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
MDLDLLDLNPRIIAAIKKAKLKSVKEVLHFSGPDLKRLTNLSSPEVWHLLRTASLHLRGSSILTALQLHQQKERFPTQHQRLSLGCPVLDALLRGGLPLDGITELAGRSSAGKTQLALQLCLAVQFPRQHGGLEAGAVYICTEDAFPHKRLQQLMAQQPRLRTDVPGELLQKLRFGSQIFIEHVADVDTLLECVNKKVPVLLSRGMARLVVIDSVAAPFRCEFDSQASAPRARHLQSLGATLRELSSAFQSPVLCINQVTEAMEEQGAAHGPLGFWDERVSPALGITWANQLLVRLLADRLREEEAALGCPARTLRVLSA...
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 ce...
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 recru...
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]; negat...
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 r...
Homo sapiens (Human)
O43548
TGM5_HUMAN
MAQGLEVALTDLQSSRNNVRHHTEEITVDHLLVRRGQAFNLTLYFRNRSFQPGLDNIIFVVETGPLPDLALGTRAVFSLARHHSPSPWIAWLETNGATSTEVSLCAPPTAAVGRYLLKIHIDSFQGSVTAYQLGEFILLFNPWCPEDAVYLDSEPQRQEYVMNDYGFIYQGSKNWIRPCPWNYGQFEDKIIDICLKLLDKSLHFQTDPATDCALRGSPVYVSRVVCAMINSNDDNGVLNGNWSENYTDGANPAEWTGSVAILKQWNATGCQPVRYGQCWVFAAVMCTVMRCLGIPTRVITNFDSGHDTDGNLIIDEYYDN...
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...
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
MQLPRWWELGDPCAWTGQGRGTRRMSPATTGTFLLTVYSIFSKVHSDRNVYPSAGVLFVHVLEREYFKGEFPPYPKPGEISNDPITFNTNLMGYPDRPGWLRYIQRTPYSDGVLYGSPTAENVGKPTIIEITAYNRRTFETARHNLIINIMSAEDFPLPYQAEFFIKNMNVEEMLASEVLGDFLGAVKNVWQPERLNAINITSALDRGGRVPLPINDLKEGVYVMVGADVPFSSCLREVENPQNQLRCSQEMEPVITCDKKFRTQFYIDWCKISLVDKTKQVSTYQEVIRGEGILPDGGEYKPPSDSLKSRDYYTDFLIT...
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]; positiv...
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:1075430...
Homo sapiens (Human)
O43559
FRS3_HUMAN
MGSCCSCLNRDSVPDNHPTKFKVTNVDDEGVELGSGVMELTQSELVLHLHRREAVRWPYLCLRRYGYDSNLFSFESGRRCQTGQGIFAFKCSRAEEIFNLLQDLMQCNSINVMEEPVIITRNSHPAELDLPRAPQPPNALGYTVSSFSNGCPGEGPRFSAPRRLSTSSLRHPSLGEESTHALIAPDEQSHTYVNTPASEDDHRRGRHCLQPLPEGQAPFLPQARGPDQRDPQVFLQPGQVKFVLGPTPARRHMVKCQGLCPSLHDPPHHNNNNEAPSECPAQPKCTYENVTGGLWRGAGWRLSPEEPGWNGLAHRRAALL...
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...
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. Phosphorylat...
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 i...
Homo sapiens (Human)
O43566
RGS14_HUMAN
MPGKPKHLGVPNGRMVLAVSDGELSSTTGPQGQGEGRGSSLSIHSLPSGPSSPFPTEEQPVASWALSFERLLQDPLGLAYFTEFLKKEFSAENVTFWKACERFQQIPASDTQQLAQEARNIYQEFLSSQALSPVNIDRQAWLGEEVLAEPRPDMFRAQQLQIFNLMKFDSYARFVKSPLYRECLLAEAEGRPLREPGSSRLGSPDATRKKPKLKPGKSLPLGVEELGQLPPVEGPGGRPLRKSFRRELGGTANAALRRESQGSLNSSASLDLGFLAFVSSKSESHRKSLGSTEGESESRPGKYCCVYLPDGTASLALARP...
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]; nega...
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...
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 ...
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}. Cy...
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...
Homo sapiens (Human)
O43567
RNF13_HUMAN
MLLSIGMLMLSATQVYTILTVQLFAFLNLLPVEADILAYNFENASQTFDDLPARFGYRLPAEGLKGFLINSKPENACEPIVPPPVKDNSSGTFIVLIRRLDCNFDIKVLNAQRAGYKAAIVHNVDSDDLISMGSNDIEVLKKIDIPSVFIGESSANSLKDEFTYEKGGHLILVPEFSLPLEYYLIPFLIIVGICLILIVIFMITKFVQDRHRARRNRLRKDQLKKLPVHKFKKGDEYDVCAICLDEYEDGDKLRILPCSHAYHCKCVDPWLTKTKKTCPVCKQKVVPSQGDSDSDTDSSQEENEVTEHTPLLRPLASVSA...
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]; nucleopl...
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...
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...
Homo sapiens (Human)
O43570
CAH12_HUMAN
MPRRSLHAAAVLLLVILKEQPSSPAPVNGSKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQGLQSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFSHLQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPREMINNFRQVQKFDERLVYTSFSQVQVCTAAGLSLGIILSLALAGILGICIVV...
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
MRGAGPSPRQSPRTLRPDPGPAMSFFRRKVKGKEQEKTSDVKSIKASISVHSPQKSTKNHALLEAAGPSHVAINAISANMDSFSSSRTATLKKQPSHMEAAHFGDLGRSCLDYQTQETKSSLSKTLEQVLHDTIVLPYFIQFMELRRMEHLVKFWLEAESFHSTTWSRIRAHSLNTVKQSSLAEPVSPSKKHETTASFLTDSLDKRLEDSGSAQLFMTHSEGIDLNNRTNSTQNHLLLSQECDSAHSLRLEMARAGTHQVSMETQESSSTLTVASRNSPASPLKELSGKLMKSIEQDAVNTFTKYISPDAAKPIPITEAM...
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...
Homo sapiens (Human)
O43581
SYT7_HUMAN
MYRDPEAASPGAPSRDVLLVSAIITVSLSVTVVLCGLCHWCQRKLGKRYKNSLETVGTPDSGRGRSEKKAIKLPAGGKAVNTAPVPGQTPHDESDRRTEPRSSVSDLVNSLTSEMLMLSPGSEEDEAHEGCSRENLGRIQFSVGYNFQESTLTVKIMKAQELPAKDFSGTSDPFVKIYLLPDKKHKLETKVKRKNLNPHWNETFLFEGFPYEKVVQRILYLQVLDYDRFSRNDPIGEVSIPLNKVDLTQMQTFWKDLKPCSDGSGSRGELLLSLCYNPSANSIIVNIIKARNLKAMDIGGTSDPYVKVWLMYKDKRVEKK...
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 e...
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 ...
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-p...
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 exocytos...
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 ABCE...
Homo sapiens (Human)
O43586
PPIP1_HUMAN
MMPQLQFKDAFWCRDFTAHTGYEVLLQRLLDGRKMCKDMEELLRQRAQAEERYGKELVQIARKAGGQTEINSLRASFDSLKQQMENVGSSHIQLALTLREELRSLEEFRERQKEQRKKYEAVMDRVQKSKLSLYKKAMESKKTYEQKCRDADDAEQAFERISANGHQKQVEKSQNKARQCKDSATEAERVYRQSIAQLEKVRAEWEQEHRTTCEAFQLQEFDRLTILRNALWVHSNQLSMQCVKDDELYEEVRLTLEGCSIDADIDSFIQAKSTGTEPPAPVPYQNYYDREVTPLTSSPGIQPSCGMIKRFSGLLHGSPK...
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 a...
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|Pub...
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 c...
Homo sapiens (Human)
O43592
XPOT_HUMAN
MDEQALLGLNPNADSDFRQRALAYFEQLKISPDAWQVCAEALAQRTYSDDHVKFFCFQVLEHQVKYKYSELTTVQQQLIRETLISWLQAQMLNPQPEKTFIRNKAAQVFALLFVTEYLTKWPKFFFDILSVVDLNPRGVDLYLRILMAIDSELVDRDVVHTSEEARRNTLIKDTMREQCIPNLVESWYQILQNYQFTNSEVTCQCLEVVGAYVSWIDLSLIANDRFINMLLGHMSIEVLREEACDCLFEVVNKGMDPVDKMKLVESLCQVLQSAGFFSIDQEEDVDFLARFSKLVNGMGQSLIVSWSKLIKNGDIKNAQE...
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, disa...
Homo sapiens (Human)
O43593
HAIR_HUMAN
MESTPSFLKGTPTWEKTAPENGIVRQEPGSPPRDGLHHGPLCLGEPAPFWRGVLSTPDSWLPPGFPQGPKDMLPLVEGEGPQNGERKVNWLGSKEGLRWKEAMLTHPLAFCGPACPPRCGPLMPEHSGGHLKSDPVAFRPWHCPFLLETKILERAPFWVPTCLPPYLVSGLPPEHPCDWPLTPHPWVYSGGQPKVPSAFSLGSKGFYYKDPSIPRLAKEPLAAAEPGLFGLNSGGHLQRAGEAERPSLHQRDGEMGAGRQQNPCPLFLGQPDTVPWTSWPACPPGLVHTLGNVWAGPGDGNLGYQLGPPATPRCPSPEPP...
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:29...
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...
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:108...
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)....
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; Xre...
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...
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)...
Homo sapiens (Human)
O43602
DCX_HUMAN
MELDFGHFDERDKTSRNMRGSRMNGLPSPTHSAHCSFYRTRTLQALSNEKKAKKVRFYRNGDRYFKGIVYAVSSDRFRSFDALLADLTRSLSDNINLPQGVRYIYTIDGSRKIGSMDELEEGESYVCSSDNFFKKVEYTKNVNPNWSVNVKTSANMKAPQSLASSNSAQARENKDFVRPKLVTIIRSGVKPRKAVRVLLNKKTAHSFEQVLTDITEAIKLETGVVKKLYTLDGKQVTCLHDFFGDDDVFIACGPEKFRYAQDDFSLDENECRVMKGNPSATAGPKASPTPQKTSAKSPGPMRRSKSPADSGNDQDANGTS...
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:...
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...
Homo sapiens (Human)
O43603
GALR2_HUMAN
MNVSGCPGAGNASQAGGGGGWHPEAVIVPLLFALIFLVGTVGNTLVLAVLLRGGQAVSTTNLFILNLGVADLCFILCCVPFQATIYTLDGWVFGSLLCKAVHFLIFLTMHASSFTLAAVSLDRYLAIRYPLHSRELRTPRNALAAIGLIWGLSLLFSGPYLSYYRQSQLANLTVCHPAWSAPRRRAMDICTFVFSYLLPVLVLGLTYARTLRYLWRAVDPVAAGSGARRAKRKVTRMILIVAALFCLCWMPHHALILCVWFGQFPLTRATYALRILSHLVSYANSCVNPIVYALVSKHFRKGFRTICAGLLGRAPGRASG...
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 ...
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|...
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]...
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 regula...
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 fibrobla...
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 sig...
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:O55...
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, horm...
Homo sapiens (Human)
O43613
OX1R_HUMAN
MEPSATPGAQMGVPPGSREPSPVPPDYEDEFLRYLWRDYLYPKQYEWVLIAAYVAVFVVALVGNTLVCLAVWRNHHMRTVTNYFIVNLSLADVLVTAICLPASLLVDITESWLFGHALCKVIPYLQAVSVSVAVLTLSFIALDRWYAICHPLLFKSTARRARGSILGIWAVSLAIMVPQAAVMECSSVLPELANRTRLFSVCDERWADDLYPKIYHSCFFIVTYLAPLGLMAMAYFQIFRKLWGRQIPGTTSALVRNWKRPSDQLGDLEQGLSGEPQPRARAFLAEVKQMRARRKTAKMLMVVLLVFALCYLPISVLNVL...
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:9...
Homo sapiens (Human)
O43614
OX2R_HUMAN
MSGTKLEDSPPCRNWSSASELNETQEPFLNPTDYDDEEFLRYLWREYLHPKEYEWVLIAGYIIVFVVALIGNVLVCVAVWKNHHMRTVTNYFIVNLSLADVLVTITCLPATLVVDITETWFFGQSLCKVIPYLQTVSVSVSVLTLSCIALDRWYAICHPLMFKSTAKRARNSIVIIWIVSCIIMIPQAIVMECSTVFPGLANKTTLFTVCDERWGGEIYPKMYHICFFLVTYMAPLCLMVLAYLQIFRKLWCRQIPGTSSVVQRKWKPLQPVSQPRGPGQPTKSRMSAVAAEIKQIRARRKTARMLMIVLLVFAICYLPI...
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 [...
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
MAAAALRSGWCRCPRRCLGSGIQFLSSHNLPHGSTYQMRRPGGELPLSKSYSSGNRKGFLSGLLDNVKQELAKNKEMKESIKKFRDEARRLEESDVLQEARRKYKTIESETVRTSEVLRKKLGELTGTVKESLHEVSKSDLGRKIKEGVEEAAKTAKQSAESVSKGGEKLGRTAAFRALSQGVESVKKEIDDSVLGQTGPYRRPQRLRKRTEFAGDKFKEEKVFEPNEEALGVVLHKDSKWYQQWKDFKENNVVFNRFFEMKMKYDESDNAFIRASRALTDKVTDLLGGLFSKTEMSEVLTEILRVDPAFDKDRFLKQCE...
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 ...
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 d...
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...
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 ...
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 e...
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 [G...
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}. No...
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 limi...
Homo sapiens (Human)
O43639
NCK2_HUMAN
MTEEVIVIAKWDYTAQQDQELDIKKNERLWLLDDSKTWWRVRNAANRTGYVPSNYVERKNSLKKGSLVKNLKDTLGLGKTRRKTSARDASPTPSTDAEYPANGSGADRIYDLNIPAFVKFAYVAEREDELSLVKGSRVTVMEKCSDGWWRGSYNGQIGWFPSNYVLEEVDEAAAESPSFLSLRKGASLSNGQGSRVLHVVQTLYPFSSVTEEELNFEKGETMEVIEKPENDPEWWKCKNARGQVGLVPKNYVVVLSDGPALHPAHAPQISYTGPSSSGRFAGREWYYGNVTRHQAECALNERGVEGDFLIRDSESSPSDF...
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 re...
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:0...
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:bet...
Homo sapiens (Human)
O43660
PLRG1_HUMAN
MVEEVQKHSVHTLVFRSLKRTHDMFVADNGKPVPLDEESHKRKMAIKLRNEYGPVLHMPTSKENLKEKGPQNATDSYVHKQYPANQGQEVEYFVAGTHPYPPGPGVALTADTKIQRMPSESAAQSLAVALPLQTKADANRTAPSGSEYRHPGASDRPQPTAMNSIVMETGNTKNSALMAKKAPTMPKPQWHPPWKLYRVISGHLGWVRCIAVEPGNQWFVTGSADRTIKIWDLASGKLKLSLTGHISTVRGVIVSTRSPYLFSCGEDKQVKCWDLEYNKVIRHYHGHLSAVYGLDLHPTIDVLVTCSRDSTARIWDVRTK...
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 ...
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, in...
Homo sapiens (Human)
O43663
PRC1_HUMAN
MRRSEVLAEESIVCLQKALNHLREIWELIGIPEDQRLQRTEVVKKHIKELLDMMIAEEESLKERLIKSISVCQKELNTLCSELHVEPFQEEGETTILQLEKDLRTQVELMRKQKKERKQELKLLQEQDQELCEILCMPHYDIDSASVPSLEELNQFRQHVTTLRETKASRREEFVSIKRQIILCMEALDHTPDTSFERDVVCEDEDAFCLSLENIATLQKLLRQLEMQKSQNEAVCEGLRTQIRELWDRLQIPEEEREAVATIMSGSKAKVRKALQLEVDRLEELKMQNMKKVIEAIRVELVQYWDQCFYSQEQRQAFAP...
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]; spindl...
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. Dephosphory...
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=Coloca...
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 spindl...
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:1...
Homo sapiens (Human)
O43670
ZN207_HUMAN
MGRKKKKQLKPWCWYCNRDFDDEKILIQHQKAKHFKCHICHKKLYTGPGLAIHCMQVHKETIDAVPNAIPGRTDIELEIYGMEGIPEKDMDERRRLLEQKTQESQKKKQQDDSDEYDDDDSAASTSFQPQPVQPQQGYIPPMAQPGLPPVPGAPGMPPGIPPLMPGVPPLMPGMPPVMPGMPPGMMPMGGMMPPGPGIPPLMPGMPPGMPPPVPRPGIPPMTQAQAVSAPGILNRPPAPTATVPAPQPPVTKPLFPSAGQMGTPVTSSSTASSNSESLSASSKALFPSTAQAQAAVQGPVGTDFKPLNSTPATTTEPPKP...
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:0007...
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...
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. Coacerva...
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. ...
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. ...
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. ...
Homo sapiens (Human)
O43679
LDB2_HUMAN
MSSTPHDPFYSSPFGPFYRRHTPYMVQPEYRIYEMNKRLQSRTEDSDNLWWDAFATEFFEDDATLTLSFCLEDGPKRYTIGRTLIPRYFSTVFEGGVTDLYYILKHSKESYHNSSITVDCDQCTMVTQHGKPMFTKVCTEGRLILEFTFDDLMRIKTWHFTIRQYRELVPRSILAMHAQDPQVLDQLSKNITRMGLTNFTLNYLRLCVILEPMQELMSRHKTYNLSPRDCLKTCLFQKWQRMVAPPAEPTRQPTTKRRKRKNSTSSTSNSSAGNNANSTGSKKKTTAANLSLSSQVPDVMVVGEPTLMGGEFGDEDERLI...
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 ...
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:00...
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 ...
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
MAAGVAGWGVEAEEFEDAPDVEPLEPTLSNIIEQRSLKWIFVGGKGGVGKTTCSCSLAVQLSKGRESVLIISTDPAHNISDAFDQKFSKVPTKVKGYDNLFAMEIDPSLGVAELPDEFFEEDNMLSMGKKMMQEAMSAFPGIDEAMSYAEVMRLVKGMNFSVVVFDTAPTGHTLRLLNFPTIVERGLGRLMQIKNQISPFISQMCNMLGLGDMNADQLASKLEETLPVIRSVSEQFKDPEQTTFICVCIAEFLSLYETERLIQELAKCKIDTHNIIVNQLVFPDPEKPCKMCEARHKIQAKYLDQMEDLYEDFHIVKLPL...
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, ...
Homo sapiens (Human)
O43683
BUB1_HUMAN
MDTPENVLQMLEAHMQSYKGNDPLGEWERYIQWVEENFPENKEYLITLLEHLMKEFLDKKKYHNDPRFISYCLKFAEYNSDLHQFFEFLYNHGIGTLSSPLYIAWAGHLEAQGELQHASAVLQRGIQNQAEPREFLQQQYRLFQTRLTETHLPAQARTSEPLHNVQVLNQMITSKSNPGNNMACISKNQGSELSGVISSACDKESNMERRVITISKSEYSVHSSLASKVDVEQVVMYCKEKLIRGESEFSFEELRAQKYNQRRKHEQWVNEDRHYMKRKEANAFEEQLLKQKMDELHKKLHQVVETSHEDLPASQERSEV...
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,...
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 inte...
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...
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-[pr...
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, B...
Homo sapiens (Human)
O43684
BUB3_HUMAN
MTGSNEFKLNQPPEDGISSVKFSPNTSQFLLVSSWDTSVRLYDVPANSMRLKYQHTGAVLDCAFYDPTHAWSGGLDHQLKMHDLNTDQENLVGTHDAPIRCVEYCPEVNVMVTGSWDQTVKLWDPRTPCNAGTFSQPEKVYTLSVSGDRLIVGTAGRRVLVWDLRNMGYVQQRRESSLKYQTRCIRAFPNKQGYVLSSIEGRVAVEYLDPSPEVQKKKYAFKCHRLKENNIEQIYPVNAISFHNIHNTFATGGSDGFVNIWDPFNKKRLCQFHRYPTSIASLAFSNDGTTLAIASSYMYEMDDTEHPEDGIFIRQVTDAE...
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 mei...
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]; prote...
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 i...
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 membr...
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}; Phy...
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....
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 ...
Homo sapiens (Human)
O43699
SIGL6_HUMAN
MQGAQEASASEMLPLLLPLLWAGALAQERRFQLEGPESLTVQEGLCVLVPCRLPTTLPASYYGYGYWFLEGADVPVATNDPDEEVQEETRGRFHLLWDPRRKNCSLSIRDARRRDNAAYFFRLKSKWMKYGYTSSKLSVRVMALTHRPNISIPGTLESGHPSNLTCSVPWVCEQGTPPIFSWMSAAPTSLGPRTTQSSVLTITPRPQDHSTNLTCQVTFPGAGVTMERTIQLNVSYAPQKVAISIFQGNSAAFKILQNTSSLPVLEGQALRLLCDADGNPPAHLSWFQGFPALNATPISNTGVLELPQVGSAEEGDFTCR...
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:00...
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,...
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'...
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:2808...
Homo sapiens (Human)
O43707
ACTN4_HUMAN
MVDYHAANQSYQYGPSSAGNGAGGGGSMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYEKLASDLLEWIRRTIPWLEDRV...
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-c...
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]; perinuc...
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...
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|UniPr...
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 n...
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:CHE...
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 oxy...
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...
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:258...
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 ...
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 ...
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 r...
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 mitochondr...
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, C...
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
MSGTNLDGNDEFDEQLRMQELYGDGKDGDTQTDAGGEPDSLGQQPTDTPYEWDLDKKAWFPKITEDFIATYQANYGFSNDGASSSTANVEDVHARTAEEPPQEKAPEPTDARKKGEKRKAESGWFHVEEDRNTNVYVSGLPPDITVDEFIQLMSKFGIIMRDPQTEEFKVKLYKDNQGNLKGDGLCCYLKRESVELALKLLDEDEIRGYKLHVEVAKFQLKGEYDASKKKKKCKDYKKKLSMQQKQLDWRPERRAGPSRMRHERVVIIKNMFHPMDFEDDPLVLNEIREDLRVECSKFGQIRKLLLFDRHPDGVASVSFR...
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 ...
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:00002...
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
MPPQLQETRMNRSIPVEVDESEPYPSQLLKPIPEYSPEEESEPPAPNIRNMAPNSLSAPTMLHNSSGDFSQAHSTLKLANHQRPVSRQVTCLRTQVLEDSEDSFCRRHPGLGKAFPSGCSAVSEPASESVVGALPAEHQFSFMEKRNQWLVSQLSAASPDTGHDSDKSDQSLPNASADSLGGSQEMVQRPQPHRNRAGLDLPTIDTGYDSQPQDVLGIRQLERPLPLTSVCYPQDLPRPLRSREFPQFEPQRYPACAQMLPPNLSPHAPWNYHYHCPGSPDHQVPYGHDYPRAAYQQVIQPALPGQPLPGASVRGLHPVQ...
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 imm...
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...
Homo sapiens (Human)
O43739
CYH3_HUMAN
MDEDGGGEGGGVPEDLSLEEREELLDIRRRKKELIDDIERLKYEIAEVMTEIDNLTSVEESKTTQRNKQIAMGRKKFNMDPKKGIQFLIENDLLQSSPEDVAQFLYKGEGLNKTVIGDYLGERDEFNIKVLQAFVELHEFADLNLVQALRQFLWSFRLPGEAQKIDRMMEAFASRYCLCNPGVFQSTDTCYVLSFAIIMLNTSLHNHNVRDKPTAERFIAMNRGINEGGDLPEELLRNLYESIKNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVE...
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 membran...
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...
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 re...
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 nucle...
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 ...
Homo sapiens (Human)
O43747
AP1G1_HUMAN
MPAPIRLRELIRTIRTARTQAEEREMIQKECAAIRSSFREEDNTYRCRNVAKLLYMHMLGYPAHFGQLECLKLIASQKFTDKRIGYLGAMLLLDERQDVHLLMTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALCAVHVIRKVPELMEMFLPATKNLLNEKNHGVLHTSVVLLTEMCERSPDMLAHFRKLVPQLVRILKNLIMSGYSPEHDVSGISDPFLQVRILRLLRILGRNDDDSSEAMNDILAQVATNTETSKNVGNAILYETVLTIMDIKSESGLRVLAINILGRFLLNN...
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 organ...
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...
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, perinuc...
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 ...
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:...
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]; rec...
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}; ...
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 recy...
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:000026...
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 simi...
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 wit...
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:0...
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 dou...
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 motilit...
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 ...
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 membra...
Homo sapiens (Human)
O43766
LIAS_HUMAN
MSLRCGDAARTLGPRVFGRYFCSPVRPLSSLPDKKKELLQNGPDLQDFVSGDLADRSTWDEYKGNLKRQKGERLRLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGEYATATATIMLMGDTCTRGCRFCSVKTARNPPPLDASEPYNTAKAIAEWGLDYVVLTSVDRDDMPDGGAEHIAKTVSYLKERNPKILVECLTPDFRGDLKAIEKVALSGLDVYAHNVETVPELQSKVRDPRANFDQSLRVLKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCLTLGQYMQPTRRHLKVE...
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...
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 [...
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 activi...
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)-ca...
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...
Homo sapiens (Human)
O43776
SYNC_HUMAN
MVLAELYVSDREGSDATGDGTKEKPFKTGLKALMTVGKEPFPTIYVDSQKENERWNVISKSQLKNIKKMWHREQMKSESREKKEAEDSLRREKNLEEAKKITIKNDPSLPEPKCVKIGALEGYRGQRVKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVLADELCQCYNGVLLSTESSVAVYGMLNLTPKGKQAPGGHELSCDFWELIGLAPAGGADNLINEESDVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQS...
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...
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...
Homo sapiens (Human)
O43781
DYRK3_HUMAN
MGGTARGPGRKDAGPPGAGLPPQQRRLGDGVYDTFMMIDETKCPPCSNVLCNPSEPPPPRRLNMTTEQFTGDHTQHFLDGGEMKVEQLFQEFGNRKSNTIQSDGISDSEKCSPTVSQGKSSDCLNTVKSNSSSKAPKVVPLTPEQALKQYKHHLTAYEKLEIINYPEIYFVGPNAKKRHGVIGGPNNGGYDDADGAYIHVPRDHLAYRYEVLKIIGKGSFGQVARVYDHKLRQYVALKMVRNEKRFHRQAAEEIRILEHLKKQDKTGSMNVIHMLESFTFRNHVCMAFELLSIDLYELIKKNKFQGFSVQLVRKFAQSIL...
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:190...
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 pr...
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}. Cyto...
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:000026...
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 th...
Homo sapiens (Human)
O43790
KRT86_HUMAN
MTCGSYCGGRAFSCISACGPRPGRCCITAAPYRGISCYRGLTGGFGSHSVCGGFRAGSCGRSFGYRSGGVCGPSPPCITTVSVNESLLTPLNLEIDPNAQCVKQEEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFYQNRECCQSNLEPLFEGYIETLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFLRRLYEEEIRVLQSHISDTSVVVKLDNSRDLNMDCIIAEIKAQYDDIVTRSRAEAESWYRSKCEEMKATVIRHGETLRRTKE...
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
MSRVPSPPPPAEMSSGPVAESWCYTQIKVVKFSYMWTINNFSFCREEMGEVIKSSTFSSGANDKLKWCLRVNPKGLDEESKDYLSLYLLLVSCPKSEVRAKFKFSILNAKGEETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQDSVNISGQNTMNMVKVPECRLADELGGLWENSRFTDCCLCVAGQEFQAHKAILAARSPVFSAMFEHEMEESKKNRVEINDVEPEVFKEMMCFIYTGKAPNLDKMADDLLAAADKYALERLKVMCEDALCSNLSVENAAEILILADLHSADQLKTQ...
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 GL...
Homo sapiens (Human)
O43795
MYO1B_HUMAN
MAKMEVKTSLLDNMIGVGDMVLLEPLNEETFINNLKKRFDHSEIYTYIGSVVISVNPYRSLPIYSPEKVEEYRNRNFYELSPHIFALSDEAYRSLRDQDKDQCILITGESGAGKTEASKLVMSYVAAVCGKGAEVNQVKEQLLQSNPVLEAFGNAKTVRNDNSSRFGKYMDIEFDFKGDPLGGVISNYLLEKSRVVKQPRGERNFHVFYQLLSGASEELLNKLKLERDFSRYNYLSLDSAKVNGVDDAANFRTVRNAMQIVGFMDHEAESVLAVVAAVLKLGNIEFKPESRVNGLDESKIKDKNELKEICELTGIDQSVL...
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:000590...
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:253906...
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 t...
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];...
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:...
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 ...
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 regu...
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 w...
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, P...
Homo sapiens (Human)
O43813
LANC1_HUMAN
MAQRAFPNPYADYNKSLAEGYFDAAGRLTPEFSQRLTNKIRELLQQMERGLKSADPRDGTGYTGWAGIAVLYLHLYDVFGDPAYLQLAHGYVKQSLNCLTKRSITFLCGDAGPLAVAAVLYHKMNNEKQAEDCITRLIHLNKIDPHAPNEMLYGRIGYIYALLFVNKNFGVEKIPQSHIQQICETILTSGENLARKRNFTAKSPLMYEWYQEYYVGAAHGLAGIYYYLMQPSLQVSQGKLHSLVKPSVDYVCQLKFPSGNYPPCIGDNRDLLVHWCHGAPGVIYMLIQAYKVFREEKYLCDAYQCADVIWQYGLLKKGYG...
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-dinit...
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 antio...
Homo sapiens (Human)
O43815
STRN_HUMAN
MDEQAGPGVFFSNNHPGAGGAKGLGPLAEAAAAGDGAAAAGAARAQYSLPGILHFLQHEWARFEVERAQWEVERAELQAQIAFLQGERKGQENLKKDLVRRIKMLEYALKQERAKYHKLKYGTELNQGDMKPPSYDSDEGNETEVQPQQNSQLMWKQGRQLLRQYLQEVGYTDTILDVKSKRVRALLGFSSDVTDREDDKNQDSVVNGTEAEVKETAMIAKSELTDSASVLDNFKFLESAAADFSDEDEDDDVDGREKSVIDTSTIVRKKALPDSGEDRDTKEALKEFDFLVTSEEGDNESRSAGDGTDWEKEDQCLMPE...
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:P70...
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 an...
Homo sapiens (Human)
O43818
U3IP2_HUMAN
MSATAAARKRGKPASGAGAGAGAGKRRRKADSAGDRGKSKGGGKMNEEISSDSESESLAPRKPEEEEEEELEETAQEKKLRLAKLYLEQLRQQEEEKAEARAFEEDQVAGRLKEDVLEQRGRLQKLVAKEIQAPASADIRVLRGHQLSITCLVVTPDDSAIFSAAKDCSIIKWSVESGRKLHVIPRAKKGAEGKPPGHSSHVLCMAISSDGKYLASGDRSKLILIWEAQSCQHLYTFTGHRDAVSGLAFRRGTHQLYSTSHDRSVKVWNVAENSYVETLFGHQDAVAALDALSRECCVTAGGRDGTVRVWKIPEESQLVF...
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 ...
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 i...
Homo sapiens (Human)
O43820
HYAL3_HUMAN
MTTQLGPALVLGVALCLGCGQPLPQVPERPFSVLWNVPSAHCEARFGVHLPLNALGIIANRGQHFHGQNMTIFYKNQLGLYPYFGPRGTAHNGGIPQALPLDRHLALAAYQIHHSLRPGFAGPAVLDWEEWCPLWAGNWGRRRAYQAASWAWAQQVFPDLDPQEQLYKAYTGFEQAARALMEDTLRVAQALRPHGLWGFYHYPACGNGWHSMASNYTGRCHAATLARNTQLHWLWAASSALFPSIYLPPRLPPAHHQAFVRHRLEEAFRVALVGHRHPLPVLAYVRLTHRRSGRFLSQDDLVQSIGVSAALGAAGVVLWG...
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 regul...
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-de...
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 c...
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...
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
MDQGYGGYGAWSAGPANTQGAYGTGVASWQGYENYNYYGAQNTSVTTGATYSYGPASWEAAKANDGGLAAGAPAMHMASYGPEPCTDNSDSLIAKINQRLDMMSKEGGRGGSGGGGEGIQDRESSFRFQPFESYDSRPCLPEHNPYRPSYSYDYEFDLGSDRNGSFGGQYSECRDPARERGSLDGFMRGRGQGRFQDRSNPGTFMRSDPFVPPAASSEPLSTPWNELNYVGGRGLGGPSPSRPPPSLFSQSMAPDYGVMGMQGAGGYDSTMPYGCGRSQPRMRDRDRPKRRGFDRFGPDGTGRKRKQFQLYEEPDTKLAR...
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 facto...
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 ...
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 ...
Homo sapiens (Human)
O43825
B3GT2_HUMAN
MLQWRRRHCCFAKMTWNAKRSLFRTHLIGVLSLVFLFAMFLFFNHHDWLPGRAGFKENPVTYTFRGFRSTKSETNHSSLRNIWKETVPQTLRPQTATNSNNTDLSPQGVTGLENTLSANGSIYNEKGTGHPNSYHFKYIINEPEKCQEKSPFLILLIAAEPGQIEARRAIRQTWGNESLAPGIQITRIFLLGLSIKLNGYLQRAILEESRQYHDIIQQEYLDTYYNLTIKTLMGMNWVATYCPHIPYVMKTDSDMFVNTEYLINKLLKPDLPPRHNYFTGYLMRGYAPNRNKDSKWYMPPDLYPSERYPVFCSGTGYVFS...
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={...
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 gly...
Homo sapiens (Human)
O43826
G6PT1_HUMAN
MAAQGYGYYRTVIFSAMFGGYSLYYFNRKTFSFVMPSLVEEIPLDKDDLGFITSSQSAAYAISKFVSGVLSDQMSARWLFSSGLLLVGLVNIFFAWSSTVPVFAALWFLNGLAQGLGWPPCGKVLRKWFEPSQFGTWWAILSTSMNLAGGLGPILATILAQSYSWRSTLALSGALCVVVSFLCLLLIHNEPADVGLRNLDPMPSEGKKGSLKEESTLQELLLSPYLWVLSTGYLVVFGVKTCCTDWGQFFLIQEKGQSALVGSSYMSALEVGGLVGSIAAGYLSDRAMAKAGLSNYGNPRHGLLLFMMAGMTVSMYLFRV...
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 responsib...
Homo sapiens (Human)
O43827
ANGL7_HUMAN
MLKKPLSAVTWLCIFIVAFVSHPAWLQKLSKHKTPAQPQLKAANCCEEVKELKAQVANLSSLLSELNKKQERDWVSVVMQVMELESNSKRMESRLTDAESKYSEMNNQIDIMQLQAAQTVTQTSADAIYDCSSLYQKNYRISGVYKLPPDDFLGSPELEVFCDMETSGGGWTIIQRRKSGLVSFYRDWKQYKQGFGSIRGDFWLGNEHIHRLSRQPTRLRVEMEDWEGNLRYAEYSHFVLGNELNSYRLFLGNYTGNVGNDALQYHNNTAFSTKDKDNDNCLDKCAQLRKGGYWYNCCTDSNLNGVYYRLGEHNKHLDGI...
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:211...
Homo sapiens (Human)
O43829
ZBT14_HUMAN
MEFFISMSETIKYNDDDHKTLFLKTLNEQRLEGEFCDIAIVVEDVKFRAHRCVLAACSTYFKKLFKKLEVDSSSVIEIDFLRSDIFEEVLNYMYTAKISVKKEDVNLMMSSGQILGIRFLDKLCSQKRDVSSPDENNGQSKSKYCLKINRPIGDAADTQDDDVEEIGDQDDSPSDDTVEGTPPSQEDGKSPTTTLRVQEAILKELGSEEVRKVNCYGQEVESMETPESKDLGSQTPQALTFNDGMSEVKDEQTPGWTTAASDMKFEYLLYGHHREQIACQACGKTFSDEGRLRKHEKLHTADRPFVCEMCTKGFTTQAHL...
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 transcript...
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...
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. {E...
Homo sapiens (Human)
O43837
IDH3B_HUMAN
MAALSGVRWLTRALVSAGNPGAWRGLSTSAAAHAASRSQAEDVRVEGSFPVTMLPGDGVGPELMHAVKEVFKAAAVPVEFQEHHLSEVQNMASEEKLEQVLSSMKENKVAIIGKIHTPMEYKGELASYDMRLRRKLDLFANVVHVKSLPGYMTRHNNLDLVIIREQTEGEYSSLEHESARGVIECLKIVTRAKSQRIAKFAFDYATKKGRGKVTAVHKANIMKLGDGLFLQCCEEVAELYPKIKFETMIIDNCCMQLVQNPYQFDVLVMPNLYGNIIDNLAAGLVGGAGVVPGESYSAEYAVFETGARHPFAQAVGRNIA...
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)...
Homo sapiens (Human)
O43847
NRDC_HUMAN
MLRRVTVAAVCATRRKLCEAGRELAALWGIETRGRCEDSAAARPFPILAMPGRNKAKSTCSCPDLQPNGQDLGENSRVARLGADESEEEGRRGSLSNAGDPEIVKSPSDPKQYRYIKLQNGLQALLISDLSNMEGKTGNTTDDEEEEEVEEEEEDDDEDSGAEIEDDDEEGFDDEDEFDDEHDDDLDTEDNELEELEERAEARKKTTEKQSAAALCVGVGSFADPDDLPGLAHFLEHMVFMGSLKYPDENGFDAFLKKHGGSDNASTDCERTVFQFDVQRKYFKEALDRWAQFFIHPLMIRDAIDREVEAVDSEYQLARP...
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]; posi...
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 dehydrogenas...
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 st...
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
MKRSVAVWLLVGLSLGVPQFGKGDICDPNPCENGGICLPGLADGSFSCECPDGFTDPNCSSVVEVASDEEEPTSAGPCTPNPCHNGGTCEISEAYRGDTFIGYVCKCPRGFNGIHCQHNINECEVEPCKNGGICTDLVANYSCECPGEFMGRNCQYKCSGPLGIEGGIISNQQITASSTHRALFGLQKWYPYYARLNKKGLINAWTAAENDRWPWIQINLQRKMRVTGVITQGAKRIGSPEYIKSYKIAYSNDGKTWAMYKVKGTNEDMVFRGNIDNNTPYANSFTPPIKAQYVRLYPQVCRRHCTLRMELLGCELSGCS...
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
MADQIPLYPVRSAAAAAANRKRAAYYSAAGPRPGADRHSRYQLEDESAHLDEMPLMMSEEGFENEESDYHTLPRARIMQRKRGLEWFVCDGWKFLCTSCCGWLINICRRKKELKARTVWLGCPEKCEEKHPRNSIKNQKYNVFTFIPGVLYEQFKFFLNLYFLVISCSQFVPALKIGYLYTYWAPLGFVLAVTMTREAIDEFRRFQRDKEVNSQLYSKLTVRGKVQVKSSDIQVGDLIIVEKNQRIPSDMVFLRTSEKAGSCFIRTDQLDGETDWKLKVAVSCTQQLPALGDLFSISAYVYAQKPQMDIHSFEGTFTRED...
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
MSMPDAMPLPGVGEELKQAKEIEDAEKYSFMATVTKAPKKQIQFADDMQEFTKFPTKTGRRSLSRSISQSSTDSYSSAASYTDSSDDEVSPREKQQTNSKGSSNFCVKNIKQAEFGRREIEIAEQDMSALISLRKRAQGEKPLAGAKIVGCTHITAQTAVLIETLCALGAQCRWSACNIYSTQNEVAAALAEAGVAVFAWKGESEDDFWWCIDRCVNMDGWQANMILDDGGDLTHWVYKKYPNVFKKIRGIVEESVTGVHRLYQLSKAGKLCVPAMNVNDSVTKQKFDNLYCCRESILDGLKRTTDVMFGGKQVVVCGYG...
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 nuc...
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:192249...
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 membran...
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 endogenou...
Homo sapiens (Human)
O43866
CD5L_HUMAN
MALLFSLILAICTRPGFLASPSGVRLVGGLHRCEGRVEVEQKGQWGTVCDDGWDIKDVAVLCRELGCGAASGTPSGILYEPPAEKEQKVLIQSVSCTGTEDTLAQCEQEEVYDCSHDEDAGASCENPESSFSPVPEGVRLADGPGHCKGRVEVKHQNQWYTVCQTGWSLRAAKVVCRQLGCGRAVLTQKRCNKHAYGRKPIWLSQMSCSGREATLQDCPSGPWGKNTCNHDEDTWVECEDPFDLRLVGGDNLCSGRLEVLHKGVWGSVCDDNWGEKEDQVVCKQLGCGKSLSPSFRDRKCYGPGVGRIWLDNVRCSGEEQ...
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|UniPr...
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 adi...
Homo sapiens (Human)
O43868
S28A2_HUMAN
MEKASGRQSIALSTVETGTVNPGLELMEKEVEPEGSKRTDAQGHSLGDGLGPSTYQRRSRWPFSKARSFCKTHASLFKKILLGLLCLAYAAYLLAACILNFQRALALFVITCLVIFVLVHSFLKKLLGKKLTRCLKPFENSRLRLWTKWVFAGVSLVGLILWLALDTAQRPEQLIPFAGICMFILILFACSKHHSAVSWRTVFSGLGLQFVFGILVIRTDLGYTVFQWLGEQVQIFLNYTVAGSSFVFGDTLVKDVFAFQALPIIIFFGCVVSILYYLGLVQWVVQKVAWFLQITMGTTATETLAVAGNIFVGMTEAPLL...
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]; p...
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- an...
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:000026...
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...
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 ...
Homo sapiens (Human)
O43889
CREB3_HUMAN
MELELDAGDQDLLAFLLEESGDLGTAPDEAVRAPLDWALPLSEVPSDWEVDDLLCSLLSPPASLNILSSSNPCLVHHDHTYSLPRETVSMDLESESCRKEGTQMTPQHMEELAEQEIARLVLTDEEKSLLEKEGLILPETLPLTKTEEQILKRVRRKIRNKRSAQESRRKKKVYVGGLESRVLKYTAQNMELQNKVQLLEEQNLSLLDQLRKLQAMVIEISNKTSSSSTCILVLLVSFCLLLVPAMYSSDTRGSLPAEHGVLSRQLRALPSEDPYQLELPALQSEVPKDSTHQWLDGSDCVLQAPGNTSCLLHYMPQAPS...
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...
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]; n...
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 t...
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 ...
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 neuron...
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-induce...
Homo sapiens (Human)
O43895
XPP2_HUMAN
MARAHWGCCPWLVLLCACAWGHTKPVDLGGQDVRNCSTNPPYLPVTVVNTTMSLTALRQQMQTQNLSAYIIPGTDAHMNEYIGQHDERRAWITGFTGSAGTAVVTMKKAAVWTDSRYWTQAERQMDCNWELHKEVGTTPIVTWLLTEIPAGGRVGFDPFLLSIDTWESYDLALQGSNRQLVSITTNLVDLVWGSERPPVPNQPIYALQEAFTGSTWQEKVSGVRSQMQKHQKVPTAVLLSALEETAWLFNLRASDIPYNPFFYSYTLLTDSSIRLFANKSRFSSETLSYLNSSCTGPMCVQIEDYSQVRDSIQAYSLGDV...
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...
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
MAGASVKVAVRVRPFNARETSQDAKCVVSMQGNTTSIINPKQSKDAPKSFTFDYSYWSHTSTEDPQFASQQQVYRDIGEEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGRQEPGQQGIVPQLCEDLFSRVSENQSAQLSYSVEVSYMEIYCERVRDLLNPKSRGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRCHDQLTGLDSEKVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADMQSKKRKSDFIPYRDSVLTWLLKENLGGNSRTA...
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...
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)