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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O43169
|
CYB5B_HUMAN
|
MSGSMATAEASGSDGKGQEVETSVTYYRLEEVAKRNSLKELWLVIHGRVYDVTRFLNEHPGGEEVLLEQAGVDASESFEDVGHSSDAREMLKQYYIGDIHPSDLKPESGSKDPSKNDTCKSCWAYWILPIIGAVLLGFLYRYYTSESKSS
| null | null |
nitric oxide biosynthetic process [GO:0006809]; response to oxidative stress [GO:0006979]; xenobiotic metabolic process [GO:0006805]
|
endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; nitric-oxide synthase complex [GO:1903958]
|
enzyme activator activity [GO:0008047]; heme binding [GO:0020037]; metal ion binding [GO:0046872]
|
PF00173;
|
3.10.120.10;
|
Cytochrome b5 family
| null |
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P04166}.
| null | null | null | null | null |
FUNCTION: Cytochrome b5 is a membrane-bound hemoprotein functioning as an electron carrier for several membrane-bound oxygenases. {ECO:0000250}.
|
Homo sapiens (Human)
|
O43172
|
PRP4_HUMAN
|
MASSRASSTQATKTKAPDDLVAPVVKKPHIYYGSLEEKERERLAKGESGILGKDGLKAGIEAGNINITSGEVFEIEEHISERQAEVLAEFERRKRARQINVSTDDSEVKACLRALGEPITLFGEGPAERRERLRNILSVVGTDALKKTKKDDEKSKKSKEEYQQTWYHEGPNSLKVARLWIANYSLPRAMKRLEEARLHKEIPETTRTSQMQELHKSLRSLNNFCSQIGDDRPISYCHFSPNSKMLATACWSGLCKLWSVPDCNLLHTLRGHNTNVGAIVFHPKSTVSLDPKDVNLASCAADGSVKLWSLDSDEPVADIEGHTVRVARVMWHPSGRFLGTTCYDRSWRLWDLEAQEEILHQEGHSMGVYDIAFHQDGSLAGTGGLDAFGRVWDLRTGRCIMFLEGHLKEIYGINFSPNGYHIATGSGDNTCKVWDLRQRRCVYTIPAHQNLVTGVKFEPIHGNFLLTGAYDNTAKIWTHPGWSPLKTLAGHEGKVMGLDISSDGQLIATCSYDRTFKLWMAE
| null | null |
mRNA splicing, via spliceosome [GO:0000398]; RNA processing [GO:0006396]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]
|
Cajal body [GO:0015030]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]; spliceosomal snRNP complex [GO:0097525]; U2-type precatalytic spliceosome [GO:0071005]; U4/U6 snRNP [GO:0071001]; U4/U6 x U5 tri-snRNP complex [GO:0046540]
|
U4 snRNA binding [GO:0030621]; U6 snRNA binding [GO:0017070]
|
PF08799;PF00400;
|
4.10.280.110;2.130.10.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25383878, ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:9257651, ECO:0000269|PubMed:9328476, ECO:0000269|PubMed:9404889}. Nucleus speckle {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Plays a role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). {ECO:0000269|PubMed:25383878, ECO:0000269|PubMed:28781166}.
|
Homo sapiens (Human)
|
O43173
|
SIA8C_HUMAN
|
MRNCKMARVASVLGLVMLSVALLILSLISYVSLKKENIFTTPKYASPGAPRMYMFHAGFRSQFALKFLDPSFVPITNSLTQELQEKPSKWKFNRTAFLHQRQEILQHVDVIKNFSLTKNSVRIGQLMHYDYSSHKYVFSISNNFRSLLPDVSPIMNKHYNICAVVGNSGILTGSQCGQEIDKSDFVFRCNFAPTEAFQRDVGRKTNLTTFNPSILEKYYNNLLTIQDRNNFFLSLKKLDGAILWIPAFFFHTSATVTRTLVDFFVEHRGQLKVQLAWPGNIMQHVNRYWKNKHLSPKRLSTGILMYTLASAICEEIHLYGFWPFGFDPNTREDLPYHYYDKKGTKFTTKWQESHQLPAEFQLLYRMHGEGLTKLTLSHCA
|
2.4.3.-; 2.4.3.8
| null |
ganglioside biosynthetic process [GO:0001574]; glycoprotein metabolic process [GO:0009100]; glycosphingolipid biosynthetic process [GO:0006688]; N-glycan processing [GO:0006491]; oligosaccharide metabolic process [GO:0009311]; protein glycosylation [GO:0006486]; sialylation [GO:0097503]
|
Golgi membrane [GO:0000139]
|
alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity [GO:0003828]; identical protein binding [GO:0042802]; sialic acid binding [GO:0033691]
|
PF00777;
|
3.90.1480.20;
|
Glycosyltransferase 29 family
|
PTM: Autopolysialylated. {ECO:0000269|PubMed:10766765}.
|
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305|PubMed:10766765}; Single-pass type II membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=[N-acetyl-alpha-D-neuraminosyl-(2->8)](n) + CMP-N-acetyl-beta-neuraminate = [N-acetyl-alpha-D-neuraminosyl-(2->8)](n+1) + CMP + H(+); Xref=Rhea:RHEA:77367, Rhea:RHEA-COMP:14315, Rhea:RHEA-COMP:18878, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:139252; Evidence={ECO:0000269|PubMed:10766765, ECO:0000269|PubMed:9826427}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77368; Evidence={ECO:0000269|PubMed:10766765, ECO:0000269|PubMed:9826427}; CATALYTIC ACTIVITY: Reaction=alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-6S-D-GlcNAc + CMP-N-acetyl-beta-neuraminate = alpha-Neu5Ac-(2->8)-alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-6S-D-GlcNAc + CMP + H(+); Xref=Rhea:RHEA:77391, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:197339, ChEBI:CHEBI:197340; Evidence={ECO:0000269|PubMed:26192331}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77392; Evidence={ECO:0000269|PubMed:26192331}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM3 (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate = a ganglioside GD3 (d18:1(4E)) + CMP + H(+); Xref=Rhea:RHEA:41760, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60065, ChEBI:CHEBI:60377, ChEBI:CHEBI:78436; Evidence={ECO:0000250|UniProtKB:Q64689}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41761; Evidence={ECO:0000250|UniProtKB:Q64689}; CATALYTIC ACTIVITY: Reaction=a ganglioside GM3 + CMP-N-acetyl-beta-neuraminate = a ganglioside GD3 + CMP + H(+); Xref=Rhea:RHEA:48288, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:79210, ChEBI:CHEBI:79214; Evidence={ECO:0000250|UniProtKB:Q64689}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48289; Evidence={ECO:0000250|UniProtKB:Q64689}; CATALYTIC ACTIVITY: Reaction=an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-neuraminyl-(2->8)-N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl derivative + CMP + H(+); Xref=Rhea:RHEA:19313, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:140308, ChEBI:CHEBI:140309; EC=2.4.3.8; Evidence={ECO:0000250|UniProtKB:Q64689}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19314; Evidence={ECO:0000250|UniProtKB:Q64689}; CATALYTIC ACTIVITY: Reaction=an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + CMP-N-acetyl-beta-neuraminate = an alpha-Neu5Ac-(2->8)-alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc derivative + CMP + H(+); Xref=Rhea:RHEA:77387, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:136545, ChEBI:CHEBI:197334; Evidence={ECO:0000250|UniProtKB:Q64689}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77388; Evidence={ECO:0000250|UniProtKB:Q64689};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=30 mM for N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-D-glucose (with a constant CMP-Neu5Ac concentration of 1 mM) {ECO:0000269|PubMed:26192331}; KM=2.6 mM for 3'-sialyl-N-acetyllactosamine-6-sulfate (with a constant CMP-Neu5Ac concentration of 1 mM) {ECO:0000269|PubMed:26192331}; KM=0.21 mM for CMP-Neu5Ac (with a constant 3-sialyl-N-acetyllactosamine-6-sulfate concentration of 10 mM) {ECO:0000269|PubMed:26192331};
|
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:9826427, ECO:0000305|PubMed:10766765, ECO:0000305|PubMed:26192331}.
| null | null |
FUNCTION: Catalyzes the transfer of sialic acid from a CMP-linked sialic acid donor onto a terminal alpha-2,3-, alpha-2,6-, or alpha-2,8-linked sialic acid of an acceptor, such as N-linked oligosaccharides of glycoproteins and glycolipids through alpha-2,8-linkages (PubMed:10766765, PubMed:26192331, PubMed:9826427). Forms oligosialic and polysialic acid on various sialylated N-acetyllactosamine oligosaccharides of glycoproteins, including FETUB N-glycans, a2-HS-glycoprotein (AHSG) and alpha 2,3-sialylated glycosphingolipids, such as alpha 2,3-sialylparagloboside and ganglioside GM3 and to a lesser extent NCAM1 N-glycans (PubMed:10766765, PubMed:9826427). However, it is much more specific to N-linked oligosaccharides of glycoproteins than glycosphingolipids (By similarity). 2,3-sialylparagloboside serves as the best acceptor substrate among the glycolipids (By similarity). alpha-Neu5Ac-(2->8)-alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-6S-D-GlcNAc and monosialyl and disialyl N-acetyllactosamines are the best acceptor substrates among glycoproteins (PubMed:10766765, PubMed:26192331). May plays critical role in the striatum by mediating the formation of disialylated and trisialylated terminal glycotopes on N- and O-glycans of specific striatal proteins, regulating their distribution in lipid rafts, affecting their interaction with other binding partners, and subsequently modulating striatal functions (By similarity). {ECO:0000250|UniProtKB:Q64689, ECO:0000269|PubMed:10766765, ECO:0000269|PubMed:26192331, ECO:0000269|PubMed:9826427}.
|
Homo sapiens (Human)
|
O43174
|
CP26A_HUMAN
|
MGLPALLASALCTFVLPLLLFLAAIKLWDLYCVSGRDRSCALPLPPGTMGFPFFGETLQMVLQRRKFLQMKRRKYGFIYKTHLFGRPTVRVMGADNVRRILLGEHRLVSVHWPASVRTILGSGCLSNLHDSSHKQRKKVIMRAFSREALECYVPVITEEVGSSLEQWLSCGERGLLVYPEVKRLMFRIAMRILLGCEPQLAGDGDSEQQLVEAFEEMTRNLFSLPIDVPFSGLYRGMKARNLIHARIEQNIRAKICGLRASEAGQGCKDALQLLIEHSWERGERLDMQALKQSSTELLFGGHETTASAATSLITYLGLYPHVLQKVREELKSKGLLCKSNQDNKLDMEILEQLKYIGCVIKETLRLNPPVPGGFRVALKTFELNGYQIPKGWNVIYSICDTHDVAEIFTNKEEFNPDRFMLPHPEDASRFSFIPFGGGLRSCVGKEFAKILLKIFTVELARHCDWQLLNGPPTMKTSPTVYPVDNLPARFTHFHGEI
|
1.14.13.-
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
|
kidney development [GO:0001822]; negative regulation of retinoic acid receptor signaling pathway [GO:0048387]; response to retinoic acid [GO:0032526]; response to vitamin A [GO:0033189]; retinoic acid catabolic process [GO:0034653]; retinoic acid metabolic process [GO:0042573]; sterol metabolic process [GO:0016125]; vitamin metabolic process [GO:0006766]; xenobiotic metabolic process [GO:0006805]
|
endoplasmic reticulum membrane [GO:0005789]
|
all-trans retinoic acid 18-hydroxylase activity [GO:0062183]; all-trans retinoic acid 4-hydrolase activity [GO:0062182]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen [GO:0016709]; oxygen binding [GO:0019825]; retinoic acid 4-hydroxylase activity [GO:0008401]; retinoic acid binding [GO:0001972]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:9716180}; Peripheral membrane protein. Microsome membrane {ECO:0000269|PubMed:9716180}; Peripheral membrane protein.
|
CATALYTIC ACTIVITY: Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-(4S)-hydroxyretinoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51492, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:35291, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:134185; Evidence={ECO:0000269|PubMed:22020119}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51493; Evidence={ECO:0000305|PubMed:22020119}; CATALYTIC ACTIVITY: Reaction=all-trans-(4S)-hydroxyretinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-(4S,16)-dihydroxyretinoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51632, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:134185, ChEBI:CHEBI:134233; Evidence={ECO:0000269|PubMed:22020119}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51633; Evidence={ECO:0000305|PubMed:22020119}; CATALYTIC ACTIVITY: Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-18-hydroxyretinoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:55856, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:35291, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:139258; Evidence={ECO:0000269|PubMed:22020119}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55857; Evidence={ECO:0000305|PubMed:22020119};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=50.1 nM for all-trans-retinoate (4-hydroxylation) {ECO:0000269|PubMed:22020119}; KM=48.9 nM for all-trans-retinoate (18-hydroxylation) {ECO:0000269|PubMed:22020119}; KM=0.24 uM for tazarotenic acid (tazarotenic acid sulfoxide formation) {ECO:0000269|PubMed:26937021}; KM=0.39 uM for tazarotenic acid (hydroxytazarotenic acid formation) {ECO:0000269|PubMed:26937021}; Vmax=9.5 pmol/min/pmol enzyme toward all-trans-retinoate (4-hydroxylation) {ECO:0000269|PubMed:22020119}; Vmax=5 pmol/min/pmol enzyme toward all-trans-retinoate (18-hydroxylation) {ECO:0000269|PubMed:22020119};
| null | null | null |
FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of retinoates (RAs), the active metabolites of vitamin A, and critical signaling molecules in animals (PubMed:22020119, PubMed:9228017, PubMed:9716180). RAs exist as at least four different isomers: all-trans-RA (atRA), 9-cis-RA, 13-cis-RA, and 9,13-dicis-RA, where atRA is considered to be the biologically active isomer, although 9-cis-RA and 13-cis-RA also have activity (Probable). Catalyzes the hydroxylation of atRA primarily at C-4 and C-18, thereby contributing to the regulation of atRA homeostasis and signaling (PubMed:22020119, PubMed:9228017, PubMed:9716180). Hydroxylation of atRA limits its biological activity and initiates a degradative process leading to its eventual elimination (Probable). Involved in the convertion of atRA to all-trans-4-oxo-RA. Able to metabolize other RAs such as 9-cis, 13-cis and 9,13-di-cis RA (By similarity) (PubMed:9228017). Can oxidize all-trans-13,14-dihydroretinoate (DRA) to metabolites which could include all-trans-4-oxo-DRA, all-trans-4-hydroxy-DRA, all-trans-5,8-epoxy-DRA, and all-trans-18-hydroxy-DRA (By similarity). May play a role in the oxidative metabolism of xenobiotics such as tazarotenic acid (PubMed:26937021). {ECO:0000250|UniProtKB:O55127, ECO:0000269|PubMed:22020119, ECO:0000269|PubMed:26937021, ECO:0000269|PubMed:9228017, ECO:0000269|PubMed:9716180, ECO:0000305|PubMed:22020119, ECO:0000305|PubMed:9228017}.
|
Homo sapiens (Human)
|
O43175
|
SERA_HUMAN
|
MAFANLRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLEAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQSFGMKTIGYDPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGALLRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMVKGKSLTGVVNAQALTSAFSPHTKPWIGLAEALGTLMRAWAGSPKGTIQVITQGTSLKNAGNCLSPAVIVGLLKEASKQADVNLVNAKLLVKEAGLNVTTSHSPAAPGEQGFGECLLAVALAGAPYQAVGLVQGTTPVLQGLNGAVFRPEVPLRRDLPLLLFRTQTSDPAMLPTMIGLLAEAGVRLLSYQTSLVSDGETWHVMGISSLLPSLEAWKQHVTEAFQFHF
|
1.1.1.37; 1.1.1.399; 1.1.1.95
| null |
brain development [GO:0007420]; G1 to G0 transition [GO:0070314]; gamma-aminobutyric acid metabolic process [GO:0009448]; glial cell development [GO:0021782]; glutamine metabolic process [GO:0006541]; glycine metabolic process [GO:0006544]; L-serine biosynthetic process [GO:0006564]; neural tube development [GO:0021915]; neuron projection development [GO:0031175]; regulation of gene expression [GO:0010468]; spinal cord development [GO:0021510]; taurine metabolic process [GO:0019530]; threonine metabolic process [GO:0006566]
|
cytosol [GO:0005829]; extracellular exosome [GO:0070062]
|
electron transfer activity [GO:0009055]; L-malate dehydrogenase activity [GO:0030060]; NAD binding [GO:0051287]; phosphoglycerate dehydrogenase activity [GO:0004617]
|
PF00389;PF02826;PF19304;
|
3.40.50.720;
|
D-isomer specific 2-hydroxyacid dehydrogenase family
| null | null |
CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378, ChEBI:CHEBI:18110, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58272; EC=1.1.1.95; Evidence={ECO:0000269|PubMed:11751922}; CATALYTIC ACTIVITY: Reaction=(R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + H(+) + NADH; Xref=Rhea:RHEA:49612, ChEBI:CHEBI:15378, ChEBI:CHEBI:15801, ChEBI:CHEBI:16810, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.399; Evidence={ECO:0000269|PubMed:25406093}; CATALYTIC ACTIVITY: Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate; Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37; Evidence={ECO:0000269|PubMed:25406093};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=21.6 uM for 3-phosphonooxypyruvate {ECO:0000269|PubMed:19235232}; KM=0.26 mM for 3-phosphoglycerate {ECO:0000269|PubMed:25406093}; KM=6.5 mM for oxaloacetate {ECO:0000269|PubMed:25406093}; KM=10.1 mM for 2-oxoglutarate {ECO:0000269|PubMed:25406093}; KM=22 uM for NAD(+) {ECO:0000269|PubMed:25406093}; KM=4 uM for NADH {ECO:0000269|PubMed:25406093}; Vmax=35 nmol/min/mg enzyme with 3-phosphohydroxypyruvate as substrate (in patient-derived fibroblasts) {ECO:0000269|PubMed:19235232}; Vmax=168 nmol/min/mg enzyme with 3-phosphohydroxypyruvate as substrate (in 3-PGDH overexpressed cells) {ECO:0000269|PubMed:19235232}; Note=kcat is 4.5 min(-1) for 3-phosphoglycerate oxidation. kcat is 10.6 min(-1) for oxaloacetate reduction. kcat is 4.7 min(-1) for 2-oxoglutarate reduction. {ECO:0000269|PubMed:25406093};
|
PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3.
| null | null |
FUNCTION: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate and the reversible oxidation of (S)-malate to oxaloacetate. {ECO:0000269|PubMed:11751922, ECO:0000269|PubMed:25406093}.
|
Homo sapiens (Human)
|
O43181
|
NDUS4_HUMAN
|
MAAVSMSVVLRQTLWRRRAVAVAALSVSRVPTRSLRTSTWRLAQDQTQDTQLITVDEKLDITTLTGVPEEHIKTRKVRIFVPARNNMQSGVNNTKKWKMEFDTRERWENPLMGWASTADPLSNMVLTFSTKEDAVSFAEKNGWSYDIEERKVPKPKSKSYGANFSWNKRTRVSTK
| null | null |
aerobic respiration [GO:0009060]; brain development [GO:0007420]; cellular respiration [GO:0045333]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; positive regulation of fibroblast proliferation [GO:0048146]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]; reactive oxygen species metabolic process [GO:0072593]; regulation of protein phosphorylation [GO:0001932]; response to cAMP [GO:0051591]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
|
PF04800;
|
3.30.160.190;
|
Complex I NDUFS4 subunit family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:11181577, ECO:0000269|PubMed:12611891, ECO:0000269|PubMed:31206022}; Peripheral membrane protein {ECO:0000269|PubMed:12611891}; Matrix side {ECO:0000269|PubMed:12611891}. Note=The interaction with BCAP31 mediates mitochondria localization. {ECO:0000269|PubMed:31206022}.
| null | null | null | null | null |
FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000269|PubMed:11181577, ECO:0000269|PubMed:12611891, ECO:0000269|PubMed:9463323}.
|
Homo sapiens (Human)
|
O43182
|
RHG06_HUMAN
|
MSAQSLLHSVFSCSSPASSSAASAKGFSKRKLRQTRSLDPALIGGCGSDEAGAEGSARGATAGRLYSPSLPAESLGPRLASSSRGPPPRATRLPPPGPLCSSFSTPSTPQEKSPSGSFHFDYEVPLGRGGLKKSMAWDLPSVLAGPASSRSASSILCSSGGGPNGIFASPRRWLQQRKFQSPPDSRGHPYVVWKSEGDFTWNSMSGRSVRLRSVPIQSLSELERARLQEVAFYQLQQDCDLSCQITIPKDGQKRKKSLRKKLDSLGKEKNKDKEFIPQAFGMPLSQVIANDRAYKLKQDLQRDEQKDASDFVASLLPFGNKRQNKELSSSNSSLSSTSETPNESTSPNTPEPAPRARRRGAMSVDSITDLDDNQSRLLEALQLSLPAEAQSKKEKARDKKLSLNPIYRQVPRLVDSCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVSLEEEHSVHDVAALLKEFLRDMPDPLLTRELYTAFINTLLLEPEEQLGTLQLLIYLLPPCNCDTLHRLLQFLSIVARHADDNISKDGQEVTGNKMTSLNLATIFGPNLLHKQKSSDKEFSVQSSARAEESTAIIAVVQKMIENYEALFMVPPDLQNEVLISLLETDPDVVDYLLRRKASQSSSPDMLQSEVSFSVGGRHSSTDSNKASSGDISPYDNNSPVLSERSLLAMQEDAAPGGSEKLYRVPGQFMLVGHLSSSKSRESSPGPRLGKDLSEEPFDIWGTWHSTLKSGSKDPGMTGSSGDIFESSSLRAGPCSLSQGNLSPNWPRWQGSPAELDSDTQGARRTQAAAPATEGRAHPAVSRACSTPHVQVAGKAERPTARSEQYLTLSGAHDLSESELDVAGLQSRATPQCQRPHGSGRDDKRPPPPYPGPGKPAAAAAWIQGPPEGVETPTDQGGQAAEREQQVTQKKLSSANSLPAGEQDSPRLGDAGWLDWQRERWQIWELLSTDNPDALPETLV
| null | null |
actin filament polymerization [GO:0030041]; activation of phospholipase C activity [GO:0007202]; focal adhesion assembly [GO:0048041]; negative regulation of focal adhesion assembly [GO:0051895]; negative regulation of stress fiber assembly [GO:0051497]; positive regulation of phospholipase activity [GO:0010518]; regulation of small GTPase mediated signal transduction [GO:0051056]; Rho protein signal transduction [GO:0007266]
|
actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
GTPase activator activity [GO:0005096]; phospholipase activator activity [GO:0016004]; phospholipase binding [GO:0043274]; SH3 domain binding [GO:0017124]
|
PF00620;
|
1.10.555.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10699171}.
| null | null | null | null | null |
FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Could regulate the interactions of signaling molecules with the actin cytoskeleton. Promotes continuous elongation of cytoplasmic processes during cell motility and simultaneous retraction of the cell body changing the cell morphology. {ECO:0000269|PubMed:10699171}.
|
Homo sapiens (Human)
|
O43184
|
ADA12_HUMAN
|
MAARPLPVSPARALLLALAGALLAPCEARGVSLWNQGRADEVVSASVGSGDLWIPVKSFDSKNHPEVLNIRLQRESKELIINLERNEGLIASSFTETHYLQDGTDVSLARNYTVILGHCYYHGHVRGYSDSAVSLSTCSGLRGLIVFENESYVLEPMKSATNRYKLFPAKKLKSVRGSCGSHHNTPNLAAKNVFPPPSQTWARRHKRETLKATKYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNIRIVLVGVEVWNDMDKCSVSQDPFTSLHEFLDWRKMKLLPRKSHDNAQLVSGVYFQGTTIGMAPIMSMCTADQSGGIVMDHSDNPLGAAVTLAHELGHNFGMNHDTLDRGCSCQMAVEKGGCIMNASTGYPFPMVFSSCSRKDLETSLEKGMGVCLFNLPEVRESFGGQKCGNRFVEEGEECDCGEPEECMNRCCNATTCTLKPDAVCAHGLCCEDCQLKPAGTACRDSSNSCDLPEFCTGASPHCPANVYLHDGHSCQDVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGDPYGNCGKVSKSSFAKCEMRDAKCGKIQCQGGASRPVIGTNAVSIETNIPLQQGGRILCRGTHVYLGDDMPDPGLVLAGTKCADGKICLNRQCQNISVFGVHECAMQCHGRGVCNNRKNCHCEAHWAPPFCDKFGFGGSTDSGPIRQADNQGLTIGILVTILCLLAAGFVVYLKRKTLIRLLFTNKKTTIEKLRCVRPSRPPRGFQPCQAHLGHLGKGLMRKPPDSYPPKDNPRRLLQCQNVDISRPLNGLNVPQPQSTQRVLPPLHRAPRAPSVPARPLPAKPALRQAQGTCKPNPPQKPLPADPLARTTRLTHALARTPGQWETGLRLAPLRPAPQYPHQVPRSTHTAYIK
|
3.4.24.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.;
|
cell adhesion [GO:0007155]; myoblast fusion [GO:0007520]; positive regulation of angiogenesis [GO:0045766]; proteolysis [GO:0006508]
|
extracellular region [GO:0005576]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
|
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; SH3 domain binding [GO:0017124]
|
PF08516;PF00200;PF01562;PF01421;
|
3.40.390.10;4.10.70.10;
| null |
PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 4]: Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Involved in skeletal muscle regeneration, specifically at the onset of cell fusion. Also involved in macrophage-derived giant cells (MGC) and osteoclast formation from mononuclear precursors (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O43186
|
CRX_HUMAN
|
MMAYMNPGPHYSVNALALSGPSVDLMHQAVPYPSAPRKQRRERTTFTRSQLEELEALFAKTQYPDVYAREEVALKINLPESRVQVWFKNRRAKCRQQRQQQKQQQQPPGGQAKARPAKRKAGTSPRPSTDVCPDPLGISDSYSPPLPGPSGSPTTAVATVSIWSPASESPLPEAQRAGLVASGPSLTSAPYAMTYAPASAFCSSPSAYGSPSSYFSGLDPYLSPMVPQLGGPALSPLSGPSVGPSLAQSPTSLSGQSYGAYSPVDSLEFKDPTGTWKFTYNPMDPLDYKDQSAWKFQIL
| null | null |
animal organ morphogenesis [GO:0009887]; cell differentiation [GO:0030154]; nervous system development [GO:0007399]; 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]; response to stimulus [GO:0050896]; visual perception [GO:0007601]
|
chromatin [GO:0000785]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]
|
DNA-binding transcription activator activity [GO:0001216]; 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]; leucine zipper domain binding [GO:0043522]; nuclear receptor binding [GO:0016922]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00046;PF03529;
|
1.10.10.60;
|
Paired homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
| null | null | null | null | null |
FUNCTION: Transcription factor that binds and transactivates the sequence 5'-TAATC[CA]-3' which is found upstream of several photoreceptor-specific genes, including the opsin genes. Acts synergistically with other transcription factors, such as NRL, RORB and RAX, to regulate photoreceptor cell-specific gene transcription. Essential for the maintenance of mammalian photoreceptors. {ECO:0000269|PubMed:10625658}.
|
Homo sapiens (Human)
|
O43187
|
IRAK2_HUMAN
|
MACYIYQLPSWVLDDLCRNMDALSEWDWMEFASYVITDLTQLRKIKSMERVQGVSITRELLWWWGMRQATVQQLVDLLCRLELYRAAQIILNWKPAPEIRCPIPAFPDSVKPEKPLAASVRKAEDEQEEGQPVRMATFPGPGSSPARAHQPAFLQPPEEDAPHSLRSDLPTSSDSKDFSTSIPKQEKLLSLAGDSLFWSEADVVQATDDFNQNRKISQGTFADVYRGHRHGKPFVFKKLRETACSSPGSIERFFQAELQICLRCCHPNVLPVLGFCAARQFHSFIYPYMANGSLQDRLQGQGGSDPLPWPQRVSICSGLLCAVEYLHGLEIIHSNVKSSNVLLDQNLTPKLAHPMAHLCPVNKRSKYTMMKTHLLRTSAAYLPEDFIRVGQLTKRVDIFSCGIVLAEVLTGIPAMDNNRSPVYLKDLLLSDIPSSTASLCSRKTGVENVMAKEICQKYLEKGAGRLPEDCAEALATAACLCLRRRNTSLQEVCGSVAAVEERLRGRETLLPWSGLSEGTGSSSNTPEETDDVDNSSLDASSSMSVAPWAGAATPLLPTENGEGRLRVIVGREADSSSEACVGLEPPQDVTETSWQIEINEAKRKLMENILLYKEEKVDSIELFGP
| null | null |
canonical NF-kappaB signal transduction [GO:0007249]; cellular response to lipopolysaccharide [GO:0071222]; inflammatory response [GO:0006954]; interleukin-1-mediated signaling pathway [GO:0070498]; intracellular signal transduction [GO:0035556]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; protein phosphorylation [GO:0006468]; regulation of cytokine-mediated signaling pathway [GO:0001959]; response to interleukin-1 [GO:0070555]; Toll signaling pathway [GO:0008063]; toll-like receptor 4 signaling pathway [GO:0034142]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome membrane [GO:0010008]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; molecular adaptor activity [GO:0060090]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; signaling adaptor activity [GO:0035591]
|
PF00531;PF00069;
|
1.10.533.10;1.10.510.10;
|
Protein kinase superfamily, TKL Ser/Thr protein kinase family, Pelle subfamily
| null | null | null | null | null | null | null |
FUNCTION: Binds to the IL-1 type I receptor following IL-1 engagement, triggering intracellular signaling cascades leading to transcriptional up-regulation and mRNA stabilization. {ECO:0000269|PubMed:10383454, ECO:0000269|PubMed:9374458}.
|
Homo sapiens (Human)
|
O43189
|
PHF1_HUMAN
|
MAQPPRLSRSGASSLWDPASPAPTSGPRPRLWEGQDVLARWTDGLLYLGTIKKVDSAREVCLVQFEDDSQFLVLWKDISPAALPGEELLCCVCRSETVVPGNRLVSCEKCRHAYHQDCHVPRAPAPGEGEGTSWVCRQCVFAIATKRGGALKKGPYARAMLGMKLSLPYGLKGLDWDAGHLSNRQQSYCYCGGPGEWNLKMLQCRSCLQWFHEACTQCLSKPLLYGDRFYEFECCVCRGGPEKVRRLQLRWVDVAHLVLYHLSVCCKKKYFDFDREILPFTSENWDSLLLGELSDTPKGERSSRLLSALNSHKDRFISGREIKKRKCLFGLHARMPPPVEPPTGDGALTSFPSGQGPGGGVSRPLGKRRRPEPEPLRRRQKGKVEELGPPSAVRNQPEPQEQRERAHLQRALQASVSPPSPSPNQSYQGSSGYNFRPTDARCLPSSPIRMFASFHPSASTAGTSGDSGPPDRSPLELHIGFPTDIPKSAPHSMTASSSSVSSPSPGLPRRSAPPSPLCRSLSPGTGGGVRGGVGYLSRGDPVRVLARRVRPDGSVQYLVEWGGGGIF
| null | null |
chromatin organization [GO:0006325]; DNA repair-dependent chromatin remodeling [GO:0140861]; regulation of DNA-templated transcription [GO:0006355]
|
centrosome [GO:0005813]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of double-strand break [GO:0035861]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; histone methyltransferase binding [GO:1990226]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; methylated histone binding [GO:0035064]; transcription corepressor binding [GO:0001222]
|
PF14061;PF00628;PF18104;
|
2.30.30.140;3.90.980.20;3.30.40.10;
|
Polycomblike family
| null |
SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Localizes specifically to the promoters of numerous target genes. Localizes to double-strand breaks (DSBs) sites following DNA damage. Co-localizes with NEK6 in the centrosome.
| null | null | null | null | null |
FUNCTION: Polycomb group (PcG) that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex. Involved in DNA damage response and is recruited at double-strand breaks (DSBs). Acts by binding to H3K36me3, a mark for transcriptional activation, and recruiting the PRC2 complex: it is however unclear whether recruitment of the PRC2 complex to H3K36me3 leads to enhance or inhibit H3K27me3 methylation mediated by the PRC2 complex. According to some reports, PRC2 recruitment by PHF1 promotes H3K27me3 and subsequent gene silencing by inducing spreading of PRC2 and H3K27me3 into H3K36me3 loci (PubMed:18285464, PubMed:23273982). According to another report, PHF1 recruits the PRC2 complex at double-strand breaks (DSBs) and inhibits the activity of PRC2 (PubMed:23142980). Regulates p53/TP53 stability and prolonges its turnover: may act by specifically binding to a methylated from of p53/TP53. {ECO:0000269|PubMed:18086877, ECO:0000269|PubMed:18285464, ECO:0000269|PubMed:18385154, ECO:0000269|PubMed:23142980, ECO:0000269|PubMed:23150668, ECO:0000269|PubMed:23273982}.
|
Homo sapiens (Human)
|
O43193
|
MTLR_HUMAN
|
MGSPWNGSDGPEGAREPPWPALPPCDERRCSPFPLGALVPVTAVCLCLFVVGVSGNVVTVMLIGRYRDMRTTTNLYLGSMAVSDLLILLGLPFDLYRLWRSRPWVFGPLLCRLSLYVGEGCTYATLLHMTALSVERYLAICRPLRARVLVTRRRVRALIAVLWAVALLSAGPFLFLVGVEQDPGISVVPGLNGTARIASSPLASSPPLWLSRAPPPSPPSGPETAEAAALFSRECRPSPAQLGALRVMLWVTTAYFFLPFLCLSILYGLIGRELWSSRRPLRGPAASGRERGHRQTVRVLLVVVLAFIICWLPFHVGRIIYINTEDSRMMYFSQYFNIVALQLFYLSASINPILYNLISKKYRAAAFKLLLARKSRPRGFHRSRDTAGEVAGDTGGDTVGYTETSANVKTMG
| null | null |
G protein-coupled receptor signaling pathway [GO:0007186]
|
cytosol [GO:0005829]; plasma membrane [GO:0005886]
|
G protein-coupled peptide receptor activity [GO:0008528]; hormone binding [GO:0042562]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Receptor for motilin. {ECO:0000269|PubMed:11322507}.
|
Homo sapiens (Human)
|
O43194
|
GPR39_HUMAN
|
MASPSLPGSDCSQIIDHSHVPEFEVATWIKITLILVYLIIFVMGLLGNSATIRVTQVLQKKGYLQKEVTDHMVSLACSDILVFLIGMPMEFYSIIWNPLTTSSYTLSCKLHTFLFEACSYATLLHVLTLSFERYIAICHPFRYKAVSGPCQVKLLIGFVWVTSALVALPLLFAMGTEYPLVNVPSHRGLTCNRSSTRHHEQPETSNMSICTNLSSRWTVFQSSIFGAFVVYLVVLLSVAFMCWNMMQVLMKSQKGSLAGGTRPPQLRKSESEESRTARRQTIIFLRLIVVTLAVCWMPNQIRRIMAAAKPKHDWTRSYFRAYMILLPFSETFFYLSSVINPLLYTVSSQQFRRVFVQVLCCRLSLQHANHEKRLRVHAHSTTDSARFVQRPLLFASRRQSSARRTEKIFLSTFQSEAEPQSKSQSLSLESLEPNSGAKPANSAAENGFQEHEV
| null | null |
G protein-coupled receptor signaling pathway [GO:0007186]
|
plasma membrane [GO:0005886]
|
G protein-coupled receptor activity [GO:0004930]; metal ion binding [GO:0046872]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26365466}; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Zinc-sensing receptor that can sense changes in extracellular Zn(2+), mediate Zn(2+) signal transmission, and participates in the regulation of numerous physiological processes including glucose homeostasis regulation, gastrointestinal mobility, hormone secretion and cell death (PubMed:18180304). Activation by Zn(2+) in keratinocytes increases the intracellular concentration of Ca(2+) and activates the ERK/MAPK and PI3K/AKT signaling pathways leading to epithelial repair (PubMed:20522546). Plays an essential role in normal wound healing by inducing the production of cytokines including the major inflammatory cytokine IL6 via the PKC/MAPK/CEBPB pathway (By similarity). Regulates adipose tissue metabolism, especially lipolysis, and regulates the function of lipases, such as hormone-sensitive lipase and adipose triglyceride lipase (By similarity). Plays a role in the inhibition of cell death and protects against oxidative, endoplasmic reticulum and mitochondrial stress by inducing secretion of the cytoprotective pigment epithelium-derived growth factor (PEDF) and probably other protective transcripts in a GNA13/RHOA/SRE-dependent manner (PubMed:18180304). Forms dynamic heteroreceptor complexes with HTR1A and GALR1 depending on cell type or specific physiological states, resulting in signaling diversity: HTR1A-GPR39 shows additive increase in signaling along the serum response element (SRE) and NF-kappa-B pathways while GALR1 acts as an antagonist blocking SRE (PubMed:26365466). {ECO:0000250|UniProtKB:Q5U431, ECO:0000269|PubMed:18180304, ECO:0000269|PubMed:20522546, ECO:0000269|PubMed:26365466}.
|
Homo sapiens (Human)
|
O43196
|
MSH5_HUMAN
|
MASLGANPRRTPQGPRPGAASSGFPSPAPVPGPREAEEEEVEEEEELAEIHLCVLWNSGYLGIAYYDTSDSTIHFMPDAPDHESLKLLQRVLDEINPQSVVTSAKQDENMTRFLGKLASQEHREPKRPEIIFLPSVDFGLEISKQRLLSGNYSFIPDAMTATEKILFLSSIIPFDCLLTVRALGGLLKFLGRRRIGVELEDYNVSVPILGFKKFMLTHLVNIDQDTYSVLQIFKSESHPSVYKVASGLKEGLSLFGILNRCHCKWGEKLLRLWFTRPTHDLGELSSRLDVIQFFLLPQNLDMAQMLHRLLGHIKNVPLILKRMKLSHTKVSDWQVLYKTVYSALGLRDACRSLPQSIQLFRDIAQEFSDDLHHIASLIGKVVDFEGSLAENRFTVLPNIDPEIDEKKRRLMGLPSFLTEVARKELENLDSRIPSCSVIYIPLIGFLLSIPRLPSMVEASDFEINGLDFMFLSEEKLHYRSARTKELDALLGDLHCEIRDQETLLMYQLQCQVLARAAVLTRVLDLASRLDVLLALASAARDYGYSRPRYSPQVLGVRIQNGRHPLMELCARTFVPNSTECGGDKGRVKVITGPNSSGKSIYLKQVGLITFMALVGSFVPAEEAEIGAVDAIFTRIHSCESISLGLSTFMIDLNQVAKAVNNATAQSLVLIDEFGKGTNTVDGLALLAAVLRHWLARGPTCPHIFVATNFLSLVQLQLLPQGPLVQYLTMETCEDGNDLVFFYQVCEGVAKASHASHTAAQAGLPDKLVARGKEVSDLIRSGKPIKPVKDLLKKNQMENCQTLVDKFMKLDLEDPNLDLNVFMSQEVLPAATSIL
| null | null |
chiasma assembly [GO:0051026]; mismatch repair [GO:0006298]
|
nucleus [GO:0005634]
|
ATP binding [GO:0005524]; ATP-dependent DNA damage sensor activity [GO:0140664]; double-stranded DNA binding [GO:0003690]; mismatched DNA binding [GO:0030983]
|
PF05192;PF05190;PF00488;
|
1.10.1420.10;3.40.50.300;
|
DNA mismatch repair MutS family
| null | null | null | null | null | null | null |
FUNCTION: Involved in DNA mismatch repair and meiotic recombination processes. Facilitates crossovers between homologs during meiosis (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O43236
|
SEPT4_HUMAN
|
MDRSLGWQGNSVPEDRTEAGIKRFLEDTTDDGELSKFVKDFSGNASCHPPEAKTWASRPQVPEPRPQAPDLYDDDLEFRPPSRPQSSDNQQYFCAPAPLSPSARPRSPWGKLDPYDSSEDDKEYVGFATLPNQVHRKSVKKGFDFTLMVAGESGLGKSTLVNSLFLTDLYRDRKLLGAEERIMQTVEITKHAVDIEEKGVRLRLTIVDTPGFGDAVNNTECWKPVAEYIDQQFEQYFRDESGLNRKNIQDNRVHCCLYFISPFGHGLRPLDVEFMKALHQRVNIVPILAKADTLTPPEVDHKKRKIREEIEHFGIKIYQFPDCDSDEDEDFKLQDQALKESIPFAVIGSNTVVEARGRRVRGRLYPWGIVEVENPGHCDFVKLRTMLVRTHMQDLKDVTRETHYENYRAQCIQSMTRLVVKERNRNKLTRESGTDFPIPAVPPGTDPETEKLIREKDEELRRMQEMLHKIQKQMKENY
| null | null |
apoptotic process [GO:0006915]; cytoskeleton-dependent cytokinesis [GO:0061640]; flagellated sperm motility [GO:0030317]; hematopoietic stem cell homeostasis [GO:0061484]; neuron migration [GO:0001764]; positive regulation of apoptotic process [GO:0043065]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of protein ubiquitination [GO:0031398]; regulation of apoptotic process [GO:0042981]; regulation of exocytosis [GO:0017157]; spermatid differentiation [GO:0048515]
|
axon [GO:0030424]; cell division site [GO:0032153]; cytosol [GO:0005829]; dendrite [GO:0030425]; microtubule cytoskeleton [GO:0015630]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perikaryon [GO:0043204]; septin complex [GO:0031105]; septin ring [GO:0005940]; sperm annulus [GO:0097227]; synaptic vesicle [GO:0008021]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; molecular adaptor activity [GO:0060090]; structural molecule activity [GO:0005198]
|
PF00735;
|
3.40.50.300;
|
TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Septin GTPase family
|
PTM: Phosphorylated by DYRK1A. {ECO:0000250|UniProtKB:P28661}.; PTM: Ubiquitinated by AREL1. {ECO:0000269|PubMed:23479728}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28661}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:25588830}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:15116257}. Cell projection, axon {ECO:0000250|UniProtKB:P28661}. Cell projection, dendrite {ECO:0000250|UniProtKB:P28661}. Perikaryon {ECO:0000250|UniProtKB:P28661}. Synapse {ECO:0000269|PubMed:17296554}. Note=In platelets, found in areas surrounding alpha-granules (PubMed:15116257). Found in the sperm annulus, a fibrous ring structure connecting the midpiece and the principal piece of the sperm flagellum (PubMed:25588830). Expressed and colocalized with SLC6A3 and SNCA in axon terminals, especially at the varicosities (By similarity). {ECO:0000250|UniProtKB:P28661, ECO:0000269|PubMed:15116257, ECO:0000269|PubMed:25588830}.; SUBCELLULAR LOCATION: [Isoform ARTS]: Mitochondrion {ECO:0000269|PubMed:11146656, ECO:0000269|PubMed:15029247, ECO:0000269|PubMed:21695558}. Nucleus {ECO:0000269|PubMed:11146656, ECO:0000269|PubMed:15029247}. Note=While predominantly localized in the mitochondria under resting conditions, translocates into the nucleus after TGF-beta treatment and apoptosis induction. {ECO:0000269|PubMed:11146656}.
| null | null | null | null | null |
FUNCTION: Filament-forming cytoskeletal GTPase (Probable). Pro-apoptotic protein involved in LGR5-positive intestinal stem cell and Paneth cell expansion in the intestines, via its interaction with XIAP (By similarity). May also play a role in the regulation of cell fate in the intestine (By similarity). Positive regulator of apoptosis involved in hematopoietic stem cell homeostasis; via its interaction with XIAP (By similarity). Negative regulator of repair and hair follicle regeneration in response to injury, due to inhibition of hair follicle stem cell proliferation, potentially via its interaction with XIAP (By similarity). Plays an important role in male fertility and sperm motility (By similarity). During spermiogenesis, essential for the establishment of the annulus (a fibrous ring structure connecting the midpiece and the principal piece of the sperm flagellum) which is a requisite for the structural and mechanical integrity of the sperm (By similarity). Involved in the migration of cortical neurons and the formation of neuron leading processes during embryonic development (By similarity). Required for dopaminergic metabolism in presynaptic autoreceptors; potentially via activity as a presynaptic scaffold protein (By similarity). {ECO:0000250|UniProtKB:P28661, ECO:0000305}.; FUNCTION: [Isoform ARTS]: Required for the induction of cell death mediated by TGF-beta and possibly by other apoptotic stimuli (PubMed:11146656, PubMed:15837787). Induces apoptosis through binding and inhibition of XIAP resulting in significant reduction in XIAP levels, leading to caspase activation and cell death (PubMed:15029247). Mediates the interaction between BCL2 and XIAP, thereby positively regulating the ubiquitination and degradation of BCL2 and promoting apoptosis (PubMed:29020630). {ECO:0000269|PubMed:11146656, ECO:0000269|PubMed:15029247, ECO:0000269|PubMed:15837787, ECO:0000269|PubMed:29020630}.
|
Homo sapiens (Human)
|
O43237
|
DC1L2_HUMAN
|
MAPVGVEKKLLLGPNGPAVAAAGDLTSEEEEGQSLWSSILSEVSTRARSKLPSGKNILVFGEDGSGKTTLMTKLQGAEHGKKGRGLEYLYLSVHDEDRDDHTRCNVWILDGDLYHKGLLKFAVSAESLPETLVIFVADMSRPWTVMESLQKWASVLREHIDKMKIPPEKMRELERKFVKDFQDYMEPEEGCQGSPQRRGPLTSGSDEENVALPLGDNVLTHNLGIPVLVVCTKCDAVSVLEKEHDYRDEHLDFIQSHLRRFCLQYGAALIYTSVKEEKNLDLLYKYIVHKTYGFHFTTPALVVEKDAVFIPAGWDNEKKIAILHENFTTVKPEDAYEDFIVKPPVRKLVHDKELAAEDEQVFLMKQQSLLAKQPATPTRASESPARGPSGSPRTQGRGGPASVPSSSPGTSVKKPDPNIKNNAASEGVLASFFNSLLSKKTGSPGSPGAGGVQSTAKKSGQKTVLSNVQEELDRMTRKPDSMVTNSSTENEA
| null | null |
cellular response to nerve growth factor stimulus [GO:1990090]; centrosome localization [GO:0051642]; microtubule cytoskeleton organization [GO:0000226]; microtubule-based movement [GO:0007018]
|
centrosome [GO:0005813]; cytoplasmic dynein complex [GO:0005868]; cytosol [GO:0005829]; dynein complex [GO:0030286]; kinetochore [GO:0000776]; late endosome [GO:0005770]; membrane [GO:0016020]; microtubule [GO:0005874]
|
ATP binding [GO:0005524]; dynein heavy chain binding [GO:0045504]; identical protein binding [GO:0042802]
|
PF05783;
|
3.40.50.300;
|
Dynein light intermediate chain family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:36071160}.
| null | null | null | null | null |
FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes. {ECO:0000305|PubMed:36071160}.
|
Homo sapiens (Human)
|
O43240
|
KLK10_HUMAN
|
MRAPHLHLSAASGARALAKLLPLLMAQLWAAEAALLPQNDTRLDPEAYGSPCARGSQPWQVSLFNGLSFHCAGVLVDQSWVLTAAHCGNKPLWARVGDDHLLLLQGEQLRRTTRSVVHPKYHQGSGPILPRRTDEHDLMLLKLARPVVLGPRVRALQLPYRCAQPGDQCQVAGWGTTAARRVKYNKGLTCSSITILSPKECEVFYPGVVTNNMICAGLDRGQDPCQSDSGGPLVCDETLQGILSWGVYPCGSAQHPAVYTQICKYMSWINKVIRSN
|
3.4.21.-
| null |
cell cycle [GO:0007049]; proteolysis [GO:0006508]
|
extracellular region [GO:0005576]; secretory granule [GO:0030141]
|
serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family, Kallikrein subfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Has a tumor-suppressor role for NES1 in breast and prostate cancer.
|
Homo sapiens (Human)
|
O43242
|
PSMD3_HUMAN
|
MKQEGSARRRGADKAKPPPGGGEQEPPPPPAPQDVEMKEEAATGGGSTGEADGKTAAAAAEHSQRELDTVTLEDIKEHVKQLEKAVSGKEPRFVLRALRMLPSTSRRLNHYVLYKAVQGFFTSNNATRDFLLPFLEEPMDTEADLQFRPRTGKAASTPLLPEVEAYLQLLVVIFMMNSKRYKEAQKISDDLMQKISTQNRRALDLVAAKCYYYHARVYEFLDKLDVVRSFLHARLRTATLRHDADGQATLLNLLLRNYLHYSLYDQAEKLVSKSVFPEQANNNEWARYLYYTGRIKAIQLEYSEARRTMTNALRKAPQHTAVGFKQTVHKLLIVVELLLGEIPDRLQFRQPSLKRSLMPYFLLTQAVRTGNLAKFNQVLDQFGEKFQADGTYTLIIRLRHNVIKTGVRMISLSYSRISLADIAQKLQLDSPEDAEFIVAKAIRDGVIEASINHEKGYVQSKEMIDIYSTREPQLAFHQRISFCLDIHNMSVKAMRFPPKSYNKDLESAEERREREQQDLEFAKEMAEDDDDSFP
| null | null |
proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; regulation of protein catabolic process [GO:0042176]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome accessory complex [GO:0022624]; proteasome complex [GO:0000502]; proteasome regulatory particle, lid subcomplex [GO:0008541]; secretory granule lumen [GO:0034774]
|
enzyme regulator activity [GO:0030234]
|
PF01399;PF08375;
|
1.25.40.570;1.25.40.10;
|
Proteasome subunit S3 family
| null | null | null | null | null | null | null |
FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. {ECO:0000269|PubMed:1317798}.
|
Homo sapiens (Human)
|
O43248
|
HXC11_HUMAN
|
MFNSVNLGNFCSPSRKERGADFGERGSCASNLYLPSCTYYMPEFSTVSSFLPQAPSRQISYPYSAQVPPVREVSYGLEPSGKWHHRNSYSSCYAAADELMHRECLPPSTVTEILMKNEGSYGGHHHPSAPHATPAGFYSSVNKNSVLPQAFDRFFDNAYCGGGDPPAEPPCSGKGEAKGEPEAPPASGLASRAEAGAEAEAEEENTNPSSSGSAHSVAKEPAKGAAPNAPRTRKKRCPYSKFQIRELEREFFFNVYINKEKRLQLSRMLNLTDRQVKIWFQNRRMKEKKLSRDRLQYFSGNPLL
| null | null |
anterior/posterior pattern specification [GO:0009952]; embryonic digit morphogenesis [GO:0042733]; embryonic skeletal joint morphogenesis [GO:0060272]; endoderm development [GO:0007492]; metanephros development [GO:0001656]; organ induction [GO:0001759]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proximal/distal pattern formation [GO:0009954]; 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]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF12045;PF00046;
|
1.10.10.60;
|
Abd-B homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Binds to a promoter element of the lactase-phlorizin hydrolase gene.
|
Homo sapiens (Human)
|
O43251
|
RFOX2_HUMAN
|
MQNEPLTPGYHGFPARDSQGNQEPTTTPDAMVQPFTTIPFPPPPQNGIPTEYGVPHTQDYAGQTGEHNLTLYGSTQAHGEQSSNSPSTQNGSLTTEGGAQTDGQQSQTQSSENSESKSTPKRLHVSNIPFRFRDPDLRQMFGQFGKILDVEIIFNERGSKGFGFVTFENSADADRAREKLHGTVVEGRKIEVNNATARVMTNKKMVTPYANGWKLSPVVGAVYGPELYAASSFQADVSLGNDAAVPLSGRGGINTYIPLISLPLVPGFPYPTAATTAAAFRGAHLRGRGRTVYGAVRAVPPTAIPAYPGVVYQDGFYGADLYGGYAAYRYAQPATATAATAAAAAAAAYSDGYGRVYTADPYHALAPAASYGVGAVASLYRGGYSRFAPY
| null | null |
intracellular estrogen receptor signaling pathway [GO:0030520]; mRNA processing [GO:0006397]; negative regulation of DNA-templated transcription [GO:0045892]; nervous system development [GO:0007399]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of cell population proliferation [GO:0042127]; RNA metabolic process [GO:0016070]; RNA splicing [GO:0008380]
|
cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA-binding transcription factor binding [GO:0140297]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]; transcription corepressor activity [GO:0003714]
|
PF12414;PF00076;
|
3.30.70.330;
| null | null |
SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: RNA-binding protein that regulates alternative splicing events by binding to 5'-UGCAUGU-3' elements. Prevents binding of U2AF2 to the 3'-splice site. Regulates alternative splicing of tissue-specific exons and of differentially spliced exons during erythropoiesis (By similarity). RNA-binding protein that seems to act as a coregulatory factor of ER-alpha. Together with RNA binding proteins RBPMS and MBNL1/2, activates vascular smooth muscle cells alternative splicing events (PubMed:37548402). {ECO:0000250, ECO:0000269|PubMed:11875103, ECO:0000269|PubMed:37548402}.
|
Homo sapiens (Human)
|
O43252
|
PAPS1_HUMAN
|
MEIPGSLCKKVKLSNNAQNWGMQRATNVTYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGASLPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKTDSCDVNDCVQQVVELLQERDIVPVDASYEVKELYVPENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGGVINLSVPIVLTATHEDKERLDGCTAFALMYEGRRVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDRVYWNDGLDQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHALLMQDTHKQLLERGYRRPVLLLHPLGGWTKDDDVPLMWRMKQHAAVLEEGVLNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPSHGAKVLTMAPGLITLEIVPFRVAAYNKKKKRMDYYDSEHHEDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTEYYKSLEKA
|
2.7.1.25; 2.7.7.4
| null |
3'-phosphoadenosine 5'-phosphosulfate biosynthetic process [GO:0050428]; phosphorylation [GO:0016310]; skeletal system development [GO:0001501]; sulfate assimilation [GO:0000103]
|
cytosol [GO:0005829]
|
adenylylsulfate kinase activity [GO:0004020]; ATP binding [GO:0005524]; nucleotidyltransferase activity [GO:0016779]; protein homodimerization activity [GO:0042803]; sulfate adenylyltransferase (ATP) activity [GO:0004781]
|
PF01583;PF01747;PF14306;
|
3.40.50.620;3.40.50.300;3.10.400.10;
|
APS kinase family; Sulfate adenylyltransferase family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58243; EC=2.7.7.4; Evidence={ECO:0000269|PubMed:14747722, ECO:0000269|PubMed:9576487, ECO:0000269|PubMed:9648242, ECO:0000269|PubMed:9668121}; CATALYTIC ACTIVITY: Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339, ChEBI:CHEBI:456216; EC=2.7.1.25; Evidence={ECO:0000269|PubMed:14747722, ECO:0000269|PubMed:17276460, ECO:0000269|PubMed:17540769, ECO:0000269|PubMed:9576487, ECO:0000269|PubMed:9648242, ECO:0000269|PubMed:9668121};
| null |
PATHWAY: Sulfur metabolism; sulfate assimilation. {ECO:0000269|PubMed:14747722, ECO:0000269|PubMed:9576487, ECO:0000269|PubMed:9648242, ECO:0000269|PubMed:9668121}.
| null | null |
FUNCTION: Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate-activation pathway (PubMed:14747722, PubMed:9576487, PubMed:9648242, PubMed:9668121). Required for normal biosynthesis of sulfated L-selectin ligands in endothelial cells (PubMed:9576487). {ECO:0000269|PubMed:14747722, ECO:0000269|PubMed:9576487, ECO:0000269|PubMed:9648242, ECO:0000269|PubMed:9668121}.
|
Homo sapiens (Human)
|
O43255
|
SIAH2_HUMAN
|
MSRPSSTGPSANKPCSKQPPPQPQHTPSPAAPPAAATISAAGPGSSAVPAAAAVISGPGGGGGAGPVSPQHHELTSLFECPVCFDYVLPPILQCQAGHLVCNQCRQKLSCCPTCRGALTPSIRNLAMEKVASAVLFPCKYATTGCSLTLHHTEKPEHEDICEYRPYSCPCPGASCKWQGSLEAVMSHLMHAHKSITTLQGEDIVFLATDINLPGAVDWVMMQSCFGHHFMLVLEKQEKYEGHQQFFAIVLLIGTRKQAENFAYRLELNGNRRRLTWEATPRSIHDGVAAAIMNSDCLVFDTAIAHLFADNGNLGINVTISTCCP
|
2.3.2.27
| null |
amyloid fibril formation [GO:1990000]; apoptotic process [GO:0006915]; canonical Wnt signaling pathway [GO:0060070]; cell cycle [GO:0007049]; negative regulation of apoptotic process [GO:0043066]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ubiquitination [GO:0016567]; regulation of circadian rhythm [GO:0042752]; regulation of protein ubiquitination [GO:0031396]; rhythmic process [GO:0048511]; small GTPase-mediated signal transduction [GO:0007264]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; intracellular membrane-bounded organelle [GO:0043231]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]
|
transcription corepressor activity [GO:0003714]; ubiquitin conjugating enzyme binding [GO:0031624]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]
|
PF21362;PF03145;PF21361;
|
3.30.40.10;
|
SINA (Seven in absentia) family
|
PTM: Phosphorylated at Ser-28 by MAPK14, which mediates the degradation by the proteasome of EGLN3 (By similarity). Phosphorylated at Ser-28 by DYRK2; this increases the ubiquitin ligase activity and promotes degradation of EGLN3. {ECO:0000250|UniProtKB:Q06986, ECO:0000269|PubMed:22878263}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19224863, ECO:0000269|PubMed:22878263}. Nucleus {ECO:0000269|PubMed:22878263}. Note=Predominantly cytoplasmic. Partially nuclear. {ECO:0000269|PubMed:22878263}.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27;
| null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:11483518, PubMed:19224863, PubMed:9334332). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed:11483518, PubMed:19224863, PubMed:9334332). Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes (PubMed:11483518, PubMed:19224863, PubMed:9334332). Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation (GPS2, POU2AF1, PML, NCOR1), a cell surface receptor (DCC), an antiapoptotic protein (BAG1), and a protein involved in synaptic vesicle function in neurons (SYP) (PubMed:11483518, PubMed:19224863, PubMed:9334332). Mediates ubiquitination and proteasomal degradation of DYRK2 in response to hypoxia (PubMed:22878263). It is thereby involved in apoptosis, tumor suppression, cell cycle, transcription and signaling processes (PubMed:11483518, PubMed:19224863, PubMed:22878263, PubMed:9334332). Has some overlapping function with SIAH1 (PubMed:11483518, PubMed:19224863, PubMed:9334332). Triggers the ubiquitin-mediated degradation of TRAF2, whereas SIAH1 does not (PubMed:12411493). Promotes monoubiquitination of SNCA (PubMed:19224863). Regulates cellular clock function via ubiquitination of the circadian transcriptional repressors NR1D1 and NR1D2 leading to their proteasomal degradation (PubMed:26392558). Plays an important role in mediating the rhythmic degradation/clearance of NR1D1 and NR1D2 contributing to their circadian profile of protein abundance (PubMed:26392558). Mediates ubiquitination and degradation of EGLN2 and EGLN3 in response to the unfolded protein response (UPR), leading to their degradation and subsequent stabilization of ATF4 (By similarity). Also part of the Wnt signaling pathway in which it mediates the Wnt-induced ubiquitin-mediated proteasomal degradation of AXIN1. {ECO:0000250|UniProtKB:Q06986, ECO:0000269|PubMed:11483518, ECO:0000269|PubMed:12411493, ECO:0000269|PubMed:19224863, ECO:0000269|PubMed:22878263, ECO:0000269|PubMed:26392558, ECO:0000269|PubMed:28546513, ECO:0000269|PubMed:9334332}.
|
Homo sapiens (Human)
|
O43257
|
ZNHI1_HUMAN
|
MVEKKTSVRSQDPGQRRVLDRAARQRRINRQLEALENDNFQDDPHAGLPQLGKRLPQFDDDADTGKKKKKTRGDHFKLRFRKNFQALLEEQNLSVAEGPNYLTACAGPPSRPQRPFCAVCGFPSPYTCVSCGARYCTVRCLGTHQETRCLKWTV
| null | null |
calcium ion homeostasis [GO:0055074]; chromatin remodeling [GO:0006338]; heart process [GO:0003015]; intestinal stem cell homeostasis [GO:0036335]; muscle cell differentiation [GO:0042692]; positive regulation of DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator [GO:1902164]; positive regulation of lymphoid progenitor cell differentiation [GO:1905458]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261]; regulation of DNA-templated transcription [GO:0006355]
|
nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634]; Swr1 complex [GO:0000812]
|
histone binding [GO:0042393]; metal ion binding [GO:0046872]; nucleosome binding [GO:0031491]
|
PF04438;
|
3.30.60.190;
|
ZNHIT1 family
|
PTM: Phosphorylated on Thr by MAPK11 or MAPK14 (PubMed:17380123). Phosphorylation is required for MYOG induction, for deposition of histone H2AZ1 at the MYOG promoter and for SRCAP complex integrity (PubMed:20473270). {ECO:0000269|PubMed:17380123, ECO:0000269|PubMed:20473270}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17892483}.
| null | null | null | null | null |
FUNCTION: Plays a role in chromatin remodeling by promoting the incorporation of histone variant H2AZ1/H2A.Z into the genome to regulate gene expression (PubMed:20473270, PubMed:35175558). Promotes SRCAP complex-mediated deposition of histone variant H2AZ1 to lymphoid fate regulator genes, enhancing lymphoid lineage commitment (By similarity). Recruited to the promoter of the transcriptional activator MYOG at the early stages of muscle differentiation where it mediates binding of histone H2AZ1 to chromatin and induces muscle-specific gene expression (PubMed:20473270). Maintains hematopoietic stem cell (HSC) quiescence by determining the chromatin accessibility at distal enhancers of HSC quiescence genes such as PTEN, FSTL1 and KLF4, enhancing deposition of H2AZ1 to promote their sustained transcription and restricting PI3K-AKT signaling inhibition (By similarity). Plays a role in intestinal stem cell maintenance by promoting H2AZ1 deposition at the transcription start sites of genes involved in intestinal stem cell fate determination including LGR5, TGFB1 and TGFBR2, thereby contributing to gene transcription (By similarity). Promotes phosphorylation of the H2AZ1 chaperone VPS72/YL1 which enhances the interaction between HZAZ1 and VPS72 (By similarity). Regulates the entry of male germ cells into meiosis by controlling histone H2AZ1 deposition which facilitates the expression of meiotic genes such as MEIOSIN, leading to the initiation of meiosis (By similarity). Required for postnatal heart function through its role in maintenance of cardiac Ca(2+) homeostasis by modulating the expression of Ca(2+)-regulating proteins CASQ1 and ATP2A2/SERCA2A via deposition of histone H2AZ1 at their promoters (By similarity). During embryonic heart development, required for mitochondrial maturation and oxidative metabolism by functioning through H2AZ1 deposition to activate transcription of metabolic genes and is also required to maintain the stability of the respiratory complex (By similarity). In neural cells, increases deposition of the H2AZ1 histone variant and promotes neurite growth (PubMed:35175558). Plays a role in TP53/p53-mediated apoptosis induction by stimulating the transcriptional activation of several proapoptotic p53 target genes such as PMAIP1/NOXA and BBC3/PUMA (PubMed:17380123). Mediates cell cycle arrest induced in response to gamma-irradiation by enhancing recruitment of TP53/p53 to the promoter of the cell cycle inhibitor CDKN1A, leading to its transcriptional activation (PubMed:17700068). Recruited to the promoter of cyclin-dependent kinase CDK6 and inhibits its transcription, possibly by decreasing the acetylation level of histone H4, leading to cell cycle arrest at the G1 phase (By similarity). Plays a role in lens fiber cell differentiation by regulating the expression of cell cycle regulator CDKN1A/p21Cip1 (By similarity). Binds to transcriptional repressor NR1D2 and relieves it of its inhibitory effect on the transcription of apolipoprotein APOC3 without affecting its DNA-binding activity (PubMed:17892483). {ECO:0000250|UniProtKB:Q8R331, ECO:0000269|PubMed:17380123, ECO:0000269|PubMed:17700068, ECO:0000269|PubMed:17892483, ECO:0000269|PubMed:20473270, ECO:0000269|PubMed:35175558}.
|
Homo sapiens (Human)
|
O43264
|
ZW10_HUMAN
|
MASFVTEVLAHSGRLEKEDLGTRISRLTRRVEEIKGEVCNMISKKYSEFLPSMQSAQGLITQVDKLSEDIDLLKSRIESEVRRDLHVSTGEFTDLKQQLERDSVVLSLLKQLQEFSTAIEEYNCALTEKKYVTGAQRLEEAQKCLKLLKSRKCFDLKILKSLSMELTIQKQNILYHLGEEWQKLIVWKFPPSKDTSSLESYLQTELHLYTEQSHKEEKTPMPPISSVLLAFSVLGELHSKLKSFGQMLLKYILRPLASCPSLHAVIESQPNIVIIRFESIMTNLEYPSPSEVFTKIRLVLEVLQKQLLDLPLDTDLENEKTSTVPLAEMLGDMIWEDLSECLIKNCLVYSIPTNSSKLQQYEEIIQSTEEFENALKEMRFLKGDTTDLLKYARNINSHFANKKCQDVIVAARNLMTSEIHNTVKIIPDSKINVPELPTPDEDNKLEVQKVSNTQYHEVMNLEPENTLDQHSFSLPTCRISESVKKLMELAYQTLLEATTSSDQCAVQLFYSVRNIFHLFHDVVPTYHKENLQKLPQLAAIHHNNCMYIAHHLLTLGHQFRLRLAPILCDGTATFVDLVPGFRRLGTECFLAQMRAQKGELLERLSSARNFSNMDDEENYSAASKAVRQVLHQLKRLGIVWQDVLPVNIYCKAMGTLLNTAISEVIGKITALEDISTEDGDRLYSLCKTVMDEGPQVFAPLSEESKNKKYQEEVPVYVPKWMPFKELMMMLQASLQEIGDRWADGKGPLAAAFSSSEVKALIRALFQNTERRAAALAKIK
| null | null |
cell division [GO:0051301]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; establishment of mitotic spindle orientation [GO:0000132]; Golgi organization [GO:0007030]; meiotic cell cycle [GO:0051321]; mitotic metaphase chromosome alignment [GO:0007080]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle assembly checkpoint signaling [GO:0007094]; protein localization to kinetochore [GO:0034501]; protein transport [GO:0015031]; protein-containing complex assembly [GO:0065003]; regulation of attachment of spindle microtubules to kinetochore [GO:0051988]; regulation of exit from mitosis [GO:0007096]; retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum [GO:0006890]
|
cytosol [GO:0005829]; Dsl1/NZR complex [GO:0070939]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; lipid droplet [GO:0005811]; membrane [GO:0016020]; nucleus [GO:0005634]; RZZ complex [GO:1990423]; spindle pole [GO:0000922]
|
centromeric DNA binding [GO:0019237]
|
PF20666;PF20665;PF06248;
|
1.10.357.150;
|
ZW10 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15029241}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15029241}; Peripheral membrane protein {ECO:0000269|PubMed:15029241}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:11590237, ECO:0000269|PubMed:15485811, ECO:0000269|PubMed:15824131}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11590237}. Lipid droplet {ECO:0000269|PubMed:30970241}. Note=Dynamic pattern of localization during the cell cycle. In most cells at interphase, present diffusely in the cytoplasm (PubMed:15029241). In prometaphase, associated with the kinetochore. At metaphase, detected both at the kinetochores and, most prominently, at the spindle, particularly at the spindle poles. In very early anaphase, detected on segregating kinetochores. In late anaphase and telophase, accumulates at the spindle midzone (PubMed:11590237). {ECO:0000269|PubMed:11590237, ECO:0000269|PubMed:15029241}.
| null | null | null | null | null |
FUNCTION: Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its function related to the spindle assembly machinery is proposed to depend on its association in the mitotic RZZ complex (PubMed:11590237, PubMed:15485811, PubMed:15824131). Involved in regulation of membrane traffic between the Golgi and the endoplasmic reticulum (ER); the function is proposed to depend on its association in the interphase NRZ complex which is believed to play a role in SNARE assembly at the ER (PubMed:15029241). {ECO:0000269|PubMed:11590237, ECO:0000269|PubMed:15029241, ECO:0000269|PubMed:15094189, ECO:0000269|PubMed:15485811, ECO:0000269|PubMed:15824131, ECO:0000305}.
|
Homo sapiens (Human)
|
O43272
|
PROD_HUMAN
|
MALRRALPALRPCIPRFVPLSTAPASREQPAAGPAAVPGGGSATAVRPPVPAVDFGNAQEAYRSRRTWELARSLLVLRLCAWPALLARHEQLLYVSRKLLGQRLFNKLMKMTFYGHFVAGEDQESIQPLLRHYRAFGVSAILDYGVEEDLSPEEAEHKEMESCTSAAERDGSGTNKRDKQYQAHWAFGDRRNGVISARTYFYANEAKCDSHMETFLRCIEASGRVSDDGFIAIKLTALGRPQFLLQFSEVLAKWRCFFHQMAVEQGQAGLAAMDTKLEVAVLQESVAKLGIASRAEIEDWFTAETLGVSGTMDLLDWSSLIDSRTKLSKHLVVPNAQTGQLEPLLSRFTEEEELQMTRMLQRMDVLAKKATEMGVRLMVDAEQTYFQPAISRLTLEMQRKFNVEKPLIFNTYQCYLKDAYDNVTLDVELARREGWCFGAKLVRGAYLAQERARAAEIGYEDPINPTYEATNAMYHRCLDYVLEELKHNAKAKVMVASHNEDTVRFALRRMEELGLHPADHRVYFGQLLGMCDQISFPLGQAGYPVYKYVPYGPVMEVLPYLSRRALENSSLMKGTHRERQLLWLELLRRLRTGNLFHRPA
|
1.5.5.2
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:15662599};
|
4-hydroxyproline catabolic process [GO:0019470]; intrinsic apoptotic signaling pathway in response to oxidative stress [GO:0008631]; proline catabolic process [GO:0006562]; proline catabolic process to glutamate [GO:0010133]; proline metabolic process [GO:0006560]; regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway [GO:1903376]
|
intracellular membrane-bounded organelle [GO:0043231]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]
|
FAD binding [GO:0071949]; proline dehydrogenase activity [GO:0004657]
|
PF01619;
|
3.20.20.220;
|
Proline oxidase family
| null |
SUBCELLULAR LOCATION: Mitochondrion matrix.
|
CATALYTIC ACTIVITY: Reaction=a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a quinol + H(+); Xref=Rhea:RHEA:23784, ChEBI:CHEBI:15378, ChEBI:CHEBI:17388, ChEBI:CHEBI:24646, ChEBI:CHEBI:60039, ChEBI:CHEBI:132124; EC=1.5.5.2; Evidence={ECO:0000269|PubMed:15662599};
| null |
PATHWAY: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 1/2.
| null | null |
FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate. {ECO:0000269|PubMed:15662599}.
|
Homo sapiens (Human)
|
O43278
|
SPIT1_HUMAN
|
MAPARTMARARLAPAGIPAVALWLLCTLGLQGTQAGPPPAPPGLPAGADCLNSFTAGVPGFVLDTNASVSNGATFLESPTVRRGWDCVRACCTTQNCNLALVELQPDRGEDAIAACFLINCLYEQNFVCKFAPREGFINYLTREVYRSYRQLRTQGFGGSGIPKAWAGIDLKVQPQEPLVLKDVENTDWRLLRGDTDVRVERKDPNQVELWGLKEGTYLFQLTVTSSDHPEDTANVTVTVLSTKQTEDYCLASNKVGRCRGSFPRWYYDPTEQICKSFVYGGCLGNKNNYLREEECILACRGVQGGPLRGSSGAQATFPQGPSMERRHPVCSGTCQPTQFRCSNGCCIDSFLECDDTPNCPDASDEAACEKYTSGFDELQRIHFPSDKGHCVDLPDTGLCKESIPRWYYNPFSEHCARFTYGGCYGNKNNFEEEQQCLESCRGISKKDVFGLRREIPIPSTGSVEMAVAVFLVICIVVVVAILGYCFFKNQRKDFHGHHHHPPPTPASSTVSTTEDTEHLVYNHTTRPL
| null | null |
branching involved in labyrinthine layer morphogenesis [GO:0060670]; cellular response to BMP stimulus [GO:0071773]; epidermis development [GO:0008544]; epithelium development [GO:0060429]; extracellular matrix organization [GO:0030198]; negative regulation of neural precursor cell proliferation [GO:2000178]; neural tube closure [GO:0001843]; placenta blood vessel development [GO:0060674]; positive regulation of glial cell differentiation [GO:0045687]
|
cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
serine-type endopeptidase inhibitor activity [GO:0004867]
|
PF00014;PF00057;PF07502;
|
2.60.40.10;4.10.400.10;4.10.410.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9045658}. Cytoplasm {ECO:0000269|PubMed:28710277}. Cell membrane {ECO:0000269|PubMed:28710277}.
| null | null | null | null | null |
FUNCTION: Inhibitor of HGFAC (PubMed:9045658). Inhibits serine protease activity of ST14/matriptase in vitro (PubMed:28710277). Inhibits serine protease activity of TMPRSS13, via the BPTI/Kunitz inhibitor 1 domain (PubMed:20977675). {ECO:0000269|PubMed:20977675, ECO:0000269|PubMed:28710277, ECO:0000269|PubMed:9045658}.
|
Homo sapiens (Human)
|
O43280
|
TREA_HUMAN
|
MPGRTWELCLLLLLGLGLGSQEALPPPCESEIYCHGELLNQVQMAKLYQDDKQFVDMPLSIAPEQVLQTFTELSRDHNHSIPREQLQAFVHEHFQAKGQELQPWTPADWKDSPQFLQKISDAKLRAWAGQLHQLWKKLGKKMKPEVLSHPERFSLIYSEHPFIVPGGRFVEFYYWDSYWVMEGLLLSEMAETVKGMLQNFLDLVKTYGHVPNGGRVYYLQRSQPPLLTLMMDCYLTHTNDTAFLQENIETLALELDFWTKNRTVSVSLEGKNYLLNRYYVPYGGPRPESYSKDVELADTLPEGDREALWAELKAGAESGWDFSSRWLIGGPNPNSLSGIRTSKLVPVDLNAFLCQAEELMSNFYSRLGNDSQATKYRILRSQRLAALNTVLWDEQTGAWFDYDLEKKKKNREFYPSNLTPLWAGCFSDPGVADKALKYLEDNRILTYQYGIPTSLQKTGQQWDFPNAWAPLQDLVIRGLAKAPLRRAQEVAFQLAQNWIRTNFDVYSQKSAMYEKYDVSNGGQPGGGGEYEVQEGFGWTNGVVLMLLDRYGDRLTSGAKLAFLEPHCLAATLLPSLLLSLLPW
|
3.2.1.28
| null |
animal organ morphogenesis [GO:0009887]; trehalose catabolic process [GO:0005993]; trehalose metabolic process [GO:0005991]
|
extracellular exosome [GO:0070062]; membrane [GO:0016020]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
|
alpha,alpha-trehalase activity [GO:0004555]
|
PF01204;
|
1.50.10.10;
|
Glycosyl hydrolase 37 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P19813}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P19813}.
|
CATALYTIC ACTIVITY: Reaction=alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-glucose; Xref=Rhea:RHEA:32675, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:16551, ChEBI:CHEBI:17925; EC=3.2.1.28; Evidence={ECO:0000269|PubMed:8773341, ECO:0000269|PubMed:9427547};
| null | null | null | null |
FUNCTION: Intestinal trehalase is probably involved in the hydrolysis of ingested trehalose. {ECO:0000269|PubMed:8773341, ECO:0000269|PubMed:9427547}.
|
Homo sapiens (Human)
|
O43281
|
EFS_HUMAN
|
MAIATSTQLARALYDNTAESPQELSFRRGDVLRVLQREGAGGLDGWCLCSLHGQQGIVPANRVKLLPAGPAPKPSLSPASPAQPGSPYPAPDHSNEDQEVYVVPPPARPCPTSGPPAGPCPPSPDLIYKIPRASGTQLAAPRDALEVYDVPPTALRVPSSGPYDCPASFSHPLTRVAPQPPGEDDAPYDVPLTPKPPAELEPDLEWEGGREPGPPIYAAPSNLKRASALLNLYEAPEELLADGEGGGTDEGIYDVPLLGPEAPPSPEPPGALASHDQDTLAQLLARSPPPPHRPRLPSAESLSRRPLPALPVPEAPSPSPVPSPAPGRKGSIQDRPLPPPPPRLPGYGGPKVEGDPEGREMEDDPAGHHNEYEGIPMAEEYDYVHLKGMDKAQGSRPPDQACTGDPELPERGMPAPQEALSPGEPLVVSTGDLQLLYFYAGQCQSHYSALQAAVAALMSSTQANQPPRLFVPHSKRVVVAAHRLVFVGDTLGRLAASAPLRAQVRAAGTALGQALRATVLAVKGAALGYPSSPAIQEMVQCVTELAGQALQFTTLLTSLAP
| null | null |
cell adhesion [GO:0007155]; cell migration [GO:0016477]; intracellular signal transduction [GO:0035556]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]
|
protein domain specific binding [GO:0019904]; SH3 domain binding [GO:0017124]
|
PF12026;PF14604;
|
1.20.120.230;2.30.30.40;
|
CAS family
|
PTM: Phosphorylated on multiple tyrosine residues. Phosphorylated on tyrosines by FYN and SRC (By similarity). {ECO:0000250}.
| null | null | null | null | null | null |
FUNCTION: Docking protein which plays a central coordinating role for tyrosine-kinase-based signaling related to cell adhesion. May serve as an activator of SRC and a downstream effector. Interacts with the SH3 domain of FYN and with CRK, SRC, and YES (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O43283
|
M3K13_HUMAN
|
MANFQEHLSCSSSPHLPFSESKTFNGLQDELTAMGNHPSPKLLEDQQEKGMVRTELIESVHSPVTTTVLTSVSEDSRDQFENSVLQLREHDESETAVSQGNSNTVDGESTSGTEDIKIQFSRSGSGSGGFLEGLFGCLRPVWNIIGKAYSTDYKLQQQDTWEVPFEEISELQWLGSGAQGAVFLGKFRAEEVAIKKVREQNETDIKHLRKLKHPNIIAFKGVCTQAPCYCIIMEYCAHGQLYEVLRAGRKITPRLLVDWSTGIASGMNYLHLHKIIHRDLKSPNVLVTHTDAVKISDFGTSKELSDKSTKMSFAGTVAWMAPEVIRNEPVSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNSLHLPVPSTCPDGFKILMKQTWQSKPRNRPSFRQTLMHLDIASADVLATPQETYFKSQAEWREEVKKHFEKIKSEGTCIHRLDEELIRRRREELRHALDIREHYERKLERANNLYMELSAIMLQLEMREKELIKREQAVEKKYPGTYKRHPVRPIIHPNAMEKLMKRKGVPHKSGMQTKRPDLLRSEGIPTTEVAPTASPLSGSPKMSTSSSKSRYRSKPRHRRGNSRGSHSDFAAILKNQPAQENSPHPTYLHQAQSQYPSLHHHNSLQQQYQQPPPAMSQSHHPRLNMHGQDIATCANNLRYFGPAAALRSPLSNHAQRQLPGSSPDLISTAMAADCWRSSEPDKGQAGPWGCCQADAYDPCLQCRPEQYGSLDIPSAEPVGRSPDLSKSPAHNPLLENAQSSEKTEENEFSGCRSESSLGTSHLGTPPALPRKTRPLQKSGDDSSEEEEGEVDSEVEFPRRQRPHRCISSCQSYSTFSSENFSVSDGEEGNTSDHSNSPDELADKLEDRLAEKLDDLLSQTPEIPIDISSHSDGLSDKECAVRRVKTQMSLGKLCVEERGYENPMQFEESDCDSSDGECSDATVRTNKHYSSATW
|
2.7.11.25
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q60700};
|
JNK cascade [GO:0007254]; peptidyl-serine phosphorylation [GO:0018105]; positive regulation of axon extension [GO:0045773]; positive regulation of branching morphogenesis of a nerve [GO:1905492]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of neuron maturation [GO:0014042]; positive regulation of neuron projection arborization [GO:0150012]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; stress-activated MAPK cascade [GO:0051403]
|
cytoplasm [GO:0005737]; membrane [GO:0016020]
|
ATP binding [GO:0005524]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; IkappaB kinase complex binding [GO:0106137]; JUN kinase kinase kinase activity [GO:0004706]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activator activity [GO:0043539]; protein serine/threonine kinase activity [GO:0004674]
|
PF07714;
|
1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily
|
PTM: Autophosphorylated on serine and threonine residues. {ECO:0000269|PubMed:9353328}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9353328}. Membrane {ECO:0000269|PubMed:9353328}; Peripheral membrane protein {ECO:0000269|PubMed:9353328}.
|
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=2.7.11.25; Evidence={ECO:0000269|PubMed:9353328}; 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=2.7.11.25; Evidence={ECO:0000269|PubMed:9353328};
| null | null | null | null |
FUNCTION: Activates the JUN N-terminal pathway through activation of the MAP kinase kinase MAP2K7. Acts synergistically with PRDX3 to regulate the activation of NF-kappa-B in the cytosol. This activation is kinase-dependent and involves activating the IKK complex, the IKBKB-containing complex that phosphorylates inhibitors of NF-kappa-B. {ECO:0000269|PubMed:11726277, ECO:0000269|PubMed:12492477, ECO:0000269|PubMed:9353328}.
|
Homo sapiens (Human)
|
O43286
|
B4GT5_HUMAN
|
MRARRGLLRLPRRSLLAALFFFSLSSSLLYFVYVAPGIVNTYLFMMQAQGILIRDNVRTIGAQVYEQVLRSAYAKRNSSVNDSDYPLDLNHSETFLQTTTFLPEDFTYFANHTCPERLPSMKGPIDINMSEIGMDYIHELFSKDPTIKLGGHWKPSDCMPRWKVAILIPFRNRHEHLPVLFRHLLPMLQRQRLQFAFYVVEQVGTQPFNRAMLFNVGFQEAMKDLDWDCLIFHDVDHIPESDRNYYGCGQMPRHFATKLDKYMYLLPYTEFFGGVSGLTVEQFRKINGFPNAFWGWGGEDDDLWNRVQNAGYSVSRPEGDTGKYKSIPHHHRGEVQFLGRYALLRKSKERQGLDGLNNLNYFANITYDALYKNITVNLTPELAQVNEY
|
2.4.1.-; 2.4.1.274
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9UBX8};
|
carbohydrate metabolic process [GO:0005975]; central nervous system myelination [GO:0022010]; central nervous system neuron axonogenesis [GO:0021955]; ganglioside biosynthetic process via lactosylceramide [GO:0010706]; glycoprotein biosynthetic process [GO:0009101]; glycosylation [GO:0070085]; neuron maturation [GO:0042551]; O-glycan processing [GO:0016266]; poly-N-acetyllactosamine biosynthetic process [GO:0030311]; positive regulation of embryonic development [GO:0040019]; protein glycosylation [GO:0006486]; regulation of protein stability [GO:0031647]
|
Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]
|
galactosyltransferase activity [GO:0008378]; metal ion binding [GO:0046872]; N-acetyllactosamine synthase activity [GO:0003945]; UDP-galactose:glucosylceramide beta-1,4-galactosyltransferase activity [GO:0008489]
|
PF02709;PF13733;
| null |
Glycosyltransferase 7 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:P15291}; Single-pass type II membrane protein. Golgi apparatus {ECO:0000250|UniProtKB:A0A1S6M251}. Note=Trans cisternae of Golgi stack. {ECO:0000250|UniProtKB:P15291}.
|
CATALYTIC ACTIVITY: Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + UDP-alpha-D-galactose = a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:31495, ChEBI:CHEBI:15378, ChEBI:CHEBI:17950, ChEBI:CHEBI:22801, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.274; Evidence={ECO:0000269|PubMed:24498430}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31496; Evidence={ECO:0000305|PubMed:24498430};
| null |
PATHWAY: Protein modification; protein glycosylation.; PATHWAY: Sphingolipid metabolism.
| null | null |
FUNCTION: Catalyzes the synthesis of lactosylceramide (LacCer) via the transfer of galactose from UDP-galactose to glucosylceramide (GlcCer) (PubMed:24498430). LacCer is the starting point in the biosynthesis of all gangliosides (membrane-bound glycosphingolipids) which play pivotal roles in the CNS including neuronal maturation and axonal and myelin formation (By similarity). Plays a role in the glycosylation of BMPR1A and regulation of its protein stability (By similarity). Essential for extraembryonic development during early embryogenesis (By similarity). {ECO:0000250|UniProtKB:Q9JMK0, ECO:0000269|PubMed:24498430}.
|
Homo sapiens (Human)
|
O43290
|
SNUT1_HUMAN
|
MGSSKKHRGEKEAAGTTAAAGTGGATEQPPRHREHKKHKHRSGGSGGSGGERRKRSRERGGERGSGRRGAEAEARSSTHGRERSQAEPSERRVKREKRDDGYEAAASSKTSSGDASSLSIEETNKLRAKLGLKPLEVNAIKKEAGTKEEPVTADVINPMALRQREELREKLAAAKEKRLLNQKLGKIKTLGEDDPWLDDTAAWIERSRQLQKEKDLAEKRAKLLEEMDQEFGVSTLVEEEFGQRRQDLYSARDLQGLTVEHAIDSFREGETMILTLKDKGVLQEEEDVLVNVNLVDKERAEKNVELRKKKPDYLPYAEDESVDDLAQQKPRSILSKYDEELEGERPHSFRLEQGGTADGLRERELEEIRAKLRLQAQSLSTVGPRLASEYLTPEEMVTFKKTKRRVKKIRKKEKEVVVRADDLLPLGDQTQDGDFGSRLRGRGRRRVSEVEEEKEPVPQPLPSDDTRVENMDISDEEEGGAPPPGSPQVLEEDEAELELQKQLEKGRRLRQLQQLQQLRDSGEKVVEIVKKLESRQRGWEEDEDPERKGAIVFNATSEFCRTLGEIPTYGLAGNREEQEELMDFERDEERSANGGSESDGEENIGWSTVNLDEEKQQQDFSASSTTILDEEPIVNRGLAAALLLCQNKGLLETTVQKVARVKAPNKSLPSAVYCIEDKMAIDDKYSRREEYRGFTQDFKEKDGYKPDVKIEYVDETGRKLTPKEAFRQLSHRFHGKGSGKMKTERRMKKLDEEALLKKMSSSDTPLGTVALLQEKQKAQKTPYIVLSGSGKSMNANTITK
| null | null |
maturation of 5S rRNA [GO:0000481]; mRNA cis splicing, via spliceosome [GO:0045292]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of cytotoxic T cell differentiation [GO:0045585]; spliceosomal snRNP assembly [GO:0000387]
|
Cajal body [GO:0015030]; catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; U2-type precatalytic spliceosome [GO:0071005]; U4/U6 x U5 tri-snRNP complex [GO:0046540]
|
RNA binding [GO:0003723]
|
PF19252;PF03343;
| null |
SNU66/SART1 family
|
PTM: Sumoylated with SUMO2.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11350945, ECO:0000269|PubMed:9449708}. Note=Found in the nucleus of mitogen-activated peripheral blood mononuclear cells (PBMCs), tumor cells, or normal cell lines, but not in normal tissues except testis and fetal liver or in unstimulated PBMCs, suggesting preferential expression in proliferating cells.
| null | null | null | null | null |
FUNCTION: Plays a role in mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the spliceosome. May also bind to DNA. {ECO:0000269|PubMed:11350945, ECO:0000269|PubMed:25092792}.
|
Homo sapiens (Human)
|
O43291
|
SPIT2_HUMAN
|
MAQLCGLRRSRAFLALLGSLLLSGVLAADRERSIHDFCLVSKVVGRCRASMPRWWYNVTDGSCQLFVYGGCDGNSNNYLTKEECLKKCATVTENATGDLATSRNAADSSVPSAPRRQDSEDHSSDMFNYEEYCTANAVTGPCRASFPRWYFDVERNSCNNFIYGGCRGNKNSYRSEEACMLRCFRQQENPPLPLGSKVVVLAGLFVMVLILFLGASMVYLIRVARRNQERALRTVWSSGDDKEQLVKNTYVL
| null | null |
basement membrane organization [GO:0071711]; cellular response to BMP stimulus [GO:0071773]; epithelial cell morphogenesis involved in placental branching [GO:0060672]; establishment or maintenance of cell polarity [GO:0007163]; negative regulation of cell motility [GO:2000146]; negative regulation of cell-cell adhesion [GO:0022408]; negative regulation of neural precursor cell proliferation [GO:2000178]; neural tube closure [GO:0001843]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
endopeptidase inhibitor activity [GO:0004866]; serine-type endopeptidase inhibitor activity [GO:0004867]
|
PF00014;
|
4.10.410.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28710277, ECO:0000269|PubMed:34562451}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:28710277}.
| null | null | null | null | null |
FUNCTION: Inhibitor of HGFAC (PubMed:9346890). Also inhibits plasmin, and plasma and tissue kallikrein (PubMed:9115294). Inhibits serine protease activity of TMPRSS13 (PubMed:20977675, PubMed:28710277). Inhibits serine protease activity of ST14/matriptase in vitro (PubMed:28710277). {ECO:0000269|PubMed:20977675, ECO:0000269|PubMed:28710277, ECO:0000269|PubMed:9115294, ECO:0000269|PubMed:9346890}.
|
Homo sapiens (Human)
|
O43292
|
GPAA1_HUMAN
|
MGLLSDPVRRRALARLVLRLNAPLCVLSYVAGIAWFLALVFPPLTQRTYMSENAMGSTMVEEQFAGGDRARAFARDFAAHRKKSGALPVAWLERTMRSVGLEVYTQSFSRKLPFPDETHERYMVSGTNVYGILRAPRAASTESLVLTVPCGSDSTNSQAVGLLLALAAHFRGQIYWAKDIVFLVTEHDLLGTEAWLEAYHDVNVTGMQSSPLQGRAGAIQAAVALELSSDVVTSLDVAVEGLNGQLPNLDLLNLFQTFCQKGGLLCTLQGKLQPEDWTSLDGPLQGLQTLLLMVLRQASGRPHGSHGLFLRYRVEALTLRGINSFRQYKYDLVAVGKALEGMFRKLNHLLERLHQSFFLYLLPGLSRFVSIGLYMPAVGFLLLVLGLKALELWMQLHEAGMGLEEPGGAPGPSVPLPPSQGVGLASLVAPLLISQAMGLALYVLPVLGQHVATQHFPVAEAEAVVLTLLAIYAAGLALPHNTHRVVSTQAPDRGWMALKLVALIYLALQLGCIALTNFSLGFLLATTMVPTAALAKPHGPRTLYAALLVLTSPAATLLGSLFLWRELQEAPLSLAEGWQLFLAALAQGVLEHHTYGALLFPLLSLGLYPCWLLFWNVLFWK
| null | null |
attachment of GPI anchor to protein [GO:0016255]; protein retention in ER lumen [GO:0006621]; protein-containing complex assembly [GO:0065003]
|
centrosome [GO:0005813]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; GPI-anchor transamidase complex [GO:0042765]; membrane [GO:0016020]; mitochondrion [GO:0005739]
|
tubulin binding [GO:0015631]
|
PF04114;
|
3.40.630.10;
| null | null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11483512}; Multi-pass membrane protein {ECO:0000269|PubMed:11483512}.
| null | null |
PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
| null | null |
FUNCTION: Component of the GPI transamidase complex, necessary for transfer of GPI to proteins (PubMed:34576938). Essential for GPI-anchoring of precursor proteins but not for GPI synthesis. Acts before or during formation of the carbonyl intermediate. {ECO:0000269|PubMed:29100095, ECO:0000269|PubMed:34576938, ECO:0000269|PubMed:9468317}.
|
Homo sapiens (Human)
|
O43293
|
DAPK3_HUMAN
|
MSTFRQEDVEDHYEMGEELGSGQFAIVRKCRQKGTGKEYAAKFIKKRRLSSSRRGVSREEIEREVNILREIRHPNIITLHDIFENKTDVVLILELVSGGELFDFLAEKESLTEDEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNPRIKLIDFGIAHKIEAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSNTSELAKDFIRRLLVKDPKRRMTIAQSLEHSWIKAIRRRNVRGEDSGRKPERRRLKTTRLKEYTIKSHSSLPPNNSYADFERFSKVLEEAAAAEEGLRELQRSRRLCHEDVEALAAIYEEKEAWYREESDSLGQDLRRLRQELLKTEALKRQAQEEAKGALLGTSGLKRRFSRLENRYEALAKQVASEMRFVQDLVRALEQEKLQGVECGLR
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10356987};
|
apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; cellular response to type II interferon [GO:0071346]; chromatin organization [GO:0006325]; intracellular signal transduction [GO:0035556]; negative regulation of translation [GO:0017148]; positive regulation of apoptotic process [GO:0043065]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell migration [GO:0030335]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of apoptotic process [GO:0042981]; regulation of autophagy [GO:0010506]; regulation of cell motility [GO:2000145]; regulation of cell shape [GO:0008360]; regulation of DNA-templated transcription [GO:0006355]; regulation of focal adhesion assembly [GO:0051893]; regulation of mitotic cell cycle [GO:0007346]; regulation of mitotic nuclear division [GO:0007088]; regulation of myosin II filament organization [GO:0043519]; regulation of smooth muscle contraction [GO:0006940]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]
|
ATP binding [GO:0005524]; cAMP response element binding protein binding [GO:0008140]; identical protein binding [GO:0042802]; leucine zipper domain binding [GO:0043522]; protein homodimerization activity [GO:0042803]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; small GTPase binding [GO:0031267]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, DAP kinase subfamily
|
PTM: The phosphorylation status is critical for kinase activity, oligomerization and intracellular localization. Phosphorylation at Thr-180, Thr-225 and Thr-265 is essential for activity. The phosphorylated form is localized in the cytoplasm promoted by phosphorylation at Thr-299; nuclear translocation or retention is maximal when it is not phosphorylated. Phosphorylation increases the trimeric form, and its dephosphorylation favors a kinase-inactive monomeric form. Both isoform 1 and isoform 2 can undergo autophosphorylation. {ECO:0000269|PubMed:15367680, ECO:0000269|PubMed:15611134, ECO:0000269|PubMed:17158456, ECO:0000269|PubMed:20854903}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15367680, ECO:0000269|PubMed:15910542, ECO:0000269|PubMed:20854903}. Cytoplasm {ECO:0000269|PubMed:15367680, ECO:0000269|PubMed:15611134, ECO:0000269|PubMed:17953487, ECO:0000269|PubMed:20854903}. Note=Predominantly localizes to the cytoplasm but can shuttle between the nucleus and cytoplasm; cytoplasmic localization is promoted by phosphorylation at Thr-299 and involves Rho/Rock signaling. {ECO:0000269|PubMed:17953487, ECO:0000269|PubMed:20854903}.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000269|PubMed:17126281}. Cytoplasm {ECO:0000269|PubMed:17126281}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:17126281}. Cytoplasm {ECO:0000269|PubMed:17126281}.
|
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:10356987, ECO:0000269|PubMed:11384979, ECO:0000269|PubMed:11781833, ECO:0000269|PubMed:15096528, ECO:0000269|PubMed:17126281, ECO:0000269|PubMed:18995835}; 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:10356987, ECO:0000269|PubMed:11384979, ECO:0000269|PubMed:11781833, ECO:0000269|PubMed:15096528, ECO:0000269|PubMed:17126281, ECO:0000269|PubMed:18995835};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12 uM for myosin (isoform 2) {ECO:0000269|PubMed:17126281}; KM=6.2 uM for myosin (isoform 1) {ECO:0000269|PubMed:17126281}; KM=73 uM for MYL12B (isoform 2) {ECO:0000269|PubMed:17126281}; KM=10.4 uM for MYL12B (isoform 1) {ECO:0000269|PubMed:17126281}; Vmax=248 nmol/min/mg enzyme toward myosin (isoform 2) {ECO:0000269|PubMed:17126281}; Vmax=120 nmol/min/mg enzyme toward myosin (isoform 1) {ECO:0000269|PubMed:17126281}; Vmax=1.3 umol/min/mg enzyme toward MYL12B (isoform 2) {ECO:0000269|PubMed:17126281}; Vmax=271 nmol/min/mg enzyme toward MYL12B (isoform 1) {ECO:0000269|PubMed:17126281};
| null | null | null |
FUNCTION: Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation and actin cytoskeleton reorganization. Involved in the regulation of smooth muscle contraction. Regulates both type I (caspase-dependent) apoptotic and type II (caspase-independent) autophagic cell deaths signal, depending on the cellular setting. Involved in regulation of starvation-induced autophagy. Regulates myosin phosphorylation in both smooth muscle and non-muscle cells. In smooth muscle, regulates myosin either directly by phosphorylating MYL12B and MYL9 or through inhibition of smooth muscle myosin phosphatase (SMPP1M) via phosphorylation of PPP1R12A; the inhibition of SMPP1M functions to enhance muscle responsiveness to Ca(2+) and promote a contractile state. Phosphorylates MYL12B in non-muscle cells leading to reorganization of actin cytoskeleton. Isoform 2 can phosphorylate myosin, PPP1R12A and MYL12B. Overexpression leads to condensation of actin stress fibers into thick bundles. Involved in actin filament focal adhesion dynamics. The function in both reorganization of actin cytoskeleton and focal adhesion dissolution is modulated by RhoD. Positively regulates canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2. Phosphorylates RPL13A on 'Ser-77' upon interferon-gamma activation which is causing RPL13A release from the ribosome, RPL13A association with the GAIT complex and its subsequent involvement in transcript-selective translation inhibition. Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Involved in regulation of cell cycle progression and cell proliferation. May be a tumor suppressor. {ECO:0000269|PubMed:10356987, ECO:0000269|PubMed:11384979, ECO:0000269|PubMed:11781833, ECO:0000269|PubMed:12917339, ECO:0000269|PubMed:15096528, ECO:0000269|PubMed:15367680, ECO:0000269|PubMed:16219639, ECO:0000269|PubMed:17126281, ECO:0000269|PubMed:17158456, ECO:0000269|PubMed:18084323, ECO:0000269|PubMed:18995835, ECO:0000269|PubMed:21169990, ECO:0000269|PubMed:21408167, ECO:0000269|PubMed:21454679, ECO:0000269|PubMed:21487036, ECO:0000269|PubMed:23454120}.
|
Homo sapiens (Human)
|
O43294
|
TGFI1_HUMAN
|
MEDLDALLSDLETTTSHMPRSGAPKERPAEPLTPPPSYGHQPQTGSGESSGASGDKDHLYSTVCKPRSPKPAAPAAPPFSSSSGVLGTGLCELDRLLQELNATQFNITDEIMSQFPSSKVASGEQKEDQSEDKKRPSLPSSPSPGLPKASATSATLELDRLMASLSDFRVQNHLPASGPTQPPVVSSTNEGSPSPPEPTGKGSLDTMLGLLQSDLSRRGVPTQAKGLCGSCNKPIAGQVVTALGRAWHPEHFVCGGCSTALGGSSFFEKDGAPFCPECYFERFSPRCGFCNQPIRHKMVTALGTHWHPEHFCCVSCGEPFGDEGFHEREGRPYCRRDFLQLFAPRCQGCQGPILDNYISALSALWHPDCFVCRECFAPFSGGSFFEHEGRPLCENHFHARRGSLCATCGLPVTGRCVSALGRRFHPDHFTCTFCLRPLTKGSFQERAGKPYCQPCFLKLFG
| null | null |
actin cytoskeleton organization [GO:0030036]; cell adhesion [GO:0007155]; cell fate commitment [GO:0045165]; epithelial cell differentiation [GO:0030855]; fat cell differentiation [GO:0045444]; heart development [GO:0007507]; morphogenesis of embryonic epithelium [GO:0016331]; muscle structure development [GO:0061061]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of fat cell differentiation [GO:0045599]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; positive regulation of ubiquitin-dependent protein catabolic process [GO:2000060]; Wnt signaling pathway [GO:0016055]
|
adherens junction [GO:0005912]; cytosol [GO:0005829]; filamentous actin [GO:0031941]; focal adhesion [GO:0005925]; intracellular membrane-bounded organelle [GO:0043231]; nuclear matrix [GO:0016363]; stress fiber [GO:0001725]; Z disc [GO:0030018]
|
actin binding [GO:0003779]; I-SMAD binding [GO:0070411]; metal ion binding [GO:0046872]; muscle alpha-actinin binding [GO:0051371]; nuclear androgen receptor binding [GO:0050681]; Roundabout binding [GO:0048495]; transcription coactivator activity [GO:0003713]
|
PF00412;PF03535;
|
2.10.110.10;
|
Paxillin family
|
PTM: Phosphorylated by gonadotropin-releasing hormone-activated SRC. {ECO:0000269|PubMed:10838081, ECO:0000269|PubMed:11311131, ECO:0000269|PubMed:11856738, ECO:0000269|PubMed:17202804, ECO:0000269|PubMed:17233630}.
|
SUBCELLULAR LOCATION: Cell junction, focal adhesion. Nucleus matrix. Cytoplasm, cytoskeleton. Note=Associated with the actin cytoskeleton; colocalizes with stress fibers.
| null | null | null | null | null |
FUNCTION: Functions as a molecular adapter coordinating multiple protein-protein interactions at the focal adhesion complex and in the nucleus. Links various intracellular signaling modules to plasma membrane receptors and regulates the Wnt and TGFB signaling pathways. May also regulate SLC6A3 and SLC6A4 targeting to the plasma membrane hence regulating their activity. In the nucleus, functions as a nuclear receptor coactivator regulating glucocorticoid, androgen, mineralocorticoid and progesterone receptor transcriptional activity. May play a role in the processes of cell growth, proliferation, migration, differentiation and senescence. May have a zinc-dependent DNA-binding activity. {ECO:0000269|PubMed:10075738, ECO:0000269|PubMed:11463817, ECO:0000269|PubMed:11856738, ECO:0000269|PubMed:12177201, ECO:0000269|PubMed:12445807, ECO:0000269|PubMed:12700349, ECO:0000269|PubMed:15211577, ECO:0000269|PubMed:15561701, ECO:0000269|PubMed:16141357, ECO:0000269|PubMed:16624805, ECO:0000269|PubMed:16803896, ECO:0000269|PubMed:16849583, ECO:0000269|PubMed:17166536, ECO:0000269|PubMed:17233630, ECO:0000269|PubMed:9032249}.
|
Homo sapiens (Human)
|
O43295
|
SRGP3_HUMAN
|
MSSQTKFKKDKEIIAEYEAQIKEIRTQLVEQFKCLEQQSESRLQLLQDLQEFFRRKAEIELEYSRSLEKLAERFSSKIRSSREHQFKKDQYLLSPVNCWYLVLHQTRRESRDHATLNDIFMNNVIVRLSQISEDVIRLFKKSKEIGLQMHEELLKVTNELYTVMKTYHMYHAESISAESKLKEAEKQEEKQFNKSGDLSMNLLRHEDRPQRRSSVKKIEKMKEKRQAKYSENKLKCTKARNDYLLNLAATNAAISKYYIHDVSDLIDCCDLGFHASLARTFRTYLSAEYNLETSRHEGLDVIENAVDNLDSRSDKHTVMDMCNQVFCPPLKFEFQPHMGDEVCQVSAQQPVQTELLMRYHQLQSRLATLKIENEEVRKTLDATMQTLQDMLTVEDFDVSDAFQHSRSTESVKSAASETYMSKINIAKRRANQQETEMFYFTKFKEYVNGSNLITKLQAKHDLLKQTLGEGERAECGTTRPPCLPPKPQKMRRPRPLSVYSHKLFNGSMEAFIKDSGQAIPLVVESCIRYINLYGLQQQGIFRVPGSQVEVNDIKNSFERGEDPLVDDQNERDINSVAGVLKLYFRGLENPLFPKERFQDLISTIKLENPAERVHQIQQILVTLPRVVIVVMRYLFAFLNHLSQYSDENMMDPYNLAICFGPTLMHIPDGQDPVSCQAHINEVIKTIIIHHEAIFPSPRELEGPVYEKCMAGGEEYCDSPHSEPGAIDEVDHDNGTEPHTSDEEVEQIEAIAKFDYMGRSPRELSFKKGASLLLYHRASEDWWEGRHNGVDGLIPHQYIVVQDMDDAFSDSLSQKADSEASSGPLLDDKASSKNDLQSPTEHISDYGFGGVMGRVRLRSDGAAIPRRRSGGDTHSPPRGLGPSIDTPPRAAACPSSPHKIPLTRGRIESPEKRRMATFGSAGSINYPDKKALSEGHSMRSTCGSTRHSSLGDHKSLEAEALAEDIEKTMSTALHELRELERQNTVKQAPDVVLDTLEPLKNPPGPVSSEPASPLHTIVIRDPDAAMRRSSSSSTEMMTTFKPALSARLAGAQLRPPPMRPVRPVVQHRSSSSSSSGVGSPAVTPTEKMFPNSSADKSGTM
| null | null |
negative regulation of cell migration [GO:0030336]; regulation of small GTPase mediated signal transduction [GO:0051056]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
GTPase activator activity [GO:0005096]
|
PF00611;PF00620;PF00018;
|
1.20.1270.60;1.10.555.10;2.30.30.40;
| null | null | null | null | null | null | null | null |
FUNCTION: GTPase-activating protein for RAC1 and perhaps Cdc42, but not for RhoA small GTPase. May attenuate RAC1 signaling in neurons. {ECO:0000269|PubMed:12195014, ECO:0000269|PubMed:12447388}.
|
Homo sapiens (Human)
|
O43296
|
ZN264_HUMAN
|
MAAAVLTDRAQVSVTFDDVAVTFTKEEWGQLDLAQRTLYQEVMLENCGLLVSLGCPVPKAELICHLEHGQEPWTRKEDLSQDTCPGDKGKPKTTEPTTCEPALSEGISLQGQVTQGNSVDSQLGQAEDQDGLSEMQEGHFRPGIDPQEKSPGKMSPECDGLGTADGVCSRIGQEQVSPGDRVRSHNSCESGKDPMIQEEENNFKCSECGKVFNKKHLLAGHEKIHSGVKPYECTECGKTFIKSTHLLQHHMIHTGERPYECMECGKAFNRKSYLTQHQRIHSGEKPYKCNECGKAFTHRSNFVLHNRRHTGEKSFVCTECGQVFRHRPGFLRHYVVHSGENPYECLECGKVFKHRSYLMWHQQTHTGEKPYECSECGKVFLESAALIHHYVIHTGEKPFECLECGKAFNHRSYLKRHQRIHTGEKPFVCSECGKAFTHCSTFILHKRAHTGEKPFECKECGKAFSNRKDLIRHFSIHTGEKPYECVECGKAFTRMSGLTRHKRIHSGEKPYECVECGKSFCWSTNLIRHAIIHTGEKPYKCSECGKAFSRSSSLTQHQRMHTGKNPISVTDVGRPFTSGQTSVTLRELLLGKDFLNVTTEANILPEETSSSASDQPYQRETPQVSSL
| null | null |
regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleus [GO:0005634]
|
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;PF00096;
|
6.10.140.140;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)
|
O43298
|
ZBT43_HUMAN
|
MEPGTNSFRVEFPDFSSTILQKLNQQRQQGQLCDVSIVVQGHIFRAHKAVLAASSPYFCDQVLLKNSRRIVLPDVMNPRVFENILLSSYTGRLVMPAPEIVSYLTAASFLQMWHVVDKCTEVLEGNPTVLCQKLNHGSDHQSPSSSSYNGLVESFELGSGGHTDFPKAQELRDGENEEESTKDELSSQLTEHEYLPSNSSTEHDRLSTEMASQDGEEGASDSAEFHYTRPMYSKPSIMAHKRWIHVKPERLEQACEGMDVHATYDEHQVTESINTVQTEHTVQPSGVEEDFHIGEKKVEAEFDEQADESNYDEQVDFYGSSMEEFSGERSDGNLIGHRQEAALAAGYSENIEMVTGIKEEASHLGFSATDKLYPCQCGKSFTHKSQRDRHMSMHLGLRPYGCGVCGKKFKMKHHLVGHMKIHTGIKPYECNICAKRFMWRDSFHRHVTSCTKSYEAAKAEQNTTEAN
| null | null |
regulation of transcription by RNA polymerase II [GO:0006357]
|
chromatin [GO:0000785]; nucleus [GO:0005634]
|
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]; RNA polymerase III general transcription initiation factor binding [GO:0001025]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00651;
|
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)
|
O43299
|
AP5Z1_HUMAN
|
MFSAGAESLLHQAREIQDEELKKFCSRICKLLQAEDLGPDTLDSLQRLFLIISATKYSRRLEKTCVDLLQATLGLPACPEQLQVLCAAILREMSPSDSLSLAWDHTQNSRQLSLVASVLLAQGDRNEEVRAVGQGVLRALESRQPEGPSLRHLLPVMAKVVVLSPGTLQEDQATLLSKRLVDWLRYASLQQGLPHSGGFFSTPRARQPGPVTEVDGAVATDFFTVLSSGHRFTDDQWLNVQAFSMLRAWLLHSGPEGPGTLDTDDRSEQEGSTLSVISATSSAGRLLPPRERLREVAFEYCQRLIEQSNRRALRKGDSDLQKACLVEAVLVLDVLCRQDPSFLYRSLSCLKALHGRVRGDPASVRVLLPLAHFFLSHGEAAAVDSEAVYQHLFTRIPVEQFHSPMLAFEFIQFCRDNLHLFSGHLSTLRLSFPNLFKFLAWNSPPLTSEFVALLPALVDAGTALEMLHALLDLPCLTAVLDLQLRSAPAASERPLWDTSLRAPSCLEAFRDPQFQGLFQYLLRPKASGATERLAPLHQLLQPMAGCARVAQCAQAVPTLLQAFFSAVTQVADGSLINQLALLLLGRSDSLYPAPGYAAGVHSVLSSQFLALCTLKPSLVVELARDLLEFLGSVNGLCSRASLVTSVVWAIGEYLSVTYDRRCTVEQINKFFEALEALLFEVTQCRPSAALPRCPPQVVTVLMTTLTKLASRSQDLIPRASLLLSKMRTLAHSPATSSTHSEEGAEAIRTRATELLTLLKMPSVAQFVLTPSTEVCSPRYHRDANTALPLALRTVSRLVEREAGLMPG
| null | null |
double-strand break repair via homologous recombination [GO:0000724]; endosomal transport [GO:0016197]; protein transport [GO:0015031]; vesicle-mediated transport [GO:0016192]
|
AP-5 adaptor complex [GO:0044599]; AP-type membrane coat adaptor complex [GO:0030119]; cytoplasm [GO:0005737]; late endosome [GO:0005770]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
| null |
PF14764;
|
1.25.10.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20613862}. Nucleus {ECO:0000269|PubMed:20613862}. Note=By SDS-PAGE, 2 isoforms have been observed, the shorter seems to be predominantly nuclear and the longer is mostly cytoplasmic. {ECO:0000269|PubMed:20613862}.
| null | null | null | null | null |
FUNCTION: As part of AP-5, a probable fifth adaptor protein complex it may be involved in endosomal transport. According to PubMed:20613862 it is a putative helicase required for efficient homologous recombination DNA double-strand break repair. {ECO:0000269|PubMed:20613862, ECO:0000269|PubMed:22022230}.
|
Homo sapiens (Human)
|
O43300
|
LRRT2_HUMAN
|
MGLHFKWPLGAPMLAAIYAMSMVLKMLPALGMACPPKCRCEKLLFYCDSQGFHSVPNATDKGSLGLSLRHNHITELERDQFASFSQLTWLHLDHNQISTVKEDAFQGLYKLKELILSSNKIFYLPNTTFTQLINLQNLDLSFNQLSSLHPELFYGLRKLQTLHLRSNSLRTIPVRLFWDCRSLEFLDLSTNRLRSLARNGFAGLIKLRELHLEHNQLTKINFAHFLRLSSLHTLFLQWNKISNLTCGMEWTWGTLEKLDLTGNEIKAIDLTVFETMPNLKILLMDNNKLNSLDSKILNSLRSLTTVGLSGNLWECSARICALASWLGSFQGRWEHSILCHSPDHTQGEDILDAVHGFQLCWNLSTTVTVMATTYRDPTTEYTKRISSSSYHVGDKEIPTTAGIAVTTEEHFPEPDNAIFTQRVITGTMALLFSFFFIIFIVFISRKCCPPTLRRIRQCSMVQNHRQLRSQTRLHMSNMSDQGPYNEYEPTHEGPFIIINGYGQCKCQQLPYKECEV
| null | null |
long-term synaptic potentiation [GO:0060291]; negative regulation of receptor internalization [GO:0002091]; positive regulation of synapse assembly [GO:0051965]; regulation of postsynaptic density assembly [GO:0099151]; synapse organization [GO:0050808]
|
excitatory synapse [GO:0060076]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; postsynaptic density membrane [GO:0098839]; postsynaptic specialization membrane [GO:0099634]; Schaffer collateral - CA1 synapse [GO:0098685]
|
neurexin family protein binding [GO:0042043]
|
PF13855;
|
3.80.10.10;
|
LRRTM family
| null |
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Postsynaptic cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Localized to excitatory synapses. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Involved in the development and maintenance of excitatory synapses in the vertebrate nervous system. Regulates surface expression of AMPA receptors and instructs the development of functional glutamate release sites. Acts as a ligand for the presynaptic receptors NRXN1-A and NRXN1-B (By similarity). {ECO:0000250|UniProtKB:D4A7P2}.
|
Homo sapiens (Human)
|
O43303
|
CP110_HUMAN
|
MEEYEKFCEKSLARIQEASLSTESFLPAQSESISLIRFHGVAILSPLLNIEKRKEMQQEKQKALDVEARKQVNRKKALLTRVQEILDNVQVRKAPNASDFDQWEMETVYSNSEVRNLNVPATFPNSFPSHTEHSTAAKLDKIAGILPLDNEDQCKTDGIDLARDSEGFNSPKQCDSSNISHVENEAFPKTSSATPQETLISDGPFSVNEQQDLPLLAEVIPDPYVMSLQNLMKKSKEYIEREQSRRSLRGSINRIVNESHLDKEHDAVEVADCVKEKGQLTGKHCVSVIPDKPSLNKSNVLLQGASTQASSMSMPVLASFSKVDIPIRTGHPTVLESNSDFKVIPTFVTENNVIKSLTGSYAKLPSPEPSMSPKMHRRRSRTSSACHILINNPINACELSPKGKEQAMDLIIQDTDENTNVPEIMPKLPTDLAGVCSSKVYVGKNTSEVKEDVVLGKSNQVCQSSGNHLENKVTHGLVTVEGQLTSDERGAHIMNSTCAAMPKLHEPYASSQCIASPNFGTVSGLKPASMLEKNCSLQTELNKSYDVKNPSPLLMQNQNTRQQMDTPMVSCGNEQFLDNSFEKVKRRLDLDIDGLQKENCPYVITSGITEQERQHLPEKRYPKGSGFVNKNKMLGTSSKESEELLKSKMLAFEEMRKRLEEQHAQQLSLLIAEQEREQERLQKEIEEQEKMLKEKKAMTAEASELDINNAVELEWRKISDSSLLETMLSQADSLHTSNSNSSGFTNSAMQYSFVSANEAPFYLWGSSTSGLTKLSVTRPFGRAKTRWSQVFSLEIQAKFNKITAVAKGFLTRRLMQTDKLKQLRQTVKDTMEFIRSFQSEAPLKRGIVSAQDASLQERVLAQLRAALYGIHDIFFVMDAAERMSILHHDREVRKEKMLRQMDKMKSPRVALSAATQKSLDRKKYMKAAEMGMPNKKFLVKQNPSETRVLQPNQGQNAPVHRLLSRQGTPKTSVKGVVQNRQKPSQSRVPNRVPVSGVYAGKIQRKRPNVATI
| null | null |
centriole replication [GO:0007099]; centrosome duplication [GO:0051298]; ciliary basal body organization [GO:0032053]; negative regulation of centriole elongation [GO:1903723]; negative regulation of cilium assembly [GO:1902018]; positive regulation of cilium assembly [GO:0045724]; regulation of cytokinesis [GO:0032465]
|
centriole [GO:0005814]; centrosome [GO:0005813]; cilium [GO:0005929]; cytosol [GO:0005829]; protein-containing complex [GO:0032991]
| null |
PF16025;
| null | null |
PTM: Phosphorylated by CDKs. {ECO:0000269|PubMed:12361598}.; PTM: Ubiquitinated by the SCF(CCNF) during G2 phase, leading to its degradation by the proteasome and preventing centrosome reduplication. Deubiquitinated by USP33 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate. {ECO:0000269|PubMed:20596027, ECO:0000269|PubMed:23486064}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:12361598, ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:16760425, ECO:0000269|PubMed:17681131, ECO:0000269|PubMed:17719545, ECO:0000269|PubMed:20596027, ECO:0000269|PubMed:21620453, ECO:0000269|PubMed:30375385}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:30375385}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q7TSH4}. Note=Recruited early and then associates with the growing distal tips. Recruited to the mother centriole by KIF24 (PubMed:21620453). Removed from centrioles by TTBK2, leading to initiation of ciliogenesis and localizes only to the daughter centriole in ciliated cells. In cytotoxic T lymphocytes remains associated with the mother centriole during docking of the centrosome at the immunological synapse upon target contact (By similarity). Recruited at the distal end of the mother centriole by MPHOSPH9 (PubMed:30375385). {ECO:0000250|UniProtKB:Q7TSH4, ECO:0000269|PubMed:21620453, ECO:0000269|PubMed:30375385}.
| null | null | null | null | null |
FUNCTION: Necessary for centrosome duplication at different stages of procentriole formation. Acts as a key negative regulator of ciliogenesis in collaboration with CEP97 by capping the mother centriole thereby preventing cilia formation (PubMed:17681131, PubMed:17719545, PubMed:23486064, PubMed:30375385, PubMed:35301795). Also involved in promoting ciliogenesis. May play a role in the assembly of the mother centriole subdistal appendages (SDA) thereby effecting the fusion of recycling endosomes to basal bodies during cilia formation (By similarity). Required for correct spindle formation and has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CETN2 (PubMed:16760425). {ECO:0000250|UniProtKB:Q7TSH4, ECO:0000269|PubMed:12361598, ECO:0000269|PubMed:16760425, ECO:0000269|PubMed:17681131, ECO:0000269|PubMed:17719545, ECO:0000269|PubMed:23486064, ECO:0000269|PubMed:30375385, ECO:0000269|PubMed:35301795}.
|
Homo sapiens (Human)
|
O43306
|
ADCY6_HUMAN
|
MSWFSGLLVPKVDERKTAWGERNGQKRSRRRGTRAGGFCTPRYMSCLRDAEPPSPTPAGPPRCPWQDDAFIRRGGPGKGKELGLRAVALGFEDTEVTTTAGGTAEVAPDAVPRSGRSCWRRLVQVFQSKQFRSAKLERLYQRYFFQMNQSSLTLLMAVLVLLTAVLLAFHAAPARPQPAYVALLACAAALFVGLMVVCNRHSFRQDSMWVVSYVVLGILAAVQVGGALAADPRSPSAGLWCPVFFVYIAYTLLPIRMRAAVLSGLGLSTLHLILAWQLNRGDAFLWKQLGANVLLFLCTNVIGICTHYPAEVSQRQAFQETRGYIQARLHLQHENRQQERLLLSVLPQHVAMEMKEDINTKKEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGVDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGRAGRIHITRATLQYLNGDYEVEPGRGGERNAYLKEQHIETFLILGASQKRKEEKAMLAKLQRTRANSMEGLMPRWVPDRAFSRTKDSKAFRQMGIDDSSKDNRGTQDALNPEDEVDEFLSRAIDARSIDQLRKDHVRRFLLTFQREDLEKKYSRKVDPRFGAYVACALLVFCFICFIQLLIFPHSTLMLGIYASIFLLLLITVLICAVYSCGSLFPKALQRLSRSIVRSRAHSTAVGIFSVLLVFTSAIANMFTCNHTPIRSCAARMLNLTPADITACHLQQLNYSLGLDAPLCEGTMPTCSFPEYFIGNMLLSLLASSVFLHISSIGKLAMIFVLGLIYLVLLLLGPPATIFDNYDLLLGVHGLASSNETFDGLDCPAAGRVALKYMTPVILLVFALALYLHAQQVESTARLDFLWKLQATGEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIISEERFRQLEKIKTIGSTYMAASGLNASTYDQVGRSHITALADYAMRLMEQMKHINEHSFNNFQMKIGLNMGPVVAGVIGARKPQYDIWGNTVNVSSRMDSTGVPDRIQVTTDLYQVLAAKGYQLECRGVVKVKGKGEMTTYFLNGGPSS
|
4.6.1.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15385642}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:15385642}; Note=Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). {ECO:0000250|UniProtKB:P30803};
|
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; blood vessel diameter maintenance [GO:0097746]; cAMP biosynthetic process [GO:0006171]; cellular response to catecholamine stimulus [GO:0071870]; cellular response to forskolin [GO:1904322]; cellular response to prostaglandin E stimulus [GO:0071380]; cellular response to vasopressin [GO:1904117]; dopamine receptor signaling pathway [GO:0007212]; intracellular signal transduction [GO:0035556]; negative regulation of neuron projection development [GO:0010977]; negative regulation of urine volume [GO:0035811]; renal water homeostasis [GO:0003091]
|
cilium [GO:0005929]; membrane [GO:0016020]; plasma membrane [GO:0005886]; stereocilium [GO:0032420]
|
adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein kinase binding [GO:0019901]; protein kinase C binding [GO:0005080]
|
PF16214;PF06327;PF00211;
|
3.30.70.1230;
|
Adenylyl cyclase class-4/guanylyl cyclase family
|
PTM: Phosphorylation by RAF1 increases enzyme activity. Phosphorylation by PKA at Ser-662 inhibits the GNAS-mediated increase in catalytic activity. Phosphorylation by PKC at Ser-556, Ser-662 and Thr-919 inhibits catalytic activity. {ECO:0000250|UniProtKB:Q03343}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17110384}; Multi-pass membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000250|UniProtKB:Q01341}. Cell projection, stereocilium {ECO:0000250|UniProtKB:Q01341}.
|
CATALYTIC ACTIVITY: Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1; Evidence={ECO:0000269|PubMed:17110384, ECO:0000269|PubMed:17916776};
| null | null | null | null |
FUNCTION: Catalyzes the formation of the signaling molecule cAMP downstream of G protein-coupled receptors (PubMed:17110384, PubMed:17916776). Functions in signaling cascades downstream of beta-adrenergic receptors in the heart and in vascular smooth muscle cells (PubMed:17916776). Functions in signaling cascades downstream of the vasopressin receptor in the kidney and has a role in renal water reabsorption. Functions in signaling cascades downstream of PTH1R and plays a role in regulating renal phosphate excretion. Functions in signaling cascades downstream of the VIP and SCT receptors in pancreas and contributes to the regulation of pancreatic amylase and fluid secretion (By similarity). Signaling mediates cAMP-dependent activation of protein kinase PKA. This promotes increased phosphorylation of various proteins, including AKT. Plays a role in regulating cardiac sarcoplasmic reticulum Ca(2+) uptake and storage, and is required for normal heart ventricular contractibility. May contribute to normal heart function (By similarity). Mediates vasodilatation after activation of beta-adrenergic receptors by isoproterenol (PubMed:17916776). Contributes to bone cell responses to mechanical stimuli (By similarity). {ECO:0000250|UniProtKB:Q01341, ECO:0000250|UniProtKB:Q03343, ECO:0000269|PubMed:17110384, ECO:0000269|PubMed:17916776}.
|
Homo sapiens (Human)
|
O43307
|
ARHG9_HUMAN
|
MTLLITGDSIVSAEAVWDHVTMANRELAFKAGDVIKVLDASNKDWWWGQIDDEEGWFPASFVRLWVNQEDEVEEGPSDVQNGHLDPNSDCLCLGRPLQNRDQMRANVINEIMSTERHYIKHLKDICEGYLKQCRKRRDMFSDEQLKVIFGNIEDIYRFQMGFVRDLEKQYNNDDPHLSEIGPCFLEHQDGFWIYSEYCNNHLDACMELSKLMKDSRYQHFFEACRLLQQMIDIAIDGFLLTPVQKICKYPLQLAELLKYTAQDHSDYRYVAAALAVMRNVTQQINERKRRLENIDKIAQWQASVLDWEGEDILDRSSELIYTGEMAWIYQPYGRNQQRVFFLFDHQMVLCKKDLIRRDILYYKGRIDMDKYEVVDIEDGRDDDFNVSMKNAFKLHNKETEEIHLFFAKKLEEKIRWLRAFREERKMVQEDEKIGFEISENQKRQAAMTVRKVPKQKGVNSARSVPPSYPPPQDPLNHGQYLVPDGIAQSQVFEFTEPKRSQSPFWQNFSRLTPFKK
| null | null |
regulation of postsynaptic specialization assembly [GO:0099150]; regulation of small GTPase mediated signal transduction [GO:0051056]
|
cytosol [GO:0005829]; GABA-ergic synapse [GO:0098982]; postsynaptic density [GO:0014069]; postsynaptic specialization [GO:0099572]
|
guanyl-nucleotide exchange factor activity [GO:0005085]
|
PF00169;PF00621;PF07653;
|
1.20.900.10;2.30.29.30;2.30.30.40;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10559246}. Postsynaptic density {ECO:0000250|UniProtKB:Q3UTH8}.
| null | null | null | null | null |
FUNCTION: Acts as a guanine nucleotide exchange factor (GEF) for CDC42. Promotes formation of GPHN clusters (By similarity). {ECO:0000250|UniProtKB:Q9QX73, ECO:0000269|PubMed:10559246}.
|
Homo sapiens (Human)
|
O43309
|
ZSC12_HUMAN
|
MASTWAIQAHMDQDEPLEVKIEEEKYTTRQDWDLRKNNTHSREVFRQYFRQFCYQETSGPREALSRLRELCHQWLRPETHTKEQILELLVLEQFLTILPEELQAWVQEQHPESGEEVVTVLEDLERELDEPGEQVSVHTGEQEMFLQETVRLRKEGEPSMSLQSMKAQPKYESPELESQQEQVLDVETGNEYGNLKQEVSEEMEPHGKTSSKFENDMSKSARCGETREPEEITEEPSACSREDKQPTCDENGVSLTENSDHTEHQRICPGEESYGCDDCGKAFSQHSHLIEHQRIHTGDRPYKCEECGKAFRGRTVLIRHKIIHTGEKPYKCNECGKAFGRWSALNQHQRLHTGEKHYHCNDCGKAFSQKAGLFHHIKIHTRDKPYQCTQCNKSFSRRSILTQHQGVHTGAKPYECNECGKAFVYNSSLVSHQEIHHKEKCYQCKECGKSFSQSGLIQHQRIHTGEKPYKCDVCEKAFIQRTSLTEHQRIHTGERPYKCDKCGKAFTQRSVLTEHQRIHTGERPYKCDECGNAFRGITSLIQHQRIHTGEKPYQCDECGKAFRQRSDLSKHQRIHNRRGTYVCKECGKSFRQNSALTQHQTIHKGEKSVSV
| null | null |
regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleus [GO:0005634]
|
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]
|
PF02023;PF00096;
|
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)
|
O43310
|
CTIF_HUMAN
|
MENSSAASASSEAGSSRSQEIEELERFIDSYVLEYQVQGLLADKTEGDGESERTQSHISQWTADCSEPLDSSCSFSRGRAPPQQNGSKDNSLDMLGTDIWAANTFDSFSGATWDLQPEKLDFTQFHRKVRHTPKQPLPHIDREGCGKGKLEDGDGINLNDIEKVLPAWQGYHPMPHEVEIAHTKKLFRRRRNDRRRQQRPPGGNKPQQHGDHQPGSAKHNRDHQKSYQGGSAPHPSGRPTHHGYSQNRRWHHGNMKHPPGDKGEAGAHRNAKETMTIENPKLEDTAGDTGHSSLEAPRSPDTLAPVASERLPPQQSGGPEVETKRKDSILPERIGERPKITLLQSSKDRLRRRLKEKDEVAVETTTPQQNKMDKLIEILNSMRNNSSDVDTKLTTFMEEAQNSTNSEEMLGEIVRTIYQKAVSDRSFAFTAAKLCDKMALFMVEGTKFRSLLLNMLQKDFTVREELQQQDVERWLGFITFLCEVFGTMRSSTGEPFRVLVCPIYTCLRELLQSQDVKEDAVLCCSMELQSTGRLLEEQLPEMMTELLASARDKMLCPSESMLTRSLLLEVIELHANSWNPLTPPITQYYNRTIQKLTA
| null | null |
nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; regulation of translational initiation [GO:0006446]
|
cytosol [GO:0005829]; perinuclear region of cytoplasm [GO:0048471]
|
RNA binding [GO:0003723]; translation activator activity [GO:0008494]
|
PF02854;
|
1.25.40.180;
|
CTIF family
| null |
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:19648179}.
| null | null | null | null | null |
FUNCTION: Specifically required for the pioneer round of mRNA translation mediated by the cap-binding complex (CBC), that takes place during or right after mRNA export via the nuclear pore complex (NPC). Acts via its interaction with the NCBP1/CBP80 component of the CBC complex and recruits the 40S small subunit of the ribosome via eIF3. In contrast, it is not involved in steady state translation, that takes place when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. Also required for nonsense-mediated mRNA decay (NMD), the pioneer round of mRNA translation mediated by the cap-binding complex playing a central role in nonsense-mediated mRNA decay (NMD). {ECO:0000269|PubMed:19648179}.
|
Homo sapiens (Human)
|
O43312
|
MTSS1_HUMAN
|
MEAVIEKECSALGGLFQTIISDMKGSYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGGTREIGSALTRMCMRHRSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKGRGDIQPQLDSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTISEDLKSLTMDPHKLPSSSEQVILDLKGSDYSWSYQTPPSSPSTTMSRKSSVCSSLNSVNSSDSRSSGSHSHSPSSHYRYRSSNLAQQAPVRLSSVSSHDSGFISQDAFQSKSPSPMPPEAPNQLSNGFSHYSLSSESHVGPTGAGLFPHCLPASRLLPRVTSVHLPDYAHYYTIGPGMFPSSQIPSWKDWAKPGPYDQPLVNTLQRRKEKREPDPNGGGPTTASGPPAAAEEAQRPRSMTVSAATRPGEEMEACEELALALSRGLQLDTQRSSRDSLQCSSGYSTQTTTPCCSEDTIPSQVSDYDYFSVSGDQEADQQEFDKSSTIPRNSDISQSYRRMFQAKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKTPTVPDLPGVLPAPPDGPEERGEHSPESPSVGEGPQGVTSMPSSMWSGQASVNPPLPGPKPSIPEEHRQAIPESEAEDQEREPPSATVSPGQIPESDPADLSPRDTPQGEDMLNAIRRGVKLKKTTTNDRSAPRFS
| null | null |
actin cytoskeleton organization [GO:0030036]; adherens junction maintenance [GO:0034334]; cell adhesion [GO:0007155]; cellular response to fluid shear stress [GO:0071498]; epithelial cell proliferation involved in renal tubule morphogenesis [GO:2001013]; glomerulus morphogenesis [GO:0072102]; microspike assembly [GO:0030035]; negative regulation of epithelial cell proliferation [GO:0050680]; nephron tubule epithelial cell differentiation [GO:0072160]; plasma membrane organization [GO:0007009]; positive regulation of actin filament bundle assembly [GO:0032233]; renal tubule morphogenesis [GO:0061333]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; endocytic vesicle [GO:0030139]; ruffle [GO:0001726]
|
actin binding [GO:0003779]; actin monomer binding [GO:0003785]; identical protein binding [GO:0042802]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102]
|
PF08397;PF02205;
|
1.20.1270.60;
|
MTSS family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
| null | null | null | null | null |
FUNCTION: May be related to cancer progression or tumor metastasis in a variety of organ sites, most likely through an interaction with the actin cytoskeleton.
|
Homo sapiens (Human)
|
O43313
|
ATMIN_HUMAN
|
MAASEAAAAAGSAALAAGARAVPAATTGAAAAASGPWVPPGPRLRGSRPRPAGATQQPAVPAPPAGELIQPSVSELSRAVRTNILCTVRGCGKILPNSPALNMHLVKSHRLQDGIVNPTIRKDLKTGPKFYCCPIEGCPRGPERPFSQFSLVKQHFMKMHAEKKHKCSKCSNSYGTEWDLKRHAEDCGKTFRCTCGCPYASRTALQSHIYRTGHEIPAEHRDPPSKKRKMENCAQNQKLSNKTIESLNNQPIPRPDTQELEASEIKLEPSFEDSCGSNTDKQTLTTPPRYPQKLLLPKPKVALVKLPVMQFSVMPVFVPTADSSAQPVVLGVDQGSATGAVHLMPLSVGTLILGLDSEACSLKESLPLFKIANPIAGEPISTGVQVNFGKSPSNPLQELGNTCQKNSISSINVQTDLSYASQNFIPSAQWATADSSVSSCSQTDLSFDSQVSLPISVHTQTFLPSSKVTSSIAAQTDAFMDTCFQSGGVSRETQTSGIESPTDDHVQMDQAGMCGDIFESVHSSYNVATGNIISNSLVAETVTHSLLPQNEPKTLNQDIEKSAPIINFSAQNSMLPSQNMTDNQTQTIDLLSDLENILSSNLPAQTLDHRSLLSDTNPGPDTQLPSGPAQNPGIDFDIEEFFSASNIQTQTEESELSTMTTEPVLESLDIETQTDFLLADTSAQSYGCRGNSNFLGLEMFDTQTQTDLNFFLDSSPHLPLGSILKHSSFSVSTDSSDTETQTEGVSTAKNIPALESKVQLNSTETQTMSSGFETLGSLFFTSNETQTAMDDFLLADLAWNTMESQFSSVETQTSAEPHTVSNF
| null | null |
DNA damage response [GO:0006974]; motile cilium assembly [GO:0044458]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of non-motile cilium assembly [GO:1902857]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nuclear body [GO:0016604]; 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]; dynein complex binding [GO:0070840]; metal ion binding [GO:0046872]; transcription cis-regulatory region binding [GO:0000976]
| null |
3.30.160.60;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15933716, ECO:0000269|PubMed:17525732}. Note=Nuclear, in discrete foci during G1 phase.
| null | null | null | null | null |
FUNCTION: Transcription factor. Plays a crucial role in cell survival and RAD51 foci formation in response to methylating DNA damage. Involved in regulating the activity of ATM in the absence of DNA damage. May play a role in stabilizing ATM. Binds to the DYNLL1 promoter and activates its transcription. {ECO:0000269|PubMed:15933716, ECO:0000269|PubMed:17525732, ECO:0000269|PubMed:22167198}.
|
Homo sapiens (Human)
|
O43314
|
VIP2_HUMAN
|
MSEAPRFFVGPEDTEINPGNYRHFFHHADEDDEEEDDSPPERQIVVGICSMAKKSKSKPMKEILERISLFKYITVVVFEEEVILNEPVENWPLCDCLISFHSKGFPLDKAVAYAKLRNPFVINDLNMQYLIQDRREVYSILQAEGILLPRYAILNRDPNNPKECNLIEGEDHVEVNGEVFQKPFVEKPVSAEDHNVYIYYPTSAGGGSQRLFRKIGSRSSVYSPESNVRKTGSYIYEEFMPTDGTDVKVYTVGPDYAHAEARKSPALDGKVERDSEGKEVRYPVILNAREKLIAWKVCLAFKQTVCGFDLLRANGQSYVCDVNGFSFVKNSMKYYDDCAKILGNIVMRELAPQFHIPWSIPLEAEDIPIVPTTSGTMMELRCVIAVIRHGDRTPKQKMKMEVRHQKFFDLFEKCDGYKSGKLKLKKPKQLQEVLDIARQLLMELGQNNDSEIEENKPKLEQLKTVLEMYGHFSGINRKVQLTYLPHGCPKTSSEEEDSRREEPSLLLVLKWGGELTPAGRVQAEELGRAFRCMYPGGQGDYAGFPGCGLLRLHSTYRHDLKIYASDEGRVQMTAAAFAKGLLALEGELTPILVQMVKSANMNGLLDSDSDSLSSCQQRVKARLHEILQKDRDFTAEDYEKLTPSGSISLIKSMHLIKNPVKTCDKVYSLIQSLTSQIRHRMEDPKSSDIQLYHSETLELMLRRWSKLEKDFKTKNGRYDISKIPDIYDCIKYDVQHNGSLKLENTMELYRLSKALADIVIPQEYGITKAEKLEIAKGYCTPLVRKIRSDLQRTQDDDTVNKLHPVYSRGVLSPERHVRTRLYFTSESHVHSLLSILRYGALCNESKDEQWKRAMDYLNVVNELNYMTQIVIMLYEDPNKDLSSEERFHVELHFSPGAKGCEEDKNLPSGYGYRPASRENEGRRPFKIDNDDEPHTSKRDEVDRAVILFKPMVSEPIHIHRKSPLPRSRKTATNDEESPLSVSSPEGTGTWLHYTSGVGTGRRRRRSGEQITSSPVSPKSLAFTSSIFGSWQQVVSENANYLRTPRTLVEQKQNPTVGSHCAGLFSTSVLGGSSSAPNLQDYARTHRKKLTSSGCIDDATRGSAVKRFSISFARHPTNGFELYSMVPSICPLETLHNALSLKQVDEFLASIASPSSDVPRKTAEISSTALRSSPIMRKKVSLNTYTPAKILPTPPATLKSTKASSKPATSGPSSAVVPNTSSRKKNITSKTETHEHKKNTGKKK
|
2.7.4.24
| null |
inositol metabolic process [GO:0006020]; inositol phosphate biosynthetic process [GO:0032958]; inositol phosphate metabolic process [GO:0043647]; phosphorylation [GO:0016310]; sensory perception of sound [GO:0007605]
|
cytosol [GO:0005829]
|
ATP binding [GO:0005524]; diphosphoinositol-pentakisphosphate kinase activity [GO:0033857]; inositol heptakisphosphate kinase activity [GO:0000829]; inositol hexakisphosphate 1-kinase activity [GO:0052723]; inositol hexakisphosphate 3-kinase activity [GO:0052724]; inositol hexakisphosphate 5-kinase activity [GO:0000832]; inositol hexakisphosphate kinase activity [GO:0000828]; inositol-1,3,4,5,6-pentakisphosphate kinase activity [GO:0000827]
|
PF00328;PF18086;
|
3.40.50.11950;3.30.470.20;3.40.50.1240;
|
Histidine acid phosphatase family, VIP1 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17690096}.
|
CATALYTIC ACTIVITY: Reaction=1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:37459, ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:74946, ChEBI:CHEBI:456216; EC=2.7.4.24; Evidence={ECO:0000269|PubMed:21222653, ECO:0000269|PubMed:29590114}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37460; Evidence={ECO:0000305|PubMed:29590114}; CATALYTIC ACTIVITY: Reaction=5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP + H(+) = 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate + ADP; Xref=Rhea:RHEA:10276, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58628, ChEBI:CHEBI:77983, ChEBI:CHEBI:456216; EC=2.7.4.24; Evidence={ECO:0000269|PubMed:21222653, ECO:0000269|PubMed:22119861, ECO:0000269|PubMed:29590114}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10277; Evidence={ECO:0000269|PubMed:22119861};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.13 uM for InsP6 {ECO:0000269|PubMed:17690096}; KM=0.19 uM for InsP7 {ECO:0000269|PubMed:17690096}; Vmax=0.39 nmol/min/mg enzyme with InsP6 as substrate {ECO:0000269|PubMed:17690096}; Vmax=1.38 nmol/min/mg enzyme with InsP7 as substrate {ECO:0000269|PubMed:17690096};
| null | null | null |
FUNCTION: Bifunctional inositol kinase that acts in concert with the IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4 (PubMed:17690096, PubMed:17702752, PubMed:21222653, PubMed:29590114). PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, exocytosis, insulin signaling and neutrophil activation (PubMed:17690096, PubMed:17702752, PubMed:21222653, PubMed:29590114). Phosphorylates inositol hexakisphosphate (InsP6) at position 1 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4 (PubMed:17690096, PubMed:17702752). Alternatively, phosphorylates PP-InsP5 at position 1, produced by IP6Ks from InsP6, to produce (PP)2-InsP4 (PubMed:17690096, PubMed:17702752). Required for normal hearing (PubMed:29590114). {ECO:0000269|PubMed:17690096, ECO:0000269|PubMed:17702752, ECO:0000269|PubMed:21222653, ECO:0000269|PubMed:29590114}.
|
Homo sapiens (Human)
|
O43315
|
AQP9_HUMAN
|
MQPEGAEKGKSFKQRLVLKSSLAKETLSEFLGTFILIVLGCGCVAQAILSRGRFGGVITINVGFSMAVAMAIYVAGGVSGGHINPAVSLAMCLFGRMKWFKLPFYVGAQFLGAFVGAATVFGIYYDGLMSFAGGKLLIVGENATAHIFATYPAPYLSLANAFADQVVATMILLIIVFAIFDSRNLGAPRGLEPIAIGLLIIVIASSLGLNSGCAMNPARDLSPRLFTALAGWGFEVFRAGNNFWWIPVVGPLVGAVIGGLIYVLVIEIHHPEPDSVFKTEQSEDKPEKYELSVIM
| null | null |
amine transport [GO:0015837]; canalicular bile acid transport [GO:0015722]; cellular response to cAMP [GO:0071320]; glycerol transmembrane transport [GO:0015793]; purine nucleobase transport [GO:0006863]; pyrimidine nucleobase transport [GO:0015855]; response to pain [GO:0048265]; urea transmembrane transport [GO:0071918]; water transport [GO:0006833]
|
basolateral plasma membrane [GO:0016323]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]
|
glycerol channel activity [GO:0015254]; purine nucleobase transmembrane transporter activity [GO:0005345]; pyrimidine nucleobase transmembrane transporter activity [GO:0005350]; urea channel activity [GO:0015265]; urea transmembrane transporter activity [GO:0015204]; water channel activity [GO:0015250]
|
PF00230;
|
1.20.1080.10;
|
MIP/aquaporin (TC 1.A.8) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10564231, ECO:0000269|PubMed:9514918}; Multi-pass membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Forms a water channel with a broad specificity. Also permeable glycerol and urea. Mediates passage of a wide variety of small, non-charged solutes including carbamides, polyols, purines, and pyrimidines. {ECO:0000269|PubMed:10564231, ECO:0000269|PubMed:30420639, ECO:0000269|PubMed:9514918}.
|
Homo sapiens (Human)
|
O43316
|
PAX4_HUMAN
|
MHQDGISSMNQLGGLFVNGRPLPLDTRQQIVRLAVSGMRPCDISRILKVSNGCVSKILGRYYRTGVLEPKGIGGSKPRLATPPVVARIAQLKGECPALFAWEIQRQLCAEGLCTQDKTPSVSSINRVLRALQEDQGLPCTRLRSPAVLAPAVLTPHSGSETPRGTHPGTGHRNRTIFSPSQAEALEKEFQRGQYPDSVARGKLATATSLPEDTVRVWFSNRRAKWRRQEKLKWEMQLPGASQGLTVPRVAPGIISAQQSPGSVPTAALPALEPLGPSCYQLCWATAPERCLSDTPPKACLKPCWDCGSFLLPVIAPSCVDVAWPCLDASLAHHLIGGAGKATPTHFSHWP
| null | null |
animal organ morphogenesis [GO:0009887]; cell differentiation [GO:0030154]; regulation of transcription by RNA polymerase II [GO:0006357]
|
chromatin [GO:0000785]; nucleoplasm [GO:0005654]
|
DNA binding [GO:0003677]; 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 double-stranded DNA binding [GO:1990837]
|
PF00046;PF00292;
|
1.10.10.60;1.10.10.10;
|
Paired homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Plays an important role in the differentiation and development of pancreatic islet beta cells. Transcriptional repressor that binds to a common element in the glucagon, insulin and somatostatin promoters. Competes with PAX6 for this same promoter binding site. Isoform 2 appears to be a dominant negative form antagonizing PAX4 transcriptional activity.
|
Homo sapiens (Human)
|
O43318
|
M3K7_HUMAN
|
MSTASAASSSSSSSAGEMIEAPSQVLNFEEIDYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYFPGADEPLQYPCQYSDEGQSNSATSTGSFMDIASTNTSNKSDTNMEQVPATNDTIKRLESKLLKNQAKQQSESGRLSLGASRGSSVESLPPTSEGKRMSADMSEIEARIAATTAYSKPKRGHRKTASFGNILDVPEIVISGNGQPRRRSIQDLTVTGTEPGQVSSRSSSPSVRMITTSGPTSEKPTRSHPWTPDDSTDTNGSDNSIPMAYLTLDHQLQPLAPCPNSKESMAVFEQHCKMAQEYMKVQTEIALLLQRKQELVAELDQDEKDQQNTSRLVQEHKKLLDENKSLSTYYQQCKKQLEVIRSQQQKRQGTS
|
2.7.11.25
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:16289117};
|
activation of NF-kappaB-inducing kinase activity [GO:0007250]; anoikis [GO:0043276]; canonical NF-kappaB signal transduction [GO:0007249]; cellular response to angiotensin [GO:1904385]; cellular response to hypoxia [GO:0071456]; cellular response to tumor necrosis factor [GO:0071356]; cytoplasmic pattern recognition receptor signaling pathway [GO:0002753]; defense response to bacterium [GO:0042742]; Fc-epsilon receptor signaling pathway [GO:0038095]; I-kappaB phosphorylation [GO:0007252]; immune response [GO:0006955]; inflammatory response [GO:0006954]; interleukin-1-mediated signaling pathway [GO:0070498]; interleukin-17A-mediated signaling pathway [GO:0038173]; interleukin-33-mediated signaling pathway [GO:0038172]; JNK cascade [GO:0007254]; MAPK cascade [GO:0000165]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; negative regulation of gene expression [GO:0010629]; nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [GO:0035872]; p38MAPK cascade [GO:0038066]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell cycle [GO:0045787]; positive regulation of cell size [GO:0045793]; positive regulation of cGAS/STING signaling pathway [GO:0141111]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of macroautophagy [GO:0016239]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of T cell cytokine production [GO:0002726]; positive regulation of vascular associated smooth muscle cell migration [GO:1904754]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; 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]; toll-like receptor 4 signaling pathway [GO:0034142]; transforming growth factor beta receptor signaling pathway [GO:0007179]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]
|
ATAC complex [GO:0140672]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; DNA-binding transcription factor binding [GO:0140297]; histone kinase activity [GO:0035173]; identical protein binding [GO:0042802]; linear polyubiquitin binding [GO:1990450]; magnesium ion binding [GO:0000287]; MAP kinase activity [GO:0004707]; MAP kinase kinase kinase activity [GO:0004709]; MAP kinase kinase kinase kinase activity [GO:0008349]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine kinase binding [GO:0120283]; receptor tyrosine kinase binding [GO:0030971]; scaffold protein binding [GO:0097110]; transcription coactivator binding [GO:0001223]; type II transforming growth factor beta receptor binding [GO:0005114]; ubiquitin protein ligase binding [GO:0031625]
|
PF07714;
|
1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily
|
PTM: Association with TAB1/MAP3K7IP1 promotes autophosphorylation at Ser-192 and subsequent activation. Association with TAB2/MAP3K7IP2, itself associated with free unanchored Lys-63 polyubiquitin chain, promotes autophosphorylation and subsequent activation of MAP3K7. Dephosphorylation at Ser-192 by PPM1B/PP2CB and at Thr-187 by PP2A and PPP6C leads to inactivation. {ECO:0000269|PubMed:10702308, ECO:0000269|PubMed:10838074, ECO:0000269|PubMed:16845370, ECO:0000269|PubMed:17548520, ECO:0000269|PubMed:19675569, ECO:0000269|PubMed:21512573, ECO:0000269|PubMed:37832545}.; PTM: 'Lys-48'-linked polyubiquitination at Lys-72 is induced by TNFalpha, and leads to proteasomal degradation. Undergoes 'Lys-48'-linked polyubiquitination catalyzed by ITCH (By similarity). Requires 'Lys-63'-linked polyubiquitination for autophosphorylation and subsequent activation. 'Lys-63'-linked ubiquitination does not lead to proteasomal degradation. Deubiquitinated by CYLD, a protease that selectively cleaves 'Lys-63'-linked ubiquitin chains. Deubiquitinated by Y.enterocolitica YopP. {ECO:0000250|UniProtKB:Q62073, ECO:0000269|PubMed:17548520, ECO:0000269|PubMed:22406003}.; PTM: (Microbial infection) Cleaved and inactivated by the proteases 3C of coxsackievirus A16 and human enterovirus D68, allowing the virus to disrupt TRAF6-triggered NF-kappa-B induction. {ECO:0000269|PubMed:28424289}.; PTM: (Microbial infection) Acetylation of Thr-184 and Thr-187 by Yersinia YopJ prevents phosphorylation and activation, thus blocking the MAPK signaling pathway. {ECO:0000269|PubMed:22520462, ECO:0000269|PubMed:22802624}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12242293}. Cell membrane {ECO:0000269|PubMed:12242293}; Peripheral membrane protein {ECO:0000269|PubMed:12242293}; Cytoplasmic side {ECO:0000269|PubMed:12242293}. Note=Although the majority of MAP3K7/TAK1 is found in the cytosol, when complexed with TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2, it is also localized at the cell membrane.
|
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=2.7.11.25; Evidence={ECO:0000269|PubMed:10094049, ECO:0000269|PubMed:10838074, ECO:0000269|PubMed:12589052, ECO:0000269|PubMed:37832545}; 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=2.7.11.25; Evidence={ECO:0000269|PubMed:10094049, ECO:0000269|PubMed:10838074, ECO:0000269|PubMed:12589052};
| null | null | null | null |
FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway (PubMed:10094049, PubMed:11460167, PubMed:12589052, PubMed:16845370, PubMed:16893890, PubMed:21512573, PubMed:8663074, PubMed:9079627). Plays an important role in the cascades of cellular responses evoked by changes in the environment (PubMed:10094049, PubMed:11460167, PubMed:12589052, PubMed:16845370, PubMed:16893890, PubMed:21512573, PubMed:8663074, PubMed:9079627). Mediates signal transduction of TRAF6, various cytokines including interleukin-1 (IL-1), transforming growth factor-beta (TGFB), TGFB-related factors like BMP2 and BMP4, toll-like receptors (TLR), tumor necrosis factor receptor CD40 and B-cell receptor (BCR) (PubMed:16893890, PubMed:9079627). Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K1/MEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7 (PubMed:11460167, PubMed:8663074). These MAP2Ks in turn activate p38 MAPKs and c-jun N-terminal kinases (JNKs); both p38 MAPK and JNK pathways control the transcription factors activator protein-1 (AP-1) (PubMed:11460167, PubMed:12589052, PubMed:8663074). Independently of MAP2Ks and p38 MAPKs, acts as a key activator of NF-kappa-B by promoting activation of the I-kappa-B-kinase (IKK) core complex (PubMed:12589052, PubMed:8663074). Mechanistically, recruited to polyubiquitin chains of RIPK2 and IKBKG/NEMO via TAB2/MAP3K7IP2 and TAB3/MAP3K7IP3, and catalyzes phosphorylation and activation of IKBKB/IKKB component of the IKK complex, leading to NF-kappa-B activation (PubMed:10094049, PubMed:11460167). In osmotic stress signaling, plays a major role in the activation of MAPK8/JNK1, but not that of NF-kappa-B (PubMed:16893890). Promotes TRIM5 capsid-specific restriction activity (PubMed:21512573). Phosphorylates RIPK1 at 'Ser-321' which positively regulates RIPK1 interaction with RIPK3 to promote necroptosis but negatively regulates RIPK1 kinase activity and its interaction with FADD to mediate apoptosis (By similarity). Phosphorylates STING1 in response to cGAMP-activation, promoting association between STEEP1 and STING1 and STING1 translocation to COPII vesicles (PubMed:37832545). {ECO:0000250|UniProtKB:Q62073, ECO:0000269|PubMed:10094049, ECO:0000269|PubMed:11460167, ECO:0000269|PubMed:12589052, ECO:0000269|PubMed:16845370, ECO:0000269|PubMed:16893890, ECO:0000269|PubMed:21512573, ECO:0000269|PubMed:37832545, ECO:0000269|PubMed:8663074, ECO:0000269|PubMed:9079627}.
|
Homo sapiens (Human)
|
O43320
|
FGF16_HUMAN
|
MAEVGGVFASLDWDLHGFSSSLGNVPLADSPGFLNERLGQIEGKLQRGSPTDFAHLKGILRRRQLYCRTGFHLEIFPNGTVHGTRHDHSRFGILEFISLAVGLISIRGVDSGLYLGMNERGELYGSKKLTRECVFREQFEENWYNTYASTLYKHSDSERQYYVALNKDGSPREGYRTKRHQKFTHFLPRPVDPSKLPSMSRDLFHYR
| null | null |
animal organ morphogenesis [GO:0009887]; cell differentiation [GO:0030154]; cell-cell signaling [GO:0007267]; fibroblast growth factor receptor signaling pathway [GO:0008543]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of endothelial cell chemotaxis to fibroblast growth factor [GO:2000546]; positive regulation of gene expression [GO:0010628]; positive regulation of protein phosphorylation [GO:0001934]; response to temperature stimulus [GO:0009266]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083]
|
PF00167;
|
2.80.10.50;
|
Heparin-binding growth factors family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O54769}.
| null | null | null | null | null |
FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation, and is required for normal cardiomyocyte proliferation and heart development. {ECO:0000269|PubMed:16597617}.
|
Homo sapiens (Human)
|
O43323
|
DHH_HUMAN
|
MALLTNLLPLCCLALLALPAQSCGPGRGPVGRRRYARKQLVPLLYKQFVPGVPERTLGASGPAEGRVARGSERFRDLVPNYNPDIIFKDEENSGADRLMTERCKERVNALAIAVMNMWPGVRLRVTEGWDEDGHHAQDSLHYEGRALDITTSDRDRNKYGLLARLAVEAGFDWVYYESRNHVHVSVKADNSLAVRAGGCFPGNATVRLWSGERKGLRELHRGDWVLAADASGRVVPTPVLLFLDRDLQRRASFVAVETEWPPRKLLLTPWHLVFAARGPAPAPGDFAPVFARRLRAGDSVLAPGGDALRPARVARVAREEAVGVFAPLTAHGTLLVNDVLASCYAVLESHQWAHRAFAPLRLLHALGALLPGGAVQPTGMHWYSRLLYRLAEELLG
|
3.1.-.-
| null |
cell fate specification [GO:0001708]; cell-cell signaling [GO:0007267]; Leydig cell differentiation [GO:0033327]; male sex determination [GO:0030238]; myelination [GO:0042552]; osteoblast differentiation [GO:0001649]; positive regulation of smoothened signaling pathway [GO:0045880]; protein autoprocessing [GO:0016540]; regulation of gene expression [GO:0010468]; regulation of steroid biosynthetic process [GO:0050810]; response to estradiol [GO:0032355]; response to estrogen [GO:0043627]; self proteolysis [GO:0097264]; smoothened signaling pathway [GO:0007224]; spermatid development [GO:0007286]
|
endoplasmic reticulum membrane [GO:0005789]; extracellular space [GO:0005615]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; cholesterol-protein transferase activity [GO:0140853]; patched binding [GO:0005113]; peptidase activity [GO:0008233]; zinc ion binding [GO:0008270]
|
PF01085;PF01079;
|
3.30.1380.10;2.170.16.10;
|
Hedgehog family
|
PTM: [Desert hedgehog protein]: Partially autoproteolyzed (PubMed:24342078, PubMed:30298535). The C-terminal domain displays an autoproteolysis activity and a cholesterol transferase activity (By similarity). Both activities result in the cleavage of the full-length protein and covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-terminal fragment (DhhN) (By similarity). {ECO:0000250|UniProtKB:Q15465, ECO:0000250|UniProtKB:Q62226, ECO:0000269|PubMed:24342078, ECO:0000269|PubMed:30298535}.; PTM: [Desert hedgehog protein N-product]: N-palmitoylation by HHAT of DhhN is required for desert hedgehog protein N-product multimerization and full activity (By similarity). {ECO:0000250|UniProtKB:Q62226}.
|
SUBCELLULAR LOCATION: [Desert hedgehog protein N-product]: Cell membrane {ECO:0000250|UniProtKB:Q62226}; Lipid-anchor {ECO:0000250|UniProtKB:Q62226}.; SUBCELLULAR LOCATION: [Desert hedgehog protein]: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15465}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q15465}. Secreted {ECO:0000269|PubMed:33063110}. Cell membrane {ECO:0000269|PubMed:24342078}. Note=Co-localizes with HHAT in the ER and Golgi membrane. {ECO:0000250|UniProtKB:Q15465}.
|
CATALYTIC ACTIVITY: [Desert hedgehog protein]: Reaction=cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]-C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl-[protein]; Xref=Rhea:RHEA:59504, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:15369, Rhea:RHEA-COMP:15374, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:65250, ChEBI:CHEBI:143135, ChEBI:CHEBI:143140; Evidence={ECO:0000250|UniProtKB:Q62226}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59505; Evidence={ECO:0000250|UniProtKB:Q62226};
| null | null | null | null |
FUNCTION: [Desert hedgehog protein]: The C-terminal part of the desert hedgehog protein precursor displays an autoproteolysis and a cholesterol transferase activity (By similarity). Both activities result in the cleavage of the full-length protein into two parts (N-product and C-product) followed by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). Both activities occur in the reticulum endoplasmic (By similarity). Functions in cell-cell mediated juxtacrine signaling (PubMed:24342078). Promotes endothelium integrity (PubMed:33063110). Binds to PTCH1 receptor, which functions in association with smoothened (SMO), to activate the transcription of target genes in endothelial cells (PubMed:33063110). In Schwann cells, controls the development of the peripheral nerve sheath and the transition of mesenchymal cells to form the epithelium-like structure of the perineurial tube (By similarity). {ECO:0000250|UniProtKB:Q61488, ECO:0000250|UniProtKB:Q62226, ECO:0000269|PubMed:24342078, ECO:0000269|PubMed:33063110}.; FUNCTION: [Desert hedgehog protein N-product]: The dually lipidated desert hedgehog protein N-product is essential for a variety of patterning events during development (By similarity). Binds to the patched (PTCH1) receptor, which functions in association with smoothened (SMO), to activate the transcription of target genes (PubMed:11472839, PubMed:33063110). Required for normal testis development and spermatogenesis, namely for the formation of adult-type Leydig cells and normal development of peritubular cells and seminiferous tubules (By similarity). Activates primary cilia signaling on neighboring valve interstitial cells through a paracrine mechanism (By similarity). May induce motor neurons in lateral neural tube and may have a polarizing activity (PubMed:11472839). Prevents the desert hedgehog protein precursor binding to PTCH1 (PubMed:33063110). {ECO:0000250|UniProtKB:Q15465, ECO:0000250|UniProtKB:Q61488, ECO:0000250|UniProtKB:Q62226, ECO:0000269|PubMed:11472839, ECO:0000269|PubMed:33063110}.
|
Homo sapiens (Human)
|
O43324
|
MCA3_HUMAN
|
MAAAAELSLLEKSLGLSKGNKYSAQGERQIPVLQTNNGPSLTGLTTIAAHLVKQANKEYLLGSTAEEKAIVQQWLEYRVTQVDGHSSKNDIHTLLKDLNSYLEDKVYLTGYNFTLADILLYYGLHRFIVDLTVQEKEKYLNVSRWFCHIQHYPGIRQHLSSVVFIKNRLYTNSH
| null | null |
cellular response to leukemia inhibitory factor [GO:1990830]; negative regulation of cell population proliferation [GO:0008285]; positive regulation of apoptotic process [GO:0043065]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of cellular senescence [GO:2000774]; positive regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043517]; translation [GO:0006412]
|
aminoacyl-tRNA synthetase multienzyme complex [GO:0017101]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
| null |
PF00043;
|
1.20.1050.10;3.40.30.90;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15680327}. Cytoplasm, cytosol {ECO:0000269|PubMed:19289464}. Nucleus {ECO:0000269|PubMed:15680327}. Note=Cytoplasmic under growth arrest conditions. Translocated into the nucleus when growth resumes (S phase) and following DNA damage.
| null | null | null | null | null |
FUNCTION: Positive modulator of ATM response to DNA damage. {ECO:0000250|UniProtKB:Q9D1M4}.
|
Homo sapiens (Human)
|
O43353
|
RIPK2_HUMAN
|
MNGEAICSALPTIPYHKLADLRYLSRGASGTVSSARHADWRVQVAVKHLHIHTPLLDSERKDVLREAEILHKARFSYILPILGICNEPEFLGIVTEYMPNGSLNELLHRKTEYPDVAWPLRFRILHEIALGVNYLHNMTPPLLHHDLKTQNILLDNEFHVKIADFGLSKWRMMSLSQSRSSKSAPEGGTIIYMPPENYEPGQKSRASIKHDIYSYAVITWEVLSRKQPFEDVTNPLQIMYSVSQGHRPVINEESLPYDIPHRARMISLIESGWAQNPDERPSFLKCLIELEPVLRTFEEITFLEAVIQLKKTKLQSVSSAIHLCDKKKMELSLNIPVNHGPQEESCGSSQLHENSGSPETSRSLPAPQDNDFLSRKAQDCYFMKLHHCPGNHSWDSTISGSQRAAFCDHKTTPCSSAIINPLSTAGNSERLQPGIAQQWIQSKREDIVNQMTEACLNQSLDALLSRDLIMKEDYELVSTKPTRTSKVRQLLDTTDIQGEEFAKVIVQKLKDNKQMGLQPYPEILVVSRSPSLNLLQNKSM
|
2.7.10.2; 2.7.11.1
| null |
activation of cysteine-type endopeptidase activity [GO:0097202]; adaptive immune response [GO:0002250]; apoptotic process [GO:0006915]; canonical NF-kappaB signal transduction [GO:0007249]; CD4-positive, alpha-beta T cell proliferation [GO:0035739]; cellular response to lipoteichoic acid [GO:0071223]; cellular response to muramyl dipeptide [GO:0071225]; cellular response to peptidoglycan [GO:0071224]; cytokine-mediated signaling pathway [GO:0019221]; defense response to bacterium [GO:0042742]; defense response to Gram-positive bacterium [GO:0050830]; ERK1 and ERK2 cascade [GO:0070371]; immature T cell proliferation in thymus [GO:0033080]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; JNK cascade [GO:0007254]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; nucleotide-binding oligomerization domain containing 1 signaling pathway [GO:0070427]; nucleotide-binding oligomerization domain containing 2 signaling pathway [GO:0070431]; phosphorylation [GO:0016310]; positive regulation of apoptotic process [GO:0043065]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of CD4-positive, alpha-beta T cell proliferation [GO:2000563]; positive regulation of chemokine production [GO:0032722]; positive regulation of cytokine-mediated signaling pathway [GO:0001961]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of immature T cell proliferation in thymus [GO:0033092]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of JNK cascade [GO:0046330]; positive regulation of macrophage cytokine production [GO:0060907]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of peptidyl-threonine phosphorylation [GO:0010800]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of protein binding [GO:0032092]; positive regulation of protein K63-linked ubiquitination [GO:1902523]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of stress-activated MAPK cascade [GO:0032874]; positive regulation of T-helper 1 cell differentiation [GO:0045627]; positive regulation of T-helper 1 type immune response [GO:0002827]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of type II interferon production [GO:0032729]; positive regulation of xenophagy [GO:1904417]; protein homooligomerization [GO:0051260]; response to exogenous dsRNA [GO:0043330]; response to interleukin-1 [GO:0070555]; response to interleukin-12 [GO:0070671]; response to interleukin-18 [GO:0070673]; signal transduction [GO:0007165]; stress-activated MAPK cascade [GO:0051403]; T cell receptor signaling pathway [GO:0050852]; toll-like receptor 2 signaling pathway [GO:0034134]; toll-like receptor 4 signaling pathway [GO:0034142]; xenophagy [GO:0098792]
|
cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; vesicle [GO:0031982]
|
ATP binding [GO:0005524]; CARD domain binding [GO:0050700]; caspase binding [GO:0089720]; identical protein binding [GO:0042802]; JUN kinase kinase kinase activity [GO:0004706]; LIM domain binding [GO:0030274]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein homodimerization activity [GO:0042803]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; signaling adaptor activity [GO:0035591]; signaling receptor binding [GO:0005102]
|
PF00619;PF07714;
|
1.10.533.10;1.10.510.10;
|
Protein kinase superfamily, TKL Ser/Thr protein kinase family
|
PTM: Polyubiquitinated via both 'Lys-63'- and 'Met-1'-linked polyubiquitin following recruitment by NOD1 or NOD2, creating docking sites for downstream effectors, triggering activation of the NF-kappa-B and MAP kinases signaling (PubMed:22607974, PubMed:29452636, PubMed:30026309). 'Lys-63'-linked polyubiquitination by XIAP is essential for NOD2 signaling and promotes recruitment of the LUBAC complex (PubMed:22607974, PubMed:29452636, PubMed:30026309). Also polyubiquitinated with 'Lys-63'-linked chains by PELI3, BIRC2/c-IAP1 and BIRC3/c-IAP2 (PubMed:19464198, PubMed:21931591). Ubiquitinated on Lys-209 via 'Lys-63'-linked by ITCH (PubMed:18079694, PubMed:19592251). Undergoes 'Lys-63'-linked deubiquitination by MYSM1 to attenuate NOD2-mediated inflammation and tissue damage (By similarity). Polyubiquitinated with 'Lys-63'-linked chains in response to Shigella infection, promoting its SQSTM1/p62-dependent autophagic degradation (PubMed:36221902). Undergoes 'Met-1'-linked polyubiquitination; the head-to-tail linear polyubiquitination is mediated by the LUBAC complex in response to NOD2 stimulation 'Met-1'-linked polyubiquitination (PubMed:23806334). 'Lys-63'-linked polyubiquitination by XIAP is required for recruimtent of the LUBAC complex and subsequent (PubMed:22607974). Linear polyubiquitination is restricted by FAM105B/otulin, probably to limit NOD2-dependent pro-inflammatory signaling activation of NF-kappa-B (PubMed:23806334). Ubiquitination at Lys-503 by ZNRF4 via 'Lys-48'-linked polyubiquitination promotes RIPK2 degradation by the proteasome; ubiquitination by ZNRF4 takes place during both acute and NOD2 tolerance conditions (PubMed:28656966). {ECO:0000250|UniProtKB:P58801, ECO:0000269|PubMed:18079694, ECO:0000269|PubMed:19464198, ECO:0000269|PubMed:19592251, ECO:0000269|PubMed:21931591, ECO:0000269|PubMed:22607974, ECO:0000269|PubMed:23806334, ECO:0000269|PubMed:28656966, ECO:0000269|PubMed:29452636, ECO:0000269|PubMed:30026309, ECO:0000269|PubMed:36221902}.; PTM: Autophosphorylated (PubMed:16824733, PubMed:21123652, PubMed:28545134, PubMed:29452636). Phosphorylated at Ser-176, either via autophosphorylation or by LRRK2, enhancing activity (PubMed:16824733, PubMed:27830463). Autophosphorylation at Tyr-474 is required for effective NOD2 signaling (PubMed:21123652). Autophosphorylation is however not essential for NOD2 signaling (PubMed:29452636). Phosphorylation at Tyr-381 by Src kinase CSK occurs in a ARHGEF2-dependent manner and is required for NOD2-dependent innate immune activation (PubMed:21887730). {ECO:0000269|PubMed:16824733, ECO:0000269|PubMed:21123652, ECO:0000269|PubMed:21887730, ECO:0000269|PubMed:27830463, ECO:0000269|PubMed:28545134, ECO:0000269|PubMed:29452636}.; PTM: Degraded via selective autophagy following interaction with IRGM (PubMed:36221902). IRGM promotes NOD1/NOD2-RIPK2 RIPosome recruitment to autophagosome membranes (PubMed:36221902). RIPK2 biquitinated via 'Lys-63'-linked chains is then recognized by SQSTM1/p62, leading to the SQSTM1/p62-dependent autophagic degradation of the NOD1/NOD2-RIPK2 RIPosome (PubMed:36221902). {ECO:0000269|PubMed:36221902}.; PTM: (Microbial infection) Acetylation of Ser-174, Ser-176 and Ser-178 by Yersinia YopJ prevents phosphorylation and activation, thereby promoting cell death. {ECO:0000269|PubMed:22520462}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21887730}. Cell membrane {ECO:0000269|PubMed:17355968}; Peripheral membrane protein {ECO:0000305|PubMed:17355968}. Endoplasmic reticulum {ECO:0000269|PubMed:28656966}. Note=Recruited to the cell membrane by NOD2 following stimulation by bacterial peptidoglycans. {ECO:0000269|PubMed:17355968}.
|
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:16824733}; 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; 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=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10027, ECO:0000269|PubMed:21123652};
| null | null | null | null |
FUNCTION: Serine/threonine/tyrosine-protein kinase that plays an essential role in modulation of innate and adaptive immune responses (PubMed:14638696, PubMed:17054981, PubMed:21123652, PubMed:28656966, PubMed:9575181, PubMed:9642260). Acts as a key effector of NOD1 and NOD2 signaling pathways: upon activation by bacterial peptidoglycans, NOD1 and NOD2 oligomerize and recruit RIPK2 via CARD-CARD domains, leading to the formation of RIPK2 filaments (PubMed:17054981, PubMed:17562858, PubMed:21123652, PubMed:22607974, PubMed:28656966, PubMed:29452636, PubMed:30026309). Once recruited, RIPK2 autophosphorylates and undergoes 'Lys-63'-linked polyubiquitination by E3 ubiquitin ligases XIAP, BIRC2 and BIRC3, as well as 'Met-1'-linked (linear) polyubiquitination by the LUBAC complex, becoming a scaffolding protein for downstream effectors (PubMed:22607974, PubMed:28545134, PubMed:29452636, PubMed:30026309, PubMed:30279485, PubMed:30478312). 'Met-1'-linked polyubiquitin chains attached to RIPK2 recruit IKBKG/NEMO, which undergoes 'Lys-63'-linked polyubiquitination in a RIPK2-dependent process (PubMed:17562858, PubMed:22607974, PubMed:29452636, PubMed:30026309). 'Lys-63'-linked polyubiquitin chains attached to RIPK2 serve as docking sites for TAB2 and TAB3 and mediate the recruitment of MAP3K7/TAK1 to IKBKG/NEMO, inducing subsequent activation of IKBKB/IKKB (PubMed:18079694). In turn, NF-kappa-B is released from NF-kappa-B inhibitors and translocates into the nucleus where it activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis (PubMed:18079694). The protein kinase activity is dispensable for the NOD1 and NOD2 signaling pathways (PubMed:29452636, PubMed:30026309). Contributes to the tyrosine phosphorylation of the guanine exchange factor ARHGEF2 through Src tyrosine kinase leading to NF-kappa-B activation by NOD2 (PubMed:21887730). Also involved in adaptive immunity: plays a role during engagement of the T-cell receptor (TCR) in promoting BCL10 phosphorylation and subsequent NF-kappa-B activation (PubMed:14638696). Plays a role in the inactivation of RHOA in response to NGFR signaling (PubMed:26646181). {ECO:0000269|PubMed:14638696, ECO:0000269|PubMed:17054981, ECO:0000269|PubMed:17562858, ECO:0000269|PubMed:18079694, ECO:0000269|PubMed:21123652, ECO:0000269|PubMed:21887730, ECO:0000269|PubMed:22607974, ECO:0000269|PubMed:26646181, ECO:0000269|PubMed:28545134, ECO:0000269|PubMed:28656966, ECO:0000269|PubMed:29452636, ECO:0000269|PubMed:30026309, ECO:0000269|PubMed:30279485, ECO:0000269|PubMed:30478312, ECO:0000269|PubMed:9575181, ECO:0000269|PubMed:9642260}.
|
Homo sapiens (Human)
|
O43364
|
HXA2_HUMAN
|
MNYEFEREIGFINSQPSLAECLTSFPPVADTFQSSSIKTSTLSHSTLIPPPFEQTIPSLNPGSHPRHGAGGRPKPSPAGSRGSPVPAGALQPPEYPWMKEKKAAKKTALLPAAAAAATAAATGPACLSHKESLEIADGSGGGSRRLRTAYTNTQLLELEKEFHFNKYLCRPRRVEIAALLDLTERQVKVWFQNRRMKHKRQTQCKENQNSEGKCKSLEDSEKVEEDEEEKTLFEQALSVSGALLEREGYTFQQNALSQQQAPNGHNGDSQSFPVSPLTSNEKNLKHFQHQSPTVPNCLSTMGQNCGAGLNNDSPEALEVPSLQDFSVFSTDSCLQLSDAVSPSLPGSLDSPVDISADSLDFFTDTLTTIDLQHLNY
| null | null |
anterior/posterior pattern specification [GO:0009952]; brain segmentation [GO:0035284]; cell fate determination [GO:0001709]; cellular response to retinoic acid [GO:0071300]; dorsal/ventral pattern formation [GO:0009953]; embryonic viscerocranium morphogenesis [GO:0048703]; middle ear morphogenesis [GO:0042474]; motor neuron axon guidance [GO:0008045]; muscle structure development [GO:0061061]; negative regulation of neuron differentiation [GO:0045665]; negative regulation of osteoblast differentiation [GO:0045668]; osteoblast development [GO:0002076]; pharyngeal system development [GO:0060037]; positive regulation of transcription by RNA polymerase II [GO:0045944]; rhombomere 2 development [GO:0021568]; rhombomere 3 morphogenesis [GO:0021658]; segment specification [GO:0007379]
|
chromatin [GO:0000785]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00046;
|
1.10.10.60;
|
Antp homeobox family, Proboscipedia subfamily
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
|
Homo sapiens (Human)
|
O43365
|
HXA3_HUMAN
|
MQKATYYDSSAIYGGYPYQAANGFAYNANQQPYPASAALGADGEYHRPACSLQSPSSAGGHPKAHELSEACLRTLSAPPSQPPSLGEPPLHPPPPQAAPPAPQPPQPAPQPPAPTPAAPPPPSSASPPQNASNNPTPANAAKSPLLNSPTVAKQIFPWMKESRQNTKQKTSSSSSGESCAGDKSPPGQASSKRARTAYTSAQLVELEKEFHFNRYLCRPRRVEMANLLNLTERQIKIWFQNRRMKYKKDQKGKGMLTSSGGQSPSRSPVPPGAGGYLNSMHSLVNSVPYEPQSPPPFSKPPQGTYGLPPASYPASLPSCAPPPPPQKRYTAAGAGAGGTPDYDPHAHGLQGNGSYGTPHIQGSPVFVGGSYVEPMSNSGPALFGLTHLPHAASGAMDYGGAGPLGSGHHHGPGPGEPHPTYTDLTGHHPSQGRIQEAPKLTHL
| null | null |
angiogenesis [GO:0001525]; animal organ formation [GO:0048645]; anterior/posterior pattern specification [GO:0009952]; blood vessel remodeling [GO:0001974]; cartilage development [GO:0051216]; embryonic skeletal system morphogenesis [GO:0048704]; gene expression [GO:0010467]; glossopharyngeal nerve morphogenesis [GO:0021615]; parathyroid gland development [GO:0060017]; positive regulation of stem cell proliferation [GO:2000648]; regulation of transcription by RNA polymerase II [GO:0006357]; specification of animal organ position [GO:0010159]; stem cell proliferation [GO:0072089]; thymus development [GO:0048538]; thyroid gland development [GO:0030878]
|
chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; HMG box domain binding [GO:0071837]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF13293;PF00046;
|
1.10.10.60;
|
Antp homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
|
Homo sapiens (Human)
|
O43374
|
RASL2_HUMAN
|
MAKRSSLYIRIVEGKNLPAKDITGSSDPYCIVKVDNEPIIRTATVWKTLCPFWGEEYQVHLPPTFHAVAFYVMDEDALSRDDVIGKVCLTRDTIASHPKGFSGWAHLTEVDPDEEVQGEIHLRLEVWPGARACRLRCSVLEARDLAPKDRNGTSDPFVRVRYKGRTRETSIVKKSCYPRWNETFEFELQEGAMEALCVEAWDWDLVSRNDFLGKVVIDVQRLRVVQQEEGWFRLQPDQSKSRRHDEGNLGSLQLEVRLRDETVLPSSYYQPLVHLLCHEVKLGMQGPGQLIPLIEETTSTECRQDVATNLLKLFLGQGLAKDFLDLLFQLELSRTSETNTLFRSNSLASKSMESFLKVAGMQYLHGVLGPIINKVFEEKKYVELDPSKVEVKDVGCSGLHRPQTEAEVLEQSAQTLRAHLGALLSALSRSVRACPAVVRATFRQLFRRVRERFPGAQHENVPFIAVTSFLCLRFFSPAIMSPKLFHLRERHADARTSRTLLLLAKAVQNVGNMDTPASRAKEAWMEPLQPTVRQGVAQLKDFITKLVDIEEKDELDLQRTLSLQAPPVKEGPLFIHRTKGKGPLMSSSFKKLYFSLTTEALSFAKTPSSKKSALIKLANIRAAEKVEEKSFGGSHVMQVIYTDDAGRPQTAYLQCKCVNELNQWLSALRKVSINNTGLLGSYHPGVFRGDKWSCCHQKEKTGQGCDKTRSRVTLQEWNDPLDHDLEAQLIYRHLLGVEAMLWERHRELSGGAEAGTVPTSPGKVPEDSLARLLRVLQDLREAHSSSPAGSPPSEPNCLLELQT
| null |
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; Note=Binds 3 Ca(2+) ions per C2 domain. {ECO:0000255|PROSITE-ProRule:PRU00041};
|
cellular response to calcium ion [GO:0071277]; intracellular signal transduction [GO:0035556]; negative regulation of GTPase activity [GO:0034260]; negative regulation of Ras protein signal transduction [GO:0046580]
|
cytosol [GO:0005829]; plasma membrane [GO:0005886]
|
GTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]; phospholipid binding [GO:0005543]
|
PF00779;PF00168;PF00169;PF00616;
|
2.60.40.150;2.30.29.30;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11448776}. Cell membrane {ECO:0000269|PubMed:11448776}; Peripheral membrane protein {ECO:0000269|PubMed:11448776}. Note=Localized to the cytosol as a result of its lack of phosphoinositide binding activity. Upon agonist-stimulated calcium mobilization, utilizes the C2A and C2B domains to associate with the plasma membrane.
| null | null | null | null | null |
FUNCTION: Ca(2+)-dependent Ras GTPase-activating protein, that switches off the Ras-MAPK pathway following a stimulus that elevates intracellular calcium. Functions as an adaptor for Cdc42 and Rac1 during FcR-mediated phagocytosis. {ECO:0000269|PubMed:11448776}.
|
Homo sapiens (Human)
|
O43379
|
WDR62_HUMAN
|
MAAVGSGGYARNDAGEKLPSVMAGVPARRGQSSPPPAPPICLRRRTRLSTASEETVQNRVSLEKVLGITAQNSSGLTCDPGTGHVAYLAGCVVVILDPKENKQQHIFNTARKSLSALAFSPDGKYIVTGENGHRPAVRIWDVEEKNQVAEMLGHKYGVACVAFSPNMKHIVSMGYQHDMVLNVWDWKKDIVVASNKVSCRVIALSFSEDSSYFVTVGNRHVRFWFLEVSTETKVTSTVPLVGRSGILGELHNNIFCGVACGRGRMAGSTFCVSYSGLLCQFNEKRVLEKWINLKVSLSSCLCVSQELIFCGCTDGIVRIFQAHSLHYLANLPKPHYLGVDVAQGLEPSFLFHRKAEAVYPDTVALTFDPIHQWLSCVYKDHSIYIWDVKDINRVGKVWSELFHSSYVWNVEVYPEFEDQRACLPSGSFLTCSSDNTIRFWNLDSSPDSHWQKNIFSNTLLKVVYVENDIQHLQDMSHFPDRGSENGTPMDVKAGVRVMQVSPDGQHLASGDRSGNLRIHELHFMDELVKVEAHDAEVLCLEYSKPETGLTLLASASRDRLIHVLNVEKNYNLEQTLDDHSSSITAIKFAGNRDIQMISCGADKSIYFRSAQQGSDGLHFVRTHHVAEKTTLYDMDIDITQKYVAVACQDRNVRVYNTVNGKQKKCYKGSQGDEGSLLKVHVDPSGTFLATSCSDKSISVIDFYSGECIAKMFGHSEIITSMKFTYDCHHLITVSGDSCVFIWHLGPEITNCMKQHLLEIDHRQQQQHTNDKKRSGHPRQDTYVSTPSEIHSLSPGEQTEDDLEEECEPEEMLKTPSKDSLDPDPRCLLTNGKLPLWAKRLLGDDDVADGLAFHAKRSYQPHGRWAERAGQEPLKTILDAQDLDCYFTPMKPESLENSILDSLEPQSLASLLSESESPQEAGRGHPSFLPQQKESSEASELILYSLEAEVTVTGTDSQYCRKEVEAGPGDQQGDSYLRVSSDSPKDQSPPEDSGESEADLECSFAAIHSPAPPPDPAPRFATSLPHFPGCAGPTEDELSLPEGPSVPSSSLPQTPEQEKFLRHHFETLTESPCRALGDVEASEAEDHFFNPRLSISTQFLSSLQKASRFTHTFPPRATQCLVKSPEVKLMDRGGSQPRAGTGYASPDRTHVLAAGKAEETLEAWRPPPPCLTSLASCVPASSVLPTDRNLPTPTSAPTPGLAQGVHAPSTCSYMEATASSRARISRSISLGDSEGPIVATLAQPLRRPSSVGELASLGQELQAITTATTPSLDSEGQEPALRSWGNHEARANLRLTLSSACDGLLQPPVDTQPGVTVPAVSFPAPSPVEESALRLHGSAFRPSLPAPESPGLPAHPSNPQLPEARPGIPGGTASLLEPTSGALGLLQGSPARWSEPWVPVEALPPSPLELSRVGNILHRLQTTFQEALDLYRVLVSSGQVDTGQQQARTELVSTFLWIHSQLEAECLVGTSVAPAQALPSPGPPSPPTLYPLASPDLQALLEHYSELLVQAVRRKARGH
| null | null |
centriole replication [GO:0007099]; cerebral cortex development [GO:0021987]; mitotic spindle organization [GO:0007052]; neurogenesis [GO:0022008]; positive regulation of neuroblast proliferation [GO:0002052]; positive regulation of neuron migration [GO:2001224]; regulation of centrosome cycle [GO:0046605]; regulation of neuron differentiation [GO:0045664]
|
centriolar satellite [GO:0034451]; centriole [GO:0005814]; centrosome [GO:0005813]; cytosol [GO:0005829]; mitotic spindle [GO:0072686]; nucleus [GO:0005634]; spindle pole [GO:0000922]
| null |
PF12894;PF00400;
|
2.130.10.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20729831, ECO:0000269|PubMed:21496009}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:20890278, ECO:0000269|PubMed:20890279, ECO:0000269|PubMed:28089251}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20890278, ECO:0000269|PubMed:21496009, ECO:0000269|PubMed:26297806}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:26297806}. Note=Shows cell cycle-dependent localization. Accumulates to the spindle pole during mitosis. Colocalizes with CDK5RAP2, CEP152 and WDR62 in a discrete ring around the proximal end of the parental centriole. At this site, a cohesive structure is predicted to engage parental centrioles and procentrioles. {ECO:0000269|PubMed:20890278, ECO:0000269|PubMed:26297806}.
| null | null | null | null | null |
FUNCTION: Required for cerebral cortical development. Plays a role in neuronal proliferation and migration (PubMed:20729831, PubMed:20890278). Plays a role in mother-centriole-dependent centriole duplication; the function seems also to involve CEP152, CDK5RAP2 and CEP63 through a stepwise assembled complex at the centrosome that recruits CDK2 required for centriole duplication (PubMed:26297806). {ECO:0000269|PubMed:20729831, ECO:0000269|PubMed:20890278, ECO:0000269|PubMed:26297806}.
|
Homo sapiens (Human)
|
O43390
|
HNRPR_HUMAN
|
MANQVNGNAVQLKEEEEPMDTSSVTHTEHYKTLIEAGLPQKVAERLDEIFQTGLVAYVDLDERAIDALREFNEEGALSVLQQFKESDLSHVQNKSAFLCGVMKTYRQREKQGSKVQESTKGPDEAKIKALLERTGYTLDVTTGQRKYGGPPPDSVYSGVQPGIGTEVFVGKIPRDLYEDELVPLFEKAGPIWDLRLMMDPLSGQNRGYAFITFCGKEAAQEAVKLCDSYEIRPGKHLGVCISVANNRLFVGSIPKNKTKENILEEFSKVTEGLVDVILYHQPDDKKKNRGFCFLEYEDHKSAAQARRRLMSGKVKVWGNVVTVEWADPVEEPDPEVMAKVKVLFVRNLATTVTEEILEKSFSEFGKLERVKKLKDYAFVHFEDRGAAVKAMDEMNGKEIEGEEIEIVLAKPPDKKRKERQAARQASRSTAYEDYYYHPPPRMPPPIRGRGRGGGRGGYGYPPDYYGYEDYYDDYYGYDYHDYRGGYEDPYYGYDDGYAVRGRGGGRGGRGAPPPPRGRGAPPPRGRAGYSQRGAPLGPPRGSRGGRGGPAQQQRGRGSRGSRGNRGGNVGGKRKADGYNQPDSKRRQTNNQQNWGSQPIAQQPLQQGGDYSGNYGYNNDNQEFYQDTYGQQWK
| null | null |
mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]
|
catalytic step 2 spliceosome [GO:0071013]; endoplasmic reticulum [GO:0005783]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]; spliceosomal complex [GO:0005681]
|
mRNA binding [GO:0003729]; RNA binding [GO:0003723]
|
PF18360;PF00076;
|
3.30.70.330;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31079900}. Microsome {ECO:0000250|UniProtKB:Q7TMK9}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17289661}. Cytoplasm {ECO:0000269|PubMed:17289661}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. The tyrosine phosphorylated form bound to RNA is found in microsomes (By similarity). {ECO:0000250|UniProtKB:Q7TMK9, ECO:0000269|PubMed:17289661}.
| null | null | null | null | null |
FUNCTION: Component of ribonucleosomes, which are complexes of at least 20 other different heterogeneous nuclear ribonucleoproteins (hnRNP). hnRNP play an important role in processing of precursor mRNA in the nucleus.
|
Homo sapiens (Human)
|
O43395
|
PRPF3_HUMAN
|
MALSKRELDELKPWIEKTVKRVLGFSEPTVVTAALNCVGKGMDKKKAADHLKPFLDDSTLRFVDKLFEAVEEGRSSRHSKSSSDRSRKRELKEVFGDDSEISKESSGVKKRRIPRFEEVEEEPEVIPGPPSESPGMLTKLQIKQMMEAATRQIEERKKQLSFISPPTPQPKTPSSSQPERLPIGNTIQPSQAATFMNDAIEKARKAAELQARIQAQLALKPGLIGNANMVGLANLHAMGIAPPKVELKDQTKPTPLILDEQGRTVDATGKEIELTHRMPTLKANIRAVKREQFKQQLKEKPSEDMESNTFFDPRVSIAPSQRQRRTFKFHDKGKFEKIAQRLRTKAQLEKLQAEISQAARKTGIHTSTRLALIAPKKELKEGDIPEIEWWDSYIIPNGFDLTEENPKREDYFGITNLVEHPAQLNPPVDNDTPVTLGVYLTKKEQKKLRRQTRREAQKELQEKVRLGLMPPPEPKVRISNLMRVLGTEAVQDPTKVEAHVRAQMAKRQKAHEEANAARKLTAEQRKVKKIKKLKEDISQGVHISVYRVRNLSNPAKKFKIEANAGQLYLTGVVVLHKDVNVVVVEGGPKAQKKFKRLMLHRIKWDEQTSNTKGDDDEESDEEAVKKTNKCVLVWEGTAKDRSFGEMKFKQCPTENMAREHFKKHGAEHYWDLALSESVLESTD
| null | null |
mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]; spliceosomal tri-snRNP complex assembly [GO:0000244]
|
Cajal body [GO:0015030]; cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]; U2-type precatalytic spliceosome [GO:0071005]; U4/U6 x U5 tri-snRNP complex [GO:0046540]
|
identical protein binding [GO:0042802]; RNA binding [GO:0003723]
|
PF08572;PF06544;PF01480;
|
1.20.1390.10;
| null |
PTM: Ubiquitinated. Undergoes 'Lys-63'-linked polyubiquitination by PRPF19 and deubiquitination by USP4. 'Lys-63'-linked ubiquitination increases the affinity for PRPF8 and may regulate the assembly of the U4/U6-U5 tri-snRNP complex. {ECO:0000269|PubMed:20595234}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17932117, ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:9328476, ECO:0000269|PubMed:9404889}. Nucleus speckle.
| null | null | null | null | null |
FUNCTION: Plays a role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). {ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166, ECO:0000305|PubMed:20595234}.
|
Homo sapiens (Human)
|
O43396
|
TXNL1_HUMAN
|
MVGVKPVGSDPDFQPELSGAGSRLAVVKFTMRGCGPCLRIAPAFSSMSNKYPQAVFLEVDVHQCQGTAATNNISATPTFLFFRNKVRIDQYQGADAVGLEEKIKQHLENDPGSNEDTDIPKGYMDLMPFINKAGCECLNESDEHGFDNCLRKDTTFLESDCDEQLLITVAFNQPVKLYSMKFQGPDNGQGPKYVKIFINLPRSMDFEEAERSEPTQALELTEDDIKEDGIVPLRYVKFQNVNSVTIFVQSNQGEEETTRISYFTFIGTPVQATNMNDFKRVVGKKGESH
| null | null | null |
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; proteasome complex [GO:0000502]
|
disulfide oxidoreductase activity [GO:0015036]; protein-disulfide reductase activity [GO:0015035]
|
PF06201;PF00085;
|
3.40.30.10;2.60.120.470;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19349277}. Nucleus {ECO:0000269|PubMed:19349277}. Note=At least 85% of the cellular TXNL1 is proteasome-associated.
| null | null | null | null | null |
FUNCTION: Active thioredoxin with a redox potential of about -250 mV. {ECO:0000269|PubMed:19349277}.
|
Homo sapiens (Human)
|
O43399
|
TPD54_HUMAN
|
MDSAGQDINLNSPNKGLLSDSMTDVPVDTGVAARTPAVEGLTEAEEEELRAELTKVEEEIVTLRQVLAAKERHCGELKRRLGLSTLGELKQNLSRSWHDVQVSSAYVKTSEKLGEWNEKVTQSDLYKKTQETLSQAGQKTSAALSTVGSAISRKLGDMRNSATFKSFEDRVGTIKSKVVGDRENGSDNLPSSAGSGDKPLSDPAPF
| null | null |
carbohydrate metabolic process [GO:0005975]; regulation of cell population proliferation [GO:0042127]
|
cytoplasm [GO:0005737]; perinuclear region of cytoplasm [GO:0048471]
|
protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723]
|
PF04201;
|
1.50.10.10;
|
TPD52 family
| null | null | null | null | null | null | null | null |
Homo sapiens (Human)
|
O43402
|
EMC8_HUMAN
|
MPGVKLTTQAYCKMVLHGAKYPHCAVNGLLVAEKQKPRKEHLPLGGPGAHHTLFVDCIPLFHGTLALAPMLEVALTLIDSWCKDHSYVIAGYYQANERVKDASPNQVAEKVASRIAEGFSDTALIMVDNTKFTMDCVAPTIHVYEHHENRWRCRDPHHDYCEDWPEAQRISASLLDSRSYETLVDFDNHLDDIRNDWTNPEINKAVLHLC
| null | null |
protein insertion into ER membrane by stop-transfer membrane-anchor sequence [GO:0045050]; tail-anchored membrane protein insertion into ER membrane [GO:0071816]
|
cytoplasm [GO:0005737]; EMC complex [GO:0072546]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]
| null |
PF03665;
| null |
EMC8/EMC9 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22119785}; Peripheral membrane protein {ECO:0000305|PubMed:32439656}; Cytoplasmic side {ECO:0000269|PubMed:32439656}.
| null | null | null | null | null |
FUNCTION: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins (PubMed:29242231, PubMed:29809151, PubMed:30415835, PubMed:32439656, PubMed:32459176). Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues (PubMed:29242231, PubMed:29809151, PubMed:30415835). Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices (PubMed:29809151, PubMed:30415835). It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes (PubMed:29242231, PubMed:29809151). By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors (PubMed:30415835). By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes (Probable). {ECO:0000269|PubMed:29242231, ECO:0000269|PubMed:29809151, ECO:0000269|PubMed:30415835, ECO:0000269|PubMed:32439656, ECO:0000269|PubMed:32459176, ECO:0000305}.
|
Homo sapiens (Human)
|
O43405
|
COCH_HUMAN
|
MSAAWIPALGLGVCLLLLPGPAGSEGAAPIAITCFTRGLDIRKEKADVLCPGGCPLEEFSVYGNIVYASVSSICGAAVHRGVISNSGGPVRVYSLPGRENYSSVDANGIQSQMLSRWSASFTVTKGKSSTQEATGQAVSTAHPPTGKRLKKTPEKKTGNKDCKADIAFLIDGSFNIGQRRFNLQKNFVGKVALMLGIGTEGPHVGLVQASEHPKIEFYLKNFTSAKDVLFAIKEVGFRGGNSNTGKALKHTAQKFFTVDAGVRKGIPKVVVVFIDGWPSDDIEEAGIVAREFGVNVFIVSVAKPIPEELGMVQDVTFVDKAVCRNNGFFSYHMPNWFGTTKYVKPLVQKLCTHEQMMCSKTCYNSVNIAFLIDGSSSVGDSNFRLMLEFVSNIAKTFEISDIGAKIAAVQFTYDQRTEFSFTDYSTKENVLAVIRNIRYMSGGTATGDAISFTVRNVFGPIRESPNKNFLVIVTDGQSYDDVQGPAAAAHDAGITIFSVGVAWAPLDDLKDMASKPKESHAFFTREFTGLEPIVSDVIRGICRDFLESQQ
| null | null |
regulation of cell shape [GO:0008360]; sensory perception of sound [GO:0007605]
|
collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]
|
collagen binding [GO:0005518]
|
PF03815;PF00092;
|
2.170.130.20;3.40.50.410;
| null |
PTM: N-glycosylated. {ECO:0000269|PubMed:12843317}.; PTM: A 50 kDa form is created by proteolytic cleavage. {ECO:0000269|PubMed:12843317}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:12843317, ECO:0000269|PubMed:22610276}.
| null | null | null | null | null |
FUNCTION: Plays a role in the control of cell shape and motility in the trabecular meshwork. {ECO:0000269|PubMed:21886777}.
|
Homo sapiens (Human)
|
O43422
|
P52K_HUMAN
|
MPNFCAAPNCTRKSTQSDLAFFRFPRDPARCQKWVENCRRADLEDKTPDQLNKHYRLCAKHFETSMICRTSPYRTVLRDNAIPTIFDLTSHLNNPHSRHRKRIKELSEDEIRTLKQKKIDETSEQEQKHKETNNSNAQNPSEEEGEGQDEDILPLTLEEKENKEYLKSLFEILILMGKQNIPLDGHEADEIPEGLFTPDNFQALLECRINSGEEVLRKRFETTAVNTLFCSKTQQRQMLEICESCIREETLREVRDSHFFSIITDDVVDIAGEEHLPVLVRFVDESHNLREEFIGFLPYEADAEILAVKFHTMITEKWGLNMEYCRGQAYIVSSGFSSKMKVVASRLLEKYPQAIYTLCSSCALNMWLAKSVPVMGVSVALGTIEEVCSFFHRSPQLLLELDNVISVLFQNSKERGKELKEICHSQWTGRHDAFEILVELLQALVLCLDGINSDTNIRWNNYIAGRAFVLCSAVSDFDFIVTIVVLKNVLSFTRAFGKNLQGQTSDVFFAAGSLTAVLHSLNEVMENIEVYHEFWFEEATNLATKLDIQMKLPGKFRRAHQGNLESQLTSESYYKETLSVPTVEHIIQELKDIFSEQHLKALKCLSLVPSVMGQLKFNTSEEHHADMYRSDLPNPDTLSAELHCWRIKWKHRGKDIELPSTIYEALHLPDIKFFPNVYALLKVLCILPVMKVENERYENGRKRLKAYLRNTLTDQRSSNLALLNINFDIKHDLDLMVDTYIKLYTSKSELPTDNSETVENT
| null | null |
negative regulation of cell population proliferation [GO:0008285]; signal transduction [GO:0007165]
|
nucleus [GO:0005634]
|
DNA binding [GO:0003677]; metal ion binding [GO:0046872]; protein dimerization activity [GO:0046983]
|
PF05699;PF14291;PF05485;
| null | null | null | null | null | null | null | null | null |
FUNCTION: Upstream regulator of interferon-induced serine/threonine protein kinase R (PKR). May block the PKR-inhibitory function of DNAJC3, resulting in restoration of kinase activity and suppression of cell growth.
|
Homo sapiens (Human)
|
O43424
|
GRID2_HUMAN
|
MEVFPFLLVLSVWWSRTWDSANADSIIHIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQSLADAMHIPHLFIQRSTAGTPRSGCGLTRSNRNDDYTLSVRPPVYLHDVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDKVSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTLRRAILVMNPATAKSFITEVVETNLVAFDCHWIIINEEINDVDVQELVRRSIGRLTIIRQTFPVPQNISQRCFRGNHRISSTLCDPKDPFAQNMEISNLYIYDTVLLLANAFHKKLEDRKWHSMASLSCIRKNSKPWQGGRSMLETIKKGGVSGLTGELEFGENGGNPNVHFEILGTNYGEELGRGVRKLGCWNPVTGLNGSLTDKKLENNMRGVVLRVVTVLEEPFVMVSENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYMDYSVGVLLRRAEKTVDMFACLAPFDLSLWACIAGTVLLVGLLVYLLNWLNPPRLQMGSMTSTTLYNSMWFVYGSFVQQGGEVPYTTLATRMMMGAWWLFALIVISSYTANLAAFLTITRIESSIQSLQDLSKQTEIPYGTVLDSAVYEHVRMKGLNPFERDSMYSQMWRMINRSNGSENNVLESQAGIQKVKYGNYAFVWDAAVLEYVAINDPDCSFYTIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWWPKNGQCDLYSSVDTKQKGGALDIKSFAGVFCILAAGIVLSCFIAMLETWWNKRKGSRVPSKEDDKEIDLEHLHRRVNSLCTDDDSPHKQFSTSSIDLTPLDIDTLPTRQALEQISDFRNTHITTTTFIPEQIQTLSRTLSAKAASGFTFGNVPEHRTGPFRHRAPNGGFFRSPIKTMSSIPYQPTPTLGLNLGNDPDRGTSI
| null | null |
cerebellar granule cell differentiation [GO:0021707]; excitatory postsynaptic potential [GO:0060079]; excitatory synapse assembly [GO:1904861]; glutamate receptor signaling pathway [GO:0007215]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; modulation of chemical synaptic transmission [GO:0050804]; positive regulation of long-term synaptic depression [GO:1900454]; positive regulation of synapse assembly [GO:0051965]; prepulse inhibition [GO:0060134]; protein localization [GO:0008104]; regulation of neuron apoptotic process [GO:0043523]; regulation of neuron projection development [GO:0010975]; regulation of postsynaptic density assembly [GO:0099151]; regulation of presynapse assembly [GO:1905606]; synaptic transmission, glutamatergic [GO:0035249]
|
dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; ionotropic glutamate receptor complex [GO:0008328]; parallel fiber to Purkinje cell synapse [GO:0098688]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; synapse [GO:0045202]
|
glutamate receptor activity [GO:0008066]; identical protein binding [GO:0042802]; PDZ domain binding [GO:0030165]; scaffold protein binding [GO:0097110]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315]
|
PF01094;PF00060;PF10613;
|
1.10.287.70;3.40.50.2300;3.40.190.10;
|
Glutamate-gated ion channel (TC 1.A.10.1) family, GRID2 subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. Promotes synaptogenesis and mediates the D-Serine-dependent long term depression signals and AMPA receptor endocytosis of cerebellar parallel fiber-Purkinje cell (PF-PC) synapses through the beta-NRX1-CBLN1-GRID2 triad complex (PubMed:27418511). {ECO:0000269|PubMed:27418511}.
|
Homo sapiens (Human)
|
O43426
|
SYNJ1_HUMAN
|
MAFSKGFRIYHKLDPPPFSLIVETRHKEECLMFESGAVAVLSSAEKEAIKGTYSKVLDAYGLLGVLRLNLGDTMLHYLVLVTGCMSVGKIQESEVFRVTSTEFISLRIDSSDEDRISEVRKVLNSGNFYFAWSASGISLDLSLNAHRSMQEQTTDNRFFWNQSLHLHLKHYGVNCDDWLLRLMCGGVEIRTIYAAHKQAKACLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVVYLDDSVSSFIQIRGSVPLFWEQPGLQVGSHRVRMSRGFEANAPAFDRHFRTLKNLYGKQIIVNLLGSKEGEHMLSKAFQSHLKASEHAADIQMVNFDYHQMVKGGKAEKLHSVLKPQVQKFLDYGFFYFNGSEVQRCQSGTVRTNCLDCLDRTNSVQAFLGLEMLAKQLEALGLAEKPQLVTRFQEVFRSMWSVNGDSISKIYAGTGALEGKAKLKDGARSVTRTIQNNFFDSSKQEAIDVLLLGNTLNSDLADKARALLTTGSLRVSEQTLQSASSKVLKSMCENFYKYSKPKKIRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNIVSASTTNQKLWAVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKERNEDFIEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRGFLEGKVTFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRAELKTSDHRPVVALIDIDIFEVEAEERQNIYKEVIAVQGPPDGTVLVSIKSSLPENNFFDDALIDELLQQFASFGEVILIRFVEDKMWVTFLEGSSALNVLSLNGKELLNRTITIALKSPDWIKNLEEEMSLEKISIALPSSTSSTLLGEDAEVAADFDMEGDVDDYSAEVEELLPQHLQPSSSSGLGTSPSSSPRTSPCQSPTISEGPVPSLPIRPSRAPSRTPGPPSAQSSPIDAQPATPLPQKDPAQPLEPKRPPPPRPVAPPTRPAPPQRPPPPSGARSPAPTRKEFGGIGAPPSPGVARREMEAPKSPGTTRKDNIGRSQPSPQAGLAGPGPAGYSTARPTIPPRAGVISAPQSHARASAGRLTPESQSKTSETSKGSTFLPEPLKPQAAFPPQSSLPPPAQRLQEPLVPVAAPMPQSGPQPNLETPPQPPPRSRSSHSLPSEASSQPQVKTNGISDGKRESPLKIDPFEDLSFNLLAVSKAQLSVQTSPVPTPDPKRLIQLPSATQSNVLSSVSCMPTMPPIPARSQSQENMRSSPNPFITGLTRTNPFSDRTAAPGNPFRAKSEESEATSWFSKEEPVTISPFPSLQPLGHNKSRASSSLDGFKDSFDLQGQSTLKISNPKGWVTFEEEEDFGVKGKSKSACSDLLGNQPSSFSGSNLTLNDDWNKGTNVSFCVLPSRRPPPPPVPLLPPGTSPPVDPFTTLASKASPTLDFTER
|
3.1.3.36
| null |
inositol phosphate metabolic process [GO:0043647]; learning [GO:0007612]; membrane organization [GO:0061024]; neurotransmitter transport [GO:0006836]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol dephosphorylation [GO:0046856]; phosphatidylinositol metabolic process [GO:0046488]; positive regulation of endosome organization [GO:1904980]; synaptic vesicle endocytosis [GO:0048488]; synaptic vesicle priming [GO:0016082]; synaptic vesicle transport [GO:0048489]; synaptic vesicle uncoating [GO:0016191]
|
clathrin coat of coated pit [GO:0030132]; cytosol [GO:0005829]; membrane coat [GO:0030117]; perinuclear region of cytoplasm [GO:0048471]; presynapse [GO:0098793]; synaptic membrane [GO:0097060]; terminal bouton [GO:0043195]; vesicle membrane [GO:0012506]
|
inositol-1,4,5-trisphosphate 5-phosphatase activity [GO:0052658]; phosphatidylinositol phosphate 4-phosphatase activity [GO:0034596]; phosphatidylinositol phosphate 5-phosphatase activity [GO:0034595]; phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity [GO:0052629]; phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity [GO:0043813]; phosphatidylinositol-3-phosphate phosphatase activity [GO:0004438]; phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity [GO:0004439]; phosphatidylinositol-4-phosphate phosphatase activity [GO:0043812]; RNA binding [GO:0003723]; SH3 domain binding [GO:0017124]
|
PF08952;PF02383;
|
3.30.70.330;3.60.10.10;
|
Synaptojanin family; Inositol 1,4,5-trisphosphate 5-phosphatase family
| null |
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O18964}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456; EC=3.1.3.36; Evidence={ECO:0000269|PubMed:23804563, ECO:0000269|PubMed:27435091};
| null | null | null | null |
FUNCTION: Phosphatase that acts on various phosphoinositides, including phosphatidylinositol 4-phosphate, phosphatidylinositol (4,5)-bisphosphate and phosphatidylinositol (3,4,5)-trisphosphate (PubMed:23804563, PubMed:27435091). Has a role in clathrin-mediated endocytosis (By similarity). Hydrolyzes PIP2 bound to actin regulatory proteins resulting in the rearrangement of actin filaments downstream of tyrosine kinase and ASH/GRB2 (By similarity). {ECO:0000250|UniProtKB:O18964, ECO:0000250|UniProtKB:Q62910, ECO:0000269|PubMed:23804563, ECO:0000269|PubMed:27435091}.
|
Homo sapiens (Human)
|
O43427
|
FIBP_HUMAN
|
MTSELDIFVGNTTLIDEDVYRLWLDGYSVTDAVALRVRSGILEQTGATAAVLQSDTMDHYRTFHMLERLLHAPPKLLHQLIFQIPPSRQALLIERYYAFDEAFVREVLGKKLSKGTKKDLDDISTKTGITLKSCRRQFDNFKRVFKVVEEMRGSLVDNIQQHFLLSDRLARDYAAIVFFANNRFETGKKKLQYLSFGDFAFCAELMIQNWTLGAVGEAPTDPDSQMDDMDMDLDKEFLQDLKELKVLVADKDLLDLHKSLVCTALRGKLGVFSEMEANFKNLSRGLVNVAAKLTHNKDVRDLFVDLVEKFVEPCRSDHWPLSDVRFFLNQYSASVHSLDGFRHQALWDRYMGTLRGCLLRLYHD
| null | null |
fibroblast growth factor receptor signaling pathway [GO:0008543]; platelet aggregation [GO:0070527]
|
endomembrane system [GO:0012505]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleus [GO:0005634]
|
fibroblast growth factor binding [GO:0017134]
|
PF05427;
| null | null | null |
SUBCELLULAR LOCATION: Nucleus. Endomembrane system; Peripheral membrane protein. Note=Also associated with cytoplasmic membranes, particularly of mitochondria.
| null | null | null | null | null |
FUNCTION: May be involved in mitogenic function of FGF1. May mediate with IER2 FGF-signaling in the establishment of laterality in the embryo (By similarity). {ECO:0000250|UniProtKB:Q6T938, ECO:0000269|PubMed:9806903}.
|
Homo sapiens (Human)
|
O43432
|
IF4G3_HUMAN
|
MNSQPQTRSPFFQRPQIQPPRATIPNSSPSIRPGAQTPTAVYQANQHIMMVNHLPMPYPVPQGPQYCIPQYRHSGPPYVGPPQQYPVQPPGPGPFYPGPGPGDFPNAYGTPFYPSQPVYQSAPIIVPTQQQPPPAKREKKTIRIRDPNQGGKDITEEIMSGGGSRNPTPPIGRPTSTPTPPQQLPSQVPEHSPVVYGTVESAHLAASTPVTAASDQKQEEKPKPDPVLKSPSPVLRLVLSGEKKEQEGQTSETTAIVSIAELPLPPSPTTVSSVARSTIAAPTSSALSSQPIFTTAIDDRCELSSPREDTIPIPSLTSCTETSDPLPTNENDDDICKKPCSVAPNDIPLVSSTNLINEINGVSEKLSATESIVEIVKQEVLPLTLELEILENPPEEMKLECIPAPITPSTVPSFPPTPPTPPASPPHTPVIVPAAATTVSSPSAAITVQRVLEEDESIRTCLSEDAKEIQNKIEVEADGQTEEILDSQNLNSRRSPVPAQIAITVPKTWKKPKDRTRTTEEMLEAELELKAEEELSIDKVLESEQDKMSQGFHPERDPSDLKKVKAVEENGEEAEPVRNGAESVSEGEGIDANSGSTDSSGDGVTFPFKPESWKPTDTEGKKQYDREFLLDFQFMPACIQKPEGLPPISDVVLDKINQPKLPMRTLDPRILPRGPDFTPAFADFGRQTPGGRGVPLLNVGSRRSQPGQRREPRKIITVSVKEDVHLKKAENAWKPSQKRDSQADDPENIKTQELFRKVRSILNKLTPQMFNQLMKQVSGLTVDTEERLKGVIDLVFEKAIDEPSFSVAYANMCRCLVTLKVPMADKPGNTVNFRKLLLNRCQKEFEKDKADDDVFEKKQKELEAASAPEERTRLHDELEEAKDKARRRSIGNIKFIGELFKLKMLTEAIMHDCVVKLLKNHDEESLECLCRLLTTIGKDLDFEKAKPRMDQYFNQMEKIVKERKTSSRIRFMLQDVIDLRLCNWVSRRADQGPKTIEQIHKEAKIEEQEEQRKVQQLMTKEKRRPGVQRVDEGGWNTVQGAKNSRVLDPSKFLKITKPTIDEKIQLVPKAQLGSWGKGSSGGAKASETDALRSSASSLNRFSALQPPAPSGSTPSTPVEFDSRRTLTSRGSMGREKNDKPLPSATARPNTFMRGGSSKDLLDNQSQEEQRREMLETVKQLTGGVDVERNSTEAERNKTRESAKPEISAMSAHDKAALSEEELERKSKSIIDEFLHINDFKEAMQCVEELNAQGLLHVFVRVGVESTLERSQITRDHMGQLLYQLVQSEKLSKQDFFKGFSETLELADDMAIDIPHIWLYLAELVTPMLKEGGISMRELTIEFSKPLLPVGRAGVLLSEILHLLCKQMSHKKVGALWREADLSWKDFLPEGEDVHNFLLEQKLDFIESDSPCSSEALSKKELSAEELYKRLEKLIIEDKANDEQIFDWVEANLDEIQMSSPTFLRALMTAVCKAAIIADSSTFRVDTAVIKQRVPILLKYLDSDTEKELQALYALQASIVKLDQPANLLRMFFDCLYDEEVISEDAFYKWESSKDPAEQNGKGVALKSVTAFFTWLREAEEESEDN
| null | null |
positive regulation of translation [GO:0045727]; regulation of translational initiation [GO:0006446]; spermatid development [GO:0007286]; translational initiation [GO:0006413]
|
cytosol [GO:0005829]; eukaryotic translation initiation factor 4F complex [GO:0016281]; intracellular non-membrane-bounded organelle [GO:0043232]
|
mRNA binding [GO:0003729]; RNA binding [GO:0003723]; RNA cap binding [GO:0000339]; translation factor activity, RNA binding [GO:0008135]; translation initiation factor activity [GO:0003743]
|
PF02847;PF02854;PF02020;
|
1.25.40.180;
|
Eukaryotic initiation factor 4G family
|
PTM: Following infection by certain enteroviruses, rhinoviruses and aphthoviruses, EIF4G1 is cleaved by the viral protease 2A, or the leader protease in the case of aphthoviruses. This shuts down the capped cellular mRNA transcription. {ECO:0000269|PubMed:12663812, ECO:0000269|PubMed:15016848}.
| null | null | null | null | null | null |
FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (PubMed:9418880). Functional homolog of EIF4G1 (PubMed:9418880). {ECO:0000269|PubMed:9418880}.
|
Homo sapiens (Human)
|
O43435
|
TBX1_HUMAN
|
MHFSTVTRDMEAFTASSLSSLGAAGGFPGAASPGADPYGPREPPPPPPRYDPCAAAAPGAPGPPPPPHAYPFAPAAGAATSAAAEPEGPGASCAAAAKAPVKKNAKVAGVSVQLEMKALWDEFNQLGTEMIVTKAGRRMFPTFQVKLFGMDPMADYMLLMDFVPVDDKRYRYAFHSSSWLVAGKADPATPGRVHYHPDSPAKGAQWMKQIVSFDKLKLTNNLLDDNGHIILNSMHRYQPRFHVVYVDPRKDSEKYAEENFKTFVFEETRFTAVTAYQNHRITQLKIASNPFAKGFRDCDPEDWPRNHRPGALPLMSAFARSRNPVASPTQPSGTEKGGHVLKDKEVKAETSRNTPEREVELLRDAGGCVNLGLPCPAECQPFNTQGLVAGRTAGDRLC
| null | null |
angiogenesis [GO:0001525]; anterior/posterior pattern specification [GO:0009952]; aorta morphogenesis [GO:0035909]; artery morphogenesis [GO:0048844]; blood vessel development [GO:0001568]; blood vessel morphogenesis [GO:0048514]; cell fate specification [GO:0001708]; cell population proliferation [GO:0008283]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to retinoic acid [GO:0071300]; cochlea morphogenesis [GO:0090103]; coronary artery morphogenesis [GO:0060982]; determination of left/right symmetry [GO:0007368]; ear morphogenesis [GO:0042471]; embryonic cranial skeleton morphogenesis [GO:0048701]; embryonic viscerocranium morphogenesis [GO:0048703]; enamel mineralization [GO:0070166]; epithelial cell differentiation [GO:0030855]; face morphogenesis [GO:0060325]; heart development [GO:0007507]; heart morphogenesis [GO:0003007]; inner ear morphogenesis [GO:0042472]; lymph vessel development [GO:0001945]; mesenchymal cell apoptotic process [GO:0097152]; mesoderm development [GO:0007498]; middle ear morphogenesis [GO:0042474]; muscle cell fate commitment [GO:0042693]; muscle organ development [GO:0007517]; muscle organ morphogenesis [GO:0048644]; muscle tissue morphogenesis [GO:0060415]; negative regulation of cell differentiation [GO:0045596]; negative regulation of mesenchymal cell apoptotic process [GO:2001054]; neural crest cell migration [GO:0001755]; odontogenesis of dentin-containing tooth [GO:0042475]; outer ear morphogenesis [GO:0042473]; outflow tract morphogenesis [GO:0003151]; outflow tract septum morphogenesis [GO:0003148]; parathyroid gland development [GO:0060017]; pattern specification process [GO:0007389]; pharyngeal system development [GO:0060037]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of mesenchymal cell proliferation [GO:0002053]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of tongue muscle cell differentiation [GO:2001037]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of animal organ morphogenesis [GO:2000027]; regulation of transcription by RNA polymerase II [GO:0006357]; retinoic acid receptor signaling pathway [GO:0048384]; semicircular canal morphogenesis [GO:0048752]; sensory perception of sound [GO:0007605]; social behavior [GO:0035176]; soft palate development [GO:0060023]; somatic stem cell population maintenance [GO:0035019]; thymus development [GO:0048538]; thyroid gland development [GO:0030878]; tongue morphogenesis [GO:0043587]; vagus nerve morphogenesis [GO:0021644]
|
chromatin [GO:0000785]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; protein homodimerization activity [GO:0042803]; 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]
|
PF00907;
|
2.60.40.820;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}.
| null | null | null | null | null |
FUNCTION: Transcription factor that plays a key role in cardiovascular development by promoting pharyngeal arch segmentation during embryonic development (By similarity). Also involved in craniofacial muscle development (By similarity). Together with NKX2-5, acts as a regulator of asymmetric cardiac morphogenesis by promoting expression of PITX2 (By similarity). Acts upstream of TBX1 for the formation of the thymus and parathyroid glands from the third pharyngeal pouch (By similarity). Required for hair follicle stem cell self-renewal (By similarity). Binds to the palindromic T site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence (PubMed:11111039, PubMed:22095455). {ECO:0000250|UniProtKB:P70323, ECO:0000269|PubMed:11111039, ECO:0000269|PubMed:22095455}.
|
Homo sapiens (Human)
|
O43439
|
MTG8R_HUMAN
|
MAKESGISLKEIQVLARQWKVGPEKRVPAMPGSPVEVKIQSRSSPPTMPPLPPINPGGPRPVSFTPTALSNGINHSPPTLNGAPSPPQRFSNGPASSTSSALTNQQLPATCGARQLSKLKRFLTTLQQFGNDISPEIGEKVRTLVLALVNSTVTIEEFHCKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARAAKQTPSQYLAQHEHLLLNTSIASPADSSELLMEVHGNGKRPSPERREENSFDRDTIAPEPPAKRVCTISPAPRHSPALTVPLMNPGGQFHPTPPPLQHYTLEDIATSHLYREPNKMLEHREVRDRHHSLGLNGGYQDELVDHRLTEREWADEWKHLDHALNCIMEMVEKTRRSMAVLRRCQESDREELNYWKRRYNENTELRKTGTELVSRQHSPGSADSLSNDSQREFNSRPGTGYVPVEFWKKTEEAVNKVKIQAMSEVQKAVAEAEQKAFEVIATERARMEQTIADVKRQAAEDAFLVINEQEESTENCWNCGRKASETCSGCNIARYCGSFCQHKDWERHHRLCGQNLHGQSPHGQGRPLLPVGRGSSARSADCSVPSPALDKTSATTSRSSTPASVTAIDTNGL
| null | null |
DNA-templated transcription [GO:0006351]; intestinal epithelial cell differentiation [GO:0060575]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of neuron projection development [GO:0010977]; negative regulation of Notch signaling pathway [GO:0045746]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of neuron projection development [GO:0010976]
|
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; transcription corepressor activity [GO:0003714]
|
PF08788;PF07531;PF01753;
|
6.10.140.2220;6.10.250.230;1.20.120.1110;
|
CBFA2T family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Transcriptional corepressor which facilitates transcriptional repression via its association with DNA-binding transcription factors and recruitment of other corepressors and histone-modifying enzymes (PubMed:12559562, PubMed:15203199). Via association with PRDM14 is involved in regulation of embryonic stem cell (ESC) pluripotency (PubMed:27281218). Involved in primordial germ cell (PCG) formation. Stabilizes PRDM14 and OCT4 on chromatin in a homooligomerization-dependent manner (By similarity). Can repress the expression of MMP7 in a ZBTB33-dependent manner (PubMed:23251453). May function as a complex with the chimeric protein RUNX1/AML1-CBFA2T1/MTG8 (AML1-MTG8/ETO fusion protein) which is produced in acute myeloid leukemia with the chromosomal translocation t(8;21). May thus be involved in the repression of AML1-dependent transcription and the induction of G-CSF/CSF3-dependent cell growth. May be a tumor suppressor gene candidate involved in myeloid tumors with the deletion of the 20q11 region. Through heteromerization with CBFA2T3/MTG16 may be involved in regulation of the proliferation and the differentiation of erythroid progenitors by repressing the expression of TAL1 target genes (By similarity). Required for the maintenance of the secretory cell lineage in the small intestine. Can inhibit Notch signaling probably by association with RBPJ and may be involved in GFI1-mediated Paneth cell differentiation (By similarity). {ECO:0000250|UniProtKB:O70374, ECO:0000269|PubMed:23251453, ECO:0000303|PubMed:12559562, ECO:0000303|PubMed:15203199}.
|
Homo sapiens (Human)
|
O43447
|
PPIH_HUMAN
|
MAVANSSPVNPVVFFDVSIGGQEVGRMKIELFADVVPKTAENFRQFCTGEFRKDGVPIGYKGSTFHRVIKDFMIQGGDFVNGDGTGVASIYRGPFADENFKLRHSAPGLLSMANSGPSTNGCQFFITCSKCDWLDGKHVVFGKIIDGLLVMRKIENVPTGPNNKPKLPVVISQCGEM
|
5.2.1.8
| null |
mRNA splicing, via spliceosome [GO:0000398]; positive regulation of viral genome replication [GO:0045070]; protein folding [GO:0006457]; protein peptidyl-prolyl isomerization [GO:0000413]; protein-containing complex assembly [GO:0065003]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; spliceosomal complex [GO:0005681]; U4/U6 snRNP [GO:0071001]; U4/U6 x U5 tri-snRNP complex [GO:0046540]
|
cyclosporin A binding [GO:0016018]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; ribonucleoprotein complex binding [GO:0043021]
|
PF00160;
|
2.40.100.10;
|
Cyclophilin-type PPIase family, PPIase H subfamily
| null |
SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:9570313}. Cytoplasm {ECO:0000269|PubMed:9570313}. Note=Colocalizes with spliceosomal snRNPs. A small proportion may also be cytoplasmic.
|
CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000269|PubMed:20676357};
| null | null | null | null |
FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:20676357). Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone. {ECO:0000269|PubMed:11823439, ECO:0000269|PubMed:12875835, ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:9570313}.
|
Homo sapiens (Human)
|
O43448
|
KCAB3_HUMAN
|
MQVSIACTEQNLRSRSSEDRLCGPRPGPGGGNGGPAGGGHGNPPGGGGSGPKARAALVPRPPAPAGALRESTGRGTGMKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVITTKIFWGGQAETERGLSRKHIIEGLRGSLERLQLGYVDIVFANRSDPNCPMEEIVRAMTYVINQGLALYWGTSRWGAAEIMEAYSMARQFNLIPPVCEQAEHHLFQREKVEMQLPELYHKIGVGSVTWYPLACGLITSKYDGRVPDTCRASIKGYQWLKDKVQSEDGKKQQAKVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVLSQLTPQTVMEIDGLLGNKPHSKK
|
1.1.1.-
| null |
potassium ion transport [GO:0006813]; regulation of potassium ion transmembrane transport [GO:1901379]
|
cytoplasm [GO:0005737]; plasma membrane [GO:0005886]; voltage-gated potassium channel complex [GO:0008076]
|
aldo-keto reductase (NADP) activity [GO:0004033]; potassium channel regulator activity [GO:0015459]; transmembrane transporter binding [GO:0044325]; voltage-gated potassium channel activity [GO:0005249]
|
PF00248;
|
3.20.20.100;
|
Shaker potassium channel beta subunit family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. Alters the functional properties of Kv1.5. {ECO:0000269|PubMed:9857044}.
|
Homo sapiens (Human)
|
O43451
|
MGA_HUMAN
|
MARKKLKKFTTLEIVLSVLLLVLFIISIVLIVLLAKESLKSTAPDPGTTGTPDPGTTGTPDPGTTGTTHARTTGPPDPGTTGTTPVSAECPVVNELERINCIPDQPPTKATCDQRGCCWNPQGAVSVPWCYYSKNHSYHVEGNLVNTNAGFTARLKNLPSSPVFGSNVDNVLLTAEYQTSNRFHFKLTDQTNNRFEVPHEHVQSFSGNAAASLTYQVEISRQPFSIKVTRRSNNRVLFDSSIGPLLFADQFLQLSTRLPSTNVYGLGEHVHQQYRHDMNWKTWPIFNRDTTPNGNGTNLYGAQTFFLCLEDASGLSFGVFLMNSNAMEVVLQPAPAITYRTIGGILDFYVFLGNTPEQVVQEYLELIGRPALPSYWALGFHLSRYEYGTLDNMREVVERNRAAQLPYDVQHADIDYMDERRDFTYDSVDFKGFPEFVNELHNNGQKLVIIVDPAISNNSSSSKPYGPYDRGSDMKIWVNSSDGVTPLIGEVWPGQTVFPDYTNPNCAVWWTKEFELFHNQVEFDGIWIDMNEVSNFVDGSVSGCSTNNLNNPPFTPRILDGYLFCKTLCMDAVQHWGKQYDIHNLYGYSMAVATAEAAKTVFPNKRSFILTRSTFAGSGKFAAHWLGDNTATWDDLRWSIPGVLEFNLFGIPMVGPDICGFALDTPEELCRRWMQLGAFYPFSRNHNGQGYKDQDPASFGADSLLLNSSRHYLNIRYTLLPYLYTLFFRAHSRGDTVARPLLHEFYEDNSTWDVHQQFLWGPGLLITPVLDEGAEKVMAYVPDAVWYDYETGSQVRWRKQKVEMELPGDKIGLHLRGGYIFPTQQPNTTTLASRKNPLGLIIALDENKEAKGELFWDNGETKDTVANKVYLLCEFSVTQNRLEVNISQSTYKDPNNLAFNEIKILGTEEPSNVTVKHNGVPSQTSPTVTYDSNLKVAIITDIDLLLGEAYTVEWSIKIRDEEKIDCYPDENGASAENCTARGCIWEASNSSGVPFCYFVNDLYSVSDVQYNSHGATADISLKSSVYANAFPSTPVNPLRLDVTYHKNEMLQFKIYDPNKNRYEVPVPLNIPSMPSSTPEGQLYDVLIKKNPFGIEIRRKSTGTIIWDSQLLGFTFSDMFIRISTRLPSKYLYGFGETEHRSYRRDLEWHTWGMFSRDQPPGYKKNSYGVHPYYMGLEEDGSAHGVLLLNSNAMDVTFQPLPALTYRTTGGVLDFYVFLGPTPELVTQQYTELIGRPVMVPYWSLGFQLCRYGYQNDSEIASLYDEMVAAQIPYDVQYSDIDYMERQLDFTLSPKFAGFPALINRMKADGMRVILILDPAISGNETQPYPAFTRGVEDDVFIKYPNDGDIVWGKVWPDFPDVVVNGSLDWDSQVELYRAYVAFPDFFRNSTAKWWKREIEELYNNPQNPERSLKFDGMWIDMNEPSSFVNGAVSPGCRDASLNHPPYMPHLESRDRGLSSKTLCMESQQILPDGSLVQHYNVHNLYGWSQTRPTYEAVQEVTGQRGVVITRSTFPSSGRWAGHWLGDNTAAWDQLKKSIIGMMEFSLFGISYTGADICGFFQDAEYEMCVRWMQLGAFYPFSRNHNTIGTRRQDPVSWDAAFVNISRNVLQTRYTLLPYLYTLMQKAHTEGVTVVRPLLHEFVSDQVTWDIDSQFLLGPAFLVSPVLERNARNVTAYFPRARWYDYYTGVDINARGEWKTLPAPLDHINLHVRGGYILPWQEPALNTHLSRKNPLGLIIALDENKEAKGELFWDDGQTKDTVAKKVYLLCEFSVTQNHLEVTISQSTYKDPNNLAFNEIKILGMEEPSNVTVKHNGVPSQTSPTVTYDSNLKVAIITDINLFLGEAYTVEWSIKIRDEEKIDCYPDENGDSAENCTARGCIWEASNSSGVPFCYFVNDLYSVSDVQYNSHGATADISLKSSVHANAFPSTPVNPLRLDVTYHKNEMLQFKIYDPNNNRYEVPVPLNIPSVPSSTPEGQLYDVLIKKNPFGIEIRRKSTGTIIWDSQLLGFTFNDMFIRISTRLPSKYLYGFGETEHTSYRRDLEWHTWGMFSRDQPPGYKKNSYGVHPYYMGLEEDGSAHGVLLLNSNAMDVTFQPLPALTYRTTGGVLDFYVFLGPTPELVTQQYTELIGRPVMVPYWSLGFQLCRYGYQNDSEISSLYDEMVAAQIPYDVQYSDIDYMERQLDFTLSPKFAGFPALINRMKADGMRVILILDPAISGNETQPYPAFTRGVEDDVFIKYPNDGDIVWGKVWPDFPDVVVNGSLDWDSQVELYRAYVAFPDFFRNSTAKWWKREIEELYNNPQNPERSLKFDGMWIDMNEPSSFVNGAVSPGCRDASLNHPPYMPYLESRDRGLSSKTLCMESQQILPDGSPVQHYNVHNLYGWSQTRPTYEAVQEVTGQRGVVITRSTFPSSGRWAGHWLGDNTAAWDQLKKSIIGMMEFSLFGISYTGADICGFFQDAEYEMCVRWMQLGAFYPFSRNHNTIGTRRQDPVSWDVAFVNISRTVLQTRYTLLPYLYTLMHKAHTEGVTVVRPLLHEFVSDQVTWDIDSQFLLGPAFLVSPVLERNARNVTAYFPRARWYDYYTGVDINARGEWKTLPAPLDHINLHVRGGYILPWQEPALNTHLSRQKFMGFKIALDDEGTAGGWLFWDDGQSIDTYGKGLYYLASFSASQNTMQSHIIFNNYITGTNPLKLGYIEIWGVGSVPVTSVSISVSGMVITPSFNNDPTTQVLSIDVTDRNISLHNFTSLTWISTL
|
3.2.1.20
| null |
dextrin catabolic process [GO:1901027]; maltose catabolic process [GO:0000025]; starch catabolic process [GO:0005983]
|
apical plasma membrane [GO:0016324]; extracellular exosome [GO:0070062]; ficolin-1-rich granule membrane [GO:0101003]; plasma membrane [GO:0005886]; tertiary granule membrane [GO:0070821]
|
alpha-1,4-glucosidase activity [GO:0004558]; amylase activity [GO:0016160]; carbohydrate binding [GO:0030246]; catalytic activity [GO:0003824]; glucan 1,4-alpha-glucosidase activity [GO:0004339]; maltose alpha-glucosidase activity [GO:0032450]
|
PF13802;PF01055;PF21365;PF00088;
|
3.20.20.80;2.60.40.1760;2.60.40.1180;4.10.110.10;
|
Glycosyl hydrolase 31 family
|
PTM: N- and O-glycosylated. {ECO:0000269|PubMed:18036614, ECO:0000269|PubMed:3143729}.; PTM: Does not undergo intracellular or extracellular proteolytic cleavage. {ECO:0000269|PubMed:3143729}.; PTM: Sulfated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type II membrane protein. Note=Brush border. {ECO:0000269|PubMed:3143729}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.; EC=3.2.1.20; Evidence={ECO:0000269|PubMed:12547908, ECO:0000269|PubMed:18036614, ECO:0000269|PubMed:18356321, ECO:0000269|PubMed:22058037, ECO:0000269|PubMed:27480812}; CATALYTIC ACTIVITY: Reaction=D-maltoheptaose + H2O = alpha-D-glucose + D-maltohexaose; Xref=Rhea:RHEA:29643, ChEBI:CHEBI:15377, ChEBI:CHEBI:17925, ChEBI:CHEBI:143182, ChEBI:CHEBI:143183; Evidence={ECO:0000269|PubMed:22058037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29644; Evidence={ECO:0000305|PubMed:22058037}; CATALYTIC ACTIVITY: Reaction=D-maltohexaose + H2O = alpha-D-glucose + D-maltopentaose; Xref=Rhea:RHEA:29639, ChEBI:CHEBI:15377, ChEBI:CHEBI:17925, ChEBI:CHEBI:143181, ChEBI:CHEBI:143182; Evidence={ECO:0000269|PubMed:22058037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29640; Evidence={ECO:0000305|PubMed:22058037}; CATALYTIC ACTIVITY: Reaction=D-maltopentaose + H2O = alpha-D-glucose + D-maltotetraose; Xref=Rhea:RHEA:29635, ChEBI:CHEBI:15377, ChEBI:CHEBI:17925, ChEBI:CHEBI:143180, ChEBI:CHEBI:143181; Evidence={ECO:0000269|PubMed:18036614, ECO:0000269|PubMed:18356321, ECO:0000269|PubMed:22058037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29636; Evidence={ECO:0000305|PubMed:22058037}; CATALYTIC ACTIVITY: Reaction=D-maltotetraose + H2O = alpha-D-glucose + D-maltotriose; Xref=Rhea:RHEA:29631, ChEBI:CHEBI:15377, ChEBI:CHEBI:17925, ChEBI:CHEBI:140999, ChEBI:CHEBI:143180; Evidence={ECO:0000269|PubMed:18036614, ECO:0000269|PubMed:18356321, ECO:0000269|PubMed:22058037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29632; Evidence={ECO:0000305|PubMed:18036614, ECO:0000305|PubMed:18356321, ECO:0000305|PubMed:22058037}; CATALYTIC ACTIVITY: Reaction=D-maltotriose + H2O = alpha-D-glucose + D-maltose; Xref=Rhea:RHEA:27970, ChEBI:CHEBI:15377, ChEBI:CHEBI:17306, ChEBI:CHEBI:17925, ChEBI:CHEBI:140999; Evidence={ECO:0000269|PubMed:18036614, ECO:0000269|PubMed:18356321, ECO:0000269|PubMed:22058037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27971; Evidence={ECO:0000305|PubMed:18036614, ECO:0000305|PubMed:18356321, ECO:0000305|PubMed:22058037}; CATALYTIC ACTIVITY: Reaction=D-maltose + H2O = alpha-D-glucose + D-glucose; Xref=Rhea:RHEA:68796, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:17306, ChEBI:CHEBI:17925; Evidence={ECO:0000269|PubMed:18036614, ECO:0000269|PubMed:18356321, ECO:0000269|PubMed:22058037, ECO:0000269|PubMed:27480812}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68797; Evidence={ECO:0000305|PubMed:18036614, ECO:0000305|PubMed:18356321, ECO:0000305|PubMed:22058037, ECO:0000305|PubMed:27480812}; CATALYTIC ACTIVITY: Reaction=H2O + nigerose = alpha-D-glucose + D-glucose; Xref=Rhea:RHEA:68800, ChEBI:CHEBI:4167, ChEBI:CHEBI:7570, ChEBI:CHEBI:15377, ChEBI:CHEBI:17925; Evidence={ECO:0000269|PubMed:27480812}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68801; Evidence={ECO:0000305|PubMed:27480812}; CATALYTIC ACTIVITY: Reaction=H2O + kojibiose = alpha-D-glucose + D-glucose; Xref=Rhea:RHEA:68804, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:17925, ChEBI:CHEBI:142460; Evidence={ECO:0000269|PubMed:27480812}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68805; Evidence={ECO:0000305|PubMed:27480812}; CATALYTIC ACTIVITY: Reaction=H2O + isomaltose = alpha-D-glucose + D-glucose; Xref=Rhea:RHEA:68864, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:17925, ChEBI:CHEBI:28189; Evidence={ECO:0000269|PubMed:27480812}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68865; Evidence={ECO:0000305|PubMed:27480812}; CATALYTIC ACTIVITY: Reaction=6-O-alpha-D-glucopyranosyl-D-fructose + H2O = alpha-D-glucose + D-fructose; Xref=Rhea:RHEA:68808, ChEBI:CHEBI:15377, ChEBI:CHEBI:17925, ChEBI:CHEBI:18394, ChEBI:CHEBI:37721; Evidence={ECO:0000269|PubMed:27480812}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68809; Evidence={ECO:0000305|PubMed:27480812};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.27 mM for maltoheptaose (with ctMGAM) {ECO:0000269|PubMed:22058037}; KM=1.05 mM for maltohexaose (with ctMGAM) {ECO:0000269|PubMed:22058037}; KM=0.61 mM for maltopentaose (with ctMGAM) {ECO:0000269|PubMed:22058037}; KM=0.96 mM for maltotetraose (with ctMGAM) {ECO:0000269|PubMed:22058037}; KM=0.91 mM for maltotriose (with ctMGAM) {ECO:0000269|PubMed:22058037}; KM=5.67 mM for maltose (with ctMGAM) {ECO:0000269|PubMed:22058037}; KM=13.12 mM for maltoheptaose (with ntMGAM) {ECO:0000269|PubMed:22058037}; KM=9.76 mM for maltohexaose (with ntMGAM) {ECO:0000269|PubMed:22058037}; KM=9.14 mM for maltopentaose (with ntMGAM) {ECO:0000269|PubMed:22058037}; KM=3.39 mM for maltotetraose (with ntMGAM) {ECO:0000269|PubMed:22058037}; KM=4.44 mM for maltotriose (with ntMGAM) {ECO:0000269|PubMed:22058037}; KM=6.4 mM for maltose (with ntMGAM) {ECO:0000269|PubMed:22058037}; KM=6.7 mM for maltopentaose (with ntMGAM) {ECO:0000269|PubMed:18036614}; KM=3 mM for maltotetraose (with ntMGAM) {ECO:0000269|PubMed:18036614, ECO:0000269|PubMed:18356321}; KM=4.6 mM for maltotriose (with ntMGAM) {ECO:0000269|PubMed:18036614, ECO:0000269|PubMed:18356321}; KM=7.7 mM for maltose (with ntMGAM) {ECO:0000269|PubMed:18036614}; KM=8.7 mM for maltose (with ntMGAM) {ECO:0000269|PubMed:27480812}; KM=27.1 mM for nigerose (with ntMGAM) {ECO:0000269|PubMed:27480812}; KM=11.6 mM for kojibiose (with ntMGAM) {ECO:0000269|PubMed:27480812}; KM=128 mM for isomaltose (with ntMGAM) {ECO:0000269|PubMed:27480812}; KM=6.66 mM for maltopentaose (with ntMGAM) {ECO:0000269|PubMed:18356321}; KM=7.71 mM for maltose (with ntMGAM) {ECO:0000269|PubMed:18356321}; KM=4.34 mM for maltodextrin (with ntMGAM) {ECO:0000269|PubMed:18356321}; KM=7 mM for alpha-limit dextrin (with ntMGAM) {ECO:0000269|PubMed:18356321}; Vmax=6.97 umol/min/mg enzyme toward maltopentaose (with ntMGAM) {ECO:0000269|PubMed:18356321}; Vmax=7.65 umol/min/mg enzyme toward maltotetraose (with ntMGAM) {ECO:0000269|PubMed:18356321}; Vmax=9.58 umol/min/mg enzyme toward maltotriose (with ntMGAM) {ECO:0000269|PubMed:18356321}; Vmax=8.26 umol/min/mg enzyme toward maltose (with ntMGAM) {ECO:0000269|PubMed:18356321}; Vmax=7.51 umol/min/mg enzyme toward maltodextrin (with ntMGAM) {ECO:0000269|PubMed:18356321}; Vmax=11 umol/min/mg enzyme toward alpha-limit dextrin (with ntMGAM) {ECO:0000269|PubMed:18356321};
|
PATHWAY: Carbohydrate degradation. {ECO:0000305|PubMed:18036614, ECO:0000305|PubMed:22058037, ECO:0000305|PubMed:27480812}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. Has substantial activity at acidic pH. {ECO:0000269|PubMed:18356321};
| null |
FUNCTION: Alpha-(1,4) exo-glucosidase involved in breakdown of dietary starch oligosaccharides in small intestine. Cleaves the non-reducing alpha-(1,4)-linked glucose residue in linear dextrins with retention of anomeric center stereochemistry (PubMed:12547908, PubMed:18036614, PubMed:18356321, PubMed:22058037, PubMed:27480812). Mainly hydrolyzes short length oligomaltoses having two to seven glucose residues (PubMed:12547908, PubMed:18036614, PubMed:18356321, PubMed:22058037, PubMed:27480812). Can cleave alpha-(1,2), alpha-(1,3) and alpha-(1,6) glycosidic linkages with lower efficiency, whereas beta glycosidic linkages are usually not hydrolyzed (PubMed:27480812). {ECO:0000269|PubMed:12547908, ECO:0000269|PubMed:18036614, ECO:0000269|PubMed:18356321, ECO:0000269|PubMed:22058037, ECO:0000269|PubMed:27480812}.
|
Homo sapiens (Human)
|
O43462
|
MBTP2_HUMAN
|
MIPVSLVVVVVGGWTVVYLTDLVLKSSVYFKHSYEDWLENNGLSISPFHIRWQTAVFNRAFYSWGRRKARMLYQWFNFGMVFGVIAMFSSFFLLGKTLMQTLAQMMADSPSSYSSSSSSSSSSSSSSSSSSSSSSSLHNEQVLQVVVPGINLPVNQLTYFFTAVLISGVVHEIGHGIAAIREQVRFNGFGIFLFIIYPGAFVDLFTTHLQLISPVQQLRIFCAGIWHNFVLALLGILALVLLPVILLPFYYTGVGVLITEVAEDSPAIGPRGLFVGDLVTHLQDCPVTNVQDWNECLDTIAYEPQIGYCISASTLQQLSFPVRAYKRLDGSTECCNNHSLTDVCFSYRNNFNKRLHTCLPARKAVEATQVCRTNKDCKKSSSSSFCIIPSLETHTRLIKVKHPPQIDMLYVGHPLHLHYTVSITSFIPRFNFLSIDLPVVVETFVKYLISLSGALAIVNAVPCFALDGQWILNSFLDATLTSVIGDNDVKDLIGFFILLGGSVLLAANVTLGLWMVTAR
|
3.4.24.85
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:10805775}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:10805775};
|
ATF6-mediated unfolded protein response [GO:0036500]; bone maturation [GO:0070977]; cholesterol metabolic process [GO:0008203]; endoplasmic reticulum unfolded protein response [GO:0030968]; membrane protein intracellular domain proteolysis [GO:0031293]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein maturation [GO:0051604]; regulation of cholesterol biosynthetic process [GO:0045540]; regulation of response to endoplasmic reticulum stress [GO:1905897]; response to endoplasmic reticulum stress [GO:0034976]
|
cytoplasm [GO:0005737]; Golgi membrane [GO:0000139]; membrane [GO:0016020]
|
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; transcription regulator activator activity [GO:0140537]
|
PF02163;
|
2.30.42.10;
|
Peptidase M50A family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:19361614}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:19361614}. Golgi apparatus membrane {ECO:0000305|PubMed:16417584}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=Cleaves several transcription factors that are type-2 transmembrane proteins within membrane-spanning domains. Known substrates include sterol regulatory element-binding protein (SREBP) -1, SREBP-2 and forms of the transcriptional activator ATF6. SREBP-2 is cleaved at the site 477-DRSRILL-|-CVLTFLCLSFNPLTSLLQWGGA-505. The residues Asn-Pro, 11 residues distal to the site of cleavage in the membrane-spanning domain, are important for cleavage by S2P endopeptidase. Replacement of either of these residues does not prevent cleavage, but there is no cleavage if both of these residues are replaced.; EC=3.4.24.85; Evidence={ECO:0000269|PubMed:10805775, ECO:0000269|PubMed:11163209};
| null | null | null | null |
FUNCTION: Zinc metalloprotease that mediates intramembrane proteolysis of proteins such as ATF6, ATF6B, SREBF1/SREBP1 and SREBF2/SREBP2 (PubMed:10805775, PubMed:11163209). Catalyzes the second step in the proteolytic activation of the sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2: cleaves SREBPs within the first transmembrane segment, thereby releasing the N-terminal segment with a portion of the transmembrane segment attached (PubMed:10805775, PubMed:27380894, PubMed:9659902). Mature N-terminal SREBP fragments shuttle to the nucleus and activate gene transcription (PubMed:10805775, PubMed:27380894, PubMed:9659902). Also mediates the second step in the proteolytic activation of the cyclic AMP-dependent transcription factor ATF-6 (ATF6 and ATF6B) (PubMed:11163209). Involved in intramembrane proteolysis during bone formation (PubMed:27380894). In astrocytes and osteoblasts, upon DNA damage and ER stress, mediates the second step of the regulated intramembrane proteolytic activation of the transcription factor CREB3L1, leading to the inhibition of cell-cycle progression (PubMed:16417584). {ECO:0000269|PubMed:10805775, ECO:0000269|PubMed:11163209, ECO:0000269|PubMed:16417584, ECO:0000269|PubMed:27380894, ECO:0000269|PubMed:9659902}.
|
Homo sapiens (Human)
|
O43463
|
SUV91_HUMAN
|
MAENLKGCSVCCKSSWNQLQDLCRLAKLSCPALGISKRNLYDFEVEYLCDYKKIREQEYYLVKWRGYPDSESTWEPRQNLKCVRILKQFHKDLERELLRRHHRSKTPRHLDPSLANYLVQKAKQRRALRRWEQELNAKRSHLGRITVENEVDLDGPPRAFVYINEYRVGEGITLNQVAVGCECQDCLWAPTGGCCPGASLHKFAYNDQGQVRLRAGLPIYECNSRCRCGYDCPNRVVQKGIRYDLCIFRTDDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIRAGEELTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIECKCGTESCRKYLF
|
2.1.1.355
| null |
cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cellular response to glucose starvation [GO:0042149]; cellular response to hypoxia [GO:0071456]; chromatin organization [GO:0006325]; circadian rhythm [GO:0007623]; DNA damage response [GO:0006974]; energy homeostasis [GO:0097009]; epigenetic programming in the zygotic pronuclei [GO:0044725]; methylation [GO:0032259]; negative regulation of cell cycle [GO:0045786]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; rDNA heterochromatin formation [GO:0000183]; regulation of transcription by glucose [GO:0046015]; rRNA processing [GO:0006364]
|
chromatin silencing complex [GO:0005677]; chromosome, centromeric region [GO:0000775]; condensed nuclear chromosome [GO:0000794]; cytoplasmic vesicle [GO:0031410]; eNoSc complex [GO:0061773]; heterochromatin [GO:0000792]; nuclear lamina [GO:0005652]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; rDNA heterochromatin [GO:0033553]
|
chromatin binding [GO:0003682]; histone H3 methyltransferase activity [GO:0140938]; histone H3K9 methyltransferase activity [GO:0046974]; histone H3K9 trimethyltransferase activity [GO:0140949]; histone methyltransferase activity [GO:0042054]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]; transcription cis-regulatory region binding [GO:0000976]; zinc ion binding [GO:0008270]
|
PF00385;PF05033;PF00856;
|
2.40.50.40;2.170.270.10;
|
Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, Suvar3-9 subfamily
|
PTM: Phosphorylated on serine residues, and to a lesser degree, on threonine residues. The phosphorylated form is stabilized by SBF1 and is less active in its transcriptional repressor function. {ECO:0000269|PubMed:10671371}.; PTM: Ubiquitinated by the DCX(DCAF13) E3 ubiquitin ligase complex, leading to its degradation. {ECO:0000269|PubMed:30111536}.; PTM: Acetylated at Lys-266, leading to inhibition of enzyme activity. SIRT1-mediated deacetylation relieves this inhibition. {ECO:0000269|PubMed:18004385}.; PTM: (Microbial infection) A higher molecular weight form is also seen in M.bovis infected cells. {ECO:0000269|PubMed:29170282}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29170282, ECO:0000269|PubMed:30111536}. Nucleus lamina. Nucleus, nucleoplasm. Chromosome, centromere. Note=Associates with centromeric constitutive heterochromatin.; SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome lumen {ECO:0000269|PubMed:29170282}. Cell membrane {ECO:0000269|PubMed:29170282}. Note=(Microbial infection) Upon infection with M.bovis most protein is found associated with bacteria in phagolysosomes, while part is also found in the cell membrane; localization requires bacterial HupB, when it is deleted SUV39H1 is not phagosomal. {ECO:0000269|PubMed:29170282}.
|
CATALYTIC ACTIVITY: Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA-COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.355; Evidence={ECO:0000255|PROSITE-ProRule:PRU00912, ECO:0000269|PubMed:10949293, ECO:0000269|PubMed:18004385};
| null | null | null | null |
FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. Also weakly methylates histone H1 (in vitro). H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation. {ECO:0000269|PubMed:14765126, ECO:0000269|PubMed:16449642, ECO:0000269|PubMed:16818776, ECO:0000269|PubMed:16858404, ECO:0000269|PubMed:18004385, ECO:0000269|PubMed:18485871, ECO:0000269|PubMed:30111536}.; FUNCTION: (Microbial infection) Plays a role in defense against mycobacterial infections. Methylates M.tuberculosis HupB on 'Lys-140', probably methylates HupB of M.bovis also. Methylation has an inhibitory effect on mycobacterial growth in the host. Macrophages expressing about 60% SUV39H1 are slightly more susceptible to M.bovis or M.tuberculosis infection. Chaetocin (an inhibitor of this enzyme) increases macrophage survival of M.tuberculosis. This protein inhibits biofilm formation by M.tuberculosis via 'Lys-140' trimethylation. {ECO:0000269|PubMed:29170282}.
|
Homo sapiens (Human)
|
O43464
|
HTRA2_HUMAN
|
MAAPRAGRGAGWSLRAWRALGGIRWGRRPRLTPDLRALLTSGTSDPRARVTYGTPSLWARLSVGVTEPRACLTSGTPGPRAQLTAVTPDTRTREASENSGTRSRAWLAVALGAGGAVLLLLWGGGRGPPAVLAAVPSPPPASPRSQYNFIADVVEKTAPAVVYIEILDRHPFLGREVPISNGSGFVVAADGLIVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIATLRIQTKEPLPTLPLGRSADVRQGEFVVAMGSPFALQNTITSGIVSSAQRPARDLGLPQTNVEYIQTDAAIDFGNSGGPLVNLDGEVIGVNTMKVTAGISFAIPSDRLREFLHRGEKKNSSSGISGSQRRYIGVMMLTLSPSILAELQLREPSFPDVQHGVLIHKVILGSPAHRAGLRPGDVILAIGEQMVQNAEDVYEAVRTQSQLAVQIRRGRETLTLYVTPEVTE
|
3.4.21.108
| null |
adult walking behavior [GO:0007628]; cellular response to growth factor stimulus [GO:0071363]; cellular response to heat [GO:0034605]; cellular response to interferon-beta [GO:0035458]; cellular response to oxidative stress [GO:0034599]; cellular response to retinoic acid [GO:0071300]; ceramide metabolic process [GO:0006672]; execution phase of apoptosis [GO:0097194]; forebrain development [GO:0030900]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; mitochondrial protein catabolic process [GO:0035694]; negative regulation of cell cycle [GO:0045786]; negative regulation of mitophagy in response to mitochondrial depolarization [GO:1904924]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902176]; neuron apoptotic process [GO:0051402]; neuron development [GO:0048666]; pentacyclic triterpenoid metabolic process [GO:0019742]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:2001269]; positive regulation of execution phase of apoptosis [GO:1900119]; positive regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001241]; positive regulation of mitochondrion organization [GO:0010822]; positive regulation of protein targeting to mitochondrion [GO:1903955]; programmed cell death [GO:0012501]; protein autoprocessing [GO:0016540]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508]; regulation of autophagy of mitochondrion [GO:1903146]; regulation of multicellular organism growth [GO:0040014]; response to herbicide [GO:0009635]
|
CD40 receptor complex [GO:0035631]; chromatin [GO:0000785]; cytoplasmic side of plasma membrane [GO:0009898]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; mitochondrial intermembrane space [GO:0005758]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; serine-type endopeptidase complex [GO:1905370]
|
identical protein binding [GO:0042802]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]; unfolded protein binding [GO:0051082]
|
PF17820;PF13365;
|
2.30.42.10;2.40.10.120;
|
Peptidase S1C family
|
PTM: Autoproteolytically activated. {ECO:0000269|PubMed:10873535}.
|
SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Mitochondrion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Predominantly present in the intermembrane space. Released into the cytosol following apoptotic stimuli, such as UV treatment, and stimulation of mitochondria with caspase-8 truncated BID/tBID.; SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum {ECO:0000269|PubMed:10644717}.
|
CATALYTIC ACTIVITY: Reaction=Cleavage of non-polar aliphatic amino-acids at the P1 position, with a preference for Val, Ile and Met. At the P2 and P3 positions, Arg is selected most strongly with a secondary preference for other hydrophilic residues.; EC=3.4.21.108;
| null | null | null | null |
FUNCTION: Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism. Cleaves THAP5 and promotes its degradation during apoptosis. Isoform 2 seems to be proteolytically inactive. {ECO:0000269|PubMed:15200957, ECO:0000269|PubMed:19502560}.
|
Homo sapiens (Human)
|
O43474
|
KLF4_HUMAN
|
MRQPPGESDMAVSDALLPSFSTFASGPAGREKTLRQAGAPNNRWREELSHMKRLPPVLPGRPYDLAAATVATDLESGGAGAACGGSNLAPLPRRETEEFNDLLDLDFILSNSLTHPPESVAATVSSSASASSSSSPSSSGPASAPSTCSFTYPIRAGNDPGVAPGGTGGGLLYGRESAPPPTAPFNLADINDVSPSGGFVAELLRPELDPVYIPPQQPQPPGGGLMGKFVLKASLSAPGSEYGSPSVISVSKGSPDGSHPVVVAPYNGGPPRTCPKIKQEAVSSCTHLGAGPPLSNGHRPAAHDFPLGRQLPSRTTPTLGLEEVLSSRDCHPALPLPPGFHPHPGPNYPSFLPDQMQPQVPPLHYQGQSRGFVARAGEPCVCWPHFGTHGMMLTPPSSPLELMPPGSCMPEEPKPKRGRRSWPRKRTATHTCDYAGCGKTYTKSSHLKAHLRTHTGEKPYHCDWDGCGWKFARSDELTRHYRKHTGHRPFQCQKCDRAFSRSDHLALHMKRHF
| null | null |
canonical Wnt signaling pathway [GO:0060070]; cellular response to cycloheximide [GO:0071409]; cellular response to growth factor stimulus [GO:0071363]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to laminar fluid shear stress [GO:0071499]; cellular response to leukemia inhibitory factor [GO:1990830]; cellular response to peptide [GO:1901653]; cellular response to retinoic acid [GO:0071300]; defense response to tumor cell [GO:0002357]; epidermal cell differentiation [GO:0009913]; epidermis morphogenesis [GO:0048730]; establishment of skin barrier [GO:0061436]; fat cell differentiation [GO:0045444]; glandular epithelial cell differentiation [GO:0002067]; mesodermal cell fate determination [GO:0007500]; negative regulation of angiogenesis [GO:0016525]; negative regulation of cell migration involved in sprouting angiogenesis [GO:0090051]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of chemokine (C-X-C motif) ligand 2 production [GO:2000342]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of gene expression [GO:0010629]; negative regulation of heterotypic cell-cell adhesion [GO:0034115]; negative regulation of inflammatory response [GO:0050728]; negative regulation of interleukin-8 production [GO:0032717]; negative regulation of leukocyte adhesion to arterial endothelial cell [GO:1904998]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of response to cytokine stimulus [GO:0060761]; negative regulation of smooth muscle cell proliferation [GO:0048662]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of hemoglobin biosynthetic process [GO:0046985]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of protein metabolic process [GO:0051247]; positive regulation of sprouting angiogenesis [GO:1903672]; positive regulation of telomerase activity [GO:0051973]; positive regulation of transcription by RNA polymerase II [GO:0045944]; post-embryonic camera-type eye development [GO:0031077]; post-embryonic hemopoiesis [GO:0035166]; regulation of axon regeneration [GO:0048679]; regulation of blastocyst development [GO:0120222]; regulation of cell differentiation [GO:0045595]; regulation of transcription by RNA polymerase II [GO:0006357]; somatic stem cell population maintenance [GO:0035019]; stem cell population maintenance [GO:0019827]; transcription by RNA polymerase II [GO:0006366]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; euchromatin [GO:0000791]; microtubule cytoskeleton [GO:0015630]; nucleoplasm [GO:0005654]; transcription regulator complex [GO:0005667]
|
beta-catenin binding [GO:0008013]; chromatin DNA binding [GO:0031490]; 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]; histone deacetylase binding [GO:0042826]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II sequence-specific DNA-binding transcription factor recruiting activity [GO:0001010]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific double-stranded DNA binding [GO:1990837]; transcription cis-regulatory region binding [GO:0000976]; transcription coregulator binding [GO:0001221]; zinc ion binding [GO:0008270]
|
PF00096;
|
3.30.160.60;
|
Krueppel C2H2-type zinc-finger protein family
|
PTM: Ubiquitinated. 'Lys-48'-linked ubiquitinated and targeted for proteasomal degradation by the SCF(BTRC) E3 ubiquitin-protein ligase complex, thereby negatively regulating cell pluripotency maintenance and embryogenesis. {ECO:0000250|UniProtKB:Q60793}.; PTM: Polyglutamylated by TTLL1 and TTLL4 at Glu-411, which inhibits KLF4 binding with E3 ligase component BTRC, thereby impeding ubiquitination. Deglutamylated by CCP1 and CCP6; deglutamylation promotes KLF4 ubiquitination. KLF4 glutamylation state plays a critical role in the regulation of its function in cell reprogramming, pluripotency maintenance and embryogenesis. {ECO:0000250|UniProtKB:Q60793}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q60793}. Cytoplasm {ECO:0000250|UniProtKB:Q60793}.
| null | null | null | null | null |
FUNCTION: Transcription factor; can act both as activator and as repressor. Binds the 5'-CACCC-3' core sequence. Binds to the promoter region of its own gene and can activate its own transcription. Regulates the expression of key transcription factors during embryonic development. Plays an important role in maintaining embryonic stem cells, and in preventing their differentiation. Required for establishing the barrier function of the skin and for postnatal maturation and maintenance of the ocular surface. Involved in the differentiation of epithelial cells and may also function in skeletal and kidney development. Contributes to the down-regulation of p53/TP53 transcription. {ECO:0000269|PubMed:17308127, ECO:0000269|PubMed:20071344}.
|
Homo sapiens (Human)
|
O43482
|
MS18B_HUMAN
|
MAAQPLRHRSRCATPPRGDFCGGTERAIDQASFTTSMEWDTQVVKGSSPLGPAGLGAEEPAAGPQLPSWLQPERCAVFQCAQCHAVLADSVHLAWDLSRSLGAVVFSRVTNNVVLEAPFLVGIEGSLKGSTYNLLFCGSCGIPVGFHLYSTHAALAALRGHFCLSSDKMVCYLLKTKAIVNASEMDIQNVPLSEKIAELKEKIVLTHNRLKSLMKILSEVTPDQSKPEN
| null | null |
cell communication [GO:0007154]; cell division [GO:0051301]; CENP-A containing chromatin assembly [GO:0034080]; chromosome segregation [GO:0007059]
|
Cajal body [GO:0015030]; chromatin [GO:0000785]; chromocenter [GO:0010369]; chromosome, centromeric region [GO:0000775]; intracellular membrane-bounded organelle [GO:0043231]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
identical protein binding [GO:0042802]; metal ion binding [GO:0046872]
|
PF03226;
| null |
Mis18 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17199038}. Chromosome {ECO:0000269|PubMed:17199038}. Chromosome, centromere {ECO:0000269|PubMed:17199038}. Note=Associated with centromeres in interphase cells, from late anaphase to the G1 phase. Not detected on centromeres during earlier phases of mitosis. Associated with chromatin.
| null | null | null | null | null |
FUNCTION: Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis. {ECO:0000269|PubMed:17199038}.
|
Homo sapiens (Human)
|
O43488
|
ARK72_HUMAN
|
MLSAASRVVSRAAVHCALRSPPPEARALAMSRPPPPRVASVLGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANPWDGKSLKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPTVYQGMYNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGNSWAETYRNRFWKEHHFEAIALVEKALQAAYGASAPSVTSAALRWMYHHSQLQGAHGDAVILGMSSLEQLEQNLAATEEGPLEPAVVDAFNQAWHLVAHECPNYFR
|
1.1.1.n11
| null |
carbohydrate metabolic process [GO:0005975]; cellular aldehyde metabolic process [GO:0006081]; daunorubicin metabolic process [GO:0044597]; doxorubicin metabolic process [GO:0044598]; lipid metabolic process [GO:0006629]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]
|
alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; aldo-keto reductase (NADP) activity [GO:0004033]; electron transfer activity [GO:0009055]; phenanthrene-9,10-epoxide hydrolase activity [GO:0019119]
|
PF00248;
|
3.20.20.100;
|
Aldo/keto reductase family, Aldo/keto reductase 2 subfamily
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}. Golgi apparatus {ECO:0000250|UniProtKB:Q8CG45}. Cytoplasm {ECO:0000269|PubMed:9576847}.
|
CATALYTIC ACTIVITY: Reaction=4-hydroxybutanoate + NADP(+) = H(+) + NADPH + succinate semialdehyde; Xref=Rhea:RHEA:26381, ChEBI:CHEBI:15378, ChEBI:CHEBI:16724, ChEBI:CHEBI:57706, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.n11; Evidence={ECO:0000269|PubMed:10510318};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20 uM for succinic semialdehyde {ECO:0000269|PubMed:10510318}; KM=17 uM for 2-carboxybenzaldehyde {ECO:0000269|PubMed:10510318}; KM=8 uM for 9,10-phenanthrenequinone {ECO:0000269|PubMed:10510318}; KM=102 uM for 1,2-naphthoquinone {ECO:0000269|PubMed:10510318};
| null | null | null |
FUNCTION: Catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate. May have an important role in producing the neuromodulator gamma-hydroxybutyrate (GHB). Has broad substrate specificity. Has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). Can reduce 1,2-naphthoquinone and 9,10-phenanthrenequinone (in vitro). Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen. {ECO:0000269|PubMed:17591773, ECO:0000269|PubMed:9576847}.
|
Homo sapiens (Human)
|
O43490
|
PROM1_HUMAN
|
MALVLGSLLLLGLCGNSFSGGQPSSTDAPKAWNYELPATNYETQDSHKAGPIGILFELVHIFLYVVQPRDFPEDTLRKFLQKAYESKIDYDKPETVILGLKIVYYEAGIILCCVLGLLFIILMPLVGYFFCMCRCCNKCGGEMHQRQKENGPFLRKCFAISLLVICIIISIGIFYGFVANHQVRTRIKRSRKLADSNFKDLRTLLNETPEQIKYILAQYNTTKDKAFTDLNSINSVLGGGILDRLRPNIIPVLDEIKSMATAIKETKEALENMNSTLKSLHQQSTQLSSSLTSVKTSLRSSLNDPLCLVHPSSETCNSIRLSLSQLNSNPELRQLPPVDAELDNVNNVLRTDLDGLVQQGYQSLNDIPDRVQRQTTTVVAGIKRVLNSIGSDIDNVTQRLPIQDILSAFSVYVNNTESYIHRNLPTLEEYDSYWWLGGLVICSLLTLIVIFYYLGLLCGVCGYDRHATPTTRGCVSNTGGVFLMVGVGLSFLFCWILMIIVVLTFVFGANVEKLICEPYTSKELFRVLDTPYLLNEDWEYYLSGKLFNKSKMKLTFEQVYSDCKKNRGTYGTLHLQNSFNISEHLNINEHTGSISSELESLKVNLNIFLLGAAGRKNLQDFAACGIDRMNYDSYLAQTGKSPAGVNLLSFAYDLEAKANSLPPGNLRNSLKRDAQTIKTIHQQRVLPIEQSLSTLYQSVKILQRTGNGLLERVTRILASLDFAQNFITNNTSSVIIEETKKYGRTIIGYFEHYLQWIEFSISEKVASCKPVATALDTAVDVFLCSYIIDPLNLFWFGIGKATVFLLPALIFAVKLAKYYRRMDSEDVYDDVETIPMKNMENGNNGYHKDHVYGIHNPVMTSPSQH
| null | null |
camera-type eye photoreceptor cell differentiation [GO:0060219]; glomerular parietal epithelial cell differentiation [GO:0072139]; photoreceptor cell maintenance [GO:0045494]; podocyte differentiation [GO:0072112]; positive regulation of nephron tubule epithelial cell differentiation [GO:2000768]; retina layer formation [GO:0010842]; retina morphogenesis in camera-type eye [GO:0060042]
|
apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; cilium [GO:0005929]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; microvillus [GO:0005902]; microvillus membrane [GO:0031528]; photoreceptor outer segment [GO:0001750]; photoreceptor outer segment membrane [GO:0042622]; plasma membrane [GO:0005886]; prominosome [GO:0071914]; vesicle [GO:0031982]
|
actinin binding [GO:0042805]; cadherin binding [GO:0045296]; cholesterol binding [GO:0015485]
|
PF05478;
| null |
Prominin family
|
PTM: Isoform 1 and isoform 2 are glycosylated. {ECO:0000269|PubMed:12042327}.; PTM: Acetylation at Lys-225, Lys-257 and Lys-264 by NAT8 and NAT8B may control PROM1 protein expression and its function in cell apoptosis. {ECO:0000269|PubMed:24556617}.
|
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, microvillus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250}. Endoplasmic reticulum. Endoplasmic reticulum-Golgi intermediate compartment. Note=Found in extracellular membrane particles in various body fluids such as cerebrospinal fluid, saliva, seminal fluid and urine.
| null | null | null | null | null |
FUNCTION: May play a role in cell differentiation, proliferation and apoptosis (PubMed:24556617). Binds cholesterol in cholesterol-containing plasma membrane microdomains and may play a role in the organization of the apical plasma membrane in epithelial cells. During early retinal development acts as a key regulator of disk morphogenesis. Involved in regulation of MAPK and Akt signaling pathways. In neuroblastoma cells suppresses cell differentiation such as neurite outgrowth in a RET-dependent manner (PubMed:20818439). {ECO:0000269|PubMed:20818439, ECO:0000269|PubMed:24556617}.
|
Homo sapiens (Human)
|
O43491
|
E41L2_HUMAN
|
MTTEVGSVSEVKKDSSQLGTDATKEKPKEVAENQQNQSSDPEEEKGSQPPPAAESQSSLRRQKREKETSESRGISRFIPPWLKKQKSYTLVVAKDGGDKKEPTQAVVEEQVLDKEEPLPEEQRQAKGDAEEMAQKKQEIKVEVKEEKPSVSKEEKPSVSKVEMQPTELVSKEREEKVKETQEDKLEGGAAKRETKEVQTNELKAEKASQKVTKKTKTVQCKVTLLDGTEYSCDLEKHAKGQVLFDKVCEHLNLLEKDYFGLLFQESPEQKNWLDPAKEIKRQLRNLPWLFTFNVKFYPPDPSQLTEDITRYFLCLQLRQDIASGRLPCSFVTHALLGSYTLQAELGDYDPEEHGSIDLSEFQFAPTQTKELEEKVAELHKTHRGLSPAQADSQFLENAKRLSMYGVDLHHAKDSEGVDIKLGVCANGLLIYKDRLRINRFAWPKILKISYKRSNFYIKVRPAELEQFESTIGFKLPNHRAAKRLWKVCVEHHTFYRLVSPEQPPKAKFLTLGSKFRYSGRTQAQTRQASTLIDRPAPHFERTSSKRVSRSLDGAPIGVMDQSLMKDFPGAAGEISAYGPGLVSIAVVQDGDGRREVRSPTKAPHLQLIEGKKNSLRVEGDNIYVRHSNLMLEELDKAQEDILKHQASISELKRNFMESTPEPRPNEWEKRRITPLSLQTQGSSHETLNIVEEKKRAEVGKDERVITEEMNGKEISPGSGPGEIRKVEPVTQKDSTSLSSESSSSSSESEEEDVGEYRPHHRVTEGTIREEQEYEEEVEEEPRPAAKVVEREEAVPEASPVTQAGASVITVETVIQENVGAQKIPGEKSVHEGALKQDMGEEAEEEPQKVNGEVSHVDIDVLPQIICCSEPPVVKTEMVTISDASQRTEISTKEVPIVQTETKTITYESPQIDGGAGGDSGTLLTAQTITSESVSTTTTTHITKTVKGGISETRIEKRIVITGDGDIDHDQALAQAIREAREQHPDMSVTRVVVHKETELAEEGED
| null | null |
actomyosin structure organization [GO:0031032]; cell cycle [GO:0007049]; cell division [GO:0051301]; cortical actin cytoskeleton organization [GO:0030866]; positive regulation of protein localization to cell cortex [GO:1904778]
|
cell cortex [GO:0005938]; cell junction [GO:0030054]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; spectrin [GO:0008091]
|
actin binding [GO:0003779]; PH domain binding [GO:0042731]; spectrin binding [GO:0030507]; structural molecule activity [GO:0005198]
|
PF05902;PF08736;PF09380;PF00373;PF09379;PF04382;
|
1.20.80.10;2.30.29.30;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000269|PubMed:23870127}. Cell membrane {ECO:0000269|PubMed:22361696}.
| null | null | null | null | null |
FUNCTION: Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase (PubMed:23870127). {ECO:0000269|PubMed:23870127}.
|
Homo sapiens (Human)
|
O43493
|
TGON2_HUMAN
|
MRFVVALVLLNVAAAGAVPLLATESVKQEEAGVRPSAGNVSTHPSLSQRPGGSTKSHPEPQTPKDSPSKSSAEAQTPEDTPNKSGAEAKTQKDSSNKSGAEAKTQKGSTSKSGSEAQTTKDSTSKSHPELQTPKDSTGKSGAEAQTPEDSPNRSGAEAKTQKDSPSKSGSEAQTTKDVPNKSGADGQTPKDGSSKSGAEDQTPKDVPNKSGAEKQTPKDGSNKSGAEEQGPIDGPSKSGAEEQTSKDSPNKVVPEQPSRKDHSKPISNPSDNKELPKADTNQLADKGKLSPHAFKTESGEETDLISPPQEEVKSSEPTEDVEPKEAEDDDTGPEEGSPPKEEKEKMSGSASSENREGTLSDSTGSEKDDLYPNGSGNGSAESSHFFAYLVTAAILVAVLYIAHHNKRKIIAFVLEGKRSKVTRRPKASDYQRLDQKS
| null | null | null |
clathrin-coated endocytic vesicle membrane [GO:0030669]; endoplasmic reticulum lumen [GO:0005788]; endosome [GO:0005768]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]; trans-Golgi network transport vesicle [GO:0030140]; transport vesicle [GO:0030133]
| null |
PF17818;
| null | null | null |
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein. Note=Primarily in trans-Golgi network. Cycles between the trans-Golgi network and the cell surface returning via endosomes.
| null | null | null | null | null |
FUNCTION: May be involved in regulating membrane traffic to and from trans-Golgi network.
|
Homo sapiens (Human)
|
O43497
|
CAC1G_HUMAN
|
MDEEEDGAGAEESGQPRSFMRLNDLSGAGGRPGPGSAEKDPGSADSEAEGLPYPALAPVVFFYLSQDSRPRSWCLRTVCNPWFERISMLVILLNCVTLGMFRPCEDIACDSQRCRILQAFDDFIFAFFAVEMVVKMVALGIFGKKCYLGDTWNRLDFFIVIAGMLEYSLDLQNVSFSAVRTVRVLRPLRAINRVPSMRILVTLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNRCFLPENFSLPLSVDLERYYQTENEDESPFICSQPRENGMRSCRSVPTLRGDGGGGPPCGLDYEAYNSSSNTTCVNWNQYYTNCSAGEHNPFKGAINFDNIGYAWIAIFQVITLEGWVDIMYFVMDAHSFYNFIYFILLIIVGSFFMINLCLVVIATQFSETKQRESQLMREQRVRFLSNASTLASFSEPGSCYEELLKYLVYILRKAARRLAQVSRAAGVRVGLLSSPAPLGGQETQPSSSCSRSHRRLSVHHLVHHHHHHHHHYHLGNGTLRAPRASPEIQDRDANGSRRLMLPPPSTPALSGAPPGGAESVHSFYHADCHLEPVRCQAPPPRSPSEASGRTVGSGKVYPTVHTSPPPETLKEKALVEVAASSGPPTLTSLNIPPGPYSSMHKLLETQSTGACQSSCKISSPCLKADSGACGPDSCPYCARAGAGEVELADREMPDSDSEAVYEFTQDAQHSDLRDPHSRRQRSLGPDAEPSSVLAFWRLICDTFRKIVDSKYFGRGIMIAILVNTLSMGIEYHEQPEELTNALEISNIVFTSLFALEMLLKLLVYGPFGYIKNPYNIFDGVIVVISVWEIVGQQGGGLSVLRTFRLMRVLKLVRFLPALQRQLVVLMKTMDNVATFCMLLMLFIFIFSILGMHLFGCKFASERDGDTLPDRKNFDSLLWAIVTVFQILTQEDWNKVLYNGMASTSSWAALYFIALMTFGNYVLFNLLVAILVEGFQAEEISKREDASGQLSCIQLPVDSQGGDANKSESEPDFFSPSLDGDGDRKKCLALVSLGEHPELRKSLLPPLIIHTAATPMSLPKSTSTGLGEALGPASRRTSSSGSAEPGAAHEMKSPPSARSSPHSPWSAASSWTSRRSSRNSLGRAPSLKRRSPSGERRSLLSGEGQESQDEEESSEEERASPAGSDHRHRGSLEREAKSSFDLPDTLQVPGLHRTASGRGSASEHQDCNGKSASGRLARALRPDDPPLDGDDADDEGNLSKGERVRAWIRARLPACCLERDSWSAYIFPPQSRFRLLCHRIITHKMFDHVVLVIIFLNCITIAMERPKIDPHSAERIFLTLSNYIFTAVFLAEMTVKVVALGWCFGEQAYLRSSWNVLDGLLVLISVIDILVSMVSDSGTKILGMLRVLRLLRTLRPLRVISRAQGLKLVVETLMSSLKPIGNIVVICCAFFIIFGILGVQLFKGKFFVCQGEDTRNITNKSDCAEASYRWVRHKYNFDNLGQALMSLFVLASKDGWVDIMYDGLDAVGVDQQPIMNHNPWMLLYFISFLLIVAFFVLNMFVGVVVENFHKCRQHQEEEEARRREEKRLRRLEKKRRNLMLDDVIASGSSASAASEAQCKPYYSDYSRFRLLVHHLCTSHYLDLFITGVIGLNVVTMAMEHYQQPQILDEALKICNYIFTVIFVLESVFKLVAFGFRRFFQDRWNQLDLAIVLLSIMGITLEEIEVNASLPINPTIIRIMRVLRIARVLKLLKMAVGMRALLDTVMQALPQVGNLGLLFMLLFFIFAALGVELFGDLECDETHPCEGLGRHATFRNFGMAFLTLFRVSTGDNWNGIMKDTLRDCDQESTCYNTVISPIYFVSFVLTAQFVLVNVVIAVLMKHLEESNKEAKEEAELEAELELEMKTLSPQPHSPLGSPFLWPGVEGPDSPDSPKPGALHPAAHARSASHFSLEHPTDRQLFDTISLLIQGSLEWELKLMDELAGPGGQPSAFPSAPSLGGSDPQIPLAEMEALSLTSEIVSEPSCSLALTDDSLPDDMHTLLLSALESNMQPHPTELPGPDLLTVRKSGVSRTHSLPNDSYMCRHGSTAEGPLGHRGWGLPKAQSGSVLSVHSQPADTSYILQLPKDAPHLLQPHSAPTWGTIPKLPPPGRSPLAQRPLRRQAAIRTDSLDVQGLGSREDLLAEVSGPSPPLARAYSFWGQSSTQAQQHSRSHSKISKHMTPPAPCPGPEPNWGKGPPETRSSLELDTELSWISGDLLPPGGQEEPPSPRDLKKCYSVEAQSCQRRPTSWLDEQRRHSIAVSCLDSGSQPHLGTDPSNLGGQPLGGPGSRPKKKLSPPSITIDPPESQGPRTPPSPGICLRRRAPSSDSKDPLASGPPDSMAASPSPKKDVLSLSGLSSDPADLDP
| null | null |
AV node cell action potential [GO:0086016]; AV node cell to bundle of His cell signaling [GO:0086027]; calcium ion import [GO:0070509]; calcium ion import across plasma membrane [GO:0098703]; calcium ion transmembrane transport [GO:0070588]; cardiac muscle cell action potential involved in contraction [GO:0086002]; chemical synaptic transmission [GO:0007268]; membrane depolarization during AV node cell action potential [GO:0086045]; membrane depolarization during SA node cell action potential [GO:0086046]; positive regulation of calcium ion-dependent exocytosis [GO:0045956]; regulation of atrial cardiac muscle cell membrane depolarization [GO:0060371]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of membrane potential [GO:0042391]; response to nickel cation [GO:0010045]; SA node cell action potential [GO:0086015]; SA node cell to atrial cardiac muscle cell signaling [GO:0086018]; sinoatrial node development [GO:0003163]
|
cytoplasm [GO:0005737]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; synapse [GO:0045202]; voltage-gated calcium channel complex [GO:0005891]; voltage-gated sodium channel complex [GO:0001518]
|
high voltage-gated calcium channel activity [GO:0008331]; low voltage-gated calcium channel activity [GO:0008332]; scaffold protein binding [GO:0097110]; voltage-gated calcium channel activity involved in AV node cell action potential [GO:0086056]; voltage-gated calcium channel activity involved SA node cell action potential [GO:0086059]; voltage-gated sodium channel activity [GO:0005248]
|
PF00520;
|
1.10.287.70;1.20.120.350;
|
Calcium channel alpha-1 subunit (TC 1.A.1.11) family, CACNA1G subfamily
|
PTM: In response to raising of intracellular calcium, the T-type channels are activated by CaM-kinase II.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26715324}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:26715324}.
| null | null | null | null | null |
FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1G gives rise to T-type calcium currents. T-type calcium channels belong to the 'low-voltage activated (LVA)' group and are strongly blocked by mibefradil. A particularity of this type of channel is an opening at quite negative potentials and a voltage-dependent inactivation. T-type channels serve pacemaking functions in both central neurons and cardiac nodal cells and support calcium signaling in secretory cells and vascular smooth muscle. They may also be involved in the modulation of firing patterns of neurons which is important for information processing as well as in cell growth processes. {ECO:0000269|PubMed:10648811, ECO:0000269|PubMed:10692398, ECO:0000269|PubMed:26456284, ECO:0000269|PubMed:26715324, ECO:0000269|PubMed:29878067}.
|
Homo sapiens (Human)
|
O43502
|
RA51C_HUMAN
|
MRGKTFRFEMQRDLVSFPLSPAVRVKLVSAGFQTAEELLEVKPSELSKEVGISKAEALETLQIIRRECLTNKPRYAGTSESHKKCTALELLEQEHTQGFIITFCSALDDILGGGVPLMKTTEICGAPGVGKTQLCMQLAVDVQIPECFGGVAGEAVFIDTEGSFMVDRVVDLATACIQHLQLIAEKHKGEEHRKALEDFTLDNILSHIYYFRCRDYTELLAQVYLLPDFLSEHSKVRLVIVDGIAFPFRHDLDDLSLRTRLLNGLAQQMISLANNHRLAVILTNQMTTKIDRNQALLVPALGESWGHAATIRLIFHWDRKQRLATLYKSPSQKECTVLFQIKPQGFRDTVVTSACSLQTEGSLSTRKRSRDPEEEL
| null | null |
DNA recombination [GO:0006310]; DNA repair [GO:0006281]; double-strand break repair via homologous recombination [GO:0000724]; female meiosis sister chromatid cohesion [GO:0007066]; male meiosis I [GO:0007141]; meiotic DNA recombinase assembly [GO:0000707]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; reciprocal meiotic recombination [GO:0007131]; sister chromatid cohesion [GO:0007062]; spermatogenesis [GO:0007283]; telomere maintenance via recombination [GO:0000722]
|
cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; Rad51B-Rad51C-Rad51D-XRCC2 complex [GO:0033063]; Rad51C-XRCC3 complex [GO:0033065]; replication fork [GO:0005657]
|
ATP binding [GO:0005524]; ATP-dependent DNA damage sensor activity [GO:0140664]; crossover junction DNA endonuclease activity [GO:0008821]; DNA binding [GO:0003677]; four-way junction DNA binding [GO:0000400]
|
PF08423;
|
1.10.150.20;3.40.50.300;
|
RecA family, RAD51 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12966089, ECO:0000269|PubMed:16215984}. Cytoplasm {ECO:0000269|PubMed:16215984}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16215984}. Mitochondrion {ECO:0000269|PubMed:20413593}. Note=DNA damage induces an increase in nuclear levels. Accumulates in DNA damage induced nuclear foci or RAD51C foci which is formed during the S or G2 phase of cell cycle. Accumulation at DNA lesions requires the presence of NBN/NBS1, ATM and RPA.
| null | null | null | null | null |
FUNCTION: Essential for the homologous recombination (HR) pathway of DNA repair. Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. Part of the RAD51 paralog protein complexes BCDX2 and CX3 which act at different stages of the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 seems to act downstream of BRCA2 recruitment and upstream of RAD51 recruitment; CX3 seems to act downstream of RAD51 recruitment; both complexes bind predominantly to the intersection of the four duplex arms of the Holliday junction (HJ) and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. The BCDX2 subcomplex RAD51B:RAD51C exhibits single-stranded DNA-dependent ATPase activity suggesting an involvement in early stages of the HR pathway. Involved in RAD51 foci formation in response to DNA damage suggesting an involvement in early stages of HR probably in the invasion step. Has an early function in DNA repair in facilitating phosphorylation of the checkpoint kinase CHEK2 and thereby transduction of the damage signal, leading to cell cycle arrest and HR activation. Participates in branch migration and HJ resolution and thus is important for processing HR intermediates late in the DNA repair process; the function may be linked to the CX3 complex. Part of a PALB2-scaffolded HR complex containing BRCA2 and which is thought to play a role in DNA repair by HR. Protects RAD51 from ubiquitin-mediated degradation that is enhanced following DNA damage. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51 and XRCC3. Contributes to DNA cross-link resistance, sister chromatid cohesion and genomic stability. Involved in maintaining centrosome number in mitosis. {ECO:0000269|PubMed:14716019, ECO:0000269|PubMed:16215984, ECO:0000269|PubMed:16395335, ECO:0000269|PubMed:19451272, ECO:0000269|PubMed:19783859, ECO:0000269|PubMed:20413593, ECO:0000269|PubMed:23108668, ECO:0000269|PubMed:23149936}.
|
Homo sapiens (Human)
|
O43504
|
LTOR5_HUMAN
|
MEATLEQHLEDTMKNPSIVGVLCTDSQGLNLGCRGTLSDEHAGVISVLAQQAAKLTSDPTDIPVVCLESDNGNIMIQKHDGITVAVHKMAS
| null | null |
cellular response to amino acid stimulus [GO:0071230]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of gene expression [GO:0010628]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of RNA polymerase II regulatory region sequence-specific DNA binding [GO:1905636]; positive regulation of TOR signaling [GO:0032008]; positive regulation of TORC1 signaling [GO:1904263]; protein localization to lysosome [GO:0061462]; regulation of cell size [GO:0008361]; response to virus [GO:0009615]; TORC1 signaling [GO:0038202]; viral genome replication [GO:0019079]
|
cytosol [GO:0005829]; FNIP-folliculin RagC/D GAP [GO:1990877]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; protein-containing complex [GO:0032991]; Ragulator complex [GO:0071986]
|
guanyl-nucleotide exchange factor activity [GO:0005085]
|
PF16672;
|
3.30.450.30;
|
LAMTOR5 family
| null |
SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:22980980}. Cytoplasm, cytosol {ECO:0000269|PubMed:12773388}.
| null | null | null | null | null |
FUNCTION: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids (PubMed:22980980, PubMed:29158492, PubMed:30181260). Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator plays a dual role for the small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD): it (1) acts as a guanine nucleotide exchange factor (GEF), activating the small GTPases Rag and (2) mediates recruitment of Rag GTPases to the lysosome membrane (PubMed:22980980, PubMed:28935770, PubMed:29107538, PubMed:29158492, PubMed:30181260). Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated (PubMed:22980980, PubMed:29158492, PubMed:30181260). When complexed to BIRC5, interferes with apoptosome assembly, preventing recruitment of pro-caspase-9 to oligomerized APAF1, thereby selectively suppressing apoptosis initiated via the mitochondrial/cytochrome c pathway (PubMed:12773388). {ECO:0000269|PubMed:12773388, ECO:0000269|PubMed:22980980, ECO:0000269|PubMed:28935770, ECO:0000269|PubMed:29107538, ECO:0000269|PubMed:29158492, ECO:0000269|PubMed:30181260}.
|
Homo sapiens (Human)
|
O43505
|
B4GA1_HUMAN
|
MQMSYAIRCAFYQLLLAALMLVAMLQLLYLSLLSGLHGQEEQDQYFEFFPPSPRSVDQVKAQLRTALASGGVLDASGDYRVYRGLLKTTMDPNDVILATHASVDNLLHLSGLLERWEGPLSVSVFAATKEEAQLATVLAYALSSHCPDMRARVAMHLVCPSRYEAAVPDPREPGEFALLRSCQEVFDKLARVAQPGINYALGTNVSYPNNLLRNLAREGANYALVIDVDMVPSEGLWRGLREMLDQSNQWGGTALVVPAFEIRRARRMPMNKNELVQLYQVGEVRPFYYGLCTPCQAPTNYSRWVNLPEESLLRPAYVVPWQDPWEPFYVAGGKVPTFDERFRQYGFNRISQACELHVAGFDFEVLNEGFLVHKGFKEALKFHPQKEAENQHNKILYRQFKQELKAKYPNSPRRC
|
2.4.1.-
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:25279699};
|
axon guidance [GO:0007411]; keratan sulfate biosynthetic process [GO:0018146]; protein O-linked mannosylation [GO:0035269]
|
extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
|
glucuronosyltransferase activity [GO:0015020]; metal ion binding [GO:0046872]; N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase activity [GO:0008532]
|
PF13896;
| null |
Glycosyltransferase 49 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:19587235, ECO:0000269|PubMed:23359570, ECO:0000269|PubMed:25279699}; Single-pass type II membrane protein {ECO:0000269|PubMed:23359570}. Note=Localizes near the trans-Golgi apparatus. {ECO:0000269|PubMed:25279699}.
|
CATALYTIC ACTIVITY: Reaction=3-O-[beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + UDP-alpha-D-glucuronate = 3-O-[beta-D-GlcA-(1->3)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + H(+) + UDP; Xref=Rhea:RHEA:46860, Rhea:RHEA-COMP:15023, Rhea:RHEA-COMP:17482, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:142405, ChEBI:CHEBI:177336; Evidence={ECO:0000269|PubMed:19587235, ECO:0000269|PubMed:23359570, ECO:0000269|PubMed:25279697, ECO:0000269|PubMed:25279699};
| null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:25279697, ECO:0000269|PubMed:25279699, ECO:0000269|PubMed:9405606}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:25279699};
| null |
FUNCTION: Beta-1,4-glucuronyltransferase involved in O-mannosylation of alpha-dystroglycan (DAG1) (PubMed:19587235, PubMed:23359570, PubMed:25279697, PubMed:25279699). Transfers a glucuronic acid (GlcA) residue onto a xylose (Xyl) acceptor to produce the glucuronyl-beta-1,4-xylose-beta disaccharide primer, which is further elongated by LARGE1, during synthesis of phosphorylated O-mannosyl glycan (PubMed:25279697, PubMed:25279699). Phosphorylated O-mannosyl glycan is a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity (PubMed:25279697, PubMed:25279699). Required for axon guidance; via its function in O-mannosylation of alpha-dystroglycan (DAG1) (By similarity). {ECO:0000250|UniProtKB:Q8BWP8, ECO:0000269|PubMed:19587235, ECO:0000269|PubMed:23359570, ECO:0000269|PubMed:25279697, ECO:0000269|PubMed:25279699}.
|
Homo sapiens (Human)
|
O43506
|
ADA20_HUMAN
|
MAVGEPLVHIRVTLLLLWFGMFLSISGHSQARPSQYFTSPEVVIPLKVISRGRGAKAPGWLSYSLRFGGQRYIVHMRVNKLLFAAHLPVFTYTEQHALLQDQPFIQDDCYYHGYVEGVPESLVALSTCSGGFLGMLQINDLVYEIKPISVSATFEHLVYKIDSDDTQFPPMRCGLTEEKIAHQMELQLSYNFTLKQSSFVGWWTHQRFVELVVVVDNIRYLFSQSNATTVQHEVFNVVNIVDSFYHPLEVDVILTGIDIWTASNPLPTSGDLDNVLEDFSIWKNYNLNNRLQHDVAHLFIKDTQGMKLGVAYVKGICQNPFNTGVDVFEDNRLVVFAITLGHELGHNLGMQHDTQWCVCELQWCIMHAYRKVTTKFSNCSYAQYWDSTISSGLCIQPPPYPGNIFRLKYCGNLVVEEGEECDCGTIRQCAKDPCCLLNCTLHPGAACAFGICCKDCKFLPSGTLCRQQVGECDLPEWCNGTSHQCPDDVYVQDGISCNVNAFCYEKTCNNHDIQCKEIFGQDARSASQSCYQEINTQGNRFGHCGIVGTTYVKCWTPDIMCGRVQCENVGVIPNLIEHSTVQQFHLNDTTCWGTDYHLGMAIPDIGEVKDGTVCGPEKICIRKKCASMVHLSQACQPKTCNMRGICNNKQHCHCNHEWAPPYCKDKGYGGSADSGPPPKNNMEGLNVMGKLRYLSLLCLLPLVAFLLFCLHVLFKKRTKSKEDEEG
|
3.4.24.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; Note=Binds 1 zinc ion per subunit. {ECO:0000305};
|
male gonad development [GO:0008584]; proteolysis [GO:0006508]; single fertilization [GO:0007338]
|
external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]; sperm head plasma membrane [GO:1990913]
|
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]
|
PF08516;PF00200;PF01562;PF01421;
|
3.40.390.10;4.10.70.10;
| null |
PTM: Has no obvious cleavage site for furin endopeptidase, suggesting that the proteolytic processing is regulated.
|
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: May be involved in sperm maturation and/or fertilization.
|
Homo sapiens (Human)
|
O43508
|
TNF12_HUMAN
|
MAARRSQRRRGRRGEPGTALLVPLALGLGLALACLGLLLAVVSLGSRASLSAQEPAQEELVAEEDQDPSELNPQTEESQDPAPFLNRLVRPRRSAPKGRKTRARRAIAAHYEVHPRPGQDGAQAGVDGTVSGWEEARINSSSPLRYNRQIGEFIVTRAGLYYLYCQVHFDEGKAVYLKLDLLVDGVLALRCLEEFSATAASSLGPQLRLCQVSGLLALRPGSSLRIRTLPWAHLKAAPFLTYFGLFQVH
| null | null |
angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; cell differentiation [GO:0030154]; endothelial cell migration [GO:0043542]; extrinsic apoptotic signaling pathway [GO:0097191]; immune response [GO:0006955]; positive regulation of angiogenesis [GO:0045766]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of isotype switching to IgA isotypes [GO:0048298]; positive regulation of protein catabolic process [GO:0045732]; signal transduction [GO:0007165]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
|
cytokine activity [GO:0005125]; receptor ligand activity [GO:0048018]; signaling receptor binding [GO:0005102]; tumor necrosis factor receptor binding [GO:0005164]
|
PF00229;
|
2.60.120.40;
|
Tumor necrosis factor family
|
PTM: The soluble form derives from the membrane form by proteolytic processing.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12411489}; Single-pass type II membrane protein {ECO:0000269|PubMed:12411489}.; SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member 12, secreted form]: Secreted.; SUBCELLULAR LOCATION: [Isoform TWE-PRIL]: Cell membrane; Single-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Binds to FN14 and possibly also to TNRFSF12/APO3. Weak inducer of apoptosis in some cell types. Mediates NF-kappa-B activation. Promotes angiogenesis and the proliferation of endothelial cells. Also involved in induction of inflammatory cytokines. Promotes IL8 secretion. {ECO:0000269|PubMed:10085077, ECO:0000269|PubMed:23667509}.
|
Homo sapiens (Human)
|
O43511
|
S26A4_HUMAN
|
MAAPGGRSEPPQLPEYSCSYMVSRPVYSELAFQQQHERRLQERKTLRESLAKCCSCSRKRAFGVLKTLVPILEWLPKYRVKEWLLSDVISGVSTGLVATLQGMAYALLAAVPVGYGLYSAFFPILTYFIFGTSRHISVGPFPVVSLMVGSVVLSMAPDEHFLVSSSNGTVLNTTMIDTAARDTARVLIASALTLLVGIIQLIFGGLQIGFIVRYLADPLVGGFTTAAAFQVLVSQLKIVLNVSTKNYNGVLSIIYTLVEIFQNIGDTNLADFTAGLLTIVVCMAVKELNDRFRHKIPVPIPIEVIVTIIATAISYGANLEKNYNAGIVKSIPRGFLPPELPPVSLFSEMLAASFSIAVVAYAIAVSVGKVYATKYDYTIDGNQEFIAFGISNIFSGFFSCFVATTALSRTAVQESTGGKTQVAGIISAAIVMIAILALGKLLEPLQKSVLAAVVIANLKGMFMQLCDIPRLWRQNKIDAVIWVFTCIVSIILGLDLGLLAGLIFGLLTVVLRVQFPSWNGLGSIPSTDIYKSTKNYKNIEEPQGVKILRFSSPIFYGNVDGFKKCIKSTVGFDAIRVYNKRLKALRKIQKLIKSGQLRATKNGIISDAVSTNNAFEPDEDIEDLEELDIPTKEIEIQVDWNSELPVKVNVPKVPIHSLVLDCGAISFLDVVGVRSLRVIVKEFQRIDVNVYFASLQDYVIEKLEQCGFFDDNIRKDTFFLTVHDAILYLQNQVKSQEGQGSILETITLIQDCKDTLELIETELTEEELDVQDEAMRTLAS
| null | null |
inorganic anion transport [GO:0015698]; iodide transport [GO:0015705]; monoatomic ion transport [GO:0006811]; regulation of pH [GO:0006885]; regulation of protein localization [GO:0032880]; sensory perception of sound [GO:0007605]; sulfate transport [GO:0008272]
|
apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
bicarbonate transmembrane transporter activity [GO:0015106]; chloride transmembrane transporter activity [GO:0015108]; chloride:bicarbonate antiporter activity [GO:0140900]; iodide transmembrane transporter activity [GO:0015111]; oxalate transmembrane transporter activity [GO:0019531]; secondary active sulfate transmembrane transporter activity [GO:0008271]; sulfate transmembrane transporter activity [GO:0015116]
|
PF01740;PF00916;
|
3.30.750.24;
|
SLC26A/SulP transporter (TC 2.A.53) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11932316, ECO:0000269|PubMed:24051746}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:11274445, ECO:0000269|PubMed:35601831}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:10192399, ECO:0000269|PubMed:24051746}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29825; Evidence={ECO:0000305|PubMed:10192399}; CATALYTIC ACTIVITY: Reaction=iodide(out) = iodide(in); Xref=Rhea:RHEA:66324, ChEBI:CHEBI:16382; Evidence={ECO:0000269|PubMed:10192399, ECO:0000269|PubMed:11932316, ECO:0000269|PubMed:12107249, ECO:0000269|PubMed:16684826}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66325; Evidence={ECO:0000305|PubMed:12107249}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:66326; Evidence={ECO:0000305|PubMed:12107249}; CATALYTIC ACTIVITY: Reaction=chloride(out) + hydrogencarbonate(in) = chloride(in) + hydrogencarbonate(out); Xref=Rhea:RHEA:72363, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:24051746, ECO:0000269|PubMed:35601831}; CATALYTIC ACTIVITY: Reaction=hydrogencarbonate(out) + iodide(in) = hydrogencarbonate(in) + iodide(out); Xref=Rhea:RHEA:72375, ChEBI:CHEBI:16382, ChEBI:CHEBI:17544; Evidence={ECO:0000250|UniProtKB:Q9R155}; CATALYTIC ACTIVITY: Reaction=chloride(out) + iodide(in) = chloride(in) + iodide(out); Xref=Rhea:RHEA:72379, ChEBI:CHEBI:16382, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:15155570, ECO:0000269|PubMed:24051746}; CATALYTIC ACTIVITY: Reaction=chloride(out) + formate(in) = chloride(in) + formate(out); Xref=Rhea:RHEA:72267, ChEBI:CHEBI:15740, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:10644529};
| null | null | null | null |
FUNCTION: Sodium-independent transporter of chloride and iodide (PubMed:10192399, PubMed:11932316, PubMed:12107249, PubMed:16684826, PubMed:24051746). Mediates electroneutral chloride-bicarbonate, chloride-iodide and chloride-formate exchange with 1:1 stoichiometry (PubMed:10644529, PubMed:15155570, PubMed:24051746, PubMed:35601831). Mediates electroneutral iodide-bicarbonate exchange (By similarity). {ECO:0000250|UniProtKB:Q9R155, ECO:0000269|PubMed:10192399, ECO:0000269|PubMed:10644529, ECO:0000269|PubMed:11932316, ECO:0000269|PubMed:12107249, ECO:0000269|PubMed:15155570, ECO:0000269|PubMed:16684826, ECO:0000269|PubMed:24051746, ECO:0000269|PubMed:35601831}.
|
Homo sapiens (Human)
|
O43513
|
MED7_HUMAN
|
MGEPQQVSALPPPPMQYIKEYTDENIQEGLAPKPPPPIKDSYMMFGNQFQCDDLIIRPLESQGIERLHPMQFDHKKELRKLNMSILINFLDLLDILIRSPGSIKREEKLEDLKLLFVHVHHLINEYRPHQARETLRVMMEVQKRQRLETAERFQKHLERVIEMIQNCLASLPDDLPHSEAGMRVKTEPMDADDSNNCTGQNEHQRENSGHRRDQIIEKDAALCVLIDEMNERP
| null | null |
positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261]; protein ubiquitination [GO:0016567]; regulation of transcription by RNA polymerase II [GO:0006357]; RNA polymerase II preinitiation complex assembly [GO:0051123]; somatic stem cell population maintenance [GO:0035019]; transcription initiation at RNA polymerase II promoter [GO:0006367]
|
core mediator complex [GO:0070847]; mediator complex [GO:0016592]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]; ubiquitin ligase complex [GO:0000151]
|
transcription coactivator activity [GO:0003713]; ubiquitin protein ligase activity [GO:0061630]
|
PF05983;
|
6.10.140.200;
|
Mediator complex subunit 7 family
|
PTM: Constitutively sumoylated. {ECO:0000269|PubMed:17709345}.
|
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
|
Homo sapiens (Human)
|
O43516
|
WIPF1_HUMAN
|
MPVPPPPAPPPPPTFALANTEKPTLNKTEQAGRNALLSDISKGKKLKKTVTNDRSAPILDKPKGAGAGGGGGGFGGGGGFGGGGGGGGGGSFGGGGPPGLGGLFQAGMPKLRSTANRDNDSGGSRPPLLPPGGRSTSAKPFSPPSGPGRFPVPSPGHRSGPPEPQRNRMPPPRPDVGSKPDSIPPPVPSTPRPIQSSPHNRGSPPVPGGPRQPSPGPTPPPFPGNRGTALGGGSIRQSPLSSSSPFSNRPPLPPTPSRALDDKPPPPPPPVGNRPSIHREAVPPPPPQNNKPPVPSTPRPSASSQAPPPPPPPSRPGPPPLPPSSSGNDETPRLPQRNLSLSSSTPPLPSPGRSGPLPPPPSERPPPPVRDPPGRSGPLPPPPPVSRNGSTSRALPATPQLPSRSGVDSPRSGPRPPLPPDRPSAGAPPPPPPSTSIRNGFQDSPCEDEWESRFYFHPISDLPPPEPYVQTTKSYPSKLARNESRSGSNRRERGAPPLPPIPR
| null | null |
actin filament-based movement [GO:0030048]; actin polymerization or depolymerization [GO:0008154]; protein-containing complex assembly [GO:0065003]; response to other organism [GO:0051707]
|
actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; ruffle [GO:0001726]
|
actin binding [GO:0003779]; profilin binding [GO:0005522]; protein folding chaperone [GO:0044183]; SH3 domain binding [GO:0017124]
|
PF02205;
|
2.30.29.30;
|
Verprolin family
| null |
SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, ruffle {ECO:0000269|PubMed:19910490}. Note=Vesicle surfaces and along actin tails. Colocalizes with actin stress fibers. When coexpressed with WASL, no longer associated with actin filaments but accumulated in perinuclear and cortical areas like WASL (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Plays a role in the reorganization of the actin cytoskeleton. Contributes with NCK1 and GRB2 in the recruitment and activation of WASL. May participate in regulating the subcellular localization of WASL, resulting in the disassembly of stress fibers in favor of filopodia formation. Plays a role in the formation of cell ruffles (By similarity). Plays an important role in the intracellular motility of vaccinia virus by functioning as an adapter for recruiting WASL to vaccinia virus. {ECO:0000250, ECO:0000269|PubMed:10878810, ECO:0000269|PubMed:19910490, ECO:0000269|PubMed:9405671}.
|
Homo sapiens (Human)
|
O43520
|
AT8B1_HUMAN
|
MSTERDSETTFDEDSQPNDEVVPYSDDETEDELDDQGSAVEPEQNRVNREAEENREPFRKECTWQVKANDRKYHEQPHFMNTKFLCIKESKYANNAIKTYKYNAFTFIPMNLFEQFKRAANLYFLALLILQAVPQISTLAWYTTLVPLLVVLGVTAIKDLVDDVARHKMDKEINNRTCEVIKDGRFKVAKWKEIQVGDVIRLKKNDFVPADILLLSSSEPNSLCYVETAELDGETNLKFKMSLEITDQYLQREDTLATFDGFIECEEPNNRLDKFTGTLFWRNTSFPLDADKILLRGCVIRNTDFCHGLVIFAGADTKIMKNSGKTRFKRTKIDYLMNYMVYTIFVVLILLSAGLAIGHAYWEAQVGNSSWYLYDGEDDTPSYRGFLIFWGYIIVLNTMVPISLYVSVEVIRLGQSHFINWDLQMYYAEKDTPAKARTTTLNEQLGQIHYIFSDKTGTLTQNIMTFKKCCINGQIYGDHRDASQHNHNKIEQVDFSWNTYADGKLAFYDHYLIEQIQSGKEPEVRQFFFLLAVCHTVMVDRTDGQLNYQAASPDEGALVNAARNFGFAFLARTQNTITISELGTERTYNVLAILDFNSDRKRMSIIVRTPEGNIKLYCKGADTVIYERLHRMNPTKQETQDALDIFANETLRTLCLCYKEIEEKEFTEWNKKFMAASVASTNRDEALDKVYEEIEKDLILLGATAIEDKLQDGVPETISKLAKADIKIWVLTGDKKETAENIGFACELLTEDTTICYGEDINSLLHARMENQRNRGGVYAKFAPPVQESFFPPGGNRALIITGSWLNEILLEKKTKRNKILKLKFPRTEEERRMRTQSKRRLEAKKEQRQKNFVDLACECSAVICCRVTPKQKAMVVDLVKRYKKAITLAIGDGANDVNMIKTAHIGVGISGQEGMQAVMSSDYSFAQFRYLQRLLLVHGRWSYIRMCKFLRYFFYKNFAFTLVHFWYSFFNGYSAQTAYEDWFITLYNVLYTSLPVLLMGLLDQDVSDKLSLRFPGLYIVGQRDLLFNYKRFFVSLLHGVLTSMILFFIPLGAYLQTVGQDGEAPSDYQSFAVTIASALVITVNFQIGLDTSYWTFVNAFSIFGSIALYFGIMFDFHSAGIHVLFPSAFQFTGTASNALRQPYIWLTIILAVAVCLLPVVAIRFLSMTIWPSESDKIQKHRKRLKAEEQWQRRQQVFRRGVSTRRSAYAFSHQRGYADLISSGRSIRKKRSPLDAIVADGTAEYRRTGDS
|
7.6.2.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9Y2Q0};
|
apical protein localization [GO:0045176]; bile acid and bile salt transport [GO:0015721]; bile acid metabolic process [GO:0008206]; Golgi organization [GO:0007030]; inner ear receptor cell development [GO:0060119]; monoatomic ion transmembrane transport [GO:0034220]; negative regulation of DNA-templated transcription [GO:0045892]; phospholipid translocation [GO:0045332]; regulation of chloride transport [GO:2001225]; regulation of microvillus assembly [GO:0032534]; regulation of plasma membrane organization [GO:1903729]; sensory perception of sound [GO:0007605]; vestibulocochlear nerve formation [GO:0021650]; xenobiotic transmembrane transport [GO:0006855]
|
apical plasma membrane [GO:0016324]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; phospholipid-translocating ATPase complex [GO:1990531]; plasma membrane [GO:0005886]; stereocilium [GO:0032420]; trans-Golgi network [GO:0005802]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; cardiolipin binding [GO:1901612]; magnesium ion binding [GO:0000287]; phosphatidylcholine flippase activity [GO:0140345]; phosphatidylcholine floppase activity [GO:0090554]; phosphatidylserine flippase activity [GO:0140346]; phosphatidylserine floppase activity [GO:0090556]
|
PF13246;PF00122;PF16212;PF16209;
|
3.40.1110.10;2.70.150.10;3.40.50.1000;
|
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IV subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17948906, ECO:0000269|PubMed:20947505, ECO:0000269|PubMed:20961850, ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:25315773}; Multi-pass membrane protein. Apical cell membrane {ECO:0000269|PubMed:20512993}. Cell projection, stereocilium {ECO:0000250|UniProtKB:Q148W0}. Endoplasmic reticulum {ECO:0000269|PubMed:17948906, ECO:0000269|PubMed:20947505, ECO:0000269|PubMed:20961850, ECO:0000269|PubMed:21914794}. Golgi apparatus {ECO:0000269|PubMed:20961850}. Note=Exit from the endoplasmic reticulum requires the presence of TMEM30A or TMEM30B (PubMed:20947505). Localizes to apical membranes in epithelial cells (PubMed:20512993). {ECO:0000269|PubMed:20512993, ECO:0000269|PubMed:20947505}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000269|PubMed:17948906, ECO:0000269|PubMed:25315773}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57643, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:25315773}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38584; Evidence={ECO:0000305|PubMed:25315773}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57262, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:17948906}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568; Evidence={ECO:0000305|PubMed:17948906};
| null | null | null | null |
FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phospholipids, in particular phosphatidylcholines (PC), from the outer to the inner leaflet of the plasma membrane (PubMed:17948906, PubMed:25315773). May participate in the establishment of the canalicular membrane integrity by ensuring asymmetric distribution of phospholipids in the canicular membrane (By similarity). Thus may have a role in the regulation of bile acids transport into the canaliculus, uptake of bile acids from intestinal contents into intestinal mucosa or both and protect hepatocytes from bile salts (By similarity). Involved in the microvillus formation in polarized epithelial cells; the function seems to be independent from its flippase activity (PubMed:20512993). Participates in correct apical membrane localization of CDC42, CFTR and SLC10A2 (PubMed:25239307, PubMed:27301931). Enables CDC42 clustering at the apical membrane during enterocyte polarization through the interaction between CDC42 polybasic region and negatively charged membrane lipids provided by ATP8B1 (By similarity). Together with TMEM30A is involved in uptake of the synthetic drug alkylphospholipid perifosine (PubMed:20510206). Required for the preservation of cochlear hair cells in the inner ear (By similarity). May act as cardiolipin transporter during inflammatory injury (By similarity). {ECO:0000250|UniProtKB:Q148W0, ECO:0000269|PubMed:17948906, ECO:0000269|PubMed:20510206, ECO:0000269|PubMed:20512993, ECO:0000269|PubMed:25239307, ECO:0000269|PubMed:27301931}.
|
Homo sapiens (Human)
|
O43521
|
B2L11_HUMAN
|
MAKQPSDVSSECDREGRQLQPAERPPQLRPGAPTSLQTEPQGNPEGNHGGEGDSCPHGSPQGPLAPPASPGPFATRSPLFIFMRRSSLLSRSSSGYFSFDTDRSPAPMSCDKSTQTPSPPCQAFNHYLSAMASMRQAEPADMRPEIWIAQELRRIGDEFNAYYARRVFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH
| null | null |
activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; apoptotic process [GO:0006915]; apoptotic process involved in embryonic digit morphogenesis [GO:1902263]; B cell homeostasis [GO:0001782]; cell-matrix adhesion [GO:0007160]; cellular response to glucocorticoid stimulus [GO:0071385]; developmental pigmentation [GO:0048066]; ear development [GO:0043583]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; in utero embryonic development [GO:0001701]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; kidney development [GO:0001822]; male gonad development [GO:0008584]; mammary gland development [GO:0030879]; meiosis I [GO:0007127]; myeloid cell homeostasis [GO:0002262]; odontogenesis of dentin-containing tooth [GO:0042475]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell cycle [GO:0045787]; positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902237]; positive regulation of fibroblast apoptotic process [GO:2000271]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of IRE1-mediated unfolded protein response [GO:1903896]; positive regulation of mitochondrial membrane permeability involved in apoptotic process [GO:1902110]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of protein-containing complex assembly [GO:0031334]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; positive regulation of T cell apoptotic process [GO:0070234]; post-embryonic development [GO:0009791]; regulation of apoptotic process [GO:0042981]; regulation of developmental pigmentation [GO:0048070]; regulation of organ growth [GO:0046620]; response to endoplasmic reticulum stress [GO:0034976]; spermatogenesis [GO:0007283]; spleen development [GO:0048536]; T cell homeostasis [GO:0043029]; thymocyte apoptotic process [GO:0070242]; thymus development [GO:0048538]; tube formation [GO:0035148]
|
Bcl-2 family protein complex [GO:0097136]; BIM-BCL-2 complex [GO:0097141]; BIM-BCL-xl complex [GO:0097140]; cytosol [GO:0005829]; endomembrane system [GO:0012505]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]
|
microtubule binding [GO:0008017]; protein kinase binding [GO:0019901]
|
PF08945;PF06773;
| null |
Bcl-2 family
|
PTM: Phosphorylation at Ser-69 by MAPK1/MAPK3 leads to interaction with TRIM2 and polyubiquitination, followed by proteasomal degradation (PubMed:15486195, PubMed:21478148). Deubiquitination catalyzed by USP27X stabilizes the protein (By similarity). {ECO:0000250|UniProtKB:O54918, ECO:0000269|PubMed:15486195, ECO:0000269|PubMed:21478148}.; PTM: Ubiquitination by TRIM2 following phosphorylation by MAPK1/MAPK3 leads to proteasomal degradation. Conversely, deubiquitination catalyzed by USP27X stabilizes the protein. {ECO:0000250|UniProtKB:O54918}.
|
SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Associated with intracytoplasmic membranes. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform BimEL]: Mitochondrion. Note=Translocates from microtubules to mitochondria on loss of cell adherence.; SUBCELLULAR LOCATION: [Isoform BimL]: Mitochondrion.; SUBCELLULAR LOCATION: [Isoform BimS]: Mitochondrion.; SUBCELLULAR LOCATION: [Isoform Bim-alpha1]: Mitochondrion.
| null | null | null | null | null |
FUNCTION: Induces apoptosis and anoikis. Isoform BimL is more potent than isoform BimEL. Isoform Bim-alpha1, isoform Bim-alpha2 and isoform Bim-alpha3 induce apoptosis, although less potent than isoform BimEL, isoform BimL and isoform BimS. Isoform Bim-gamma induces apoptosis. Isoform Bim-alpha3 induces apoptosis possibly through a caspase-mediated pathway. Isoform BimAC and isoform BimABC lack the ability to induce apoptosis. {ECO:0000269|PubMed:11997495, ECO:0000269|PubMed:15486195, ECO:0000269|PubMed:15661735, ECO:0000269|PubMed:9430630}.
|
Homo sapiens (Human)
|
O43524
|
FOXO3_HUMAN
|
MAEAPASPAPLSPLEVELDPEFEPQSRPRSCTWPLQRPELQASPAKPSGETAADSMIPEEEDDEDDEDGGGRAGSAMAIGGGGGSGTLGSGLLLEDSARVLAPGGQDPGSGPATAAGGLSGGTQALLQPQQPLPPPQPGAAGGSGQPRKCSSRRNAWGNLSYADLITRAIESSPDKRLTLSQIYEWMVRCVPYFKDKGDSNSSAGWKNSIRHNLSLHSRFMRVQNEGTGKSSWWIINPDGGKSGKAPRRRAVSMDNSNKYTKSRGRAAKKKAALQTAPESADDSPSQLSKWPGSPTSRSSDELDAWTDFRSRTNSNASTVSGRLSPIMASTELDEVQDDDAPLSPMLYSSSASLSPSVSKPCTVELPRLTDMAGTMNLNDGLTENLMDDLLDNITLPPSQPSPTGGLMQRSSSFPYTTKGSGLGSPTSSFNSTVFGPSSLNSLRQSPMQTIQENKPATFSSMSHYGNQTLQDLLTSDSLSHSDVMMTQSDPLMSQASTAVSAQNSRRNVMLRNDPMMSFAAQPNQGSLVNQNLLHHQHQTQGALGGSRALSNSVSNMGLSESSSLGSAKHQQQSPVSQSMQTLSDSLSGSSLYSTSANLPVMGHEKFPSDLDLDMFNGSLECDMESIIRSELMDADGLDFNFDSLISTQNVVGLNVGNFTGAKQASSQSWVPG
| null | null |
antral ovarian follicle growth [GO:0001547]; brain morphogenesis [GO:0048854]; canonical Wnt signaling pathway [GO:0060070]; cellular response to amyloid-beta [GO:1904646]; cellular response to corticosterone stimulus [GO:0071386]; cellular response to glucose starvation [GO:0042149]; cellular response to glucose stimulus [GO:0071333]; cellular response to hypoxia [GO:0071456]; cellular response to nerve growth factor stimulus [GO:1990090]; cellular response to oxidative stress [GO:0034599]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; initiation of primordial ovarian follicle growth [GO:0001544]; mitochondrial transcription [GO:0006390]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cell migration [GO:0030336]; negative regulation of neuron differentiation [GO:0045665]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuronal stem cell population maintenance [GO:0097150]; oocyte maturation [GO:0001556]; ovulation from ovarian follicle [GO:0001542]; positive regulation of apoptotic process [GO:0043065]; positive regulation of autophagy [GO:0010508]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of endothelial cell apoptotic process [GO:2000353]; positive regulation of erythrocyte differentiation [GO:0045648]; positive regulation of hydrogen peroxide-mediated programmed cell death [GO:1901300]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of muscle atrophy [GO:0014737]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of reactive oxygen species biosynthetic process [GO:1903428]; positive regulation of regulatory T cell differentiation [GO:0045591]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of neural precursor cell proliferation [GO:2000177]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of translation [GO:0006417]; response to dexamethasone [GO:0071548]; response to fatty acid [GO:0070542]; response to starvation [GO:0042594]; response to water-immersion restraint stress [GO:1990785]; response to xenobiotic stimulus [GO:0009410]; tumor necrosis factor-mediated signaling pathway [GO:0033209]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrial outer membrane [GO:0005741]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; RNA polymerase II transcription repressor complex [GO:0090571]
|
beta-catenin binding [GO:0008013]; chromatin DNA binding [GO:0031490]; 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]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; mitochondrial transcription factor activity [GO:0034246]; protein kinase binding [GO:0019901]; 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]; transcription coregulator binding [GO:0001221]
|
PF00250;PF16676;PF16675;
|
6.10.250.1690;1.10.10.10;
| null |
PTM: In the presence of survival factors such as IGF-1, phosphorylated on Thr-32 and Ser-253 by AKT1/PKB (PubMed:10102273). This phosphorylated form then interacts with 14-3-3 proteins and is retained in the cytoplasm (PubMed:10102273). Survival factor withdrawal induces dephosphorylation and promotes translocation to the nucleus where the dephosphorylated protein induces transcription of target genes and triggers apoptosis (PubMed:10102273). Although AKT1/PKB doesn't appear to phosphorylate Ser-315 directly, it may activate other kinases that trigger phosphorylation at this residue (PubMed:10102273, PubMed:11154281). Phosphorylated by STK4/MST1 on Ser-209 upon oxidative stress, which leads to dissociation from YWHAB/14-3-3-beta and nuclear translocation (PubMed:16751106). Phosphorylated by PIM1 (PubMed:18593906). Phosphorylation by AMPK leads to the activation of transcriptional activity without affecting subcellular localization (PubMed:17711846). In response to metabolic stress, phosphorylated by AMPK on Ser-30 which mediates FOXO3 mitochondrial translocation (PubMed:29445193). Phosphorylation by MAPKAPK5 promotes nuclear localization and DNA-binding, leading to induction of miR-34b and miR-34c expression, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent its translation (PubMed:21329882). Phosphorylated by CHUK/IKKA and IKBKB/IKKB (PubMed:15084260). TNF-induced inactivation of FOXO3 requires its phosphorylation at Ser-644 by IKBKB/IKKB which promotes FOXO3 retention in the cytoplasm, polyubiquitination and ubiquitin-mediated proteasomal degradation (PubMed:15084260). May be dephosphorylated by calcineurin A on Ser-299 which abolishes FOXO3 transcriptional activity (By similarity). In cancer cells, ERK mediated-phosphorylation of Ser-12 is required for mitochondrial translocation of FOXO3 in response to metabolic stress or chemotherapeutic agents (PubMed:29445193). Phosphorylation at Ser-253 promotes its degradation by the proteasome (PubMed:30513302). Dephosphorylation at Ser-253 by protein phosphatase 2A (PPP2CA) promotes its stabilization; interaction with PPP2CA is enhanced by AMBRA1 (PubMed:30513302). {ECO:0000250|UniProtKB:Q9WVH4, ECO:0000269|PubMed:10102273, ECO:0000269|PubMed:11154281, ECO:0000269|PubMed:15084260, ECO:0000269|PubMed:16751106, ECO:0000269|PubMed:17711846, ECO:0000269|PubMed:18593906, ECO:0000269|PubMed:21329882, ECO:0000269|PubMed:29445193, ECO:0000269|PubMed:30513302}.; PTM: Deacetylation by SIRT1 or SIRT2 stimulates interaction of FOXO3 with SKP2 and facilitates SCF(SKP2)-mediated FOXO3 ubiquitination and proteasomal degradation (PubMed:21841822). Deacetylation by SIRT2 stimulates FOXO3-mediated transcriptional activity in response to oxidative stress (By similarity). Deacetylated by SIRT3 (PubMed:23283301). Deacetylation by SIRT3 stimulates FOXO3-mediated mtDNA transcriptional activity in response to metabolic stress (PubMed:23283301). {ECO:0000250|UniProtKB:Q9WVH4, ECO:0000269|PubMed:21841822, ECO:0000269|PubMed:23283301}.; PTM: Heavily methylated by SET9 which decreases stability, while moderately increasing transcriptional activity. The main methylation site is Lys-271. Methylation doesn't affect subcellular location. {ECO:0000269|PubMed:22820736}.; PTM: Polyubiquitinated. Ubiquitinated by a SCF complex containing SKP2, leading to proteasomal degradation. {ECO:0000269|PubMed:21841822}.; PTM: The N-terminus is cleaved following import into the mitochondrion. {ECO:0000269|PubMed:29445193}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10102273, ECO:0000269|PubMed:15084260, ECO:0000269|PubMed:16751106, ECO:0000269|PubMed:17711846, ECO:0000269|PubMed:21329882, ECO:0000269|PubMed:22313691, ECO:0000269|PubMed:22761832, ECO:0000269|PubMed:23283301}. Nucleus {ECO:0000269|PubMed:10102273, ECO:0000269|PubMed:15084260, ECO:0000269|PubMed:16751106, ECO:0000269|PubMed:17711846, ECO:0000269|PubMed:21329882, ECO:0000269|PubMed:22313691, ECO:0000269|PubMed:22761832, ECO:0000269|PubMed:23283301, ECO:0000269|PubMed:29445193}. Mitochondrion matrix {ECO:0000269|PubMed:23283301, ECO:0000269|PubMed:29445193}. Mitochondrion outer membrane {ECO:0000269|PubMed:29445193}; Peripheral membrane protein {ECO:0000269|PubMed:29445193}; Cytoplasmic side {ECO:0000269|PubMed:29445193}. Note=Retention in the cytoplasm contributes to its inactivation (PubMed:10102273, PubMed:15084260, PubMed:16751106). Translocates to the nucleus upon oxidative stress and in the absence of survival factors (PubMed:10102273, PubMed:16751106). Translocates from the cytosol to the nucleus following dephosphorylation in response to autophagy-inducing stimuli (By similarity). Translocates in a AMPK-dependent manner into the mitochondrion in response to metabolic stress (PubMed:23283301, PubMed:29445193). Serum deprivation increases localization to the nucleus, leading to activate expression of SOX9 and subsequent chondrogenesis (By similarity). {ECO:0000250|UniProtKB:Q9WVH4, ECO:0000269|PubMed:10102273, ECO:0000269|PubMed:15084260, ECO:0000269|PubMed:16751106, ECO:0000269|PubMed:23283301, ECO:0000269|PubMed:29445193}.
| null | null | null | null | null |
FUNCTION: Transcriptional activator that recognizes and binds to the DNA sequence 5'-[AG]TAAA[TC]A-3' and regulates different processes, such as apoptosis and autophagy (PubMed:10102273, PubMed:16751106, PubMed:21329882, PubMed:30513302). Acts as a positive regulator of autophagy in skeletal muscle: in starved cells, enters the nucleus following dephosphorylation and binds the promoters of autophagy genes, such as GABARAP1L, MAP1LC3B and ATG12, thereby activating their expression, resulting in proteolysis of skeletal muscle proteins (By similarity). Triggers apoptosis in the absence of survival factors, including neuronal cell death upon oxidative stress (PubMed:10102273, PubMed:16751106). Participates in post-transcriptional regulation of MYC: following phosphorylation by MAPKAPK5, promotes induction of miR-34b and miR-34c expression, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent its translation (PubMed:21329882). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription (PubMed:23283301). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription. Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Also acts as a key regulator of regulatory T-cells (Treg) differentiation by activating expression of FOXP3 (PubMed:30513302). {ECO:0000250|UniProtKB:Q9WVH4, ECO:0000269|PubMed:10102273, ECO:0000269|PubMed:16751106, ECO:0000269|PubMed:21329882, ECO:0000269|PubMed:23283301, ECO:0000269|PubMed:30513302}.
|
Homo sapiens (Human)
|
O43525
|
KCNQ3_HUMAN
|
MGLKARRAAGAAGGGGDGGGGGGGAANPAGGDAAAAGDEERKVGLAPGDVEQVTLALGAGADKDGTLLLEGGGRDEGQRRTPQGIGLLAKTPLSRPVKRNNAKYRRIQTLIYDALERPRGWALLYHALVFLIVLGCLILAVLTTFKEYETVSGDWLLLLETFAIFIFGAEFALRIWAAGCCCRYKGWRGRLKFARKPLCMLDIFVLIASVPVVAVGNQGNVLATSLRSLRFLQILRMLRMDRRGGTWKLLGSAICAHSKELITAWYIGFLTLILSSFLVYLVEKDVPEVDAQGEEMKEEFETYADALWWGLITLATIGYGDKTPKTWEGRLIAATFSLIGVSFFALPAGILGSGLALKVQEQHRQKHFEKRRKPAAELIQAAWRYYATNPNRIDLVATWRFYESVVSFPFFRKEQLEAASSQKLGLLDRVRLSNPRGSNTKGKLFTPLNVDAIEESPSKEPKPVGLNNKERFRTAFRMKAYAFWQSSEDAGTGDPMAEDRGYGNDFPIEDMIPTLKAAIRAVRILQFRLYKKKFKETLRPYDVKDVIEQYSAGHLDMLSRIKYLQTRIDMIFTPGPPSTPKHKKSQKGSAFTFPSQQSPRNEPYVARPSTSEIEDQSMMGKFVKVERQVQDMGKKLDFLVDMHMQHMERLQVQVTEYYPTKGTSSPAEAEKKEDNRYSDLKTIICNYSETGPPEPPYSFHQVTIDKVSPYGFFAHDPVNLPRGGPSSGKVQATPPSSATTYVERPTVLPILTLLDSRVSCHSQADLQGPYSDRISPRQRRSITRDSDTPLSLMSVNHEELERSPSGFSISQDRDDYVFGPNGGSSWMREKRYLAEGETDTDTDPFTPSGSMPLSSTGDGISDSVWTPSNKPI
| null | null |
action potential initiation [GO:0099610]; apoptosome assembly [GO:0097314]; cellular response to calcium ion [GO:0071277]; cellular response to xenobiotic stimulus [GO:0071466]; chemical synaptic transmission [GO:0007268]; endocytosis [GO:0006897]; excitatory chemical synaptic transmission [GO:0098976]; exocytosis [GO:0006887]; gene expression [GO:0010467]; inhibitory chemical synaptic transmission [GO:0098977]; membrane hyperpolarization [GO:0060081]; mitochondrial depolarization [GO:0051882]; nerve development [GO:0021675]; neuron apoptotic process [GO:0051402]; neuron remodeling [GO:0016322]; neuronal action potential [GO:0019228]; potassium ion transmembrane transport [GO:0071805]; protein import into nucleus [GO:0006606]; protein targeting [GO:0006605]; psychomotor behavior [GO:0036343]; regulation of action potential firing threshold [GO:0099611]; regulation of synaptic plasticity [GO:0048167]; response to auditory stimulus [GO:0010996]; response to organic cyclic compound [GO:0014070]; sensory perception of sound [GO:0007605]; substantia propria of cornea development [GO:1903701]
|
axon initial segment [GO:0043194]; cell surface [GO:0009986]; mitochondrion [GO:0005739]; node of Ranvier [GO:0033268]; plasma membrane [GO:0005886]; synapse [GO:0045202]; voltage-gated potassium channel complex [GO:0008076]
|
calmodulin binding [GO:0005516]; voltage-gated potassium channel activity [GO:0005249]
|
PF00520;PF03520;PF11956;
|
1.10.287.70;6.10.140.1910;
|
Potassium channel family, KQT (TC 1.A.1.15) subfamily, Kv7.3/KCNQ3 sub-subfamily
|
PTM: KCNQ2/KCNQ3 are ubiquitinated by NEDD4L. Ubiquitination leads to protein degradation (Probable). Degradation induced by NEDD4L is inhibited by USP36 (PubMed:27445338). {ECO:0000269|PubMed:27445338, ECO:0000305|PubMed:27445338}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10788442}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Associates with KCNQ2 or KCNQ5 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs. Therefore, it is important in the regulation of neuronal excitability. KCNQ2-KCNQ3 channel is selectively permeable to other cations besides potassium, in decreasing order of affinity K(+) > Rb(+) > Cs(+) > Na(+). Associates with Na(+)-coupled myo-inositol symporter SLC5A3 forming a coregulatory complex that alters ion selectivity, increasing Na(+) and Cs(+) permeation relative to K(+) permeation (PubMed:28793216). {ECO:0000269|PubMed:11159685, ECO:0000269|PubMed:14534157, ECO:0000269|PubMed:16319223, ECO:0000269|PubMed:28793216, ECO:0000269|PubMed:9872318}.
|
Homo sapiens (Human)
|
O43526
|
KCNQ2_HUMAN
|
MVQKSRNGGVYPGPSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSILSKPRAGGAGAGKPPKRNAFYRKLQNFLYNVLERPRGWAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASIAVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVYLAEKGENDHFDTYADALWWGLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTWQYYERTVTVPMYSSQTQTYGASRLIPPLNQLELLRNLKSKSGLAFRKDPPPEPSPSKGSPCRGPLCGCCPGRSSQKVSLKDRVFSSPRGVAAKGKGSPQAQTVRRSPSADQSLEDSPSKVPKSWSFGDRSRARQAFRIKGAASRQNSEEASLPGEDIVDDKSCPCEFVTEDLTPGLKVSIRAVCVMRFLVSKRKFKESLRPYDVMDVIEQYSAGHLDMLSRIKSLQSRVDQIVGRGPAITDKDRTKGPAEAELPEDPSMMGRLGKVEKQVLSMEKKLDFLVNIYMQRMGIPPTETEAYFGAKEPEPAPPYHSPEDSREHVDRHGCIVKIVRSSSSTGQKNFSAPPAAPPVQCPPSTSWQPQSHPRQGHGTSPVGDHGSLVRIPPPPAHERSLSAYGGGNRASMEFLRQEDTPGCRPPEGNLRDSDTSISIPSVDHEELERSFSGFSISQSKENLDALNSCYAAVAPCAKVRPYIAEGESDTDSDLCTPCGPPPRSATGEGPFGDVGWAGPRK
| null | null |
chemical synaptic transmission [GO:0007268]; nervous system development [GO:0007399]; potassium ion transmembrane transport [GO:0071805]
|
axon initial segment [GO:0043194]; node of Ranvier [GO:0033268]; plasma membrane [GO:0005886]; synapse [GO:0045202]; voltage-gated potassium channel complex [GO:0008076]
|
ankyrin binding [GO:0030506]; calmodulin binding [GO:0005516]; voltage-gated potassium channel activity [GO:0005249]
|
PF00520;PF16642;PF03520;PF11956;
|
1.10.287.70;6.10.140.1910;
|
Potassium channel family, KQT (TC 1.A.1.15) subfamily, Kv7.2/KCNQ2 sub-subfamily
|
PTM: KCNQ2/KCNQ3 heteromeric current can be increased by intracellular cyclic AMP, an effect that depends on phosphorylation of Ser-52 in the N-terminal region. {ECO:0000269|PubMed:16319223, ECO:0000269|PubMed:9872318}.; PTM: KCNQ2/KCNQ3 are ubiquitinated by NEDD4L. Ubiquitination leads to protein degradation (Probable). Degradation induced by NEDD4L is inhibited by USP36 (PubMed:27445338). {ECO:0000269|PubMed:27445338, ECO:0000305|PubMed:27445338}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10788442, ECO:0000269|PubMed:9836639}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Associates with KCNQ3 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs. Therefore, it is important in the regulation of neuronal excitability. KCNQ2/KCNQ3 current is blocked by linopirdine and XE991, and activated by the anticonvulsant retigabine (PubMed:11572947, PubMed:12742592, PubMed:14534157, PubMed:17872363, PubMed:9836639). As the native M-channel, the potassium channel composed of KCNQ2 and KCNQ3 is also suppressed by activation of the muscarinic acetylcholine receptor CHRM1 (PubMed:10684873). KCNQ2-KCNQ3 channel is selectively permeable to other cations besides potassium, in decreasing order of affinity K(+) > Rb(+) > Cs(+) > Na(+). Associates with Na(+)-coupled myo-inositol symporter SLC5A3 forming a coregulatory complex that alters ion selectivity, increasing Na(+) and Cs(+) permeation relative to K(+) permeation. {ECO:0000269|PubMed:10684873, ECO:0000269|PubMed:11572947, ECO:0000269|PubMed:12742592, ECO:0000269|PubMed:14534157, ECO:0000269|PubMed:17872363, ECO:0000269|PubMed:25740509, ECO:0000269|PubMed:28793216, ECO:0000269|PubMed:9836639}.
|
Homo sapiens (Human)
|
O43529
|
CHSTA_HUMAN
|
MHHQWLLLAACFWVIFMFMVASKFITLTFKDPDVYSAKQEFLFLTTMPEVRKLPEEKHIPEELKPTGKELPDSQLVQPLVYMERLELIRNVCRDDALKNLSHTPVSKFVLDRIFVCDKHKILFCQTPKVGNTQWKKVLIVLNGAFSSIEEIPENVVHDHEKNGLPRLSSFSDAEIQKRLKTYFKFFIVRDPFERLISAFKDKFVHNPRFEPWYRHEIAPGIIRKYRRNRTETRGIQFEDFVRYLGDPNHRWLDLQFGDHIIHWVTYVELCAPCEIMYSVIGHHETLEDDAPYILKEAGIDHLVSYPTIPPGITVYNRTKVEHYFLGISKRDIRRLYARFEGDFKLFGYQKPDFLLN
|
2.8.2.-
| null |
androgen metabolic process [GO:0008209]; carbohydrate biosynthetic process [GO:0016051]; cell adhesion [GO:0007155]; estrogen metabolic process [GO:0008210]; learning [GO:0007612]; long-term memory [GO:0007616]; proteoglycan biosynthetic process [GO:0030166]
|
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]
|
HNK-1 sulfotransferase activity [GO:0016232]; sulfotransferase activity [GO:0008146]
|
PF03567;
| null |
Sulfotransferase 2 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:O54702}; Single-pass type II membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + 3-O-{beta-D-GlcA-(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-(1->](n)-4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] = 3-O-{O-3-S-beta-D-GlcA-(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-(1->](n)-4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68304, Rhea:RHEA-COMP:17486, Rhea:RHEA-COMP:17487, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:177355, ChEBI:CHEBI:177363; Evidence={ECO:0000269|PubMed:32149355}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68305; Evidence={ECO:0000305|PubMed:32149355}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol 3-O-(beta-D-glucuronate) + 3'-phosphoadenylyl sulfate = 17beta-estradiol 3-O-(3-sulfo-beta-D-glucuronate) + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68696, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136641, ChEBI:CHEBI:178093; Evidence={ECO:0000269|PubMed:23269668}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68697; Evidence={ECO:0000305|PubMed:23269668}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol 3-O-(beta-D-glucuronate) 17-sulfate + 3'-phosphoadenylyl sulfate = 17beta-estradiol 3-O-(3-sulfo-beta-D-glucuronate) 17-sulfate + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68660, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:178094, ChEBI:CHEBI:178095; Evidence={ECO:0000269|PubMed:23269668}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68661; Evidence={ECO:0000305|PubMed:23269668}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol 17-O-(beta-D-glucuronate) + 3'-phosphoadenylyl sulfate = 17beta-estradiol 17-O-(3-sulfo-beta-D-glucuronate) + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68664, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:82961, ChEBI:CHEBI:178096; Evidence={ECO:0000269|PubMed:23269668}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68665; Evidence={ECO:0000305|PubMed:23269668}; CATALYTIC ACTIVITY: Reaction=16alpha,17beta-estriol 3-O-(beta-D-glucuronate) + 3'-phosphoadenylyl sulfate = 16alpha,17beta-estriol 3-O-(3-sulfo-beta-D-glucuronate) + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68668, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136649, ChEBI:CHEBI:178097; Evidence={ECO:0000269|PubMed:23269668}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68669; Evidence={ECO:0000305|PubMed:23269668}; CATALYTIC ACTIVITY: Reaction=16alpha,17beta-estriol 16-O-(beta-D-glucuronate) + 3'-phosphoadenylyl sulfate = 16alpha,17beta-estriol 16-O-(3-sulfo-beta-D-glucuronate) + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68672, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136650, ChEBI:CHEBI:178098; Evidence={ECO:0000269|PubMed:23269668}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68673; Evidence={ECO:0000305|PubMed:23269668}; CATALYTIC ACTIVITY: Reaction=16alpha,17beta-estriol 17-O-(beta-D-glucuronate) + 3'-phosphoadenylyl sulfate = 16alpha,17beta-estriol 17-O-(3-sulfo-beta-D-glucuronate) + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68700, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:178099, ChEBI:CHEBI:178100; Evidence={ECO:0000269|PubMed:23269668}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68701; Evidence={ECO:0000305|PubMed:23269668}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + estrone 3-O-(beta-D-glucuronate) = adenosine 3',5'-bisphosphate + estrone 3-O-(3-sulfo-beta-D-glucuronate) + H(+); Xref=Rhea:RHEA:68676, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136634, ChEBI:CHEBI:178101; Evidence={ECO:0000269|PubMed:23269668}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68677; Evidence={ECO:0000305|PubMed:23269668}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + 3alpha,20alpha-dihydroxy-5beta-pregnane 3-O-(beta-D-glucuronate) = 3alpha,20alpha-dihydroxy-5beta-pregnane 3-O-(3-sulfo-beta-D-glucuronate) + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68680, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:178102, ChEBI:CHEBI:178103; Evidence={ECO:0000269|PubMed:23269668}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68681; Evidence={ECO:0000305|PubMed:23269668}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + testosterone 17-O-(beta-D-glucuronate) = adenosine 3',5'-bisphosphate + H(+) + testosterone 17-O-(3-sulfo-beta-D-glucuronate); Xref=Rhea:RHEA:68684, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136639, ChEBI:CHEBI:178104; Evidence={ECO:0000269|PubMed:23269668}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68685; Evidence={ECO:0000305|PubMed:23269668}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + 3beta-androst-5-en-17-one 3-O-(beta-D-glucuronate) = 3beta-androst-5-en-17-one 3-O-(3-sulfo-beta-D-glucuronate) + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68688, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:178105, ChEBI:CHEBI:178106; Evidence={ECO:0000269|PubMed:23269668}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68689; Evidence={ECO:0000305|PubMed:23269668}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + 3alpha,17alpha-dihydroxy-5beta-androstane-11-one-17beta-carboxylate 3-O-(beta-D-glucuronate) = 3alpha,17alpha-dihydroxy-5beta-androstane-11-one-17beta-carboxylate 3-O-(3-sulfo-beta-D-glucuronate) + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68692, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:178107, ChEBI:CHEBI:178108; Evidence={ECO:0000269|PubMed:23269668}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68693; Evidence={ECO:0000305|PubMed:23269668}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + 3alpha-hydroxyetiocholan-17-one 3-O-(beta-D-glucuronate) = 3alpha-hydroxyetiocholan-17-one 3-O-(3-sulfo-beta-D-glucuronate) + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:68704, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:178197, ChEBI:CHEBI:178198; Evidence={ECO:0000269|PubMed:23269668}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68705; Evidence={ECO:0000305|PubMed:23269668};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.21 mM for dehydroepiandrosterone 3-O-(beta-D-glucuronate) (GlcUA-3-DHEA) {ECO:0000269|PubMed:23269668}; KM=0.321 mM for 17beta-estradiol 3-O-(beta-D-glucuronate) (GlcUA-3-E2) {ECO:0000269|PubMed:23269668}; KM=1.518 mM for N-acetyllactosamine 3-O-(beta-D-glucuronate) (GlcUA-3-LacNAc) {ECO:0000269|PubMed:23269668}; Vmax=3194 pmol/min/mg enzyme toward dehydroepiandrosterone 3-O-(beta-D-glucuronate) (GlcUA-3-DHEA) {ECO:0000269|PubMed:23269668}; Vmax=3858 pmol/min/mg enzyme toward 17beta-estradiol 3-O-(beta-D-glucuronate) (GlcUA-3-E2) {ECO:0000269|PubMed:23269668}; Vmax=1723 pmol/min/mg enzyme toward N-acetyllactosamine 3-O-(beta-D-glucuronate) (GlcUA-3-LacNAc) {ECO:0000269|PubMed:23269668};
|
PATHWAY: Steroid metabolism. {ECO:0000269|PubMed:23269668}.; PATHWAY: Protein modification; carbohydrate sulfation. {ECO:0000269|PubMed:32149355}.
| null | null |
FUNCTION: Catalyzes the transfer of sulfate from 3'-phosphoadenylyl sulfate (PAPS) to position 3 of terminal glucuronic acid of both protein- and lipid-linked oligosaccharides. Participates in biosynthesis of HNK-1 carbohydrate structure 3-O-sulfo-beta-D-GlcA-(1->3)-beta-D-Gal-(1->4)-D-GlcNAc-R, a sulfated glucuronyl-lactosaminyl residue carried by many neural recognition molecules, which is involved in cell interactions during ontogenetic development and in synaptic plasticity in the adult. May be indirectly involved in synapse plasticity of the hippocampus, via its role in HNK-1 biosynthesis (PubMed:9478973). Sulfates terminal glucuronyl residue of the laminin globular (LG)-domain binding epitope on DAG1/alpha-dystroglycan and prevents further polymerization by LARGE1 glycosyltransferase. Likely defines the chain length of LG epitope, conferring binding specificity to extracellular matrix components (PubMed:32149355). Plays a role in down-regulating the steroid hormones. Sulfates glucuronidated estrogens and androgens with an impact in hormone cycle and fertility. Has a preference for glucuronyl moiety at the 3-hydroxyl group of a sterol ring rather than the 17-hydroxyl group, showing high catalytic efficiency for 17beta-estradiol 3-O-(beta-D-glucuronate) and dehydroepiandrosterone 3-O-(beta-D-glucuronate) hormones (PubMed:23269668). {ECO:0000269|PubMed:23269668, ECO:0000269|PubMed:32149355, ECO:0000269|PubMed:9478973}.
|
Homo sapiens (Human)
|
O43541
|
SMAD6_HUMAN
|
MFRSKRSGLVRRLWRSRVVPDREEGGSGGGGGGDEDGSLGSRAEPAPRAREGGGCGRSEVRPVAPRRPRDAVGQRGAQGAGRRRRAGGPPRPMSEPGAGAGSSLLDVAEPGGPGWLPESDCETVTCCLFSERDAAGAPRDASDPLAGAALEPAGGGRSREARSRLLLLEQELKTVTYSLLKRLKERSLDTLLEAVESRGGVPGGCVLVPRADLRLGGQPAPPQLLLGRLFRWPDLQHAVELKPLCGCHSFAAAADGPTVCCNPYHFSRLCGPESPPPPYSRLSPRDEYKPLDLSDSTLSYTETEATNSLITAPGEFSDASMSPDATKPSHWCSVAYWEHRTRVGRLYAVYDQAVSIFYDLPQGSGFCLGQLNLEQRSESVRRTRSKIGFGILLSKEPDGVWAYNRGEHPIFVNSPTLDAPGGRALVVRKVPPGYSIKVFDFERSGLQHAPEPDAADGPYDPNSVRISFAKGWGPCYSRQFITSCPCWLEILLNNPR
| null | null |
anatomical structure morphogenesis [GO:0009653]; aorta development [GO:0035904]; aortic valve morphogenesis [GO:0003180]; BMP signaling pathway [GO:0030509]; cell differentiation [GO:0030154]; cell-substrate adhesion [GO:0031589]; coronary vasculature development [GO:0060976]; fat cell differentiation [GO:0045444]; immune response [GO:0006955]; mitral valve morphogenesis [GO:0003183]; negative regulation of activin receptor signaling pathway [GO:0032926]; negative regulation of apoptotic process [GO:0043066]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of ossification [GO:0030279]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of SMAD protein signal transduction [GO:0060392]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; outflow tract septum morphogenesis [GO:0003148]; positive regulation of miRNA transcription [GO:1902895]; pulmonary valve morphogenesis [GO:0003184]; regulation of transcription by RNA polymerase II [GO:0006357]; response to estrogen [GO:0043627]; response to laminar fluid shear stress [GO:0034616]; response to lipopolysaccharide [GO:0032496]; SMAD protein signal transduction [GO:0060395]; transforming growth factor beta receptor signaling pathway [GO:0007179]; ureteric bud development [GO:0001657]; ventricular septum development [GO:0003281]; zygotic specification of dorsal/ventral axis [GO:0007352]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; heteromeric SMAD protein complex [GO:0071144]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
|
chromatin binding [GO:0003682]; co-SMAD binding [GO:0070410]; I-SMAD binding [GO:0070411]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein sequestering activity [GO:0140311]; R-SMAD binding [GO:0070412]; transcription cis-regulatory region binding [GO:0000976]; transcription regulator inhibitor activity [GO:0140416]; type I activin receptor binding [GO:0070698]; type I transforming growth factor beta receptor binding [GO:0034713]; ubiquitin protein ligase binding [GO:0031625]
|
PF03165;PF03166;
|
2.60.200.10;3.90.520.10;
|
Dwarfin/SMAD family
|
PTM: Phosphorylated by BMP type 1 receptor kinase and by PRKX. {ECO:0000269|PubMed:16491121}.; PTM: Monoubiquitinated at Lys-173 by the E2/E3 hybrid ubiquitin-protein ligase UBE2O, leading to reduced binding affinity for the activated BMP type I receptor ACVR1/ALK2, thereby enhancing BMP7 and regulating adipocyte differentiation (PubMed:23455153). Ubiquitinated by WWP1 (By similarity). Ubiquitinated by ARK2C, promoting proteasomal degradation, leading to enhance the BMP-Smad signaling (By similarity). {ECO:0000250|UniProtKB:O35182, ECO:0000269|PubMed:23455153}.; PTM: Arginine methylation by PRMT1, which is recruited by BMPR2, initiates BMP-Induced signaling and induces dissociation from the BMPR1B receptor at the cell surface leading to derepress downstream Smad1/Smad5 signaling. {ECO:0000250|UniProtKB:O35182}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16491121}.
| null | null | null | null | null |
FUNCTION: Transforming growth factor-beta superfamily receptors signaling occurs through the Smad family of intracellular mediators. SMAD6 is an inhibitory Smad (i-Smad) that negatively regulates signaling downstream of type I transforming growth factor-beta (PubMed:10647776, PubMed:10708948, PubMed:10708949, PubMed:16951688, PubMed:22275001, PubMed:30848080, PubMed:9436979, PubMed:9759503). Acts as a mediator of TGF-beta and BMP anti-inflammatory activities. Suppresses IL1R-TLR signaling through its direct interaction with PEL1, preventing NF-kappa-B activation, nuclear transport and NF-kappa-B-mediated expression of pro-inflammatory genes (PubMed:16951688). Blocks the BMP-SMAD1 signaling pathway by competing with SMAD4 for receptor-activated SMAD1-binding (PubMed:30848080, PubMed:9436979). Binds to regulatory elements in target promoter regions (PubMed:16491121). {ECO:0000269|PubMed:16491121, ECO:0000269|PubMed:16951688, ECO:0000269|PubMed:22275001, ECO:0000269|PubMed:30848080, ECO:0000269|PubMed:9436979, ECO:0000303|PubMed:10647776, ECO:0000303|PubMed:10708948, ECO:0000303|PubMed:10708949, ECO:0000303|PubMed:9759503}.
|
Homo sapiens (Human)
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.