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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O43542
|
XRCC3_HUMAN
|
MDLDLLDLNPRIIAAIKKAKLKSVKEVLHFSGPDLKRLTNLSSPEVWHLLRTASLHLRGSSILTALQLHQQKERFPTQHQRLSLGCPVLDALLRGGLPLDGITELAGRSSAGKTQLALQLCLAVQFPRQHGGLEAGAVYICTEDAFPHKRLQQLMAQQPRLRTDVPGELLQKLRFGSQIFIEHVADVDTLLECVNKKVPVLLSRGMARLVVIDSVAAPFRCEFDSQASAPRARHLQSLGATLRELSSAFQSPVLCINQVTEAMEEQGAAHGPLGFWDERVSPALGITWANQLLVRLLADRLREEEAALGCPARTLRVLSAPHLPPSSCSYTISAEGVRGTPGTQSH
| null | null |
DNA damage response [GO:0006974]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; double-strand break repair via homologous recombination [GO:0000724]; double-strand break repair via synthesis-dependent strand annealing [GO:0045003]; interstrand cross-link repair [GO:0036297]; positive regulation of mitotic cell cycle spindle assembly checkpoint [GO:0090267]; regulation of centrosome duplication [GO:0010824]; resolution of mitotic recombination intermediates [GO:0071140]; response to organic substance [GO:0010033]; t-circle formation [GO:0090656]; telomere maintenance via recombination [GO:0000722]; telomere maintenance via telomere trimming [GO:0090737]; telomeric loop disassembly [GO:0090657]
|
chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; Rad51C-XRCC3 complex [GO:0033065]; replication fork [GO:0005657]
|
ATP binding [GO:0005524]; ATP-dependent DNA damage sensor activity [GO:0140664]; four-way junction DNA binding [GO:0000400]
|
PF08423;
|
3.40.50.300;
|
RecA family, RAD51 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Mitochondrion. Note=Accumulates in discrete nuclear foci prior to DNA damage, and these foci persist throughout the time course of DNA repair.
| null | null | null | null | null |
FUNCTION: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA, thought to repair chromosomal fragmentation, translocations and deletions. Part of the RAD51 paralog protein complex CX3 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, CX3 acts downstream of RAD51 recruitment; the complex binds predominantly to the intersection of the four duplex arms of the Holliday junction (HJ) and to junctions of replication forks. Involved in HJ resolution and thus in processing HR intermediates late in the DNA repair process; the function may be linked to the CX3 complex and seems to involve GEN1 during mitotic cell cycle progression. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51 and RAD51C. {ECO:0000269|PubMed:14716019, ECO:0000269|PubMed:20413593, ECO:0000269|PubMed:23108668, ECO:0000269|PubMed:23149936}.
|
Homo sapiens (Human)
|
O43543
|
XRCC2_HUMAN
|
MCSAFHRAESGTELLARLEGRSSLKEIEPNLFADEDSPVHGDILEFHGPEGTGKTEMLYHLTARCILPKSEGGLEVEVLFIDTDYHFDMLRLVTILEHRLSQSSEEIIKYCLGRFFLVYCSSSTHLLLTLYSLESMFCSHPSLCLLILDSLSAFYWIDRVNGGESVNLQESTLRKCSQCLEKLVNDYRLVLFATTQTIMQKASSSSEEPSHASRRLCDVDIDYRPYLCKAWQQLVKHRMFFSKQDDSQSSNQFSLVSRCLKSNSLKKHFFIIGESGVEFC
| null | null |
centrosome cycle [GO:0007098]; DNA repair [GO:0006281]; DNA strand invasion [GO:0042148]; double-strand break repair via homologous recombination [GO:0000724]; in utero embryonic development [GO:0001701]; meiotic cell cycle [GO:0051321]; mitotic cell cycle [GO:0000278]; multicellular organism growth [GO:0035264]; negative regulation of neuron apoptotic process [GO:0043524]; neurogenesis [GO:0022008]; positive regulation of neurogenesis [GO:0050769]; regulation of fibroblast apoptotic process [GO:2000269]; response to gamma radiation [GO:0010332]; response to X-ray [GO:0010165]; somitogenesis [GO:0001756]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; Rad51B-Rad51C-Rad51D-XRCC2 complex [GO:0033063]; replication fork [GO:0005657]
|
ATP binding [GO:0005524]; ATP-dependent DNA damage sensor activity [GO:0140664]; four-way junction DNA binding [GO:0000400]
|
PF08423;
|
3.40.50.300;
|
RecA family, RAD51 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21276791}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:21276791}.
| null | null | null | null | null |
FUNCTION: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA, thought to repair chromosomal fragmentation, translocations and deletions. Part of the RAD51 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction 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. {ECO:0000269|PubMed:11751635, ECO:0000269|PubMed:11834724, ECO:0000269|PubMed:21276791, ECO:0000269|PubMed:23149936, ECO:0000269|PubMed:27233470}.
|
Homo sapiens (Human)
|
O43548
|
TGM5_HUMAN
|
MAQGLEVALTDLQSSRNNVRHHTEEITVDHLLVRRGQAFNLTLYFRNRSFQPGLDNIIFVVETGPLPDLALGTRAVFSLARHHSPSPWIAWLETNGATSTEVSLCAPPTAAVGRYLLKIHIDSFQGSVTAYQLGEFILLFNPWCPEDAVYLDSEPQRQEYVMNDYGFIYQGSKNWIRPCPWNYGQFEDKIIDICLKLLDKSLHFQTDPATDCALRGSPVYVSRVVCAMINSNDDNGVLNGNWSENYTDGANPAEWTGSVAILKQWNATGCQPVRYGQCWVFAAVMCTVMRCLGIPTRVITNFDSGHDTDGNLIIDEYYDNTGRILGNKKKDTIWNFHVWNECWMARKDLPPAYGGWQVLDATPQEMSNGVYCCGPASVRAIKEGEVDLNYDTPFVFSMVNADCMSWLVQGGKEQKLHQDTSSVGNFISTKSIQSDERDDITENYKYEEGSLQERQVFLKALQKLKARSFHGSQRGAELQPSRPTSLSQDSPRSLHTPSLRPSDVVQVSLKFKLLDPPNMGQDICFVLLALNMSSQFKDLKVNLSAQSLLHDGSPLSPFWQDTAFITLSPKEAKTYPCKISYSQYSQYLSTDKLIRISALGEEKSSPEKILVNKIITLSYPSITINVLGAAVVNQPLSIQVIFSNPLSEQVEDCVLTVEGSGLFKKQQKVFLGVLKPQHQASIILETVPFKSGQRQIQANMRSNKFKDIKGYRNVYVDFAL
|
2.3.2.13
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
|
epidermis development [GO:0008544]; protein modification process [GO:0036211]
|
cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
|
metal ion binding [GO:0046872]; protein-glutamine gamma-glutamyltransferase activity [GO:0003810]
|
PF00927;PF01841;PF00868;
|
2.60.40.10;3.90.260.10;
|
Transglutaminase superfamily, Transglutaminase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15290349}. Note=Associated with intermediate filaments.
|
CATALYTIC ACTIVITY: Reaction=L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:54816, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14005, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:30011, ChEBI:CHEBI:138370; EC=2.3.2.13; Evidence={ECO:0000255|PROSITE-ProRule:PRU10024};
| null | null | null | null |
FUNCTION: Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Contributes to the formation of the cornified cell envelope of keratinocytes.
|
Homo sapiens (Human)
|
O43556
|
SGCE_HUMAN
|
MQLPRWWELGDPCAWTGQGRGTRRMSPATTGTFLLTVYSIFSKVHSDRNVYPSAGVLFVHVLEREYFKGEFPPYPKPGEISNDPITFNTNLMGYPDRPGWLRYIQRTPYSDGVLYGSPTAENVGKPTIIEITAYNRRTFETARHNLIINIMSAEDFPLPYQAEFFIKNMNVEEMLASEVLGDFLGAVKNVWQPERLNAINITSALDRGGRVPLPINDLKEGVYVMVGADVPFSSCLREVENPQNQLRCSQEMEPVITCDKKFRTQFYIDWCKISLVDKTKQVSTYQEVIRGEGILPDGGEYKPPSDSLKSRDYYTDFLITLAVPSAVALVLFLILAYIMCCRREGVEKRNMQTPDIQLVHHSAIQKSTKELRDMSKNREIAWPLSTLPVFHPVTGEIIPPLHTDNYDSTNMPLMQTQQNLPHQTQIPQQQTTGKWYP
| null | null |
cell-matrix adhesion [GO:0007160]; muscle organ development [GO:0007517]
|
cytoskeleton [GO:0005856]; dendrite membrane [GO:0032590]; dystrophin-associated glycoprotein complex [GO:0016010]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]; sarcoglycan complex [GO:0016012]; sarcolemma [GO:0042383]
| null |
PF05510;PF20989;
| null |
Sarcoglycan alpha/epsilon family
|
PTM: N-glycosylated. {ECO:0000250}.; PTM: Ubiquitinated, leading to its degradation by the proteasome. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Golgi apparatus {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.
|
Homo sapiens (Human)
|
O43557
|
TNF14_HUMAN
|
MEESVVRPSVFVVDGQTDIPFTRLGRSHRRQSCSVARVGLGLLLLLMGAGLAVQGWFLLQLHWRLGEMVTRLPDGPAGSWEQLIQERRSHEVNPAAHLTGANSSLTGSGGPLLWETQLGLAFLRGLSYHDGALVVTKAGYYYIYSKVQLGGVGCPLGLASTITHGLYKRTPRYPEELELLVSQQSPCGRATSSSRVWWDSSFLGGVVHLEAGEKVVVRVLDERLVRLRDGTRSYFGAFMV
| null | null |
apoptotic process [GO:0006915]; cellular response to mechanical stimulus [GO:0071260]; immune response [GO:0006955]; positive regulation of myoblast differentiation [GO:0045663]; positive regulation of myoblast fusion [GO:1901741]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of T cell chemotaxis [GO:0010820]; signal transduction [GO:0007165]; T cell activation [GO:0042110]; T cell chemotaxis [GO:0010818]; T cell costimulation [GO:0031295]; T cell homeostasis [GO:0043029]; T cell proliferation [GO:0042098]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; cytokine activity [GO:0005125]; identical protein binding [GO:0042802]; signaling receptor binding [GO:0005102]; tumor necrosis factor receptor binding [GO:0005164]
|
PF00229;
|
2.60.120.40;
|
Tumor necrosis factor family
|
PTM: N-glycosylated. {ECO:0000269|Ref.10}.; PTM: The soluble form of isoform 1 derives from the membrane form by proteolytic processing. {ECO:0000269|PubMed:11673523}.
|
SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member 14, membrane form]: Cell membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member 14, soluble form]: Secreted.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
| null | null | null | null | null |
FUNCTION: Cytokine that binds to TNFRSF3/LTBR. Binding to the decoy receptor TNFRSF6B modulates its effects. Acts as a ligand for TNFRSF14/HVEM (PubMed:10754304, PubMed:9462508). Upon binding to TNFRSF14/HVEM, delivers costimulatory signals to T cells, leading to T cell proliferation and IFNG production (PubMed:10754304). {ECO:0000269|PubMed:10754304, ECO:0000269|PubMed:9462508}.
|
Homo sapiens (Human)
|
O43559
|
FRS3_HUMAN
|
MGSCCSCLNRDSVPDNHPTKFKVTNVDDEGVELGSGVMELTQSELVLHLHRREAVRWPYLCLRRYGYDSNLFSFESGRRCQTGQGIFAFKCSRAEEIFNLLQDLMQCNSINVMEEPVIITRNSHPAELDLPRAPQPPNALGYTVSSFSNGCPGEGPRFSAPRRLSTSSLRHPSLGEESTHALIAPDEQSHTYVNTPASEDDHRRGRHCLQPLPEGQAPFLPQARGPDQRDPQVFLQPGQVKFVLGPTPARRHMVKCQGLCPSLHDPPHHNNNNEAPSECPAQPKCTYENVTGGLWRGAGWRLSPEEPGWNGLAHRRAALLHYENLPPLPPVWESQAQQLGGEAGDDGDSRDGLTPSSNGFPDGEEDETPLQKPTSTRAAIRSHGSFPVPLTRRRGSPRVFNFDFRRPGPEPPRQLNYIQVELKGWGGDRPKGPQNPSSPQAPMPTTHPARSSDSYAVIDLKKTVAMSNLQRALPRDDGTARKTRHNSTDLPL
| null | null |
fibroblast growth factor receptor signaling pathway [GO:0008543]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
|
fibroblast growth factor receptor binding [GO:0005104]; identical protein binding [GO:0042802]; transmembrane receptor protein tyrosine kinase adaptor activity [GO:0005068]
|
PF02174;
|
2.30.29.30;
| null |
PTM: Phosphorylated by ULK2 in vitro (By similarity). Phosphorylated on tyrosine residues upon stimulation by BFGF or NGFB. {ECO:0000250, ECO:0000269|PubMed:15094036, ECO:0000269|PubMed:9660748}.
|
SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
| null | null | null | null | null |
FUNCTION: Adapter protein that links FGF and NGF receptors to downstream signaling pathways. Involved in the activation of MAP kinases. Down-regulates ERK2 signaling by interfering with the phosphorylation and nuclear translocation of ERK2. {ECO:0000269|PubMed:15094036}.
|
Homo sapiens (Human)
|
O43561
|
LAT_HUMAN
|
MEEAILVPCVLGLLLLPILAMLMALCVHCHRLPGSYDSTSSDSLYPRGIQFKRPHTVAPWPPAYPPVTSYPPLSQPDLLPIPRSPQPLGGSHRTPSSRRDSDGANSVASYENEGASGIRGAQAGWGVWGPSWTRLTPVSLPPEPACEDADEDEDDYHNPGYLVVLPDSTPATSTAAPSAPALSTPGIRDSAFSMESIDDYVNVPESGESAEASLDGSREYVNVSQELHPGAAKTEPAALSSQEAEEVEEEGAPDYENLQELN
| null | null |
adaptive immune response [GO:0002250]; calcium-mediated signaling [GO:0019722]; gene expression [GO:0010467]; immune response [GO:0006955]; inflammatory response [GO:0006954]; integrin-mediated signaling pathway [GO:0007229]; intracellular signal transduction [GO:0035556]; lymphocyte homeostasis [GO:0002260]; mast cell degranulation [GO:0043303]; membrane raft distribution [GO:0031580]; positive regulation of protein kinase activity [GO:0045860]; Ras protein signal transduction [GO:0007265]; regulation of T cell activation [GO:0050863]; T cell activation [GO:0042110]; T cell receptor signaling pathway [GO:0050852]
|
cell-cell junction [GO:0005911]; COP9 signalosome [GO:0008180]; Golgi apparatus [GO:0005794]; immunological synapse [GO:0001772]; membrane [GO:0016020]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; TCR signalosome [GO:0036398]
|
molecular condensate scaffold activity [GO:0140693]; protein kinase binding [GO:0019901]; signaling receptor complex adaptor activity [GO:0030159]
|
PF15234;
| null | null |
PTM: Phosphorylated on tyrosines by ZAP70 upon TCR activation, or by SYK upon other immunoreceptor activation; which leads to the recruitment of multiple signaling molecules. Is one of the most prominently tyrosine-phosphorylated proteins detected following TCR engagement. May be dephosphorylated by PTPRJ. Phosphorylated by ITK leading to the recruitment of VAV1 to LAT-containing complexes.; PTM: Palmitoylation of Cys-26 and Cys-29 is required for raft targeting and efficient phosphorylation. {ECO:0000269|PubMed:9729044}.; PTM: 'Lys-63'-linked ubiquitinated by TRAF6. {ECO:0000269|PubMed:23514740, ECO:0000269|PubMed:25907557}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9489702, ECO:0000269|PubMed:9729044}; Single-pass type III membrane protein {ECO:0000269|PubMed:9489702, ECO:0000269|PubMed:9729044}. Note=Present in lipid rafts.
| null | null | null | null | null |
FUNCTION: Required for TCR (T-cell antigen receptor)- and pre-TCR-mediated signaling, both in mature T-cells and during their development (PubMed:23514740, PubMed:25907557). Involved in FCGR3 (low affinity immunoglobulin gamma Fc region receptor III)-mediated signaling in natural killer cells and FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Couples activation of these receptors and their associated kinases with distal intracellular events such as mobilization of intracellular calcium stores, PKC activation, MAPK activation or cytoskeletal reorganization through the recruitment of PLCG1, GRB2, GRAP2, and other signaling molecules. {ECO:0000269|PubMed:10072481, ECO:0000269|PubMed:23514740, ECO:0000269|PubMed:25907557}.
|
Homo sapiens (Human)
|
O43566
|
RGS14_HUMAN
|
MPGKPKHLGVPNGRMVLAVSDGELSSTTGPQGQGEGRGSSLSIHSLPSGPSSPFPTEEQPVASWALSFERLLQDPLGLAYFTEFLKKEFSAENVTFWKACERFQQIPASDTQQLAQEARNIYQEFLSSQALSPVNIDRQAWLGEEVLAEPRPDMFRAQQLQIFNLMKFDSYARFVKSPLYRECLLAEAEGRPLREPGSSRLGSPDATRKKPKLKPGKSLPLGVEELGQLPPVEGPGGRPLRKSFRRELGGTANAALRRESQGSLNSSASLDLGFLAFVSSKSESHRKSLGSTEGESESRPGKYCCVYLPDGTASLALARPGLTIRDMLAGICEKRGLSLPDIKVYLVGNEQALVLDQDCTVLADQEVRLENRITFELELTALERVVRISAKPTKRLQEALQPILEKHGLSPLEVVLHRPGEKQPLDLGKLVSSVAAQRLVLDTLPGVKISKARDKSPCRSQGCPPRTQDKATHPPPASPSSLVKVPSSATGKRQTCDIEGLVELLNRVQSSGAHDQRGLLRKEDLVLPEFLQLPAQGPSSEETPPQTKSAAQPIGGSLNSTTDSAL
| null | null |
cell division [GO:0051301]; chromosome segregation [GO:0007059]; G protein-coupled receptor signaling pathway [GO:0007186]; learning [GO:0007612]; long-term memory [GO:0007616]; long-term synaptic potentiation [GO:0060291]; mitotic cell cycle [GO:0000278]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of G protein-coupled receptor signaling pathway [GO:0045744]; negative regulation of MAP kinase activity [GO:0043407]; negative regulation of synaptic plasticity [GO:0031914]; nucleocytoplasmic transport [GO:0006913]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of neurogenesis [GO:0050769]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; response to oxidative stress [GO:0006979]; spindle organization [GO:0007051]; visual learning [GO:0008542]; zygote asymmetric cell division [GO:0010070]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; microtubule [GO:0005874]; nuclear body [GO:0016604]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; PML body [GO:0016605]; postsynaptic density [GO:0014069]; spindle [GO:0005819]; spindle pole [GO:0000922]
|
G-protein alpha-subunit binding [GO:0001965]; GDP-dissociation inhibitor activity [GO:0005092]; GTPase activating protein binding [GO:0032794]; GTPase activator activity [GO:0005096]; GTPase activity [GO:0003924]; microtubule binding [GO:0008017]; protein kinase binding [GO:0019901]; signaling receptor complex adaptor activity [GO:0030159]
|
PF02188;PF02196;PF00615;
|
1.10.196.10;1.10.167.10;
| null |
PTM: Phosphorylated by PKC. Phosphorylation is increased in presence of forskolin and may enhance the GDI activity on G(i) alpha subunit GNAI1 (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, PML body {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:15917656}. Membrane {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15917656}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Postsynaptic density {ECO:0000250}. Note=Associates with the perinuclear sheaths of microtubules (MTs) surrounding the pronuclei, prior to segregating to the anastral mitotic apparatus and subsequently the barrel-shaped cytoplasmic bridge between the nascent nuclei of the emerging 2-cell embryo. Localizes to a perinuclear compartment near the microtubule-organizing center (MTOC). Expressed in the nucleus during interphase and segregates to the centrosomes and astral MTs during mitosis. Relocalizes to the nucleus in PML nuclear bodies in response to heat stress. Colocalizes with RIC8A in CA2 hippocampal neurons. Localizes to spindle poles during metaphase. Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner. Recruited from the cytosol to the plasma membrane by the inactive GDP-bound forms of G(i) alpha subunits GNAI1 and GNAI3. Recruited from the cytosol to membranes by the active GTP-bound form of HRAS. Colocalizes with G(i) alpha subunit GNAI1 and RIC8A at the plasma membrane. Colocalizes with BRAF and RAF1 in both the cytoplasm and membranes (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Besides, modulates signal transduction via G protein alpha subunits by functioning as a GDP-dissociation inhibitor (GDI). Has GDI activity on G(i) alpha subunits GNAI1 and GNAI3, but not on GNAI2 and G(o)-alpha subunit GNAO1. Has GAP activity on GNAI0, GNAI2 and GNAI3. May act as a scaffold integrating G protein and Ras/Raf MAPkinase signaling pathways. Inhibits platelet-derived growth factor (PDGF)-stimulated ERK1/ERK2 phosphorylation; a process depending on its interaction with HRAS and that is reversed by G(i) alpha subunit GNAI1. Acts as a positive modulator of microtubule polymerisation and spindle organization through a G(i)-alpha-dependent mechanism. Plays a role in cell division. Required for the nerve growth factor (NGF)-mediated neurite outgrowth. Involved in stress resistance. May be involved in visual memory processing capacity and hippocampal-based learning and memory. {ECO:0000269|PubMed:15917656, ECO:0000269|PubMed:17635935}.
|
Homo sapiens (Human)
|
O43567
|
RNF13_HUMAN
|
MLLSIGMLMLSATQVYTILTVQLFAFLNLLPVEADILAYNFENASQTFDDLPARFGYRLPAEGLKGFLINSKPENACEPIVPPPVKDNSSGTFIVLIRRLDCNFDIKVLNAQRAGYKAAIVHNVDSDDLISMGSNDIEVLKKIDIPSVFIGESSANSLKDEFTYEKGGHLILVPEFSLPLEYYLIPFLIIVGICLILIVIFMITKFVQDRHRARRNRLRKDQLKKLPVHKFKKGDEYDVCAICLDEYEDGDKLRILPCSHAYHCKCVDPWLTKTKKTCPVCKQKVVPSQGDSDSDTDSSQEENEVTEHTPLLRPLASVSAQSFGALSESRSHQNMTESSDYEEDDNEDTDSSDAENEINEHDVVVQLQPNGERDYNIANTV
|
2.3.2.27
| null |
organelle localization [GO:0051640]; positive regulation of JNK cascade [GO:0046330]; protein autoubiquitination [GO:0051865]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; intracellular membrane-bounded organelle [GO:0043231]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; nuclear inner membrane [GO:0005637]; nucleoplasm [GO:0005654]
|
JUN kinase binding [GO:0008432]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]
|
PF02225;PF13639;
|
3.50.30.30;3.30.40.10;
| null |
PTM: Autoubiquitinated. {ECO:0000269|PubMed:18794910}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18794910, ECO:0000269|PubMed:23378536, ECO:0000269|PubMed:24387786}; Single-pass type I membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000305|PubMed:24387786}; Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:17897319}; Single-pass type I membrane protein {ECO:0000255}. Nucleus inner membrane {ECO:0000250|UniProtKB:O54965}; Single-pass type I membrane protein {ECO:0000255}. Note=Under certain conditions, relocalizes to recycling endosomes and to the inner nuclear membrane. {ECO:0000250|UniProtKB:O54965}.
|
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; Evidence={ECO:0000269|PubMed:18794910, ECO:0000269|PubMed:24387786};
| null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:18794910, ECO:0000269|PubMed:24387786}.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase that regulates cell proliferation (PubMed:18794910, PubMed:23378536, PubMed:30595371). Involved in apoptosis regulation (PubMed:23378536, PubMed:30595371). Mediates ER stress-induced activation of JNK signaling pathway and apoptosis by promoting ERN1 activation and splicing of XBP1 mRNA (PubMed:23378536, PubMed:30595371). Also involved in protein trafficking and localization (PubMed:24387786). {ECO:0000269|PubMed:18794910, ECO:0000269|PubMed:23378536, ECO:0000269|PubMed:24387786, ECO:0000269|PubMed:30595371}.
|
Homo sapiens (Human)
|
O43570
|
CAH12_HUMAN
|
MPRRSLHAAAVLLLVILKEQPSSPAPVNGSKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQGLQSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFSHLQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPREMINNFRQVQKFDERLVYTSFSQVQVCTAAGLSLGIILSLALAGILGICIVVVVSIWLFRRKSIKKGDNKGVIYKPATKMETEAHA
|
4.2.1.1
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:11493685};
|
chloride ion homeostasis [GO:0055064]; estrous cycle [GO:0044849]; one-carbon metabolic process [GO:0006730]
|
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
carbonate dehydratase activity [GO:0004089]; zinc ion binding [GO:0008270]
|
PF00194;
|
3.10.200.10;
|
Alpha-carbonic anhydrase family
| null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Cell membrane {ECO:0000269|PubMed:26911677}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17544; EC=4.2.1.1; Evidence={ECO:0000269|PubMed:26911677};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12 mM for CO(2) {ECO:0000269|PubMed:18618712, ECO:0000269|PubMed:21035102};
| null | null | null |
FUNCTION: Reversible hydration of carbon dioxide. {ECO:0000269|PubMed:26911677}.
|
Homo sapiens (Human)
|
O43572
|
AKA10_HUMAN
|
MRGAGPSPRQSPRTLRPDPGPAMSFFRRKVKGKEQEKTSDVKSIKASISVHSPQKSTKNHALLEAAGPSHVAINAISANMDSFSSSRTATLKKQPSHMEAAHFGDLGRSCLDYQTQETKSSLSKTLEQVLHDTIVLPYFIQFMELRRMEHLVKFWLEAESFHSTTWSRIRAHSLNTVKQSSLAEPVSPSKKHETTASFLTDSLDKRLEDSGSAQLFMTHSEGIDLNNRTNSTQNHLLLSQECDSAHSLRLEMARAGTHQVSMETQESSSTLTVASRNSPASPLKELSGKLMKSIEQDAVNTFTKYISPDAAKPIPITEAMRNDIIARICGEDGQVDPNCFVLAQSIVFSAMEQEHFSEFLRSHHFCKYQIEVLTSGTVYLADILFCESALFYFSEYMEKEDAVNILQFWLAADNFQSQLAAKKGQYDGQEAQNDAMILYDKYFSLQATHPLGFDDVVRLEIESNICREGGPLPNCFTTPLRQAWTTMEKVFLPGFLSSNLYYKYLNDLIHSVRGDEFLGGNVSLTAPGSVGPPDESHPGSSDSSASQSSVKKASIKILKNFDEAIIVDAASLDPESLYQRTYAGKMTFGRVSDLGQFIRESEPEPDVRKSKGSMFSQAMKKWVQGNTDEAQEELAWKIAKMIVSDIMQQAQYDQPLEKSTKL
| null | null |
protein localization [GO:0008104]; signal transduction [GO:0007165]
|
cytosol [GO:0005829]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
|
protein kinase A binding [GO:0051018]
|
PF00615;
|
1.10.167.10;
| null | null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11248059}. Membrane {ECO:0000269|PubMed:11248059}. Cytoplasm {ECO:0000269|PubMed:11248059}. Note=Predominantly mitochondrial but also membrane associated and cytoplasmic.
| null | null | null | null | null |
FUNCTION: Differentially targeted protein that binds to type I and II regulatory subunits of protein kinase A and anchors them to the mitochondria or the plasma membrane. Although the physiological relevance between PKA and AKAPS with mitochondria is not fully understood, one idea is that BAD, a proapoptotic member, is phosphorylated and inactivated by mitochondria-anchored PKA. It cannot be excluded too that it may facilitate PKA as well as G protein signal transduction, by acting as an adapter for assembling multiprotein complexes. With its RGS domain, it could lead to the interaction to G-alpha proteins, providing a link between the signaling machinery and the downstream kinase (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O43581
|
SYT7_HUMAN
|
MYRDPEAASPGAPSRDVLLVSAIITVSLSVTVVLCGLCHWCQRKLGKRYKNSLETVGTPDSGRGRSEKKAIKLPAGGKAVNTAPVPGQTPHDESDRRTEPRSSVSDLVNSLTSEMLMLSPGSEEDEAHEGCSRENLGRIQFSVGYNFQESTLTVKIMKAQELPAKDFSGTSDPFVKIYLLPDKKHKLETKVKRKNLNPHWNETFLFEGFPYEKVVQRILYLQVLDYDRFSRNDPIGEVSIPLNKVDLTQMQTFWKDLKPCSDGSGSRGELLLSLCYNPSANSIIVNIIKARNLKAMDIGGTSDPYVKVWLMYKDKRVEKKKTVTMKRNLNPIFNESFAFDIPTEKLRETTIIITVMDKDKLSRNDVIGKIYLSWKSGPGEVKHWKDMIARPRQPVAQWHQLKA
| 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};
|
calcium ion regulated lysosome exocytosis [GO:1990927]; calcium ion-regulated exocytosis of neurotransmitter [GO:0048791]; cellular response to calcium ion [GO:0071277]; phagocytosis [GO:0006909]; phagosome-lysosome fusion [GO:0090385]; plasma membrane repair [GO:0001778]; positive regulation of calcium ion-dependent exocytosis [GO:0045956]; regulation of bone remodeling [GO:0046850]; regulation of calcium ion-dependent exocytosis [GO:0017158]; regulation of dopamine secretion [GO:0014059]; regulation of glucagon secretion [GO:0070092]; regulation of insulin secretion [GO:0050796]; regulation of phagocytosis [GO:0050764]; regulation of synaptic vesicle endocytosis [GO:1900242]; short-term synaptic potentiation [GO:1990926]; synaptic vesicle recycling [GO:0036465]; vesicle fusion [GO:0006906]; vesicle-mediated cholesterol transport [GO:0090119]
|
axon [GO:0030424]; cytosol [GO:0005829]; dense core granule [GO:0031045]; early phagosome [GO:0032009]; extracellular exosome [GO:0070062]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]; synapse [GO:0045202]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; calmodulin binding [GO:0005516]; clathrin binding [GO:0030276]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylserine binding [GO:0001786]; SNARE binding [GO:0000149]; syntaxin binding [GO:0019905]
|
PF00168;
|
2.60.40.150;
|
Synaptotagmin family
|
PTM: Palmitoylated at its vesicular N-terminus; palmitoylation is required for localization to lysosome and phagocytosis in macrophages. {ECO:0000250|UniProtKB:Q9R0N7}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q62747}; Single-pass membrane protein {ECO:0000255}. Presynaptic cell membrane {ECO:0000250|UniProtKB:Q9R0N7}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q9R0N7}; Single-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q9R0N7}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9R0N7}; Single-pass membrane protein {ECO:0000255}. Peroxisome membrane {ECO:0000250|UniProtKB:Q9R0N7}; Single-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q62747}; Single-pass membrane protein {ECO:0000255}. Note=Localization to lysosomes is dependent on N-terminal palmitoylation and interaction with CD63. {ECO:0000250|UniProtKB:Q9R0N7}.
| null | null | null | null | null |
FUNCTION: Ca(2+) sensor involved in Ca(2+)-dependent exocytosis of secretory and synaptic vesicles through Ca(2+) and phospholipid binding to the C2 domain (By similarity). Ca(2+) induces binding of the C2-domains to phospholipid membranes and to assembled SNARE-complexes; both actions contribute to triggering exocytosis (By similarity). SYT7 binds Ca(2+) with high affinity and slow kinetics compared to other synaptotagmins (By similarity). Involved in Ca(2+)-triggered lysosomal exocytosis, a major component of the plasma membrane repair (PubMed:11342594). Ca(2+)-regulated delivery of lysosomal membranes to the cell surface is also involved in the phagocytic uptake of particles by macrophages (By similarity). Ca(2+)-triggered lysosomal exocytosis also plays a role in bone remodeling by regulating secretory pathways in osteoclasts and osteoblasts (By similarity). In case of infection, involved in participates cell invasion by Trypanosoma cruzi via Ca(2+)-triggered lysosomal exocytosis (PubMed:11342594, PubMed:15811535). Involved in cholesterol transport from lysosome to peroxisome by promoting membrane contacts between lysosomes and peroxisomes: probably acts by promoting vesicle fusion by binding phosphatidylinositol-4,5-bisphosphate on peroxisomal membranes (By similarity). Acts as a key mediator of synaptic facilitation, a process also named short-term synaptic potentiation: synaptic facilitation takes place at synapses with a low initial release probability and is caused by influx of Ca(2+) into the axon terminal after spike generation, increasing the release probability of neurotransmitters (By similarity). Probably mediates synaptic facilitation by directly increasing the probability of release (By similarity). May also contribute to synaptic facilitation by regulating synaptic vesicle replenishment, a process required to ensure that synaptic vesicles are ready for the arrival of the next action potential: SYT7 is required for synaptic vesicle replenishment by acting as a sensor for Ca(2+) and by forming a complex with calmodulin (By similarity). Also acts as a regulator of Ca(2+)-dependent insulin and glucagon secretion in beta-cells (By similarity). Triggers exocytosis by promoting fusion pore opening and fusion pore expansion in chromaffin cells (By similarity). Also regulates the secretion of some non-synaptic secretory granules of specialized cells (By similarity). {ECO:0000250|UniProtKB:Q62747, ECO:0000250|UniProtKB:Q9R0N7, ECO:0000269|PubMed:11342594, ECO:0000269|PubMed:15811535}.
|
Homo sapiens (Human)
|
O43583
|
DENR_HUMAN
|
MAADISESSGADCKGDPRNSAKLDADYPLRVLYCGVCSLPTEYCEYMPDVAKCRQWLEKNFPNEFAKLTVENSPKQEAGISEGQGTAGEEEEKKKQKRGGRGQIKQKKKTVPQKVTIAKIPRAKKKYVTRVCGLATFEIDLKEAQRFFAQKFSCGASVTGEDEIIIQGDFTDDIIDVIQEKWPEVDDDSIEDLGEVKK
| null | null |
formation of translation preinitiation complex [GO:0001731]; IRES-dependent viral translational initiation [GO:0075522]; ribosome disassembly [GO:0032790]; translation reinitiation [GO:0002188]
| null |
mRNA binding [GO:0003729]; translation initiation factor activity [GO:0003743]
|
PF21023;PF01253;
|
3.30.780.10;
|
DENR family
| null | null | null | null | null | null | null |
FUNCTION: May be involved in the translation of target mRNAs by scanning and recognition of the initiation codon. Involved in translation initiation; promotes recruitmnet of aminoacetyled initiator tRNA to P site of 40S ribosomes. Can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits. Plays a role in the modulation of the translational profile of a subset of cancer-related mRNAs when recruited to the translational initiation complex by the oncogene MCTS1. {ECO:0000269|PubMed:16982740, ECO:0000269|PubMed:17878526, ECO:0000269|PubMed:20713520}.
|
Homo sapiens (Human)
|
O43586
|
PPIP1_HUMAN
|
MMPQLQFKDAFWCRDFTAHTGYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTEINSLRASFDSLKQQMENVGSSHIQLALTLREELRSLEEFRERQKEQRKKYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDAEQAFERISANGHQKQVEKSQNKARQCKDSATEAERVYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNALWVHSNQLSMQCVKDDELYEEVRLTLEGCSIDADIDSFIQAKSTGTEPPAPVPYQNYYDREVTPLTSSPGIQPSCGMIKRFSGLLHGSPKTTSLAASAASTETLTPTPERNEGVYTAIAVQEIQGNPASPAQEYRALYDYTAQNPDELDLSAGDILEVILEGEDGWWTVERNGQRGFVPGSYLEKL
| null | null |
actin filament polymerization [GO:0030041]; cell adhesion [GO:0007155]; endocytosis [GO:0006897]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; signal transduction [GO:0007165]
|
actin filament [GO:0005884]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; lamellipodium [GO:0030027]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; uropod [GO:0001931]
|
actin filament binding [GO:0051015]; identical protein binding [GO:0042802]
|
PF00611;PF00018;
|
1.20.1270.60;2.30.30.40;
| null |
PTM: Dephosphorylated on Tyr-345 by PTPN18, this event negatively regulates the association of PSTPIP1 with SH2 domain-containing proteins as tyrosine kinase. Phosphorylation of Tyr-345 is probably required for subsequent phosphorylation at other tyrosine residues. Phosphorylation is induced by activation of the EGFR and PDGFR in a ABL1 dependent manner. The phosphorylation regulates the interaction with WAS and with MEFV (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9857189}. Cell membrane {ECO:0000269|PubMed:18480402, ECO:0000269|PubMed:9857189}; Peripheral membrane protein {ECO:0000269|PubMed:9857189}. Cell projection, uropodium {ECO:0000269|PubMed:18480402}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19109554, ECO:0000269|PubMed:19584923}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P97814}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P97814}. Cleavage furrow {ECO:0000250|UniProtKB:P97814}. Note=Mainly cytoplasmic in T-cells (PubMed:9857189). Colocalizes in cluster with CD2 near the cell surface membrane in activated T-cells (PubMed:9857189). In monocytes, forms a branched filamentous network in the cytoplasm (PubMed:19584923). In transfected cells, forms relatively straight filaments radiating out from the nucleus (PubMed:19584923). Filament formation requires an intact tubulin cytoskeleton (PubMed:19584923). In migrating neutrophils, colocalizes with PIP5K1C and DNM2 to the trailing edge of the uropod in a actin-dependent manner (PubMed:18480402). Colocalized with PTPN12 in the cytoplasm and the perinuclear region. During interphase, colocalizes with F-actin in the cortical cytoskeleton, lamellipodia, and stress fibers. In dividing cells, colocalizes with the F-actin rich cytokinetic cleavage furrow. Colocalized with CD2AP and WAS in the actin cytoskeleton within the cytoplasm. Colocalized with CD2, CD2AP and WAS at the site of T-cell:APC contact (By similarity). {ECO:0000250|UniProtKB:P97814, ECO:0000269|PubMed:18480402, ECO:0000269|PubMed:19584923, ECO:0000269|PubMed:9857189}.
| null | null | null | null | null |
FUNCTION: Involved in regulation of the actin cytoskeleton. May regulate WAS actin-bundling activity. Bridges the interaction between ABL1 and PTPN18 leading to ABL1 dephosphorylation. May play a role as a scaffold protein between PTPN12 and WAS and allow PTPN12 to dephosphorylate WAS. Has the potential to physically couple CD2 and CD2AP to WAS. Acts downstream of CD2 and CD2AP to recruit WAS to the T-cell:APC contact site so as to promote the actin polymerization required for synapse induction during T-cell activation (By similarity). Down-regulates CD2-stimulated adhesion through the coupling of PTPN12 to CD2. Also has a role in innate immunity and the inflammatory response. Recruited to inflammasomes by MEFV. Induces formation of pyroptosomes, large supramolecular structures composed of oligomerized PYCARD dimers which form prior to inflammatory apoptosis. Binding to MEFV allows MEFV to bind to PYCARD and facilitates pyroptosome formation. Regulates endocytosis and cell migration in neutrophils. {ECO:0000250, ECO:0000269|PubMed:17964261, ECO:0000269|PubMed:18480402, ECO:0000269|PubMed:19109554, ECO:0000269|PubMed:19584923, ECO:0000269|PubMed:9857189}.
|
Homo sapiens (Human)
|
O43592
|
XPOT_HUMAN
|
MDEQALLGLNPNADSDFRQRALAYFEQLKISPDAWQVCAEALAQRTYSDDHVKFFCFQVLEHQVKYKYSELTTVQQQLIRETLISWLQAQMLNPQPEKTFIRNKAAQVFALLFVTEYLTKWPKFFFDILSVVDLNPRGVDLYLRILMAIDSELVDRDVVHTSEEARRNTLIKDTMREQCIPNLVESWYQILQNYQFTNSEVTCQCLEVVGAYVSWIDLSLIANDRFINMLLGHMSIEVLREEACDCLFEVVNKGMDPVDKMKLVESLCQVLQSAGFFSIDQEEDVDFLARFSKLVNGMGQSLIVSWSKLIKNGDIKNAQEALQAIETKVALMLQLLIHEDDDISSNIIGFCYDYLHILKQLTVLSDQQKANVEAIMLAVMKKLTYDEEYNFENEGEDEAMFVEYRKQLKLLLDRLAQVSPELLLASVRRVFSSTLQNWQTTRFMEVEVAIRLLYMLAEALPVSHGAHFSGDVSKASALQDMMRTLVTSGVSSYQHTSVTLEFFETVVRYEKFFTVEPQHIPCVLMAFLDHRGLRHSSAKVRSRTAYLFSRFVKSLNKQMNPFIEDILNRIQDLLELSPPENGHQSLLSSDDQLFIYETAGVLIVNSEYPAERKQALMRNLLTPLMEKFKILLEKLMLAQDEERQASLADCLNHAVGFASRTSKAFSNKQTVKQCGCSEVYLDCLQTFLPALSCPLQKDILRSGVRTFLHRMIICLEEEVLPFIPSASEHMLKDCEAKDLQEFIPLINQITAKFKIQVSPFLQQMFMPLLHAIFEVLLRPAEENDQSAALEKQMLRRSYFAFLQTVTGSGMSEVIANQGAENVERVLVTVIQGAVEYPDPIAQKTCFIILSKLVELWGGKDGPVGFADFVYKHIVPACFLAPLKQTFDLADAQTVLALSECAVTLKTIHLKRGPECVQYLQQEYLPSLQVAPEIIQEFCQALQQPDAKVFKNYLKVFFQRAKP
| null | null |
intracellular protein transport [GO:0006886]; tRNA export from nucleus [GO:0006409]; tRNA re-export from nucleus [GO:0071528]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear matrix [GO:0016363]; nuclear pore [GO:0005643]; nucleoplasm [GO:0005654]
|
small GTPase binding [GO:0031267]; tRNA binding [GO:0000049]
|
PF19282;PF03810;PF08389;
|
1.25.10.10;
|
Exportin family
| null |
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear, once bound to tRNA and Ran the complex translocates to the cytoplasm. Shuttles between the nucleus and the cytoplasm.
| null | null | null | null | null |
FUNCTION: Mediates the nuclear export of aminoacylated tRNAs. In the nucleus binds to tRNA and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the tRNA from the export receptor. XPOT then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. {ECO:0000269|PubMed:12138183, ECO:0000269|PubMed:9512417, ECO:0000269|PubMed:9660920}.
|
Homo sapiens (Human)
|
O43593
|
HAIR_HUMAN
|
MESTPSFLKGTPTWEKTAPENGIVRQEPGSPPRDGLHHGPLCLGEPAPFWRGVLSTPDSWLPPGFPQGPKDMLPLVEGEGPQNGERKVNWLGSKEGLRWKEAMLTHPLAFCGPACPPRCGPLMPEHSGGHLKSDPVAFRPWHCPFLLETKILERAPFWVPTCLPPYLVSGLPPEHPCDWPLTPHPWVYSGGQPKVPSAFSLGSKGFYYKDPSIPRLAKEPLAAAEPGLFGLNSGGHLQRAGEAERPSLHQRDGEMGAGRQQNPCPLFLGQPDTVPWTSWPACPPGLVHTLGNVWAGPGDGNLGYQLGPPATPRCPSPEPPVTQRGCCSSYPPTKGGGLGPCGKCQEGLEGGASGASEPSEEVNKASGPRACPPSHHTKLKKTWLTRHSEQFECPRGCPEVEERPVARLRALKRAGSPEVQGAMGSPAPKRPPDPFPGTAEQGAGGWQEVRDTSIGNKDVDSGQHDEQKGPQDGQASLQDPGLQDIPCLALPAKLAQCQSCAQAAGEGGGHACHSQQVRRSPLGGELQQEEDTATNSSSEEGPGSGPDSRLSTGLAKHLLSGLGDRLCRLLRREREALAWAQREGQGPAVTEDSPGIPRCCSRCHHGLFNTHWRCPRCSHRLCVACGRVAGTGRAREKAGFQEQSAEECTQEAGHAACSLMLTQFVSSQALAELSTAMHQVWVKFDIRGHCPCQADARVWAPGDAGQQKESTQKTPPTPQPSCNGDTHRTKSIKEETPDSAETPAEDRAGRGPLPCPSLCELLASTAVKLCLGHERIHMAFAPVTPALPSDDRITNILDSIIAQVVERKIQEKALGPGLRAGPGLRKGLGLPLSPVRPRLPPPGALLWLQEPQPCPRRGFHLFQEHWRQGQPVLVSGIQRTLQGNLWGTEALGALGGQVQALSPLGPPQPSSLGSTTFWEGFSWPELRPKSDEGSVLLLHRALGDEDTSRVENLAASLPLPEYCALHGKLNLASYLPPGLALRPLEPQLWAAYGVSPHRGHLGTKNLCVEVADLVSILVHADTPLPAWHRAQKDFLSGLDGEGLWSPGSQVSTVWHVFRAQDAQRIRRFLQMVCPAGAGALEPGAPGSCYLDAGLRRRLREEWGVSCWTLLQAPGEAVLVPAGAPHQVQGLVSTVSVTQHFLSPETSALSAQLCHQGPSLPPDCHLLYAQMDWAVFQAVKVAVGTLQEAK
|
1.14.11.65
|
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
|
regulation of transcription by RNA polymerase II [GO:0006357]
|
chromatin [GO:0000785]; histone deacetylase complex [GO:0000118]; nucleoplasm [GO:0005654]
|
chromatin DNA binding [GO:0031490]; histone H3K9 demethylase activity [GO:0032454]; histone H3K9me/H3K9me2 demethylase activity [GO:0140683]; metal ion binding [GO:0046872]; transcription coregulator activity [GO:0003712]
|
PF02373;
|
2.60.120.650;
| null | null |
SUBCELLULAR LOCATION: Nucleus.
|
CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(9)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60188, Rhea:RHEA-COMP:15541, Rhea:RHEA-COMP:15546, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, ChEBI:CHEBI:61976; EC=1.14.11.65; Evidence={ECO:0000269|PubMed:24334705};
| null | null | null | null |
FUNCTION: Histone demethylase that specifically demethylates both mono- and dimethylated 'Lys-9' of histone H3. May act as a transcription regulator controlling hair biology (via targeting of collagens), neural activity, and cell cycle. {ECO:0000269|PubMed:24334705}.
|
Homo sapiens (Human)
|
O43597
|
SPY2_HUMAN
|
MEARAQSGNGSQPLLQTPRDGGRQRGEPDPRDALTQQVHVLSLDQIRAIRNTNEYTEGPTVVPRPGLKPAPRPSTQHKHERLHGLPEHRQPPRLQHSQVHSSARAPLSRSISTVSSGSRSSTRTSTSSSSSEQRLLGSSFSSGPVADGIIRVQPKSELKPGELKPLSKEDLGLHAYRCEDCGKCKCKECTYPRPLPSDWICDKQCLCSAQNVIDYGTCVCCVKGLFYHCSNDDEDNCADNPCSCSQSHCCTRWSAMGVMSLFLPCLWCYLPAKGCLKLCQGCYDRVNRPGCRCKNSNTVCCKVPTVPPRNFEKPT
| null | null |
animal organ development [GO:0048513]; bud elongation involved in lung branching [GO:0060449]; cell fate commitment [GO:0045165]; cellular response to leukemia inhibitory factor [GO:1990830]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; ERK1 and ERK2 cascade [GO:0070371]; establishment of mitotic spindle orientation [GO:0000132]; fibroblast growth factor receptor signaling pathway [GO:0008543]; inner ear morphogenesis [GO:0042472]; lung growth [GO:0060437]; negative regulation of angiogenesis [GO:0016525]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cell projection organization [GO:0031345]; negative regulation of epithelial to mesenchymal transition [GO:0010719]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of fibroblast growth factor receptor signaling pathway [GO:0040037]; negative regulation of lens fiber cell differentiation [GO:1902747]; negative regulation of neurotrophin TRK receptor signaling pathway [GO:0051387]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of Ras protein signal transduction [GO:0046580]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; negative regulation of vascular endothelial growth factor signaling pathway [GO:1900747]; positive regulation of cell migration [GO:0030335]; positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of gene expression [GO:0010628]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; sensory perception of sound [GO:0007605]
|
actin cytoskeleton [GO:0015629]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; microtubule end [GO:1990752]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587]
|
protein kinase binding [GO:0019901]; protein serine/threonine kinase activator activity [GO:0043539]; protein serine/threonine kinase inhibitor activity [GO:0030291]; ubiquitin-protein transferase inhibitor activity [GO:0055105]
|
PF05210;
| null |
Sprouty family
|
PTM: Cleaved at Pro-144 by the prolyl endopeptidase FAP (seprase) activity (in vitro). {ECO:0000269|PubMed:21288888}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10887178}. Cell projection, ruffle membrane {ECO:0000269|PubMed:10887178}. Note=Associated with microtubules in unstimulated cells but is translocated to the membrane ruffles in cells stimulated with EGF (epidermal growth factor). {ECO:0000269|PubMed:10887178}.
| null | null | null | null | null |
FUNCTION: Antagonist of fibroblast growth factor (FGF) pathways via inhibition of FGF-mediated phosphorylation of ERK1/2 (By similarity). Thereby acts as an antagonist of FGF-induced retinal lens fiber differentiation, may inhibit limb bud outgrowth and may negatively modulate respiratory organogenesis (By similarity). Inhibits TGFB-induced epithelial-to-mesenchymal transition in retinal lens epithelial cells (By similarity). Inhibits CBL/C-CBL-mediated EGFR ubiquitination (PubMed:17974561). {ECO:0000250|UniProtKB:Q9QXV8, ECO:0000269|PubMed:17974561}.
|
Homo sapiens (Human)
|
O43598
|
DNPH1_HUMAN
|
MAAAMVPGRSESWERGEPGRPALYFCGSIRGGREDRTLYERIVSRLRRFGTVLTEHVAAAELGARGEEAAGGDRLIHEQDLEWLQQADVVVAEVTQPSLGVGYELGRAVAFNKRILCLFRPQSGRVLSAMIRGAADGSRFQVWDYEEGEVEALLDRYFEADPPGQVAASPDPTT
|
3.2.2.-
| null |
deoxyribonucleoside monophosphate catabolic process [GO:0009159]; epithelial cell differentiation [GO:0030855]; nucleoside salvage [GO:0043174]; positive regulation of cell growth [GO:0030307]; purine nucleotide catabolic process [GO:0006195]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]
|
deoxyribonucleoside 5'-monophosphate N-glycosidase activity [GO:0070694]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]
|
PF05014;
|
3.40.50.450;
|
2'-deoxynucleoside 5'-phosphate N-hydrolase 1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18726892}. Nucleus {ECO:0000269|PubMed:9271375}.
|
CATALYTIC ACTIVITY: Reaction=5-hydroxymethyl-dUMP + H2O = 2-deoxy-D-ribose 5-phosphate + 5-hydroxymethyluracil; Xref=Rhea:RHEA:77099, ChEBI:CHEBI:15377, ChEBI:CHEBI:16964, ChEBI:CHEBI:62877, ChEBI:CHEBI:90409; Evidence={ECO:0000269|PubMed:33833118, ECO:0000269|PubMed:37142196}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77100; Evidence={ECO:0000269|PubMed:33833118, ECO:0000269|PubMed:37142196};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.3 uM for 5-hydroxymethyl-dUMP (at pH 7.0 and 37 degrees Celsius) {ECO:0000269|PubMed:37142196}; KM=57 uM for dGMP {ECO:0000269|PubMed:24260472}; KM=97 uM for dAMP {ECO:0000269|PubMed:24260472}; KM=104 uM for dIMP {ECO:0000269|PubMed:24260472}; KM=2500 uM for dCMP {ECO:0000269|PubMed:24260472}; KM=7800 uM for dUMP {ECO:0000269|PubMed:24260472}; KM=25000 uM for dTMP {ECO:0000269|PubMed:24260472}; Note=kcat is 0.33 sec(-1) with 5-hydroxymethyl-dUMP as substrate (PubMed:37142196). kcat is 0.014 sec(-1) with dUMP as substrate (PubMed:37142196). {ECO:0000269|PubMed:37142196};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-7 at 37 degrees Celsius. {ECO:0000269|PubMed:37142196};
| null |
FUNCTION: Part of a nucleotide salvage pathway that eliminates epigenetically modified 5-hydroxymethyl-dCMP (hmdCMP) in a two-step process entailing deamination to cytotoxic 5-hydroxymethyl-dUMP (hmdUMP), followed by its hydrolysis into 5-hydroxymethyluracil (hmU) and 2-deoxy-D-ribose 5-phosphate (deoxyribosephosphate) (PubMed:33833118). Catalyzes the second step in that pathway, the hydrolysis of the N-glycosidic bond in hmdUMP, degrading this cytotoxic nucleotide to avoid its genomic integration (PubMed:33833118). {ECO:0000269|PubMed:33833118}.
|
Homo sapiens (Human)
|
O43602
|
DCX_HUMAN
|
MELDFGHFDERDKTSRNMRGSRMNGLPSPTHSAHCSFYRTRTLQALSNEKKAKKVRFYRNGDRYFKGIVYAVSSDRFRSFDALLADLTRSLSDNINLPQGVRYIYTIDGSRKIGSMDELEEGESYVCSSDNFFKKVEYTKNVNPNWSVNVKTSANMKAPQSLASSNSAQARENKDFVRPKLVTIIRSGVKPRKAVRVLLNKKTAHSFEQVLTDITEAIKLETGVVKKLYTLDGKQVTCLHDFFGDDDVFIACGPEKFRYAQDDFSLDENECRVMKGNPSATAGPKASPTPQKTSAKSPGPMRRSKSPADSGNDQDANGTSSSQLSTPKSKQSPISTPTSPGSLRKHKDLYLPLSLDDSDSLGDSM
| null | null |
axoneme assembly [GO:0035082]; central nervous system development [GO:0007417]; intracellular signal transduction [GO:0035556]; nervous system development [GO:0007399]; neuron migration [GO:0001764]; retina development in camera-type eye [GO:0060041]
|
cytoskeleton [GO:0005856]; cytosol [GO:0005829]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875]; microtubule organizing center [GO:0005815]; neuron projection [GO:0043005]
|
microtubule binding [GO:0008017]; protein kinase binding [GO:0019901]
|
PF03607;
|
3.10.20.230;
| null |
PTM: Phosphorylation by MARK1, MARK2 and PKA regulates its ability to bind microtubules (By similarity). Phosphorylation at Ser-265 and Ser-297 seems to occur only in neonatal brain, the levels falling precipitously by postnatal day 21 (By similarity). {ECO:0000250|UniProtKB:O88809, ECO:0000250|UniProtKB:Q9ESI7}.; PTM: Ubiquitinated by MDM2, leading to its degradation by the proteasome. Ubiquitinated by MDM2 and subsequent degradation leads to reduce the dendritic spine density of olfactory bulb granule cells. {ECO:0000250|UniProtKB:O88809}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q9ESI7}. Note=Localizes at neurite tips. {ECO:0000250|UniProtKB:Q9ESI7}.
| null | null | null | null | null |
FUNCTION: Microtubule-associated protein required for initial steps of neuronal dispersion and cortex lamination during cerebral cortex development. May act by competing with the putative neuronal protein kinase DCLK1 in binding to a target protein. May in that way participate in a signaling pathway that is crucial for neuronal interaction before and during migration, possibly as part of a calcium ion-dependent signal transduction pathway. May be part with PAFAH1B1/LIS-1 of overlapping, but distinct, signaling pathways that promote neuronal migration. {ECO:0000269|PubMed:22359282}.
|
Homo sapiens (Human)
|
O43603
|
GALR2_HUMAN
|
MNVSGCPGAGNASQAGGGGGWHPEAVIVPLLFALIFLVGTVGNTLVLAVLLRGGQAVSTTNLFILNLGVADLCFILCCVPFQATIYTLDGWVFGSLLCKAVHFLIFLTMHASSFTLAAVSLDRYLAIRYPLHSRELRTPRNALAAIGLIWGLSLLFSGPYLSYYRQSQLANLTVCHPAWSAPRRRAMDICTFVFSYLLPVLVLGLTYARTLRYLWRAVDPVAAGSGARRAKRKVTRMILIVAALFCLCWMPHHALILCVWFGQFPLTRATYALRILSHLVSYANSCVNPIVYALVSKHFRKGFRTICAGLLGRAPGRASGRVCAAARGTHSGSVLERESSDLLHMSEAAGALRPCPGASQPCILEPCPGPSWQGPKAGDSILTVDVA
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; cell surface receptor signaling pathway [GO:0007166]; feeding behavior [GO:0007631]; galanin-activated signaling pathway [GO:0090663]; inositol phosphate metabolic process [GO:0043647]; learning or memory [GO:0007611]; muscle contraction [GO:0006936]; neuron projection development [GO:0031175]; neuropeptide signaling pathway [GO:0007218]; phosphatidylinositol metabolic process [GO:0046488]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of large conductance calcium-activated potassium channel activity [GO:1902608]; positive regulation of transcription by RNA polymerase II [GO:0045944]
|
cilium [GO:0005929]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
galanin receptor activity [GO:0004966]; neuropeptide binding [GO:0042923]; peptide hormone binding [GO:0017046]
|
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 the hormone galanin and GALP. Receptor for the hormone spexin-1 (PubMed:24517231). The activity of this receptor is mediated by G proteins that activate the phospholipase C/protein kinase C pathway (via G(q)) and that inhibit adenylyl cyclase (via G(i)). {ECO:0000269|PubMed:24517231, ECO:0000269|PubMed:25691535, ECO:0000269|PubMed:9480833, ECO:0000269|PubMed:9685625, ECO:0000269|PubMed:9832121, ECO:0000269|PubMed:9880084}.
|
Homo sapiens (Human)
|
O43609
|
SPY1_HUMAN
|
MDPQNQHGSGSSLVVIQQPSLDSRQRLDYEREIQPTAILSLDQIKAIRGSNEYTEGPSVVKRPAPRTAPRQEKHERTHEIIPINVNNNYEHRHTSHLGHAVLPSNARGPILSRSTSTGSAASSGSNSSASSEQGLLGRSPPTRPVPGHRSERAIRTQPKQLIVDDLKGSLKEDLTQHKFICEQCGKCKCGECTAPRTLPSCLACNRQCLCSAESMVEYGTCMCLVKGIFYHCSNDDEGDSYSDNPCSCSQSHCCSRYLCMGAMSLFLPCLLCYPPAKGCLKLCRRCYDWIHRPGCRCKNSNTVYCKLESCPSRGQGKPS
| null | null |
animal organ development [GO:0048513]; bud elongation involved in lung branching [GO:0060449]; epithelial to mesenchymal transition involved in cardiac fibroblast development [GO:0060940]; ERK1 and ERK2 cascade [GO:0070371]; establishment of mitotic spindle orientation [GO:0000132]; metanephros development [GO:0001656]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of epithelial to mesenchymal transition [GO:0010719]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of fibroblast growth factor receptor signaling pathway [GO:0040037]; negative regulation of lens fiber cell differentiation [GO:1902747]; negative regulation of neurotrophin TRK receptor signaling pathway [GO:0051387]; negative regulation of Ras protein signal transduction [GO:0046580]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; organ induction [GO:0001759]; ureteric bud development [GO:0001657]
|
cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
| null |
PF05210;
| null |
Sprouty family
| null |
SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Note=Found in the cytoplasm in unstimulated cells but is translocated to the membrane ruffles in cells stimulated with EGF (epidermal growth factor).
| null | null | null | null | null |
FUNCTION: Inhibits fibroblast growth factor (FGF)-induced retinal lens fiber differentiation, probably by inhibiting FGF-mediated phosphorylation of ERK1/2 (By similarity). Inhibits TGFB-induced epithelial-to-mesenchymal transition in lens epithelial cells (By similarity). {ECO:0000250|UniProtKB:Q9QXV9}.
|
Homo sapiens (Human)
|
O43610
|
SPY3_HUMAN
|
MDAAVTDDFQQILPIEQLRSTHASNDYVERPPAPCKQALSSPSLIVQTHKSDWSLATMPTSLPRSLSQCHQLQPLPQHLSQSSIASSMSHSTTASDQRLLASITPSPSGQSIIRTQPGAGVHPKADGALKGEAEQSAGHPSEHLFICEECGRCKCVPCTAARPLPSCWLCNQRCLCSAESLLDYGTCLCCVKGLFYHCSTDDEDNCADEPCSCGPSSCFVRWAAMSLISLFLPCLCCYLPTRGCLHLCQQGYDSLRRPGCRCKRHTNTVCRKISSGSAPFPKAQEKSV
| null | null |
animal organ development [GO:0048513]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of fibroblast growth factor receptor signaling pathway [GO:0040037]; negative regulation of MAPK cascade [GO:0043409]; negative regulation of neuron projection arborization [GO:0150013]; negative regulation of Ras protein signal transduction [GO:0046580]; nervous system development [GO:0007399]
|
cytosol [GO:0005829]; membrane [GO:0016020]
| null |
PF05210;
| null |
Sprouty family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
| null | null | null | null | null |
FUNCTION: Inhibits neurite branching, arbor length and neurite complexity (By similarity). Inhibits EGF-mediated p42/44 ERK signaling (By similarity). Negatively regulates the MAPK cascade, resulting in a reduction of extracellular matrix protein accumulation (PubMed:30878395). May function as an antagonist of fibroblast growth factor (FGF) pathways and may negatively modulate respiratory organogenesis (PubMed:9458049). {ECO:0000250|UniProtKB:Q3UUD2, ECO:0000269|PubMed:30878395, ECO:0000269|PubMed:9458049}.
|
Homo sapiens (Human)
|
O43612
|
OREX_HUMAN
|
MNLPSTKVSWAAVTLLLLLLLLPPALLSSGAAAQPLPDCCRQKTCSCRLYELLHGAGNHAAGILTLGKRRSGPPGLQGRLQRLLQASGNHAAGILTMGRRAGAEPAPRPCLGRRCSAPAAASVAPGGQSGI
| null | null |
chemical synaptic transmission [GO:0007268]; eating behavior [GO:0042755]; excitatory postsynaptic potential [GO:0060079]; negative regulation of DNA replication [GO:0008156]; negative regulation of potassium ion transport [GO:0043267]; negative regulation of transmission of nerve impulse [GO:0051970]; neuropeptide signaling pathway [GO:0007218]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of calcium ion transport [GO:0051928]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of transmission of nerve impulse [GO:0051971]; protein kinase C-activating G protein-coupled receptor signaling pathway [GO:0007205]; regulation of neurotransmitter secretion [GO:0046928]; response to starvation [GO:0042594]; sleep [GO:0030431]; temperature homeostasis [GO:0001659]
|
extracellular region [GO:0005576]; perinuclear region of cytoplasm [GO:0048471]; postsynapse [GO:0098794]; rough endoplasmic reticulum [GO:0005791]; secretory granule [GO:0030141]; synaptic vesicle [GO:0008021]
|
neuropeptide hormone activity [GO:0005184]; type 1 orexin receptor binding [GO:0031771]; type 2 orexin receptor binding [GO:0031772]
|
PF02072;
| null |
Orexin family
|
PTM: Specific enzymatic cleavages at paired basic residues yield the different active peptides. {ECO:0000303|PubMed:9491897}.
|
SUBCELLULAR LOCATION: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:O55232}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:O55232}. Synapse {ECO:0000250|UniProtKB:O55232}. Note=Associated with perikaryal rough endoplasmic reticulum as well as cytoplasmic large granular vesicles at synapses. {ECO:0000250|UniProtKB:O55232}.
| null | null | null | null | null |
FUNCTION: Neuropeptides that play a significant role in the regulation of food intake and sleep-wakefulness, possibly by coordinating the complex behavioral and physiologic responses of these complementary homeostatic functions. A broader role in the homeostatic regulation of energy metabolism, autonomic function, hormonal balance and the regulation of body fluids, is also suggested. {ECO:0000250|UniProtKB:O55232}.; FUNCTION: [Orexin-A]: Binds to orexin receptors HCRTR1/OX1R and HCRTR2/OX2R with a high affinity (By similarity). Stimulates food intake (By similarity). Modulates pituitary luteinizing hormone secretion in an ovarian steroid-dependent manner (By similarity). {ECO:0000250|UniProtKB:O55232}.; FUNCTION: [Orexin-B]: Binds to orexin receptor HCRTR2/OX2R only (By similarity). Stimulates food intake (By similarity). Modulates pituitary luteinizing hormone secretion in an ovarian steroid-dependent manner (By similarity). {ECO:0000250|UniProtKB:O55232}.
|
Homo sapiens (Human)
|
O43613
|
OX1R_HUMAN
|
MEPSATPGAQMGVPPGSREPSPVPPDYEDEFLRYLWRDYLYPKQYEWVLIAAYVAVFVVALVGNTLVCLAVWRNHHMRTVTNYFIVNLSLADVLVTAICLPASLLVDITESWLFGHALCKVIPYLQAVSVSVAVLTLSFIALDRWYAICHPLLFKSTARRARGSILGIWAVSLAIMVPQAAVMECSSVLPELANRTRLFSVCDERWADDLYPKIYHSCFFIVTYLAPLGLMAMAYFQIFRKLWGRQIPGTTSALVRNWKRPSDQLGDLEQGLSGEPQPRARAFLAEVKQMRARRKTAKMLMVVLLVFALCYLPISVLNVLKRVFGMFRQASDREAVYACFTFSHWLVYANSAANPIIYNFLSGKFREQFKAAFSCCLPGLGPCGSLKAPSPRSSASHKSLSLQSRCSISKISEHVVLTSVTTVLP
| null | null |
cellular response to hormone stimulus [GO:0032870]; chemical synaptic transmission [GO:0007268]; feeding behavior [GO:0007631]; neuropeptide signaling pathway [GO:0007218]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; regulation of cytosolic calcium ion concentration [GO:0051480]
|
plasma membrane [GO:0005886]; synapse [GO:0045202]
|
G protein-coupled receptor activity [GO:0004930]; orexin receptor activity [GO:0016499]; peptide binding [GO:0042277]; peptide hormone binding [GO:0017046]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26950369, ECO:0000269|PubMed:9491897}; Multi-pass membrane protein {ECO:0000269|PubMed:26950369}.
| null | null | null | null | null |
FUNCTION: Moderately selective excitatory receptor for orexin-A and, with a lower affinity, for orexin-B neuropeptide (PubMed:26950369, PubMed:9491897). Triggers an increase in cytoplasmic Ca(2+) levels in response to orexin-A binding (PubMed:26950369, PubMed:9491897). {ECO:0000269|PubMed:26950369, ECO:0000269|PubMed:9491897}.
|
Homo sapiens (Human)
|
O43614
|
OX2R_HUMAN
|
MSGTKLEDSPPCRNWSSASELNETQEPFLNPTDYDDEEFLRYLWREYLHPKEYEWVLIAGYIIVFVVALIGNVLVCVAVWKNHHMRTVTNYFIVNLSLADVLVTITCLPATLVVDITETWFFGQSLCKVIPYLQTVSVSVSVLTLSCIALDRWYAICHPLMFKSTAKRARNSIVIIWIVSCIIMIPQAIVMECSTVFPGLANKTTLFTVCDERWGGEIYPKMYHICFFLVTYMAPLCLMVLAYLQIFRKLWCRQIPGTSSVVQRKWKPLQPVSQPRGPGQPTKSRMSAVAAEIKQIRARRKTARMLMIVLLVFAICYLPISILNVLKRVFGMFAHTEDRETVYAWFTFSHWLVYANSAANPIIYNFLSGKFREEFKAAFSCCCLGVHHRQEDRLTRGRTSTESRKSLTTQISNFDNISKLSEQVVLTSISTLPAANGAGPLQNW
| null | null |
cellular response to hormone stimulus [GO:0032870]; chemical synaptic transmission [GO:0007268]; circadian sleep/wake cycle process [GO:0022410]; feeding behavior [GO:0007631]; locomotion [GO:0040011]; neuropeptide signaling pathway [GO:0007218]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; regulation of circadian sleep/wake cycle, wakefulness [GO:0010840]; regulation of cytosolic calcium ion concentration [GO:0051480]
|
plasma membrane [GO:0005886]; synapse [GO:0045202]
|
neuropeptide receptor activity [GO:0008188]; orexin receptor activity [GO:0016499]; peptide binding [GO:0042277]; peptide hormone binding [GO:0017046]
|
PF00001;PF03827;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26950369, ECO:0000269|PubMed:9491897, ECO:0000305|PubMed:25533960}; Multi-pass membrane protein {ECO:0000269|PubMed:25533960}.
| null | null | null | null | null |
FUNCTION: Nonselective, high-affinity receptor for both orexin-A and orexin-B neuropeptides (PubMed:26950369, PubMed:9491897). Triggers an increase in cytoplasmic Ca(2+) levels in response to orexin-A binding (PubMed:26950369, PubMed:9491897). {ECO:0000269|PubMed:26950369, ECO:0000269|PubMed:9491897}.
|
Homo sapiens (Human)
|
O43615
|
TIM44_HUMAN
|
MAAAALRSGWCRCPRRCLGSGIQFLSSHNLPHGSTYQMRRPGGELPLSKSYSSGNRKGFLSGLLDNVKQELAKNKEMKESIKKFRDEARRLEESDVLQEARRKYKTIESETVRTSEVLRKKLGELTGTVKESLHEVSKSDLGRKIKEGVEEAAKTAKQSAESVSKGGEKLGRTAAFRALSQGVESVKKEIDDSVLGQTGPYRRPQRLRKRTEFAGDKFKEEKVFEPNEEALGVVLHKDSKWYQQWKDFKENNVVFNRFFEMKMKYDESDNAFIRASRALTDKVTDLLGGLFSKTEMSEVLTEILRVDPAFDKDRFLKQCENDIIPNVLEAMISGELDILKDWCYEATYSQLAHPIQQAKALGLQFHSRILDIDNVDLAMGKMMEQGPVLIITFQAQLVMVVRNPKGEVVEGDPDKVLRMLYVWALCRDQDELNPYAAWRLLDISASSTEQIL
| null | null |
intracellular protein transport [GO:0006886]; protein import into mitochondrial matrix [GO:0030150]; protein targeting to mitochondrion [GO:0006626]
|
fibrillar center [GO:0001650]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; TIM23 mitochondrial import inner membrane translocase complex [GO:0005744]
|
ATP binding [GO:0005524]; protein-folding chaperone binding [GO:0051087]
|
PF04280;
|
3.10.450.240;
|
Tim44 family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:10339406}; Peripheral membrane protein {ECO:0000269|PubMed:10339406}; Matrix side {ECO:0000269|PubMed:10339406}. Mitochondrion matrix {ECO:0000269|PubMed:10339406}.
| null | null | null | null | null |
FUNCTION: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner (By similarity). Recruits mitochondrial HSP70 to drive protein translocation into the matrix using ATP as an energy source (By similarity). {ECO:0000250|UniProtKB:O35857, ECO:0000250|UniProtKB:Q01852}.
|
Homo sapiens (Human)
|
O43617
|
TPPC3_HUMAN
|
MSRQANRGTESKKMSSELFTLTYGALVTQLCKDYENDEDVNKQLDKMGFNIGVRLIEDFLARSNVGRCHDFRETADVIAKVAFKMYLGITPSITNWSPAGDEFSLILENNPLVDFVELPDNHSSLIYSNLLCGVLRGALEMVQMAVEAKFVQDTLKGDGVTEIRMRFIRRIEDNLPAGEE
| null | null |
COPII vesicle coating [GO:0048208]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; intra-Golgi vesicle-mediated transport [GO:0006891]; vesicle coating [GO:0006901]; vesicle tethering [GO:0099022]
|
cis-Golgi network membrane [GO:0033106]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; TRAPP complex [GO:0030008]; TRAPPII protein complex [GO:1990071]; TRAPPIII protein complex [GO:1990072]
| null |
PF04051;
|
3.30.1380.20;
|
TRAPP small subunits family, BET3 subfamily
| null |
SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi.
|
Homo sapiens (Human)
|
O43623
|
SNAI2_HUMAN
|
MPRSFLVKKHFNASKKPNYSELDTHTVIISPYLYESYSMPVIPQPEILSSGAYSPITVWTTAAPFHAQLPNGLSPLSGYSSSLGRVSPPPPSDTSSKDHSGSESPISDEEERLQSKLSDPHAIEAEKFQCNLCNKTYSTFSGLAKHKQLHCDAQSRKSFSCKYCDKEYVSLGALKMHIRTHTLPCVCKICGKAFSRPWLLQGHIRTHTGEKPFSCPHCNRAFADRSNLRAHLQTHSDVKKYQCKNCSKTFSRMSLLHKHEESGCCVAH
| null | null |
aortic valve morphogenesis [GO:0003180]; cartilage morphogenesis [GO:0060536]; cell migration involved in endocardial cushion formation [GO:0003273]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to ionizing radiation [GO:0071479]; chromatin organization [GO:0006325]; desmosome disassembly [GO:0035921]; endothelial cell migration [GO:0043542]; epithelial to mesenchymal transition [GO:0001837]; epithelial to mesenchymal transition involved in endocardial cushion formation [GO:0003198]; epithelium development [GO:0060429]; hematopoietic stem cell proliferation [GO:0071425]; myeloid cell apoptotic process [GO:0033028]; negative regulation of anoikis [GO:2000811]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cell adhesion involved in substrate-bound cell migration [GO:0006933]; negative regulation of cell adhesion mediated by integrin [GO:0033629]; negative regulation of chondrocyte differentiation [GO:0032331]; negative regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043518]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; negative regulation of hematopoietic stem cell proliferation [GO:1902034]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage [GO:1902230]; negative regulation of keratinocyte proliferation [GO:0010839]; negative regulation of myeloid cell apoptotic process [GO:0033033]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of vitamin D biosynthetic process [GO:0010957]; negative regulation of vitamin D receptor signaling pathway [GO:0070563]; neural crest cell development [GO:0014032]; Notch signaling pathway [GO:0007219]; osteoblast differentiation [GO:0001649]; pigmentation [GO:0043473]; positive regulation of cell migration [GO:0030335]; positive regulation of fat cell differentiation [GO:0045600]; regulation of bicellular tight junction assembly [GO:2000810]; regulation of branching involved in salivary gland morphogenesis [GO:0060693]; regulation of chemokine production [GO:0032642]; regulation of DNA-templated transcription [GO:0006355]; regulation of osteoblast differentiation [GO:0045667]; roof of mouth development [GO:0060021]; sensory perception of sound [GO:0007605]; white fat cell differentiation [GO:0050872]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00096;
|
3.30.160.60;
|
Snail C2H2-type zinc-finger protein family
|
PTM: GSK3B-mediated phosphorylation results in cytoplasmic localization and degradation. {ECO:0000269|PubMed:22727060}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25893292}. Cytoplasm. Note=Observed in discrete foci in interphase nuclei. These nuclear foci do not overlap with the nucleoli, the SP100 and the HP1 heterochromatin or the coiled body, suggesting SNAI2 is associated with active transcription or active splicing regions.
| null | null | null | null | null |
FUNCTION: Transcriptional repressor that modulates both activator-dependent and basal transcription. Involved in the generation and migration of neural crest cells. Plays a role in mediating RAF1-induced transcriptional repression of the TJ protein, occludin (OCLN) and subsequent oncogenic transformation of epithelial cells (By similarity). Represses BRCA2 expression by binding to its E2-box-containing silencer and recruiting CTBP1 and HDAC1 in breast cells. In epidermal keratinocytes, binds to the E-box in ITGA3 promoter and represses its transcription. Involved in the regulation of ITGB1 and ITGB4 expression and cell adhesion and proliferation in epidermal keratinocytes. Binds to E-box2 domain of BSG and activates its expression during TGFB1-induced epithelial-mesenchymal transition (EMT) in hepatocytes. Represses E-Cadherin/CDH1 transcription via E-box elements. Involved in osteoblast maturation. Binds to RUNX2 and SOC9 promoters and may act as a positive and negative transcription regulator, respectively, in osteoblasts. Binds to CXCL12 promoter via E-box regions in mesenchymal stem cells and osteoblasts. Plays an essential role in TWIST1-induced EMT and its ability to promote invasion and metastasis. {ECO:0000250, ECO:0000269|PubMed:10866665, ECO:0000269|PubMed:11912130, ECO:0000269|PubMed:15734731, ECO:0000269|PubMed:16707493, ECO:0000269|PubMed:19756381, ECO:0000269|PubMed:21182836}.
|
Homo sapiens (Human)
|
O43633
|
CHM2A_HUMAN
|
MDLLFGRRKTPEELLRQNQRALNRAMRELDRERQKLETQEKKIIADIKKMAKQGQMDAVRIMAKDLVRTRRYVRKFVLMRANIQAVSLKIQTLKSNNSMAQAMKGVTKAMGTMNRQLKLPQIQKIMMEFERQAEIMDMKEEMMNDAIDDAMGDEEDEEESDAVVSQVLDELGLSLTDELSNLPSTGGSLSVAAGGKKAEAAASALADADADLEERLKNLRRD
| null | null |
autophagosome maturation [GO:0097352]; autophagy [GO:0006914]; endosome transport via multivesicular body sorting pathway [GO:0032509]; ESCRT III complex disassembly [GO:1904903]; establishment of protein localization [GO:0045184]; exit from mitosis [GO:0010458]; late endosome to lysosome transport [GO:1902774]; late endosome to vacuole transport [GO:0045324]; macroautophagy [GO:0016236]; membrane fission [GO:0090148]; membrane invagination [GO:0010324]; midbody abscission [GO:0061952]; mitotic metaphase chromosome alignment [GO:0007080]; multivesicular body assembly [GO:0036258]; multivesicular body sorting pathway [GO:0071985]; multivesicular body-lysosome fusion [GO:0061763]; negative regulation of centriole elongation [GO:1903723]; nuclear membrane reassembly [GO:0031468]; nucleus organization [GO:0006997]; plasma membrane repair [GO:0001778]; positive regulation of exosomal secretion [GO:1903543]; protein homooligomerization [GO:0051260]; protein polymerization [GO:0051258]; protein transport [GO:0015031]; regulation of centrosome duplication [GO:0010824]; regulation of mitotic spindle assembly [GO:1901673]; ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043162]; vesicle fusion with vacuole [GO:0051469]; viral budding from plasma membrane [GO:0046761]; viral budding via host ESCRT complex [GO:0039702]; viral release from host cell [GO:0019076]
|
amphisome membrane [GO:1904930]; autophagosome membrane [GO:0000421]; chromatin [GO:0000785]; cytosol [GO:0005829]; ESCRT III complex [GO:0000815]; extracellular exosome [GO:0070062]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; membrane coat [GO:0030117]; midbody [GO:0030496]; multivesicular body [GO:0005771]; multivesicular body membrane [GO:0032585]; nuclear envelope [GO:0005635]; nuclear pore [GO:0005643]; plasma membrane [GO:0005886]
|
phosphatidylcholine binding [GO:0031210]; protein domain specific binding [GO:0019904]
|
PF03357;
|
6.10.140.1230;
|
SNF7 family
|
PTM: ISGylated in a CHMP5-dependent manner. Isgylation weakens and inhibits its interactions with VPS4A and VTA1 respectively. {ECO:0000269|PubMed:21543490}.
|
SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:16730941, ECO:0000269|PubMed:17853893}; Peripheral membrane protein {ECO:0000269|PubMed:16730941, ECO:0000269|PubMed:17853893}; Cytoplasmic side {ECO:0000269|PubMed:16730941, ECO:0000269|PubMed:17853893}. Nucleus envelope {ECO:0000269|PubMed:28242692}. Note=Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Fleming body. Localizes to the reforming nuclear envelope on chromatin disks during late anaphase (PubMed:28242692). {ECO:0000269|PubMed:28242692}.
| null | null | null | null | null |
FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis (PubMed:21310966). Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase (PubMed:26040712). Recruited to the reforming nuclear envelope (NE) during anaphase by LEMD2 (PubMed:28242692). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. {ECO:0000269|PubMed:21310966, ECO:0000269|PubMed:26040712, ECO:0000269|PubMed:28242692, ECO:0000305}.; FUNCTION: (Microbial infection) The ESCRT machinery functions in topologically equivalent membrane fission events, such as the budding of enveloped viruses (HIV-1 and other lentiviruses). Involved in HIV-1 p6- and p9-dependent virus release. {ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14519844}.
|
Homo sapiens (Human)
|
O43639
|
NCK2_HUMAN
|
MTEEVIVIAKWDYTAQQDQELDIKKNERLWLLDDSKTWWRVRNAANRTGYVPSNYVERKNSLKKGSLVKNLKDTLGLGKTRRKTSARDASPTPSTDAEYPANGSGADRIYDLNIPAFVKFAYVAEREDELSLVKGSRVTVMEKCSDGWWRGSYNGQIGWFPSNYVLEEVDEAAAESPSFLSLRKGASLSNGQGSRVLHVVQTLYPFSSVTEEELNFEKGETMEVIEKPENDPEWWKCKNARGQVGLVPKNYVVVLSDGPALHPAHAPQISYTGPSSSGRFAGREWYYGNVTRHQAECALNERGVEGDFLIRDSESSPSDFSVSLKASGKNKHFKVQLVDNVYCIGQRRFHTMDELVEHYKKAPIFTSEHGEKLYLVRALQ
| null | null |
actin filament organization [GO:0007015]; cell migration [GO:0016477]; dendritic spine development [GO:0060996]; ephrin receptor signaling pathway [GO:0048013]; epidermal growth factor receptor signaling pathway [GO:0007173]; immunological synapse formation [GO:0001771]; lamellipodium assembly [GO:0030032]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation [GO:1903912]; negative regulation of PERK-mediated unfolded protein response [GO:1903898]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902237]; positive regulation of peptidyl-serine dephosphorylation [GO:1902310]; positive regulation of T cell proliferation [GO:0042102]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of translation in response to endoplasmic reticulum stress [GO:0036493]; signal complex assembly [GO:0007172]; signal transduction [GO:0007165]; T cell activation [GO:0042110]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; postsynaptic density [GO:0014069]; vesicle membrane [GO:0012506]
|
cytoskeletal anchor activity [GO:0008093]; phosphotyrosine residue binding [GO:0001784]; protein-containing complex binding [GO:0044877]; receptor tyrosine kinase binding [GO:0030971]; scaffold protein binding [GO:0097110]; signaling adaptor activity [GO:0035591]; signaling receptor complex adaptor activity [GO:0030159]
|
PF00017;PF00018;PF14604;
|
3.30.505.10;2.30.30.40;
| null |
PTM: Phosphorylated. {ECO:0000269|PubMed:10026169}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16835242}. Endoplasmic reticulum {ECO:0000269|PubMed:16835242}.
| null | null | null | null | null |
FUNCTION: Adapter protein which associates with tyrosine-phosphorylated growth factor receptors or their cellular substrates. Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in ELK1-dependent transcriptional activation in response to activated Ras signaling. {ECO:0000269|PubMed:10026169, ECO:0000269|PubMed:16835242}.
|
Homo sapiens (Human)
|
O43653
|
PSCA_HUMAN
|
MAGLALQPGTALLCYSCKAQVSNEDCLQVENCTQLGEQCWTARIRAVGLLTVISKGCSLNCVDDSQDYYVGKKNITCCDTDLCNASGAHALQPAAAILALLPALGLLLWGPGQL
| null | null |
negative regulation of ERK1 and ERK2 cascade [GO:0070373]; regulation of neurotransmitter receptor activity [GO:0099601]
|
extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
|
acetylcholine receptor binding [GO:0033130]
|
PF00021;
|
2.10.60.10;
| null |
PTM: N-glycosylated. {ECO:0000269|PubMed:9465086}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9465086}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:9465086}.
| null | null | null | null | null |
FUNCTION: May be involved in the regulation of cell proliferation. Has a cell-proliferation inhibition activity in vitro. {ECO:0000269|PubMed:18488030}.; FUNCTION: May act as a modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro inhibits nicotine-induced signaling probably implicating alpha-3:beta-2- or alpha-7-containing nAChRs. {ECO:0000305|PubMed:25680266}.
|
Homo sapiens (Human)
|
O43660
|
PLRG1_HUMAN
|
MVEEVQKHSVHTLVFRSLKRTHDMFVADNGKPVPLDEESHKRKMAIKLRNEYGPVLHMPTSKENLKEKGPQNATDSYVHKQYPANQGQEVEYFVAGTHPYPPGPGVALTADTKIQRMPSESAAQSLAVALPLQTKADANRTAPSGSEYRHPGASDRPQPTAMNSIVMETGNTKNSALMAKKAPTMPKPQWHPPWKLYRVISGHLGWVRCIAVEPGNQWFVTGSADRTIKIWDLASGKLKLSLTGHISTVRGVIVSTRSPYLFSCGEDKQVKCWDLEYNKVIRHYHGHLSAVYGLDLHPTIDVLVTCSRDSTARIWDVRTKASVHTLSGHTNAVATVRCQAAEPQIITGSHDTTIRLWDLVAGKTRVTLTNHKKSVRAVVLHPRHYTFASGSPDNIKQWKFPDGSFIQNLSGHNAIINTLTVNSDGVLVSGADNGTMHLWDWRTGYNFQRVHAAVQPGSLDSESGIFACAFDQSESRLLTAEADKTIKVYREDDTATEETHPVSWKPEIIKRKRF
| null | null |
mRNA splicing, via spliceosome [GO:0000398]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; protein localization to nucleus [GO:0034504]
|
catalytic step 2 spliceosome [GO:0071013]; fibrillar center [GO:0001650]; nuclear membrane [GO:0031965]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; precatalytic spliceosome [GO:0071011]; Prp19 complex [GO:0000974]; spliceosomal complex [GO:0005681]; U2-type catalytic step 2 spliceosome [GO:0071007]
| null |
PF00400;
|
2.130.10.10;
|
WD repeat PRL1/PRL2 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11101529, ECO:0000269|PubMed:20176811, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}. Nucleus speckle {ECO:0000269|PubMed:11544257}.
| null | null | null | null | null |
FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome (PubMed:28076346, PubMed:28502770). Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing (PubMed:11101529, PubMed:11544257). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). {ECO:0000269|PubMed:11101529, ECO:0000269|PubMed:11544257, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000305|PubMed:33509932}.
|
Homo sapiens (Human)
|
O43663
|
PRC1_HUMAN
|
MRRSEVLAEESIVCLQKALNHLREIWELIGIPEDQRLQRTEVVKKHIKELLDMMIAEEESLKERLIKSISVCQKELNTLCSELHVEPFQEEGETTILQLEKDLRTQVELMRKQKKERKQELKLLQEQDQELCEILCMPHYDIDSASVPSLEELNQFRQHVTTLRETKASRREEFVSIKRQIILCMEALDHTPDTSFERDVVCEDEDAFCLSLENIATLQKLLRQLEMQKSQNEAVCEGLRTQIRELWDRLQIPEEEREAVATIMSGSKAKVRKALQLEVDRLEELKMQNMKKVIEAIRVELVQYWDQCFYSQEQRQAFAPFCAEDYTESLLQLHDAEIVRLKNYYEVHKELFEGVQKWEETWRLFLEFERKASDPNRFTNRGGNLLKEEKQRAKLQKMLPKLEEELKARIELWEQEHSKAFMVNGQKFMEYVAEQWEMHRLEKERAKQERQLKNKKQTETEMLYGSAPRTPSKRRGLAPNTPGKARKLNTTTMSNATANSSIRPIFGGTVYHSPVSRLPPSGSKPVAASTCSGKKTPRTGRHGANKENLELNGSILSGGYPGSAPLQRNFSINSVASTYSEFAKDPSLSDSSTVGLQRELSKASKSDATSGILNSTNIQS
| null | null |
cell division [GO:0051301]; microtubule cytoskeleton organization [GO:0000226]; mitotic spindle elongation [GO:0000022]; mitotic spindle midzone assembly [GO:0051256]; positive regulation of cell population proliferation [GO:0008284]; regulation of cytokinesis [GO:0032465]
|
chromosome [GO:0005694]; contractile ring [GO:0070938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intercellular bridge [GO:0045171]; microtubule cytoskeleton [GO:0015630]; midbody [GO:0030496]; mitotic spindle midzone [GO:1990023]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; spindle [GO:0005819]; spindle microtubule [GO:0005876]; spindle pole [GO:0000922]
|
identical protein binding [GO:0042802]; kinesin binding [GO:0019894]; microtubule binding [GO:0008017]; protein kinase binding [GO:0019901]
|
PF03999;
|
1.20.58.1520;
|
MAP65/ASE1 family
|
PTM: Phosphorylation by CDK1 in early mitosis holds PRC1 in an inactive monomeric state, during the metaphase to anaphase transition, PRC1 is dephosphorylated, promoting interaction with KIF4A, which then translocates PRC1 along mitotic spindles to the plus ends of antiparallel interdigitating microtubules. Dephosphorylation also promotes MT-bundling activity by allowing dimerization. Phosphorylation by CDK1 prevents PLK1-binding: upon degradation of CDK1 at anaphase and dephosphorylation, it is then phosphorylated by PLK1, leading to cytokinesis. {ECO:0000269|PubMed:17351640, ECO:0000269|PubMed:17438553, ECO:0000269|PubMed:9885575}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17409436}. Cytoplasm. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:15625105}. Midbody {ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:15625105, ECO:0000269|PubMed:17409436}. Chromosome {ECO:0000269|PubMed:15297875}. Note=Colocalized with KIF20B in the nucleus of bladder carcinoma cells at the interphase. Colocalized with KIF20B in bladder carcinoma cells at prophase, metaphase, early anaphase, at the midzone in late anaphase and at the contractile ring in telophase (PubMed:17409436). Predominantly localized to the nucleus of interphase cells. During mitosis becomes associated with the mitotic spindle poles and localizes with the cell midbody during cytokinesis. Co-localizes with PRC1 in early mitosis and at the spindle midzone from anaphase B to telophase (PubMed:15297875, PubMed:15625105). {ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:15625105, ECO:0000269|PubMed:17409436}.
| null | null | null | null | null |
FUNCTION: Key regulator of cytokinesis that cross-links antiparrallel microtubules at an average distance of 35 nM. Essential for controlling the spatiotemporal formation of the midzone and successful cytokinesis. Required for KIF14 localization to the central spindle and midbody. Required to recruit PLK1 to the spindle. Stimulates PLK1 phosphorylation of RACGAP1 to allow recruitment of ECT2 to the central spindle. Acts as an oncogene for promoting bladder cancer cells proliferation, apoptosis inhibition and carcinogenic progression (PubMed:17409436). {ECO:0000269|PubMed:12082078, ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:15625105, ECO:0000269|PubMed:16431929, ECO:0000269|PubMed:17409436, ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:20691902, ECO:0000269|PubMed:9885575}.
|
Homo sapiens (Human)
|
O43665
|
RGS10_HUMAN
|
MFNRAVSRLSRKRPPSDIHDSDGSSSSSHQSLKSTAKWAASLENLLEDPEGVKRFREFLKKEFSEENVLFWLACEDFKKMQDKTQMQEKAKEIYMTFLSSKASSQVNVEGQSRLNEKILEEPHPLMFQKLQDQIFNLMKYDSYSRFLKSDLFLKHKRTEEEEEDLPDAQTAAKRASRIYNT
| null | null |
G protein-coupled acetylcholine receptor signaling pathway [GO:0007213]; G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of signal transduction [GO:0009968]; positive regulation of GTPase activity [GO:0043547]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]
|
cytosol [GO:0005829]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; synapse [GO:0045202]
|
G-protein alpha-subunit binding [GO:0001965]; GTPase activator activity [GO:0005096]; GTPase activity [GO:0003924]
|
PF00615;
|
1.10.196.10;1.10.167.10;
| null | null |
SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytosol {ECO:0000269|PubMed:11443111}. Nucleus {ECO:0000269|PubMed:11443111}. Note=Forskolin treatment promotes phosphorylation and translocation to the nucleus. {ECO:0000269|PubMed:11443111}.; SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10791963}.
| null | null | null | null | null |
FUNCTION: Regulates G protein-coupled receptor signaling cascades, including signaling downstream of the muscarinic acetylcholine receptor CHRM2. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form (PubMed:10608901, PubMed:11443111, PubMed:18434541, PubMed:8774883, PubMed:9353196). Modulates the activity of potassium channels that are activated in response to CHRM2 signaling (PubMed:11443111). Activity on GNAZ is inhibited by palmitoylation of the G-protein (PubMed:9353196). {ECO:0000269|PubMed:10608901, ECO:0000269|PubMed:11443111, ECO:0000269|PubMed:18434541, ECO:0000269|PubMed:8774883, ECO:0000269|PubMed:9353196}.
|
Homo sapiens (Human)
|
O43670
|
ZN207_HUMAN
|
MGRKKKKQLKPWCWYCNRDFDDEKILIQHQKAKHFKCHICHKKLYTGPGLAIHCMQVHKETIDAVPNAIPGRTDIELEIYGMEGIPEKDMDERRRLLEQKTQESQKKKQQDDSDEYDDDDSAASTSFQPQPVQPQQGYIPPMAQPGLPPVPGAPGMPPGIPPLMPGVPPLMPGMPPVMPGMPPGMMPMGGMMPPGPGIPPLMPGMPPGMPPPVPRPGIPPMTQAQAVSAPGILNRPPAPTATVPAPQPPVTKPLFPSAGQMGTPVTSSSTASSNSESLSASSKALFPSTAQAQAAVQGPVGTDFKPLNSTPATTTEPPKPTFPAYTQSTASTTSTTNSTAAKPAASITSKPATLTTTSATSKLIHPDEDISLEERRAQLPKYQRNLPRPGQAPIGNPPVGPIGGMMPPQPGIPQQQGMRPPMPPHGQYGGHHQGMPGYLPGAMPPYGQGPPMVPPYQGGPPRPPMGMRPPVMSQGGRY
| null | null |
attachment of spindle microtubules to kinetochore [GO:0008608]; cell division [GO:0051301]; microtubule bundle formation [GO:0001578]; microtubule polymerization [GO:0046785]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle assembly [GO:0090307]; mitotic spindle assembly checkpoint signaling [GO:0007094]; protein stabilization [GO:0050821]; regulation of chromosome segregation [GO:0051983]
|
cytoplasm [GO:0005737]; kinetochore [GO:0000776]; microtubule [GO:0005874]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819]; spindle matrix [GO:1990047]
|
DNA binding [GO:0003677]; heparin binding [GO:0008201]; metal ion binding [GO:0046872]; microtubule binding [GO:0008017]; RNA binding [GO:0003723]
| null | null | null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24462186, ECO:0000269|PubMed:24462187}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:24462186, ECO:0000269|PubMed:24462187}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:26388440}. Note=Localizes primarily to the nucleus in interphase, concentrates at kinetochores prior to nuclear envelope breakdown and during early prometaphase, and disappears from kinetochores upon microtubule-binding. {ECO:0000269|PubMed:24462186, ECO:0000269|PubMed:24462187}.
| null | null | null | null | null |
FUNCTION: Kinetochore- and microtubule-binding protein that plays a key role in spindle assembly (PubMed:24462186, PubMed:24462187, PubMed:26388440). ZNF207/BuGZ is mainly composed of disordered low-complexity regions and undergoes phase transition or coacervation to form temperature-dependent liquid droplets. Coacervation promotes microtubule bundling and concentrates tubulin, promoting microtubule polymerization and assembly of spindle and spindle matrix by concentrating its building blocks (PubMed:26388440). Also acts as a regulator of mitotic chromosome alignment by mediating the stability and kinetochore loading of BUB3 (PubMed:24462186, PubMed:24462187). Mechanisms by which BUB3 is protected are unclear: according to a first report, ZNF207/BuGZ may act by blocking ubiquitination and proteasomal degradation of BUB3 (PubMed:24462186). According to another report, the stabilization is independent of the proteasome (PubMed:24462187). {ECO:0000269|PubMed:24462186, ECO:0000269|PubMed:24462187, ECO:0000269|PubMed:26388440}.
|
Homo sapiens (Human)
|
O43674
|
NDUB5_HUMAN
|
MAAMSLLRRVSVTAVAALSGRPLGTRLGFGGFLTRGFPKAAAPVRHSGDHGKRLFVIRPSRFYDRRFLKLLRFYIALTGIPVAIFITLVNVFIGQAELAEIPEGYVPEHWEYYKHPISRWIARNFYDSPEKIYERTMAVLQIEAEKAELRVKELEVRKLMHVRGDGPWYYYETIDKELIDHSPKATPDN
| null | null |
aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
|
PF09781;
| null |
Complex I NDUFB5 subunit family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Single-pass membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.
| 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:27626371}.
|
Homo sapiens (Human)
|
O43676
|
NDUB3_HUMAN
|
MAHEHGHEHGHHKMELPDYRQWKIEGTPLETIQKKLAAKGLRDPWGRNEAWRYMGGFAKSVSFSDVFFKGFKWGFAAFVVAVGAEYYLESLNKDKKHH
| null | null |
aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
|
PF08122;
| null |
Complex I NDUFB3 subunit family
|
PTM: Methylation at His residues by METTL9 enhances complex I-mediated mitochondrial respiration. {ECO:0000269|PubMed:33563959}.
|
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Single-pass membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.
| 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:27626371}.
|
Homo sapiens (Human)
|
O43678
|
NDUA2_HUMAN
|
MAAAAASRGVGAKLGLREIRIHLCQRSPGSQGVRDFIEKRYVELKKANPDLPILIRECSDVQPKLWARYAFGQETNVPLNNFSADQVTRALENVLSGKA
| null | null |
aerobic respiration [GO:0009060]; blastocyst hatching [GO:0001835]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex I [GO:0005747]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
|
PF05047;
|
3.40.30.10;
|
Complex I NDUFA2 subunit family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Peripheral membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.
| 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:27626371}.
|
Homo sapiens (Human)
|
O43679
|
LDB2_HUMAN
|
MSSTPHDPFYSSPFGPFYRRHTPYMVQPEYRIYEMNKRLQSRTEDSDNLWWDAFATEFFEDDATLTLSFCLEDGPKRYTIGRTLIPRYFSTVFEGGVTDLYYILKHSKESYHNSSITVDCDQCTMVTQHGKPMFTKVCTEGRLILEFTFDDLMRIKTWHFTIRQYRELVPRSILAMHAQDPQVLDQLSKNITRMGLTNFTLNYLRLCVILEPMQELMSRHKTYNLSPRDCLKTCLFQKWQRMVAPPAEPTRQPTTKRRKRKNSTSSTSNSSAGNNANSTGSKKKTTAANLSLSSQVPDVMVVGEPTLMGGEFGDEDERLITRLENTQYDAANGMDDEEDFNNSPALGNNSPWNSKPPATQETKSENPPPQASQ
| null | null |
cellular component biogenesis [GO:0044085]; epithelial structure maintenance [GO:0010669]; hair follicle development [GO:0001942]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nervous system development [GO:0007399]; positive regulation of cellular component biogenesis [GO:0044089]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cell migration [GO:0030334]; regulation of kinase activity [GO:0043549]; somatic stem cell population maintenance [GO:0035019]
|
cell leading edge [GO:0031252]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; transcription regulator complex [GO:0005667]
|
enzyme binding [GO:0019899]; LIM domain binding [GO:0030274]; transcription coregulator activity [GO:0003712]
|
PF17916;PF01803;
|
2.10.110.10;
|
LDB family
|
PTM: Ubiquitinated by RLIM/RNF12, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:O55203}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9853615}.
| null | null | null | null | null |
FUNCTION: Transcription cofactor. Binds to the LIM domain of a wide variety of LIM domain-containing transcription factors. {ECO:0000250|UniProtKB:O55203}.
|
Homo sapiens (Human)
|
O43680
|
TCF21_HUMAN
|
MSTGSLSDVEDLQEVEMLECDGLKMDSNKEFVTSNESTEESSNCENGSPQKGRGGLGKRRKAPTKKSPLSGVSQEGKQVQRNAANARERARMRVLSKAFSRLKTTLPWVPPDTKLSKLDTLRLASSYIAHLRQILANDKYENGYIHPVNLTWPFMVAGKPESDLKEVVTASRLCGTTAS
| null | null |
branching involved in ureteric bud morphogenesis [GO:0001658]; branchiomeric skeletal muscle development [GO:0014707]; bronchiole development [GO:0060435]; developmental process [GO:0032502]; diaphragm development [GO:0060539]; embryonic digestive tract morphogenesis [GO:0048557]; epithelial cell differentiation [GO:0030855]; gland development [GO:0048732]; glomerulus development [GO:0032835]; kidney development [GO:0001822]; lung alveolus development [GO:0048286]; lung morphogenesis [GO:0060425]; lung vasculature development [GO:0060426]; metanephric glomerular capillary formation [GO:0072277]; metanephric mesenchymal cell differentiation [GO:0072162]; morphogenesis of a branching structure [GO:0001763]; negative regulation of androgen receptor signaling pathway [GO:0060766]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; reproductive structure development [GO:0048608]; respiratory system development [GO:0060541]; roof of mouth development [GO:0060021]; Sertoli cell differentiation [GO:0060008]; sex determination [GO:0007530]; spleen development [GO:0048536]; ureteric bud development [GO:0001657]; vasculature development [GO:0001944]
|
chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
bHLH transcription factor binding [GO:0043425]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; histone deacetylase binding [GO:0042826]; nuclear androgen receptor binding [GO:0050681]; protein dimerization activity [GO:0046983]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00010;
|
4.10.280.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Involved in epithelial-mesenchymal interactions in kidney and lung morphogenesis that include epithelial differentiation and branching morphogenesis. May play a role in the specification or differentiation of one or more subsets of epicardial cell types.
|
Homo sapiens (Human)
|
O43681
|
GET3_HUMAN
|
MAAGVAGWGVEAEEFEDAPDVEPLEPTLSNIIEQRSLKWIFVGGKGGVGKTTCSCSLAVQLSKGRESVLIISTDPAHNISDAFDQKFSKVPTKVKGYDNLFAMEIDPSLGVAELPDEFFEEDNMLSMGKKMMQEAMSAFPGIDEAMSYAEVMRLVKGMNFSVVVFDTAPTGHTLRLLNFPTIVERGLGRLMQIKNQISPFISQMCNMLGLGDMNADQLASKLEETLPVIRSVSEQFKDPEQTTFICVCIAEFLSLYETERLIQELAKCKIDTHNIIVNQLVFPDPEKPCKMCEARHKIQAKYLDQMEDLYEDFHIVKLPLLPHEVRGADKVNTFSALLLEPYKPPSAQ
|
3.6.-.-
| null |
post-translational protein targeting to endoplasmic reticulum membrane [GO:0006620]; protein insertion into ER membrane [GO:0045048]; tail-anchored membrane protein insertion into ER membrane [GO:0071816]
|
cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; GET complex [GO:0043529]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]
|
arsenite transmembrane transporter activity [GO:0015105]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; membrane insertase activity [GO:0032977]; metal ion binding [GO:0046872]
|
PF02374;
|
3.40.50.300;
|
ArsA ATPase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17382883, ECO:0000269|PubMed:21444755, ECO:0000269|PubMed:9736449}. Endoplasmic reticulum {ECO:0000269|PubMed:17382883, ECO:0000269|PubMed:21444755, ECO:0000269|PubMed:31461301}. Nucleus, nucleolus {ECO:0000269|PubMed:21444755, ECO:0000269|PubMed:9736449}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.22 mM for ATP {ECO:0000269|PubMed:9712828}; Vmax=16.6 nmol/min/mg enzyme for ATP {ECO:0000269|PubMed:9712828};
| null | null | null |
FUNCTION: ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors GET1/WRB and CAMLG/GET2, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the GET1-CAMLG receptor, and returning it to the cytosol to initiate a new round of targeting. May be involved in insulin signaling. {ECO:0000255|HAMAP-Rule:MF_03112, ECO:0000269|PubMed:17382883, ECO:0000269|PubMed:18477612, ECO:0000269|PubMed:23041287, ECO:0000269|PubMed:25535373, ECO:0000269|PubMed:31461301}.
|
Homo sapiens (Human)
|
O43683
|
BUB1_HUMAN
|
MDTPENVLQMLEAHMQSYKGNDPLGEWERYIQWVEENFPENKEYLITLLEHLMKEFLDKKKYHNDPRFISYCLKFAEYNSDLHQFFEFLYNHGIGTLSSPLYIAWAGHLEAQGELQHASAVLQRGIQNQAEPREFLQQQYRLFQTRLTETHLPAQARTSEPLHNVQVLNQMITSKSNPGNNMACISKNQGSELSGVISSACDKESNMERRVITISKSEYSVHSSLASKVDVEQVVMYCKEKLIRGESEFSFEELRAQKYNQRRKHEQWVNEDRHYMKRKEANAFEEQLLKQKMDELHKKLHQVVETSHEDLPASQERSEVNPARMGPSVGSQQELRAPCLPVTYQQTPVNMEKNPREAPPVVPPLANAISAALVSPATSQSIAPPVPLKAQTVTDSMFAVASKDAGCVNKSTHEFKPQSGAEIKEGCETHKVANTSSFHTTPNTSLGMVQATPSKVQPSPTVHTKEALGFIMNMFQAPTLPDISDDKDEWQSLDQNEDAFEAQFQKNVRSSGAWGVNKIISSLSSAFHVFEDGNKENYGLPQPKNKPTGARTFGERSVSRLPSKPKEEVPHAEEFLDDSTVWGIRCNKTLAPSPKSPGDFTSAAQLASTPFHKLPVESVHILEDKENVVAKQCTQATLDSCEENMVVPSRDGKFSPIQEKSPKQALSSHMYSASLLRLSQPAAGGVLTCEAELGVEACRLTDTDAAIAEDPPDAIAGLQAEWMQMSSLGTVDAPNFIVGNPWDDKLIFKLLSGLSKPVSSYPNTFEWQCKLPAIKPKTEFQLGSKLVYVHHLLGEGAFAQVYEATQGDLNDAKNKQKFVLKVQKPANPWEFYIGTQLMERLKPSMQHMFMKFYSAHLFQNGSVLVGELYSYGTLLNAINLYKNTPEKVMPQGLVISFAMRMLYMIEQVHDCEIIHGDIKPDNFILGNGFLEQDDEDDLSAGLALIDLGQSIDMKLFPKGTIFTAKCETSGFQCVEMLSNKPWNYQIDYFGVAATVYCMLFGTYMKVKNEGGECKPEGLFRRLPHLDMWNEFFHVMLNIPDCHHLPSLDLLRQKLKKVFQQHYTNKIRALRNRLIVLLLECKRSRK
|
2.7.11.1
| null |
apoptotic process [GO:0006915]; cell division [GO:0051301]; chromosome segregation [GO:0007059]; meiotic sister chromatid cohesion, centromeric [GO:0051754]; mitotic spindle assembly checkpoint signaling [GO:0007094]; phosphorylation [GO:0016310]; positive regulation of maintenance of mitotic sister chromatid cohesion, centromeric [GO:2000720]; regulation of chromosome segregation [GO:0051983]; regulation of sister chromatid cohesion [GO:0007063]
|
cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; kinetochore [GO:0000776]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; outer kinetochore [GO:0000940]
|
ATP binding [GO:0005524]; histone H2A kinase activity [GO:0140995]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF08311;PF00069;
|
1.25.40.430;6.10.130.20;1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, BUB1 subfamily
|
PTM: Upon spindle-assembly checkpoint activation it is hyperphosphorylated and its kinase activity toward CDC20 is stimulated. Phosphorylation at Thr-609 is required for interaction with PLK1, phosphorylation at this site probably creates a binding site for the POLO-box domain of PLK1, thus enhancing the PLK1-BUB1 interaction. {ECO:0000269|PubMed:10198256, ECO:0000269|PubMed:15525512, ECO:0000269|PubMed:16760428}.; PTM: Ubiquitinated and degraded during mitotic exit by APC/C-Cdh1. {ECO:0000269|PubMed:17158872}.
|
SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore. Note=Nuclear in interphase cells. Accumulates gradually during G1 and S phase of the cell cycle, peaks at G2/M, and drops dramatically after mitosis. Localizes to the outer kinetochore. Kinetochore localization is required for normal mitotic timing and checkpoint response to spindle damage and occurs very early in prophase. AURKB, KNL1 and INCENP are required for kinetochore localization (By similarity). {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase that performs 2 crucial functions during mitosis: it is essential for spindle-assembly checkpoint signaling and for correct chromosome alignment. Has a key role in the assembly of checkpoint proteins at the kinetochore, being required for the subsequent localization of CENPF, BUB1B, CENPE and MAD2L1. Required for the kinetochore localization of PLK1. Required for centromeric enrichment of AUKRB in prometaphase. Plays an important role in defining SGO1 localization and thereby affects sister chromatid cohesion. Promotes the centromeric localization of TOP2A (PubMed:35044816). Acts as a substrate for anaphase-promoting complex or cyclosome (APC/C) in complex with its activator CDH1 (APC/C-Cdh1). Necessary for ensuring proper chromosome segregation and binding to BUB3 is essential for this function. Can regulate chromosome segregation in a kinetochore-independent manner. Can phosphorylate BUB3. The BUB1-BUB3 complex plays a role in the inhibition of APC/C when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1. Kinase activity is essential for inhibition of APC/CCDC20 and for chromosome alignment but does not play a major role in the spindle-assembly checkpoint activity. Mediates cell death in response to chromosome missegregation and acts to suppress spontaneous tumorigenesis. {ECO:0000269|PubMed:10198256, ECO:0000269|PubMed:15020684, ECO:0000269|PubMed:15525512, ECO:0000269|PubMed:15723797, ECO:0000269|PubMed:16760428, ECO:0000269|PubMed:17158872, ECO:0000269|PubMed:19487456, ECO:0000269|PubMed:20739936, ECO:0000269|PubMed:35044816}.
|
Homo sapiens (Human)
|
O43684
|
BUB3_HUMAN
|
MTGSNEFKLNQPPEDGISSVKFSPNTSQFLLVSSWDTSVRLYDVPANSMRLKYQHTGAVLDCAFYDPTHAWSGGLDHQLKMHDLNTDQENLVGTHDAPIRCVEYCPEVNVMVTGSWDQTVKLWDPRTPCNAGTFSQPEKVYTLSVSGDRLIVGTAGRRVLVWDLRNMGYVQQRRESSLKYQTRCIRAFPNKQGYVLSSIEGRVAVEYLDPSPEVQKKKYAFKCHRLKENNIEQIYPVNAISFHNIHNTFATGGSDGFVNIWDPFNKKRLCQFHRYPTSIASLAFSNDGTTLAIASSYMYEMDDTEHPEDGIFIRQVTDAETKPKSPCT
| null | null |
attachment of spindle microtubules to kinetochore [GO:0008608]; cell division [GO:0051301]; meiotic cell cycle [GO:0051321]; mitotic spindle assembly checkpoint signaling [GO:0007094]; protein localization to kinetochore [GO:0034501]
|
bub1-bub3 complex [GO:1990298]; cytosol [GO:0005829]; kinetochore [GO:0000776]; mitotic checkpoint complex [GO:0033597]; nucleoplasm [GO:0005654]
|
ubiquitin binding [GO:0043130]
|
PF00400;
|
2.130.10.10;
|
WD repeat BUB3 family
|
PTM: Poly-ADP-ribosylated by PARP1. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Starts to localize at kinetochores in prometaphase I (Pro-MI) stage and maintains the localization until the metaphase I-anaphase I (MI-AI) transition. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Has a dual function in spindle-assembly checkpoint signaling and in promoting the establishment of correct kinetochore-microtubule (K-MT) attachments. Promotes the formation of stable end-on bipolar attachments. Necessary for kinetochore localization of BUB1. Regulates chromosome segregation during oocyte meiosis. The BUB1/BUB3 complex plays a role in the inhibition of anaphase-promoting complex or cyclosome (APC/C) when spindle-assembly checkpoint is activated and inhibits the ubiquitin ligase activity of APC/C by phosphorylating its activator CDC20. This complex can also phosphorylate MAD1L1. {ECO:0000269|PubMed:10198256, ECO:0000269|PubMed:15525512, ECO:0000269|PubMed:18199686}.
|
Homo sapiens (Human)
|
O43687
|
AKA7A_HUMAN
|
MGQLCCFPFSRDEGKISELESSSSAVLQRYSKDIPSWSSGEKNGGEPDDAELVRLSKRLVENAVLKAVQQYLEETQNKNKPGEGSSVKTEAADQNGNDNENNRK
| null | null |
action potential [GO:0001508]; cellular response to cAMP [GO:0071320]; intracellular signal transduction [GO:0035556]; monoatomic ion transport [GO:0006811]; positive regulation of delayed rectifier potassium channel activity [GO:1902261]; positive regulation of potassium ion transmembrane transport [GO:1901381]; protein localization [GO:0008104]; regulation of membrane repolarization [GO:0060306]
|
apical plasma membrane [GO:0016324]; lateral plasma membrane [GO:0016328]; plasma membrane [GO:0005886]
|
protein kinase A binding [GO:0051018]
|
PF10470;
| null | null | null |
SUBCELLULAR LOCATION: [Isoform Alpha]: Lateral cell membrane; Lipid-anchor. Note=Targeted predominantly to the lateral membrane.; SUBCELLULAR LOCATION: [Isoform Beta]: Apical cell membrane; Lipid-anchor. Note=Targeted predominantly to the apical membrane.
| null | null | null | null | null |
FUNCTION: Targets the cAMP-dependent protein kinase (PKA) to the plasma membrane, and permits functional coupling to the L-type calcium channel. The membrane-associated form reduces epithelial sodium channel (ENaC) activity, whereas the free cytoplasmic form may negatively regulate ENaC channel feedback inhibition by intracellular sodium. {ECO:0000269|PubMed:10613906, ECO:0000269|PubMed:17244820, ECO:0000269|PubMed:9545239}.
|
Homo sapiens (Human)
|
O43688
|
PLPP2_HUMAN
|
MQRRWVFVLLDVLCLLVASLPFAILTLVNAPYKRGFYCGDDSIRYPYRPDTITHGLMAGVTITATVILVSAGEAYLVYTDRLYSRSDFNNYVAAVYKVLGTFLFGAAVSQSLTDLAKYMIGRLRPNFLAVCDPDWSRVNCSVYVQLEKVCRGNPADVTEARLSFYSGHSSFGMYCMVFLALYVQARLCWKWARLLRPTVQFFLVAFALYVGYTRVSDYKHHWSDVLVGLLQGALVAALTVCYISDFFKARPPQHCLKEEELERKPSLSLTLTLGEADHNHYGYPHSSS
|
3.1.3.-; 3.1.3.4
| null |
ceramide metabolic process [GO:0006672]; phospholipid dephosphorylation [GO:0046839]; phospholipid metabolic process [GO:0006644]; signal transduction [GO:0007165]; sphingolipid catabolic process [GO:0030149]; sphingosine metabolic process [GO:0006670]
|
caveola [GO:0005901]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
ceramide-1-phosphate phosphatase activity [GO:0106235]; phosphatidate phosphatase activity [GO:0008195]; sphingosine-1-phosphate phosphatase activity [GO:0042392]
|
PF01569;
|
1.20.144.10;
|
PA-phosphatase related phosphoesterase family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:9705349}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16467304, ECO:0000269|PubMed:9705349}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:16467304, ECO:0000269|PubMed:9705349}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:16467304}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16467304}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377, ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4; Evidence={ECO:0000269|PubMed:16467304, ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430; Evidence={ECO:0000305|PubMed:9705349}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1,2-dihexadecanoyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:43236, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:72859, ChEBI:CHEBI:82929; Evidence={ECO:0000269|PubMed:9705349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43237; Evidence={ECO:0000305|PubMed:9705349}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1,2-di-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43244, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52333, ChEBI:CHEBI:74546; Evidence={ECO:0000269|PubMed:9607309}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43245; Evidence={ECO:0000305|PubMed:9607309}; CATALYTIC ACTIVITY: Reaction=H2O + monoacyl-sn-glycero-3-phosphate = a monoacylglycerol + phosphate; Xref=Rhea:RHEA:46736, ChEBI:CHEBI:15377, ChEBI:CHEBI:17408, ChEBI:CHEBI:43474, ChEBI:CHEBI:77589; Evidence={ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46737; Evidence={ECO:0000305|PubMed:9705349}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-sn-glycero-3-phosphate + H2O = (9Z-octadecenoyl)-glycerol + phosphate; Xref=Rhea:RHEA:50884, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:75937, ChEBI:CHEBI:84973; Evidence={ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50885; Evidence={ECO:0000305|PubMed:9705349}; CATALYTIC ACTIVITY: Reaction=H2O + sphing-4-enine 1-phosphate = phosphate + sphing-4-enine; Xref=Rhea:RHEA:27518, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57756, ChEBI:CHEBI:60119; Evidence={ECO:0000269|PubMed:9705349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27519; Evidence={ECO:0000305|PubMed:9705349}; CATALYTIC ACTIVITY: Reaction=an N-acylsphing-4-enine 1-phosphate + H2O = an N-acylsphing-4-enine + phosphate; Xref=Rhea:RHEA:33743, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52639, ChEBI:CHEBI:57674; Evidence={ECO:0000269|PubMed:9705349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33744; Evidence={ECO:0000305|PubMed:9705349}; CATALYTIC ACTIVITY: Reaction=H2O + N-(octanoyl)-sphing-4-enine-1-phosphate = N-octanoylsphing-4-enine + phosphate; Xref=Rhea:RHEA:62040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:45815, ChEBI:CHEBI:85376; Evidence={ECO:0000269|PubMed:9705349}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62041; Evidence={ECO:0000305|PubMed:9705349}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-ethanolamine phosphate = N-(9Z-octadecenoyl) ethanolamine + phosphate; Xref=Rhea:RHEA:62160, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:71466, ChEBI:CHEBI:145465; Evidence={ECO:0000269|PubMed:9607309}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62161; Evidence={ECO:0000305|PubMed:9607309};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=150 uM for 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate {ECO:0000269|PubMed:9607309}; KM=340 uM for (9Z)-octadecenoyl-sn-glycero-3-phosphate {ECO:0000269|PubMed:9607309}; KM=138 uM for N-oleoyl ethanolamine phosphatidic acid {ECO:0000269|PubMed:9607309}; Vmax=0.15 nmol/min/mg enzyme with 1,2-dihexadecanoyl-sn-glycero-3-phosphate as substrate {ECO:0000269|PubMed:9705349}; Vmax=0.2 nmol/min/mg enzyme with (9Z)-octadecenoyl-sn-glycero-3-phosphate as substrate {ECO:0000269|PubMed:9705349}; Vmax=0.17 nmol/min/mg enzyme with N-(octanoyl)-sphing-4-enine-1-phosphate as substrate {ECO:0000269|PubMed:9705349}; Vmax=0.69 nmol/min/mg enzyme with sphing-4-enine 1-phosphate as substrate {ECO:0000269|PubMed:9705349}; Vmax=34 nmol/min/mg enzyme with 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate as substrate {ECO:0000269|PubMed:9607309}; Vmax=49 nmol/min/mg enzyme with (9Z)-octadecenoyl-sn-glycero-3-phosphate as substrate {ECO:0000269|PubMed:9607309}; Vmax=17 nmol/min/mg enzyme with N-oleoyl ethanolamine phosphatidic acid as substrate {ECO:0000269|PubMed:9607309};
|
PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000269|PubMed:16467304, ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349}.
| null | null |
FUNCTION: Magnesium-independent phospholipid phosphatase that catalyzes the dephosphorylation of a variety of glycerolipid and sphingolipid phosphate esters including phosphatidate/PA, lysophosphatidate/LPA, sphingosine 1-phosphate/S1P and ceramide 1-phosphate/C1P (PubMed:16467304, PubMed:9607309, PubMed:9705349). Has no apparent extracellular phosphatase activity and therefore most probably acts intracellularly (PubMed:16467304). Also acts on N-oleoyl ethanolamine phosphate/N-(9Z-octadecenoyl)-ethanolamine phosphate, a potential physiological compound (PubMed:9607309). Through dephosphorylation of these bioactive lipid mediators produces new bioactive compounds and may regulate signal transduction in different cellular processes (Probable). Indirectly regulates, for instance, cell cycle G1/S phase transition through its phospholipid phosphatase activity (By similarity). {ECO:0000250|UniProtKB:Q8K593, ECO:0000269|PubMed:16467304, ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349, ECO:0000305|PubMed:16467304}.
|
Homo sapiens (Human)
|
O43699
|
SIGL6_HUMAN
|
MQGAQEASASEMLPLLLPLLWAGALAQERRFQLEGPESLTVQEGLCVLVPCRLPTTLPASYYGYGYWFLEGADVPVATNDPDEEVQEETRGRFHLLWDPRRKNCSLSIRDARRRDNAAYFFRLKSKWMKYGYTSSKLSVRVMALTHRPNISIPGTLESGHPSNLTCSVPWVCEQGTPPIFSWMSAAPTSLGPRTTQSSVLTITPRPQDHSTNLTCQVTFPGAGVTMERTIQLNVSYAPQKVAISIFQGNSAAFKILQNTSSLPVLEGQALRLLCDADGNPPAHLSWFQGFPALNATPISNTGVLELPQVGSAEEGDFTCRAQHPLGSLQISLSLFVHWKPEGRAGGVLGAVWGASITTLVFLCVCFIFRVKTRRKKAAQPVQNTDDVNPVMVSGSRGHQHQFQTGIVSDHPAEAGPISEDEQELHYAVLHFHKVQPQEPKVTDTEYSEIKIHK
| null | null |
cell adhesion [GO:0007155]; cell-cell signaling [GO:0007267]
|
cytosol [GO:0005829]; extracellular region [GO:0005576]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
carbohydrate binding [GO:0030246]; sialic acid binding [GO:0033691]
|
PF07679;PF00047;PF07686;
|
2.60.40.10;
|
Immunoglobulin superfamily, SIGLEC (sialic acid binding Ig-like lectin) family
| null |
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
| null | null | null | null | null |
FUNCTION: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.
|
Homo sapiens (Human)
|
O43704
|
ST1B1_HUMAN
|
MLSPKDILRKDLKLVHGYPMTCAFASNWEKIEQFHSRPDDIVIATYPKSGTTWVSEIIDMILNDGDIEKCKRGFITEKVPMLEMTLPGLRTSGIEQLEKNPSPRIVKTHLPTDLLPKSFWENNCKMIYLARNAKDVSVSYYHFDLMNNLQPFPGTWEEYLEKFLTGKVAYGSWFTHVKNWWKKKEEHPILFLYYEDMKENPKEEIKKIIRFLEKNLNDEILDRIIHHTSFEVMKDNPLVNYTHLPTTVMDHSKSPFMRKGTAGDWKNYFTVAQNEKFDAIYETEMSKTALQFRTEI
|
2.8.2.1
| null |
3'-phosphoadenosine 5'-phosphosulfate metabolic process [GO:0050427]; biogenic amine metabolic process [GO:0006576]; epithelial cell differentiation [GO:0030855]; ethanol catabolic process [GO:0006068]; flavonoid metabolic process [GO:0009812]; phenol-containing compound metabolic process [GO:0018958]; sulfation [GO:0051923]; thyroid hormone metabolic process [GO:0042403]; xenobiotic metabolic process [GO:0006805]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
aryl sulfotransferase activity [GO:0004062]; sulfotransferase activity [GO:0008146]
|
PF00685;
|
3.40.50.300;
|
Sulfotransferase 1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9443824, ECO:0000269|PubMed:9463486}.
|
CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate + H(+); Xref=Rhea:RHEA:12164, ChEBI:CHEBI:15378, ChEBI:CHEBI:33853, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:140317; EC=2.8.2.1; Evidence={ECO:0000269|PubMed:28084139, ECO:0000269|PubMed:9443824, ECO:0000269|PubMed:9463486}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12165; Evidence={ECO:0000305|PubMed:9443824}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + 3,3',5-triiodo-L-thyronine = 3,3',5-triiodo-L-thyronine sulfate + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:67876, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:176511, ChEBI:CHEBI:533015; Evidence={ECO:0000269|PubMed:9443824, ECO:0000269|PubMed:9463486}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67877; Evidence={ECO:0000305|PubMed:9463486}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + 3,3',5'-triiodo-L-thyronine = 3,3',5'-triiodo-L-thyronine sulfate + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:67888, ChEBI:CHEBI:15378, ChEBI:CHEBI:57261, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:176513; Evidence={ECO:0000269|PubMed:9463486}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67889; Evidence={ECO:0000305|PubMed:9463486}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + 3,3'-diiodo-L-thyronine = 3,3'-diiodo-L-thyronine sulfate + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:67892, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:176514, ChEBI:CHEBI:176515; Evidence={ECO:0000269|PubMed:9463486}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67893; Evidence={ECO:0000305|PubMed:9463486}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + dopamine = adenosine 3',5'-bisphosphate + dopamine 3-O-sulfate + H(+); Xref=Rhea:RHEA:67880, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:59905, ChEBI:CHEBI:133524; Evidence={ECO:0000269|PubMed:9443824}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67881; Evidence={ECO:0000305|PubMed:9443824}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + dopamine = adenosine 3',5'-bisphosphate + dopamine 4-O-sulfate + H(+); Xref=Rhea:RHEA:67884, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:59905, ChEBI:CHEBI:133529; Evidence={ECO:0000269|PubMed:9443824}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67885; Evidence={ECO:0000305|PubMed:9443824}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + 4-ethylphenol = 4-ethylphenyl sulfate + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:70607, ChEBI:CHEBI:15378, ChEBI:CHEBI:49584, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:133681; Evidence={ECO:0000269|PubMed:35165440}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70608; Evidence={ECO:0000305|PubMed:35165440};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=63.5 uM for 3,3',5-triiodo-L-thyronine (T3) {ECO:0000269|PubMed:9443824}; KM=7.2 uM for p-nitrophenol {ECO:0000269|PubMed:28084139}; KM=24.1 uM for p-nitrophenol {ECO:0000269|PubMed:9443824}; KM=1.4 uM for 1-naphtol {ECO:0000269|PubMed:28084139}; KM=141 uM for 3,3',5'-triiodo-L-thyronine (rT3) {ECO:0000269|PubMed:9463486}; KM=1.4 uM for 3,3'-diiodo-L-thyronine (T2) {ECO:0000269|PubMed:9463486}; KM=1.2 uM for PAPS {ECO:0000269|PubMed:9463486}; KM=1.3 uM for PAPS {ECO:0000269|PubMed:28084139}; KM=23 uM for thyroxine (T4) {ECO:0000269|PubMed:9463486}; Vmax=5.1 nmol/min/mg enzyme with p-nitrophenol as substrate {ECO:0000269|PubMed:28084139};
| null | null | null |
FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of dopamine, small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3'-diiodothyronine, triidothyronine (T3) and reverse triiodothyronine (rT3) (PubMed:28084139, PubMed:9443824, PubMed:9463486). May play a role in gut microbiota-host metabolic interaction. O-sulfonates 4-ethylphenol (4-EP), a dietary tyrosine-derived metabolite produced by gut bacteria. The product 4-EPS crosses the blood-brain barrier and may negatively regulate oligodendrocyte maturation and myelination, affecting the functional connectivity of different brain regions associated with the limbic system (PubMed:35165440). {ECO:0000269|PubMed:28084139, ECO:0000269|PubMed:35165440, ECO:0000269|PubMed:9443824, ECO:0000269|PubMed:9463486}.
|
Homo sapiens (Human)
|
O43707
|
ACTN4_HUMAN
|
MVDYHAANQSYQYGPSSAGNGAGGGGSMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYEKLASDLLEWIRRTIPWLEDRVPQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGKMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKHRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNTRCQKICDQWDALGSLTHSRREALEKTEKQLEAIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEEQSKQQSNEHLRRQFASQANVVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDVENDRQGEAEFNRIMSLVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGPDAVPGALDYKSFSTALYGESDL
| null | null |
actin cytoskeleton organization [GO:0030036]; muscle cell development [GO:0055001]; negative regulation of substrate adhesion-dependent cell spreading [GO:1900025]; peroxisome proliferator activated receptor signaling pathway [GO:0035357]; positive regulation of cell migration [GO:0030335]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of sodium:proton antiporter activity [GO:0032417]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein transport [GO:0015031]; regulation of apoptotic process [GO:0042981]; retinoic acid receptor signaling pathway [GO:0048384]; tumor necrosis factor-mediated signaling pathway [GO:0033209]; vesicle transport along actin filament [GO:0030050]
|
actin cytoskeleton [GO:0015629]; cell junction [GO:0030054]; cell projection [GO:0042995]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; platelet alpha granule lumen [GO:0031093]; protein-containing complex [GO:0032991]; pseudopodium [GO:0031143]; ribonucleoprotein complex [GO:1990904]; stress fiber [GO:0001725]; Z disc [GO:0030018]
|
actin binding [GO:0003779]; actin filament binding [GO:0051015]; calcium ion binding [GO:0005509]; chromatin DNA binding [GO:0031490]; integrin binding [GO:0005178]; nuclear receptor binding [GO:0016922]; nuclear receptor coactivator activity [GO:0030374]; nuclear retinoic acid receptor binding [GO:0042974]; nucleoside binding [GO:0001882]; protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; transcription coactivator activity [GO:0003713]; transmembrane transporter binding [GO:0044325]
|
PF00307;PF08726;PF00435;
|
1.20.58.60;1.10.418.10;1.10.238.10;
|
Alpha-actinin family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22351778, ECO:0000269|PubMed:9508771}. Cytoplasm {ECO:0000269|PubMed:22351778, ECO:0000269|PubMed:9508771}. Cell junction {ECO:0000250|UniProtKB:P57780}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:9508771}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P57780}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Expressed in the perinuclear rim and manchette structure in early elongating spermatids during spermiogenesis (By similarity). Nuclear translocation can be induced by the PI3 kinase inhibitor wortmannin or by cytochalasin D. Exclusively localized in the nucleus in a limited number of cell lines (breast cancer cell line MCF-7, oral floor cancer IMC-2, and bladder cancer KU-7). {ECO:0000250|UniProtKB:P57780, ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:9508771}.
| null | null | null | null | null |
FUNCTION: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (Probable). Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation (PubMed:15772161). Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions (By similarity). May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA (PubMed:22351778). {ECO:0000250|UniProtKB:P57780, ECO:0000269|PubMed:15772161, ECO:0000269|PubMed:22351778, ECO:0000305|PubMed:9508771}.
|
Homo sapiens (Human)
|
O43708
|
MAAI_HUMAN
|
MQAGKPILYSYFRSSCSWRVRIALALKGIDYKTVPINLIKDRGQQFSKDFQALNPMKQVPTLKIDGITIHQSLAIIEYLEEMRPTPRLLPQDPKKRASVRMISDLIAGGIQPLQNLSVLKQVGEEMQLTWAQNAITCGFNALEQILQSTAGIYCVGDEVTMADLCLVPQVANAERFKVDLTPYPTISSINKRLLVLEAFQVSHPCRQPDTPTELRA
|
2.5.1.18; 5.2.1.2
|
COFACTOR: Name=glutathione; Xref=ChEBI:CHEBI:57925; Note=Glutathione is required for the MAAI activity.;
|
glutathione metabolic process [GO:0006749]; L-phenylalanine catabolic process [GO:0006559]; tyrosine catabolic process [GO:0006572]
|
cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
|
glutathione peroxidase activity [GO:0004602]; glutathione transferase activity [GO:0004364]; identical protein binding [GO:0042802]; maleylacetoacetate isomerase activity [GO:0016034]; protein homodimerization activity [GO:0042803]
|
PF14497;PF13409;
|
1.20.1050.10;3.40.30.10;
|
GST superfamily, Zeta family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=4-maleylacetoacetate = 4-fumarylacetoacetate; Xref=Rhea:RHEA:14817, ChEBI:CHEBI:17105, ChEBI:CHEBI:18034; EC=5.2.1.2; Evidence={ECO:0000269|PubMed:10739172}; CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000269|PubMed:10739172};
| null |
PATHWAY: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 5/6.
| null | null |
FUNCTION: Bifunctional enzyme showing minimal glutathione-conjugating activity with ethacrynic acid and 7-chloro-4-nitrobenz-2-oxa-1,3-diazole and maleylacetoacetate isomerase activity. Has also low glutathione peroxidase activity with T-butyl and cumene hydroperoxides. Is able to catalyze the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid. {ECO:0000269|PubMed:10739172}.
|
Homo sapiens (Human)
|
O43709
|
BUD23_HUMAN
|
MASRGRRPEHGGPPELFYDETEARKYVRNSRMIDIQTRMAGRALELLYLPENKPCYLLDIGCGTGLSGSYLSDEGHYWVGLDISPAMLDEAVDREIEGDLLLGDMGQGIPFKPGTFDGCISISAVQWLCNANKKSENPAKRLYCFFASLFSVLVRGSRAVLQLYPENSEQLELITTQATKAGFSGGMVVDYPNSAKAKKFYLCLFSGPSTFIPEGLSENQDEVEPRESVFTNERFPLRMSRRGMVRKSRAWVLEKKERHRRQGREVRPDTQYTGRKRKPRF
|
2.1.1.-
| null |
chromatin organization [GO:0006325]; positive regulation of rRNA processing [GO:2000234]; rRNA (guanine-N7)-methylation [GO:0070476]
|
nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
|
methyltransferase activity [GO:0008168]; protein heterodimerization activity [GO:0046982]; RNA binding [GO:0003723]; rRNA (guanine) methyltransferase activity [GO:0016435]
|
PF08241;PF12589;
|
3.40.50.150;
|
Class I-like SAM-binding methyltransferase superfamily, BUD23/WBSCR22 family
|
PTM: May be ubiquitinated and targeted to degradation in response to pro-inflammatory cytokine signaling. {ECO:0000305}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24086612, ECO:0000269|PubMed:24488492, ECO:0000269|PubMed:34948388}. Nucleus, nucleoplasm {ECO:0000269|PubMed:25851604}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:25851604}. Cytoplasm {ECO:0000269|PubMed:24488492}. Note=Localized diffusely throughout the nucleus and the cytoplasm (PubMed:24488492). Localizes to a polarized perinuclear structure, overlapping partially with the Golgi and lysosomes (PubMed:25851604). Localization is not affected by glucocorticoid treatment (PubMed:24488492). {ECO:0000269|PubMed:24488492, ECO:0000269|PubMed:25851604}.
|
CATALYTIC ACTIVITY: Reaction=a guanosine in 18S rRNA + S-adenosyl-L-methionine = an N(7)-methylguanosine in 18S rRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54584, Rhea:RHEA-COMP:13937, Rhea:RHEA-COMP:13938, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, ChEBI:CHEBI:74480; Evidence={ECO:0000269|PubMed:25851604};
| null | null | null | null |
FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(7) position of a guanine in 18S rRNA (PubMed:25851604). Requires the methyltransferase adapter protein TRM112 for full rRNA methyltransferase activity (PubMed:25851604). Involved in the pre-rRNA processing steps leading to small-subunit rRNA production independently of its RNA-modifying catalytic activity (PubMed:25851604). Important for biogenesis end export of the 40S ribosomal subunit independent on its methyltransferase activity (PubMed:24086612). Locus-specific steroid receptor coactivator. Potentiates transactivation by glucocorticoid (NR3C1), mineralocorticoid (NR3C2), androgen (AR) and progesterone (PGR) receptors (PubMed:24488492). Required for the maintenance of open chromatin at the TSC22D3/GILZ locus to facilitate NR3C1 loading on the response elements (PubMed:24488492). Required for maintenance of dimethylation on histone H3 'Lys-79' (H3K79me2), although direct histone methyltransferase activity is not observed in vitro (PubMed:24488492). {ECO:0000250, ECO:0000269|PubMed:24086612, ECO:0000269|PubMed:24488492, ECO:0000269|PubMed:25851604}.
|
Homo sapiens (Human)
|
O43711
|
TLX3_HUMAN
|
MEAPASAQTPHPHEPISFGIDQILNSPDQDSAPAPRGPDGASYLGGPPGGRPGATYPSLPASFAGLGAPFEDAGSYSVNLSLAPAGVIRVPAHRPLPGAVPPPLPSALPAMPSVPTVSSLGGLNFPWMESSRRFVKDRFTAAAALTPFTVTRRIGHPYQNRTPPKRKKPRTSFSRVQICELEKRFHRQKYLASAERAALAKSLKMTDAQVKTWFQNRRTKWRRQTAEEREAERQQASRLMLQLQHDAFQKSLNDSIQPDPLCLHNSSLFALQNLQPWEEDSSKVPAVTSLV
| null | null |
animal organ development [GO:0048513]; central nervous system development [GO:0007417]; GABAergic neuron differentiation [GO:0097154]; negative regulation of neuron differentiation [GO:0045665]; neuron fate specification [GO:0048665]; neuron migration [GO:0001764]; regulation of respiratory gaseous exchange by nervous system process [GO:0002087]; regulation of transcription by RNA polymerase II [GO:0006357]; respiratory gaseous exchange by respiratory system [GO:0007585]
|
chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
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;
|
1.10.10.60;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null | null |
Homo sapiens (Human)
|
O43715
|
TRIA1_HUMAN
|
MNSVGEACTDMKREYDQCFNRWFAEKFLKGDSSGDPCTDLFKRYQQCVQKAIKEKEIPIEGLEFMGHGKEKPENSS
| null | null |
apoptotic process [GO:0006915]; cellular response to UV [GO:0034644]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:1902166]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; phospholipid translocation [GO:0045332]; phospholipid transport [GO:0015914]; positive regulation of phospholipid transport [GO:2001140]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of membrane lipid distribution [GO:0097035]
|
cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
|
p53 binding [GO:0002039]; phosphatidic acid transfer activity [GO:1990050]
|
PF05254;
| null |
TRIAP1/MDM35 family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15735003, ECO:0000269|PubMed:23931759}. Mitochondrion intermembrane space {ECO:0000269|PubMed:23931759}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphate(in) = a 1,2-diacyl-sn-glycero-3-phosphate(out); Xref=Rhea:RHEA:36435, ChEBI:CHEBI:58608; Evidence={ECO:0000269|PubMed:23931759};
| null | null | null | null |
FUNCTION: Involved in the modulation of the mitochondrial apoptotic pathway by ensuring the accumulation of cardiolipin (CL) in mitochondrial membranes. In vitro, the TRIAP1:PRELID1 complex mediates the transfer of phosphatidic acid (PA) between liposomes and probably functions as a PA transporter across the mitochondrion intermembrane space to provide PA for CL synthesis in the inner membrane (PubMed:23931759). Likewise, the TRIAP1:PRELID3A complex mediates the transfer of phosphatidic acid (PA) between liposomes (in vitro) and probably functions as a PA transporter across the mitochondrion intermembrane space (in vivo) (PubMed:26071602). Mediates cell survival by inhibiting activation of caspase-9 which prevents induction of apoptosis (PubMed:15735003). {ECO:0000269|PubMed:15735003, ECO:0000269|PubMed:23931759, ECO:0000269|PubMed:26071602}.
|
Homo sapiens (Human)
|
O43716
|
GATC_HUMAN
|
MWSRLVWLGLRAPLGGRQGFTSKADPQGSGRITAAVIEHLERLALVDFGSREAVARLEKAIAFADRLRAVDTDGVEPMESVLEDRCLYLRSDNVVEGNCADELLQNSHRVVEEYFVAPPGNISLPKLDEQEPFPHS
|
6.3.5.-
| null |
glutaminyl-tRNAGln biosynthesis via transamidation [GO:0070681]; mitochondrial translation [GO:0032543]; regulation of translational fidelity [GO:0006450]
|
glutamyl-tRNA(Gln) amidotransferase complex [GO:0030956]; mitochondrion [GO:0005739]
|
ATP binding [GO:0005524]; glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity [GO:0050567]
|
PF02686;
| null |
GatC family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03149, ECO:0000269|PubMed:19805282}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate; Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216; Evidence={ECO:0000255|HAMAP-Rule:MF_03149};
| null | null | null | null |
FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). {ECO:0000255|HAMAP-Rule:MF_03149, ECO:0000269|PubMed:19805282}.
|
Homo sapiens (Human)
|
O43719
|
HTSF1_HUMAN
|
MSGTNLDGNDEFDEQLRMQELYGDGKDGDTQTDAGGEPDSLGQQPTDTPYEWDLDKKAWFPKITEDFIATYQANYGFSNDGASSSTANVEDVHARTAEEPPQEKAPEPTDARKKGEKRKAESGWFHVEEDRNTNVYVSGLPPDITVDEFIQLMSKFGIIMRDPQTEEFKVKLYKDNQGNLKGDGLCCYLKRESVELALKLLDEDEIRGYKLHVEVAKFQLKGEYDASKKKKKCKDYKKKLSMQQKQLDWRPERRAGPSRMRHERVVIIKNMFHPMDFEDDPLVLNEIREDLRVECSKFGQIRKLLLFDRHPDGVASVSFRDPEEADYCIQTLDGRWFGGRQITAQAWDGTTDYQVEETSREREERLRGWEAFLNAPEANRGLRRSDSVSASERAGPSRARHFSEHPSTSKMNAQETATGMAFEEPIDEKKFEKTEDGGEFEEGASENNAKESSPEKEAEEGCPEKESEEGCPKRGFEGSCSQKESEEGNPVRGSEEDSPKKESKKKTLKNDCEENGLAKESEDDLNKESEEEVGPTKESEEDDSEKESDEDCSEKQSEDGSEREFEENGLEKDLDEEGSEKELHENVLDKELEENDSENSEFEDDGSEKVLDEEGSEREFDEDSDEKEEEEDTYEKVFDDESDEKEDEEYADEKGLEAADKKAEEGDADEKLFEESDDKEDEDADGKEVEDADEKLFEDDDSNEKLFDEEEDSSEKLFDDSDERGTLGGFGSVEEGPLSTGSSFILSSDDDDDDI
| null | null |
double-strand break repair via homologous recombination [GO:0000724]; mRNA splicing, via spliceosome [GO:0000398]; protein localization to site of double-strand break [GO:1990166]; U2-type prespliceosome assembly [GO:1903241]
|
nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of double-strand break [GO:0035861]; spliceosomal complex [GO:0005681]; U2 snRNP [GO:0005686]; U2-type spliceosomal complex [GO:0005684]
|
chromatin-protein adaptor activity [GO:0140463]; poly-ADP-D-ribose modification-dependent protein binding [GO:0160004]; RNA binding [GO:0003723]
|
PF00076;
|
3.30.70.330;
|
HTATSF1 family
|
PTM: Phosphorylation at Ser-748 by CK2 during S-phase in response to DNA damage promotes interaction with TOPBP1 and double-strand break (DSB) repair via homologous recombination. {ECO:0000269|PubMed:35597237}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15485897, ECO:0000269|PubMed:8849451}. Chromosome {ECO:0000269|PubMed:35597237}. Note=Recruited to DNA damage sites during S-phase following interaction with poly-ADP-ribosylated RPA1. {ECO:0000269|PubMed:35597237}.
| null | null | null | null | null |
FUNCTION: Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:30567737, PubMed:32494006, PubMed:34822310). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing (PubMed:30567737, PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, HTATSF1 is required to stabilize the branchpoint-interacting stem loop (PubMed:34822310). HTATSF1 is displaced from the 17S U2 SnRNP complex before the stable addition of the 17S U2 SnRNP complex to the spliceosome, destabilizing the branchpoint-interacting stem loop and allowing to probe intron branch site sequences (PubMed:32494006, PubMed:34822310). Also acts as a regulator of transcriptional elongation, possibly by mediating the reciprocal stimulatory effect of splicing on transcriptional elongation (PubMed:10454543, PubMed:10913173, PubMed:11780068). Involved in double-strand break (DSB) repair via homologous recombination in S-phase by promoting the recruitment of TOPBP1 to DNA damage sites (PubMed:35597237). Mechanistically, HTATSF1 is (1) recruited to DNA damage sites in S-phase via interaction with poly-ADP-ribosylated RPA1 and (2) phosphorylated by CK2, promoting recruitment of TOPBP1, thereby facilitating RAD51 nucleofilaments formation and RPA displacement, followed by homologous recombination (PubMed:35597237). {ECO:0000269|PubMed:10454543, ECO:0000269|PubMed:10913173, ECO:0000269|PubMed:11780068, ECO:0000269|PubMed:30567737, ECO:0000269|PubMed:32494006, ECO:0000269|PubMed:34822310, ECO:0000269|PubMed:35597237}.; FUNCTION: (Microbial infection) In case of infection by HIV-1, it is up-regulated by the HIV-1 proteins NEF and gp120, acts as a cofactor required for the Tat-enhanced transcription of the virus. {ECO:0000269|PubMed:10393184, ECO:0000269|PubMed:11420046, ECO:0000269|PubMed:15905670, ECO:0000269|PubMed:8849451, ECO:0000269|PubMed:9765201}.
|
Homo sapiens (Human)
|
O43731
|
ERD23_HUMAN
|
MNVFRILGDLSHLLAMILLLGKIWRSKCCKGISGKSQILFALVFTTRYLDLFTNFISIYNTVMKVVFLLCAYVTVYMIYGKFRKTFDSENDTFRLEFLLVPVIGLSFLENYSFTLLEILWTFSIYLESVAILPQLFMISKTGEAETITTHYLFFLGLYRALYLANWIRRYQTENFYDQIAVVSGVVQTIFYCDFFYLYVTKVLKGKKLSLPMPI
| null | null |
endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; protein retention in ER lumen [GO:0006621]; protein transport [GO:0015031]; retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum [GO:0006890]
|
cis-Golgi network [GO:0005801]; COPI-coated vesicle membrane [GO:0030663]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; transport vesicle [GO:0030133]
|
ER retention sequence binding [GO:0046923]; KDEL sequence binding [GO:0005046]
|
PF00810;
| null |
ERD2 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18086916}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5ZKX9}. Golgi apparatus membrane {ECO:0000269|PubMed:18086916}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5ZKX9}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000269|PubMed:18086916}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5ZKX9}. Note=Localized in the Golgi in the absence of bound proteins with the sequence motif K-D-E-L. Trafficks back to the endoplasmic reticulum together with cargo proteins containing the sequence motif K-D-E-L. {ECO:0000305|PubMed:18086916}.
| null | null | null | null | null |
FUNCTION: Receptor for the C-terminal sequence motif K-D-E-L that is present on endoplasmic reticulum resident proteins and that mediates their recycling from the Golgi back to the endoplasmic reticulum. {ECO:0000269|PubMed:18086916}.
|
Homo sapiens (Human)
|
O43734
|
CIKS_HUMAN
|
MPPQLQETRMNRSIPVEVDESEPYPSQLLKPIPEYSPEEESEPPAPNIRNMAPNSLSAPTMLHNSSGDFSQAHSTLKLANHQRPVSRQVTCLRTQVLEDSEDSFCRRHPGLGKAFPSGCSAVSEPASESVVGALPAEHQFSFMEKRNQWLVSQLSAASPDTGHDSDKSDQSLPNASADSLGGSQEMVQRPQPHRNRAGLDLPTIDTGYDSQPQDVLGIRQLERPLPLTSVCYPQDLPRPLRSREFPQFEPQRYPACAQMLPPNLSPHAPWNYHYHCPGSPDHQVPYGHDYPRAAYQQVIQPALPGQPLPGASVRGLHPVQKVILNYPSPWDHEERPAQRDCSFPGLPRHQDQPHHQPPNRAGAPGESLECPAELRPQVPQPPSPAAVPRPPSNPPARGTLKTSNLPEELRKVFITYSMDTAMEVVKFVNFLLVNGFQTAIDIFEDRIRGIDIIKWMERYLRDKTVMIIVAISPKYKQDVEGAESQLDEDEHGLHTKYIHRMMQIEFIKQGSMNFRFIPVLFPNAKKEHVPTWLQNTHVYSWPKNKKNILLRLLREEEYVAPPRGPLPTLQVVPL
|
2.3.2.27
| null |
B cell affinity maturation [GO:0002344]; B cell apoptotic process [GO:0001783]; B cell homeostasis [GO:0001782]; CD40 signaling pathway [GO:0023035]; eosinophil homeostasis [GO:1990959]; eosinophil mediated immunity [GO:0002447]; establishment of T cell polarity [GO:0001768]; heart development [GO:0007507]; humoral immune response [GO:0006959]; inflammatory response [GO:0006954]; interleukin-17-mediated signaling pathway [GO:0097400]; interleukin-17A-mediated signaling pathway [GO:0038173]; intracellular signal transduction [GO:0035556]; kidney development [GO:0001822]; leukocyte activation involved in inflammatory response [GO:0002269]; lymph node development [GO:0048535]; mRNA stabilization [GO:0048255]; mucus secretion [GO:0070254]; neutrophil activation [GO:0042119]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of defense response to virus by host [GO:0002230]; protein import into nucleus [GO:0006606]; protein K63-linked ubiquitination [GO:0070534]; protein localization to P-body [GO:0110012]; response to xenobiotic stimulus [GO:0009410]; signal transduction involved in regulation of gene expression [GO:0023019]; skin development [GO:0043588]; spleen development [GO:0048536]; T cell differentiation [GO:0030217]; T-helper 17 type immune response [GO:0072538]; transitional two stage B cell differentiation [GO:0002334]; tumor necrosis factor-mediated signaling pathway [GO:0033209]; type 2 immune response [GO:0042092]
|
cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; nucleus [GO:0005634]
|
signaling receptor binding [GO:0005102]; ubiquitin protein ligase activity [GO:0061630]
|
PF08357;
|
3.40.50.11530;
| null | null | null |
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; Evidence={ECO:0000269|PubMed:19825828};
| null | null | null | null |
FUNCTION: E3 ubiquitin ligase that catalyzes 'Lys-63'-linked polyubiquitination of target protein, enhancing protein-protein interaction and cell signaling (PubMed:19825828). Transfers ubiquitin from E2 ubiquitin-conjugating enzyme UBE2V1-UBE2N to substrate protein (PubMed:19825828). Essential adapter molecule in IL17A-mediated signaling (PubMed:19825828, PubMed:24120361). Upon IL17A stimulation, interacts with IL17RA and IL17RC receptor chains through SEFIR domains and catalyzes 'Lys-63'-linked polyubiquitination of TRAF6, leading to TRAF6-mediated activation of NF-kappa-B and MAPkinase pathways (PubMed:19825828). {ECO:0000269|PubMed:19825828, ECO:0000269|PubMed:24120361, ECO:0000269|PubMed:33723527}.
|
Homo sapiens (Human)
|
O43739
|
CYH3_HUMAN
|
MDEDGGGEGGGVPEDLSLEEREELLDIRRRKKELIDDIERLKYEIAEVMTEIDNLTSVEESKTTQRNKQIAMGRKKFNMDPKKGIQFLIENDLLQSSPEDVAQFLYKGEGLNKTVIGDYLGERDEFNIKVLQAFVELHEFADLNLVQALRQFLWSFRLPGEAQKIDRMMEAFASRYCLCNPGVFQSTDTCYVLSFAIIMLNTSLHNHNVRDKPTAERFIAMNRGINEGGDLPEELLRNLYESIKNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVEDPRKPNCFELYNPSHKGQVIKACKTEADGRVVEGNHVVYRISAPSPEEKEEWMKSIKASISRDPFYDMLATRKRRIANKK
| null | null |
establishment of epithelial cell polarity [GO:0090162]; Golgi vesicle transport [GO:0048193]; positive regulation of cell adhesion [GO:0045785]; regulation of ARF protein signal transduction [GO:0032012]
|
adherens junction [GO:0005912]; bicellular tight junction [GO:0005923]; cytosol [GO:0005829]; Golgi membrane [GO:0000139]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; ruffle [GO:0001726]
|
guanyl-nucleotide exchange factor activity [GO:0005085]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]
|
PF00169;PF01369;
|
1.10.220.20;1.10.1000.11;2.30.29.30;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane {ECO:0000250|UniProtKB:O08967}; Peripheral membrane protein {ECO:0000250|UniProtKB:O08967}. Cell junction, adherens junction {ECO:0000250|UniProtKB:O08967}. Cell junction, tight junction {ECO:0000250|UniProtKB:O08967}. Note=Translocates from the cytosol to membranes enriched in phosphatidylinositol 3,4,5-trisphosphate. {ECO:0000250|UniProtKB:O08967}.
| null | null | null | null | null |
FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF6. Promotes the activation of ARF factors through replacement of GDP with GTP. Plays a role in the epithelial polarization (By similarity). {ECO:0000250|UniProtKB:O08967, ECO:0000269|PubMed:23940353, ECO:0000269|PubMed:9707577}.
|
Homo sapiens (Human)
|
O43741
|
AAKB2_HUMAN
|
MGNTTSDRVSGERHGAKAARSEGAGGHAPGKEHKIMVGSTDDPSVFSLPDSKLPGDKEFVSWQQDLEDSVKPTQQARPTVIRWSEGGKEVFISGSFNNWSTKIPLIKSHNDFVAILDLPEGEHQYKFFVDGQWVHDPSEPVVTSQLGTINNLIHVKKSDFEVFDALKLDSMESSETSCRDLSSSPPGPYGQEMYAFRSEERFKSPPILPPHLLQVILNKDTNISCDPALLPEPNHVMLNHLYALSIKDSVMVLSATHRYKKKYVTTLLYKPI
| null | null |
cellular response to nutrient levels [GO:0031669]; fatty acid biosynthetic process [GO:0006633]; positive regulation of cold-induced thermogenesis [GO:0120162]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleotide-activated protein kinase complex [GO:0031588]; nucleus [GO:0005634]
|
protein kinase binding [GO:0019901]
|
PF16561;PF04739;
|
6.20.250.60;2.60.40.10;
|
5'-AMP-activated protein kinase beta subunit family
|
PTM: Phosphorylated when associated with the catalytic subunit (PRKAA1 or PRKAA2). Phosphorylated by ULK1 and ULK2; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1, ULK2 and AMPK. {ECO:0000269|PubMed:21460634}.
| null | null | null | null | null | null |
FUNCTION: Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).
|
Homo sapiens (Human)
|
O43745
|
CHP2_HUMAN
|
MGSRSSHAAVIPDGDSIRRETGFSQASLLRLHHRFRALDRNKKGYLSRMDLQQIGALAVNPLGDRIIESFFPDGSQRVDFPGFVRVLAHFRPVEDEDTETQDPKKPEPLNSRRNKLHYAFQLYDLDRDGKISRHEMLQVLRLMVGVQVTEEQLENIADRTVQEADEDGDGAVSFVEFTKSLEKMDVEQKMSIRILK
| null | null |
cellular response to calcium ion [GO:0071277]; positive regulation of calcineurin-NFAT signaling cascade [GO:0070886]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of phosphatase activity [GO:0010922]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein transport [GO:0015031]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]
|
PF13202;PF13499;
|
1.10.238.10;
|
Calcineurin regulatory subunit family, CHP subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21392185}. Cytoplasm {ECO:0000269|PubMed:21392185}. Cell membrane {ECO:0000269|PubMed:21392185}. Note=Predominantly localized in a juxtanuclear region. Colocalizes with SLC9A3 in the juxtanuclear region and at the plasma membrane (By similarity). Exported from the nucleus to the cytoplasm through a nuclear export signal (NES) pathway. May shuttle between nucleus and cytoplasm. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Functions as an integral cofactor in cell pH regulation by controlling plasma membrane-type Na(+)/H(+) exchange activity. Binds to and activates SLC9A1/NHE1 in a serum-independent manner, thus increasing pH and protecting cells from serum deprivation-induced death. Also plays a role in the regulation of cell proliferation and tumor growth by increasing the phosphatase activity of PPP3CA in a calcium-dependent manner. Activator of the calcineurin/NFAT signaling pathway. Involved in the cytoplasmic translocation of the transcription factor NFATC3 to the nucleus. {ECO:0000269|PubMed:12226101, ECO:0000269|PubMed:18815128}.
|
Homo sapiens (Human)
|
O43747
|
AP1G1_HUMAN
|
MPAPIRLRELIRTIRTARTQAEEREMIQKECAAIRSSFREEDNTYRCRNVAKLLYMHMLGYPAHFGQLECLKLIASQKFTDKRIGYLGAMLLLDERQDVHLLMTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALCAVHVIRKVPELMEMFLPATKNLLNEKNHGVLHTSVVLLTEMCERSPDMLAHFRKLVPQLVRILKNLIMSGYSPEHDVSGISDPFLQVRILRLLRILGRNDDDSSEAMNDILAQVATNTETSKNVGNAILYETVLTIMDIKSESGLRVLAINILGRFLLNNDKNIRYVALTSLLKTVQTDHNAVQRHRSTIVDCLKDLDVSIKRRAMELSFALVNGNNIRGMMKELLYFLDSCEPEFKADCASGIFLAAEKYAPSKRWHIDTIMRVLTTAGSYVRDDAVPNLIQLITNSVEMHAYTVQRLYKAILGDYSQQPLVQVAAWCIGEYGDLLVSGQCEEEEPIQVTEDEVLDILESVLISNMSTSVTRGYALTAIMKLSTRFTCTVNRIKKVVSIYGSSIDVELQQRAVEYNALFKKYDHMRSALLERMPVMEKVTTNGPTEIVQTNGETEPAPLETKPPPSGPQPTSQANDLLDLLGGNDITPVIPTAPTSKPSSAGGELLDLLGDINLTGAPAAAPAPASVPQISQPPFLLDGLSSQPLFNDIAAGIPSITAYSKNGLKIEFTFERSNTNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSIVPAFNTGTITQVIKVLNPQKQQLRMRIKLTYNHKGSAMQDLAEVNNFPPQSWQ
| null | null |
basolateral protein secretion [GO:0110010]; endosome to melanosome transport [GO:0035646]; Golgi to lysosome transport [GO:0090160]; Golgi to vacuole transport [GO:0006896]; intracellular protein transport [GO:0006886]; melanosome assembly [GO:1903232]; melanosome organization [GO:0032438]; platelet dense granule organization [GO:0060155]; positive regulation of natural killer cell degranulation [GO:0043323]; positive regulation of natural killer cell mediated cytotoxicity [GO:0045954]; synaptic vesicle budding from endosome [GO:0016182]; synaptic vesicle endocytosis [GO:0048488]; vesicle-mediated transport [GO:0016192]
|
AP-1 adaptor complex [GO:0030121]; clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; clathrin-coated vesicle membrane [GO:0030665]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; early endosome [GO:0005769]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; presynapse [GO:0098793]; recycling endosome [GO:0055037]; trans-Golgi network membrane [GO:0032588]
|
clathrin adaptor activity [GO:0035615]; collagen binding [GO:0005518]; GTP-dependent protein binding [GO:0030742]; kinesin binding [GO:0019894]; small GTPase binding [GO:0031267]
|
PF01602;PF02883;
|
2.60.40.1230;1.25.10.10;
|
Adaptor complexes large subunit family
| null |
SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:12773381}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:12773381}; Peripheral membrane protein {ECO:0000269|PubMed:12773381}; Cytoplasmic side {ECO:0000269|PubMed:12773381}. Cytoplasm {ECO:0000269|PubMed:15758025}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15758025, ECO:0000269|PubMed:34102099}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:15758025}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:34102099}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex (PubMed:12773381). Co-localizes with AFTPH/aftiphilin in the cytoplasm (PubMed:15758025). {ECO:0000269|PubMed:12773381, ECO:0000269|PubMed:15758025}.
| null | null | null | null | null |
FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. In association with AFTPH/aftiphilin in the aftiphilin/p200/gamma-synergin complex, involved in the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes (PubMed:15758025). {ECO:0000269|PubMed:15758025, ECO:0000269|PubMed:34102099}.
|
Homo sapiens (Human)
|
O43749
|
OR1F1_HUMAN
|
MSGTNQSSVSEFLLLGLSRQPQQQHLLFVFFLSMYLATVLGNLLIILSVSIDSCLHTPMYFFLSNLSFVDICFSFTTVPKMLANHILETQTISFCGCLTQMYFVFMFVDMDNFLLAVMAYDHFVAVCHPLHYTAKMTHQLCALLVAGLWVVANLNVLLHTLLMAPLSFCADNAITHFFCDVTPLLKLSCSDTHLNEVIILSEGALVMITPFLCILASYMHITCTVLKVPSTKGRWKAFSTCGSHLAVVLLFYSTIIAVYFNPLSSHSAEKDTMATVLYTVVTPMLNPFIYSLRNRYLKGALKKVVGRVVFSV
| null | null |
signal transduction [GO:0007165]
|
plasma membrane [GO:0005886]
|
G protein-coupled receptor activity [GO:0004930]; olfactory receptor activity [GO:0004984]
|
PF13853;
|
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: Odorant receptor. {ECO:0000305}.
|
Homo sapiens (Human)
|
O43752
|
STX6_HUMAN
|
MSMEDPFFVVKGEVQKAVNTAQGLFQRWTELLQDPSTATREEIDWTTNELRNNLRSIEWDLEDLDETISIVEANPRKFNLDATELSIRKAFITSTRQVVRDMKDQMSTSSVQALAERKNRQALLGDSGSQNWSTGTTDKYGRLDRELQRANSHFIEEQQAQQQLIVEQQDEQLELVSGSIGVLKNMSQRIGGELEEQAVMLEDFSHELESTQSRLDNVMKKLAKVSHMTSDRRQWCAIAILFAVLLVVLILFLVL
| null | null |
endocytic recycling [GO:0032456]; Golgi vesicle transport [GO:0048193]; intracellular protein transport [GO:0006886]; regulation of protein localization [GO:0032880]; retrograde transport, endosome to Golgi [GO:0042147]; synaptic vesicle to endosome fusion [GO:0016189]; vesicle docking [GO:0048278]; vesicle fusion [GO:0006906]
|
clathrin-coated vesicle [GO:0030136]; cytosol [GO:0005829]; early endosome [GO:0005769]; endomembrane system [GO:0012505]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; SNARE complex [GO:0031201]; synaptic vesicle membrane [GO:0030672]; trans-Golgi network [GO:0005802]; trans-Golgi network membrane [GO:0032588]
|
SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]; syntaxin binding [GO:0019905]
|
PF05739;PF09177;
|
1.20.5.110;1.20.58.90;
|
Syntaxin family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:23818989}; Single-pass type IV membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q63635}; Single-pass type IV membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q63635}; Single-pass type IV membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: SNARE promoting movement of transport vesicles to target membranes. Targets endosomes to the trans-Golgi network, and may therefore function in retrograde trafficking. Together with SNARE STX12, promotes movement of vesicles from endosomes to the cell membrane, and may therefore function in the endocytic recycling pathway. {ECO:0000250|UniProtKB:Q63635}.
|
Homo sapiens (Human)
|
O43759
|
SNG1_HUMAN
|
MEGGAYGAGKAGGAFDPYTLVRQPHTILRVVSWLFSIVVFGSIVNEGYLNSASEGEEFCIYNRNPNACSYGVAVGVLAFLTCLLYLALDVYFPQISSVKDRKKAVLSDIGVSAFWAFLWFVGFCYLANQWQVSKPKDNPLNEGTDAARAAIAFSFFSIFTWAGQAVLAFQRYQIGADSALFSQDYMDPSQDSSMPYAPYVEPTGPDPAGMGGTYQQPANTFDTEPQGYQSQGY
| null | null |
cellular response to leukemia inhibitory factor [GO:1990830]; protein targeting [GO:0006605]; regulated exocytosis [GO:0045055]; regulation of long-term neuronal synaptic plasticity [GO:0048169]; regulation of short-term neuronal synaptic plasticity [GO:0048172]; synaptic vesicle membrane organization [GO:0048499]
|
azurophil granule membrane [GO:0035577]; melanosome [GO:0042470]; membrane [GO:0016020]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; synaptic vesicle membrane [GO:0030672]
| null |
PF01284;
| null |
Synaptogyrin family
| null |
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q62876}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q62876}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000269|PubMed:17081065}.
| null | null | null | null | null |
FUNCTION: May play a role in regulated exocytosis. Modulates the localization of synaptophysin/SYP into synaptic-like microvesicles and may therefore play a role in synaptic-like microvesicle formation and/or maturation (By similarity). Involved in the regulation of short-term and long-term synaptic plasticity (By similarity). {ECO:0000250|UniProtKB:O55100, ECO:0000250|UniProtKB:Q62876}.
|
Homo sapiens (Human)
|
O43760
|
SNG2_HUMAN
|
MESGAYGAAKAGGSFDLRRFLTQPQVVARAVCLVFALIVFSCIYGEGYSNAHESKQMYCVFNRNEDACRYGSAIGVLAFLASAFFLVVDAYFPQISNATDRKYLVIGDLLFSALWTFLWFVGFCFLTNQWAVTNPKDVLVGADSVRAAITFSFFSIFSWGVLASLAYQRYKAGVDDFIQNYVDPTPDPNTAYASYPGASVDNYQQPPFTQNAETTEGYQPPPVY
| null | null |
regulated exocytosis [GO:0045055]; synaptic vesicle membrane organization [GO:0048499]
|
extracellular exosome [GO:0070062]; lipid droplet [GO:0005811]; membrane [GO:0016020]; neuromuscular junction [GO:0031594]; synaptic vesicle membrane [GO:0030672]
| null |
PF01284;
| null |
Synaptogyrin family
|
PTM: May be tyrosine phosphorylated by Src. {ECO:0000250|UniProtKB:O54980}.
|
SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:O54980}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:O54980}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to cytoplasmic vesicles associated with the recycling endosomes. {ECO:0000250|UniProtKB:O54980}.; SUBCELLULAR LOCATION: Lipid droplet. Note=(Microbial infection) Upon SFTS phlebovirus infection, the protein localizes in lipid droplets and inclusion bodies. {ECO:0000269|PubMed:27226560}.
| null | null | null | null | null |
FUNCTION: May play a role in regulated exocytosis. In neuronal cells, modulates the localization of synaptophysin/SYP into synaptic-like microvesicles and may therefore play a role in the formation and/or the maturation of this vesicles. May also play a role in GLUT4 storage and transport to the plasma membrane. {ECO:0000250|UniProtKB:O54980}.; FUNCTION: (Microbial infection) May play a role in the assembly of cytoplasmic inclusion bodies required for SFTS phlebovirus replication. {ECO:0000269|PubMed:27226560}.
|
Homo sapiens (Human)
|
O43761
|
SNG3_HUMAN
|
MEGASFGAGRAGAALDPVSFARRPQTLLRVASWVFSIAVFGPIVNEGYVNTDSGPELRCVFNGNAGACRFGVALGLGAFLACAAFLLLDVRFQQISSVRDRRRAVLLDLGFSGLWSFLWFVGFCFLTNQWQRTAPGPATTQAGDAARAAIAFSFFSILSWVALTVKALQRFRLGTDMSLFATEQLSTGASQAYPGYPVGSGVEGTETYQSPPFTETLDTSPKGYQVPAY
| null | null |
positive regulation of transporter activity [GO:0032411]; regulated exocytosis [GO:0045055]; regulation of neurotransmitter uptake [GO:0051580]; substantia nigra development [GO:0021762]
|
membrane [GO:0016020]; neuromuscular junction [GO:0031594]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]
|
SH2 domain binding [GO:0042169]
|
PF01284;
| null |
Synaptogyrin family
| null |
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q8R191}; Multi-pass membrane protein {ECO:0000255}. Synapse {ECO:0000250|UniProtKB:Q8R191}. Note=Found at the neuromuscular synapses. {ECO:0000250|UniProtKB:Q8R191}.
| null | null | null | null | null |
FUNCTION: May play a role in regulated exocytosis. May indirectly regulate the activity of the plasma membrane dopamine transporter SLC6A3 and thereby regulate dopamine transport back from the synaptic cleft into the presynaptic terminal. {ECO:0000250|UniProtKB:Q8R191}.
|
Homo sapiens (Human)
|
O43763
|
TLX2_HUMAN
|
MEPGMLGPHNLPHHEPISFGIDQILSGPETPGGGLGLGRGGQGHGENGAFSGGYHGASGYGPAGSLAPLPGSSGVGPGGVIRVPAHRPLPVPPPAGGAPAVPGPSGLGGAGGLAGLTFPWMDSGRRFAKDRLTAALSPFSGTRRIGHPYQNRTPPKRKKPRTSFSRSQVLELERRFLRQKYLASAERAALAKALRMTDAQVKTWFQNRRTKWRRQTAEEREAERHRAGRLLLHLQQDALPRPLRPPLPPDPLCLHNSSLFALQNLQPWAEDNKVASVSGLASVV
| null | null |
animal organ development [GO:0048513]; enteric nervous system development [GO:0048484]; mesoderm formation [GO:0001707]; negative regulation of dendrite morphogenesis [GO:0050774]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; 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 DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00046;
|
1.10.10.60;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Transcription activator that binds DNA elements with the consensus sequence 5'-CGGTAATTGG-3'. Binds DNA via its homeobox. Required for normal cell death of enteric neurons in the gastrointestinal tract. Required for normal development of the enteric nervous system, and for proper development of normal motility of the gastrointestinal tract (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O43765
|
SGTA_HUMAN
|
MDNKKRLAYAIIQFLHDQLRHGGLSSDAQESLEVAIQCLETAFGVTVEDSDLALPQTLPEIFEAAATGKEMPQDLRSPARTPPSEEDSAEAERLKTEGNEQMKVENFEAAVHFYGKAIELNPANAVYFCNRAAAYSKLGNYAGAVQDCERAICIDPAYSKAYGRMGLALSSLNKHVEAVAYYKKALELDPDNETYKSNLKIAELKLREAPSPTGGVGSFDIAGLLNNPGFMSMASNLMNNPQIQQLMSGMISGGNNPLGTPGTSPSQNDLASLIQAGQQFAQQMQQQNPELIEQLRSQIRSRTPSASNDDQQE
| null | null |
ERAD pathway [GO:0036503]; negative regulation of ERAD pathway [GO:1904293]; negative regulation of ubiquitin-dependent protein catabolic process [GO:2000059]; positive regulation of ERAD pathway [GO:1904294]; positive regulation of ubiquitin-dependent protein catabolic process [GO:2000060]; post-translational protein targeting to endoplasmic reticulum membrane [GO:0006620]; tail-anchored membrane protein insertion into ER membrane [GO:0071816]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]; TRC complex [GO:0072380]
|
BAT3 complex binding [GO:1904288]; identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090]; protein self-association [GO:0043621]
|
PF16546;PF00515;PF13181;
|
1.20.5.420;1.25.40.10;
|
SGT family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16580629}. Nucleus {ECO:0000269|PubMed:16580629}. Note=Co-localizes with HSP90AB1 in the cytoplasm. Increased nuclear accumulation seen during cell apoptosis. {ECO:0000269|PubMed:16580629}.
| null | null | null | null | null |
FUNCTION: Co-chaperone that binds misfolded and hydrophobic patches-containing client proteins in the cytosol. Mediates their targeting to the endoplasmic reticulum but also regulates their sorting to the proteasome when targeting fails (PubMed:28104892). Functions in tail-anchored/type II transmembrane proteins membrane insertion constituting with ASNA1 and the BAG6 complex a targeting module (PubMed:28104892). Functions upstream of the BAG6 complex and ASNA1, binding more rapidly the transmembrane domain of newly synthesized proteins (PubMed:25535373, PubMed:28104892). It is also involved in the regulation of the endoplasmic reticulum-associated misfolded protein catabolic process via its interaction with BAG6: collaborates with the BAG6 complex to maintain hydrophobic substrates in non-ubiquitinated states (PubMed:23129660, PubMed:25179605). Competes with RNF126 for interaction with BAG6, preventing the ubiquitination of client proteins associated with the BAG6 complex (PubMed:27193484). Binds directly to HSC70 and HSP70 and regulates their ATPase activity (PubMed:18759457). {ECO:0000269|PubMed:18759457, ECO:0000269|PubMed:23129660, ECO:0000269|PubMed:25179605, ECO:0000269|PubMed:25535373, ECO:0000269|PubMed:27193484, ECO:0000269|PubMed:28104892}.; FUNCTION: (Microbial infection) In case of infection by polyomavirus, involved in the virus endoplasmic reticulum membrane penetration and infection via interaction with DNAJB12, DNAJB14 and HSPA8/Hsc70 (PubMed:24675744). {ECO:0000269|PubMed:24675744}.
|
Homo sapiens (Human)
|
O43766
|
LIAS_HUMAN
|
MSLRCGDAARTLGPRVFGRYFCSPVRPLSSLPDKKKELLQNGPDLQDFVSGDLADRSTWDEYKGNLKRQKGERLRLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGEYATATATIMLMGDTCTRGCRFCSVKTARNPPPLDASEPYNTAKAIAEWGLDYVVLTSVDRDDMPDGGAEHIAKTVSYLKERNPKILVECLTPDFRGDLKAIEKVALSGLDVYAHNVETVPELQSKVRDPRANFDQSLRVLKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCLTLGQYMQPTRRHLKVEEYITPEKFKYWEKVGNELGFHYTASGPLVRSSYKAGEFFLKNLVAKRKTKDL
|
2.8.1.8
|
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|HAMAP-Rule:MF_03123}; Note=Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000255|HAMAP-Rule:MF_03123};
|
inflammatory response [GO:0006954]; lipoate biosynthetic process [GO:0009107]; neural tube closure [GO:0001843]; response to lipopolysaccharide [GO:0032496]; response to oxidative stress [GO:0006979]
|
mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
|
4 iron, 4 sulfur cluster binding [GO:0051539]; lipoate synthase activity [GO:0016992]; metal ion binding [GO:0046872]
|
PF16881;PF04055;
|
3.20.20.70;
|
Radical SAM superfamily, Lipoyl synthase family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03123}.
|
CATALYTIC ACTIVITY: Reaction=[[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-methionine + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:16585, Rhea:RHEA-COMP:9928, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:14568, Rhea:RHEA-COMP:14569, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:29034, ChEBI:CHEBI:29919, ChEBI:CHEBI:33722, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:78809, ChEBI:CHEBI:83100; EC=2.8.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_03123};
| null |
PATHWAY: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2. {ECO:0000255|HAMAP-Rule:MF_03123}.
| null | null |
FUNCTION: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. {ECO:0000255|HAMAP-Rule:MF_03123}.
|
Homo sapiens (Human)
|
O43768
|
ENSA_HUMAN
|
MSQKQEEENPAEETGEEKQDTQEKEGILPERAEEAKLKAKYPSLGQKPGGSDFLMKRLQKGQKYFDSGDYNMAKAKMKNKQLPSAGPDKNLVTGDHIPTPQDLPQRKSSLVTSKLAGGQVE
| null | null |
cell division [GO:0051301]; G2/M transition of mitotic cell cycle [GO:0000086]; mitotic cell cycle [GO:0000278]; negative regulation of protein dephosphorylation [GO:0035308]; regulation of insulin secretion [GO:0050796]; response to nutrient [GO:0007584]
|
cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]
|
ion channel inhibitor activity [GO:0008200]; phosphatase inhibitor activity [GO:0019212]; potassium channel inhibitor activity [GO:0019870]; protein phosphatase 2A binding [GO:0051721]; protein phosphatase inhibitor activity [GO:0004864]; protein phosphatase regulator activity [GO:0019888]; signaling receptor binding [GO:0005102]
|
PF04667;
| null |
Endosulfine family
|
PTM: Phosphorylation at Ser-67 by GWL during mitosis is essential for interaction with PPP2R2D (PR55-delta) and subsequent inactivation of PP2A (By similarity). Phosphorylated by PKA. {ECO:0000250, ECO:0000269|PubMed:18973346, ECO:0000269|PubMed:9653196}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-67 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase (By similarity). Also acts as a stimulator of insulin secretion by interacting with sulfonylurea receptor (ABCC8), thereby preventing sulfonylurea from binding to its receptor and reducing K(ATP) channel currents. {ECO:0000250, ECO:0000269|PubMed:9653196}.
|
Homo sapiens (Human)
|
O43772
|
MCAT_HUMAN
|
MADQPKPISPLKNLLAGGFGGVCLVFVGHPLDTVKVRLQTQPPSLPGQPPMYSGTFDCFRKTLFREGITGLYRGMAAPIIGVTPMFAVCFFGFGLGKKLQQKHPEDVLSYPQLFAAGMLSGVFTTGIMTPGERIKCLLQIQASSGESKYTGTLDCAKKLYQEFGIRGIYKGTVLTLMRDVPASGMYFMTYEWLKNIFTPEGKRVSELSAPRILVAGGIAGIFNWAVAIPPDVLKSRFQTAPPGKYPNGFRDVLRELIRDEGVTSLYKGFNAVMIRAFPANAACFLGFEVAMKFLNWATPNL
| null | null |
carnitine shuttle [GO:0006853]; carnitine transmembrane transport [GO:1902603]; in utero embryonic development [GO:0001701]; mitochondrial transport [GO:0006839]
|
cytosol [GO:0005829]; mitochondrial envelope [GO:0005740]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]
|
acyl carnitine transmembrane transporter activity [GO:0015227]
|
PF00153;
|
1.50.40.10;
|
Mitochondrial carrier (TC 2.A.29) family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein.
|
CATALYTIC ACTIVITY: Reaction=(R)-carnitine(out) + O-acetyl-(R)-carnitine(in) = (R)-carnitine(in) + O-acetyl-(R)-carnitine(out); Xref=Rhea:RHEA:49908, ChEBI:CHEBI:16347, ChEBI:CHEBI:57589; Evidence={ECO:0000269|PubMed:12892634, ECO:0000269|PubMed:18307102}; CATALYTIC ACTIVITY: Reaction=(R)-carnitine(out) + O-acyl-(R)-carnitine(in) = (R)-carnitine(in) + O-acyl-(R)-carnitine(out); Xref=Rhea:RHEA:49924, ChEBI:CHEBI:16347, ChEBI:CHEBI:75659; Evidence={ECO:0000305|PubMed:12892634, ECO:0000305|PubMed:18307102, ECO:0000305|PubMed:20347717}; CATALYTIC ACTIVITY: Reaction=(R)-carnitine(out) + O-propanoyl-(R)-carnitine(in) = (R)-carnitine(in) + O-propanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:49912, ChEBI:CHEBI:16347, ChEBI:CHEBI:53210; Evidence={ECO:0000250|UniProtKB:P97521}; CATALYTIC ACTIVITY: Reaction=(R)-carnitine(out) + O-hexadecanoyl-(R)-carnitine(in) = (R)-carnitine(in) + O-hexadecanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:49916, ChEBI:CHEBI:16347, ChEBI:CHEBI:17490; Evidence={ECO:0000250|UniProtKB:P97521}; CATALYTIC ACTIVITY: Reaction=(R)-carnitine(out) + O-octanoyl-(R)-carnitine(in) = (R)-carnitine(in) + O-octanoyl-(R)-carnitine(out); Xref=Rhea:RHEA:49920, ChEBI:CHEBI:16347, ChEBI:CHEBI:18102; Evidence={ECO:0000250|UniProtKB:P97521}; CATALYTIC ACTIVITY: Reaction=(R)-carnitine(in) = (R)-carnitine(out); Xref=Rhea:RHEA:34959, ChEBI:CHEBI:16347; Evidence={ECO:0000269|PubMed:18307102};
| null | null | null | null |
FUNCTION: Mediates the electroneutral exchange of acylcarnitines (O-acyl-(R)-carnitine or L-acylcarnitine) of different acyl chain lengths (ranging from O-acetyl-(R)-carnitine to long-chain O-acyl-(R)-carnitines) with free carnitine ((R)-carnitine or L-carnitine) across the mitochondrial inner membrane, via a ping-pong mechanism (Probable) (PubMed:12892634, PubMed:18307102). Key player in the mitochondrial oxidation pathway, it translocates the fatty acids in the form of acylcarnitines into the mitochondrial matrix, where the carnitine palmitoyltransferase 2 (CPT-2) activates them to undergo fatty acid beta-oxidation (Probable). Catalyzes the unidirectional transport (uniport) of carnitine at lower rates than the antiport (exchange) (PubMed:18307102). {ECO:0000269|PubMed:12892634, ECO:0000269|PubMed:18307102, ECO:0000305|PubMed:18307102, ECO:0000305|PubMed:20347717}.
|
Homo sapiens (Human)
|
O43776
|
SYNC_HUMAN
|
MVLAELYVSDREGSDATGDGTKEKPFKTGLKALMTVGKEPFPTIYVDSQKENERWNVISKSQLKNIKKMWHREQMKSESREKKEAEDSLRREKNLEEAKKITIKNDPSLPEPKCVKIGALEGYRGQRVKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVLADELCQCYNGVLLSTESSVAVYGMLNLTPKGKQAPGGHELSCDFWELIGLAPAGGADNLINEESDVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFDDLLNRLEDLVCDVVDRILKSPAGSIVHELNPNFQPPKRPFKRMNYSDAIVWLKEHDVKKEDGTFYEFGEDIPEAPERLMTDTINEPILLCRFPVEIKSFYMQRCPEDSRLTESVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGIDPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRFVQRCTP
|
6.1.1.22
| null |
asparaginyl-tRNA aminoacylation [GO:0006421]; cell migration [GO:0016477]; cerebral cortex development [GO:0021987]; tRNA aminoacylation for protein translation [GO:0006418]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]
|
asparagine-tRNA ligase activity [GO:0004816]; ATP binding [GO:0005524]; CCR3 chemokine receptor binding [GO:0031728]; nucleic acid binding [GO:0003676]; protein dimerization activity [GO:0046983]
|
PF20917;PF00152;PF01336;
|
3.30.1910.20;2.40.50.140;
|
Class-II aminoacyl-tRNA synthetase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:9421509}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-asparaginyl-tRNA(Asn); Xref=Rhea:RHEA:11180, Rhea:RHEA-COMP:9659, Rhea:RHEA-COMP:9674, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:78442, ChEBI:CHEBI:78515, ChEBI:CHEBI:456215; EC=6.1.1.22; Evidence={ECO:0000269|PubMed:32738225, ECO:0000269|PubMed:32788587, ECO:0000269|PubMed:9421509};
| null | null | null | null |
FUNCTION: Catalyzes the attachment of asparagine to tRNA(Asn) in a two-step reaction: asparagine is first activated by ATP to form Asn-AMP and then transferred to the acceptor end of tRNA(Asn) (PubMed:32738225, PubMed:32788587, PubMed:9421509). In addition to its essential role in protein synthesis, acts as a signaling molecule that induced migration of CCR3-expressing cells (PubMed:12235211, PubMed:30171954). Has an essential role in the development of the cerebral cortex, being required for proper proliferation of radial glial cells (PubMed:32788587). {ECO:0000269|PubMed:12235211, ECO:0000269|PubMed:30171954, ECO:0000269|PubMed:32738225, ECO:0000269|PubMed:32788587, ECO:0000269|PubMed:9421509}.
|
Homo sapiens (Human)
|
O43781
|
DYRK3_HUMAN
|
MGGTARGPGRKDAGPPGAGLPPQQRRLGDGVYDTFMMIDETKCPPCSNVLCNPSEPPPPRRLNMTTEQFTGDHTQHFLDGGEMKVEQLFQEFGNRKSNTIQSDGISDSEKCSPTVSQGKSSDCLNTVKSNSSSKAPKVVPLTPEQALKQYKHHLTAYEKLEIINYPEIYFVGPNAKKRHGVIGGPNNGGYDDADGAYIHVPRDHLAYRYEVLKIIGKGSFGQVARVYDHKLRQYVALKMVRNEKRFHRQAAEEIRILEHLKKQDKTGSMNVIHMLESFTFRNHVCMAFELLSIDLYELIKKNKFQGFSVQLVRKFAQSILQSLDALHKNKIIHCDLKPENILLKHHGRSSTKVIDFGSSCFEYQKLYTYIQSRFYRAPEIILGSRYSTPIDIWSFGCILAELLTGQPLFPGEDEGDQLACMMELLGMPPPKLLEQSKRAKYFINSKGIPRYCSVTTQADGRVVLVGGRSRRGKKRGPPGSKDWGTALKGCDDYLFIEFLKRCLHWDPSARLTPAQALRHPWISKSVPRPLTTIDKVSGKRVVNPASAFQGLGSKLPPVVGIANKLKANLMSETNGSIPLCSVLPKLIS
|
2.7.12.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10779429};
|
cell cycle [GO:0007049]; cell division [GO:0051301]; erythrocyte differentiation [GO:0030218]; negative regulation of apoptotic process [GO:0043066]; negative regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043518]; nuclear speck organization [GO:0035063]; organelle disassembly [GO:1903008]; positive regulation of cell cycle G2/M phase transition [GO:1902751]; protein phosphorylation [GO:0006468]; regulation of cellular response to stress [GO:0080135]; regulation of TORC1 signaling [GO:1903432]; stress granule disassembly [GO:0035617]
|
cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; pericentriolar material [GO:0000242]
|
ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein tyrosine kinase activity [GO:0004713]
|
PF00069;
|
3.30.10.30;1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MNB/DYRK subfamily
|
PTM: Ubiquitinated at anaphase by the anaphase-promoting complex (APC/C), leading to its degradation by the proteasome. {ECO:0000269|PubMed:29973724}.; PTM: Protein kinase activity is activated following autophosphorylation at Tyr-369 (Probable). Autophosphorylation at Ser-350 stabilizes the protein and enhances the protein kinase activity (PubMed:9748265). {ECO:0000269|PubMed:9748265, ECO:0000305|PubMed:9748265}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10779429, ECO:0000269|PubMed:20167603, ECO:0000269|PubMed:29973724}. Cytoplasm {ECO:0000269|PubMed:29973724}. Nucleus speckle {ECO:0000269|PubMed:29973724}. Cytoplasmic granule {ECO:0000269|PubMed:20167603, ECO:0000269|PubMed:23415227, ECO:0000269|PubMed:29973724}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:29973724}. Note=Associates with membraneless organelles in the cytoplasm and nucleus (PubMed:29973724). Shuttles between cytoplasm and stress granules (PubMed:20167603). Localized predominantly on distinct speckles distributed throughout the cytoplasm of the cell (PubMed:20167603). At low concentration, showns a homogeneous distribution throughout the cytoplasm and does not condense in speckles. During oxidative and osmotic stress, localizes to stress granules (PubMed:20167603). {ECO:0000269|PubMed:20167603, ECO:0000269|PubMed:29973724}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1; Evidence={ECO:0000269|PubMed:23415227, ECO:0000269|PubMed:29634919, ECO:0000269|PubMed:29973724, ECO:0000269|PubMed:9748265}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.12.1; Evidence={ECO:0000269|PubMed:23415227, ECO:0000269|PubMed:29634919, ECO:0000269|PubMed:29973724, ECO:0000269|PubMed:9748265}; CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1; Evidence={ECO:0000269|PubMed:23415227, ECO:0000269|PubMed:29634919, ECO:0000269|PubMed:29973724, ECO:0000269|PubMed:9748265};
| null | null | null | null |
FUNCTION: Dual-specificity protein kinase that promotes disassembly of several types of membraneless organelles during mitosis, such as stress granules, nuclear speckles and pericentriolar material (PubMed:29973724). Dual-specificity tyrosine-regulated kinases (DYRKs) autophosphorylate a critical tyrosine residue in their activation loop and phosphorylate their substrate on serine and threonine residues (PubMed:29634919, PubMed:9748265). Acts as a central dissolvase of membraneless organelles during the G2-to-M transition, after the nuclear-envelope breakdown: acts by mediating phosphorylation of multiple serine and threonine residues in unstructured domains of proteins, such as SRRM1 and PCM1 (PubMed:29973724). Does not mediate disassembly of all membraneless organelles: disassembly of P-body and nucleolus is not regulated by DYRK3 (PubMed:29973724). Dissolution of membraneless organelles at the onset of mitosis is also required to release mitotic regulators, such as ZNF207, from liquid-unmixed organelles where they are sequestered and keep them dissolved during mitosis (PubMed:29973724). Regulates mTORC1 by mediating the dissolution of stress granules: during stressful conditions, DYRK3 partitions from the cytosol to the stress granule, together with mTORC1 components, which prevents mTORC1 signaling (PubMed:23415227). When stress signals are gone, the kinase activity of DYRK3 is required for the dissolution of stress granule and mTORC1 relocation to the cytosol: acts by mediating the phosphorylation of the mTORC1 inhibitor AKT1S1, allowing full reactivation of mTORC1 signaling (PubMed:23415227). Also acts as a negative regulator of EPO-dependent erythropoiesis: may place an upper limit on red cell production during stress erythropoiesis (PubMed:10779429). Inhibits cell death due to cytokine withdrawal in hematopoietic progenitor cells (PubMed:10779429). Promotes cell survival upon genotoxic stress through phosphorylation of SIRT1: this in turn inhibits p53/TP53 activity and apoptosis (PubMed:20167603). {ECO:0000269|PubMed:10779429, ECO:0000269|PubMed:20167603, ECO:0000269|PubMed:23415227, ECO:0000269|PubMed:29634919, ECO:0000269|PubMed:29973724, ECO:0000269|PubMed:9748265}.
|
Homo sapiens (Human)
|
O43790
|
KRT86_HUMAN
|
MTCGSYCGGRAFSCISACGPRPGRCCITAAPYRGISCYRGLTGGFGSHSVCGGFRAGSCGRSFGYRSGGVCGPSPPCITTVSVNESLLTPLNLEIDPNAQCVKQEEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFYQNRECCQSNLEPLFEGYIETLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFLRRLYEEEIRVLQSHISDTSVVVKLDNSRDLNMDCIIAEIKAQYDDIVTRSRAEAESWYRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQGEAALSDARCKLAELEGALQKAKQDMACLIREYQEVMNSKLGLDIEIATYRRLLEGEEQRLCEGVGSVNVCVSSSRGGVVCGDLCASTTAPVVSTRVSSVPSNSNVVVGTTNACAPSARVGVCGGSCKRC
| null | null |
intermediate filament organization [GO:0045109]; keratinization [GO:0031424]
|
cytosol [GO:0005829]; extracellular space [GO:0005615]; keratin filament [GO:0045095]
|
structural constituent of skin epidermis [GO:0030280]
|
PF00038;PF16208;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
| null | null | null | null | null | null | null | null |
Homo sapiens (Human)
|
O43791
|
SPOP_HUMAN
|
MSRVPSPPPPAEMSSGPVAESWCYTQIKVVKFSYMWTINNFSFCREEMGEVIKSSTFSSGANDKLKWCLRVNPKGLDEESKDYLSLYLLLVSCPKSEVRAKFKFSILNAKGEETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQDSVNISGQNTMNMVKVPECRLADELGGLWENSRFTDCCLCVAGQEFQAHKAILAARSPVFSAMFEHEMEESKKNRVEINDVEPEVFKEMMCFIYTGKAPNLDKMADDLLAAADKYALERLKVMCEDALCSNLSVENAAEILILADLHSADQLKTQAVDFINYHASDVLETSGWKSMVVSHPHLVAEAYRSLASAQCPFLGPPRKRLKQS
| null | null |
localization [GO:0051179]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; regulation of proteolysis [GO:0030162]
|
Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
molecular function inhibitor activity [GO:0140678]; ubiquitin protein ligase binding [GO:0031625]
|
PF00651;PF00917;
|
6.10.250.3030;6.20.250.50;
|
Tdpoz family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22085717, ECO:0000269|PubMed:37622993, ECO:0000269|PubMed:38018242}. Nucleus speckle {ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:9414087}. Cytoplasm {ECO:0000269|PubMed:38018242}.
| null | null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:14528312, ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:16524876, ECO:0000269|PubMed:19818708, ECO:0000269|PubMed:22085717, ECO:0000269|PubMed:22632832, ECO:0000269|PubMed:32109420}.
| null | null |
FUNCTION: Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, leading most often to their proteasomal degradation. In complex with CUL3, involved in ubiquitination and proteasomal degradation of BRMS1, DAXX, PDX1/IPF1, GLI2 and GLI3. In complex with CUL3, involved in ubiquitination of MACROH2A1 and BMI1; this does not lead to their proteasomal degradation. Inhibits transcriptional activation of PDX1/IPF1 targets, such as insulin, by promoting PDX1/IPF1 degradation. The cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing homodimeric SPOP has higher ubiquitin ligase activity than the complex that contains the heterodimer formed by SPOP and SPOPL. Involved in the regulation of bromodomain and extra-terminal motif (BET) proteins BRD2, BRD3, BRD4 stability (PubMed:32109420). Plays an essential role for proper translation, but not for their degradation, of critical DNA replication licensing factors CDT1 and CDC6, thereby participating in DNA synthesis and cell proliferation (PubMed:36791496). Regulates interferon regulatory factor 1/IRF1 proteasomal turnover by targeting S/T-rich degrons in IRF1 (PubMed:37622993). Facilitates the lysosome-dependent degradation of enterovirus EV71 protease 2A by inducing its 'Lys-48'-linked polyubiquitination, which ultimately restricts EV71 replication (PubMed:37796126). Acts as an antiviral factor also against hepatitis B virus/HBV by promoting ubiquitination and subsequent degradation of HNF1A (PubMed:38018242). In turn, inhibits HBV transcription and replication by preventing HNF1A stimulating activity of HBV preS1 promoter and enhancer II (PubMed:38018242). {ECO:0000269|PubMed:14528312, ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:16524876, ECO:0000269|PubMed:19818708, ECO:0000269|PubMed:22085717, ECO:0000269|PubMed:22632832, ECO:0000269|PubMed:32109420, ECO:0000269|PubMed:37622993, ECO:0000269|PubMed:37796126, ECO:0000269|PubMed:38018242}.
|
Homo sapiens (Human)
|
O43795
|
MYO1B_HUMAN
|
MAKMEVKTSLLDNMIGVGDMVLLEPLNEETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAGKTEASKLVMSYVAAVCGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFKPESRVNGLDESKIKDKNELKEICELTGIDQSVLERAFSFRTVEAKQEKVSTTLNVAQAYYARDALAKNLYSRLFSWLVNRINESIKAQTKVRKKVMGVLDIYGFEIFEDNSFEQFIINYCNEKLQQIFIELTLKEEQEEYIREDIEWTHIDYFNNAIICDLIENNTNGILAMLDEECLRPGTVTDETFLEKLNQVCATHQHFESRMSKCSRFLNDTSLPHSCFRIQHYAGKVLYQVEGFVDKNNDLLYRDLSQAMWKASHALIKSLFPEGNPAKINLKRPPTAGSQFKASVATLMKNLQTKNPNYIRCIKPNDKKAAHIFNEALVCHQIRYLGLLENVRVRRAGYAFRQAYEPCLERYKMLCKQTWPHWKGPARSGVEVLFNELEIPVEEYSFGRSKIFIRNPRTLFKLEDLRKQRLEDLATLIQKIYRGWKCRTHFLLMKKSQIVIAAWYRRYAQQKRYQQTKSSALVIQSYIRGWKARKILRELKHQKRCKEAVTTIAAYWHGTQARRELRRLKEEARNKHAIAVIWAYWLGSKARRELKRLKEEARRKHAVAVIWAYWLGLKVRREYRKFFRANAGKKIYEFTLQRIVQKYFLEMKNKMPSLSPIDKNWPSRPYLFLDSTHKELKRIFHLWRCKKYRDQFTDQQKLIYEEKLEASELFKDKKALYPSSVGQPFQGAYLEINKNPKYKKLKDAIEEKIIIAEVVNKINRANGKSTSRIFLLTNNNLLLADQKSGQIKSEVPLVDVTKVSMSSQNDGFFAVHLKEGSEAASKGDFLFSSDHLIEMATKLYRTTLSQTKQKLNIEISDEFLVQFRQDKVCVKFIQGNQKNGSVPTCKRKNNRLLEVAVP
| null | null |
actin filament bundle assembly [GO:0051017]; actin filament organization [GO:0007015]; actin filament-based movement [GO:0030048]; endocytosis [GO:0006897]; post-Golgi vesicle-mediated transport [GO:0006892]; vesicle transport along actin filament [GO:0030050]
|
actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; apical part of cell [GO:0045177]; brush border [GO:0005903]; cell periphery [GO:0071944]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; filopodium [GO:0030175]; microvillus [GO:0005902]; myosin complex [GO:0016459]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
|
actin filament binding [GO:0051015]; ATP binding [GO:0005524]; cadherin binding [GO:0045296]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]
|
PF00612;PF00063;PF06017;
|
1.10.10.820;1.20.5.190;1.20.58.530;6.20.240.20;3.40.850.10;1.20.120.720;
|
TRAFAC class myosin-kinesin ATPase superfamily, Myosin family
| null | null | null | null | null | null | null |
FUNCTION: Motor protein that may participate in process critical to neuronal development and function such as cell migration, neurite outgrowth and vesicular transport. {ECO:0000250}.
|
Homo sapiens (Human)
|
O43805
|
SSNA1_HUMAN
|
MTQQGAALQNYNNELVKCIEELCQKREELCRQIQEEEDEKQRLQNEVRQLTEKLARVNENLARKIASRNEFDRTIAETEAAYLKILESSQTLLSVLKREAGNLTKATAPDQKSSGGRDS
| null | null |
axon arborization [GO:0140060]; axon extension [GO:0048675]; axonogenesis [GO:0007409]; cell cycle [GO:0007049]; cell division [GO:0051301]; intraciliary transport [GO:0042073]; microtubule cytoskeleton organization [GO:0000226]; microtubule nucleation [GO:0007020]; receptor clustering [GO:0043113]
|
axon [GO:0030424]; axoneme [GO:0005930]; centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cytosol [GO:0005829]; midbody [GO:0030496]; motile cilium [GO:0031514]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; supramolecular fiber [GO:0099512]
|
identical protein binding [GO:0042802]; microtubule binding [GO:0008017]; protein self-association [GO:0043621]
| null | null |
SSNA1 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9430706}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:12640030, ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:25390646}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:25390646}. Midbody {ECO:0000269|PubMed:25390646}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:12640030}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:12640030}. Cell projection, axon {ECO:0000250|UniProtKB:Q9JJ94}. Note=In sperm, strongly expressed in the basal body region with weaker expression in the axoneme (PubMed:12640030). Localizes to axon branching points in neurons (By similarity). {ECO:0000250|UniProtKB:Q9JJ94, ECO:0000269|PubMed:12640030}.
| null | null | null | null | null |
FUNCTION: Microtubule-binding protein which stabilizes dynamic microtubules by slowing growth and shrinkage at both plus and minus ends and serves as a sensor of microtubule damage, protecting microtubules from the microtubule-severing enzyme SPAST (PubMed:34970964). Induces microtubule branching which is mediated by the formation of long SSNA1 fibrils which guide microtubule protofilaments to split apart from the mother microtubule and form daughter microtubules (By similarity). Plays a role in axon outgrowth and branching (PubMed:25390646). Required for cell division (PubMed:25390646). {ECO:0000250|UniProtKB:Q9XF62, ECO:0000269|PubMed:25390646, ECO:0000269|PubMed:34970964}.
|
Homo sapiens (Human)
|
O43808
|
PM34_HUMAN
|
MASVLSYESLVHAVAGAVGSVTAMTVFFPLDTARLRLQVDEKRKSKTTHMVLLEIIKEEGLLAPYRGWFPVISSLCCSNFVYFYTFNSLKALWVKGQHSTTGKDLVVGFVAGVVNVLLTTPLWVVNTRLKLQGAKFRNEDIVPTNYKGIIDAFHQIIRDEGISALWNGTFPSLLLVFNPAIQFMFYEGLKRQLLKKRMKLSSLDVFIIGAVAKAIATTVTYPLQTVQSILRFGRHRLNPENRTLGSLRNILYLLHQRVRRFGIMGLYKGLEAKLLQTVLTAALMFLVYEKLTAATFTVMGLKRAHQH
| null | null |
ATP transport [GO:0015867]; fatty acid alpha-oxidation [GO:0001561]; fatty acid beta-oxidation [GO:0006635]; fatty acid transport [GO:0015908]
|
cytosol [GO:0005829]; membrane [GO:0016020]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]
|
adenine nucleotide transmembrane transporter activity [GO:0000295]; ADP transmembrane transporter activity [GO:0015217]; AMP transmembrane transporter activity [GO:0080122]; antiporter activity [GO:0015297]; ATP transmembrane transporter activity [GO:0005347]; coenzyme A transmembrane transporter activity [GO:0015228]; FAD transmembrane transporter activity [GO:0015230]; FMN transmembrane transporter activity [GO:0044610]; NAD transmembrane transporter activity [GO:0051724]; protein-folding chaperone binding [GO:0051087]
|
PF00153;
|
1.50.40.10;
|
Mitochondrial carrier (TC 2.A.29) family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14709540}. Peroxisome membrane {ECO:0000269|PubMed:11121399, ECO:0000269|PubMed:11402059, ECO:0000269|PubMed:14709540, ECO:0000269|PubMed:9874197}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=AMP(out) + CoA(in) = AMP(in) + CoA(out); Xref=Rhea:RHEA:73095, ChEBI:CHEBI:57287, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:22185573}; CATALYTIC ACTIVITY: Reaction=3'-dephospho-CoA(in) + AMP(out) = 3'-dephospho-CoA(out) + AMP(in); Xref=Rhea:RHEA:73099, ChEBI:CHEBI:57328, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:22185573}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA(in) + AMP(out) = acetyl-CoA(out) + AMP(in); Xref=Rhea:RHEA:73447, ChEBI:CHEBI:57288, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:22185573}; CATALYTIC ACTIVITY: Reaction=AMP(in) + NAD(+)(out) = AMP(out) + NAD(+)(in); Xref=Rhea:RHEA:65424, ChEBI:CHEBI:57540, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:22185573}; CATALYTIC ACTIVITY: Reaction=AMP(out) + FAD(in) = AMP(in) + FAD(out); Xref=Rhea:RHEA:73087, ChEBI:CHEBI:57692, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:22185573}; CATALYTIC ACTIVITY: Reaction=AMP(out) + FMN(in) = AMP(in) + FMN(out); Xref=Rhea:RHEA:73091, ChEBI:CHEBI:58210, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:22185573}; CATALYTIC ACTIVITY: Reaction=ADP(out) + AMP(in) = ADP(in) + AMP(out); Xref=Rhea:RHEA:72851, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:22185573}; CATALYTIC ACTIVITY: Reaction=adenosine 3',5'-bisphosphate(in) + AMP(out) = adenosine 3',5'-bisphosphate(out) + AMP(in); Xref=Rhea:RHEA:73451, ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:22185573}; CATALYTIC ACTIVITY: Reaction=CoA(out) + FAD(in) = CoA(in) + FAD(out); Xref=Rhea:RHEA:73143, ChEBI:CHEBI:57287, ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:22185573}; CATALYTIC ACTIVITY: Reaction=adenosine 3',5'-bisphosphate(out) + FAD(in) = adenosine 3',5'-bisphosphate(in) + FAD(out); Xref=Rhea:RHEA:73147, ChEBI:CHEBI:57692, ChEBI:CHEBI:58343; Evidence={ECO:0000269|PubMed:22185573}; CATALYTIC ACTIVITY: Reaction=CoA(out) + FMN(in) = CoA(in) + FMN(out); Xref=Rhea:RHEA:73151, ChEBI:CHEBI:57287, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:22185573}; CATALYTIC ACTIVITY: Reaction=adenosine 3',5'-bisphosphate(out) + FMN(in) = adenosine 3',5'-bisphosphate(in) + FMN(out); Xref=Rhea:RHEA:73155, ChEBI:CHEBI:58210, ChEBI:CHEBI:58343; Evidence={ECO:0000269|PubMed:22185573}; CATALYTIC ACTIVITY: Reaction=FAD(out) + NAD(+)(in) = FAD(in) + NAD(+)(out); Xref=Rhea:RHEA:73163, ChEBI:CHEBI:57540, ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:22185573}; CATALYTIC ACTIVITY: Reaction=FMN(out) + NAD(+)(in) = FMN(in) + NAD(+)(out); Xref=Rhea:RHEA:73159, ChEBI:CHEBI:57540, ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:22185573}; CATALYTIC ACTIVITY: Reaction=CoA(out) + NAD(+)(in) = CoA(in) + NAD(+)(out); Xref=Rhea:RHEA:73167, ChEBI:CHEBI:57287, ChEBI:CHEBI:57540; Evidence={ECO:0000269|PubMed:22185573}; CATALYTIC ACTIVITY: Reaction=adenosine 3',5'-bisphosphate(out) + NAD(+)(in) = adenosine 3',5'-bisphosphate(in) + NAD(+)(out); Xref=Rhea:RHEA:73171, ChEBI:CHEBI:57540, ChEBI:CHEBI:58343; Evidence={ECO:0000269|PubMed:22185573}; CATALYTIC ACTIVITY: Reaction=ADP(in) + FMN(out) = ADP(out) + FMN(in); Xref=Rhea:RHEA:73175, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:22185573}; CATALYTIC ACTIVITY: Reaction=ADP(in) + FAD(out) = ADP(out) + FAD(in); Xref=Rhea:RHEA:73183, ChEBI:CHEBI:57692, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:22185573}; CATALYTIC ACTIVITY: Reaction=ADP(out) + CoA(in) = ADP(in) + CoA(out); Xref=Rhea:RHEA:72839, ChEBI:CHEBI:57287, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:22185573}; CATALYTIC ACTIVITY: Reaction=adenosine 3',5'-bisphosphate(in) + ADP(out) = adenosine 3',5'-bisphosphate(out) + ADP(in); Xref=Rhea:RHEA:72847, ChEBI:CHEBI:58343, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:22185573};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.19 mM for AMP {ECO:0000269|PubMed:22185573}; Vmax=74 umol/min/g enzyme toward AMP {ECO:0000269|PubMed:22185573};
| null | null | null |
FUNCTION: Peroxisomal transporter for multiple cofactors like coenzyme A (CoA), flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN) and nucleotide adenosine monophosphate (AMP), and to a lesser extent for nicotinamide adenine dinucleotide (NAD(+)), adenosine diphosphate (ADP) and adenosine 3',5'-diphosphate (PAP). May catalyze the transport of free CoA, FAD and NAD(+) from the cytosol into the peroxisomal matrix by a counter-exchange mechanism. {ECO:0000269|PubMed:22185573}.
|
Homo sapiens (Human)
|
O43809
|
CPSF5_HUMAN
|
MSVVPPNRSQTGWPRGVTQFGNKYIQQTKPLTLERTINLYPLTNYTFGTKEPLYEKDSSVAARFQRMREEFDKIGMRRTVEGVLIVHEHRLPHVLLLQLGTTFFKLPGGELNPGEDEVEGLKRLMTEILGRQDGVLQDWVIDDCIGNWWRPNFEPPQYPYIPAHITKPKEHKKLFLVQLQEKALFAVPKNYKLVAAPLFELYDNAPGYGPIISSLPQLLSRFNFIYN
| null | null |
cell differentiation [GO:0030154]; messenger ribonucleoprotein complex assembly [GO:1990120]; mRNA 3'-end processing [GO:0031124]; mRNA alternative polyadenylation [GO:0110104]; mRNA polyadenylation [GO:0006378]; mRNA processing [GO:0006397]; positive regulation of pro-B cell differentiation [GO:2000975]; positive regulation of stem cell differentiation [GO:2000738]; post-transcriptional regulation of gene expression [GO:0010608]; protein heterotetramerization [GO:0051290]; protein tetramerization [GO:0051262]
|
centriolar satellite [GO:0034451]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; mRNA cleavage and polyadenylation specificity factor complex [GO:0005847]; mRNA cleavage factor complex [GO:0005849]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; paraspeckles [GO:0042382]
|
chromatin binding [GO:0003682]; histone deacetylase binding [GO:0042826]; identical protein binding [GO:0042802]; mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA binding [GO:0003729]; protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723]
|
PF13869;
|
3.90.79.10;
|
Nudix hydrolase family, CPSF5 subfamily
|
PTM: Acetylated mainly by p300/CBP, recruited to the complex by CPSF6. Acetylation decreases interaction with PAPAO. Deacetylated by the class I/II HDACs, HDAC1, HDAC3 and HDAC10, and by the class III HDACs, SIRT1 and SIRT2. {ECO:0000269|PubMed:17172643}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15169763, ECO:0000269|PubMed:19864460, ECO:0000269|PubMed:20695905, ECO:0000269|PubMed:9659921}. Cytoplasm {ECO:0000269|PubMed:19864460}. Note=Shuttles between the nucleus and the cytoplasm in a transcription- and XPO1/CRM1-independent manner, most probably in complex with the cleavage factor Im complex (CFIm) (PubMed:19864460). In punctate subnuclear structures localized adjacent to nuclear speckles, called paraspeckles (PubMed:15169763). {ECO:0000269|PubMed:15169763, ECO:0000269|PubMed:19864460}.
| null | null | null | null | null |
FUNCTION: Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs (PubMed:14690600, PubMed:15937220, PubMed:17024186, PubMed:17098938, PubMed:29276085, PubMed:8626397, PubMed:9659921). CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals) (PubMed:14690600, PubMed:17024186, PubMed:8626397, PubMed:9659921). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation (PubMed:17098938, PubMed:23187700, PubMed:29276085). The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs (PubMed:17098938, PubMed:20695905, PubMed:29276085). NUDT21/CPSF5 activates indirectly the mRNA 3'-processing machinery by recruiting CPSF6 and/or CPSF7 (PubMed:29276085). Binds to 5'-UGUA-3' elements localized upstream of pA signals that act as enhancers of pre-mRNA 3'-end processing (PubMed:14690600, PubMed:15169763, PubMed:17024186, PubMed:20479262, PubMed:22813749, PubMed:8626397). The homodimer mediates simultaneous sequence-specific recognition of two 5'-UGUA-3' elements within the pre-mRNA (PubMed:20479262, PubMed:21295486). Plays a role in somatic cell fate transitions and pluripotency by regulating widespread changes in gene expression through an APA-dependent function (By similarity). Binds to chromatin (By similarity). Binds to, but does not hydrolyze mono- and di-adenosine nucleotides (PubMed:18445629). {ECO:0000250|UniProtKB:Q9CQF3, ECO:0000269|PubMed:14690600, ECO:0000269|PubMed:15169763, ECO:0000269|PubMed:15937220, ECO:0000269|PubMed:17024186, ECO:0000269|PubMed:17098938, ECO:0000269|PubMed:18445629, ECO:0000269|PubMed:20479262, ECO:0000269|PubMed:20695905, ECO:0000269|PubMed:21295486, ECO:0000269|PubMed:22813749, ECO:0000269|PubMed:23187700, ECO:0000269|PubMed:29276085, ECO:0000269|PubMed:8626397, ECO:0000269|PubMed:9659921}.
|
Homo sapiens (Human)
|
O43813
|
LANC1_HUMAN
|
MAQRAFPNPYADYNKSLAEGYFDAAGRLTPEFSQRLTNKIRELLQQMERGLKSADPRDGTGYTGWAGIAVLYLHLYDVFGDPAYLQLAHGYVKQSLNCLTKRSITFLCGDAGPLAVAAVLYHKMNNEKQAEDCITRLIHLNKIDPHAPNEMLYGRIGYIYALLFVNKNFGVEKIPQSHIQQICETILTSGENLARKRNFTAKSPLMYEWYQEYYVGAAHGLAGIYYYLMQPSLQVSQGKLHSLVKPSVDYVCQLKFPSGNYPPCIGDNRDLLVHWCHGAPGVIYMLIQAYKVFREEKYLCDAYQCADVIWQYGLLKKGYGLCHGSAGNAYAFLTLYNLTQDMKYLYRACKFAEWCLEYGEHGCRTPDTPFSLFEGMAGTIYFLADLLVPTKARFPAFEL
|
2.5.1.18
| null |
carbohydrate metabolic process [GO:0005975]; cellular detoxification [GO:1990748]; G protein-coupled receptor signaling pathway [GO:0007186]; peptide modification [GO:0031179]
|
cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
|
G protein-coupled receptor activity [GO:0004930]; glutathione binding [GO:0043295]; glutathione transferase activity [GO:0004364]; low-density lipoprotein particle receptor binding [GO:0050750]; SH3 domain binding [GO:0017124]; zinc ion binding [GO:0008270]
|
PF05147;
|
1.50.10.10;
|
LanC-like protein family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15811525}. Cell membrane {ECO:0000269|PubMed:10944443, ECO:0000269|PubMed:16979580}; Peripheral membrane protein {ECO:0000269|PubMed:10944443}.
|
CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000250|UniProtKB:O89112}; CATALYTIC ACTIVITY: Reaction=1-chloro-2,4-dinitrobenzene + glutathione = 2,4-dinitrophenyl-S-glutathione + chloride + H(+); Xref=Rhea:RHEA:51220, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:34718, ChEBI:CHEBI:57925, ChEBI:CHEBI:133977; EC=2.5.1.18; Evidence={ECO:0000250|UniProtKB:O89112};
| null | null | null | null |
FUNCTION: Functions as a glutathione transferase. Catalyzes conjugation of the glutathione (GSH) to artificial substrates 1-chloro-2,4-dinitrobenzene (CDNB) and p-nitrophenyl acetate. Mitigates neuronal oxidative stress during normal postnatal development and in response to oxidative stresses probably through GSH antioxidant defense mechanism (By similarity). May play a role in EPS8 signaling. Binds glutathione (PubMed:19528316). {ECO:0000250|UniProtKB:O89112, ECO:0000269|PubMed:19528316}.
|
Homo sapiens (Human)
|
O43815
|
STRN_HUMAN
|
MDEQAGPGVFFSNNHPGAGGAKGLGPLAEAAAAGDGAAAAGAARAQYSLPGILHFLQHEWARFEVERAQWEVERAELQAQIAFLQGERKGQENLKKDLVRRIKMLEYALKQERAKYHKLKYGTELNQGDMKPPSYDSDEGNETEVQPQQNSQLMWKQGRQLLRQYLQEVGYTDTILDVKSKRVRALLGFSSDVTDREDDKNQDSVVNGTEAEVKETAMIAKSELTDSASVLDNFKFLESAAADFSDEDEDDDVDGREKSVIDTSTIVRKKALPDSGEDRDTKEALKEFDFLVTSEEGDNESRSAGDGTDWEKEDQCLMPEAWNVDQGVITKLKEQYKKERKGKKGVKRPNRSKLQDMLANLRDVDELPSLQPSVGSPSRPSSSRLPEHEINRADEVEALTFPPSSGKSFIMGADEALESELGLGELAGLTVANEADSLTYDIANNKDALRKTWNPKFTLRSHFDGIRALAFHPIEPVLITASEDHTLKMWNLQKTAPAKKSTSLDVEPIYTFRAHKGPVLCVVMSSNGEQCYSGGTDGLIQGWNTTNPNIDPYDSYDPSVLRGPLLGHTDAVWGLAYSAAHQRLLSCSADGTLRLWNTTEVAPALSVFNDTKELGIPASVDLVSSDPSHMVASFSKGYTSIFNMETQQRILTLESNVDTTANSSCQINRVISHPTLPISITAHEDRHIKFYDNNTGKLIHSMVAHLEAVTSLAVDPNGLYLMSGSHDCSIRLWNLESKTCIQEFTAHRKKFEESIHDVAFHPSKCYIASAGADALAKVFV
| null | null |
bicellular tight junction assembly [GO:0070830]; dendrite development [GO:0016358]; locomotory behavior [GO:0007626]; negative regulation of cell population proliferation [GO:0008285]; Wnt signaling pathway [GO:0016055]
|
bicellular tight junction [GO:0005923]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; FAR/SIN/STRIPAK complex [GO:0090443]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]
|
armadillo repeat domain binding [GO:0070016]; calmodulin binding [GO:0005516]; nuclear estrogen receptor binding [GO:0030331]; protein phosphatase 2A binding [GO:0051721]; protein-containing complex binding [GO:0044877]
|
PF08232;PF00400;
|
1.20.5.300;2.130.10.10;
|
WD repeat striatin family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P70483}. Membrane {ECO:0000250|UniProtKB:P70483}; Peripheral membrane protein {ECO:0000250|UniProtKB:P70483}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P70483}. Note=CTTNBP2-binding may regulate dendritic spine distribution. {ECO:0000250|UniProtKB:P70483}.
| null | null | null | null | null |
FUNCTION: Calmodulin-binding scaffolding protein which is the center of the striatin-interacting phosphatase and kinase (STRIPAK) complexes (PubMed:18782753). STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (Probable). {ECO:0000269|PubMed:18782753, ECO:0000305|PubMed:26876214}.
|
Homo sapiens (Human)
|
O43818
|
U3IP2_HUMAN
|
MSATAAARKRGKPASGAGAGAGAGKRRRKADSAGDRGKSKGGGKMNEEISSDSESESLAPRKPEEEEEEELEETAQEKKLRLAKLYLEQLRQQEEEKAEARAFEEDQVAGRLKEDVLEQRGRLQKLVAKEIQAPASADIRVLRGHQLSITCLVVTPDDSAIFSAAKDCSIIKWSVESGRKLHVIPRAKKGAEGKPPGHSSHVLCMAISSDGKYLASGDRSKLILIWEAQSCQHLYTFTGHRDAVSGLAFRRGTHQLYSTSHDRSVKVWNVAENSYVETLFGHQDAVAALDALSRECCVTAGGRDGTVRVWKIPEESQLVFYGHQGSIDCIHLINEEHMVSGADDGSVALWGLSKKRPLALQREAHGLRGEPGLEQPFWISSVAALLNTDLVATGSHSSCVRLWQCGEGFRQLDLLCDIPLVGFINSLKFSSSGDFLVAGVGQEHRLGRWWRIKEARNSVCIIPLRRVPVPPAAGS
| null | null |
ribosomal small subunit biogenesis [GO:0042274]; rRNA processing [GO:0006364]
|
box C/D RNP complex [GO:0031428]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; small-subunit processome [GO:0032040]
|
RNA binding [GO:0003723]; snoRNA binding [GO:0030515]; U3 snoRNA binding [GO:0034511]
|
PF00400;
|
2.130.10.10;
|
WD repeat RRP9 family
|
PTM: Acetylation at Lys-12 and Lys-25 by KAT2B/PCAF under stress impairs pre-rRNA processing (PubMed:26867678). Deacetylation by SIRT7 enhances RRP9-binding to U3 snoRNA, which is a prerequisite for pre-rRNA processing (PubMed:26867678). {ECO:0000269|PubMed:26867678}.
|
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:26867678, ECO:0000269|PubMed:34516797, ECO:0000269|PubMed:9418896}.
| null | null | null | null | null |
FUNCTION: Component of a nucleolar small nuclear ribonucleoprotein particle (snoRNP) thought to participate in the processing and modification of pre-ribosomal RNA (pre-rRNA) (PubMed:26867678). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). {ECO:0000269|PubMed:26867678, ECO:0000269|PubMed:34516797}.
|
Homo sapiens (Human)
|
O43819
|
SCO2_HUMAN
|
MLLLTRSPTAWHRLSQLKPRVLPGTLGGQALHLRSWLLSRQGPAETGGQGQPQGPGLRTRLLITGLFGAGLGGAWLALRAEKERLQQQKRTEALRQAAVGQGDFHLLDHRGRARCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVRQLEAEPGLPPVQPVFITVDPERDDVEAMARYVQDFHPRLLGLTGSTKQVAQASHSYRVYYNAGPKDEDQDYIVDHSIAIYLLNPDGLFTDYYGRSRSAEQISDSVRRHMAAFRSVLS
| null | null |
eye development [GO:0001654]; in utero embryonic development [GO:0001701]; intracellular copper ion homeostasis [GO:0006878]; mitochondrial cytochrome c oxidase assembly [GO:0033617]; muscle system process [GO:0003012]; respiratory electron transport chain [GO:0022904]; response to activity [GO:0014823]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; myofibril [GO:0030016]
|
copper chaperone activity [GO:0016531]; copper ion binding [GO:0005507]; protein-disulfide reductase activity [GO:0015035]
|
PF02630;
|
3.40.30.10;
|
SCO1/2 family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:15229189}; Single-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Copper metallochaperone essential for the synthesis and maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Involved in transporting copper to the Cu(A) site on MT-CO2/COX2 (PubMed:15229189, PubMed:17189203). Also acts as a thiol-disulfide oxidoreductase to regulate the redox state of the cysteines in SCO1 during maturation of MT-CO2/COX2 (PubMed:19336478). {ECO:0000269|PubMed:15229189, ECO:0000269|PubMed:17189203, ECO:0000269|PubMed:19336478}.
|
Homo sapiens (Human)
|
O43820
|
HYAL3_HUMAN
|
MTTQLGPALVLGVALCLGCGQPLPQVPERPFSVLWNVPSAHCEARFGVHLPLNALGIIANRGQHFHGQNMTIFYKNQLGLYPYFGPRGTAHNGGIPQALPLDRHLALAAYQIHHSLRPGFAGPAVLDWEEWCPLWAGNWGRRRAYQAASWAWAQQVFPDLDPQEQLYKAYTGFEQAARALMEDTLRVAQALRPHGLWGFYHYPACGNGWHSMASNYTGRCHAATLARNTQLHWLWAASSALFPSIYLPPRLPPAHHQAFVRHRLEEAFRVALVGHRHPLPVLAYVRLTHRRSGRFLSQDDLVQSIGVSAALGAAGVVLWGDLSLSSSEEECWHLHDYLVDTLGPYVINVTRAAMACSHQRCHGHGRCARRDPGQMEAFLHLWPDGSLGDWKSFSCHCYWGWAGPTCQEPRPGPKEAV
|
3.2.1.35
| null |
carbohydrate metabolic process [GO:0005975]; cartilage development [GO:0051216]; cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to UV-B [GO:0071493]; hyaluronan catabolic process [GO:0030214]; inflammatory response [GO:0006954]; negative regulation of ovarian follicle development [GO:2000355]; ovarian follicle atresia [GO:0001552]; penetration of zona pellucida [GO:0007341]; positive regulation of acrosomal vesicle exocytosis [GO:2000368]; response to antibiotic [GO:0046677]; response to virus [GO:0009615]
|
acrosomal membrane [GO:0002080]; acrosomal vesicle [GO:0001669]; cytoplasmic vesicle [GO:0031410]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; lysosome [GO:0005764]; plasma membrane [GO:0005886]; sperm midpiece [GO:0097225]
|
hyaluronoglucuronidase activity [GO:0033906]; hyalurononglucosaminidase activity [GO:0004415]
|
PF01630;
|
3.20.20.70;
|
Glycosyl hydrolase 56 family
|
PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8VEI3}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8VEI3}. Cell membrane {ECO:0000250|UniProtKB:Q8VEI3}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q8VEI3}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8VEI3}. Early endosome {ECO:0000250|UniProtKB:Q8VEI3}. Note=Mostly present in low-density vesicles. Low levels in higher density vesicles of late endosomes and lysosomes. Localized in punctate cytoplasmic vesicles and in perinuclear structures, but does not colocalize with LAMP1. Localized on the plasma membrane over the acrosome and on the surface of the midpiece of the sperm tail. {ECO:0000250|UniProtKB:Q8VEI3}.
|
CATALYTIC ACTIVITY: Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35; Evidence={ECO:0000269|PubMed:12084718};
| null | null | null | null |
FUNCTION: Facilitates sperm penetration into the layer of cumulus cells surrounding the egg by digesting hyaluronic acid. Involved in induction of the acrosome reaction in the sperm. Involved in follicular atresia, the breakdown of immature ovarian follicles that are not selected to ovulate. Induces ovarian granulosa cell apoptosis, possibly via apoptotic signaling pathway involving CASP8 and CASP3 activation, and poly(ADP-ribose) polymerase (PARP) cleavage. Has no hyaluronidase activity in embryonic fibroblasts in vitro. Has no hyaluronidase activity in granulosa cells in vitro. {ECO:0000250|UniProtKB:Q8VEI3}.
|
Homo sapiens (Human)
|
O43822
|
CF410_HUMAN
|
MKLTRKMVLTRAKASELHSVRKLNCWGSRLTDISICQEMPSLEVITLSVNSISTLEPVSRCQRLSELYLRRNRIPSLAELFYLKGLPRLRVLWLAENPCCGTSPHRYRMTVLRTLPRLQKLDNQAVTEEELSRALSEGEEITAAPEREGTGHGGPKLCCTLSSLSSAAETGRDPLDSEEEATSGAQDERGLKPPSRGQFPSLSARDASSSHRGRNVLTAILLLLRELDAEGLEAVQQTVGSRLQALRGEEVQEHAE
| null | null |
cytoskeleton organization [GO:0007010]; DNA damage response [GO:0006974]; outer dynein arm assembly [GO:0036158]; regulation of cell shape [GO:0008360]; smoothened signaling pathway [GO:0007224]
|
ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrion [GO:0005739]; photoreceptor connecting cilium [GO:0032391]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]
| null | null |
3.80.10.10;
| null | null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9325172}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:26167768, ECO:0000269|PubMed:26294103}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:27548899}. Cytoplasm {ECO:0000269|PubMed:26290490}. Note=Colocalizes with NEK1 and SPATA7 at the basal body. {ECO:0000269|PubMed:26167768}.
| null | null | null | null | null |
FUNCTION: Plays a role in cilia formation and/or maintenance (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization (PubMed:21834987). Involved in DNA damage repair (PubMed:26290490). {ECO:0000250|UniProtKB:Q8C6G1, ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:26290490}.
|
Homo sapiens (Human)
|
O43823
|
AKAP8_HUMAN
|
MDQGYGGYGAWSAGPANTQGAYGTGVASWQGYENYNYYGAQNTSVTTGATYSYGPASWEAAKANDGGLAAGAPAMHMASYGPEPCTDNSDSLIAKINQRLDMMSKEGGRGGSGGGGEGIQDRESSFRFQPFESYDSRPCLPEHNPYRPSYSYDYEFDLGSDRNGSFGGQYSECRDPARERGSLDGFMRGRGQGRFQDRSNPGTFMRSDPFVPPAASSEPLSTPWNELNYVGGRGLGGPSPSRPPPSLFSQSMAPDYGVMGMQGAGGYDSTMPYGCGRSQPRMRDRDRPKRRGFDRFGPDGTGRKRKQFQLYEEPDTKLARVDSEGDFSENDDAAGDFRSGDEEFKGEDELCDSGRQRGEKEDEDEDVKKRREKQRRRDRTRDRAADRIQFACSVCKFRSFDDEEIQKHLQSKFHKETLRFISTKLPDKTVEFLQEYIVNRNKKIEKRRQELMEKETAKPKPDPFKGIGQEHFFKKIEAAHCLACDMLIPAQPQLLQRHLHSVDHNHNRRLAAEQFKKTSLHVAKSVLNNRHIVKMLEKYLKGEDPFTSETVDPEMEGDDNLGGEDKKETPEEVAADVLAEVITAAVRAVDGEGAPAPESSGEPAEDEGPTDTAEAGSDPQAEQLLEEQVPCGTAHEKGVPKARSEAAEAGNGAETMAAEAESAQTRVAPAPAAADAEVEQTDAESKDAVPTE
| null | null |
cell cycle G2/M phase transition [GO:0044839]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to prostaglandin E stimulus [GO:0071380]; innate immune response [GO:0045087]; mitotic cell cycle [GO:0000278]; mitotic chromosome condensation [GO:0007076]; negative regulation of tumor necrosis factor production [GO:0032720]; protein transport [GO:0015031]; signal transduction [GO:0007165]
|
condensed chromosome [GO:0000793]; cytoplasm [GO:0005737]; female pronucleus [GO:0001939]; membrane [GO:0016020]; nuclear matrix [GO:0016363]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
double-stranded DNA binding [GO:0003690]; histone deacetylase binding [GO:0042826]; NF-kappaB binding [GO:0051059]; protein kinase A regulatory subunit binding [GO:0034237]; RNA binding [GO:0003723]; zinc ion binding [GO:0008270]
|
PF04988;
| null |
AKAP95 family
|
PTM: Phosphorylated on tyrosine residues probably by SRC subfamily protein kinases; multiple phosphorylation is leading to dissociation from nuclear structures implicated in chromatin structural changes. {ECO:0000269|PubMed:25770215}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19277197, ECO:0000269|PubMed:26683827}. Nucleus matrix {ECO:0000269|PubMed:10601332}. Nucleus, nucleolus {ECO:0000269|PubMed:26683827}. Cytoplasm {ECO:0000250|UniProtKB:Q9DBR0}. Note=Associated with the nuclear matrix in interphase and redistributes mostly to chromatin at mitosis. However, mitotic chromatin localization has been questioned. Upon nuclear reassembly at the end of mitosis, is sequestered into the daughter nuclei where it re-acquires an interphase distribution. Exhibits partial localization to the nucleolus in interphase, where it colocalizes with UBTF/UBF, suggesting localization to the fibrillary center and/or to the dense fibrillary component. Colocalizes with GJA1 at the nuclear membrane specifically during cell cycle G1/S phase. {ECO:0000269|PubMed:10601332, ECO:0000269|PubMed:26683827, ECO:0000269|PubMed:26880274}.
| null | null | null | null | null |
FUNCTION: Anchoring protein that mediates the subcellular compartmentation of cAMP-dependent protein kinase (PKA type II) (PubMed:9473338). Acts as an anchor for a PKA-signaling complex onto mitotic chromosomes, which is required for maintenance of chromosomes in a condensed form throughout mitosis. Recruits condensin complex subunit NCAPD2 to chromosomes required for chromatin condensation; the function appears to be independent from PKA-anchoring (PubMed:10601332, PubMed:10791967, PubMed:11964380). May help to deliver cyclin D/E to CDK4 to facilitate cell cycle progression (PubMed:14641107). Required for cell cycle G2/M transition and histone deacetylation during mitosis. In mitotic cells recruits HDAC3 to the vicinity of chromatin leading to deacetylation and subsequent phosphorylation at 'Ser-10' of histone H3; in this function may act redundantly with AKAP8L (PubMed:16980585). Involved in nuclear retention of RPS6KA1 upon ERK activation thus inducing cell proliferation (PubMed:22130794). May be involved in regulation of DNA replication by acting as scaffold for MCM2 (PubMed:12740381). Enhances HMT activity of the KMT2 family MLL4/WBP7 complex and is involved in transcriptional regulation. In a teratocarcinoma cell line is involved in retinoic acid-mediated induction of developmental genes implicating H3 'Lys-4' methylation (PubMed:23995757). May be involved in recruitment of active CASP3 to the nucleus in apoptotic cells (PubMed:16227597). May act as a carrier protein of GJA1 for its transport to the nucleus (PubMed:26880274). May play a repressive role in the regulation of rDNA transcription. Preferentially binds GC-rich DNA in vitro. In cells, associates with ribosomal RNA (rRNA) chromatin, preferentially with rRNA promoter and transcribed regions (PubMed:26683827). Involved in modulation of Toll-like receptor signaling. Required for the cAMP-dependent suppression of TNF-alpha in early stages of LPS-induced macrophage activation; the function probably implicates targeting of PKA to NFKB1 (By similarity). {ECO:0000250|UniProtKB:Q63014, ECO:0000250|UniProtKB:Q9DBR0, ECO:0000269|PubMed:10601332, ECO:0000269|PubMed:10791967, ECO:0000269|PubMed:11964380, ECO:0000269|PubMed:16980585, ECO:0000269|PubMed:22130794, ECO:0000269|PubMed:26683827, ECO:0000269|PubMed:26880274, ECO:0000305|PubMed:14641107, ECO:0000305|PubMed:9473338}.
|
Homo sapiens (Human)
|
O43825
|
B3GT2_HUMAN
|
MLQWRRRHCCFAKMTWNAKRSLFRTHLIGVLSLVFLFAMFLFFNHHDWLPGRAGFKENPVTYTFRGFRSTKSETNHSSLRNIWKETVPQTLRPQTATNSNNTDLSPQGVTGLENTLSANGSIYNEKGTGHPNSYHFKYIINEPEKCQEKSPFLILLIAAEPGQIEARRAIRQTWGNESLAPGIQITRIFLLGLSIKLNGYLQRAILEESRQYHDIIQQEYLDTYYNLTIKTLMGMNWVATYCPHIPYVMKTDSDMFVNTEYLINKLLKPDLPPRHNYFTGYLMRGYAPNRNKDSKWYMPPDLYPSERYPVFCSGTGYVFSGDLAEKIFKVSLGIRRLHLEDVYVGICLAKLRIDPVPPPNEFVFNHWRVSYSSCKYSHLITSHQFQPSELIKYWNHLQQNKHNACANAAKEKAGRYRHRKLH
|
2.4.1.86
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
|
galactosylceramide biosynthetic process [GO:0006682]; oligosaccharide biosynthetic process [GO:0009312]; protein glycosylation [GO:0006486]; protein O-linked glycosylation [GO:0006493]
|
Golgi membrane [GO:0000139]
|
glucosaminylgalactosylglucosylceramide beta-galactosyltransferase activity [GO:0047275]; UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity [GO:0008499]
|
PF19341;PF01762;
|
3.90.550.50;
|
Glycosyltransferase 31 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:53432, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:61631, ChEBI:CHEBI:66914, ChEBI:CHEBI:133506; EC=2.4.1.86; Evidence={ECO:0000269|PubMed:9417100, ECO:0000269|PubMed:9582303}; CATALYTIC ACTIVITY: Reaction=a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-alpha-D-galactose = a beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1')-Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:16045, ChEBI:CHEBI:15378, ChEBI:CHEBI:17103, ChEBI:CHEBI:17292, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.86; Evidence={ECO:0000269|PubMed:9582303}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16046; Evidence={ECO:0000269|PubMed:9582303}; CATALYTIC ACTIVITY: Reaction=a neolactoside IV(3)-beta-GlcNAc-nLc4Cer(d18:1(4E)) + UDP-alpha-D-galactose = a neolactoside IV(3)-beta-[Gal-beta-(1->3)-GlcNAc]-nLc4Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:41936, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:78565, ChEBI:CHEBI:142448; Evidence={ECO:0000269|PubMed:9582303}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41937; Evidence={ECO:0000269|PubMed:9582303};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=90 uM for UDP-alpha-D-galactose {ECO:0000269|PubMed:9582303};
|
PATHWAY: Protein modification; protein glycosylation.
| null | null |
FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal beta-N-acetylglucosamine (beta-GlcNAc) residue. Can also utilize substrates with a terminal galactose residue, albeit with lower efficiency. Involved in the biosynthesis of the carbohydrate moieties of glycolipids and glycoproteins. Inactive towards substrates with terminal alpha-N-acetylglucosamine (alpha-GlcNAc) or alpha-N-acetylgalactosamine (alpha-GalNAc) residues. {ECO:0000269|PubMed:9417100, ECO:0000269|PubMed:9582303}.
|
Homo sapiens (Human)
|
O43826
|
G6PT1_HUMAN
|
MAAQGYGYYRTVIFSAMFGGYSLYYFNRKTFSFVMPSLVEEIPLDKDDLGFITSSQSAAYAISKFVSGVLSDQMSARWLFSSGLLLVGLVNIFFAWSSTVPVFAALWFLNGLAQGLGWPPCGKVLRKWFEPSQFGTWWAILSTSMNLAGGLGPILATILAQSYSWRSTLALSGALCVVVSFLCLLLIHNEPADVGLRNLDPMPSEGKKGSLKEESTLQELLLSPYLWVLSTGYLVVFGVKTCCTDWGQFFLIQEKGQSALVGSSYMSALEVGGLVGSIAAGYLSDRAMAKAGLSNYGNPRHGLLLFMMAGMTVSMYLFRVTVTSDSPKLWILVLGAVFGFSSYGPIALFGVIANESAPPNLCGTSHAIVGLMANVGGFLAGLPFSTIAKHYSWSTAFWVAEVICAASTAAFFLLRNIRTKMGRVSKKAE
| null | null |
gluconeogenesis [GO:0006094]; glucose homeostasis [GO:0042593]; glucose metabolic process [GO:0006006]; glucose-6-phosphate transport [GO:0015760]; phosphate ion transmembrane transport [GO:0035435]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
glucose 6-phosphate:inorganic phosphate antiporter activity [GO:0061513]; glucose-6-phosphate transmembrane transporter activity [GO:0015152]
|
PF07690;
|
1.20.1250.20;
|
Major facilitator superfamily, Organophosphate:Pi antiporter (OPA) (TC 2.A.1.4) family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21949678, ECO:0000269|PubMed:32884905, ECO:0000269|PubMed:33964207}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate(in) + phosphate(out) = D-glucose 6-phosphate(out) + phosphate(in); Xref=Rhea:RHEA:71535, ChEBI:CHEBI:43474, ChEBI:CHEBI:61548; Evidence={ECO:0000269|PubMed:10026167, ECO:0000269|PubMed:21949678, ECO:0000269|PubMed:33964207};
| null | null | null | null |
FUNCTION: Inorganic phosphate and glucose-6-phosphate antiporter of the endoplasmic reticulum. Transports cytoplasmic glucose-6-phosphate into the lumen of the endoplasmic reticulum and translocates inorganic phosphate into the opposite direction (PubMed:33964207). Forms with glucose-6-phosphatase the complex responsible for glucose production through glycogenolysis and gluconeogenesis. Hence, it plays a central role in homeostatic regulation of blood glucose levels. {ECO:0000269|PubMed:10026167, ECO:0000269|PubMed:21949678, ECO:0000269|PubMed:33964207}.
|
Homo sapiens (Human)
|
O43827
|
ANGL7_HUMAN
|
MLKKPLSAVTWLCIFIVAFVSHPAWLQKLSKHKTPAQPQLKAANCCEEVKELKAQVANLSSLLSELNKKQERDWVSVVMQVMELESNSKRMESRLTDAESKYSEMNNQIDIMQLQAAQTVTQTSADAIYDCSSLYQKNYRISGVYKLPPDDFLGSPELEVFCDMETSGGGWTIIQRRKSGLVSFYRDWKQYKQGFGSIRGDFWLGNEHIHRLSRQPTRLRVEMEDWEGNLRYAEYSHFVLGNELNSYRLFLGNYTGNVGNDALQYHNNTAFSTKDKDNDNCLDKCAQLRKGGYWYNCCTDSNLNGVYYRLGEHNKHLDGITWYGWHGSTYSLKRVEMKIRPEDFKP
| null | null |
negative regulation of vasculature development involved in avascular cornea development in camera-type eye [GO:1901346]; regulation of extracellular matrix organization [GO:1903053]; response to oxidative stress [GO:0006979]
|
collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
identical protein binding [GO:0042802]
|
PF00147;
|
3.90.215.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11682471}.
| null | null | null | null | null |
FUNCTION: Has a role in the formation and organization of the extracellular matrix. In the eye, it functions as a mediator of dexamethasone-induced matrix deposition in the trabecular meshwork, the tissue responsible for the outflow of the ocular aqueous humor and for the maintenance of intraocular pressure (PubMed:21199193). Is a negative regulator of angiogenesis in the cornea, and plays a major role in maintaining corneal avascularity and transparency (PubMed:25622036). {ECO:0000269|PubMed:21199193, ECO:0000269|PubMed:25622036}.
|
Homo sapiens (Human)
|
O43829
|
ZBT14_HUMAN
|
MEFFISMSETIKYNDDDHKTLFLKTLNEQRLEGEFCDIAIVVEDVKFRAHRCVLAACSTYFKKLFKKLEVDSSSVIEIDFLRSDIFEEVLNYMYTAKISVKKEDVNLMMSSGQILGIRFLDKLCSQKRDVSSPDENNGQSKSKYCLKINRPIGDAADTQDDDVEEIGDQDDSPSDDTVEGTPPSQEDGKSPTTTLRVQEAILKELGSEEVRKVNCYGQEVESMETPESKDLGSQTPQALTFNDGMSEVKDEQTPGWTTAASDMKFEYLLYGHHREQIACQACGKTFSDEGRLRKHEKLHTADRPFVCEMCTKGFTTQAHLKEHLKIHTGYKPYSCEVCGKSFIRAPDLKKHERVHSNERPFACHMCDKAFKHKSHLKDHERRHRGEKPFVCGSCTKAFAKASDLKRHENNMHSERKQVTPSAIQSETEQLQAAAMAAEAEQQLETIACS
| null | null |
cardiac septum development [GO:0003279]; coronary vasculature development [GO:0060976]; heart valve development [GO:0003170]; kidney development [GO:0001822]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of transcription by RNA polymerase II [GO:0006357]
|
aggresome [GO:0016235]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]; transcription cis-regulatory region binding [GO:0000976]
|
PF00651;PF00096;
|
3.30.160.60;
|
Krueppel C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15629158}. Note=Colocalizes with ZBTB21 in nucleus in HEK293 cells.
| null | null | null | null | null |
FUNCTION: Transcriptional activator of the dopamine transporter (DAT), binding it's promoter at the consensus sequence 5'-CCTGCACAGTTCACGGA-3'. Binds to 5'-d(GCC)(n)-3' trinucleotide repeats in promoter regions and acts as a repressor of the FMR1 gene. Transcriptional repressor of MYC and thymidine kinase promoters. {ECO:0000269|PubMed:17714511}.
|
Homo sapiens (Human)
|
O43837
|
IDH3B_HUMAN
|
MAALSGVRWLTRALVSAGNPGAWRGLSTSAAAHAASRSQAEDVRVEGSFPVTMLPGDGVGPELMHAVKEVFKAAAVPVEFQEHHLSEVQNMASEEKLEQVLSSMKENKVAIIGKIHTPMEYKGELASYDMRLRRKLDLFANVVHVKSLPGYMTRHNNLDLVIIREQTEGEYSSLEHESARGVIECLKIVTRAKSQRIAKFAFDYATKKGRGKVTAVHKANIMKLGDGLFLQCCEEVAELYPKIKFETMIIDNCCMQLVQNPYQFDVLVMPNLYGNIIDNLAAGLVGGAGVVPGESYSAEYAVFETGARHPFAQAVGRNIANPTAMLLSASNMLRHLNLEYHSSMIADAVKKVIKVGKVRTRDMGGYSTTTDFIKSVIGHLQTKGS
| null | null |
isocitrate metabolic process [GO:0006102]; tricarboxylic acid cycle [GO:0006099]
|
mitochondrial isocitrate dehydrogenase complex (NAD+) [GO:0005962]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
|
electron transfer activity [GO:0009055]; isocitrate dehydrogenase (NAD+) activity [GO:0004449]; magnesium ion binding [GO:0000287]; NAD binding [GO:0051287]
|
PF00180;
|
3.40.718.10;
|
Isocitrate and isopropylmalate dehydrogenases family
| null |
SUBCELLULAR LOCATION: Mitochondrion.
| null | null | null | null | null |
FUNCTION: Plays a structural role to facilitate the assembly and ensure the full activity of the enzyme catalyzing the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers. {ECO:0000269|PubMed:28139779}.
|
Homo sapiens (Human)
|
O43847
|
NRDC_HUMAN
|
MLRRVTVAAVCATRRKLCEAGRELAALWGIETRGRCEDSAAARPFPILAMPGRNKAKSTCSCPDLQPNGQDLGENSRVARLGADESEEEGRRGSLSNAGDPEIVKSPSDPKQYRYIKLQNGLQALLISDLSNMEGKTGNTTDDEEEEEVEEEEEDDDEDSGAEIEDDDEEGFDDEDEFDDEHDDDLDTEDNELEELEERAEARKKTTEKQSAAALCVGVGSFADPDDLPGLAHFLEHMVFMGSLKYPDENGFDAFLKKHGGSDNASTDCERTVFQFDVQRKYFKEALDRWAQFFIHPLMIRDAIDREVEAVDSEYQLARPSDANRKEMLFGSLARPGHPMGKFFWGNAETLKHEPRKNNIDTHARLREFWMRYYSSHYMTLVVQSKETLDTLEKWVTEIFSQIPNNGLPRPNFGHLTDPFDTPAFNKLYRVVPIRKIHALTITWALPPQQQHYRVKPLHYISWLVGHEGKGSILSFLRKKCWALALFGGNGETGFEQNSTYSVFSISITLTDEGYEHFYEVAYTVFQYLKMLQKLGPEKRIFEEIRKIEDNEFHYQEQTDPVEYVENMCENMQLYPLQDILTGDQLLFEYKPEVIGEALNQLVPQKANLVLLSGANEGKCDLKEKWFGTQYSIEDIENSWAELWNSNFELNPDLHLPAENKYIATDFTLKAFDCPETEYPVKIVNTPQGCLWYKKDNKFKIPKAYIRFHLISPLIQKSAANVVLFDIFVNILTHNLAEPAYEADVAQLEYKLVAGEHGLIIRVKGFNHKLPLLFQLIIDYLAEFNSTPAVFTMITEQLKKTYFNILIKPETLAKDVRLLILEYARWSMIDKYQALMDGLSLESLLSFVKEFKSQLFVEGLVQGNVTSTESMDFLKYVVDKLNFKPLEQEMPVQFQVVELPSGHHLCKVKALNKGDANSEVTVYYQSGTRSLREYTLMELLVMHMEEPCFDFLRTKQTLGYHVYPTCRNTSGILGFSVTVGTQATKYNSEVVDKKIEEFLSSFEEKIENLTEEAFNTQVTALIKLKECEDTHLGEEVDRNWNEVVTQQYLFDRLAHEIEALKSFSKSDLVNWFKAHRGPGSKMLSVHVVGYGKYELEEDGTPSSEDSNSSCEVMQLTYLPTSPLLADCIIPITDIRAFTTTLNLLPYHKIVK
|
3.4.24.61
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
|
amyloid-beta metabolic process [GO:0050435]; hormone catabolic process [GO:0042447]; negative regulation of cold-induced thermogenesis [GO:0120163]; peptide catabolic process [GO:0043171]; positive regulation of axonogenesis [GO:0050772]; positive regulation of membrane protein ectodomain proteolysis [GO:0051044]; positive regulation of myelination [GO:0031643]; proteolysis involved in protein catabolic process [GO:0051603]; regulation of endopeptidase activity [GO:0052548]
|
cell surface [GO:0009986]; cytosol [GO:0005829]; dendrite [GO:0030425]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]
|
epidermal growth factor binding [GO:0048408]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]
|
PF00675;PF05193;PF16187;
|
3.30.830.10;
|
Peptidase M16 family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:28017472}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8BHG1}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of polypeptides, preferably at -Xaa-|-Arg-Lys-, and less commonly at -Arg-|-Arg-Xaa-, in which Xaa is not Arg or Lys.; EC=3.4.24.61;
| null | null | null | null |
FUNCTION: Cleaves peptide substrates on the N-terminus of arginine residues in dibasic pairs. Is a critical activator of BACE1- and ADAM17-mediated pro-neuregulin ectodomain shedding, involved in the positive regulation of axonal maturation and myelination. Required for proper functioning of 2-oxoglutarate dehydrogenase (OGDH) (By similarity). {ECO:0000250|UniProtKB:Q8BHG1}.
|
Homo sapiens (Human)
|
O43852
|
CALU_HUMAN
|
MDLRQFLMCLSLCTAFALSKPTEKKDRVHHEPQLSDKVHNDAQSFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVSKIDGDKDGFVTVDELKDWIKFAQKRWIYEDVERQWKGHDLNEDGLVSWEEYKNATYGYVLDDPDPDDGFNYKQMMVRDERRFKMADKDGDLIATKEEFTAFLHPEEYDYMKDIVVQETMEDIDKNADGFIDLEEYIGDMYSHDGNTDEPEWVKTEREQFVEFRDKNRDGKMDKEETKDWILPSDYDHAEAEARHLVYESDQNKDGKLTKEEIVDKYDLFVGSQATDFGEALVRHDEF
| null | null | null |
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; melanosome [GO:0042470]; membrane [GO:0016020]; sarcoplasmic reticulum lumen [GO:0033018]
|
calcium ion binding [GO:0005509]
|
PF13202;
|
1.10.238.10;
|
CREC family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10222138}. Golgi apparatus {ECO:0000269|PubMed:10222138}. Secreted {ECO:0000305}. Melanosome {ECO:0000269|PubMed:12643545}. Sarcoplasmic reticulum lumen {ECO:0000305}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000269|PubMed:12643545}.
| null | null | null | null | null |
FUNCTION: Involved in regulation of vitamin K-dependent carboxylation of multiple N-terminal glutamate residues. Seems to inhibit gamma-carboxylase GGCX. Binds 7 calcium ions with a low affinity (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O43854
|
EDIL3_HUMAN
|
MKRSVAVWLLVGLSLGVPQFGKGDICDPNPCENGGICLPGLADGSFSCECPDGFTDPNCSSVVEVASDEEEPTSAGPCTPNPCHNGGTCEISEAYRGDTFIGYVCKCPRGFNGIHCQHNINECEVEPCKNGGICTDLVANYSCECPGEFMGRNCQYKCSGPLGIEGGIISNQQITASSTHRALFGLQKWYPYYARLNKKGLINAWTAAENDRWPWIQINLQRKMRVTGVITQGAKRIGSPEYIKSYKIAYSNDGKTWAMYKVKGTNEDMVFRGNIDNNTPYANSFTPPIKAQYVRLYPQVCRRHCTLRMELLGCELSGCSEPLGMKSGHIQDYQITASSIFRTLNMDMFTWEPRKARLDKQGKVNAWTSGHNDQSQWLQVDLLVPTKVTGIITQGAKDFGHVQFVGSYKLAYSNDGEHWTVYQDEKQRKDKVFQGNFDNDTHRKNVIDPPIYARHIRILPWSWYGRITLRSELLGCTEEE
| null | null |
cell adhesion [GO:0007155]; positive regulation of cell-substrate adhesion [GO:0010811]
|
collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular vesicle [GO:1903561]
|
calcium ion binding [GO:0005509]; integrin binding [GO:0005178]; signaling receptor activity [GO:0038023]
|
PF00008;PF00754;PF12661;
|
2.60.120.260;2.10.25.10;
| null | null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Promotes adhesion of endothelial cells through interaction with the alpha-v/beta-3 integrin receptor. Inhibits formation of vascular-like structures. May be involved in regulation of vascular morphogenesis of remodeling in embryonic development.
|
Homo sapiens (Human)
|
O43861
|
ATP9B_HUMAN
|
MADQIPLYPVRSAAAAAANRKRAAYYSAAGPRPGADRHSRYQLEDESAHLDEMPLMMSEEGFENEESDYHTLPRARIMQRKRGLEWFVCDGWKFLCTSCCGWLINICRRKKELKARTVWLGCPEKCEEKHPRNSIKNQKYNVFTFIPGVLYEQFKFFLNLYFLVISCSQFVPALKIGYLYTYWAPLGFVLAVTMTREAIDEFRRFQRDKEVNSQLYSKLTVRGKVQVKSSDIQVGDLIIVEKNQRIPSDMVFLRTSEKAGSCFIRTDQLDGETDWKLKVAVSCTQQLPALGDLFSISAYVYAQKPQMDIHSFEGTFTREDSDPPIHESLSIENTLWASTIVASGTVIGVVIYTGKETRSVMNTSNPKNKVGLLDLELNRLTKALFLALVALSIVMVTLQGFVGPWYRNLFRFLLLFSYIIPISLRVNLDMGKAVYGWMMMKDENIPGTVVRTSTIPEELGRLVYLLTDKTGTLTQNEMIFKRLHLGTVSYGADTMDEIQSHVRDSYSQMQSQAGGNNTGSTPLRKAQSSAPKVRKSVSSRIHEAVKAIVLCHNVTPVYESRAGVTEETEFAEADQDFSDENRTYQASSPDEVALVQWTESVGLTLVSRDLTSMQLKTPSGQVLSFCILQLFPFTSESKRMGVIVRDESTAEITFYMKGADVAMSPIVQYNDWLEEECGNMAREGLRTLVVAKKALTEEQYQDFESRYTQAKLSMHDRSLKVAAVVESLEREMELLCLTGVEDQLQADVRPTLEMLRNAGIKIWMLTGDKLETATCIAKSSHLVSRTQDIHIFRQVTSRGEAHLELNAFRRKHDCALVISGDSLEVCLKYYEHEFVELACQCPAVVCCRCSPTQKARIVTLLQQHTGRRTCAIGDGGNDVSMIQAADCGIGIEGKEGKQASLAADFSITQFRHIGRLLMVHGRNSYKRSAALGQFVMHRGLIISTMQAVFSSVFYFASVPLYQGFLMVGYATIYTMFPVFSLVLDQDVKPEMAMLYPELYKDLTKGRSLSFKTFLIWVLISIYQGGILMYGALVLFESEFVHVVAISFTALILTELLMVALTVRTWHWLMVVAEFLSLGCYVSSLAFLNEYFGIGRVSFGAFLDVAFITTVTFLWKVSAITVVSCLPLYVLKYLRRKLSPPSYCKLAS
|
7.6.2.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P40527};
|
endocytosis [GO:0006897]; phospholipid translocation [GO:0045332]; retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum [GO:0006890]
|
endosome [GO:0005768]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; magnesium ion binding [GO:0000287]
|
PF13246;PF00122;PF00702;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: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:21914794}; Multi-pass membrane protein {ECO:0000269|PubMed:21914794}. Note=Efficient exit from the endoplasmic reticulum does not require TMEM30A, nor TMEM30B.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1;
| null | null | null | null | null |
Homo sapiens (Human)
|
O43865
|
SAHH2_HUMAN
|
MSMPDAMPLPGVGEELKQAKEIEDAEKYSFMATVTKAPKKQIQFADDMQEFTKFPTKTGRRSLSRSISQSSTDSYSSAASYTDSSDDEVSPREKQQTNSKGSSNFCVKNIKQAEFGRREIEIAEQDMSALISLRKRAQGEKPLAGAKIVGCTHITAQTAVLIETLCALGAQCRWSACNIYSTQNEVAAALAEAGVAVFAWKGESEDDFWWCIDRCVNMDGWQANMILDDGGDLTHWVYKKYPNVFKKIRGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYGEVGKGCCAALKALGAIVYITEIDPICALQACMDGFRVVKLNEVIRQVDVVITCTGNKNVVTREHLDRMKNSCIVCNMGHSNTEIDVTSLRTPELTWERVRSQVDHVIWPDGKRVVLLAEGRLLNLSCSTVPTFVLSITATTQALALIELYNAPEGRYKQDVYLLPKKMDEYVASLHLPSFDAHLTELTDDQAKYLGLNKNGPFKPNYYRY
| null |
COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000269|PubMed:25237103}; Note=Binds 1 NAD(+) per subunit. {ECO:0000269|PubMed:25237103};
|
angiotensin-activated signaling pathway [GO:0038166]; apoptotic process [GO:0006915]; epithelial fluid transport [GO:0042045]; mitochondrion-endoplasmic reticulum membrane tethering [GO:1990456]; one-carbon metabolic process [GO:0006730]; positive regulation of sodium ion transport [GO:0010765]; protein export from nucleus [GO:0006611]; regulation of monoatomic anion transport [GO:0044070]; regulation of monoatomic ion transmembrane transporter activity [GO:0032412]; regulation of mRNA 3'-end processing [GO:0031440]; response to calcium ion [GO:0051592]; S-adenosylmethionine cycle [GO:0033353]
|
apical plasma membrane [GO:0016324]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; mitochondria-associated endoplasmic reticulum membrane [GO:0044233]
|
enzyme regulator activity [GO:0030234]; identical protein binding [GO:0042802]; RNA binding [GO:0003723]
|
PF05221;PF00670;
|
3.40.50.1480;3.40.50.720;
|
Adenosylhomocysteinase family
|
PTM: Phosphorylated at Ser/Thr residues between Ser-68 and Thr-72 in the PEST region: required for interaction with dATP-bound RRM1 and ITPR1. Phosphorylation at Ser-68 by PRKD1 and CAMK4 is required for further phosphorylations by CSNK1A1 (PubMed:16793548). Phosphorylation is induced by oxidative stress (PubMed:19224921). Probably phosphorylated by CAMK2A; phosphorylation at Ser-68 may be required for interaction with SLC9A3 (PubMed:20584908). Dephosphorylated in response to apoptotic stress conditions which causes translocation of both AHCYL1 and BCL2L10 from mitochondria-associated endoplasmic reticulum membranes and promotes apoptosis (PubMed:27995898). {ECO:0000269|PubMed:16793548, ECO:0000269|PubMed:19224921, ECO:0000269|PubMed:25237103, ECO:0000269|PubMed:27995898, ECO:0000305|PubMed:20584908}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:27995898, ECO:0000269|PubMed:28647132}. Cytoplasm, cytosol {ECO:0000269|PubMed:27995898}. Apical cell membrane {ECO:0000250|UniProtKB:B5DFN2}; Peripheral membrane protein {ECO:0000305}. Microsome {ECO:0000250|UniProtKB:Q80SW1}. Note=Associates with membranes when phosphorylated, probably through interaction with ITPR1 (By similarity). Localizes to mitochondria-associated endoplasmic reticulum membranes (MAMs) (PubMed:27995898). Localization to MAMs is greatly reduced under apoptotic stress conditions (PubMed:27995898). {ECO:0000250|UniProtKB:Q80SW1, ECO:0000269|PubMed:27995898}.
| null | null | null | null | null |
FUNCTION: Multifaceted cellular regulator which coordinates several essential cellular functions including regulation of epithelial HCO3(-) and fluid secretion, mRNA processing and DNA replication. Regulates ITPR1 sensitivity to inositol 1,4,5-trisphosphate, competing for the common binding site and acting as endogenous 'pseudoligand' whose inhibitory activity can be modulated by its phosphorylation status. Promotes the formation of contact points between the endoplasmic reticulum (ER) and mitochondria, facilitating transfer of Ca(2+) from the ER to mitochondria (PubMed:27995898). Under normal cellular conditions, functions cooperatively with BCL2L10 to limit ITPR1-mediated Ca(2+) release but, under apoptotic stress conditions, dephosphorylated which promotes dissociation of both AHCYL1 and BCL2L10 from mitochondria-associated endoplasmic reticulum membranes, inhibits BCL2L10 interaction with ITPR1 and leads to increased Ca(2+) transfer to mitochondria which promotes apoptosis (PubMed:27995898). In the pancreatic and salivary ducts, at resting state, attenuates inositol 1,4,5-trisphosphate-induced calcium release by interacting with ITPR1 (PubMed:16793548). When extracellular stimuli induce ITPR1 phosphorylation or inositol 1,4,5-trisphosphate production, dissociates from ITPR1 to interact with CFTR and SLC26A6, mediating their synergistic activation by calcium and cAMP that stimulates the epithelial secretion of electrolytes and fluid (By similarity). Also activates basolateral SLC4A4 isoform 1 to coordinate fluid and HCO3(-) secretion (PubMed:16769890). Inhibits the effect of STK39 on SLC4A4 and CFTR by recruiting PP1 phosphatase which activates SLC4A4, SLC26A6 and CFTR through dephosphorylation (By similarity). Mediates the induction of SLC9A3 surface expression produced by Angiotensin-2 (PubMed:20584908). Depending on the cell type, activates SLC9A3 in response to calcium or reverses SLC9A3R2-dependent calcium inhibition (PubMed:18829453). May modulate the polyadenylation state of specific mRNAs, both by controlling the subcellular location of FIP1L1 and by inhibiting PAPOLA activity, in response to a stimulus that alters its phosphorylation state (PubMed:19224921). Acts as a (dATP)-dependent inhibitor of ribonucleotide reductase large subunit RRM1, controlling the endogenous dNTP pool and ensuring normal cell cycle progression (PubMed:25237103). In vitro does not exhibit any S-adenosyl-L-homocysteine hydrolase activity (By similarity). {ECO:0000250|UniProtKB:B5DFN2, ECO:0000250|UniProtKB:Q80SW1, ECO:0000269|PubMed:16769890, ECO:0000269|PubMed:16793548, ECO:0000269|PubMed:18829453, ECO:0000269|PubMed:19224921, ECO:0000269|PubMed:20584908, ECO:0000269|PubMed:25237103, ECO:0000269|PubMed:27995898}.
|
Homo sapiens (Human)
|
O43866
|
CD5L_HUMAN
|
MALLFSLILAICTRPGFLASPSGVRLVGGLHRCEGRVEVEQKGQWGTVCDDGWDIKDVAVLCRELGCGAASGTPSGILYEPPAEKEQKVLIQSVSCTGTEDTLAQCEQEEVYDCSHDEDAGASCENPESSFSPVPEGVRLADGPGHCKGRVEVKHQNQWYTVCQTGWSLRAAKVVCRQLGCGRAVLTQKRCNKHAYGRKPIWLSQMSCSGREATLQDCPSGPWGKNTCNHDEDTWVECEDPFDLRLVGGDNLCSGRLEVLHKGVWGSVCDDNWGEKEDQVVCKQLGCGKSLSPSFRDRKCYGPGVGRIWLDNVRCSGEEQSLEQCQHRFWGFHDCTHQEDVAVICSG
| null | null |
apoptotic process [GO:0006915]; cellular defense response [GO:0006968]; immune system process [GO:0002376]; inflammatory response [GO:0006954]; positive regulation of complement-dependent cytotoxicity [GO:1903661]; regulation of complement activation [GO:0030449]; zymogen activation [GO:0031638]
|
blood microparticle [GO:0072562]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
serine-type endopeptidase activity [GO:0004252]
|
PF00530;
|
3.10.250.10;
| null |
PTM: Not N-glycosylated (PubMed:23236605). Probably not O-glycosylated (PubMed:23236605). {ECO:0000269|PubMed:23236605}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24223991, ECO:0000269|PubMed:24804991}. Cytoplasm {ECO:0000250|UniProtKB:Q9QWK4}. Note=Secreted by macrophages and circulates in the blood (PubMed:24223991, PubMed:24804991). Transported in the cytoplasm via CD36-mediated endocytosis (By similarity). {ECO:0000250|UniProtKB:Q9QWK4, ECO:0000269|PubMed:24223991, ECO:0000269|PubMed:24804991}.
| null | null | null | null | null |
FUNCTION: Secreted protein that acts as a key regulator of lipid synthesis: mainly expressed by macrophages in lymphoid and inflamed tissues and regulates mechanisms in inflammatory responses, such as infection or atherosclerosis. Able to inhibit lipid droplet size in adipocytes. Following incorporation into mature adipocytes via CD36-mediated endocytosis, associates with cytosolic FASN, inhibiting fatty acid synthase activity and leading to lipolysis, the degradation of triacylglycerols into glycerol and free fatty acids (FFA). CD5L-induced lipolysis occurs with progression of obesity: participates in obesity-associated inflammation following recruitment of inflammatory macrophages into adipose tissues, a cause of insulin resistance and obesity-related metabolic disease. Regulation of intracellular lipids mediated by CD5L has a direct effect on transcription regulation mediated by nuclear receptors ROR-gamma (RORC). Acts as a key regulator of metabolic switch in T-helper Th17 cells. Regulates the expression of pro-inflammatory genes in Th17 cells by altering the lipid content and limiting synthesis of cholesterol ligand of RORC, the master transcription factor of Th17-cell differentiation. CD5L is mainly present in non-pathogenic Th17 cells, where it decreases the content of polyunsaturated fatty acyls (PUFA), affecting two metabolic proteins MSMO1 and CYP51A1, which synthesize ligands of RORC, limiting RORC activity and expression of pro-inflammatory genes. Participates in obesity-associated autoimmunity via its association with IgM, interfering with the binding of IgM to Fcalpha/mu receptor and enhancing the development of long-lived plasma cells that produce high-affinity IgG autoantibodies (By similarity). Also acts as an inhibitor of apoptosis in macrophages: promotes macrophage survival from the apoptotic effects of oxidized lipids in case of atherosclerosis (PubMed:24295828). Involved in early response to microbial infection against various pathogens by acting as a pattern recognition receptor and by promoting autophagy (PubMed:16030018, PubMed:24223991, PubMed:24583716, PubMed:25713983). {ECO:0000250|UniProtKB:Q9QWK4, ECO:0000269|PubMed:16030018, ECO:0000269|PubMed:24223991, ECO:0000269|PubMed:24295828, ECO:0000269|PubMed:24583716, ECO:0000269|PubMed:25713983}.
|
Homo sapiens (Human)
|
O43868
|
S28A2_HUMAN
|
MEKASGRQSIALSTVETGTVNPGLELMEKEVEPEGSKRTDAQGHSLGDGLGPSTYQRRSRWPFSKARSFCKTHASLFKKILLGLLCLAYAAYLLAACILNFQRALALFVITCLVIFVLVHSFLKKLLGKKLTRCLKPFENSRLRLWTKWVFAGVSLVGLILWLALDTAQRPEQLIPFAGICMFILILFACSKHHSAVSWRTVFSGLGLQFVFGILVIRTDLGYTVFQWLGEQVQIFLNYTVAGSSFVFGDTLVKDVFAFQALPIIIFFGCVVSILYYLGLVQWVVQKVAWFLQITMGTTATETLAVAGNIFVGMTEAPLLIRPYLGDMTLSEIHAVMTGGFATISGTVLGAFIAFGVDASSLISASVMAAPCALASSKLAYPEVEESKFKSEEGVKLPRGKERNVLEAASNGAVDAIGLATNVAANLIAFLAVLAFINAALSWLGELVDIQGLTFQVICSYLLRPMVFMMGVEWTDCPMVAEMVGIKFFINEFVAYQQLSQYKNKRLSGMEEWIEGEKQWISVRAEIITTFSLCGFANLSSIGITLGGLTSIVPHRKSDLSKVVVRALFTGACVSLISACMAGILYVPRGAEADCVSFPNTSFTNRTYETYMCCRGLFQSTSLNGTNPPSFSGPWEDKEFSAMALTNCCGFYNNTVCA
| null | null |
adenosine transport [GO:0032238]; azole transmembrane transport [GO:0045117]; inosine transport [GO:0035340]; neurotransmitter transport [GO:0006836]; nucleobase-containing compound metabolic process [GO:0006139]; nucleoside transmembrane transport [GO:1901642]; purine nucleobase transmembrane transport [GO:1904823]; purine nucleoside transmembrane transport [GO:0015860]; pyrimidine-containing compound transmembrane transport [GO:0072531]; retina homeostasis [GO:0001895]; transport across blood-brain barrier [GO:0150104]; uridine transport [GO:0015862]; xenobiotic metabolic process [GO:0006805]; xenobiotic transmembrane transport [GO:0006855]
|
apicolateral plasma membrane [GO:0016327]; brush border membrane [GO:0031526]; coated vesicle [GO:0030135]; membrane [GO:0016020]; plasma membrane [GO:0005886]; vesicle membrane [GO:0012506]
|
azole transmembrane transporter activity [GO:1901474]; neurotransmitter transmembrane transporter activity [GO:0005326]; nucleoside:sodium symporter activity [GO:0005415]; purine nucleobase transmembrane transporter activity [GO:0005345]; purine nucleoside transmembrane transporter activity [GO:0015211]; pyrimidine- and adenosine-specific:sodium symporter activity [GO:0015389]; uridine transmembrane transporter activity [GO:0015213]
|
PF07670;PF07662;PF01773;
| null |
Concentrative nucleoside transporter (CNT) (TC 2.A.41) family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:9435697}; Multi-pass membrane protein {ECO:0000255}. Apicolateral cell membrane {ECO:0000269|PubMed:35307651}; Multi-pass membrane protein {ECO:0000255}. Note=Localized to the apicolateral membranes of Sertoli cells and vascular endothelial cells in testis. {ECO:0000269|PubMed:35307651}.
|
CATALYTIC ACTIVITY: Reaction=adenosine(out) + Na(+)(out) = adenosine(in) + Na(+)(in); Xref=Rhea:RHEA:69927, ChEBI:CHEBI:16335, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:10087507}; CATALYTIC ACTIVITY: Reaction=inosine(out) + Na(+)(out) = inosine(in) + Na(+)(in); Xref=Rhea:RHEA:69931, ChEBI:CHEBI:17596, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:10087507, ECO:0000269|PubMed:9435697}; CATALYTIC ACTIVITY: Reaction=guanosine(out) + Na(+)(out) = guanosine(in) + Na(+)(in); Xref=Rhea:RHEA:69935, ChEBI:CHEBI:16750, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:10087507}; CATALYTIC ACTIVITY: Reaction=Na(+)(out) + uridine(out) = Na(+)(in) + uridine(in); Xref=Rhea:RHEA:69887, ChEBI:CHEBI:16704, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:10087507, ECO:0000269|PubMed:21795683, ECO:0000269|PubMed:9435697};
| null | null | null | null |
FUNCTION: Sodium-dependent and purine-selective transporter (PubMed:10087507, PubMed:9435697). Exhibits the transport characteristics of the nucleoside transport system cif or N1 subtype (N1/cif) (selective for purine nucleosides and uridine) (PubMed:10087507, PubMed:21795683, PubMed:9435697). Plays a critical role in specific uptake and salvage of purine nucleosides in kidney and other tissues (PubMed:9435697). May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (Probable). {ECO:0000269|PubMed:10087507, ECO:0000269|PubMed:21795683, ECO:0000269|PubMed:9435697, ECO:0000305|PubMed:35307651}.
|
Homo sapiens (Human)
|
O43889
|
CREB3_HUMAN
|
MELELDAGDQDLLAFLLEESGDLGTAPDEAVRAPLDWALPLSEVPSDWEVDDLLCSLLSPPASLNILSSSNPCLVHHDHTYSLPRETVSMDLESESCRKEGTQMTPQHMEELAEQEIARLVLTDEEKSLLEKEGLILPETLPLTKTEEQILKRVRRKIRNKRSAQESRRKKKVYVGGLESRVLKYTAQNMELQNKVQLLEEQNLSLLDQLRKLQAMVIEISNKTSSSSTCILVLLVSFCLLLVPAMYSSDTRGSLPAEHGVLSRQLRALPSEDPYQLELPALQSEVPKDSTHQWLDGSDCVLQAPGNTSCLLHYMPQAPSAEPPLEWPFPDLFSEPLCRGPILPLQANLTRKGGWLPTGSPSVILQDRYSG
| null | null |
chemotaxis [GO:0006935]; cytoplasmic sequestering of transcription factor [GO:0042994]; DNA-templated transcription [GO:0006351]; endoplasmic reticulum unfolded protein response [GO:0030968]; establishment of viral latency [GO:0019043]; induction of positive chemotaxis [GO:0050930]; integrated stress response signaling [GO:0140467]; negative regulation of cell cycle [GO:0045786]; negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902236]; positive regulation of calcium ion transport [GO:0051928]; positive regulation of cell migration [GO:0030335]; positive regulation of deacetylase activity [GO:0090045]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of monocyte chemotaxis [GO:0090026]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of apoptotic process [GO:0042981]; regulation of cell growth [GO:0001558]; regulation of cell population proliferation [GO:0042127]; regulation of transcription by RNA polymerase II [GO:0006357]; release from viral latency [GO:0019046]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]
|
cAMP response element binding protein binding [GO:0008140]; CCR1 chemokine receptor binding [GO:0031726]; chromatin binding [GO:0003682]; 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]; identical protein binding [GO:0042802]; protein dimerization activity [GO:0046983]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific double-stranded DNA binding [GO:1990837]; transcription coregulator binding [GO:0001221]
|
PF00170;
|
1.20.5.170;
|
BZIP family, ATF subfamily
|
PTM: First proteolytically cleaved by site-1 protease (S1P) that generates membrane-associated N-terminus and a luminal C-terminus forms. The membrane-associated N-terminus form is further proteolytically processed probably by the site-2 protease (S2P) through a regulated intramembrane proteolysis (RIP), releasing the transcriptional active processed cyclic AMP-responsive element-binding protein 3 form, which is transported to the nucleus. The proteolytic cleavage is strongly induced during dendritic cell (DC) maturation and inhibited by DCSTAMP. That form is rapidly degraded. {ECO:0000269|PubMed:12138176, ECO:0000269|PubMed:16940180, ECO:0000269|PubMed:17054986, ECO:0000269|PubMed:18391022, ECO:0000269|PubMed:20546900}.; PTM: N-glycosylated. {ECO:0000269|PubMed:12138176, ECO:0000269|PubMed:16940180}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10623756, ECO:0000269|PubMed:12138176, ECO:0000269|PubMed:18391022}; Single-pass type II membrane protein {ECO:0000255, ECO:0000269|PubMed:12138176}. Golgi apparatus {ECO:0000269|PubMed:10623756}. Note=Colocalizes with HCFC1 in neuronal cell bodies of the trigeminal ganglia (PubMed:10623756). Colocalizes with DCSTAMP in the ER membrane of immature dendritic cell (DC) (PubMed:20546900). Colocalizes with CANX, CCR1, HCFC1 in the ER membrane (PubMed:10623756). {ECO:0000269|PubMed:10623756, ECO:0000269|PubMed:20546900}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Note=(Microbial infection) Sequestered into the cytoplasm by the HCV core protein. {ECO:0000269|PubMed:10675342}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:19779205}. Cytoplasm {ECO:0000269|PubMed:19779205}. Note=Predominantly in the nucleus (PubMed:19779205). Not associated with membranes (PubMed:19779205). {ECO:0000269|PubMed:19779205}.; SUBCELLULAR LOCATION: [Processed cyclic AMP-responsive element-binding protein 3]: Nucleus. Note=Upon RIP activation the transcriptional active processed cyclic AMP-responsive element-binding protein 3 form translocates into the nucleus. Detected in the nucleus upon dendritic cell maturation and RIP activation. Colocalizes with CREBRF in nuclear foci. Colocalizes with CREBZF in promyelocytic leukemia protein nuclear bodies (PML-NB). {ECO:0000269|PubMed:10675342, ECO:0000269|PubMed:15705566, ECO:0000269|PubMed:18391022, ECO:0000269|PubMed:20546900}.
| null | null | null | null | null |
FUNCTION: Endoplasmic reticulum (ER)-bound sequence-specific transcription factor that directly binds DNA and activates transcription (PubMed:10984507, PubMed:15845366, PubMed:16940180, PubMed:19779205, PubMed:9271389). Plays a role in the unfolded protein response (UPR), promoting cell survival versus ER stress-induced apoptotic cell death (PubMed:15845366, PubMed:16940180). Also involved in cell proliferation, migration and differentiation, tumor suppression and inflammatory gene expression. Acts as a positive regulator of LKN-1/CCL15-induced chemotaxis signaling of leukocyte cell migration (PubMed:15001559, PubMed:17296613, PubMed:19779205). Associates with chromatin to the HERPUD1 promoter (PubMed:16940180). Also induces transcriptional activation of chemokine receptors (PubMed:17296613, PubMed:18587271). {ECO:0000269|PubMed:10984507, ECO:0000269|PubMed:15001559, ECO:0000269|PubMed:15845366, ECO:0000269|PubMed:16940180, ECO:0000269|PubMed:17296613, ECO:0000269|PubMed:18587271, ECO:0000269|PubMed:19779205, ECO:0000269|PubMed:9271389}.; FUNCTION: (Microbial infection) Plays a role in human immunodeficiency virus type 1 (HIV-1) virus protein expression. {ECO:0000269|PubMed:17054986}.; FUNCTION: [Isoform 1]: (Microbial infection) May play a role as a cellular tumor suppressor that is targeted by the hepatitis C virus (HCV) core protein. {ECO:0000269|PubMed:10675342}.; FUNCTION: [Isoform 1]: (Microbial infection) Plays a role in herpes simplex virus-1 (HSV-1) latent infection and reactivation from latency. Represses the VP16-mediated transactivation of immediate early genes of the HSV-1 virus by sequestering host cell factor-1 HCFC1 in the ER membrane of sensory neurons, thereby preventing the initiation of the replicative cascade leading to latent infection. {ECO:0000269|PubMed:10623756, ECO:0000269|PubMed:15705566}.; FUNCTION: [Isoform 2]: Functions as a negative transcriptional regulator in ligand-induced transcriptional activation of the glucocorticoid receptor NR3C1 by recruiting and activating histone deacetylases (HDAC1, HDAC2 and HDAC6). Also decreases the acetylation level of histone H4. Does not promote the chemotactic activity of leukocyte cells. {ECO:0000269|PubMed:19779205}.; FUNCTION: [Processed cyclic AMP-responsive element-binding protein 3]: This is the transcriptionally active form that translocates to the nucleus and activates unfolded protein response (UPR) target genes during endoplasmic reticulum (ER) stress response. Binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AG][AG]-3') and C/EBP sequences present in many promoters to activate transcription of the genes. Binds to the unfolded protein response element (UPRE) consensus sequences sites. Binds DNA to the 5'-CCAC[GA]-3'half of ERSE II (5'-ATTGG-N-CCACG-3'). {ECO:0000269|PubMed:16940180}.; FUNCTION: [Processed cyclic AMP-responsive element-binding protein 3]: (Microbial infection) Activates transcription of genes required for reactivation of the latent HSV-1 virus. It's transcriptional activity is inhibited by CREBZF in a HCFC1-dependent manner, by the viral transactivator protein VP16. Binds DNA to the cAMP response element (CRE) (consensus: 5'-GTGACGT[AG][AG]-3') and C/EBP sequences present in many viral promoters. {ECO:0000269|PubMed:10623756}.; FUNCTION: [Processed cyclic AMP-responsive element-binding protein 3]: (Microbial infection) It's transcriptional activity is inhibited by CREBZF in a HCFC1-dependent manner, by the viral transactivator HCV core protein. {ECO:0000269|PubMed:10675342}.
|
Homo sapiens (Human)
|
O43895
|
XPP2_HUMAN
|
MARAHWGCCPWLVLLCACAWGHTKPVDLGGQDVRNCSTNPPYLPVTVVNTTMSLTALRQQMQTQNLSAYIIPGTDAHMNEYIGQHDERRAWITGFTGSAGTAVVTMKKAAVWTDSRYWTQAERQMDCNWELHKEVGTTPIVTWLLTEIPAGGRVGFDPFLLSIDTWESYDLALQGSNRQLVSITTNLVDLVWGSERPPVPNQPIYALQEAFTGSTWQEKVSGVRSQMQKHQKVPTAVLLSALEETAWLFNLRASDIPYNPFFYSYTLLTDSSIRLFANKSRFSSETLSYLNSSCTGPMCVQIEDYSQVRDSIQAYSLGDVRIWIGTSYTMYGIYEMIPKEKLVTDTYSPVMMTKAVKNSKEQALLKASHVRDAVAVIRYLVWLEKNVPKGTVDEFSGAEIVDKFRGEEQFSSGPSFETISASGLNAALAHYSPTKELNRKLSSDEMYLLDSGGQYWDGTTDITRTVHWGTPSAFQKEAYTRVLIGNIDLSRLIFPAATSGRMVEAFARRALWDAGLNYGHGTGHGIGNFLCVHEWPVGFQSNNIAMAKGMFTSIEPGYYKDGEFGIRLEDVALVVEAKTKYPGSYLTFEVVSFVPYDRNLIDVSLLSPEHLQYLNRYYQTIREKVGPELQRRQLLEEFEWLQQHTEPLAARAPDTASWASVLVVSTLAILGWSV
|
3.4.11.9
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q95333};
|
proteolysis [GO:0006508]
|
extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; membrane [GO:0016020]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
|
aminopeptidase activity [GO:0004177]; metal ion binding [GO:0046872]; metalloaminopeptidase activity [GO:0070006]
|
PF01321;PF16189;PF00557;PF16188;
|
3.90.230.10;3.40.350.10;
|
Peptidase M24B family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:15361070}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q95333}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q95333}.
|
CATALYTIC ACTIVITY: Reaction=Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.; EC=3.4.11.9; Evidence={ECO:0000269|PubMed:15361070};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.837 mM for Arg-Pro-Pro {ECO:0000269|PubMed:15361070}; KM=75 uM for Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg (bradykinin) {ECO:0000269|PubMed:15361070}; KM=56 uM for Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe (bradykinin[1-8]) {ECO:0000269|PubMed:15361070}; KM=18 uM for synthetic fluorescent substrate Lys(Dnp)-Pro-Pro-Gly-Phe-Ser-Pro-Lys(Abz)NH(2) {ECO:0000269|PubMed:15361070}; KM=20 uM for synthetic fluorescent substrate Lys(Dnp)-Pro-Pro-Gly-Lys(Abz)NH(2) {ECO:0000269|PubMed:15361070}; KM=19 uM for synthetic fluorescent substrate Lys(Dnp)-Pro-Pro-Lys(Abz)NH(2) {ECO:0000269|PubMed:15361070};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4. {ECO:0000269|PubMed:15361070};
| null |
FUNCTION: Membrane-bound metalloprotease which catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. May play a role in the metabolism of the vasodilator bradykinin. {ECO:0000269|PubMed:15361070}.
|
Homo sapiens (Human)
|
O43896
|
KIF1C_HUMAN
|
MAGASVKVAVRVRPFNARETSQDAKCVVSMQGNTTSIINPKQSKDAPKSFTFDYSYWSHTSTEDPQFASQQQVYRDIGEEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGRQEPGQQGIVPQLCEDLFSRVSENQSAQLSYSVEVSYMEIYCERVRDLLNPKSRGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRCHDQLTGLDSEKVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADMQSKKRKSDFIPYRDSVLTWLLKENLGGNSRTAMIAALSPADINYEETLSTLRYADRTKQIRCNAIINEDPNARLIRELQEEVARLRELLMAQGLSASALEGLKTEEGSVRGALPAVSSPPAPVSPSSPTTHNGELEPSFSPNTESQIGPEEAMERLQETEKIIAELNETWEEKLRKTEALRMEREALLAEMGVAVREDGGTVGVFSPKKTPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDMDIKLTGQFIREQHCLFRSIPQPDGEVVVTLEPCEGAETYVNGKLVTEPLVLKSGNRIVMGKNHVFRFNHPEQARLERERGVPPPPGPPSEPVDWNFAQKELLEQQGIDIKLEMEKRLQDLENQYRKEKEEADLLLEQQRLYADSDSGDDSDKRSCEESWRLISSLREQLPPTTVQTIVKRCGLPSSGKRRAPRRVYQIPQRRRLQGKDPRWATMADLKMQAVKEICYEVALADFRHGRAEIEALAALKMRELCRTYGKPDGPGDAWRAVARDVWDTVGEEEGGGAGSGGGSEEGARGAEVEDLRAHIDKLTGILQEVKLQNSSKDRELQALRDRMLRMERVIPLAQDHEDENEEGGEVPWAPPEGSEAAEEAAPSDRMPSARPPSPPLSSWERVSRLMEEDPAFRRGRLRWLKQEQLRLQGLQGSGGRGGGLRRPPARFVPPHDCKLRFPFKSNPQHRESWPGMGSGEAPTPLQPPEEVTPHPATPARRPPSPRRSHHPRRNSLDGGGRSRGAGSAQPEPQHFQPKKHNSYPQPPQPYPAQRPPGPRYPPYTTPPRMRRQRSAPDLKESGAAV
| null | null |
anterograde neuronal dense core vesicle transport [GO:1990048]; cytoskeleton-dependent intracellular transport [GO:0030705]; microtubule-based movement [GO:0007018]; retrograde neuronal dense core vesicle transport [GO:1990049]; retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum [GO:0006890]; vesicle-mediated transport [GO:0016192]
|
axon [GO:0030424]; axon cytoplasm [GO:1904115]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; kinesin complex [GO:0005871]; microtubule [GO:0005874]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cytoskeletal motor activity [GO:0003774]; microtubule binding [GO:0008017]; plus-end-directed microtubule motor activity [GO:0008574]; RNA binding [GO:0003723]
|
PF00498;PF00225;PF16183;
|
2.60.200.20;6.10.250.2520;3.40.850.10;
|
TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, Unc-104 subfamily
|
PTM: Phosphorylated on tyrosine residues. {ECO:0000269|PubMed:9685376}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Motor required for the retrograde transport of Golgi vesicles to the endoplasmic reticulum. Has a microtubule plus end-directed motility. {ECO:0000269|PubMed:9685376}.
|
Homo sapiens (Human)
|
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