:0008637]; calcium ion import [GO:0070509]; calcium ion import into sarcoplasmic reticulum [GO:1990036]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; intracellular calcium ion homeostasis [GO:0006874]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; maintenance of mitochondrion location [GO:0051659]; monoatomic ion transmembrane transport [GO:0034220]; negative regulation of endoplasmic reticulum calcium ion concentration [GO:0032471]; negative regulation of striated muscle contraction [GO:0045988]; positive regulation of ATPase-coupled calcium transmembrane transporter activity [GO:1901896]; positive regulation of calcium ion import into sarcoplasmic reticulum [GO:1902082]; positive regulation of cardiac muscle cell contraction [GO:0106134]; positive regulation of endoplasmic reticulum calcium ion concentration [GO:0032470]; positive regulation of fast-twitch skeletal muscle fiber contraction [GO:0031448]; positive regulation of mitochondrial calcium ion concentration [GO:0051561]; regulation of cardiac conduction [GO:1903779]; regulation of striated muscle contraction [GO:0006942]; relaxation of skeletal muscle [GO:0090076]; response to endoplasmic reticulum stress [GO:0034976]
|
calcium channel complex [GO:0034704]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; H zone [GO:0031673]; I band [GO:0031674]; membrane [GO:0016020]; mitochondrion [GO:0005739]; perinuclear region of cytoplasm [GO:0048471]; platelet dense tubular network membrane [GO:0031095]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum membrane [GO:0033017]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calcium ion binding [GO:0005509]; calcium-dependent ATPase activity [GO:0030899]; P-type calcium transporter activity [GO:0005388]; protein homodimerization activity [GO:0042803]
|
PF13246;PF00689;PF00690;PF00122;PF00702;
|
3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000;
|
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIA subfamily
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P04191}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P04191}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:P04191}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P04191}.
|
CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; Evidence={ECO:0000250|UniProtKB:P04191}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18106; Evidence={ECO:0000250|UniProtKB:P04191};
| null | null | null | null |
FUNCTION: Key regulator of striated muscle performance by acting as the major Ca(2+) ATPase responsible for the reuptake of cytosolic Ca(2+) into the sarcoplasmic reticulum. Catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen (By similarity). Contributes to calcium sequestration involved in muscular excitation/contraction (PubMed:10914677). {ECO:0000250|UniProtKB:P04191, ECO:0000269|PubMed:10914677}.
|
Homo sapiens (Human)
|
O14986
|
PI51B_HUMAN
|
MSSAAENGEAAPGKQNEEKTYKKTASSAIKGAIQLGIGYTVGNLTSKPERDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPLIELSNPGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIVVMNNVLPRSMRMHFTYDLKGSTYKRRASRKEREKSNPTFKDLDFLQDMHEGLYFDTETYNALMKTLQRDCRVLESFKIMDYSLLLGIHFLDHSLKEKEEETPQNVPDAKRTGMQKVLYSTAMESIQGPGKSGDGIITENPDTMGGIPAKSHRGEKLLLFMGIIDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFKKIQALKASPSKKRCNSIAALKATSQEIVSSISQEWKDEKRDLLTEGQSFSSLDEEALGSRHRPDLVPSTPSLFEAASLATTISSSSLYVNEHYPHDRPTLYSNSKGLPSSSTFTLEEGTIYLTAEPNTLEVQDDNASVLDVYL
|
2.7.1.68
| null |
phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphorylation [GO:0016310]; regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051896]
|
cytosol [GO:0005829]; endomembrane system [GO:0012505]; plasma membrane [GO:0005886]; uropod [GO:0001931]
|
1-phosphatidylinositol-3-phosphate 5-kinase activity [GO:0000285]; 1-phosphatidylinositol-4-phosphate 5-kinase activity [GO:0016308]; 1-phosphatidylinositol-5-kinase activity [GO:0052810]; ATP binding [GO:0005524]; phosphatidylinositol kinase activity [GO:0052742]
|
PF01504;
|
3.30.810.10;3.30.800.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P70181}. Cell membrane {ECO:0000250|UniProtKB:P70181}. Endomembrane system. Note=Associated with membranes. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:14425, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.68; Evidence={ECO:0000250|UniProtKB:P70181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14426; Evidence={ECO:0000250|UniProtKB:P70181}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 4-phosphate + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 4,5-bisphosphate + ADP + H(+); Xref=Rhea:RHEA:40363, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77136, ChEBI:CHEBI:77137, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P70181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40364; Evidence={ECO:0000250|UniProtKB:P70181}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-myo-inositol 4-phosphate + ATP = 1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-myo-inositol 4,5-bisphosphate + ADP + H(+); Xref=Rhea:RHEA:40367, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77139, ChEBI:CHEBI:77140, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P70181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40368; Evidence={ECO:0000250|UniProtKB:P70181}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-myo-inositol + ATP = 1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate + ADP + H(+); Xref=Rhea:RHEA:40379, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77163, ChEBI:CHEBI:77164, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P70181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40380; Evidence={ECO:0000250|UniProtKB:P70181}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-1D-myo-inositol + ATP = 1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate + ADP + H(+); Xref=Rhea:RHEA:40383, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77158, ChEBI:CHEBI:77159, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P70181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40384; Evidence={ECO:0000250|UniProtKB:P70181}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate + ADP + H(+); Xref=Rhea:RHEA:40375, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77160, ChEBI:CHEBI:133606, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P70181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40376; Evidence={ECO:0000250|UniProtKB:P70181}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-1D-myo-inositol + ATP = 1,2-di(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate + ADP + H(+); Xref=Rhea:RHEA:40387, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77165, ChEBI:CHEBI:77167, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P70181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40388; Evidence={ECO:0000250|UniProtKB:P70181};
| null | null | null | null |
FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility (By similarity). PtdIns(4,5)P2 can directly act as a second messenger or can be utilized as a precursor to generate other second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3/PIP3) (By similarity). Mediates RAC1-dependent reorganization of actin filaments. Contributes to the activation of phospholipase PLD2. Together with PIP5K1A, is required, after stimulation by G-protein coupled receptors, for the synthesis of IP3 that will induce stable platelet adhesion (By similarity). {ECO:0000250|UniProtKB:P70181, ECO:0000250|UniProtKB:Q99755}.
|
Homo sapiens (Human)
|
O14994
|
SYN3_HUMAN
|
MNFLRRRLSDSSFMANLPNGYMTDLQRPDSSTSSPASPAMERRHPQPLAASFSSPGSSLFSSLSSAMKQAPQATSGLMEPPGPSTPIVQRPRILLVIDDAHTDWSKYFHGKKVNGEIEIRVEQAEFSELNLAAYVTGGCMVDMQVVRNGTKVVSRSFKPDFILVRQHAYSMALGEDYRSLVIGLQYGGLPAVNSLYSVYNFCSKPWVFSQLIKIFHSLGPEKFPLVEQTFFPNHKPMVTAPHFPVVVKLGHAHAGMGKIKVENQLDFQDITSVVAMAKTYATTEAFIDSKYDIRIQKIGSNYKAYMRTSISGNWKANTGSAMLEQVAMTERYRLWVDSCSEMFGGLDICAVKAVHSKDGRDYIIEVMDSSMPLIGEHVEEDRQLMADLVVSKMSQLPMPGGTAPSPLRPWAPQIKSAKSPGQAQLGPQLGQPQPRPPPQGGPRQAQSPQPQRSGSPSQQRLSPQGQQPLSPQSGSPQQQRSPGSPQLSRASSGSSPNQASKPGATLASQPRPPVQGRSTSQQGEESKKPAPPHPHLNKSQSLTNSLSTSDTSQRGTPSEDEAKAETIRNLRKSFASLFSD
| null | null |
neurotransmitter secretion [GO:0007269]; regulation of synaptic transmission, GABAergic [GO:0032228]; synaptic vesicle clustering [GO:0097091]
|
extrinsic component of synaptic vesicle membrane [GO:0098850]; glutamatergic synapse [GO:0098978]; postsynaptic density [GO:0014069]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]
|
ATP binding [GO:0005524]
|
PF02078;PF02750;PF10581;
|
3.40.50.20;3.30.1490.20;3.30.470.20;
|
Synapsin family
|
PTM: Phosphorylation at Ser-9 dissociates synapsins from synaptic vesicles. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Note=Peripheral membrane protein localized to the cytoplasmic surface of synaptic vesicles.
| null | null | null | null | null |
FUNCTION: May be involved in the regulation of neurotransmitter release and synaptogenesis.
|
Homo sapiens (Human)
|
O15013
|
ARHGA_HUMAN
|
MRPPGFLSRAPSLNRAERGIWSCSMDQREPLPPAPAENEMKYDTNNNEEEEGEQFDFDSGDEIPEADRQAPSAPETGGAGASEAPAPTGGEDGAGAETTPVAEPTKLVLPMKVNPYSVIDITPFQEDQPPTPVPSAEEENVGLHVPCGYLVPVPCGYAVPSNLPLLLPAYSSPVIICATSLDEEAETPEVTEDRQPNSLSSEEPPTSEDQVGREDSALARWAADPANTAWMENPEEAIYDDVPRENSDSEPDEMIYDDVENGDEGGNSSLEYGWSSSEFESYEEQSDSECKNGIPRSFLRSNHKKQLSHDLTRLKEHYEKKMRDLMASTVGVVEIQQLRQKHELKMQKLVKAAKDGTKDGLERTRAAVKRGRSFIRTKSLIAQDHRSSLEEEQNLFIDVDCKHPEAILTPMPEGLSQQQVVRRYILGSVVDSEKNYVDALKRILEQYEKPLSEMEPKVLSERKLKTVFYRVKEILQCHSLFQIALASRVSEWDSVEMIGDVFVASFSKSMVLDAYSEYVNNFSTAVAVLKKTCATKPAFLEFLKQEQEASPDRTTLYSLMMKPIQRFPQFILLLQDMLKNTSKGHPDRLPLQMALTELETLAEKLNERKRDADQRCEVKQIAKAINERYLNKLLSSGSRYLIRSDDMIETVYNDRGEIVKTKERRVFMLNDVLMCATVSSRPSHDSRVMSSQRYLLKWSVPLGHVDAIEYGSSAGTGEHSRHLAVHPPESLAVVANAKPNKVYMGPGQLYQDLQNLLHDLNVIGQITQLIGNLKGNYQNLNQSVAHDWTSGLQRLILKKEDEIRAADCCRIQLQLPGKQDKSGRPTFFTAVFNTFTPAIKESWVNSLQMAKLALEEENHMGWFCVEDDGNHIKKEKHPLLVGHMPVMVAKQQEFKIECAAYNPEPYLNNESQPDSFSTAHGFLWIGSCTHQMGQIAIVSFQNSTPKVIECFNVESRILCMLYVPVEEKRREPGAPPDPETPAVRASDVPTICVGTEEGSISIYKSSQGSKKVRLQHFFTPEKSTVMSLACTSQSLYAGLVNGAVASYARAPDGSWDSEPQKVIKLGVLPVRSLLMMEDTLWAASGGQVFIISVETHAVEGQLEAHQEEGMVISHMAVSGVGIWIAFTSGSTLRLFHTETLKHLQDINIATPVHNMLPGHQRLSVTSLLVCHGLLMVGTSLGVLVALPVPRLQGIPKVTGRGMVSYHAHNSPVKFIVLATALHEKDKDKSRDSLAPGPEPQDEDQKDALPSGGAGSSLSQGDPDAAIWLGDSLGSMTQKSDLSSSSGSLSLSHGSSSLEHRSEDSTIYDLLKDPVSLRSKARRAKKAKASSALVVCGGQGHRRVHRKARQPHQEELAPTVMVWQIPLLNI
| null | null |
actin cytoskeleton organization [GO:0030036]; activation of GTPase activity [GO:0090630]; centrosome duplication [GO:0051298]; mitotic spindle assembly [GO:0090307]; myelination in peripheral nervous system [GO:0022011]; positive regulation of stress fiber assembly [GO:0051496]; regulation of small GTPase mediated signal transduction [GO:0051056]
|
centrosome [GO:0005813]; cytosol [GO:0005829]
|
guanyl-nucleotide exchange factor activity [GO:0005085]; kinesin binding [GO:0019894]
|
PF19057;PF00621;PF19056;
|
1.20.900.10;2.130.10.10;
| null |
PTM: Methylated at Gln-1338 by N6AMT1. {ECO:0000269|PubMed:26797129}.
| null | null | null | null | null | null |
FUNCTION: May play a role in developmental myelination of peripheral nerves. {ECO:0000269|PubMed:14508709}.
|
Homo sapiens (Human)
|
O15014
|
ZN609_HUMAN
|
MSLSSGASGGKGVDANPVETYDSGDEWDIGVGNLIIDLDADLEKDQQKLEMSGSKEVGIPAPNAVATLPDNIKFVTPVPGPQGKEGKSKSKRSKSGKDTSKPTPGTSLFTPSEGAASKKEVQGRSGDGANAGGLVAAIAPKGSEKAAKASRSVAGSKKEKENSSSKSKKERSEGVGTCSEKDPGVLQPVPLGGRGGQYDGSAGVDTGAVEPLGSIAIEPGAALNPLGTKPEPEEGENECRLLKKVKSEKMESPVSTPAVLPIHLLVPVVNNDISSPCEQIMVRTRSVGVNTCDVALATEPECLGPCEPGTSVNLEGIVWQETEDGMLVVNVTWRNKTYVGTLLDCTRHDWAPPRFCDSPTSDLEMRNGRGRGKRMRPNSNTPVNETATASDSKGTSNSSKTRAGANSKGRRGSQNSSEHRPPASSTSEDVKASPSSANKRKNKPLSDMELNSSSEDSKGSKRVRTNSMGSATGPLPGTKVEPTVLDRNCPSPVLIDCPHPNCNKKYKHINGLKYHQAHAHTDDDSKPEADGDSEYGEEPILHADLGSCNGASVSQKGSLSPARSATPKVRLVEPHSPSPSSKFSTKGLCKKKLSGEGDTDLGALSNDGSDDGPSVMDETSNDAFDSLERKCMEKEKCKKPSSLKPEKIPSKSLKSARPIAPAIPPQQIYTFQTATFTAASPGSSSGLTATVAQAMPNSPQLKPIQPKPTVMGEPFTVNPALTPAKDKKKKDKKKKESSKELESPLTPGKVCRAEEGKSPFRESSGDGMKMEGLLNGSSDPHQSRLASIKAEADKIYSFTDNAPSPSIGGSSRLENTTPTQPLTPLHVVTQNGAEASSVKTNSPAYSDISDAGEDGEGKVDSVKSKDAEQLVKEGAKKTLFPPQPQSKDSPYYQGFESYYSPSYAQSSPGALNPSSQAGVESQALKTKRDEEPESIEGKVKNDICEEKKPELSSSSQQPSVIQQRPNMYMQSLYYNQYAYVPPYGYSDQSYHTHLLSTNTAYRQQYEEQQKRQSLEQQQRGVDKKAEMGLKEREAALKEEWKQKPSIPPTLTKAPSLTDLVKSGPGKAKEPGADPAKSVIIPKLDDSSKLPGQAPEGLKVKLSDASHLSKEASEAKTGAECGRQAEMDPILWYRQEAEPRMWTYVYPAKYSDIKSEDERWKEERDRKLKEERSRSKDSVPKEDGKESTSSDCKLPTSEESRLGSKEPRPSVHVPVSSPLTQHQSYIPYMHGYSYSQSYDPNHPSYRSMPAVMMQNYPGSYLPSSYSFSPYGSKVSGGEDADKARASPSVTCKSSSESKALDILQQHASHYKSKSPTISDKTSQERDRGGCGVVGGGGSCSSVGGASGGERSVDRPRTSPSQRLMSTHHHHHHLGYSLLPAQYNLPYAAGLSSTAIVASQQGSTPSLYPPPRR
| null | null |
muscle organ development [GO:0007517]; positive regulation of neuron migration [GO:2001224]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of myoblast proliferation [GO:2000291]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; promoter-specific chromatin binding [GO:1990841]
| null | null | null | null |
SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:28344082}.
| null | null | null | null | null |
FUNCTION: Transcription factor, which activates RAG1, and possibly RAG2, transcription. Through the regulation of RAG1/2 expression, may regulate thymocyte maturation. Along with NIPBL and the multiprotein complex Integrator, promotes cortical neuron migration during brain development by regulating the transcription of crucial genes in this process. Preferentially binds promoters containing paused RNA polymerase II. Up-regulates the expression of SEMA3A, NRP1, PLXND1 and GABBR2 genes, among others. {ECO:0000250|UniProtKB:Q8BZ47}.; FUNCTION: [Isoform 2]: Involved in the regulation of myoblast proliferation during myogenesis. {ECO:0000269|PubMed:28344082}.
|
Homo sapiens (Human)
|
O15015
|
ZN646_HUMAN
|
MEDTPPSLSCSDCQRHFPSLPELSRHRELLHPSPNQDSEEADSIPRPYRCQQCGRGYRHPGSLVNHRRTHETGLFPCTTCGKDFSNPMALKSHMRTHAPEGRRRHRPPRPKEATPHLQGETVSTDSWGQRLGSSEGWENQTKHTEETPDCESVPDPRAASGTWEDLPTRQREGLASHPGPEDGADGWGPSTNSARAPPLPIPASSLLSNLEQYLAESVVNFTGGQEPTQSPPAEEERRYKCSQCGKTYKHAGSLTNHRQSHTLGIYPCAICFKEFSNLMALKNHSRLHAQYRPYHCPHCPRVFRLPRELLEHQQSHEGERQEPRWEEKGMPTTNGHTDESSQDQLPSAQMLNGSAELSTSGELEDSGLEEYRPFRCGDCGRTYRHAGSLINHRKSHQTGVYPCSLCSKQLFNAAALKNHVRAHHRPRQGVGENGQPSVPPAPLLLAETTHKEEEDPTTTLDHRPYKCSECGRAYRHRGSLVNHRHSHRTGEYQCSLCPRKYPNLMALRNHVRVHCKAARRSADIGAEGAPSHLKVELPPDPVEAEAAPHTDQDHVCKHEEEATDITPAADKTAAHICSICGLLFEDAESLERHGLTHGAGEKENSRTETTMSPPRAFACRDCGKSYRHSGSLINHRQTHQTGDFSCGACAKHFHTMAAMKNHLRRHSRRRSRRHRKRAGGASGGREAKLLAAESWTRELEDNEGLESPQDPSGESPHGAEGNLESDGDCLQAESEGDKCGLERDETHFQGDKESGGTGEGLERKDASLLDNLDIPGEEGGGTHFCDSLTGVDEDQKPATGQPNSSSHSANAVTGWQAGAAHTCSDCGHSFPHATGLLSHRPCHPPGIYQCSLCPKEFDSLPALRSHFQNHRPGEATSAQPFLCCLCGMIFPGRAGYRLHRRQAHSSSGMTEGSEEEGEEEGVAEAAPARSPPLQLSEAELLNQLQREVEALDSAGYGHICGCCGQTYDDLGSLERHHQSQSSGTTADKAPSPLGVAGDAMEMVVDSVLEDIVNSVSGEGGDAKSQEGAGTPLGDSLCIQGGESLLEAQPRPFRCNQCGKTYRHGGSLVNHRKIHQTGDFLCPVCSRCYPNLAAYRNHLRNHPRCKGSEPQVGPIPEAAGSSELQVGPIPEGGSNKPQHMAEEGPGQAEVEKLQEELKVEPLEEVARVKEEVWEETTVKGEEIEPRLETAEKGCQTEASSERPFSCEVCGRSYKHAGSLINHRQSHQTGHFGCQACSKGFSNLMSLKNHRRIHADPRRFRCSECGKAFRLRKQLASHQRVHMERRGGGGTRKATREDRPFRCGQCGRTYRHAGSLLNHRRSHETGQYSCPTCPKTYSNRMALKDHQRLHSENRRRRAGRSRRTAVRCALCGRSFPGRGSLERHLREHEETEREPANGQGGLDGTAASEANLTGSQGLETQLGGAEPVPHLEDGVPRPGERSQSPIRAASSEAPEPLSWGAGKAGGWPVGGGLGNHSGGWVPQFLTRSEEPEDSVHRSPCHAGDCQLNGPTLSHMDSWDNRDNSSQLQPGSHSSCSQCGKTYCQSGSLLNHNTNKTDRHYCLLCSKEFLNPVATKSHSHNHIDAQTFACPDCGKAFESHQELASHLQAHARGHSQVPAQMEEARDPKAGTGEDQVVLPGQGKAQEAPSETPRGPGESVERARGGQAVTSMAAEDKERPFRCTQCGRSYRHAGSLLNHQKAHTTGLYPCSLCPKLLPNLLSLKNHSRTHTDPKRHCCSICGKAFRTAARLEGHGRVHAPREGPFTCPHCPRHFRRRISFVQHQQQHQEEWTVAGSGAPVAPVTGRGDLPLPPPPTPTTPLLDPSPQWPADLSFSL
| null | null |
regulation of DNA-templated transcription [GO:0006355]
|
nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00096;PF13912;
|
3.30.160.60;
|
Krueppel C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: May be involved in transcriptional regulation.
|
Homo sapiens (Human)
|
O15018
|
PDZD2_HUMAN
|
MPITQDNAVLHLPLLYQWLQNSLQEGGDGPEQRLCQAAIQKLQEYIQLNFAVDESTVPPDHSPPEMEICTVYLTKELGDTETVGLSFGNIPVFGDYGEKRRGGKKRKTHQGPVLDVGCIWVTELRKNSPAGKSGKVRLRDEILSLNGQLMVGVDVSGASYLAEQCWNGGFIYLIMLRRFKHKAHSTYNGNSSNSSEPGETPTLELGDRTAKKGKRTRKFGVISRPPANKAPEESKGSAGCEVSSDPSTELENGPDPELGNGHVFQLENGPDSLKEVAGPHLERSEVDRGTEHRIPKTDAPLTTSNDKRRFSKGGKTDFQSSDCLAREEVGRIWKMELLKESDGLGIQVSGGRGSKRSPHAIVVTQVKEGGAAHRDGRLSLGDELLVINGHLLVGLSHEEAVAILRSATGMVQLVVASKENSAEDLLRLTSKSLPDLTSSVEDVSSWTDNEDQEADGEEDEGTSSSVQRAMPGTDEPQDVCGAEESKGNLESPKQGSNKIKLKSRLSGGVHRLESVEEYNELMVRNGDPRIRMLEVSRDGRKHSLPQLLDSSSASQEYHIVKKSTRSLSTTQVESPWRLIRPSVISIIGLYKEKGKGLGFSIAGGRDCIRGQMGIFVKTIFPNGSAAEDGRLKEGDEILDVNGIPIKGLTFQEAIHTFKQIRSGLFVLTVRTKLVSPSLTPCSTPTHMSRSASPNFNTSGGASAGGSDEGSSSSLGRKTPGPKDRIVMEVTLNKEPRVGLGIGACCLALENSPPGIYIHSLAPGSVAKMESNLSRGDQILEVNSVNVRHAALSKVHAILSKCPPGPVRLVIGRHPNPKVSEQEMDEVIARSTYQESKEANSSPGLGTPLKSPSLAKKDSLISESELSQYFAHDVPGPLSDFMVAGSEDEDHPGSGCSTSEEGSLPPSTSTHKEPGKPRANSLVTLGSHRASGLFHKQVTVARQASLPGSPQALRNPLLRQRKVGCYDANDASDEEEFDREGDCISLPGALPGPIRPLSEDDPRRVSISSSKGMDVHNQEERPRKTLVSKAISAPLLGSSVDLEESIPEGMVDAASYAANLTDSAEAPKGSPGSWWKKELSGSSSAPKLEYTVRTDTQSPTNTGSPSSPQQKSEGLGSRHRPVARVSPHCKRSEAEAKPSGSQTVNLTGRANDPCDLDSRVQATSVKVTVAGFQPGGAVEKESLGKLTTGDACVSTSCELASALSHLDASHLTENLPKAASELGQQPMTELDSSSDLISSPGKKGAAHPDPSKTSVDTGQVSRPENPSQPASPRVTKCKARSPVRLPHEGSPSPGEKAAAPPDYSKTRSASETSTPHNTRRVAALRGAGPGAEGMTPAGAVLPGDPLTSQEQRQGAPGNHSKALEMTGIHAPESSQEPSLLEGADSVSSRAPQASLSMLPSTDNTKEACGHVSGHCCPGGSRESPVTDIDSFIKELDASAARSPSSQTGDSGSQEGSAQGHPPAGAGGGSSCRAEPVPGGQTSSPRRAWAAGAPAYPQWASQPSVLDSINPDKHFTVNKNFLSNYSRNFSSFHEDSTSLSGLGDSTEPSLSSMYGDAEDSSSDPESLTEAPRASARDGWSPPRSRVSLHKEDPSESEEEQIEICSTRGCPNPPSSPAHLPTQAAICPASAKVLSLKYSTPRESVASPREKAACLPGSYTSGPDSSQPSSLLEMSSQEHETHADISTSQNHRPSCAEETTEVTSASSAMENSPLSKVARHFHSPPIILSSPNMVNGLEHDLLDDETLNQYETSINAAASLSSFSVDVPKNGESVLENLHISESQDLDDLLQKPKMIARRPIMAWFKEINKHNQGTHLRSKTEKEQPLMPARSPDSKIQMVSSSQKKGVTVPHSPPQPKTNLENKDLSKKSPAEMLLTNGQKAKCGPKLKRLSLKGKAKVNSEAPAANAVKAGGTDHRKPLISPQTSHKTLSKAVSQRLHVADHEDPDRNTTAAPRSPQCVLESKPPLATSGPLKPSVSDTSIRTFVSPLTSPKPVPEQGMWSRFHMAVLSEPDRGCPTTPKSPKCRAEGRAPRADSGPVSPAASRNGMSVAGNRQSEPRLASHVAADTAQPRPTGEKGGNIMASDRLERTNQLKIVEISAEAVSETVCGNKPAESDRRGGCLAQGNCQEKSEIRLYRQVAESSTSHPSSLPSHASQAEQEMSRSFSMAKLASSSSSLQTAIRKAEYSQGKSSLMSDSRGVPRNSIPGGPSGEDHLYFTPRPATRTYSMPAQFSSHFGREGHPPHSLGRSRDSQVPVTSSVVPEAKASRGGLPSLANGQGIYSVKPLLDTSRNLPATDEGDIISVQETSCLVTDKIKVTRRHYCYEQNWPHESTSFFSVKQRIKSFENLANADRPVAKSGASPFLSVSSKPPIGRRSSGSIVSGSLGHPGDAAARLLRRSLSSCSENQSEAGTLLPQMAKSPSIMTLTISRQNPPETSSKGSDSELKKSLGPLGIPTPTMTLASPVKRNKSSVRHTQPSPVSRSKLQELRALSMPDLDKLCSEDYSAGPSAVLFKTELEITPRRSPGPPAGGVSCPEKGGNRACPGGSGPKTSAAETPSSASDTGEAAQDLPFRRSWSVNLDQLLVSAGDQQRLQSVLSSVGSKSTILTLIQEAKAQSENEEDVCFIVLNRKEGSGLGFSVAGGTDVEPKSITVHRVFSQGAASQEGTMNRGDFLLSVNGASLAGLAHGNVLKVLHQAQLHKDALVVIKKGMDQPRPSARQEPPTANGKGLLSRKTIPLEPGIGRSVAVHDALCVEVLKTSAGLGLSLDGGKSSVTGDGPLVIKRVYKGGAAEQAGIIEAGDEILAINGKPLVGLMHFDAWNIMKSVPEGPVQLLIRKHRNSS
| null | null |
cell adhesion [GO:0007155]
|
cell-cell junction [GO:0005911]; centriolar satellite [GO:0034451]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; intracellular membrane-bounded organelle [GO:0043231]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
| null |
PF00595;
|
2.30.42.10;
| null |
PTM: A secreted form is produced by caspase-mediated proteolytic cleavage. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9QZR8}. Cytoplasm {ECO:0000269|PubMed:11289102}. Endoplasmic reticulum {ECO:0000269|PubMed:11289102}. Note=At cell-cell contacts in lung epithelial cells. {ECO:0000250|UniProtKB:Q9QZR8}.; SUBCELLULAR LOCATION: [Processed PDZ domain-containing protein 2]: Secreted {ECO:0000250}.
| null | null | null | null | null | null |
Homo sapiens (Human)
|
O15020
|
SPTN2_HUMAN
|
MSSTLSPTDFDSLEIQGQYSDINNRWDLPDSDWDNDSSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVTCRVGDLYSDLRDGRNLLRLLEVLSGEILPKPTKGRMRIHCLENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLVWTIILRFQIQDISVETEDNKEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLLDFESLKKCNAHYNLQNAFNLAEKELGLTKLLDPEDVNVDQPDEKSIITYVATYYHYFSKMKALAVEGKRIGKVLDHAMEAERLVEKYESLASELLQWIEQTIVTLNDRQLANSLSGVQNQLQSFNSYRTVEKPPKFTEKGNLEVLLFTIQSKLRANNQKVYTPREGRLISDINKAWERLEKAEHERELALRTELIRQEKLEQLAARFDRKAAMRETWLSENQRLVSQDNFGLELAAVEAAVRKHEAIETDIVAYSGRVQAVDAVAAELAAERYHDIKRIAARQHNVARLWDFLRQMVAARRERLLLNLELQKVFQDLLYLMDWMEEMKGRLQSQDLGRHLAGVEDLLQLHELVEADIAVQAERVRAVSASALRFCNPGKEYRPCDPQLVSERVAKLEQSYEALCELAAARRARLEESRRLWRFLWEVGEAEAWVREQQHLLASADTGRDLTGALRLLNKHTALRGEMSGRLGPLKLTLEQGQQLVAEGHPGASQASARAAELQAQWERLEALAEERAQRLAQAASLYQFQADANDMEAWLVDALRLVSSPELGHDEFSTQALARQHRALEEEIRSHRPTLDALREQAAALPPTLSRTPEVQSRVPTLERHYEELQARAGERARALEAALALYTMLSEAGACGLWVEEKEQWLNGLALPERLEDLEVVQQRFETLEPEMNTLAAQITAVNDIAEQLLKANPPGKDRIVNTQEQLNHRWQQFRRLADGKKAALTSALSIQNYHLECTETQAWMREKTKVIESTQGLGNDLAGVLALQRKLAGTERDLEAIAARVGELTREANALAAGHPAQAVAINARLREVQTGWEDLRATMRRREESLGEARRLQDFLRSLDDFQAWLGRTQTAVASEEGPATLPEAEALLAQHAALRGEVERAQSEYSRLRALGEEVTRDQADPQCLFLRQRLEALGTGWEELGRMWESRQGRLAQAHGFQGFLRDARQAEGVLSSQEYVLSHTEMPGTLQAADAAIKKLEDFMSTMDANGERIHGLLEAGRQLVSEGNIHADKIREKADSIERRHKKNQDAAQQFLGRLRDNREQQHFLQDCHELKLWIDEKMLTAQDVSYDEARNLHTKWQKHQAFMAELAANKDWLDKVDKEGRELTLEKPELKALVSEKLRDLHRRWDELETTTQAKARSLFDANRAELFAQSCCALESWLESLQAQLHSDDYGKDLTSVNILLKKQQMLEWEMAVREKEVEAIQAQAKALAQEDQGAGEVERTSRAVEEKFRALCQPMRERCRRLQASREQHQFHRDVEDEILWVTERLPMASSMEHGKDLPSVQLLMKKNQTLQKEIQGHEPRIADLRERQRALGAAAAGPELAELQEMWKRLGHELELRGKRLEDALRAQQFYRDAAEAEAWMGEQELHMMGQEKAKDELSAQAEVKKHQVLEQALADYAQTIHQLAASSQDMIDHEHPESTRISIRQAQVDKLYAGLKELAGERRERLQEHLRLCQLRRELDDLEQWIQEREVVAASHELGQDYEHVTMLRDKFREFSRDTSTIGQERVDSANALANGLIAGGHAARATVAEWKDSLNEAWADLLELLDTRGQVLAAAYELQRFLHGARQALARVQHKQQQLPDGTGRDLNAAEALQRRHCAYEHDIQALSPQVQQVQDDGHRLQKAYAGDKAEEIGRHMQAVAEAWAQLQGSSAARRQLLLDTTDKFRFFKAVRELMLWMDEVNLQMDAQERPRDVSSADLVIKNQQGIKAEIEARADRFSSCIDMGKELLARSHYAAEEISEKLSQLQARRQETAEKWQEKMDWLQLVLEVLVFGRDAGMAEAWLCSQEPLVRSAELGCTVDEVESLIKRHEAFQKSAVAWEERFCALEKLTALEEREKERKRKREEEERRKQPPAPEPTASVPPGDLVGGQTASDTTWDGTQPRPPPSTQAPSVNGVCTDGEPSQPLLGQQRLEHSSFPEGPGPGSGDEANGPRGERQTRTRGPAPSAMPQSRSTESAHAATLPPRGPEPSAQEQMEGMLCRKQEMEAFGKKAANRSWQNVYCVLRRGSLGFYKDAKAASAGVPYHGEVPVSLARAQGSVAFDYRKRKHVFKLGLQDGKEYLFQAKDEAEMSSWLRVVNAAIATASSASGEPEEPVVPSTTRGMTRAMTMPPVSPVGAEGPVVLRSKDGREREREKRFSFFKKNK
| null | null |
actin cytoskeleton organization [GO:0030036]; actin filament capping [GO:0051693]; adult behavior [GO:0030534]; cerebellar Purkinje cell layer morphogenesis [GO:0021692]; multicellular organism growth [GO:0035264]; regulation of postsynaptic specialization assembly [GO:0099150]; synapse assembly [GO:0007416]; vesicle-mediated transport [GO:0016192]
|
apical plasma membrane [GO:0016324]; cell junction [GO:0030054]; cell projection [GO:0042995]; cortical actin cytoskeleton [GO:0030864]; cytosol [GO:0005829]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; intracellular membrane-bounded organelle [GO:0043231]; neuronal cell body [GO:0043025]; parallel fiber to Purkinje cell synapse [GO:0098688]; paranodal junction [GO:0033010]; plasma membrane [GO:0005886]; postsynaptic spectrin-associated cytoskeleton [GO:0099189]; presynapse [GO:0098793]; spectrin [GO:0008091]
|
actin binding [GO:0003779]; actin filament binding [GO:0051015]; cadherin binding [GO:0045296]; phospholipid binding [GO:0005543]; structural constituent of cytoskeleton [GO:0005200]; structural constituent of postsynapse [GO:0099186]; structural constituent of synapse [GO:0098918]
|
PF00307;PF15410;PF00435;
|
1.20.58.60;1.10.418.10;2.30.29.30;
|
Spectrin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
| null | null | null | null | null |
FUNCTION: Probably plays an important role in neuronal membrane skeleton.
|
Homo sapiens (Human)
|
O15021
|
MAST4_HUMAN
|
MGEKVSEAPEPVPRGCSGHGSRTPASALVAASSPGASSAESSSGSETLSEEGEPGGFSREHQPPPPPPLGGTLGARAPAAWAPASVLLERGVLALPPPLPGGAVPPAPRGSSASQEEQDEELDHILSPPPMPFRKCSNPDVASGPGKSLKYKRQLSEDGRQLRRGSLGGALTGRYLLPNPVAGQAWPASAETSNLVRMRSQALGQSAPSLTASLKELSLPRRGSFCRTSNRKSLIGNGQSPALPRPHSPLSAHAGNSPQDSPRNFSPSASAHFSFARRTDGRRWSLASLPSSGYGTNTPSSTVSSSCSSQEKLHQLPYQPTPDELHFLSKHFCTTESIATENRCRNTPMRPRSRSLSPGRSPACCDHEIIMMNHVYKERFPKATAQMEERLKEIITSYSPDNVLPLADGVLSFTHHQIIELARDCLDKSHQGLITSRYFLELQHKLDKLLQEAHDRSESGELAFIKQLVRKILIVIARPARLLECLEFDPEEFYYLLEAAEGHAKEGQGIKTDIPRYIISQLGLNKDPLEEMAHLGNYDSGTAETPETDESVSSSNASLKLRRKPRESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNLYEGHIEKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEAPPPDAQDLITLLLRQNPLERLGTGGAYEVKQHRFFRSLDWNSLLRQKAEFIPQLESEDDTSYFDTRSEKYHHMETEEEDDTNDEDFNVEIRQFSSCSHRFSKVFSSIDRITQNSAEEKEDSVDKTKSTTLPSTETLSWSSEYSEMQQLSTSNSSDTESNRHKLSSGLLPKLAISTEGEQDEAASCPGDPHEEPGKPALPPEECAQEEPEVTTPASTISSSTLSVGSFSEHLDQINGRSECVDSTDNSSKPSSEPASHMARQRLESTEKKKISGKVTKSLSASALSLMIPGDMFAVSPLGSPMSPHSLSSDPSSSRDSSPSRDSSAASASPHQPIVIHSSGKNYGFTIRAIRVYVGDSDIYTVHHIVWNVEEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLLKSGNKVSITTTPFENTSIKTGPARRNSYKSRMVRRSKKSKKKESLERRRSLFKKLAKQPSPLLHTSRSFSCLNRSLSSGESLPGSPTHSLSPRSPTPSYRSTPDFPSGTNSSQSSSPSSSAPNSPAGSGHIRPSTLHGLAPKLGGQRYRSGRRKSAGNIPLSPLARTPSPTPQPTSPQRSPSPLLGHSLGNSKIAQAFPSKMHSPPTIVRHIVRPKSAEPPRSPLLKRVQSEEKLSPSYGSDKKHLCSRKHSLEVTQEEVQREQSQREAPLQSLDENVCDVPPLSRARPVEQGCLKRPVSRKVGRQESVDDLDRDKLKAKVVVKKADGFPEKQESHQKSHGPGSDLENFALFKLEEREKKVYPKAVERSSTFENKASMQEAPPLGSLLKDALHKQASVRASEGAMSDGRVPAEHRQGGGDFRRAPAPGTLQDGLCHSLDRGISGKGEGTEKSSQAKELLRCEKLDSKLANIDYLRKKMSLEDKEDNLCPVLKPKMTAGSHECLPGNPVRPTGGQQEPPPASESRAFVSSTHAAQMSAVSFVPLKALTGRVDSGTEKPGLVAPESPVRKSPSEYKLEGRSVSCLKPIEGTLDIALLSGPQASKTELPSPESAQSPSPSGDVRASVPPVLPSSSGKKNDTTSARELSPSSLKMNKSYLLEPWFLPPSRGLQNSPAVSLPDPEFKRDRKGPHPTARSPGTVMESNPQQREGSSPKHQDHTTDPKLLTCLGQNLHSPDLARPRCPLPPEASPSREKPGLRESSERGPPTARSERSAARADTCREPSMELCFPETAKTSDNSKNLLSVGRTHPDFYTQTQAMEKAWAPGGKTNHKDGPGEARPPPRDNSSLHSAGIPCEKELGKVRRGVEPKPEALLARRSLQPPGIESEKSEKLSSFPSLQKDGAKEPERKEQPLQRHPSSIPPPPLTAKDLSSPAARQHCSSPSHASGREPGAKPSTAEPSSSPQDPPKPVAAHSESSSHKPRPGPDPGPPKTKHPDRSLSSQKPSVGATKGKEPATQSLGGSSREGKGHSKSGPDVFPATPGSQNKASDGIGQGEGGPSVPLHTDRAPLDAKPQPTSGGRPLEVLEKPVHLPRPGHPGPSEPADQKLSAVGEKQTLSPKHPKPSTVKDCPTLCKQTDNRQTDKSPSQPAANTDRRAEGKKCTEALYAPAEGDKLEAGLSFVHSENRLKGAERPAAGVGKGFPEARGKGPGPQKPPTEADKPNGMKRSPSATGQSSFRSTALPEKSLSCSSSFPETRAGVREASAASSDTSSAKAAGGMLELPAPSNRDHRKAQPAGEGRTHMTKSDSLPSFRVSTLPLESHHPDPNTMGGASHRDRALSVTATVGETKGKDPAPAQPPPARKQNVGRDVTKPSPAPNTDRPISLSNEKDFVVRQRRGKESLRSSPHKKAL
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
cytoskeleton organization [GO:0007010]; intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]
|
ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF08926;PF17820;PF00069;
|
2.30.42.10;1.20.1480.20;1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null | null |
Homo sapiens (Human)
|
O15027
|
SC16A_HUMAN
|
MQPPPQTVPSGMAGPPPAGNPRSVFWASSPYRRRANNNAAVAPTTCPLQPVTDPFAFSRQALQSTPLGSSSKSSPPVLQGPAPAGFSQHPGLLVPHTHARDSSQGPCEPLPGPLTQPRAHASPFSGALTPSAPPGPEMNRSAEVGPSSEPEVQTLPYLPHYIPGVDPETSHGGHPHGNMPGLDRPLSRQNPHDGVVTPAASPSLPQPGLQMPGQWGPVQGGPQPSGQHRSPCPEGPVPSGVPCATSVPHFPTPSILHQGPGHEQHSPLVAPPAALPSDGRDEVSHLQSGSHLANNSDPESTFRQNPRIVNHWASPELRQNPGVKNEHRPASALVNPLARGDSPENRTHHPLGAGAGSGCAPLEADSGASGALAMFFQGGETENEENLSSEKAGLSGQADFDDFCSSPGLGRPPAPTHVGAGSLCQALLPGPSNEAAGDVWGDTASTGVPDASGSQYENVENLEFVQNQEVLPSEPLNLDPSSPSDQFRYGPLPGPAVPRHGAVCHTGAPDATLHTVHPDSVSSSYSSRSHGRLSGSARPQELVGTFIQQEVGKPEDEASGSFFKQIDSSPVGGETDETTVSQNYRGSVSQPSTPSPPKPTGIFQTSANSSFEPVKSHLVGVKPFEADRANVVGEVRETCVRQKQCRPAAALPDASPGNLEQPPDNMETLCAPQVCPLPLNSTTEAVHMLPHAGAPPLDTVYPAPEKRPSARTQGPVKCESPATTLWAQSELPDFGGNVLLAPAAPALYVCAKPQPPVVQPPEEAMSGQQSRNPSSAAPVQSRGGIGASENLENPPKMGEEEALQSQASSGYASLLSSPPTESLQNPPVLIAQPDHSYNLAQPINFSVSLSNSHEKNQSWREALVGDRPAVSSWALGGDSGENTSLSGIPTSSVLSLSLPSSVAQSNFPQGSGASEMVSNQPANLLVQPPSQPVPENLVPESQKDRKAGSALPGFANSPAGSTSVVLVPPAHGTLVPDGNKANHSSHQEDTYGALDFTLSRTLENPVNVYNPSHSDSLASQQSVASHPRQSGPGAPNLDRFYQQVTKDAQGQPGLERAQQELVPPQQQASPPQLPKAMFSELSNPESLPAQGQAQNSAQSPASLVLVDAGQQLPPRPPQSSSVSLVSSGSGQAAVPSEQPWPQPVPALAPGPPPQDLAAYYYYRPLYDAYQPQYSLPYPPEPGAASLYYQDVYSLYEPRYRPYDGAASAYAQNYRYPEPERPSSRASHSSERPPPRQGYPEGYYSSKSGWSSQSDYYASYYSSQYDYGDPGHWDRYHYSARVRDPRTYDRRYWCDAEYDAYRREHSAFGDRPEKRDNNWRYDPRFTGSFDDDPDPHRDPYGEEVDRRSVHSEHSARSLHSAHSLASRRSSLSSHSHQSQIYRSHNVAAGSYEAPLPPGSFHGDFAYGTYRSNFSSGPGFPEYGYPADTVWPAMEQVSSRPTSPEKFSVPHVCARFGPGGQLIKVIPNLPSEGQPALVEVHSMEALLQHTSEQEEMRAFPGPLAKDDTHKVDVINFAQNKAMKCLQNENLIDKESASLLWNFIVLLCRQNGTVVGTDIAELLLRDHRTVWLPGKSPNEANLIDFTNEAVEQVEEEESGEAQLSFLTGGPAAAASSLERETERFRELLLYGRKKDALESAMKNGLWGHALLLASKMDSRTHARVMTRFANSLPINDPLQTVYQLMSGRMPAASTCCGDEKWGDWRPHLAMVLSNLNNNMDVESRTMATMGDTLASRGLLDAAHFCYLMAQAGFGVYTKKTTKLVLIGSNHSLPFLKFATNEAIQRTEAYEYAQSLGAETCPLPSFQVFKFIYSCRLAEMGLATQAFHYCEAIAKSILTQPHLYSPVLISQLVQMASQLRLFDPQLKEKPEEESLAAPTWLVHLQQVERQIKEGAGVWHQDGALPQQCPGTPSSEMEQLDRPGLSQPGALGIANPLLAVPAPSPEHSSPSVRLLPSAPQTLPDGPLASPARVPMFPVPLPPGPLEPGPGCVTPGPALGFLEPSGPGLPPGVPPLQERRHLLQEARSPDPGIVPQEAPVGNSLSELSEENFDGKFANLTPSRTVPDSEAPPGWDRADSGPTQPPLSLSPAPETKRPGQAAKKETKEPKKGESWFFRWLPGKKKTEAYLPDDKNKSIVWDEKKNQWVNLNEPEEEKKAPPPPPTSMPKTVQAAPPALPGPPGAPVNMYSRRAAGTRARYVDVLNPSGTQRSEPALAPADFVAPLAPLPIPSNLFVPTPDAEEPQLPDGTGREGPAAARGLANPEPAPEPKVLSSAASLPGSELPSSRPEGSQGGELSRCSSMSSLSREVSQHFNQAPGDLPAAGGPPSGAMPFYNPAQLAQACATSGSSRLGRIGQRKHLVLN
| null | null |
autophagy [GO:0006914]; COPII vesicle coating [GO:0048208]; endoplasmic reticulum organization [GO:0007029]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; Golgi organization [GO:0007030]; Golgi to plasma membrane transport [GO:0006893]; protein exit from endoplasmic reticulum [GO:0032527]; protein localization to endoplasmic reticulum exit site [GO:0070973]; protein localization to plasma membrane [GO:0072659]; protein stabilization [GO:0050821]; regulation of COPII vesicle coating [GO:0003400]; response to endoplasmic reticulum stress [GO:0034976]; substantia nigra development [GO:0021762]
|
cytosol [GO:0005829]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi membrane [GO:0000139]; organelle membrane [GO:0031090]; perinuclear region of cytoplasm [GO:0048471]
| null |
PF12932;PF12931;
|
1.25.40.1030;
|
SEC16 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17005010, ECO:0000269|PubMed:29300766}; Peripheral membrane protein {ECO:0000269|PubMed:17005010}. Golgi apparatus membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:E9QAT4}. Cytoplasm, cytosol {ECO:0000269|PubMed:17428803, ECO:0000269|PubMed:21768384}. Microsome membrane {ECO:0000269|PubMed:17428803}. Note=SAR1A activity is required to maintain SEC16A localization at discrete locations on the ER membrane perhaps by preventing its dissociation (PubMed:17192411). Localizes to endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). MIA3 and LRRK2 are required for its proper localization to ERES (PubMed:17428803, PubMed:19638414, PubMed:22355596, PubMed:25201882, PubMed:28442536). Recruited to microsomal membrane in SAR1-dependent manner (PubMed:17428803). {ECO:0000269|PubMed:17192411, ECO:0000269|PubMed:17428803, ECO:0000269|PubMed:19638414, ECO:0000269|PubMed:22355596, ECO:0000269|PubMed:25201882, ECO:0000269|PubMed:28442536}.
| null | null | null | null | null |
FUNCTION: Acts as a molecular scaffold that plays a key role in the organization of the endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). SAR1A-GTP-dependent assembly of SEC16A on the ER membrane forms an organized scaffold defining an ERES. Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus (PubMed:17005010, PubMed:17192411, PubMed:17428803, PubMed:21768384, PubMed:22355596). Mediates the recruitment of MIA3/TANGO to ERES (PubMed:28442536). Regulates both conventional (ER/Golgi-dependent) and GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of CFTR to cell membrane (PubMed:28067262). Positively regulates the protein stability of E3 ubiquitin-protein ligases RNF152 and RNF183 and the ER localization of RNF183 (PubMed:29300766). Acts as a RAB10 effector in the regulation of insulin-induced SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the cell membrane in adipocytes (By similarity). {ECO:0000250|UniProtKB:E9QAT4, ECO:0000269|PubMed:17005010, ECO:0000269|PubMed:17192411, ECO:0000269|PubMed:17428803, ECO:0000269|PubMed:21768384, ECO:0000269|PubMed:22355596, ECO:0000269|PubMed:28067262, ECO:0000269|PubMed:28442536, ECO:0000269|PubMed:29300766}.
|
Homo sapiens (Human)
|
O15031
|
PLXB2_HUMAN
|
MALQLWALTLLGLLGAGASLRPRKLDFFRSEKELNHLAVDEASGVVYLGAVNALYQLDAKLQLEQQVATGPALDNKKCTPPIEASQCHEAEMTDNVNQLLLLDPPRKRLVECGSLFKGICALRALSNISLRLFYEDGSGEKSFVASNDEGVATVGLVSSTGPGGDRVLFVGKGNGPHDNGIIVSTRLLDRTDSREAFEAYTDHATYKAGYLSTNTQQFVAAFEDGPYVFFVFNQQDKHPARNRTLLARMCREDPNYYSYLEMDLQCRDPDIHAAAFGTCLAASVAAPGSGRVLYAVFSRDSRSSGGPGAGLCLFPLDKVHAKMEANRNACYTGTREARDIFYKPFHGDIQCGGHAPGSSKSFPCGSEHLPYPLGSRDGLRGTAVLQRGGLNLTAVTVAAENNHTVAFLGTSDGRILKVYLTPDGTSSEYDSILVEINKRVKRDLVLSGDLGSLYAMTQDKVFRLPVQECLSYPTCTQCRDSQDPYCGWCVVEGRCTRKAECPRAEEASHWLWSRSKSCVAVTSAQPQNMSRRAQGEVQLTVSPLPALSEEDELLCLFGESPPHPARVEGEAVICNSPSSIPVTPPGQDHVAVTIQLLLRRGNIFLTSYQYPFYDCRQAMSLEENLPCISCVSNRWTCQWDLRYHECREASPNPEDGIVRAHMEDSCPQFLGPSPLVIPMNHETDVNFQGKNLDTVKGSSLHVGSDLLKFMEPVTMQESGTFAFRTPKLSHDANETLPLHLYVKSYGKNIDSKLHVTLYNCSFGRSDCSLCRAANPDYRCAWCGGQSRCVYEALCNTTSECPPPVITRIQPETGPLGGGIRITILGSNLGVQAGDIQRISVAGRNCSFQPERYSVSTRIVCVIEAAETPFTGGVEVDVFGKLGRSPPNVQFTFQQPKPLSVEPQQGPQAGGTTLTIHGTHLDTGSQEDVRVTLNGVPCKVTKFGAQLQCVTGPQATRGQMLLEVSYGGSPVPNPGIFFTYRENPVLRAFEPLRSFASGGRSINVTGQGFSLIQRFAMVVIAEPLQSWQPPREAESLQPMTVVGTDYVFHNDTKVVFLSPAVPEEPEAYNLTVLIEMDGHRALLRTEAGAFEYVPDPTFENFTGGVKKQVNKLIHARGTNLNKAMTLQEAEAFVGAERCTMKTLTETDLYCEPPEVQPPPKRRQKRDTTHNLPEFIVKFGSREWVLGRVEYDTRVSDVPLSLILPLVIVPMVVVIAVSVYCYWRKSQQAEREYEKIKSQLEGLEESVRDRCKKEFTDLMIEMEDQTNDVHEAGIPVLDYKTYTDRVFFLPSKDGDKDVMITGKLDIPEPRRPVVEQALYQFSNLLNSKSFLINFIHTLENQREFSARAKVYFASLLTVALHGKLEYYTDIMHTLFLELLEQYVVAKNPKLMLRRSETVVERMLSNWMSICLYQYLKDSAGEPLYKLFKAIKHQVEKGPVDAVQKKAKYTLNDTGLLGDDVEYAPLTVSVIVQDEGVDAIPVKVLNCDTISQVKEKIIDQVYRGQPCSCWPRPDSVVLEWRPGSTAQILSDLDLTSQREGRWKRVNTLMHYNVRDGATLILSKVGVSQQPEDSQQDLPGERHALLEEENRVWHLVRPTDEVDEGKSKRGSVKEKERTKAITEIYLTRLLSVKGTLQQFVDNFFQSVLAPGHAVPPAVKYFFDFLDEQAEKHNIQDEDTIHIWKTNSLPLRFWVNILKNPHFIFDVHVHEVVDASLSVIAQTFMDACTRTEHKLSRDSPSNKLLYAKEISTYKKMVEDYYKGIRQMVQVSDQDMNTHLAEISRAHTDSLNTLVALHQLYQYTQKYYDEIINALEEDPAAQKMQLAFRLQQIAAALENKVTDL
| null | null |
brain development [GO:0007420]; excitatory synapse assembly [GO:1904861]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; negative regulation of cell adhesion [GO:0007162]; neural tube closure [GO:0001843]; neuroblast proliferation [GO:0007405]; positive regulation of axonogenesis [GO:0050772]; positive regulation of neuron projection development [GO:0010976]; positive regulation of translation [GO:0045727]; regulation of cell migration [GO:0030334]; regulation of cell shape [GO:0008360]; regulation of GTPase activity [GO:0043087]; regulation of neuron migration [GO:2001222]; regulation of protein phosphorylation [GO:0001932]; semaphorin-plexin signaling pathway [GO:0071526]; semaphorin-plexin signaling pathway involved in axon guidance [GO:1902287]
|
cell surface [GO:0009986]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]; semaphorin receptor complex [GO:0002116]
|
semaphorin receptor activity [GO:0017154]
|
PF08337;PF20170;PF01437;PF01403;PF01833;PF17960;
|
2.60.40.10;2.130.10.10;
|
Plexin family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12533544}; Single-pass type I membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Cell surface receptor for SEMA4C, SEMA4D and SEMA4G that plays an important role in cell-cell signaling (By similarity). Plays a role in glutamatergic synapse development and is required for SEMA4A-mediated excitatory synapse development (By similarity). Binding to class 4 semaphorins promotes downstream activation of RHOA and phosphorylation of ERBB2 at 'Tyr-1248' (By similarity). Required for normal differentiation and migration of neuronal cells during brain corticogenesis and for normal embryonic brain development (By similarity). Regulates the migration of cerebellar granule cells in the developing brain (By similarity). Plays a role in RHOA activation and subsequent changes of the actin cytoskeleton (PubMed:12183458). Plays a role in axon guidance, invasive growth and cell migration (PubMed:15184888). May modulate the activity of RAC1 and CDC42 (By similarity). {ECO:0000250|UniProtKB:B2RXS4, ECO:0000269|PubMed:12183458, ECO:0000269|PubMed:15184888}.
|
Homo sapiens (Human)
|
Subsets and Splits
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