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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O75473
|
LGR5_HUMAN
|
MDTSRLGVLLSLPVLLQLATGGSSPRSGVLLRGCPTHCHCEPDGRMLLRVDCSDLGLSELPSNLSVFTSYLDLSMNNISQLLPNPLPSLRFLEELRLAGNALTYIPKGAFTGLYSLKVLMLQNNQLRHVPTEALQNLRSLQSLRLDANHISYVPPSCFSGLHSLRHLWLDDNALTEIPVQAFRSLSALQAMTLALNKIHHIPDYAFGNLSSLVVLHLHNNRIHSLGKKCFDGLHSLETLDLNYNNLDEFPTAIRTLSNLKELGFHSNNIRSIPEKAFVGNPSLITIHFYDNPIQFVGRSAFQHLPELRTLTLNGASQITEFPDLTGTANLESLTLTGAQISSLPQTVCNQLPNLQVLDLSYNLLEDLPSFSVCQKLQKIDLRHNEIYEIKVDTFQQLLSLRSLNLAWNKIAIIHPNAFSTLPSLIKLDLSSNLLSSFPITGLHGLTHLKLTGNHALQSLISSENFPELKVIEMPYAYQCCAFGVCENAYKISNQWNKGDNSSMDDLHKKDAGMFQAQDERDLEDFLLDFEEDLKALHSVQCSPSPGPFKPCEHLLDGWLIRIGVWTIAVLALTCNALVTSTVFRSPLYISPIKLLIGVIAAVNMLTGVSSAVLAGVDAFTFGSFARHGAWWENGVGCHVIGFLSIFASESSVFLLTLAALERGFSVKYSAKFETKAPFSSLKVIILLCALLALTMAAVPLLGGSKYGASPLCLPLPFGEPSTMGYMVALILLNSLCFLMMTIAYTKLYCNLDKGDLENIWDCSMVKHIALLLFTNCILNCPVAFLSFSSLINLTFISPEVIKFILLVVVPLPACLNPLLYILFNPHFKEDLVSLRKQTYVWTRSKHPSLMSINSDDVEKQSCDSTQALVTFTSSSITYDLPPSSVPSPAYPVTESCHLSSVAFVPCL
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; epithelial cell proliferation involved in renal tubule morphogenesis [GO:2001013]; G protein-coupled receptor signaling pathway [GO:0007186]; hair follicle development [GO:0001942]; inner ear development [GO:0048839]; oocyte differentiation [GO:0009994]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; regulation of cell population proliferation [GO:0042127]
|
Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; trans-Golgi network membrane [GO:0032588]
|
G protein-coupled peptide receptor activity [GO:0008528]; G protein-coupled receptor activity [GO:0004930]; protein-hormone receptor activity [GO:0016500]; transmembrane signaling receptor activity [GO:0004888]
|
PF00001;PF00560;PF13855;PF01462;
|
1.20.1070.10;3.80.10.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. Note=Rapidly and constitutively internalized to the trans-Golgi network at steady state. Internalization to the trans-Golgi network may be the result of phosphorylation at Ser-861 and Ser-864; however, the phosphorylation event has not been proven (PubMed:23439653). {ECO:0000269|PubMed:23439653}.
| null | null | null | null | null |
FUNCTION: Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and acts as a stem cell marker of the intestinal epithelium and the hair follicle. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Involved in the development and/or maintenance of the adult intestinal stem cells during postembryonic development. {ECO:0000269|PubMed:21693646, ECO:0000269|PubMed:21727895, ECO:0000269|PubMed:21909076, ECO:0000269|PubMed:22815884, ECO:0000269|PubMed:23809763}.
|
Homo sapiens (Human)
|
O75475
|
PSIP1_HUMAN
|
MTRDFKPGDLIFAKMKGYPHWPARVDEVPDGAVKPPTNKLPIFFFGTHETAFLGPKDIFPYSENKEKYGKPNKRKGFNEGLWEIDNNPKVKFSSQQAATKQSNASSDVEVEEKETSVSKEDTDHEEKASNEDVTKAVDITTPKAARRGRKRKAEKQVETEEAGVVTTATASVNLKVSPKRGRPAATEVKIPKPRGRPKMVKQPCPSESDIITEEDKSKKKGQEEKQPKKQPKKDEEGQKEEDKPRKEPDKKEGKKEVESKRKNLAKTGVTSTSDSEEEGDDQEGEKKRKGGRNFQTAHRRNMLKGQHEKEAADRKRKQEEQMETEQQNKDEGKKPEVKKVEKKRETSMDSRLQRIHAEIKNSLKIDNLDVNRCIEALDELASLQVTMQQAQKHTEMITTLKKIRRFKVSQVIMEKSTMLYNKFKNMFLVGEGDSVITQVLNKSLAEQRQHEEANKTKDQGKKGPNKKLEKEQTGSKTLNGGSDAQDGNQPQHNGESNEDSKDNHEASTKKKPSSEERETEISLKDSTLDN
| null | null |
chromatin remodeling [GO:0006338]; mRNA 5'-splice site recognition [GO:0000395]; positive regulation of transcription by RNA polymerase II [GO:0045944]; response to heat [GO:0009408]; response to oxidative stress [GO:0006979]
|
cytosol [GO:0005829]; euchromatin [GO:0000791]; heterochromatin [GO:0000792]; nuclear periphery [GO:0034399]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA-binding transcription factor binding [GO:0140297]; RNA binding [GO:0003723]; supercoiled DNA binding [GO:0097100]; transcription coactivator activity [GO:0003713]
|
PF11467;PF00855;
|
2.30.30.140;1.20.930.10;
|
HDGF family
|
PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q99JF8}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15642333, ECO:0000269|PubMed:9885563}. Note=Remains chromatin-associated throughout the cell cycle.
| null | null | null | null | null |
FUNCTION: Transcriptional coactivator involved in neuroepithelial stem cell differentiation and neurogenesis. Involved in particular in lens epithelial cell gene regulation and stress responses. May play an important role in lens epithelial to fiber cell terminal differentiation. May play a protective role during stress-induced apoptosis. Isoform 2 is a more general and stronger transcriptional coactivator. Isoform 2 may also act as an adapter to coordinate pre-mRNA splicing. Cellular cofactor for lentiviral integration. {ECO:0000269|PubMed:15642333}.
|
Homo sapiens (Human)
|
O75477
|
ERLN1_HUMAN
|
MNMTQARVLVAAVVGLVAVLLYASIHKIEEGHLAVYYRGGALLTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNMLAPYAVFDIVRNYTADYDKTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNLMAPGLTIQAVRVTKPKIPEAIRRNFELMEAEKTKLLIAAQKQKVVEKEAETERKKAVIEAEKIAQVAKIRFQQKVMEKETEKRISEIEDAAFLAREKAKADAEYYAAHKYATSNKHKLTPEYLELKKYQAIASNSKIYFGSNIPNMFVDSSCALKYSDIRTGRESSLPSKEALEPSGENVIQNKESTG
| null | null |
cholesterol metabolic process [GO:0008203]; ERAD pathway [GO:0036503]; negative regulation of cholesterol biosynthetic process [GO:0045541]; negative regulation of fatty acid biosynthetic process [GO:0045717]; regulation of cholesterol biosynthetic process [GO:0045540]; SREBP signaling pathway [GO:0032933]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane raft [GO:0045121]; protein-containing complex [GO:0032991]
|
cholesterol binding [GO:0015485]; ubiquitin protein ligase binding [GO:0031625]
|
PF01145;
|
3.30.479.30;
|
Band 7/mec-2 family
|
PTM: Deubiquitinated by USP25; leading to stabilization. {ECO:0000269|PubMed:37683630}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11118313, ECO:0000269|PubMed:16835267, ECO:0000269|PubMed:19240031}; Single-pass type II membrane protein {ECO:0000269|PubMed:11118313, ECO:0000269|PubMed:16835267, ECO:0000269|PubMed:19240031}. Note=Associated with lipid raft-like domains of the endoplasmic reticulum membrane.
| null | null | null | null | null |
FUNCTION: Component of the ERLIN1/ERLIN2 complex which mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs). Involved in regulation of cellular cholesterol homeostasis by regulation the SREBP signaling pathway (PubMed:37683630). Binds cholesterol and may promote ER retention of the SCAP-SREBF complex (PubMed:24217618). {ECO:0000269|PubMed:19240031, ECO:0000269|PubMed:24217618, ECO:0000269|PubMed:37683630}.; FUNCTION: (Microbial infection) Required early in hepatitis C virus (HCV) infection to initiate RNA replication, and later in the infection to support infectious virus production. {ECO:0000269|PubMed:31810281}.
|
Homo sapiens (Human)
|
O75478
|
TAD2A_HUMAN
|
MDRLGPFSNDPSDKPPCRGCSSYLMEPYIKCAECGPPPFFLCLQCFTRGFEYKKHQSDHTYEIMTSDFPVLDPSWTAQEEMALLEAVMDCGFGNWQDVANQMCTKTKEECEKHYMKHFINNPLFASTLLNLKQAEEAKTADTAIPFHSTDDPPRPTFDSLLSRDMAGYMPARADFIEEFDNYAEWDLRDIDFVEDDSDILHALKMAVVDIYHSRLKERQRRKKIIRDHGLINLRKFQLMERRYPKEVQDLYETMRRFARIVGPVEHDKFIESHALEFELRREIKRLQEYRTAGITNFCSARTYDHLKKTREEERLKRTMLSEVLQYIQDSSACQQWLRRQADIDSGLSPSIPMASNSGRRSAPPLNLTGLPGTEKLNEKEKELCQMVRLVPGAYLEYKSALLNECNKQGGLRLAQARALIKIDVNKTRKIYDFLIREGYITKG
| null | null |
chromatin remodeling [GO:0006338]; regulation of cell cycle [GO:0051726]; regulation of cell division [GO:0051302]; regulation of DNA-templated transcription [GO:0006355]; regulation of embryonic development [GO:0045995]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of tubulin deacetylation [GO:0090043]
|
ATAC complex [GO:0140672]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SAGA complex [GO:0000124]; SAGA-type complex [GO:0070461]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; transcription coactivator activity [GO:0003713]; zinc ion binding [GO:0008270]
|
PF00249;PF04433;
|
3.30.60.90;1.10.10.60;1.10.10.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22644376}. Chromosome {ECO:0000250|UniProtKB:Q8CHV6}.
| null | null | null | null | null |
FUNCTION: Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. Required for the function of some acidic activation domains, which activate transcription from a distant site (By similarity). Binds double-stranded DNA. Binds dinucleosomes, probably at the linker region between neighboring nucleosomes. Plays a role in chromatin remodeling. May promote TP53/p53 'Lys-321' acetylation, leading to reduced TP53 stability and transcriptional activity (PubMed:22644376). May also promote XRCC6 acetylation thus facilitating cell apoptosis in response to DNA damage (PubMed:22644376). {ECO:0000250|UniProtKB:Q8CHV6, ECO:0000269|PubMed:19103755, ECO:0000269|PubMed:22644376}.
|
Homo sapiens (Human)
|
O75486
|
SUPT3_HUMAN
|
MNNTAASPMSTATSSSGRSTGKSISFATELQSMMYSLGDARRPLHETAVLVEDVVHTQLINLLQQAAEVSQLRGARVITPEDLLFLMRKDKKKLRRLLKYMFIRDYKSKIVKGIDEDDLLEDKLSGSNNANKRQKIAQDFLNSIDQTGELLAMFEDDEIDEVKQERMERAERQTRIMDSAQYAEFCESRQLSFSKKASKFRDWLDCSSMEIKPNVVAMEILAYLAYETVAQLVDLALLVRQDMVTKAGDPFSHAISATFIQYHNSAESTAACGVEAHSDAIQPCHIREAIRRYSHRIGPLSPFTNAYRRNGMAFLAC
| null | null |
positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA repair [GO:0006282]; regulation of DNA-templated transcription [GO:0006355]; regulation of RNA splicing [GO:0043484]; regulation of transcription by RNA polymerase II [GO:0006357]; RNA polymerase II preinitiation complex assembly [GO:0051123]; transcription by RNA polymerase II [GO:0006366]
|
nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SAGA complex [GO:0000124]; transcription factor TFIID complex [GO:0005669]; transcription factor TFTC complex [GO:0033276]
|
protein heterodimerization activity [GO:0046982]; transcription coactivator activity [GO:0003713]
|
PF02269;
|
1.10.20.10;
|
SPT3 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863, ECO:0000269|PubMed:9726987}.
| null | null | null | null | null |
FUNCTION: Probable transcriptional activator. {ECO:0000269|PubMed:9787080}.
|
Homo sapiens (Human)
|
O75487
|
GPC4_HUMAN
|
MARFGLPALLCTLAVLSAALLAAELKSKSCSEVRRLYVSKGFNKNDAPLHEINGDHLKICPQGSTCCSQEMEEKYSLQSKDDFKSVVSEQCNHLQAVFASRYKKFDEFFKELLENAEKSLNDMFVKTYGHLYMQNSELFKDLFVELKRYYVVGNVNLEEMLNDFWARLLERMFRLVNSQYHFTDEYLECVSKYTEQLKPFGDVPRKLKLQVTRAFVAARTFAQGLAVAGDVVSKVSVVNPTAQCTHALLKMIYCSHCRGLVTVKPCYNYCSNIMRGCLANQGDLDFEWNNFIDAMLMVAERLEGPFNIESVMDPIDVKISDAIMNMQDNSVQVSQKVFQGCGPPKPLPAGRISRSISESAFSARFRPHHPEERPTTAAGTSLDRLVTDVKEKLKQAKKFWSSLPSNVCNDERMAAGNGNEDDCWNGKGKSRYLFAVTGNGLANQGNNPEVQVDTSKPDILILRQIMALRVMTSKMKNAYNGNDVDFFDISDESSGEGSGSGCEYQQCPSEFDYNATDHAGKSANEKADSAGVRPGAQAYLLTVFCILFLVMQREWR
| null | null |
cell migration [GO:0016477]; regulation of neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0098696]; regulation of presynapse assembly [GO:1905606]; regulation of signal transduction [GO:0009966]; synaptic membrane adhesion [GO:0099560]; Wnt signaling pathway [GO:0016055]
|
cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; glutamatergic synapse [GO:0098978]; Golgi lumen [GO:0005796]; lysosomal lumen [GO:0043202]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; synapse [GO:0045202]
|
coreceptor activity [GO:0015026]
|
PF01153;
| null |
Glypican family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}; Extracellular side {ECO:0000250}.; SUBCELLULAR LOCATION: [Secreted glypican-4]: Secreted, extracellular space {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Cell surface proteoglycan that bears heparan sulfate. May be involved in the development of kidney tubules and of the central nervous system (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O75489
|
NDUS3_HUMAN
|
MAAAAVARLWWRGILGASALTRGTGRPSVLLLPVRRESAGADTRPTVRPRNDVAHKQLSAFGEYVAEILPKYVQQVQVSCFNELEVCIHPDGVIPVLTFLRDHTNAQFKSLVDLTAVDVPTRQNRFEIVYNLLSLRFNSRIRVKTYTDELTPIESAVSVFKAANWYEREIWDMFGVFFANHPDLRRILTDYGFEGHPFRKDFPLSGYVELRYDDEVKRVVAEPVELAQEFRKFDLNSPWEAFPVYRQPPESLKLEAGDKKPDAK
|
7.1.1.2
| null |
aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; negative regulation of cell growth [GO:0030308]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]; reactive oxygen species metabolic process [GO:0072593]; substantia nigra development [GO:0021762]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]; nuclear body [GO:0016604]
|
electron transfer activity [GO:0009055]; NADH dehydrogenase (ubiquinone) activity [GO:0008137]; NADH dehydrogenase activity [GO:0003954]
|
PF00329;
|
3.30.460.80;
|
Complex I 30 kDa subunit family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:18826940, ECO:0000305|PubMed:12611891, ECO:0000305|PubMed:17209039}; Peripheral membrane protein {ECO:0000305|PubMed:18826940}; Matrix side {ECO:0000269|PubMed:18826940}.
|
CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000269|PubMed:14729820, ECO:0000269|PubMed:30140060};
| null | null | null | null |
FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:14729820, PubMed:30140060). Essential for the catalytic activity and assembly of complex I (PubMed:14729820, PubMed:24028823, PubMed:30140060). {ECO:0000269|PubMed:14729820, ECO:0000269|PubMed:24028823, ECO:0000269|PubMed:30140060}.
|
Homo sapiens (Human)
|
O75494
|
SRS10_HUMAN
|
MSRYLRPPNTSLFVRNVADDTRSEDLRREFGRYGPIVDVYVPLDFYTRRPRGFAYVQFEDVRDAEDALHNLDRKWICGRQIEIQFAQGDRKTPNQMKAKEGRNVYSSSRYDDYDRYRRSRSRSYERRRSRSRSFDYNYRRSYSPRNSRPTGRPRRSRSHSDNDRFKHRNRSFSRSKSNSRSRSKSQPKKEMKAKSRSRSASHTKTRGTSKTDSKTHYKSGSRYEKESRKKEPPRSKSQSRSQSRSRSKSRSRSWTSPKSSGH
| null | null |
cytosolic transport [GO:0016482]; mRNA splice site recognition [GO:0006376]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; regulation of DNA-templated transcription [GO:0006355]; regulation of mRNA splicing, via spliceosome [GO:0048024]; RNA splicing, via transesterification reactions [GO:0000375]; spliceosomal tri-snRNP complex assembly [GO:0000244]
|
axon terminus [GO:0043679]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
RNA binding [GO:0003723]; RS domain binding [GO:0050733]; unfolded protein binding [GO:0051082]
|
PF00076;
|
3.30.70.330;
|
Splicing factor SR family
|
PTM: Phosphorylated. Fully dephosphorylated in mitosis and partially dephosphorylated on heat shock. {ECO:0000269|PubMed:12419250, ECO:0000269|PubMed:14765198}.
|
SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:11684676, ECO:0000269|PubMed:26876937}. Cytoplasm {ECO:0000269|PubMed:11684676}.
| null | null | null | null | null |
FUNCTION: Splicing factor that in its dephosphorylated form acts as a general repressor of pre-mRNA splicing (PubMed:11684676, PubMed:12419250, PubMed:14765198). Seems to interfere with the U1 snRNP 5'-splice recognition of SNRNP70 (PubMed:14765198). Required for splicing repression in M-phase cells and after heat shock (PubMed:14765198). Also acts as a splicing factor that specifically promotes exon skipping during alternative splicing (PubMed:26876937). Interaction with YTHDC1, a RNA-binding protein that recognizes and binds N6-methyladenosine (m6A)-containing RNAs, prevents SRSF10 from binding to its mRNA-binding sites close to m6A-containing regions, leading to inhibit exon skipping during alternative splicing (PubMed:26876937). May be involved in regulation of alternative splicing in neurons, with isoform 1 acting as a positive and isoform 3 as a negative regulator (PubMed:12419250). {ECO:0000269|PubMed:11684676, ECO:0000269|PubMed:12419250, ECO:0000269|PubMed:14765198, ECO:0000269|PubMed:26876937}.
|
Homo sapiens (Human)
|
O75496
|
GEMI_HUMAN
|
MNPSMKQKQEEIKENIKNSSVPRRTLKMIQPSASGSLVGRENELSAGLSKRKHRNDHLTSTTSSPGVIVPESSENKNLGGVTQESFDLMIKENPSSQYWKEVAEKRRKALYEALKENEKLHKEIEQKDNEIARLKKENKELAEVAEHVQYMAELIERLNGEPLDNFESLDNQEFDSEEETVEDSLVEDSEIGTCAEGTVSSSTDAKPCI
| null | null |
animal organ morphogenesis [GO:0009887]; DNA replication preinitiation complex assembly [GO:0071163]; negative regulation of cell cycle [GO:0045786]; negative regulation of DNA replication [GO:0008156]; negative regulation of DNA-templated DNA replication [GO:2000104]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of chromatin binding [GO:0035563]; regulation of DNA replication [GO:0006275]; regulation of DNA-templated DNA replication initiation [GO:0030174]; regulation of mitotic cell cycle [GO:0007346]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription repressor complex [GO:0017053]
|
chromatin binding [GO:0003682]; DNA-binding transcription factor binding [GO:0140297]; histone deacetylase binding [GO:0042826]; transcription corepressor activity [GO:0003714]
|
PF07412;
|
1.20.5.1180;
|
Geminin family
|
PTM: Phosphorylated during mitosis. Phosphorylation at Ser-184 by CK2 results in enhanced binding to Hox proteins and more potent inhibitory effect on Hox transcriptional activity. {ECO:0000269|PubMed:22615398, ECO:0000269|PubMed:22645314}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21543332}. Nucleus {ECO:0000269|PubMed:21543332}. Note=Mainly cytoplasmic but can be relocalized to the nucleus. {ECO:0000269|PubMed:21543332}.
| null | null | null | null | null |
FUNCTION: Inhibits DNA replication by preventing the incorporation of MCM complex into pre-replication complex (pre-RC) (PubMed:14993212, PubMed:20129055, PubMed:24064211, PubMed:9635433). It is degraded during the mitotic phase of the cell cycle (PubMed:14993212, PubMed:24064211, PubMed:9635433). Its destruction at the metaphase-anaphase transition permits replication in the succeeding cell cycle (PubMed:14993212, PubMed:24064211, PubMed:9635433). Inhibits histone acetyltransferase activity of KAT7/HBO1 in a CDT1-dependent manner, inhibiting histone H4 acetylation and DNA replication licensing (PubMed:20129055). Inhibits the transcriptional activity of a subset of Hox proteins, enrolling them in cell proliferative control (PubMed:22615398). {ECO:0000269|PubMed:14993212, ECO:0000269|PubMed:20129055, ECO:0000269|PubMed:22615398, ECO:0000269|PubMed:24064211, ECO:0000269|PubMed:9635433}.
|
Homo sapiens (Human)
|
O75503
|
CLN5_HUMAN
|
MAQEVDTAQGAEMRRGAGAARGRASWCWALALLWLAVVPGWSRVSGIPSRRHWPVPYKRFDFRPKPDPYCQAKYTFCPTGSPIPVMEGDDDIEVFRLQAPVWEFKYGDLLGHLKIMHDAIGFRSTLTGKNYTMEWYELFQLGNCTFPHLRPEMDAPFWCNQGAACFFEGIDDVHWKENGTLVQVATISGNMFNQMAKWVKQDNETGIYYETWNVKASPEKGAETWFDSYDCSKFVLRTFNKLAEFGAEFKNIETNYTRIFLYSGEPTYLGNETSVFGPTGNKTLGLAIKRFYYPFKPHLPTKEFLLSLLQIFDAVIVHKQFYLFYNFEYWFLPMKFPFIKITYEEIPLPIRNKTLSGL
|
2.3.1.-; 3.1.2.22
| null |
brain development [GO:0007420]; glycosylation [GO:0070085]; lysosomal lumen acidification [GO:0007042]; lysosome organization [GO:0007040]; neurogenesis [GO:0022008]; neuron maturation [GO:0042551]; positive regulation of GTP binding [GO:1904426]; protein catabolic process [GO:0030163]; retrograde transport, endosome to Golgi [GO:0042147]; signal peptide processing [GO:0006465]; visual perception [GO:0007601]
|
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; vacuolar lumen [GO:0005775]
|
bis(monoacylglycero)phosphate synthase activity [GO:0160121]; hydrolase activity, acting on glycosyl bonds [GO:0016798]; long-chain fatty acyl-CoA hydrolase activity [GO:0052816]; mannose binding [GO:0005537]
|
PF15014;
| null |
CLN5 family
|
PTM: N-glycosylated with both high mannose and complex type sugars. Glycosylation is important for proper folding and trafficking to the lysosomes. {ECO:0000269|PubMed:11971870, ECO:0000269|PubMed:20052765, ECO:0000269|PubMed:24038957, ECO:0000269|PubMed:24058541, ECO:0000269|PubMed:37708259}.; PTM: [Bis(monoacylglycero)phosphate synthase CLN5]: The type II membrane signal anchor is proteolytically cleaved to produce a mature form that is transported to the lysosomes (Bis(monoacylglycero)phosphate synthase CLN5, secreted form) (PubMed:20052765, PubMed:24038957, PubMed:28442266). {ECO:0000269|PubMed:20052765, ECO:0000269|PubMed:24038957, ECO:0000269|PubMed:28442266}.; PTM: Can undergo proteolytic cleavage at the C-terminus, probably by a cysteine protease and may involve the removal of approximately 10-15 residues from the C-terminal end (PubMed:26342652). {ECO:0000269|PubMed:26342652}.
|
SUBCELLULAR LOCATION: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]: Lysosome {ECO:0000269|PubMed:11971870, ECO:0000269|PubMed:20052765, ECO:0000269|PubMed:22431521, ECO:0000269|PubMed:24038957, ECO:0000269|PubMed:24058541, ECO:0000269|PubMed:28442266, ECO:0000269|PubMed:37708259}.; SUBCELLULAR LOCATION: [Bis(monoacylglycero)phosphate synthase CLN5]: Membrane {ECO:0000269|PubMed:24038957, ECO:0000269|PubMed:28442266}; Single-pass type II membrane protein {ECO:0000269|PubMed:24038957, ECO:0000269|PubMed:28442266}. Note=An amphipathic anchor region facilitates its association with the membrane. {ECO:0000269|PubMed:24038957}.
|
CATALYTIC ACTIVITY: Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:74151; EC=3.1.2.22; Evidence={ECO:0000269|PubMed:35427157}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19234; Evidence={ECO:0000305|PubMed:35427157}; CATALYTIC ACTIVITY: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]: Reaction=2 a 3-acyl-sn-glycero-1-phospho-(1'-sn-glycerol) = a 3-acyl-sn-glycero-1-phospho-(3'-acyl-1'-sn-glycerol) + sn-glycero-1-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:77619, ChEBI:CHEBI:77717, ChEBI:CHEBI:197411, ChEBI:CHEBI:197425; Evidence={ECO:0000269|PubMed:37708259}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77620; Evidence={ECO:0000269|PubMed:37708259}; CATALYTIC ACTIVITY: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]: Reaction=2 3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(1'-sn-glycerol) = 3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(3'-(9Z-octadecenoyl)-1'-sn-glycerol) + sn-glycero-1-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:77599, ChEBI:CHEBI:139150, ChEBI:CHEBI:139152, ChEBI:CHEBI:197411; Evidence={ECO:0000269|PubMed:37708259}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77600; Evidence={ECO:0000269|PubMed:37708259}; CATALYTIC ACTIVITY: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]: Reaction=2 3-octadecanoyl-sn-glycero-1-phospho-(1'-sn-glycerol) = 3-octadecanoyl-sn-glycero-1-phospho-(3'-octadecanoyl-1'-sn-glycerol) + sn-glycero-1-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:77603, ChEBI:CHEBI:197411, ChEBI:CHEBI:197412, ChEBI:CHEBI:197414; Evidence={ECO:0000269|PubMed:37708259}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77604; Evidence={ECO:0000269|PubMed:37708259}; CATALYTIC ACTIVITY: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]: Reaction=2 3-hexadecanoyl-sn-glycero-1-phospho-(1'-sn-glycerol) = 3-hexadecanoyl-sn-glycero-1-phospho-(3'-hexadecanoyl-1'-sn-glycerol) + sn-glycero-1-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:77607, ChEBI:CHEBI:44859, ChEBI:CHEBI:197411, ChEBI:CHEBI:197415; Evidence={ECO:0000269|PubMed:37708259}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77608; Evidence={ECO:0000269|PubMed:37708259}; CATALYTIC ACTIVITY: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]: Reaction=2 3-tetradecanoyl-sn-glycero-1-phospho-(1'-sn-glycerol) = 3-tetradecanoyl-sn-glycero-1-phospho-(3'-tetradecanoyl-1'-sn-glycerol) + sn-glycero-1-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:77611, ChEBI:CHEBI:197411, ChEBI:CHEBI:197413, ChEBI:CHEBI:197416; Evidence={ECO:0000269|PubMed:37708259}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77612; Evidence={ECO:0000269|PubMed:37708259};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.3 uM for lysophosphatidylglycerol 18:1 (at pH 5) {ECO:0000269|PubMed:37708259}; KM=4.752 uM for lysophosphatidylglycerol 18:1 (at pH 6.5) {ECO:0000269|PubMed:37708259};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 for bis(monoacylglycero)phosphate synthase activity (PubMed:37708259). Optimum pH of 6.5 and 8.5 is seen for palmitoyl thioesterase activity (PubMed:35427157). {ECO:0000269|PubMed:35427157, ECO:0000269|PubMed:37708259};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable. {ECO:0000269|PubMed:37708259};
|
FUNCTION: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]: Catalyzes the synthesis of bis(monoacylglycero)phosphate (BMP) via transacylation of 2 molecules of lysophosphatidylglycerol (LPG) (PubMed:37708259). BMP also known as lysobisphosphatidic acid plays a key role in the formation of intraluminal vesicles and in maintaining intracellular cholesterol homeostasis (PubMed:37708259). Can use only LPG as the exclusive lysophospholipid acyl donor for base exchange and displays BMP synthase activity towards various LPGs (LPG 14:0, LPG 16:0, LPG 18:0, LPG 18:1) with a higher preference for longer chain lengths (PubMed:37708259). Plays a role in influencing the retrograde trafficking of lysosomal sorting receptors SORT1 and IGF2R from the endosomes to the trans-Golgi network by controlling the recruitment of retromer complex to the endosomal membrane (PubMed:22431521). Regulates the localization and activation of RAB7A which is required to recruit the retromer complex to the endosomal membrane (PubMed:22431521). {ECO:0000269|PubMed:22431521, ECO:0000269|PubMed:37708259}.; FUNCTION: Exhibits palmitoyl protein thioesterase (S-depalmitoylation) activity in vitro and most likely plays a role in protein S-depalmitoylation. {ECO:0000269|PubMed:35427157}.
|
Homo sapiens (Human)
|
O75506
|
HSBP1_HUMAN
|
MAETDPKTVQDLTSVVQTLLQQMQDKFQTMSDQIIGRIDDMSSRIDDLEKNIADLMTQAGVEELESENKIPATQKS
| null | null |
axonal transport of mitochondrion [GO:0019896]; cellular heat acclimation [GO:0070370]; endodermal cell differentiation [GO:0035987]; negative regulation of transcription by RNA polymerase II [GO:0000122]
|
axon cytoplasm [GO:1904115]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
identical protein binding [GO:0042802]; transcription corepressor activity [GO:0003714]
|
PF06825;
|
1.20.5.430;
|
HSBP1 family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Negative regulator of the heat shock response. Negatively affects HSF1 DNA-binding activity. May have a role in the suppression of the activation of the stress response during the aging process.
|
Homo sapiens (Human)
|
O75508
|
CLD11_HUMAN
|
MVATCLQVVGFVTSFVGWIGVIVTTSTNDWVVTCGYTIPTCRKLDELGSKGLWADCVMATGLYHCKPLVDILILPGYVQACRALMIAASVLGLPAILLLLTVLPCIRMGQEPGVAKYRRAQLAGVLLILLALCALVATIWFPVCAHRETTIVSFGYSLYAGWIGAVLCLVGGCVILCCAGDAQAFGENRFYYTAGSSSPTHAKSAHV
| null | null |
axon ensheathment [GO:0008366]; bicellular tight junction assembly [GO:0070830]; calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules [GO:0016338]; cell adhesion [GO:0007155]; spermatogenesis [GO:0007283]; tight junction assembly [GO:0120192]
|
axon [GO:0030424]; basal part of cell [GO:0045178]; bicellular tight junction [GO:0005923]; cell junction [GO:0030054]; lipid droplet [GO:0005811]; neurofilament [GO:0005883]; plasma membrane [GO:0005886]; tight junction [GO:0070160]
|
identical protein binding [GO:0042802]; structural molecule activity [GO:0005198]
|
PF00822;
|
1.20.140.150;
|
Claudin family
| null |
SUBCELLULAR LOCATION: Cell junction, tight junction. Cell membrane {ECO:0000269|PubMed:20375010}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000250}.
|
Homo sapiens (Human)
|
O75509
|
TNR21_HUMAN
|
MGTSPSSSTALASCSRIARRATATMIAGSLLLLGFLSTTTAQPEQKASNLIGTYRHVDRATGQVLTCDKCPAGTYVSEHCTNTSLRVCSSCPVGTFTRHENGIEKCHDCSQPCPWPMIEKLPCAALTDRECTCPPGMFQSNATCAPHTVCPVGWGVRKKGTETEDVRCKQCARGTFSDVPSSVMKCKAYTDCLSQNLVVIKPGTKETDNVCGTLPSFSSSTSPSPGTAIFPRPEHMETHEVPSSTYVPKGMNSTESNSSASVRPKVLSSIQEGTVPDNTSSARGKEDVNKTLPNLQVVNHQQGPHHRHILKLLPSMEATGGEKSSTPIKGPKRGHPRQNLHKHFDINEHLPWMIVLFLLLVLVVIVVCSIRKSSRTLKKGPRQDPSAIVEKAGLKKSMTPTQNREKWIYYCNGHGIDILKLVAAQVGSQWKDIYQFLCNASEREVAAFSNGYTADHERAYAALQHWTIRGPEASLAQLISALRQHRRNDVVEKIRGLMEDTTQLETDKLALPMSPSPLSPSPIPSPNAKLENSALLTVEPSPQDKNKGFFVDESEPLLRCDSTSSGSSALSRNGSFITKEKKDTVLRQVRLDPCDLQPIFDDMLHFLNPEELRVIEEIPQAEDKLDRLFEIIGVKSQEASQTLLDSVYSHLPDLL
| null | null |
adaptive immune response [GO:0002250]; apoptotic process [GO:0006915]; axonal fasciculation [GO:0007413]; B cell apoptotic process [GO:0001783]; cellular response to tumor necrosis factor [GO:0071356]; humoral immune response [GO:0006959]; myelination [GO:0042552]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of interleukin-10 production [GO:0032693]; negative regulation of interleukin-13 production [GO:0032696]; negative regulation of interleukin-5 production [GO:0032714]; negative regulation of myelination [GO:0031642]; negative regulation of T cell proliferation [GO:0042130]; neuron apoptotic process [GO:0051402]; oligodendrocyte apoptotic process [GO:0097252]; regulation of oligodendrocyte differentiation [GO:0048713]; T cell receptor signaling pathway [GO:0050852]
|
axon [GO:0030424]; plasma membrane [GO:0005886]
| null |
PF00531;PF00020;
|
1.10.533.10;2.10.50.10;
| null |
PTM: Oxidized in response to reactive oxygen species (ROS), leading to endocytosis. {ECO:0000269|PubMed:34012073}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19654028}; Single-pass type I membrane protein {ECO:0000269|PubMed:19654028}. Note=Endocytosed following oxidation in response to reactive oxygen species (ROS). {ECO:0000269|PubMed:34012073}.
| null | null | null | null | null |
FUNCTION: Promotes apoptosis, possibly via a pathway that involves the activation of NF-kappa-B. Can also promote apoptosis mediated by BAX and by the release of cytochrome c from the mitochondria into the cytoplasm. Plays a role in neuronal apoptosis, including apoptosis in response to amyloid peptides derived from APP, and is required for both normal cell body death and axonal pruning. Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP). N-APP binds TNFRSF21; this triggers caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6). Negatively regulates oligodendrocyte survival, maturation and myelination. Plays a role in signaling cascades triggered by stimulation of T-cell receptors, in the adaptive immune response and in the regulation of T-cell differentiation and proliferation. Negatively regulates T-cell responses and the release of cytokines such as IL4, IL5, IL10, IL13 and IFNG by Th2 cells. Negatively regulates the production of IgG, IgM and IgM in response to antigens. May inhibit the activation of JNK in response to T-cell stimulation. Also acts as a regulator of pyroptosis: recruits CASP8 in response to reactive oxygen species (ROS) and subsequent oxidation, leading to activation of GSDMC (PubMed:34012073). {ECO:0000269|PubMed:21725297, ECO:0000269|PubMed:22761420, ECO:0000269|PubMed:34012073, ECO:0000269|PubMed:9714541}.
|
Homo sapiens (Human)
|
O75521
|
ECI2_HUMAN
|
MAMAYLAWRLARRSCPSSLQVTSFPVVQLHMNRTAMRASQKDFENSMNQVKLLKKDPGNEVKLKLYALYKQATEGPCNMPKPGVFDLINKAKWDAWNALGSLPKEAARQNYVDLVSSLSPSLESSSQVEPGTDRKSTGFETLVVTSEDGITKIMFNRPKKKNAINTEMYHEIMRALKAASKDDSIITVLTGNGDYYSSGNDLTNFTDIPPGGVEEKAKNNAVLLREFVGCFIDFPKPLIAVVNGPAVGISVTLLGLFDAVYASDRATFHTPFSHLGQSPEGCSSYTFPKIMSPAKATEMLIFGKKLTAGEACAQGLVTEVFPDSTFQKEVWTRLKAFAKLPPNALRISKEVIRKREREKLHAVNAEECNVLQGRWLSDECTNAVVNFLSRKSKL
|
5.3.3.8
| null |
fatty acid beta-oxidation [GO:0006635]; fatty acid catabolic process [GO:0009062]
|
cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]
|
delta(3)-delta(2)-enoyl-CoA isomerase activity [GO:0004165]; fatty-acyl-CoA binding [GO:0000062]
|
PF00887;PF00378;
|
1.20.80.10;1.10.12.10;
|
Enoyl-CoA hydratase/isomerase family
| null |
SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion {ECO:0000250|UniProtKB:Q5XIC0}.; SUBCELLULAR LOCATION: [Isoform 2]: Peroxisome matrix {ECO:0000269|PubMed:10419495}.
|
CATALYTIC ACTIVITY: Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489; EC=5.3.3.8; Evidence={ECO:0000305|PubMed:10419495}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45901; Evidence={ECO:0000305|PubMed:10419495}; CATALYTIC ACTIVITY: Reaction=(3Z)-octenoyl-CoA = (2E)-octenoyl-CoA; Xref=Rhea:RHEA:46044, ChEBI:CHEBI:62242, ChEBI:CHEBI:85640; Evidence={ECO:0000269|PubMed:10419495}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46045; Evidence={ECO:0000269|PubMed:10419495}; CATALYTIC ACTIVITY: Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097; EC=5.3.3.8; Evidence={ECO:0000250|UniProtKB:Q5XIC0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45229; Evidence={ECO:0000250|UniProtKB:Q5XIC0}; CATALYTIC ACTIVITY: Reaction=(2E)-tetradecenoyl-CoA = (3Z)-tetradecenoyl-CoA; Xref=Rhea:RHEA:29847, ChEBI:CHEBI:61405, ChEBI:CHEBI:61968; Evidence={ECO:0000250|UniProtKB:Q5XIC0}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29849; Evidence={ECO:0000250|UniProtKB:Q5XIC0}; CATALYTIC ACTIVITY: Reaction=(3E)-tetradecenoyl-CoA = (2E)-tetradecenoyl-CoA; Xref=Rhea:RHEA:47476, ChEBI:CHEBI:61405, ChEBI:CHEBI:87710; Evidence={ECO:0000250|UniProtKB:Q5XIC0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47477; Evidence={ECO:0000250|UniProtKB:Q5XIC0}; CATALYTIC ACTIVITY: Reaction=(3E)-octenoyl-CoA = (2E)-octenoyl-CoA; Xref=Rhea:RHEA:49852, ChEBI:CHEBI:62242, ChEBI:CHEBI:131962; Evidence={ECO:0000250|UniProtKB:Q5XIC0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49853; Evidence={ECO:0000250|UniProtKB:Q5XIC0}; CATALYTIC ACTIVITY: Reaction=(3E)-nonenoyl-CoA = (2E)-nonenoyl-CoA; Xref=Rhea:RHEA:46068, ChEBI:CHEBI:76292, ChEBI:CHEBI:85655; Evidence={ECO:0000250|UniProtKB:Q9WUR2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46069; Evidence={ECO:0000250|UniProtKB:Q9WUR2};
| null |
PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000269|PubMed:10419495}.
| null | null |
FUNCTION: Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species. Has a preference for 3-trans substrates. {ECO:0000269|PubMed:10419495}.
|
Homo sapiens (Human)
|
O75525
|
KHDR3_HUMAN
|
MEEKYLPELMAEKDSLDPSFTHALRLVNQEIEKFQKGEGKDEEKYIDVVINKNMKLGQKVLIPVKQFPKFNFVGKLLGPRGNSLKRLQEETLTKMSILGKGSMRDKAKEEELRKSGEAKYFHLNDDLHVLIEVFAPPAEAYARMGHALEEIKKFLIPDYNDEIRQAQLQELTYLNGGSENADVPVVRGKPTLRTRGVPAPAITRGRGGVTARPVGVVVPRGTPTPRGVLSTRGPVSRGRGLLTPRARGVPPTGYRPPPPPPTQETYGEYDYDDGYGTAYDEQSYDSYDNSYSTPAQSGADYYDYGHGLSEETYDSYGQEEWTNSRHKAPSARTAKGVYRDQPYGRY
| null | null |
mRNA processing [GO:0006397]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]
|
nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
|
identical protein binding [GO:0042802]; mRNA binding [GO:0003729]; protein domain specific binding [GO:0019904]; RNA binding [GO:0003723]; SH3 domain binding [GO:0017124]
|
PF16274;PF16568;
|
3.30.1370.10;
|
KHDRBS family
|
PTM: Phosphorylated on tyrosine residues. Isoform 1 C-terminal region is tyrosine-rich, but isoform 2 lacking this C-terminal region is also tyrosine-phosphorylated. {ECO:0000269|PubMed:10564820}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10332027, ECO:0000269|PubMed:15901763}. Note=Localized in a compartment adjacent to the nucleolus, but distinct from the peri-nucleolar one.
| null | null | null | null | null |
FUNCTION: RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds preferentially to the 5'-[AU]UAAA-3' motif in vitro. Binds optimally to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. Binds poly(A). RNA-binding abilities are down-regulated by tyrosine kinase PTK6 (PubMed:10564820, PubMed:19561594, PubMed:26758068). Involved in splice site selection of vascular endothelial growth factor (PubMed:15901763). In vitro regulates CD44 alternative splicing by direct binding to purine-rich exonic enhancer (By similarity). Can regulate alternative splicing of neurexins NRXN1-3 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners such as neuroligins and LRRTM family members (PubMed:26758068). Targeted, cell-type specific splicing regulation of NRXN1 at AS4 is involved in neuronal glutamatergic synapse function and plasticity (By similarity). May regulate expression of KHDRBS2/SLIM-1 in defined brain neuron populations by modifying its alternative splicing (By similarity). Can bind FABP9 mRNA (By similarity). May play a role as a negative regulator of cell growth. Inhibits cell proliferation. {ECO:0000250|UniProtKB:Q9JLP1, ECO:0000250|UniProtKB:Q9R226, ECO:0000269|PubMed:10564820, ECO:0000269|PubMed:15901763, ECO:0000269|PubMed:19561594, ECO:0000269|PubMed:26758068}.; FUNCTION: (Microbial infection) Involved in post-transcriptional regulation of HIV-1 gene expression. {ECO:0000269|PubMed:11741900}.
|
Homo sapiens (Human)
|
O75528
|
TADA3_HUMAN
|
MSELKDCPLQFHDFKSVDHLKVCPRYTAVLARSEDDGIGIEELDTLQLELETLLSSASRRLRVLEAETQILTDWQDKKGDRRFLKLGRDHELGAPPKHGKPKKQKLEGKAGHGPGPGPGRPKSKNLQPKIQEYEFTDDPIDVPRIPKNDAPNRFWASVEPYCADITSEEVRTLEELLKPPEDEAEHYKIPPLGKHYSQRWAQEDLLEEQKDGARAAAVADKKKGLMGPLTELDTKDVDALLKKSEAQHEQPEDGCPFGALTQRLLQALVEENIISPMEDSPIPDMSGKESGADGASTSPRNQNKPFSVPHTKSLESRIKEELIAQGLLESEDRPAEDSEDEVLAELRKRQAELKALSAHNRTKKHDLLRLAKEEVSRQELRQRVRMADNEVMDAFRKIMAARQKKRTPTKKEKDQAWKTLKERESILKLLDG
| null | null |
chromatin organization [GO:0006325]; intracellular estrogen receptor signaling pathway [GO:0030520]; mitotic cell cycle [GO:0000278]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; regulation of cell cycle [GO:0051726]; regulation of cell division [GO:0051302]; regulation of DNA repair [GO:0006282]; regulation of DNA-templated transcription [GO:0006355]; regulation of embryonic development [GO:0045995]; regulation of protein phosphorylation [GO:0001932]; regulation of protein stability [GO:0031647]; regulation of RNA splicing [GO:0043484]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of tubulin deacetylation [GO:0090043]
|
ATAC complex [GO:0140672]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SAGA complex [GO:0000124]; transcription factor TFTC complex [GO:0033276]
|
nuclear receptor binding [GO:0016922]; nuclear receptor coactivator activity [GO:0030374]; protein domain specific binding [GO:0019904]; transcription coactivator activity [GO:0003713]
|
PF10198;
| null |
NGG1 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863, ECO:0000269|PubMed:9674425}.
| null | null | null | null | null |
FUNCTION: Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex. Also known as a coactivator for p53/TP53-dependent transcriptional activation. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. {ECO:0000269|PubMed:11707411, ECO:0000269|PubMed:19103755}.
|
Homo sapiens (Human)
|
O75529
|
TAF5L_HUMAN
|
MKRVRTEQIQMAVSCYLKRRQYVDSDGPLKQGLRLSQTAEEMAANLTVQSESGCANIVSAAPCQAEPQQYEVQFGRLRNFLTDSDSQHSHEVMPLLYPLFVYLHLNLVQNSPKSTVESFYSRFHGMFLQNASQKDVIEQLQTTQTIQDILSNFKLRAFLDNKYVVRLQEDSYNYLIRYLQSDNNTALCKVLTLHIHLDVQPAKRTDYQLYASGSSSRSENNGLEPPDMPSPILQNEAALEVLQESIKRVKDGPPSLTTICFYAFYNTEQLLNTAEISPDSKLLAAGFDNSCIKLWSLRSKKLKSEPHQVDVSRIHLACDILEEEDDEDDNAGTEMKILRGHCGPVYSTRFLADSSGLLSCSEDMSIRYWDLGSFTNTVLYQGHAYPVWDLDISPYSLYFASGSHDRTARLWSFDRTYPLRIYAGHLADVDCVKFHPNSNYLATGSTDKTVRLWSAQQGNSVRLFTGHRGPVLSLAFSPNGKYLASAGEDQRLKLWDLASGTLYKELRGHTDNITSLTFSPDSGLIASASMDNSVRVWDIRNTYCSAPADGSSSELVGVYTGQMSNVLSVQFMACNLLLVTGITQENQEH
| null | null |
positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA repair [GO:0006282]; regulation of DNA-templated transcription [GO:0006355]; regulation of RNA splicing [GO:0043484]; regulation of somatic stem cell population maintenance [GO:1904672]; regulation of transcription by RNA polymerase II [GO:0006357]; transcription by RNA polymerase II [GO:0006366]
|
cytoplasmic ribonucleoprotein granule [GO:0036464]; histone acetyltransferase complex [GO:0000123]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; SAGA complex [GO:0000124]; transcription factor TFTC complex [GO:0033276]
|
transcription coactivator activity [GO:0003713]
|
PF04494;PF00400;
|
1.25.40.500;2.130.10.10;
|
WD repeat TAF5 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863, ECO:0000269|PubMed:9674425}.
| null | null | null | null | null |
FUNCTION: Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex (Probable). With TAF6L, acts as an epigenetic regulator essential for somatic reprogramming. Regulates target genes through H3K9ac deposition and MYC recruitment which trigger MYC regulatory network to orchestrate gene expression programs to control embryonic stem cell state (By similarity). {ECO:0000250|UniProtKB:Q91WQ5, ECO:0000305|PubMed:9674419}.
|
Homo sapiens (Human)
|
O75530
|
EED_HUMAN
|
MSEREVSTAPAGTDMPAAKKQKLSSDENSNPDLSGDENDDAVSIESGTNTERPDTPTNTPNAPGRKSWGKGKWKSKKCKYSFKCVNSLKEDHNQPLFGVQFNWHSKEGDPLVFATVGSNRVTLYECHSQGEIRLLQSYVDADADENFYTCAWTYDSNTSHPLLAVAGSRGIIRIINPITMQCIKHYVGHGNAINELKFHPRDPNLLLSVSKDHALRLWNIQTDTLVAIFGGVEGHRDEVLSADYDLLGEKIMSCGMDHSLKLWRINSKRMMNAIKESYDYNPNKTNRPFISQKIHFPDFSTRDIHRNYVDCVRWLGDLILSKSCENAIVCWKPGKMEDDIDKIKPSESNVTILGRFDYSQCDIWYMRFSMDFWQKMLALGNQVGKLYVWDLEVEDPHKAKCTTLTHHKCGAAIRQTSFSRDSSILIAVCDDASIWRWDRLR
| null | null |
negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; spinal cord development [GO:0021510]
|
chromosome [GO:0005694]; cytosol [GO:0005829]; ESC/E(Z) complex [GO:0035098]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
enzyme activator activity [GO:0008047]; histone methyltransferase activity [GO:0042054]; identical protein binding [GO:0042802]; nucleosome binding [GO:0031491]; transcription corepressor binding [GO:0001222]
|
PF00400;
|
2.130.10.10;
|
WD repeat ESC family
|
PTM: Methylated. Binding to histone H1 'Lys-26' promotes mono-, di-, and trimethylation of internal lysines. {ECO:0000269|PubMed:20974918}.
|
SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Transiently colocalizes with XIST at inactive X chromosomes.
| null | null | null | null | null |
FUNCTION: Polycomb group (PcG) protein. Component of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Also recognizes 'Lys-26' trimethylated histone H1 with the effect of inhibiting PRC2 complex methyltransferase activity on nucleosomal histone H3 'Lys-27', whereas H3 'Lys-27' recognition has the opposite effect, enabling the propagation of this repressive mark. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1 and CDKN2A. {ECO:0000269|PubMed:10581039, ECO:0000269|PubMed:14532106, ECO:0000269|PubMed:15225548, ECO:0000269|PubMed:15231737, ECO:0000269|PubMed:15385962, ECO:0000269|PubMed:16357870, ECO:0000269|PubMed:18285464, ECO:0000269|PubMed:20974918, ECO:0000269|PubMed:28229514, ECO:0000269|PubMed:9584199}.
|
Homo sapiens (Human)
|
O75531
|
BAF_HUMAN
|
MTTSQKHRDFVAEPMGEKPVGSLAGIGEVLGKKLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL
| null | null |
chromatin organization [GO:0006325]; chromosome organization [GO:0051276]; DNA integration [GO:0015074]; mitotic nuclear membrane reassembly [GO:0007084]; negative regulation of cGAS/STING signaling pathway [GO:0160049]; negative regulation of innate immune response [GO:0045824]; negative regulation of protein ADP-ribosylation [GO:0010836]; negative regulation of type I interferon production [GO:0032480]; negative regulation of viral genome replication [GO:0045071]; response to oxidative stress [GO:0006979]; response to virus [GO:0009615]
|
chromatin [GO:0000785]; condensed chromosome [GO:0000793]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]
|
PF02961;
|
1.10.150.40;
|
BAF family
|
PTM: Ser-4 is the major site of phosphorylation as compared to Thr-2 and Thr-3. Phosphorylation on Thr-2; Thr-3 and Ser-4 disrupts its ability to bind DNA and reduces its ability to bind LEM domain-containing proteins. Non phosphorylated BAF seems to enhance binding between EMD and LMNA. Dephosphorylated by protein phosphatase 2A (PP2A) following interaction with ANKLE2/LEM4 during mitotic exit, leading to mitotic nuclear envelope reassembly. {ECO:0000269|PubMed:16371512, ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:22770216}.; PTM: (Microbial infection) Phosphorylated by poxvirus B1 kinase (VPK1) on serine and threonine residues, leading to BANF1 relocalization to the cytoplasm, loss of dimerization and impaired DNA binding activity. {ECO:0000269|PubMed:18005698, ECO:0000269|PubMed:24600006}.; PTM: (Microbial infection) Phosphorylated at the N-terminus by vaccinia virus (VacV) B1 kinase, leading to BANF1 relocalization to the cytoplasm, loss of dimerization and impaired DNA binding activity (PubMed:16495336, PubMed:24600006). Hyperphosphorylation is linked to the loss of ability to suppress vaccinia virus replication (PubMed:24600006). {ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:24600006}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:18005698, ECO:0000269|PubMed:24600006}. Chromosome {ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:28841419, ECO:0000269|PubMed:31796734, ECO:0000269|PubMed:32792394}. Nucleus envelope {ECO:0000269|PubMed:24600006}. Cytoplasm {ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:18005698, ECO:0000269|PubMed:24600006}. Note=Significantly enriched at the nuclear inner membrane, diffusely throughout the nucleus during interphase and concentrated at the chromosomes during the M-phase (PubMed:16495336, PubMed:24600006). The phosphorylated form (by VRK1) shows a cytoplasmic localization whereas the unphosphorylated form locates almost exclusively in the nucleus (PubMed:16495336, PubMed:24600006). May be included in HIV-1 virions via its interaction with viral GAG polyprotein (PubMed:14645565). {ECO:0000269|PubMed:14645565, ECO:0000269|PubMed:16495336, ECO:0000269|PubMed:24600006}.
| null | null | null | null | null |
FUNCTION: Non-specific DNA-binding protein that plays key roles in mitotic nuclear reassembly, chromatin organization, DNA damage response, gene expression and intrinsic immunity against foreign DNA (PubMed:10908652, PubMed:11792822, PubMed:12163470, PubMed:18005698, PubMed:25991860, PubMed:28841419, PubMed:31796734, PubMed:32792394). Contains two non-specific double-stranded DNA (dsDNA)-binding sites which promote DNA cross-bridging (PubMed:9465049). Plays a key role in nuclear membrane reformation at the end of mitosis by driving formation of a single nucleus in a spindle-independent manner (PubMed:28841419). Transiently cross-bridges anaphase chromosomes via its ability to bridge distant DNA sites, leading to the formation of a dense chromatin network at the chromosome ensemble surface that limits membranes to the surface (PubMed:28841419). Also acts as a negative regulator of innate immune activation by restricting CGAS activity toward self-DNA upon acute loss of nuclear membrane integrity (PubMed:32792394). Outcompetes CGAS for DNA-binding, thereby preventing CGAS activation and subsequent damaging autoinflammatory responses (PubMed:32792394). Also involved in DNA damage response: interacts with PARP1 in response to oxidative stress, thereby inhibiting the ADP-ribosyltransferase activity of PARP1 (PubMed:31796734). Involved in the recognition of exogenous dsDNA in the cytosol: associates with exogenous dsDNA immediately after its appearance in the cytosol at endosome breakdown and is required to avoid autophagy (PubMed:25991860). In case of poxvirus infection, has an antiviral activity by blocking viral DNA replication (PubMed:18005698). {ECO:0000269|PubMed:10908652, ECO:0000269|PubMed:11792822, ECO:0000269|PubMed:12163470, ECO:0000269|PubMed:18005698, ECO:0000269|PubMed:25991860, ECO:0000269|PubMed:28841419, ECO:0000269|PubMed:31796734, ECO:0000269|PubMed:32792394, ECO:0000269|PubMed:9465049}.; FUNCTION: (Microbial infection) Exploited by retroviruses for inhibiting self-destructing autointegration of retroviral DNA, thereby promoting integration of viral DNA into the host chromosome (PubMed:11005805, PubMed:16680152, PubMed:9465049). EMD and BAF are cooperative cofactors of HIV-1 infection (PubMed:16680152). Association of EMD with the viral DNA requires the presence of BAF and viral integrase (PubMed:16680152). The association of viral DNA with chromatin requires the presence of BAF and EMD (PubMed:16680152). {ECO:0000269|PubMed:11005805, ECO:0000269|PubMed:16680152, ECO:0000269|PubMed:9465049}.
|
Homo sapiens (Human)
|
O75533
|
SF3B1_HUMAN
|
MAKIAKTHEDIEAQIREIQGKKAALDEAQGVGLDSTGYYDQEIYGGSDSRFAGYVTSIAATELEDDDDDYSSSTSLLGQKKPGYHAPVALLNDIPQSTEQYDPFAEHRPPKIADREDEYKKHRRTMIISPERLDPFADGGKTPDPKMNARTYMDVMREQHLTKEEREIRQQLAEKAKAGELKVVNGAAASQPPSKRKRRWDQTADQTPGATPKKLSSWDQAETPGHTPSLRWDETPGRAKGSETPGATPGSKIWDPTPSHTPAGAATPGRGDTPGHATPGHGGATSSARKNRWDETPKTERDTPGHGSGWAETPRTDRGGDSIGETPTPGASKRKSRWDETPASQMGGSTPVLTPGKTPIGTPAMNMATPTPGHIMSMTPEQLQAWRWEREIDERNRPLSDEELDAMFPEGYKVLPPPAGYVPIRTPARKLTATPTPLGGMTGFHMQTEDRTMKSVNDQPSGNLPFLKPDDIQYFDKLLVDVDESTLSPEEQKERKIMKLLLKIKNGTPPMRKAALRQITDKAREFGAGPLFNQILPLLMSPTLEDQERHLLVKVIDRILYKLDDLVRPYVHKILVVIEPLLIDEDYYARVEGREIISNLAKAAGLATMISTMRPDIDNMDEYVRNTTARAFAVVASALGIPSLLPFLKAVCKSKKSWQARHTGIKIVQQIAILMGCAILPHLRSLVEIIEHGLVDEQQKVRTISALAIAALAEAATPYGIESFDSVLKPLWKGIRQHRGKGLAAFLKAIGYLIPLMDAEYANYYTREVMLILIREFQSPDEEMKKIVLKVVKQCCGTDGVEANYIKTEILPPFFKHFWQHRMALDRRNYRQLVDTTVELANKVGAAEIISRIVDDLKDEAEQYRKMVMETIEKIMGNLGAADIDHKLEEQLIDGILYAFQEQTTEDSVMLNGFGTVVNALGKRVKPYLPQICGTVLWRLNNKSAKVRQQAADLISRTAVVMKTCQEEKLMGHLGVVLYEYLGEEYPEVLGSILGALKAIVNVIGMHKMTPPIKDLLPRLTPILKNRHEKVQENCIDLVGRIADRGAEYVSAREWMRICFELLELLKAHKKAIRRATVNTFGYIAKAIGPHDVLATLLNNLKVQERQNRVCTTVAIAIVAETCSPFTVLPALMNEYRVPELNVQNGVLKSLSFLFEYIGEMGKDYIYAVTPLLEDALMDRDLVHRQTASAVVQHMSLGVYGFGCEDSLNHLLNYVWPNVFETSPHVIQAVMGALEGLRVAIGPCRMLQYCLQGLFHPARKVRDVYWKIYNSIYIGSQDALIAHYPRIYNDDKNTYIRYELDYIL
| null | null |
chromatin remodeling [GO:0006338]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of transcription by RNA polymerase I [GO:0045943]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription by RNA polymerase III [GO:0045945]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]; spliceosomal complex assembly [GO:0000245]; U2-type prespliceosome assembly [GO:1903241]
|
B-WICH complex [GO:0110016]; catalytic step 2 spliceosome [GO:0071013]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]; U11/U12 snRNP [GO:0034693]; U12-type spliceosomal complex [GO:0005689]; U2 snRNP [GO:0005686]; U2-type precatalytic spliceosome [GO:0071005]; U2-type prespliceosome [GO:0071004]; U2-type spliceosomal complex [GO:0005684]
|
mRNA binding [GO:0003729]; RNA binding [GO:0003723]; splicing factor binding [GO:1990935]
|
PF08920;
|
1.25.10.10;
|
SF3B1 family
|
PTM: Phosphorylated. Phosphorylation occurs concomitantly with the splicing catalytic steps. Phosphorylation on Thr-244, Thr-248 and Thr-313 by cyclin-dependent kinases promotes interaction with PPP1R8 during mitosis. {ECO:0000269|PubMed:12105215, ECO:0000269|PubMed:9585501}.; PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q99NB9}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27720643, ECO:0000269|PubMed:28541300, ECO:0000269|PubMed:34023904}. Nucleus speckle {ECO:0000269|PubMed:12105215, ECO:0000269|PubMed:28541300, ECO:0000269|PubMed:34023904}. Note=During mitosis, transiently dispersed from the nuclear speckles to the cytoplasm. {ECO:0000269|PubMed:12105215}.
| 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:12234937, PubMed:27720643, PubMed:32494006, PubMed:34822310). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing (PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, SF3B1 is part of the SF3B subcomplex, which is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence in pre-mRNA (PubMed:12234937). Sequence independent binding of SF3A and SF3B subcomplexes upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA (PubMed:12234937). May also be involved in the assembly of the 'E' complex (PubMed:10882114). Also acts as a component of the minor spliceosome, which is involved in the splicing of U12-type introns in pre-mRNAs (PubMed:15146077, PubMed:33509932). Together with other U2 snRNP complex components may also play a role in the selective processing of microRNAs (miRNAs) from the long primary miRNA transcript, pri-miR-17-92 (By similarity). {ECO:0000250|UniProtKB:Q99NB9, ECO:0000269|PubMed:10882114, ECO:0000269|PubMed:12234937, ECO:0000269|PubMed:15146077, ECO:0000269|PubMed:27720643, ECO:0000269|PubMed:32494006, ECO:0000269|PubMed:33509932, ECO:0000269|PubMed:34822310}.
|
Homo sapiens (Human)
|
O75534
|
CSDE1_HUMAN
|
MSFDPNLLHNNGHNGYPNGTSAALRETGVIEKLLTSYGFIQCSERQARLFFHCSQYNGNLQDLKVGDDVEFEVSSDRRTGKPIAVKLVKIKQEILPEERMNGQVVCAVPHNLESKSPAAPGQSPTGSVCYERNGEVFYLTYTPEDVEGNVQLETGDKINFVIDNNKHTGAVSARNIMLLKKKQARCQGVVCAMKEAFGFIERGDVVKEIFFHYSEFKGDLETLQPGDDVEFTIKDRNGKEVATDVRLLPQGTVIFEDISIEHFEGTVTKVIPKVPSKNQNDPLPGRIKVDFVIPKELPFGDKDTKSKVTLLEGDHVRFNISTDRRDKLERATNIEVLSNTFQFTNEAREMGVIAAMRDGFGFIKCVDRDVRMFFHFSEILDGNQLHIADEVEFTVVPDMLSAQRNHAIRIKKLPKGTVSFHSHSDHRFLGTVEKEATFSNPKTTSPNKGKEKEAEDGIIAYDDCGVKLTIAFQAKDVEGSTSPQIGDKVEFSISDKQRPGQQVATCVRLLGRNSNSKRLLGYVATLKDNFGFIETANHDKEIFFHYSEFSGDVDSLELGDMVEYSLSKGKGNKVSAEKVNKTHSVNGITEEADPTIYSGKVIRPLRSVDPTQTEYQGMIEIVEEGDMKGEVYPFGIVGMANKGDCLQKGESVKFQLCVLGQNAQTMAYNITPLRRATVECVKDQFGFINYEVGDSKKLFFHVKEVQDGIELQAGDEVEFSVILNQRTGKCSACNVWRVCEGPKAVAAPRPDRLVNRLKNITLDDASAPRLMVLRQPRGPDNSMGFGAERKIRQAGVID
| null | null |
CRD-mediated mRNA stabilization [GO:0070934]; IRES-dependent viral translational initiation [GO:0075522]; male gonad development [GO:0008584]; negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:1900152]; nuclear-transcribed mRNA catabolic process, no-go decay [GO:0070966]; positive regulation of cytoplasmic translation [GO:2000767]; regulation of translational initiation [GO:0006446]; stress granule assembly [GO:0034063]
|
CRD-mediated mRNA stability complex [GO:0070937]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; mCRD-mediated mRNA stability complex [GO:0106002]; P-body [GO:0000932]; plasma membrane [GO:0005886]
|
RISC complex binding [GO:1905172]; RNA binding [GO:0003723]; RNA stem-loop binding [GO:0035613]
|
PF00313;PF12901;
|
2.40.50.140;
|
UNR family
| null |
SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, Stress granule {ECO:0000305|PubMed:29395067}. Cytoplasm, P-body {ECO:0000269|PubMed:32354837}.
| null | null | null | null | null |
FUNCTION: RNA-binding protein involved in translationally coupled mRNA turnover (PubMed:11051545, PubMed:15314026). Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain (PubMed:11051545, PubMed:15314026). Required for efficient formation of stress granules (PubMed:29395067). {ECO:0000269|PubMed:11051545, ECO:0000269|PubMed:15314026, ECO:0000269|PubMed:29395067}.; FUNCTION: (Microbial infection) Required for internal initiation of translation of human rhinovirus RNA. {ECO:0000269|PubMed:10049359}.
|
Homo sapiens (Human)
|
O75553
|
DAB1_HUMAN
|
MSTETELQVAVKTSAKKDSRKKGQDRSEATLIKRFKGEGVRYKAKLIGIDEVSAARGDKLCQDSMMKLKGVVAGARSKGEHKQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYIAKDITDHRAFGYVCGKEGNHRFVAIKTAQAAEPVILDLRDLFQLIYELKQREELEKKAQKDKQCEQAVYQTILEEDVEDPVYQYIVFEAGHEPIRDPETEENIYQVPTSQKKEGVYDVPKSQPVSNGYSFEDFEERFAAATPNRNLPTDFDEIFEATKAVTQLELFGDMSTPPDITSPPTPATPGDAFIPSSSQTLPASADVFSSVPFGTAAVPSGYVAMGAVLPSFWGQQPLVQQQMVMGAQPPVAQVMPGAQPIAWGQPGLFPATQQPWPTVAGQFPPAAFMPTQTVMPLPAAMFQGPLTPLATVPGTSDSTRSSPQTDKPRQKMGKETFKDFQMAQPPPVPSRKPDQPSLTCTSEAFSSYFNKVGVAQDTDDCDDFDISQLNLTPVTSTTPSTNSPPTPAPRQSSPSKSSASHASDPTTDDIFEEGFESPSKSEEQEAPDGSQASSNSDPFGEPSGEPSGDNISPQAGS
| null | null |
adult walking behavior [GO:0007628]; astrocyte differentiation [GO:0048708]; axonogenesis [GO:0007409]; cell-cell adhesion involved in neuronal-glial interactions involved in cerebral cortex radial glia guided migration [GO:0021813]; cerebellum structural organization [GO:0021589]; dendrite development [GO:0016358]; Golgi localization [GO:0051645]; hippocampus development [GO:0021766]; lateral motor column neuron migration [GO:0097477]; negative regulation of astrocyte differentiation [GO:0048712]; negative regulation of axonogenesis [GO:0050771]; negative regulation of cell adhesion [GO:0007162]; negative regulation of receptor signaling pathway via JAK-STAT [GO:0046426]; neuron migration [GO:0001764]; positive regulation of neuron differentiation [GO:0045666]; radial glia guided migration of Purkinje cell [GO:0021942]; radial glia-guided pyramidal neuron migration [GO:0140650]; receptor signaling pathway via JAK-STAT [GO:0007259]; small GTPase-mediated signal transduction [GO:0007264]; ventral spinal cord development [GO:0021517]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; perinuclear region of cytoplasm [GO:0048471]
| null |
PF21792;PF00640;
|
2.30.29.30;
| null |
PTM: Phosphorylated on Tyr-198 and Tyr-220 upon reelin induction in embryonic neurons. Also phosphorylated on Ser-524 independently of reelin signaling. {ECO:0000250|UniProtKB:P97318}.
| null | null | null | null | null | null |
FUNCTION: Adapter molecule functioning in neural development. May regulate SIAH1 activity. {ECO:0000250|UniProtKB:P97318}.
|
Homo sapiens (Human)
|
O75554
|
WBP4_HUMAN
|
MADYWKSQPKKFCDYCKCWIADNRPSVEFHERGKNHKENVAKRISEIKQKSLDKAKEEEKASKEFAAMEAAALKAYQEDLKRLGLESEILEPSITPVTSTIPPTSTSNQQKEKKEKKKRKKDPSKGRWVEGITSEGYHYYYDLISGASQWEKPEGFQGDLKKTAVKTVWVEGLSEDGFTYYYNTETGESRWEKPDDFIPHTSDLPSSKVNENSLGTLDESKSSDSHSDSDGEQEAEEGGVSTETEKPKIKFKEKNKNSDGGSDPETQKEKSIQKQNSLGSNEEKSKTLKKSNPYGEWQEIKQEVESHEEVDLELPSTENEYVSTSEADGGGEPKVVFKEKTVTSLGVMADGVAPVFKKRRTENGKSRNLRQRGDDQ
| null | null |
mRNA cis splicing, via spliceosome [GO:0045292]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]
|
nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; precatalytic spliceosome [GO:0071011]; U2-type precatalytic spliceosome [GO:0071005]
|
proline-rich region binding [GO:0070064]; RNA binding [GO:0003723]; zinc ion binding [GO:0008270]
|
PF00397;PF06220;
|
2.20.70.10;3.30.160.60;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28781166}. Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00130, ECO:0000269|PubMed:19592703, ECO:0000269|PubMed:9724750}.
| null | null | null | null | null |
FUNCTION: Involved in pre-mRNA splicing as a component of the spliceosome (PubMed:19592703, PubMed:28781166, PubMed:9724750). May play a role in cross-intron bridging of U1 and U2 snRNPs in the mammalian A complex (PubMed:9724750). {ECO:0000269|PubMed:19592703, ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:9724750}.
|
Homo sapiens (Human)
|
O75556
|
SG2A1_HUMAN
|
MKLLMVLMLAALLLHCYADSGCKLLEDMVEKTINSDISIPEYKELLQEFIDSDAAAEAMGKFKQCFLNQSHRTLKNFGLMMHTVYDSIWCNMKSN
| null | null |
androgen receptor signaling pathway [GO:0030521]
|
extracellular space [GO:0005615]
| null |
PF01099;
| null |
Secretoglobin family, Lipophilin subfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: May bind androgens and other steroids, may also bind estramustine, a chemotherapeutic agent used for prostate cancer. May be under transcriptional regulation of steroid hormones.
|
Homo sapiens (Human)
|
O75558
|
STX11_HUMAN
|
MKDRLAELLDLSKQYDQQFPDGDDEFDSPHEDIVFETDHILESLYRDIRDIQDENQLLVADVKRLGKQNARFLTSMRRLSSIKRDTNSIAKAIKARGEVIHCKLRAMKELSEAAEAQHGPHSAVARISRAQYNALTLTFQRAMHDYNQAEMKQRDNCKIRIQRQLEIMGKEVSGDQIEDMFEQGKWDVFSENLLADVKGARAALNEIESRHRELLRLESRIRDVHELFLQMAVLVEKQADTLNVIELNVQKTVDYTGQAKAQVRKAVQYEEKNPCRTLCCFCCPCLK
| null | null |
exocytosis [GO:0006887]; intracellular protein transport [GO:0006886]; membrane fusion [GO:0061025]; synaptic vesicle fusion to presynaptic active zone membrane [GO:0031629]; vesicle docking [GO:0048278]
|
endomembrane system [GO:0012505]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]; presynaptic active zone membrane [GO:0048787]; SNARE complex [GO:0031201]; synaptic vesicle [GO:0008021]
|
SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]
|
PF00804;
|
1.20.5.110;1.20.58.70;
|
Syntaxin family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: SNARE that acts to regulate protein transport between late endosomes and the trans-Golgi network.
|
Homo sapiens (Human)
|
O75563
|
SKAP2_HUMAN
|
MPNPSSTSSPYPLPEEIRNLLADVETFVADILKGENLSKKAKEKRESLIKKIKDVKSIYLQEFQDKGDAEDGEEYDDPFAGPPDTISLASERYDKDDEAPSDGAQFPPIAAQDLPFVLKAGYLEKRRKDHSFLGFEWQKRWCALSKTVFYYYGSDKDKQQKGEFAIDGYSVRMNNTLRKDGKKDCCFEISAPDKRIYQFTAASPKDAEEWVQQLKFVLQDMESDIIPEDYDERGELYDDVDHPLPISNPLTSSQPIDDEIYEELPEEEEDSAPVKVEEQRKMSQDSVHHTSGDKSTDYANFYQGLWDCTGAFSDELSFKRGDVIYILSKEYNRYGWWVGEMKGAIGLVPKAYIMEMYDI
| null | null |
B cell activation [GO:0042113]; negative regulation of cell population proliferation [GO:0008285]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
| null |
PF00169;PF00018;
|
6.10.250.220;2.30.29.30;2.30.30.40;
|
SKAP family
|
PTM: Phosphorylated in resting platelets. Phosphorylated by FYN on Tyr-261 upon T-cell activation (Probable). Dephosphorylated on Tyr-75 by PTPN22. {ECO:0000269|PubMed:10942756, ECO:0000269|PubMed:12893833, ECO:0000269|PubMed:21719704, ECO:0000269|PubMed:9671755, ECO:0000269|PubMed:9755858, ECO:0000305}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12893833}.
| null | null | null | null | null |
FUNCTION: May be involved in B-cell and macrophage adhesion processes. In B-cells, may act by coupling the B-cell receptor (BCR) to integrin activation. May play a role in src signaling pathway. {ECO:0000269|PubMed:12893833, ECO:0000269|PubMed:9837776}.
|
Homo sapiens (Human)
|
O75564
|
JERKY_HUMAN
|
MASKPAAGKSRGEKRKRVVLTLKEKIDICTRLEKGESRKALMQEYNVGMSTLYDIRAHKAQLLRFFASSDSNKALEQRRTLHTPKLEHLDRVLYEWFLGKRSEGVPVSGPMLIEKAKDFYEQMQLTEPCVFSGGWLWRFKARHGIKKLDASSEKQSADHQAAEQFCAFFRSLAAEHGLSAEQVYNADETGLFWRCLPNPTPEGGAVPGPKQGKDRLTVLMCANATGSHRLKPLAIGKCSGPRAFKGIQHLPVAYKAQGNAWVDKEIFSDWFHHIFVPSVREHFRTIGLPEDSKAVLLLDSSRAHPQEAELVSSNVFTIFLPASVASLVQPMEQGIRRDFMRNFINPPVPLQGPHARYNMNDAIFSVACAWNAVPSHVFRRAWRKLWPSVAFAEGSSSEEELEAECFPVKPHNKSFAHILELVKEGSSCPGQLRQRQAASWGVAGREAEGGRPPAATSPAEVVWSSEKTPKADQDGRGDPGEGEEVAWEQAAVAFDAVLRFAERQPCFSAQEVGQLRALRAVFRSQQQETVGLEDVVVTSPEELAIPKCCLEASTET
| null | null |
positive regulation of canonical Wnt signaling pathway [GO:0090263]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]
|
DNA binding [GO:0003677]; mRNA binding [GO:0003729]
|
PF04218;PF03184;PF03221;
|
1.10.10.60;
|
Tigger transposable element derived protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00583}.
| null | null | null | null | null |
FUNCTION: May bind DNA. {ECO:0000250}.
|
Homo sapiens (Human)
|
O75569
|
PRKRA_HUMAN
|
MSQSRHRAEAPPLEREDSGTFSLGKMITAKPGKTPIQVLHEYGMKTKNIPVYECERSDVQIHVPTFTFRVTVGDITCTGEGTSKKLAKHRAAEAAINILKANASICFAVPDPLMPDPSKQPKNQLNPIGSLQELAIHHGWRLPEYTLSQEGGPAHKREYTTICRLESFMETGKGASKKQAKRNAAEKFLAKFSNISPENHISLTNVVGHSLGCTWHSLRNSPGEKINLLKRSLLSIPNTDYIQLLSEIAKEQGFNITYLDIDELSANGQYQCLAELSTSPITVCHGSGISCGNAQSDAAHNALQYLKIIAERK
| null | null |
antiviral innate immune response [GO:0140374]; cellular response to oxidative stress [GO:0034599]; immune response [GO:0006955]; middle ear morphogenesis [GO:0042474]; miRNA processing [GO:0035196]; negative regulation of cell population proliferation [GO:0008285]; outer ear morphogenesis [GO:0042473]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; pre-miRNA processing [GO:0031054]; protein stabilization [GO:0050821]; regulation of regulatory ncRNA processing [GO:0070920]; response to virus [GO:0009615]; RISC complex assembly [GO:0070922]; siRNA processing [GO:0030422]; skeletal system morphogenesis [GO:0048705]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; RISC complex [GO:0016442]; RISC-loading complex [GO:0070578]
|
double-stranded RNA binding [GO:0003725]; enzyme activator activity [GO:0008047]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; pre-miRNA binding [GO:0070883]; protein homodimerization activity [GO:0042803]; protein kinase activator activity [GO:0030295]; RNA binding [GO:0003723]; siRNA binding [GO:0035197]
|
PF00035;
|
3.30.160.20;
|
PRKRA family
|
PTM: Phosphorylated at Ser-246 in unstressed cells and at Ser-287 in stressed cells. Phosphorylation at Ser-246 appears to be a prerequisite for subsequent phosphorylation at Ser-287. Phosphorylation at Ser-246 and Ser-287 are necessary for activation of EIF2AK2/PKR under conditions of stress. {ECO:0000269|PubMed:16982605}.
|
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Cytoplasm.
| null | null | null | null | null |
FUNCTION: Activates EIF2AK2/PKR in the absence of double-stranded RNA (dsRNA), leading to phosphorylation of EIF2S1/EFI2-alpha and inhibition of translation and induction of apoptosis. Required for siRNA production by DICER1 and for subsequent siRNA-mediated post-transcriptional gene silencing. Does not seem to be required for processing of pre-miRNA to miRNA by DICER1. Promotes UBC9-p53/TP53 association and sumoylation and phosphorylation of p53/TP53 at 'Lys-386' at 'Ser-392' respectively and enhances its activity in a EIF2AK2/PKR-dependent manner (By similarity). {ECO:0000250, ECO:0000269|PubMed:10336432, ECO:0000269|PubMed:11238927, ECO:0000269|PubMed:16424907, ECO:0000269|PubMed:16982605, ECO:0000269|PubMed:17452327, ECO:0000269|PubMed:9687506}.
|
Homo sapiens (Human)
|
O75570
|
RF1M_HUMAN
|
MNRHLCVWLFRHPSLNGYLQCHIQLHSHQFRQIHLDTRLQVFRQNRNCILHLLSKNWSRRYCHQDTKMLWKHKALQKYMENLSKEYQTLEQCLQHIPVNEENRRSLNRRHAELAPLAAIYQEIQETEQAIEELESMCKSLNKQDEKQLQELALEERQTIDQKINMLYNELFQSLVPKEKYDKNDVILEVTAGRTTGGDICQQFTREIFDMYQNYSCYKHWQFELLNYTPADYGGLHHAAARISGDGVYKHLKYEGGIHRVQRIPEVGLSSRMQRIHTGTMSVIVLPQPDEVDVKLDPKDLRIDTFRAKGAGGQHVNKTDSAVRLVHIPTGLVVECQQERSQIKNKEIAFRVLRARLYQQIIEKDKRQQQSARKLQVGTRAQSERIRTYNFTQDRVSDHRIAYEVRDIKEFLCGGKGLDQLIQRLLQSADEEAIAELLDEHLKSAK
| null | null |
mitochondrial translational termination [GO:0070126]
|
mitochondrion [GO:0005739]
|
translation release factor activity [GO:0003747]; translation release factor activity, codon specific [GO:0016149]
|
PF03462;PF00472;
|
3.30.160.20;3.30.70.1660;6.10.140.1950;
|
Prokaryotic/mitochondrial release factor family
|
PTM: Methylation of glutamine in the GGQ triplet by HEMK1 is conserved from bacteria to mammals. {ECO:0000269|PubMed:35260756}.
|
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:17803939, ECO:0000269|PubMed:37141370}.
| null | null | null | null | null |
FUNCTION: Mitochondrial peptide chain release factor that directs the termination of translation in response to the peptide chain non-canonical stop codons AGG and AGA (PubMed:36302763, PubMed:36596788, PubMed:37141370). Non-canonical termination codons AGG and AGA are found at the end of MT-CO1/COX1 and MT-ND6/ND6 open reading frames, respectively (PubMed:37141370). Recognizes non-canonical stop codons via a network of interactions between the codon, MTRF1 and the ribosomal RNA (rRNA): in contrast to other translation release factors, which identify the codon in the A-site via direct interactions of amino acid side chains with the bases, MTRF1 repositions the first 2 bases of the stop codon to use an intricate network of interactions that includes residues of the release factor, the rRNA of the small ribosomal subunit, as well as neighboring bases of the mRNA (PubMed:37141370). {ECO:0000269|PubMed:36302763, ECO:0000269|PubMed:36596788, ECO:0000269|PubMed:37141370}.
|
Homo sapiens (Human)
|
O75575
|
RPC9_HUMAN
|
MEVKDANSALLSNYEVFQLLTDLKEQRKESGKNKHSSGQQNLNTITYETLKYISKTPCRHQSPEIVREFLTALKSHKLTKAEKLQLLNHRPVTAVEIQLMVEESEERLTEEQIEALLHTVTSILPAEPEAEQKKNTNSNVAMDEEDPA
| null | null |
defense response to virus [GO:0051607]; innate immune response [GO:0045087]; neuropeptide signaling pathway [GO:0007218]; transcription by RNA polymerase III [GO:0006383]; transcription initiation at RNA polymerase III promoter [GO:0006384]
|
acrosomal vesicle [GO:0001669]; cytosol [GO:0005829]; DNA polymerase III complex [GO:0009360]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; RNA polymerase III complex [GO:0005666]
|
calcitonin gene-related peptide receptor activity [GO:0001635]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; nucleotide binding [GO:0000166]
|
PF03874;
|
1.20.1250.40;
|
Eukaryotic RPC9 RNA polymerase subunit family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:33335104}. Cell membrane {ECO:0000250|UniProtKB:O35427}; Peripheral membrane protein {ECO:0000250|UniProtKB:O35427}; Cytoplasmic side {ECO:0000250|UniProtKB:O35427}.
| null | null | null | null | null |
FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (PubMed:20413673, PubMed:33558764, PubMed:34675218). Specific peripheric component of RNA polymerase III (Pol III) which synthesizes small non-coding RNAs including 5S rRNA, snRNAs, tRNAs and miRNAs from at least 500 distinct genomic loci. With POLR3H/RPC8 forms a mobile stalk that protrudes from Pol III core and functions primarily in transcription initiation (By similarity) (PubMed:20413673, PubMed:33558764, PubMed:33558766, PubMed:34675218). Pol III plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF-kappa-B through the RIG-I pathway (PubMed:19609254, PubMed:19631370). {ECO:0000250|UniProtKB:Q9C0Z9, ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370, ECO:0000269|PubMed:20413673, ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:33558766, ECO:0000269|PubMed:34675218}.; FUNCTION: Accessory protein for the calcitonin gene-related peptide (CGRP) receptor. It modulates CGRP responsiveness in a variety of tissues. {ECO:0000250|UniProtKB:O35427}.
|
Homo sapiens (Human)
|
O75578
|
ITA10_HUMAN
|
MELPFVTHLFLPLVFLTGLCSPFNLDEHHPRLFPGPPEAEFGYSVLQHVGGGQRWMLVGAPWDGPSGDRRGDVYRCPVGGAHNAPCAKGHLGDYQLGNSSHPAVNMHLGMSLLETDGDGGFMACAPLWSRACGSSVFSSGICARVDASFQPQGSLAPTAQRCPTYMDVVIVLDGSNSIYPWSEVQTFLRRLVGKLFIDPEQIQVGLVQYGESPVHEWSLGDFRTKEEVVRAAKNLSRREGRETKTAQAIMVACTEGFSQSHGGRPEAARLLVVVTDGESHDGEELPAALKACEAGRVTRYGIAVLGHYLRRQRDPSSFLREIRTIASDPDERFFFNVTDEAALTDIVDALGDRIFGLEGSHAENESSFGLEMSQIGFSTHRLKDGILFGMVGAYDWGGSVLWLEGGHRLFPPRMALEDEFPPALQNHAAYLGYSVSSMLLRGGRRLFLSGAPRFRHRGKVIAFQLKKDGAVRVAQSLQGEQIGSYFGSELCPLDTDRDGTTDVLLVAAPMFLGPQNKETGRVYVYLVGQQSLLTLQGTLQPEPPQDARFGFAMGALPDLNQDGFADVAVGAPLEDGHQGALYLYHGTQSGVRPHPAQRIAAASMPHALSYFGRSVDGRLDLDGDDLVDVAVGAQGAAILLSSRPIVHLTPSLEVTPQAISVVQRDCRRRGQEAVCLTAALCFQVTSRTPGRWDHQFYMRFTASLDEWTAGARAAFDGSGQRLSPRRLRLSVGNVTCEQLHFHVLDTSDYLRPVALTVTFALDNTTKPGPVLNEGSPTSIQKLVPFSKDCGPDNECVTDLVLQVNMDIRGSRKAPFVVRGGRRKVLVSTTLENRKENAYNTSLSLIFSRNLHLASLTPQRESPIKVECAAPSAHARLCSVGHPVFQTGAKVTFLLEFEFSCSSLLSQVFVKLTASSDSLERNGTLQDNTAQTSAYIQYEPHLLFSSESTLHRYEVHPYGTLPVGPGPEFKTTLRVQNLGCYVVSGLIISALLPAVAHGGNYFLSLSQVITNNASCIVQNLTEPPGPPVHPEELQHTNRLNGSNTQCQVVRCHLGQLAKGTEVSVGLLRLVHNEFFRRAKFKSLTVVSTFELGTEEGSVLQLTEASRWSESLLEVVQTRPILISLWILIGSVLGGLLLLALLVFCLWKLGFFAHKKIPEEEKREEKLEQ
| null | null |
cell adhesion mediated by integrin [GO:0033627]; cell-cell adhesion [GO:0098609]; cell-matrix adhesion [GO:0007160]; integrin-mediated signaling pathway [GO:0007229]
|
external side of plasma membrane [GO:0009897]; integrin alpha10-beta1 complex [GO:0034680]; integrin complex [GO:0008305]; plasma membrane [GO:0005886]
|
collagen binding [GO:0005518]; collagen binding involved in cell-matrix adhesion [GO:0098639]; integrin binding [GO:0005178]; metal ion binding [GO:0046872]
|
PF01839;PF08441;PF20805;PF00092;
|
1.20.5.930;2.130.10.130;2.60.40.1460;2.60.40.1510;2.60.40.1530;3.40.50.410;
|
Integrin alpha chain family
| null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Integrin alpha-10/beta-1 is a receptor for collagen.
|
Homo sapiens (Human)
|
O75581
|
LRP6_HUMAN
|
MGAVLRSLLACSFCVLLRAAPLLLYANRRDLRLVDATNGKENATIVVGGLEDAAAVDFVFSHGLIYWSDVSEEAIKRTEFNKTESVQNVVVSGLLSPDGLACDWLGEKLYWTDSETNRIEVSNLDGSLRKVLFWQELDQPRAIALDPSSGFMYWTDWGEVPKIERAGMDGSSRFIIINSEIYWPNGLTLDYEEQKLYWADAKLNFIHKSNLDGTNRQAVVKGSLPHPFALTLFEDILYWTDWSTHSILACNKYTGEGLREIHSDIFSPMDIHAFSQQRQPNATNPCGIDNGGCSHLCLMSPVKPFYQCACPTGVKLLENGKTCKDGATELLLLARRTDLRRISLDTPDFTDIVLQLEDIRHAIAIDYDPVEGYIYWTDDEVRAIRRSFIDGSGSQFVVTAQIAHPDGIAVDWVARNLYWTDTGTDRIEVTRLNGTMRKILISEDLEEPRAIVLDPMVGYMYWTDWGEIPKIERAALDGSDRVVLVNTSLGWPNGLALDYDEGKIYWGDAKTDKIEVMNTDGTGRRVLVEDKIPHIFGFTLLGDYVYWTDWQRRSIERVHKRSAEREVIIDQLPDLMGLKATNVHRVIGSNPCAEENGGCSHLCLYRPQGLRCACPIGFELISDMKTCIVPEAFLLFSRRADIRRISLETNNNNVAIPLTGVKEASALDFDVTDNRIYWTDISLKTISRAFMNGSALEHVVEFGLDYPEGMAVDWLGKNLYWADTGTNRIEVSKLDGQHRQVLVWKDLDSPRALALDPAEGFMYWTEWGGKPKIDRAAMDGSERTTLVPNVGRANGLTIDYAKRRLYWTDLDTNLIESSNMLGLNREVIADDLPHPFGLTQYQDYIYWTDWSRRSIERANKTSGQNRTIIQGHLDYVMDILVFHSSRQSGWNECASSNGHCSHLCLAVPVGGFVCGCPAHYSLNADNRTCSAPTTFLLFSQKSAINRMVIDEQQSPDIILPIHSLRNVRAIDYDPLDKQLYWIDSRQNMIRKAQEDGSQGFTVVVSSVPSQNLEIQPYDLSIDIYSRYIYWTCEATNVINVTRLDGRSVGVVLKGEQDRPRAVVVNPEKGYMYFTNLQERSPKIERAALDGTEREVLFFSGLSKPIALALDSRLGKLFWADSDLRRIESSDLSGANRIVLEDSNILQPVGLTVFENWLYWIDKQQQMIEKIDMTGREGRTKVQARIAQLSDIHAVKELNLQEYRQHPCAQDNGGCSHICLVKGDGTTRCSCPMHLVLLQDELSCGEPPTCSPQQFTCFTGEIDCIPVAWRCDGFTECEDHSDELNCPVCSESQFQCASGQCIDGALRCNGDANCQDKSDEKNCEVLCLIDQFRCANGQCIGKHKKCDHNVDCSDKSDELDCYPTEEPAPQATNTVGSVIGVIVTIFVSGTVYFICQRMLCPRMKGDGETMTNDYVVHGPASVPLGYVPHPSSLSGSLPGMSRGKSMISSLSIMGGSSGPPYDRAHVTGASSSSSSSTKGTYFPAILNPPPSPATERSHYTMEFGYSSNSPSTHRSYSYRPYSYRHFAPPTTPCSTDVCDSDYAPSRRMTSVATAKGYTSDLNYDSEPVPPPPTPRSQYLSAEENYESCPPSPYTERSYSHHLYPPPPSPCTDSS
| null | null |
canonical Wnt signaling pathway [GO:0060070]; cell-cell adhesion [GO:0098609]; cellular response to cholesterol [GO:0071397]; chemical synaptic transmission [GO:0007268]; dopaminergic neuron differentiation [GO:0071542]; midbrain dopaminergic neuron differentiation [GO:1904948]; negative regulation of protein serine/threonine kinase activity [GO:0071901]; negative regulation of smooth muscle cell apoptotic process [GO:0034392]; neural crest cell differentiation [GO:0014033]; neural crest formation [GO:0014029]; positive regulation of cell cycle [GO:0045787]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of DNA-binding transcription factor activity [GO:0051091]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein localization to plasma membrane [GO:0072659]; receptor-mediated endocytosis involved in cholesterol transport [GO:0090118]; response to peptide hormone [GO:0043434]; Wnt signaling pathway [GO:0016055]; Wnt signaling pathway involved in somitogenesis [GO:0090244]
|
cell surface [GO:0009986]; cytoplasmic vesicle [GO:0031410]; early endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; membrane raft [GO:0045121]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; synapse [GO:0045202]; Wnt signalosome [GO:1990909]; Wnt-Frizzled-LRP5/6 complex [GO:1990851]
|
coreceptor activity [GO:0015026]; frizzled binding [GO:0005109]; identical protein binding [GO:0042802]; kinase inhibitor activity [GO:0019210]; low-density lipoprotein particle receptor activity [GO:0005041]; protein homodimerization activity [GO:0042803]; signaling receptor binding [GO:0005102]; toxin transmembrane transporter activity [GO:0019534]; Wnt receptor activity [GO:0042813]; Wnt-protein binding [GO:0017147]
|
PF14670;PF00057;PF00058;
|
2.10.25.10;4.10.400.10;2.120.10.30;
|
LDLR family
|
PTM: Dual phosphorylation of cytoplasmic PPPSP motifs sequentially by GSK3 and CK1 is required for AXIN1-binding, and subsequent stabilization and activation of beta-catenin via preventing GSK3-mediated phosphorylation of beta-catenin. Phosphorylated, in vitro, by GRK5/6 within and outside the PPPSP motifs. Phosphorylation at Ser-1490 by CDK14 during G2/M phase leads to regulation of the Wnt signaling pathway during the cell cycle. Phosphorylation by GSK3B is induced by RPSO1 binding and inhibited by DKK1. Phosphorylated, in vitro, by casein kinase I on Thr-1479. {ECO:0000269|PubMed:16341017, ECO:0000269|PubMed:16513652, ECO:0000269|PubMed:17400545, ECO:0000269|PubMed:17569865, ECO:0000269|PubMed:17698587, ECO:0000269|PubMed:18362152, ECO:0000269|PubMed:19107203, ECO:0000269|PubMed:19293931, ECO:0000269|PubMed:19801552, ECO:0000269|PubMed:20059949}.; PTM: Undergoes gamma-secretase-dependent regulated intramembrane proteolysis (RIP). The extracellular domain is first released by shedding, and then, through the action of gamma-secretase, the intracellular domain (ICD) is released into the cytoplasm where it is free to bind to GSK3B and to activate canonical Wnt signaling.; PTM: Palmitoylation on the two sites near the transmembrane domain leads to release of LRP6 from the endoplasmic reticulum. {ECO:0000269|PubMed:18378904}.; PTM: Mono-ubiquitinated which retains LRP6 in the endoplasmic reticulum. Ubiquitinated by ZNRF3, leading to its degradation by the proteasome. {ECO:0000269|PubMed:18378904, ECO:0000269|PubMed:22575959}.; PTM: N-glycosylation is required for cell surface location. {ECO:0000269|PubMed:17698587, ECO:0000269|PubMed:22000856}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26387593}; Single-pass type I membrane protein. Endoplasmic reticulum {ECO:0000269|PubMed:26387593}. Membrane raft {ECO:0000269|PubMed:23987510}. Note=On Wnt signaling, undergoes a cycle of caveolin- or clathrin-mediated endocytosis and plasma membrane location. Released from the endoplasmic reticulum on palmitoylation. Mono-ubiquitination retains it in the endoplasmic reticulum in the absence of palmitoylation. On Wnt signaling, phosphorylated, aggregates and colocalizes with AXIN1 and GSK3B at the plasma membrane in LRP6-signalosomes. Chaperoned to the plasma membrane by MESD (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalosomes. Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalosomes and inhibiting AXIN1/GSK3-mediated phosphorylation and destruction of beta-catenin. Required for posterior patterning of the epiblast during gastrulation (By similarity). {ECO:0000250, ECO:0000269|PubMed:11357136, ECO:0000269|PubMed:11448771, ECO:0000269|PubMed:15778503, ECO:0000269|PubMed:16341017, ECO:0000269|PubMed:16513652, ECO:0000269|PubMed:17326769, ECO:0000269|PubMed:17400545, ECO:0000269|PubMed:19107203, ECO:0000269|PubMed:19293931, ECO:0000269|PubMed:19801552, ECO:0000269|PubMed:28341812}.
|
Homo sapiens (Human)
|
O75582
|
KS6A5_HUMAN
|
MEEEGGSSGGAAGTSADGGDGGEQLLTVKHELRTANLTGHAEKVGIENFELLKVLGTGAYGKVFLVRKISGHDTGKLYAMKVLKKATIVQKAKTTEHTRTERQVLEHIRQSPFLVTLHYAFQTETKLHLILDYINGGELFTHLSQRERFTEHEVQIYVGEIVLALEHLHKLGIIYRDIKLENILLDSNGHVVLTDFGLSKEFVADETERAYSFCGTIEYMAPDIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRILKSEPPYPQEMSALAKDLIQRLLMKDPKKRLGCGPRDADEIKEHLFFQKINWDDLAAKKVPAPFKPVIRDELDVSNFAEEFTEMDPTYSPAALPQSSEKLFQGYSFVAPSILFKRNAAVIDPLQFHMGVERPGVTNVARSAMMKDSPFYQHYDLDLKDKPLGEGSFSICRKCVHKKSNQAFAVKIISKRMEANTQKEITALKLCEGHPNIVKLHEVFHDQLHTFLVMELLNGGELFERIKKKKHFSETEASYIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDENDNLEIKIIDFGFARLKPPDNQPLKTPCFTLHYAAPELLNQNGYDESCDLWSLGVILYTMLSGQVPFQSHDRSLTCTSAVEIMKKIKKGDFSFEGEAWKNVSQEAKDLIQGLLTVDPNKRLKMSGLRYNEWLQDGSQLSSNPLMTPDILGSSGAAVHTCVKATFHAFNKYKREGFCLQNVDKAPLAKRRKMKKTSTSTETRSSSSESSHSSSSHSHGKTTPTKTLQPSNPADSNNPETLFQFSDSVA
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:12628924, ECO:0000269|PubMed:9687510, ECO:0000269|PubMed:9873047};
|
axon guidance [GO:0007411]; inflammatory response [GO:0006954]; interleukin-1-mediated signaling pathway [GO:0070498]; intracellular signal transduction [GO:0035556]; negative regulation of cytokine production [GO:0001818]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of CREB transcription factor activity [GO:0032793]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of transcription by RNA polymerase II [GO:0045944]; post-translational protein modification [GO:0043687]; protein phosphorylation [GO:0006468]; regulation of DNA-templated transcription [GO:0006355]; regulation of postsynapse organization [GO:0099175]
|
cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; histone H2AS1 kinase activity [GO:0044024]; histone H3S10 kinase activity [GO:0035175]; histone H3S28 kinase activity [GO:0044022]; magnesium ion binding [GO:0000287]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]
|
PF00069;PF00433;
|
1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family, S6 kinase subfamily
|
PTM: Ser-376 and Thr-581 phosphorylation is required for kinase activity. Ser-376 and Ser-212 are autophosphorylated by the C-terminal kinase domain, and their phosphorylation is essential for the catalytic activity of the N-terminal kinase domain. Phosphorylated at Ser-360, Thr-581 and Thr-700 by MAPK1/ERK2, MAPK3/ERK1 and MAPK14/p38-alpha. Autophosphorylated at Ser-750, Ser-752 and Ser-758 by the N-terminal kinase domain. {ECO:0000269|PubMed:15568999, ECO:0000269|PubMed:17117922}.; PTM: Ubiquitinated. {ECO:0000269|PubMed:20596523}.
|
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly nuclear. Exported into cytoplasm in response to glucocorticoid.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:12628924, ECO:0000269|PubMed:9687510, ECO:0000269|PubMed:9873047}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:12628924, ECO:0000269|PubMed:9687510, ECO:0000269|PubMed:9873047};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase that is required for the mitogen or stress-induced phosphorylation of the transcription factors CREB1 and ATF1 and for the regulation of the transcription factors RELA, STAT3 and ETV1/ER81, and that contributes to gene activation by histone phosphorylation and functions in the regulation of inflammatory genes (PubMed:11909979, PubMed:12569367, PubMed:12763138, PubMed:18511904, PubMed:9687510, PubMed:9873047). Phosphorylates CREB1 and ATF1 in response to mitogenic or stress stimuli such as UV-C irradiation, epidermal growth factor (EGF) and anisomycin (PubMed:11909979, PubMed:9873047). Plays an essential role in the control of RELA transcriptional activity in response to TNF and upon glucocorticoid, associates in the cytoplasm with the glucocorticoid receptor NR3C1 and contributes to RELA inhibition and repression of inflammatory gene expression (PubMed:12628924, PubMed:18511904). In skeletal myoblasts is required for phosphorylation of RELA at 'Ser-276' during oxidative stress (PubMed:12628924). In erythropoietin-stimulated cells, is necessary for the 'Ser-727' phosphorylation of STAT3 and regulation of its transcriptional potential (PubMed:12763138). Phosphorylates ETV1/ER81 at 'Ser-191' and 'Ser-216', and thereby regulates its ability to stimulate transcription, which may be important during development and breast tumor formation (PubMed:12569367). Directly represses transcription via phosphorylation of 'Ser-1' of histone H2A (PubMed:15010469). Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and EGF, which results in the transcriptional activation of several immediate early genes, including proto-oncogenes c-fos/FOS and c-jun/JUN (PubMed:12773393). May also phosphorylate 'Ser-28' of histone H3 (PubMed:12773393). Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14) (PubMed:12773393). In lipopolysaccharide-stimulated primary macrophages, acts downstream of the Toll-like receptor TLR4 to limit the production of pro-inflammatory cytokines (By similarity). Functions probably by inducing transcription of the MAP kinase phosphatase DUSP1 and the anti-inflammatory cytokine interleukin 10 (IL10), via CREB1 and ATF1 transcription factors (By similarity). Plays a role in neuronal cell death by mediating the downstream effects of excitotoxic injury (By similarity). Phosphorylates TRIM7 at 'Ser-107' in response to growth factor signaling via the MEK/ERK pathway, thereby stimulating its ubiquitin ligase activity (PubMed:25851810). {ECO:0000250|UniProtKB:Q8C050, ECO:0000269|PubMed:11909979, ECO:0000269|PubMed:12569367, ECO:0000269|PubMed:12628924, ECO:0000269|PubMed:12763138, ECO:0000269|PubMed:12773393, ECO:0000269|PubMed:15010469, ECO:0000269|PubMed:18511904, ECO:0000269|PubMed:25851810, ECO:0000269|PubMed:9687510, ECO:0000269|PubMed:9873047}.
|
Homo sapiens (Human)
|
O75586
|
MED6_HUMAN
|
MAAVDIRDNLLGISWVDSSWIPILNSGSVLDYFSERSNPFYDRTCNNEVVKMQRLTLEHLNQMVGIEYILLHAQEPILFIIRKQQRQSPAQVIPLADYYIIAGVIYQAPDLGSVINSRVLTAVHGIQSAFDEAMSYCRYHPSKGYWWHFKDHEEQDKVRPKAKRKEEPSSIFQRQRVDALLLDLRQKFPPKFVQLKPGEKPVPVDQTKKEAEPIPETVKPEEKETTKNVQQTVSAKGPPEKRMRLQ
| null | null |
positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261]; protein ubiquitination [GO:0016567]; regulation of transcription by RNA polymerase II [GO:0006357]; RNA polymerase II preinitiation complex assembly [GO:0051123]; somatic stem cell population maintenance [GO:0035019]
|
core mediator complex [GO:0070847]; mediator complex [GO:0016592]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]
|
DNA binding [GO:0003677]; transcription coactivator activity [GO:0003713]; transcription coactivator binding [GO:0001223]; ubiquitin protein ligase activity [GO:0061630]
|
PF04934;
|
3.10.450.580;
|
Mediator complex subunit 6 family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. {ECO:0000269|PubMed:16595664}.
|
Homo sapiens (Human)
|
O75592
|
MYCB2_HUMAN
|
MMMCAATASPAAASSGLGGDGFYPAATFSSSPAPGALFMPVPDGSVAAAGLGLGLPAADSRGHYQLLLSGRALADRYRRIYTAALNDRDQGGGSAGHPASRNKKILNKKKLKRKQKSKSKVKTRSKSENLENTVIIPDIKLHSNPSAFNIYCNVRHCVLEWQKKEISLAAASKNSVQSGESDSDEEEESKEPPIKLPKIIEVGLCEVFELIKETRFSHPSLCLRSLQALLNVLQGQQPEGLQSEPPEVLESLFQLLLEITVRSTGMNDSTGQSLTALSCACLFSLVASWGETGRTLQAISAILTNNGSHACQTIQVPTILNSLQRSVQAVLVGKIQIQDWFSNGIKKAALMHKWPLKEISVDEDDQCLLQNDGFFLYLLCKDGLYKIGSGYSGTVRGHIYNSTSRIRNRKEKKSWLGYAQGYLLYRDVNNHSMTAIRISPETLEQDGTVMLPDCHTEGQNILFTDGEYINQIAASRDDGFVVRIFATSTEPVLQQELQLKLARKCLHACGISLFDLEKDLHIISTGFDEESAILGAGREFALMKTANGKIYYTGKYQSLGIKQGGPSAGKWVELPITKSPKIVHFSVGHDGSHALLVAEDGSIFFTGSASKGEDGESTKSRRQSKPYKPKKIIKMEGKIVVYTACNNGSSSVISKDGELYMFGKDAIYSDSSSLVTDLKGHFVTQVAMGKAHTCVLMKNGEVWTFGVNNKGQCGRDTGAMNQGGKGFGVENMATAMDEDLEEELDEKDEKSMMCPPGMHKWKLEQCMVCTVCGDCTGYGASCVSSGRPDRVPGGICGCGSGESGCAVCGCCKACARELDGQEARQRGILDAVKEMIPLDLLLAVPVPGVNIEEHLQLRQEEKRQRVIRRHRLEEGRGPLVFAGPIFMNHREQALARLRSHPAQLKHKRDKHKDGSGERGEKDASKITTYPPGSVRFDCELRAVQVSCGFHHSVVLMENGDVYTFGYGQHGQLGHGDVNSRGCPTLVQALPGPSTQVTAGSNHTAVLLMDGQVFTFGSFSKGQLGRPILDVPYWNAKPAPMPNIGSKYGRKATWIGASGDQTFLRIDEALINSHVLATSEIFASKHIIGLVPASISEPPPFKCLLINKVDGSCKTFNDSEQEDLQGFGVCLDPVYDVIWRFRPNTRELWCYNAVVADARLPSAADMQSRCSILSPELALPTGSRALTTRSHAALHILGCLDTLAAMQDLKMGVASTEEETQAVMKVYSKEDYSVVNRFESHGGGWGYSAHSVEAIRFSADTDILLGGLGLFGGRGEYTAKIKLFELGPDGGDHETDGDLLAETDVLAYDCAAREKYAMMFDEPVLLQAGWWYVAWARVSGPSSDCGSHGQASITTDDGVVFQFKSSKKSNNGTDVNAGQIPQLLYRLPTSDGSASKGKQQTSEPVHILKRSFARTVSVECFESLLSILHWSWTTLVLGVEELRGLKGFQFTATLLDLERLRFVGTCCLRLLRVYTCEIYPVSATGKAVVEETSKLAECIGKTRTLLRKILSEGVDHCMVKLDNDPQGYLSQPLSLLEAVLQECHNTFTACFHSFYPTPALQWACLCDLLNCLDQDIQEANFKTSSSRLLAAVMSALCHTSVKLTSIFPIAYDGEVLLRSIVKQVSTENDSTLVHRFPLLVAHMEKLSQSEENISGMTSFREVLEKMLVIVVLPVRNSLRRENELFSSHLVSNTCGLLASIVSELTASALGSEVDGLNSLHSVKASANRFTKTSQGRSWNTGNGSPDAICFSVDKPGIVVVGFSVYGGGGIHEYELEVLVDDSEHAGDSTHSHRWTSLELVKGTYTTDDSPSDIAEIRLDKVVPLKENVKYAVRLRNYGSRTANGDGGMTTVQCPDGVTFTFSTCSLSSNGTNQTRGQIPQILYYRSEFDGDLQSQLLSKANEEDKNCSRALSVVSTVVRASKDLLHRALAVDADDIPELLSSSSLFSMLLPLIIAYIGPVAAAIPKVAVEVFGLVQQLLPSVAILNQKYAPPAFNPNQSTDSTTGNQPEQGLSACTTSSHYAVIESEHPYKPACVMHYKVTFPECVRWMTIEFDPQCGTAQSEDVLRLLIPVRTVQNSGYGPKLTSVHENLNSWIELKKFSGSSGWPTMVLVLPGNEALFSLETASDYVKDDKASFYGFKCFAIGYEFSPGPDEGVIQLEKELANLGGVCAAALMKKDLALPIGNELEEDLEILEEAALQVCKTHSGILGKGLALSHSPTILEALEGNLPLQIQSNEQSFLDDFIACVPGSSGGRLARWLQPDSYADPQKTSLILNKDDIRCGWPTTITVQTKDQYGDVVHVPNMKVEVKAVPVSQKKMSLQQDQAKKPQRIPGSPAVTAASSNTDMTYGGLASPKLDVSYEPMIVKEARYIAITMMKVYENYSFEELRFASPTPKRPSENMLIRVNNDGTYCANWTPGAIGLYTLHVTIDGIEIDAGLEVKVKDPPKGMIPPGTQLVKPKSEPQPNKVRKFVAKDSAGLRIRSHPSLQSEQIGIVKVNGTITFIDEIHNDDGVWLRLNDETIKKYVPNMNGYTEAWCLSFNQHLGKSLLVPVDESKTNTDDFFKDINSCCPQEATMQEQDMPFLRGGPGMYKVVKTGPSGHNIRSCPNLRGIPIGMLVLGNKVKAVGEVTNSEGTWVQLDQNSMVEFCESDEGEAWSLARDRGGNQYLRHEDEQALLDQNSQTPPPSPFSVQAFNKGASCSAQGFDYGLGNSKGDRGNISTSSKPASTSGKSELSSKHSRSLKPDGRMSRTTADQKKPRGTESLSASESLILKSDAAKLRSDSHSRSLSPNHNTLQTLKSDGRMPSSSRAESPGPGSRLSSPKPKTLPANRSSPSGASSPRSSSPHDKNLPQKSTAPVKTKLDPPRERSKSDSYTLDPDTLRKKKMPLTEPLRGRSTSPKPKSVPKDSTDSPGSENRAPSPHVVQENLHSEVVEVCTSSTLKTNSLTDSTCDDSSEFKSVDEGSNKVHFSIGKAPLKDEQEMRASPKISRKCANRHTRPKKEKSSFLFKGDGSKPLEPAKQAMSPSVAECARAVFASFLWHEGIVHDAMACSSFLKFHPELSKEHAPIRSSLNSQQPTEEKETKLKNRHSLEISSALNMFNIAPHGPDISKMGSINKNKVLSMLKEPPLHEKCEDGKTETTFEMSMHNTMKSKSPLPLTLQHLVAFWEDISLATIKAASQNMIFPSPGSCAVLKKKECEKENKKSKKEKKKKEKAEVRPRGNLFGEMAQLAVGGPEKDTICELCGESHPYPVTYHMRQAHPGCGRYAGGQGYNSIGHFCGGWAGNCGDGGIGGSTWYLVCDRCREKYLREKQAAAREKVKQSRRKPMQVKTPRALPTMEAHQVIKANALFLLSLSSAAEPSILCYHPAKPFQSQLPSVKEGISEDLPVKMPCLYLQTLARHHHENFVGYQDDNLFQDEMRYLRSTSVPAPYISVTPDASPNVFEEPESNMKSMPPSLETSPITDTDLAKRTVFQRSYSVVASEYDKQHSILPARVKAIPRRRVNSGDTEVGSSLLRHPSPELSRLISAHSSLSKGERNFQWPVLAFVIQHHDLEGLEIAMKQALRKSACRVFAMEAFNWLLCNVIQTTSLHDILWHFVASLTPAPVEPEEEEDEENKTSKENSEQEKDTRVCEHPLSDIVIAGEAAHPLPHTFHRLLQTISDLMMSLPSGSSLQQMALRCWSLKFKQSDHQFLHQSNVFHHINNILSKSDDGDSEESFSISIQSGFEAMSQELCIVMCLKDLTSIVDIKTSSRPAMIGSLTDGSTETFWESGDEDKNKTKNITINCVKGINARYVSVHVDNSRDLGNKVTSMTFLTGKAVEDLCRIKQVDLDSRHIGWVTSELPGGDNHIIKIELKGPENTLRVRQVKVLGWKDGESTKIAGQISASVAQQRNCEAETLRVFRLITSQVFGKLISGDAEPTPEQEEKALLSSPEGEEKVYNATSDADLKEHMVGIIFSRSKLTNLQKQVCAHIVQAIRMEATRVREEWEHAISSKENANSQPNDEDASSDAYCFELLSMVLALSGSNVGRQYLAQQLTLLQDLFSLLHTASPRVQRQVTSLLRRVLPEVTPSRLASIIGVKSLPPADISDIIHSTEKGDWNKLGILDMFLGCIAKALTVQLKAKGTTITGTAGTTVGKGVTTVTLPMIFNSSYLRRGESHWWMKGSTPTQISEIIIKLIKDMAAGHLSEAWSRVTKNAIAETIIALTKMEEEFRSPVRCIATTRLWLALASLCVLDQDHVDRLSSGRWMGKDGQQKQMPMCDNHDDGETAAIILCNVCGNLCTDCDRFLHLHRRTKTHQRQVFKEEEEAIKVDLHEGCGRTKLFWLMALADSKTMKAMVEFREHTGKPTTSSSEACRFCGSRSGTELSAVGSVCSDADCQEYAKIACSKTHPCGHPCGGVKNEEHCLPCLHGCDKSATSLKQDADDMCMICFTEALSAAPAIQLDCSHIFHLQCCRRVLENRWLGPRITFGFISCPICKNKINHIVLKDLLDPIKELYEDVRRKALMRLEYEGLHKSEAITTPGVRFYNDPAGYAMNRYAYYVCYKCRKAYFGGEARCDAEAGRGDDYDPRELICGACSDVSRAQMCPKHGTDFLEYKCRYCCSVAVFFCFGTTHFCNACHDDFQRMTSIPKEELPHCPAGPKGKQLEGTECPLHVVHPPTGEEFALGCGVCRNAHTF
|
2.3.2.33
| null |
axon guidance [GO:0007411]; branchiomotor neuron axon guidance [GO:0021785]; central nervous system projection neuron axonogenesis [GO:0021952]; circadian regulation of gene expression [GO:0032922]; negative regulation of protein catabolic process [GO:0042177]; neuromuscular process [GO:0050905]; positive regulation of protein ubiquitination [GO:0031398]; protein K48-linked ubiquitination [GO:0070936]; protein ubiquitination [GO:0016567]; regulation of axon guidance [GO:1902667]; regulation of cytoskeleton organization [GO:0051493]; regulation of protein localization [GO:0032880]; regulation of synaptic assembly at neuromuscular junction [GO:0008582]
|
axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
guanyl-nucleotide exchange factor activity [GO:0005085]; identical protein binding [GO:0042802]; small GTPase binding [GO:0031267]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]
|
PF03256;PF08005;PF00415;PF13540;
|
2.60.120.260;2.60.40.10;2.60.120.820;2.130.10.30;3.30.40.10;
|
RING-Cys relay (RCR) family
|
PTM: Autoubiquitinated. {ECO:0000269|PubMed:18308511}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26304119, ECO:0000269|PubMed:9689053}. Cell projection, axon {ECO:0000250|UniProtKB:Q7TPH6}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q7TPH6}. Note=Localizes to axon shafts and associates with microtubule cytoskeleton (By similarity). Translocates to the nucleus following interaction with sumoylated RANGAP1 (PubMed:26304119). {ECO:0000250|UniProtKB:Q7TPH6, ECO:0000269|PubMed:26304119}.
|
CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-threonine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-3-O-ubiquitinyl-L-threonine.; EC=2.3.2.33; Evidence={ECO:0000269|PubMed:29643511};
| null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:18308511, ECO:0000269|PubMed:29643511}.
| null | null |
FUNCTION: Atypical E3 ubiquitin-protein ligase which specifically mediates ubiquitination of threonine and serine residues on target proteins, instead of ubiquitinating lysine residues (PubMed:29643511). Shows esterification activity towards both threonine and serine, with a preference for threonine, and acts via two essential catalytic cysteine residues that relay ubiquitin to its substrate via thioester intermediates (PubMed:29643511). Interacts with the E2 enzymes UBE2D1, UBE2D3, UBE2E1 and UBE2L3 (PubMed:18308511, PubMed:29643511). Plays a key role in neural development, probably by mediating ubiquitination of threonine residues on target proteins (Probable). Involved in different processes such as regulation of neurite outgrowth, synaptic growth, synaptogenesis and axon degeneration (By similarity). Required for the formation of major central nervous system axon tracts (By similarity). Required for proper axon growth by regulating axon navigation and axon branching: acts by regulating the subcellular location and stability of MAP3K12/DLK (By similarity). Required for proper localization of retinogeniculate projections but not for eye-specific segregation (By similarity). Regulates axon guidance in the olfactory system (By similarity). Involved in Wallerian axon degeneration, an evolutionarily conserved process that drives the loss of damaged axons: acts by promoting destabilization of NMNAT2, probably via ubiquitination of NMNAT2 (By similarity). Catalyzes ubiquitination of threonine and/or serine residues on NMNAT2, consequences of threonine and/or serine ubiquitination are however unknown (PubMed:29643511). Regulates the internalization of TRPV1 in peripheral sensory neurons (By similarity). Mediates ubiquitination and subsequent proteasomal degradation of TSC2/tuberin (PubMed:18308511, PubMed:27278822). Independently of the E3 ubiquitin-protein ligase activity, also acts as a guanosine exchange factor (GEF) for RAN in neurons of dorsal root ganglia (PubMed:26304119). May function as a facilitator or regulator of transcriptional activation by MYC (PubMed:9689053). Acts in concert with HUWE1 to regulate the circadian clock gene expression by promoting the lithium-induced ubiquination and degradation of NR1D1 (PubMed:20534529). {ECO:0000250|UniProtKB:Q7TPH6, ECO:0000269|PubMed:18308511, ECO:0000269|PubMed:20534529, ECO:0000269|PubMed:26304119, ECO:0000269|PubMed:27278822, ECO:0000269|PubMed:29643511, ECO:0000269|PubMed:9689053}.
|
Homo sapiens (Human)
|
O75593
|
FOXH1_HUMAN
|
MGPCSGSRLGPPEAESPSQPPKRRKKRYLRHDKPPYTYLAMIALVIQAAPSRRLKLAQIIRQVQAVFPFFREDYEGWKDSIRHNLSSNRCFRKVPKDPAKPQAKGNFWAVDVSLIPAEALRLQNTALCRRWQNGGARGAFAKDLGPYVLHGRPYRPPSPPPPPSEGFSIKSLLGGSGEGAPWPGLAPQSSPVPAGTGNSGEEAVPTPPLPSSERPLWPLCPLPGPTRVEGETVQGGAIGPSTLSPEPRAWPLHLLQGTAVPGGRSSGGHRASLWGQLPTSYLPIYTPNVVMPLAPPPTSCPQCPSTSPAYWGVAPETRGPPGLLCDLDALFQGVPPNKSIYDVWVSHPRDLAAPGPGWLLSWCSL
| null | null |
aorta morphogenesis [GO:0035909]; axial mesoderm development [GO:0048318]; cardiac right ventricle morphogenesis [GO:0003215]; cellular response to cytokine stimulus [GO:0071345]; determination of left/right asymmetry in lateral mesoderm [GO:0003140]; embryonic heart tube anterior/posterior pattern specification [GO:0035054]; heart looping [GO:0001947]; hepatocyte differentiation [GO:0070365]; negative regulation of androgen receptor signaling pathway [GO:0060766]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; negative regulation of intracellular estrogen receptor signaling pathway [GO:0033147]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nodal signaling pathway [GO:0038092]; outflow tract morphogenesis [GO:0003151]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; secondary heart field specification [GO:0003139]; transforming growth factor beta receptor signaling pathway [GO:0007179]; ventricular trabecula myocardium morphogenesis [GO:0003222]
|
activin responsive factor complex [GO:0032444]; chromatin [GO:0000785]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
bHLH transcription factor binding [GO:0043425]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; co-SMAD binding [GO:0070410]; 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 factor binding [GO:0140297]; nuclear androgen receptor binding [GO:0050681]; protein domain specific binding [GO:0019904]; R-SMAD binding [GO:0070412]; sequence-specific DNA binding [GO:0043565]; SMAD binding [GO:0046332]; transcription cis-regulatory region binding [GO:0000976]
|
PF00250;
|
1.10.10.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Transcriptional activator. Recognizes and binds to the DNA sequence 5'-TGT[GT][GT]ATT-3'. Required for induction of the goosecoid (GSC) promoter by TGF-beta or activin signaling. Forms a transcriptionally active complex containing FOXH1/SMAD2/SMAD4 on a site on the GSC promoter called TARE (TGF-beta/activin response element). {ECO:0000269|PubMed:9702198}.
|
Homo sapiens (Human)
|
O75594
|
PGRP1_HUMAN
|
MSRRSMLLAWALPSLLRLGAAQETEDPACCSPIVPRNEWKALASECAQHLSLPLRYVVVSHTAGSSCNTPASCQQQARNVQHYHMKTLGWCDVGYNFLIGEDGLVYEGRGWNFTGAHSGHLWNPMSIGISFMGNYMDRVPTPQAIRAAQGLLACGVAQGALRSNYVLKGHRDVQRTLSPGNQLYHLIQNWPHYRSP
| null | null |
antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; biological process involved in interaction with host [GO:0051701]; defense response to Gram-positive bacterium [GO:0050830]; detection of bacterium [GO:0016045]; innate immune response [GO:0045087]; killing of cells of another organism [GO:0031640]; negative regulation of inflammatory response [GO:0050728]; negative regulation of natural killer cell differentiation involved in immune response [GO:0032827]; negative regulation of type II interferon production [GO:0032689]; peptidoglycan catabolic process [GO:0009253]
|
extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; phagocytic vesicle lumen [GO:0097013]; specific granule lumen [GO:0035580]; tertiary granule lumen [GO:1904724]
|
Hsp70 protein binding [GO:0030544]; molecular adaptor activity [GO:0060090]; N-acetylmuramoyl-L-alanine amidase activity [GO:0008745]; peptidoglycan binding [GO:0042834]; peptidoglycan immune receptor activity [GO:0016019]; receptor ligand activity [GO:0048018]; zinc ion binding [GO:0008270]
|
PF01510;
|
3.40.80.10;
|
N-acetylmuramoyl-L-alanine amidase 2 family
|
PTM: N-glycosylated. N-glycosylation is required for bactericidal activity. {ECO:0000269|PubMed:16354652}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16354652}. Cytoplasmic granule {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Innate immunity protein that plays several important functions in antimicrobial and antitumor defense systems. Acts as a pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria and thus provides bactericidal activity (PubMed:9707603). Forms an equimolar complex with heat shock protein HSPA1A and induces programmed cell death through apoptosis and necroptosis in tumor cell lines by activating the TNFR1 receptor on the target cell membrane (PubMed:21247889, PubMed:26183779). In addition, acts in complex with the Ca(2+)-binding protein S100A4 as a chemoattractant able to induce lymphocyte movement (PubMed:26654597). Mechanistically, this complex acts as a ligand of the chemotactic receptors CCR5 and CXCR3 which are present on the cells of the immune system (PubMed:30713770). Promotes also the activation of lymphocytes that become able to kill virus-infected cells as well as tumor cells by modulating the spectrum of their target-cell specificity (PubMed:28977785, PubMed:29083508). Induction of cytotoxicity on monocyte surface requires interaction with TREM1 receptor (PubMed:25595774, PubMed:28977785). {ECO:0000269|PubMed:21247889, ECO:0000269|PubMed:25595774, ECO:0000269|PubMed:26183779, ECO:0000269|PubMed:26654597, ECO:0000269|PubMed:28977785, ECO:0000269|PubMed:29083508, ECO:0000269|PubMed:30713770, ECO:0000269|PubMed:9707603}.
|
Homo sapiens (Human)
|
O75600
|
KBL_HUMAN
|
MWPGNAWRAALFWVPRGRRAQSALAQLRGILEGELEGIRGAGTWKSERVITSRQGPHIRVDGVSGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGALP
|
2.3.1.29
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:Q0P5L8};
|
amino acid metabolic process [GO:0006520]; biosynthetic process [GO:0009058]; threonine catabolic process [GO:0006567]
|
mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
glycine C-acetyltransferase activity [GO:0008890]; pyridoxal phosphate binding [GO:0030170]
|
PF00155;
|
3.90.1150.10;3.40.640.10;
|
Class-II pyridoxal-phosphate-dependent aminotransferase family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q0P5L8}. Nucleus {ECO:0000269|PubMed:17688197}. Note=Translocates to the nucleus upon cold and osmotic stress. {ECO:0000269|PubMed:17688197}.
|
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + glycine = (2S)-2-amino-3-oxobutanoate + CoA; Xref=Rhea:RHEA:20736, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57305, ChEBI:CHEBI:78948; EC=2.3.1.29; Evidence={ECO:0000250|UniProtKB:Q0P5L8}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20738; Evidence={ECO:0000250|UniProtKB:Q0P5L8};
| null | null | null | null |
FUNCTION: Pyridoxal phosphate (PLP) dependent enzyme, which catalyzes the cleavage of 2-amino-3-oxobutanoate to glycine and acetyl-CoA. {ECO:0000250|UniProtKB:Q0P5L8}.
|
Homo sapiens (Human)
|
O75601
|
CASPD_BOVIN
|
MAEDKHNKNPLKMLESLGKELISGLLDDFVEKNVLKLEEEEKKKIYDAKLQDKARVLVDSIRQKNQEAGQVFVQTFLNIDKNSTSIKAPEETVAGPDESVGSAATLKLCPHEEFLKLCKERAGEIYPIKERKDRTRLALIICNTEFDHMPPRNGAALDILGMKQLLEGLGYTVEVEEKLTARDMESVLWKFAAREEHKSSDSTFLVFMSHGILDGICGTMHSEEEPDVLPYDTIFRTFNNRNCLSLKDKPKVIIVQACRGANRGELWVSDSPPALADSFSQSSENLEEDAVYKTHVEKDFIAFCSSTPHNVSWRDIKKGSLFITRLITCFQKYAWCCHLEEVFRKVQQSFEKPNVKAQMPTVERLSMTRYFYLFPGN
|
3.4.22.-
| null |
apoptotic process [GO:0006915]; positive regulation of inflammatory response [GO:0050729]; positive regulation of neuron apoptotic process [GO:0043525]; proteolysis [GO:0006508]
|
AIM2 inflammasome complex [GO:0097169]; cytoplasm [GO:0005737]; IPAF inflammasome complex [GO:0072557]; NLRP1 inflammasome complex [GO:0072558]; NLRP3 inflammasome complex [GO:0072559]
|
caspase binding [GO:0089720]; cysteine-type endopeptidase activity [GO:0004197]
|
PF00619;PF00656;
|
3.40.50.1460;1.10.533.10;
|
Peptidase C14A family
|
PTM: The two subunits are derived from the precursor sequence by an autocatalytic mechanism or by cleavage by Caspase-8.
| null | null | null | null | null | null |
FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. Might function by either activating some proteins required for cell death or inactivating proteins necessary for cell survival.
|
Bos taurus (Bovine)
|
O75602
|
SPAG6_HUMAN
|
MSQRQVLQVFEQYQKARTQFVQMVAELATRPQNIETLQNAGVMSLLRTLLLDVVPTIQQTAALALGRLANYNDDLAEAVVKCDILPQLVYSLAEQNRFYKKAAAFVLRAVGKHSPQLAQAIVDCGALDTLVICLEDFDPGVKEAAAWALRYIARHNAELSQAVVDAGAVPLLVLCIQEPEIALKRIAASALSDIAKHSPELAQTVVDAGAVAHLAQMILNPDAKLKHQILSALSQVSKHSVDLAEMVVEAEIFPVVLTCLKDKDEYVKKNASTLIREIAKHTPELSQLVVNAGGVAAVIDCIGSCKGNTRLPGIMMLGYVAAHSENLAMAVIISKGVPQLSVCLSEEPEDHIKAAAAWALGQIGRHTPEHARAVAVTNTLPVLLSLYMSTESSEDLQVKSKKAIKNILQKCTYLPALEPFLYDAPPNILKHVVGQFSKVLPHDSKARRLFVTSGGLKKVQEIKAEPGSLLQEYINSINSCYPEEIVRYYSPGYSDTLLQRVDSYQPLNN
| null | null |
epithelial cilium movement involved in extracellular fluid movement [GO:0003351]; filopodium assembly [GO:0046847]; neuron projection extension [GO:1990138]; sperm axoneme assembly [GO:0007288]
|
acrosomal vesicle [GO:0001669]; axoneme [GO:0005930]; extracellular region [GO:0005576]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]; sperm principal piece [GO:0097228]
|
microtubule binding [GO:0008017]
|
PF00514;
|
1.25.10.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10493827}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:10493827}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9JLI7}. Note=Associated with microtubules. Detected on the sperm flagellum (PubMed:10493827). Localizes in the cilium axoneme in a SPEF1-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q9JLI7, ECO:0000269|PubMed:10493827}.
| null | null | null | null | null |
FUNCTION: Important for structural integrity of the central apparatus in the sperm tail and for flagellar motility. {ECO:0000250, ECO:0000269|PubMed:10493827}.
|
Homo sapiens (Human)
|
O75603
|
GCM2_HUMAN
|
MPAAAVQEAVGVCSYGMQLSWDINDPQMPQELALFDQFREWPDGYVRFIYSSDEKKAQRHLSGWAMRNTNNHNGHILKKSCLGVVVCTQACTLPDGSRLQLRPAICDKARLKQQKKACPNCHSALELIPCRGHSGYPVTNFWRLDGNAIFFQAKGVHDHPRPESKSETEARRSAIKRQMASFYQPQKKRIRESEAEENQDSSGHFSNIPPLENPEDFDIVTETSFPIPGQPCPSFPKSDVYKATCDLATFQGDKMPPFQKYSSPRIYLPRPPCSYELANPGYTNSSPYPTLYKDSTSIPNDTDWVHLNTLQCNVNSYSSYERSFDFTNKQHGWKPALGKPSLVERTNHGQFQAMATRPYYNPELPCRYLTTPPPGAPALQTVITTTTKVSYQAYQPPAMKYSDSVREVKSLSSCNYAPEDTGMSVYPEPWGPPVTVTRAASPSGPPPMKIAGDCRAIRPTVAIPHEPVSSRTDEAETWDVCLSGLGSAVSYSDRVGPFFTYNNEDF
| null | null |
gliogenesis [GO:0042063]; intracellular calcium ion homeostasis [GO:0006874]; intracellular phosphate ion homeostasis [GO:0030643]; parathyroid gland development [GO:0060017]; regulation of transcription by RNA polymerase II [GO:0006357]; transcription by RNA polymerase II [GO:0006366]
|
chromatin [GO:0000785]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF03615;
|
2.20.25.670;3.30.70.3530;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20190276}.
| null | null | null | null | null |
FUNCTION: Transcription factor that binds specific sequences on gene promoters and activate their transcription. Through the regulation of gene transcription, may play a role in parathyroid gland development. {ECO:0000269|PubMed:20190276, ECO:0000269|PubMed:27745835, ECO:0000269|PubMed:9928992}.
|
Homo sapiens (Human)
|
O75604
|
UBP2_HUMAN
|
MSQLSSTLKRYTESARYTDAHYAKSGYGAYTPSSYGANLAASLLEKEKLGFKPVPTSSFLTRPRTYGPSSLLDYDRGRPLLRPDITGGGKRAESQTRGTERPLGSGLSGGSGFPYGVTNNCLSYLPINAYDQGVTLTQKLDSQSDLARDFSSLRTSDSYRIDPRNLGRSPMLARTRKELCTLQGLYQTASCPEYLVDYLENYGRKGSASQVPSQAPPSRVPEIISPTYRPIGRYTLWETGKGQAPGPSRSSSPGRDGMNSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLHHGSNAHTALVEEFAKLIQTIWTSSPNDVVSPSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHNEVNRVTLRPKSNPENLDHLPDDEKGRQMWRKYLEREDSRIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDVLDGDEKPTCCRCRGRKRCIKKFSIQRFPKILVLHLKRFSESRIRTSKLTTFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGTTMGGHYTAYCRSPGTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYELASPPSRM
|
3.4.19.12
| null |
cell cycle [GO:0007049]; circadian behavior [GO:0048512]; circadian regulation of gene expression [GO:0032922]; entrainment of circadian clock by photoperiod [GO:0043153]; locomotor rhythm [GO:0045475]; muscle organ development [GO:0007517]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of mitotic cell cycle [GO:0045931]; protein deubiquitination [GO:0016579]; protein stabilization [GO:0050821]; proteolysis [GO:0006508]; regulation of signal transduction by p53 class mediator [GO:1901796]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]
|
cyclin binding [GO:0030332]; cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; ubiquitin protein ligase binding [GO:0031625]
|
PF00443;
|
3.90.70.10;
|
Peptidase C19 family, USP2 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O88623}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O88623}. Note=Localizes in the spermatid head in late-elongating spermatids in the thin area between the outer acrosomal membrane and the plasma membrane. {ECO:0000250|UniProtKB:Q5U349}.; SUBCELLULAR LOCATION: [Isoform 4]: Nucleus {ECO:0000250|UniProtKB:Q5U349}. Membrane {ECO:0000250|UniProtKB:O88623}; Peripheral membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:O88623}. Note=Predominantly expressed at membranes. {ECO:0000250|UniProtKB:O88623}.
|
CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12;
| null | null | null | null |
FUNCTION: Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1 (PubMed:17290220, PubMed:19838211, PubMed:19917254). Isoform 1 and isoform 4 possess both ubiquitin-specific peptidase and isopeptidase activities (By similarity). Deubiquitinates MDM2 without reversing MDM2-mediated p53/TP53 ubiquitination and thus indirectly promotes p53/TP53 degradation and limits p53 activity (PubMed:17290220, PubMed:19838211). Has no deubiquitinase activity against p53/TP53 (PubMed:17290220). Prevents MDM2-mediated degradation of MDM4 (PubMed:17290220). Plays a role in the G1/S cell-cycle progression in normal and cancer cells (PubMed:19917254). Regulates the circadian clock by modulating its intrinsic circadian rhythm and its capacity to respond to external cues (By similarity). Associates with clock proteins and deubiquitinates core clock component PER1 but does not affect its overall stability (By similarity). Regulates the nucleocytoplasmic shuttling and nuclear retention of PER1 and its repressive role on the clock transcription factors CLOCK and BMAL1 (By similarity). Plays a role in the regulation of myogenic differentiation of embryonic muscle cells (By similarity). {ECO:0000250|UniProtKB:O88623, ECO:0000250|UniProtKB:Q5U349, ECO:0000269|PubMed:17290220, ECO:0000269|PubMed:19838211, ECO:0000269|PubMed:19917254}.; FUNCTION: [Isoform 4]: Circadian clock output effector that regulates Ca(2+) absorption in the small intestine. Probably functions by regulating protein levels of the membrane scaffold protein NHERF4 in a rhythmic manner, and is therefore likely to control Ca(2+) membrane permeability mediated by the Ca(2+) channel TRPV6 in the intestine. {ECO:0000250|UniProtKB:O88623}.
|
Homo sapiens (Human)
|
O75607
|
NPM3_HUMAN
|
MAAGTAAALAFLSQESRTRAGGVGGLRVPAPVTMDSFFFGCELSGHTRSFTFKVEEEDDAEHVLALTMLCLTEGAKDECNVVEVVARNHDHQEIAVPVANLKLSCQPMLSLDDFQLQPPVTFRLKSGSGPVRITGRHQIVTMSNDVSEEESEEEEEDSDEEEVELCPILPAKKQGGRP
| null | null |
chromatin remodeling [GO:0006338]; rRNA processing [GO:0006364]; rRNA transcription [GO:0009303]
|
actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]
|
chromatin binding [GO:0003682]; histone binding [GO:0042393]; RNA binding [GO:0003723]
|
PF03066;
|
2.60.120.340;
|
Nucleoplasmin family
|
PTM: Phosphorylated. {ECO:0000305}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11722795}. Nucleus, nucleolus {ECO:0000269|PubMed:15596447, ECO:0000269|PubMed:22362753}. Note=Mainly found in the granular component of the nucleolus. {ECO:0000269|PubMed:22362753}.
| null | null | null | null | null |
FUNCTION: Plays a role in the regulation of diverse cellular processes such as ribosome biogenesis, chromatin remodeling or protein chaperoning (PubMed:20073534, PubMed:22362753). Modulates the histone chaperone function and the RNA-binding activity of nucleolar phosphoprotein B23/NPM (PubMed:22362753). Efficiently mediates chromatin remodeling when included in a pentamer containing NPM3 and NPM (PubMed:15596447). {ECO:0000269|PubMed:15596447, ECO:0000269|PubMed:20073534, ECO:0000269|PubMed:22362753}.
|
Homo sapiens (Human)
|
O75608
|
LYPA1_HUMAN
|
MCGNNMSTPLPAIVPAARKATAAVIFLHGLGDTGHGWAEAFAGIRSSHIKYICPHAPVRPVTLNMNVAMPSWFDIIGLSPDSQEDESGIKQAAENIKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPIGGANRDISILQCHGDCDPLVPLMFGSLTVEKLKTLVNPANVTFKTYEGMMHSSCQQEMMDVKQFIDKLLPPID
|
3.1.2.-; 3.1.2.22
| null |
fatty acid metabolic process [GO:0006631]; fatty acid transport [GO:0015908]; negative regulation of aggrephagy [GO:1905336]; negative regulation of Golgi to plasma membrane protein transport [GO:0042997]; protein depalmitoylation [GO:0002084]
|
cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
|
carboxylic ester hydrolase activity [GO:0052689]; lipase activity [GO:0016298]; lysophospholipase activity [GO:0004622]; palmitoyl-(protein) hydrolase activity [GO:0008474]; phospholipase activity [GO:0004620]
|
PF02230;
|
3.40.50.1820;
|
AB hydrolase superfamily, AB hydrolase 2 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19439193}. Cell membrane {ECO:0000269|PubMed:19439193}. Nucleus membrane {ECO:0000269|PubMed:19439193}. Endoplasmic reticulum {ECO:0000269|PubMed:19439193}. Note=Shows predominantly a cytoplasmic localization with a weak expression in the cell membrane, nuclear membrane and endoplasmic reticulum. {ECO:0000269|PubMed:19439193}.
|
CATALYTIC ACTIVITY: Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:74151; EC=3.1.2.22; Evidence={ECO:0000269|PubMed:22399288, ECO:0000269|PubMed:37802024}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000269|PubMed:19439193}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000305|PubMed:19439193}; CATALYTIC ACTIVITY: Reaction=a 1-(9Z-octadecenoyl)-2-acyl-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + a 2-acyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:57875, ChEBI:CHEBI:78421; Evidence={ECO:0000269|PubMed:21393252}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41721; Evidence={ECO:0000305|PubMed:21393252};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=27.3 uM for lysophosphatidylcholine for lysophospholipase activity {ECO:0000269|PubMed:19439193}; KM=3.49 uM for thioesterase activity {ECO:0000269|PubMed:19439193}; Vmax=1.62 umol/min/mg enzyme toward lysophosphatidylcholine for lysophospholipase activity {ECO:0000269|PubMed:19439193}; Vmax=27.3 umol/min/mg enzyme for thioesterase activity {ECO:0000269|PubMed:19439193};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4 for the thioesterase activity. {ECO:0000269|PubMed:19439193};
| null |
FUNCTION: Acts as an acyl-protein thioesterase (PubMed:19439193, PubMed:20418879). Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS (PubMed:20418879). Acts as a palmitoyl thioesterase that catalyzes depalmitoylation of proteins, such as ADRB2, KCNMA1 and SQSTM1 (PubMed:22399288, PubMed:27481942, PubMed:37802024). Acts as a negative regulator of autophagy by mediating palmitoylation of SQSTM1, decreasing affinity between SQSTM1 and ATG8 proteins and recruitment of ubiquitinated cargo proteins to autophagosomes (PubMed:37802024). Acts as a lysophospholipase and hydrolyzes lysophosphatidylcholine (lyso-PC) (PubMed:19439193). Also hydrolyzes lysophosphatidylethanolamine (lyso-PE), lysophosphatidylinositol (lyso-PI) and lysophosphatidylserine (lyso-PS) (By similarity). Has much higher thioesterase activity than lysophospholipase activity (PubMed:19439193). Contributes to the production of lysophosphatidic acid (LPA) during blood coagulation by recognizing and cleaving plasma phospholipids to generate lysophospholipids which in turn act as substrates for ENPP2 to produce LPA (PubMed:21393252). {ECO:0000250|UniProtKB:P70470, ECO:0000269|PubMed:19439193, ECO:0000269|PubMed:20418879, ECO:0000269|PubMed:21393252, ECO:0000269|PubMed:22399288, ECO:0000269|PubMed:27481942, ECO:0000269|PubMed:37802024}.
|
Homo sapiens (Human)
|
O75610
|
LFTY1_HUMAN
|
MQPLWLCWALWVLPLASPGAALTGEQLLGSLLRQLQLKEVPTLDRADMEELVIPTHVRAQYVALLQRSHGDRSRGKRFSQSFREVAGRFLALEASTHLLVFGMEQRLPPNSELVQAVLRLFQEPVPKAALHRHGRLSPRSARARVTVEWLRVRDDGSNRTSLIDSRLVSVHESGWKAFDVTEAVNFWQQLSRPRQPLLLQVSVQREHLGPLASGAHKLVRFASQGAPAGLGEPQLELHTLDLGDYGAQGDCDPEAPMTEGTRCCRQEMYIDLQGMKWAENWVLEPPGFLAYECVGTCRQPPEALAFKWPFLGPRQCIASETDSLPMIVSIKEGGRTRPQVVSLPNMRVQKCSCASDGALVPRRLQP
| null | null |
anterior/posterior axis specification [GO:0009948]; determination of left/right symmetry [GO:0007368]; heart morphogenesis [GO:0003007]; negative regulation of transcription by RNA polymerase II [GO:0000122]; transforming growth factor beta receptor signaling pathway [GO:0007179]
|
extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; transforming growth factor beta receptor binding [GO:0005160]
|
PF00019;PF00688;
|
2.60.120.970;2.10.90.10;
|
TGF-beta family
|
PTM: The processing of the protein may also occur at the second R-X-X-R site located at AA 132-135. Processing appears to be regulated in a cell-type specific manner.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Required for left-right axis determination as a regulator of LEFTY2 and NODAL.
|
Homo sapiens (Human)
|
O75616
|
ERAL1_HUMAN
|
MAAPSWRGARLVQSVLRVWQVGPHVARERVIPFSSLLGFQRRCVSCVAGSAFSGPRLASASRSNGQGSALDHFLGFSQPDSSVTPCVPAVSMNRDEQDVLLVHHPDMPENSRVLRVVLLGAPNAGKSTLSNQLLGRKVFPVSRKVHTTRCQALGVITEKETQVILLDTPGIISPGKQKRHHLELSLLEDPWKSMESADLVVVLVDVSDKWTRNQLSPQLLRCLTKYSQIPSVLVMNKVDCLKQKSVLLELTAALTEGVVNGKKLKMRQAFHSHPGTHCPSPAVKDPNTQSVGNPQRIGWPHFKEIFMLSALSQEDVKTLKQYLLTQAQPGPWEYHSAVLTSQTPEEICANIIREKLLEHLPQEVPYNVQQKTAVWEEGPGGELVIQQKLLVPKESYVKLLIGPKGHVISQIAQEAGHDLMDIFLCDVDIRLSVKLLK
| null | null |
ribosomal small subunit assembly [GO:0000028]
|
cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
|
GTP binding [GO:0005525]; ribosomal small subunit binding [GO:0043024]; RNA binding [GO:0003723]; rRNA binding [GO:0019843]
|
PF01926;
|
3.30.300.20;3.40.50.300;
|
TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Era GTPase family
| null |
SUBCELLULAR LOCATION: Mitochondrion matrix. Mitochondrion inner membrane; Peripheral membrane protein. Note=Localizes on the matrix side on the mitochondrial inner membrane.
| null | null | null | null | null |
FUNCTION: Probable GTPase that plays a role in the mitochondrial ribosomal small subunit assembly. Specifically binds the 12S mitochondrial rRNA (12S mt-rRNA) to a 33 nucleotide section delineating the 3' terminal stem-loop region. May act as a chaperone that protects the 12S mt-rRNA on the 28S mitoribosomal subunit during ribosomal small subunit assembly. {ECO:0000269|PubMed:20430825, ECO:0000269|PubMed:20604745, ECO:0000269|PubMed:28449065}.
|
Homo sapiens (Human)
|
O75618
|
DEDD_HUMAN
|
MAGLKRRASQVWPEEHGEQEHGLYSLHRMFDIVGTHLTHRDVRVLSFLFVDVIDDHERGLIRNGRDFLLALERQGRCDESNFRQVLQLLRIITRHDLLPYVTLKRRRAVCPDLVDKYLEETSIRYVTPRALSDPEPRPPQPSKTVPPHYPVVCCPTSGPQMCSKRPARGRATLGSQRKRRKSVTPDPKEKQTCDIRLRVRAEYCQHETALQGNVFSNKQDPLERQFERFNQANTILKSRDLGSIICDIKFSELTYLDAFWRDYINGSLLEALKGVFITDSLKQAVGHEAIKLLVNVDEEDYELGRQKLLRNLMLQALP
| null | null |
decidualization [GO:0046697]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of transcription of nucleolar large rRNA by RNA polymerase I [GO:1901837]; regulation of apoptotic process [GO:0042981]; spermatogenesis [GO:0007283]
|
cytoplasm [GO:0005737]; nucleolus [GO:0005730]
|
DNA binding [GO:0003677]
|
PF01335;PF20694;
|
1.10.533.10;
| null |
PTM: Exists predominantly in a mono- or diubiquitinated form.
|
SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus {ECO:0000250}. Note=Translocated to the nucleus during CD95-mediated apoptosis where it is localized in the nucleoli (By similarity). Following apoptosis induction, the mono and/or diubiquitination form increases and forms filamentous structures that colocalize with KRT8 and KRT18 intermediate filament network in simple epithelial cells. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: A scaffold protein that directs CASP3 to certain substrates and facilitates their ordered degradation during apoptosis. May also play a role in mediating CASP3 cleavage of KRT18. Regulates degradation of intermediate filaments during apoptosis. May play a role in the general transcription machinery in the nucleus and might be an important regulator of the activity of GTF3C3. Inhibits DNA transcription in vitro (By similarity). {ECO:0000250, ECO:0000269|PubMed:12235123}.
|
Homo sapiens (Human)
|
O75626
|
PRDM1_HUMAN
|
MLDICLEKRVGTTLAAPKCNSSTVRFQGLAEGTKGTMKMDMEDADMTLWTEAEFEEKCTYIVNDHPWDSGADGGTSVQAEASLPRNLLFKYATNSEEVIGVMSKEYIPKGTRFGPLIGEIYTNDTVPKNANRKYFWRIYSRGELHHFIDGFNEEKSNWMRYVNPAHSPREQNLAACQNGMNIYFYTIKPIPANQELLVWYCRDFAERLHYPYPGELTMMNLTQTQSSLKQPSTEKNELCPKNVPKREYSVKEILKLDSNPSKGKDLYRSNISPLTSEKDLDDFRRRGSPEMPFYPRVVYPIRAPLPEDFLKASLAYGIERPTYITRSPIPSSTTPSPSARSSPDQSLKSSSPHSSPGNTVSPVGPGSQEHRDSYAYLNASYGTEGLGSYPGYAPLPHLPPAFIPSYNAHYPKFLLPPYGMNCNGLSAVSSMNGINNFGLFPRLCPVYSNLLGGGSLPHPMLNPTSLPSSLPSDGARRLLQPEHPREVLVPAPHSAFSFTGAAASMKDKACSPTSGSPTAGTAATAEHVVQPKATSAAMAAPSSDEAMNLIKNKRNMTGYKTLPYPLKKQNGKIKYECNVCAKTFGQLSNLKVHLRVHSGERPFKCQTCNKGFTQLAHLQKHYLVHTGEKPHECQVCHKRFSSTSNLKTHLRLHSGEKPYQCKVCPAKFTQFVHLKLHKRLHTRERPHKCSQCHKNYIHLCSLKVHLKGNCAAAPAPGLPLEDLTRINEEIEKFDISDNADRLEDVEDDISVISVVEKEILAVVRKEKEETGLKVSLQRNMGNGLLSSGCSLYESSDLPLMKLPPSNPLPLVPVKVKQETVEPMDP
|
2.1.1.-
| null |
adaptive immune response [GO:0002250]; aorta development [GO:0035904]; artery morphogenesis [GO:0048844]; cell fate commitment [GO:0045165]; coronary vasculature development [GO:0060976]; eye photoreceptor cell development [GO:0042462]; gene expression [GO:0010467]; germ cell development [GO:0007281]; heart valve development [GO:0003170]; innate immune response [GO:0045087]; intestinal epithelial cell development [GO:0060576]; kidney development [GO:0001822]; maternal placenta development [GO:0001893]; methylation [GO:0032259]; morphogenesis of a branching structure [GO:0001763]; negative regulation of gene expression [GO:0010629]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of gene expression [GO:0010628]; post-embryonic development [GO:0009791]; regulation of cell population proliferation [GO:0042127]; regulation of extrathymic T cell differentiation [GO:0033082]; regulation of natural killer cell differentiation [GO:0032823]; regulation of NK T cell differentiation [GO:0051136]; regulation of transcription by RNA polymerase II [GO:0006357]; retinal bipolar neuron differentiation [GO:0060040]; sebum secreting cell proliferation [GO:1990654]; trophoblast giant cell differentiation [GO:0060707]; ventricular septum development [GO:0003281]
|
cytoplasm [GO:0005737]; 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]; histone methyltransferase binding [GO:1990226]; metal ion binding [GO:0046872]; methyltransferase activity [GO:0008168]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF21549;PF00096;
|
3.30.160.60;2.170.270.10;
|
Class V-like SAM-binding methyltransferase superfamily
|
PTM: Sumoylation at Lys-816 by PIAS1 augments transcriptional repressor activity, and is critical for plasma cell differentiation (PubMed:22555612). Can be sumoylated with SUMO1 and SUMO2 by PML. Degradation of the wild-type protein mostly depends upon sumoylation, rather than ubiquitination (PubMed:28842558). Desumoylated by SENP1 and SENP6 (PubMed:28842558). {ECO:0000269|PubMed:22555612, ECO:0000269|PubMed:28842558}.; PTM: Ubiquitinated by the SCF(FBXO11) complex, leading to its degradation by the proteasome. {ECO:0000269|PubMed:24613396}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28842558}. Cytoplasm {ECO:0000269|PubMed:21421998}.
| null | null | null | null | null |
FUNCTION: Transcription factor that mediates a transcriptional program in various innate and adaptive immune tissue-resident lymphocyte T cell types such as tissue-resident memory T (Trm), natural killer (trNK) and natural killer T (NKT) cells and negatively regulates gene expression of proteins that promote the egress of tissue-resident T-cell populations from non-lymphoid organs. Plays a role in the development, retention and long-term establishment of adaptive and innate tissue-resident lymphocyte T cell types in non-lymphoid organs, such as the skin and gut, but also in other nonbarrier tissues like liver and kidney, and therefore may provide immediate immunological protection against reactivating infections or viral reinfection (By similarity). Binds specifically to the PRDI element in the promoter of the beta-interferon gene (PubMed:1851123). Drives the maturation of B-lymphocytes into Ig secreting cells (PubMed:12626569). Associates with the transcriptional repressor ZNF683 to chromatin at gene promoter regions (By similarity). Binds to the promoter and acts as a transcriptional repressor of IRF8, thereby promotes transcription of osteoclast differentiation factors such as NFATC1 and EEIG1 (By similarity). {ECO:0000250|UniProtKB:Q60636, ECO:0000269|PubMed:12626569, ECO:0000269|PubMed:1851123}.
|
Homo sapiens (Human)
|
O75628
|
REM1_HUMAN
|
MTLNTEQEAKTPLHRRASTPLPLSPRGHQPGRLSTVPSTQSQHPRLGQSASLNPPTQKPSPAPDDWSSESSDSEGSWEALYRVVLLGDPGVGKTSLASLFAGKQERDLHEQLGEDVYERTLTVDGEDTTLVVVDTWEAEKLDKSWSQESCLQGGSAYVIVYSIADRGSFESASELRIQLRRTHQADHVPIILVGNKADLARCREVSVEEGRACAVVFDCKFIETSATLQHNVAELFEGVVRQLRLRRRDSAAKEPPAPRRPASLAQRARRFLARLTARSARRRALKARSKSCHNLAVL
| null | null |
negative regulation of calcium ion transmembrane transport via high voltage-gated calcium channel [GO:1904878]; regulation of skeletal muscle contraction by calcium ion signaling [GO:0014722]
|
I band [GO:0031674]; plasma membrane [GO:0005886]; T-tubule [GO:0030315]
|
calcium channel regulator activity [GO:0005246]; calmodulin binding [GO:0005516]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; transmembrane transporter binding [GO:0044325]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, RGK family
| null | null | null | null | null | null | null |
FUNCTION: Promotes endothelial cell sprouting and actin cytoskeletal reorganization. May be involved in angiogenesis. May function in Ca(2+) signaling.
|
Homo sapiens (Human)
|
O75629
|
CREG1_HUMAN
|
MAGLSRGSARALLAALLASTLLALLVSPARGRGGRDHGDWDEASRLPPLPPREDAARVARFVTHVSDWGALATISTLEAVRGRPFADVLSLSDGPPGAGSGVPYFYLSPLQLSVSNLQENPYATLTMTLAQTNFCKKHGFDPQSPLCVHIMLSGTVTKVNETEMDIAKHSLFIRHPEMKTWPSSHNWFFAKLNITNIWVLDYFGGPKIVTPEEYYNVTVQ
| null | null |
autophagy [GO:0006914]; endocytosis [GO:0006897]; lysosomal lumen acidification [GO:0007042]; regulation of transcription by RNA polymerase II [GO:0006357]
|
azurophil granule lumen [GO:0035578]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; transcription regulator complex [GO:0005667]
|
transcription corepressor activity [GO:0003714]
|
PF13883;
| null |
CREG family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:10815803, ECO:0000269|PubMed:19159218}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10815803}.
| null | null | null | null | null |
FUNCTION: May contribute to the transcriptional control of cell growth and differentiation. Antagonizes transcriptional activation and cellular transformation by the adenovirus E1A protein. The transcriptional control activity of cell growth requires interaction with IGF2R. {ECO:0000269|PubMed:12934103, ECO:0000269|PubMed:9710587}.
|
Homo sapiens (Human)
|
O75631
|
UPK3A_HUMAN
|
MPPLWALLALGCLRFGSAVNLQPQLASVTFATNNPTLTTVALEKPLCMFDSKEALTGTHEVYLYVLVDSAISRNASVQDSTNTPLGSTFLQTEGGRTGPYKAVAFDLIPCSDLPSLDAIGDVSKASQILNAYLVRVGANGTCLWDPNFQGLCNAPLSAATEYRFKYVLVNMSTGLVEDQTLWSDPIRTNQLTPYSTIDTWPGRRSGGMIVITSILGSLPFFLLVGFAGAIALSLVDMGSSDGETTHDSQITQEAVPKSLGASESSYTSVNRGPPLDRAEVYSSKLQD
| null | null |
cell morphogenesis [GO:0000902]; epithelial cell differentiation [GO:0030855]; kidney development [GO:0001822]; potassium ion homeostasis [GO:0055075]; sodium ion homeostasis [GO:0055078]; urea transport [GO:0015840]; urinary bladder development [GO:0060157]; water transport [GO:0006833]
|
apical plasma membrane urothelial plaque [GO:0120001]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]
| null | null | null |
Uroplakin-3 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Heterodimer formation with UPK1B is a prerequisite to exit out of the endoplasmic reticulum (ER). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in AUM-cytoskeleton interaction in terminally differentiated urothelial cells. It also contributes to the formation of urothelial glycocalyx which may play an important role in preventing bacterial adherence (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O75636
|
FCN3_HUMAN
|
MDLLWILPSLWLLLLGGPACLKTQEHPSCPGPRELEASKVVLLPSCPGAPGSPGEKGAPGPQGPPGPPGKMGPKGEPGDPVNLLRCQEGPRNCRELLSQGATLSGWYHLCLPEGRALPVFCDMDTEGGGWLVFQRRQDGSVDFFRSWSSYRAGFGNQESEFWLGNENLHQLTLQGNWELRVELEDFNGNRTFAHYATFRLLGEVDHYQLALGKFSEGTAGDSLSLHSGRPFTTYDADHDSSNSNCAVIVHGAWWYASCYRSNLNGRYAVSEAAAHKYGIDWASGRGVGHPYRRVRMMLR
| null | null |
cell surface pattern recognition receptor signaling pathway [GO:0002752]; complement activation [GO:0006956]; complement activation, lectin pathway [GO:0001867]; defense response to virus [GO:0051607]; negative regulation of RNA biosynthetic process [GO:1902679]; negative regulation of viral entry into host cell [GO:0046597]; positive regulation of opsonization [GO:1903028]; proteolysis [GO:0006508]; recognition of apoptotic cell [GO:0043654]
|
blood microparticle [GO:0072562]; collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; serine-type endopeptidase complex [GO:1905370]
|
antigen binding [GO:0003823]; carbohydrate binding [GO:0030246]; carbohydrate derivative binding [GO:0097367]; metal ion binding [GO:0046872]; signaling receptor binding [GO:0005102]
|
PF00147;
|
3.90.215.10;4.10.530.10;
|
Ficolin lectin family
|
PTM: The N-terminus is blocked.
|
SUBCELLULAR LOCATION: Secreted. Note=Found in blood plasma, bronchus, alveolus and bile duct.
| null | null | null | null | null |
FUNCTION: May function in innate immunity through activation of the lectin complement pathway. Calcium-dependent and GlcNAc-binding lectin. Has affinity with GalNAc, GlcNAc, D-fucose, as mono/oligosaccharide and lipopolysaccharides from S.typhimurium and S.minnesota. {ECO:0000269|PubMed:11907111, ECO:0000269|PubMed:17215869}.
|
Homo sapiens (Human)
|
O75638
|
CTAG2_HUMAN
|
MQAEGRGTGGSTGDADGPGGPGIPDGPGGNAGGPGEAGATGGRGPRGAGAARASGPRGGAPRGPHGGAASAQDGRCPCGARRPDSRLLELHITMPFSSPMEAELVRRILSRDAAPLPRPGAVLKDFTVSGNLLFMSVRDQDREGAGRMRVVGWGLGSASPEGQKARDLRTPKHKVSEQRPGTPGPPPPEGAQGDGCRGVAFNVMFSAPHI
| null | null |
tRNA threonylcarbamoyladenosine metabolic process [GO:0070525]
|
centrosome [GO:0005813]
| null |
PF09341;
|
3.30.310.50;
|
CTAG/PCC1 family
| null | null | null | null | null | null | null | null |
Homo sapiens (Human)
|
O75643
|
U520_HUMAN
|
MADVTARSLQYEYKANSNLVLQADRSLIDRTRRDEPTGEVLSLVGKLEGTRMGDKAQRTKPQMQEERRAKRRKRDEDRHDINKMKGYTLLSEGIDEMVGIIYKPKTKETRETYEVLLSFIQAALGDQPRDILCGAADEVLAVLKNEKLRDKERRKEIDLLLGQTDDTRYHVLVNLGKKITDYGGDKEIQNMDDNIDETYGVNVQFESDEEEGDEDVYGEVREEASDDDMEGDEAVVRCTLSANLVASGELMSSKKKDLHPRDIDAFWLQRQLSRFYDDAIVSQKKADEVLEILKTASDDRECENQLVLLLGFNTFDFIKVLRQHRMMILYCTLLASAQSEAEKERIMGKMEADPELSKFLYQLHETEKEDLIREERSRRERVRQSRMDTDLETMDLDQGGEALAPRQVLDLEDLVFTQGSHFMANKRCQLPDGSFRRQRKGYEEVHVPALKPKPFGSEEQLLPVEKLPKYAQAGFEGFKTLNRIQSKLYRAALETDENLLLCAPTGAGKTNVALMCMLREIGKHINMDGTINVDDFKIIYIAPMRSLVQEMVGSFGKRLATYGITVAELTGDHQLCKEEISATQIIVCTPEKWDIITRKGGERTYTQLVRLIILDEIHLLHDDRGPVLEALVARAIRNIEMTQEDVRLIGLSATLPNYEDVATFLRVDPAKGLFYFDNSFRPVPLEQTYVGITEKKAIKRFQIMNEIVYEKIMEHAGKNQVLVFVHSRKETGKTARAIRDMCLEKDTLGLFLREGSASTEVLRTEAEQCKNLELKDLLPYGFAIHHAGMTRVDRTLVEDLFADKHIQVLVSTATLAWGVNLPAHTVIIKGTQVYSPEKGRWTELGALDILQMLGRAGRPQYDTKGEGILITSHGELQYYLSLLNQQLPIESQMVSKLPDMLNAEIVLGNVQNAKDAVNWLGYAYLYIRMLRSPTLYGISHDDLKGDPLLDQRRLDLVHTAALMLDKNNLVKYDKKTGNFQVTELGRIASHYYITNDTVQTYNQLLKPTLSEIELFRVFSLSSEFKNITVREEEKLELQKLLERVPIPVKESIEEPSAKINVLLQAFISQLKLEGFALMADMVYVTQSAGRLMRAIFEIVLNRGWAQLTDKTLNLCKMIDKRMWQSMCPLRQFRKLPEEVVKKIEKKNFPFERLYDLNHNEIGELIRMPKMGKTIHKYVHLFPKLELSVHLQPITRSTLKVELTITPDFQWDEKVHGSSEAFWILVEDVDSEVILHHEYFLLKAKYAQDEHLITFFVPVFEPLPPQYFIRVVSDRWLSCETQLPVSFRHLILPEKYPPPTELLDLQPLPVSALRNSAFESLYQDKFPFFNPIQTQVFNTVYNSDDNVFVGAPTGSGKTICAEFAILRMLLQSSEGRCVYITPMEALAEQVYMDWYEKFQDRLNKKVVLLTGETSTDLKLLGKGNIIISTPEKWDILSRRWKQRKNVQNINLFVVDEVHLIGGENGPVLEVICSRMRYISSQIERPIRIVALSSSLSNAKDVAHWLGCSATSTFNFHPNVRPVPLELHIQGFNISHTQTRLLSMAKPVYHAITKHSPKKPVIVFVPSRKQTRLTAIDILTTCAADIQRQRFLHCTEKDLIPYLEKLSDSTLKETLLNGVGYLHEGLSPMERRLVEQLFSSGAIQVVVASRSLCWGMNVAAHLVIIMDTQYYNGKIHAYVDYPIYDVLQMVGHANRPLQDDEGRCVIMCQGSKKDFFKKFLYEPLPVESHLDHCMHDHFNAEIVTKTIENKQDAVDYLTWTFLYRRMTQNPNYYNLQGISHRHLSDHLSELVEQTLSDLEQSKCISIEDEMDVAPLNLGMIAAYYYINYTTIELFSMSLNAKTKVRGLIEIISNAAEYENIPIRHHEDNLLRQLAQKVPHKLNNPKFNDPHVKTNLLLQAHLSRMQLSAELQSDTEEILSKAIRLIQACVDVLSSNGWLSPALAAMELAQMVTQAMWSKDSYLKQLPHFTSEHIKRCTDKGVESVFDIMEMEDEERNALLQLTDSQIADVARFCNRYPNIELSYEVVDKDSIRSGGPVVVLVQLEREEEVTGPVIAPLFPQKREEGWWVVIGDAKSNSLISIKRLTLQQKAKVKLDFVAPATGAHNYTLYFMSDAYMGCDQEYKFSVDVKEAETDSDSD
|
3.6.4.13
| null |
cis assembly of pre-catalytic spliceosome [GO:0000354]; mRNA splicing, via spliceosome [GO:0000398]; osteoblast differentiation [GO:0001649]; spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) [GO:0000388]
|
catalytic step 2 spliceosome [GO:0071013]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]; U2-type catalytic step 1 spliceosome [GO:0071006]; U2-type precatalytic spliceosome [GO:0071005]; U4/U6 x U5 tri-snRNP complex [GO:0046540]; U5 snRNP [GO:0005682]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; helicase activity [GO:0004386]; identical protein binding [GO:0042802]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]
|
PF21188;PF00270;PF00271;PF18149;PF02889;
|
1.10.150.20;2.60.40.150;3.40.50.300;1.10.3380.10;1.10.10.10;
|
Helicase family, SKI2 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316, ECO:0000269|PubMed:30315277, ECO:0000269|PubMed:30705154, ECO:0000269|PubMed:30728453, ECO:0000269|PubMed:9539711}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000269|PubMed:23045696, ECO:0000269|PubMed:35241646};
| null | null | null | null |
FUNCTION: Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, an essential step in the assembly of a catalytically active spliceosome (PubMed:35241646). Plays a role in pre-mRNA splicing as a core component of precatalytic, catalytic and postcatalytic spliceosomal complexes (PubMed:28502770, PubMed:28781166, PubMed:29301961, PubMed:29360106, PubMed:29361316, PubMed:30315277, PubMed:30705154, PubMed:30728453). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). Involved in spliceosome assembly, activation and disassembly. Mediates changes in the dynamic network of RNA-RNA interactions in the spliceosome. {ECO:0000269|PubMed:16723661, ECO:0000269|PubMed:23045696, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316, ECO:0000269|PubMed:30315277, ECO:0000269|PubMed:30705154, ECO:0000269|PubMed:30728453, ECO:0000269|PubMed:35241646, ECO:0000269|PubMed:8670905, ECO:0000269|PubMed:9539711, ECO:0000305|PubMed:33509932}.
|
Homo sapiens (Human)
|
O75648
|
MTU1_HUMAN
|
MQALRHVVCALSGGVDSAVAALLLRRRGYQVTGVFMKNWDSLDEHGVCTADKDCEDAYRVCQILDIPFHQVSYVKEYWNDVFSDFLNEYEKGRTPNPDIVCNKHIKFSCFFHYAVDNLGADAIATGHYARTSLEDEEVFEQKHVKKPEGLFRNRFEVRNAVKLLQAADSFKDQTFFLSQVSQDALRRTIFPLGGLTKEFVKKIAAENRLHHVLQKKESMGMCFIGKRNFEHFLLQYLQPRPGHFISIEDNKVLGTHKGWFLYTLGQRANIGGLREPWYVVEKDSVKGDVFVAPRTDHPALYRDLLRTSRVHWIAEEPPAALVRDKMMECHFRFRHQMALVPCVLTLNQDGTVWVTAVQAVRALATGQFAVFYKGDECLGSGKILRLGPSAYTLQKGQRRAGMATESPSDSPEDGPGLSPLL
|
2.8.1.14
| null |
tRNA wobble position uridine thiolation [GO:0002143]
|
mitochondrion [GO:0005739]
|
ATP binding [GO:0005524]; tRNA binding [GO:0000049]; tRNA-5-taurinomethyluridine 2-sulfurtransferase [GO:0061708]
|
PF03054;PF20258;PF20259;
|
2.30.30.280;3.40.50.620;2.40.30.10;
|
MnmA/TRMU family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:15509579, ECO:0000269|PubMed:15944150, ECO:0000269|PubMed:16513084, ECO:0000269|PubMed:16826519}.
|
CATALYTIC ACTIVITY: Reaction=5-taurinomethyluridine(34) in tRNA + AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] = 5-taurinomethyl-2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:47040, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11726, Rhea:RHEA-COMP:11732, Rhea:RHEA-COMP:11733, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:61963, ChEBI:CHEBI:87171, ChEBI:CHEBI:87172, ChEBI:CHEBI:456215; EC=2.8.1.14; Evidence={ECO:0000250|UniProtKB:Q12093};
| null | null | null | null |
FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base. {ECO:0000269|PubMed:15509579, ECO:0000269|PubMed:15944150, ECO:0000269|PubMed:16826519}.
|
Homo sapiens (Human)
|
O75663
|
TIPRL_HUMAN
|
MMIHGFQSSHRDFCFGPWKLTASKTHIMKSADVEKLADELHMPSLPEMMFGDNVLRIQHGSGFGIEFNATDALRCVNNYQGMLKVACAEEWQESRTEGEHSKEVIKPYDWTYTTDYKGTLLGESLKLKVVPTTDHIDTEKLKAREQIKFFEEVLLFEDELHDHGVSSLSVKIRVMPSSFFLLLRFFLRIDGVLIRMNDTRLYHEADKTYMLREYTSRESKISSLMHVPPSLFTEPNEISQYLPIKEAVCEKLIFPERIDPNPADSQKSTQVE
| null | null |
DNA damage checkpoint signaling [GO:0000077]; negative regulation of phosphoprotein phosphatase activity [GO:0032515]; TOR signaling [GO:0031929]
|
cytosol [GO:0005829]
| null |
PF04176;
| null |
TIP41 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17944932}.
| null | null | null | null | null |
FUNCTION: May be a allosteric regulator of serine/threonine-protein phosphatase 2A (PP2A). Isoform 1 inhibits catalytic activity of the PP2A(D) core complex in vitro. The PP2A(C):TIPRL complex does not show phosphatase activity. Acts as a negative regulator of serine/threonine-protein phosphatase 4 probably by inhibiting the formation of the active PPP4C:PPP4R2 complex; the function is proposed to implicate it in DNA damage response by promoting H2AX phosphorylated on Ser-140 (gamma-H2AX). May play a role in the regulation of ATM/ATR signaling pathway controlling DNA replication and repair. {ECO:0000269|PubMed:17384681, ECO:0000269|PubMed:26717153}.
|
Homo sapiens (Human)
|
O75665
|
OFD1_HUMAN
|
MMAQSNMFTVADVLSQDELRKKLYQTFKDRGILDTLKTQLRNQLIHELMHPVLSGELQPRSISVEGSSLLIGASNSLVADHLQRCGYEYSLSVFFPESGLAKEKVFTMQDLLQLIKINPTSSLYKSLVSGSDKENQKGFLMHFLKELAEYHQAKESCNMETQTSSTFNRDSLAEKLQLIDDQFADAYPQRIKFESLEIKLNEYKREIEEQLRAEMCQKLKFFKDTEIAKIKMEAKKKYEKELTMFQNDFEKACQAKSEALVLREKSTLERIHKHQEIETKEIYAQRQLLLKDMDLLRGREAELKQRVEAFELNQKLQEEKHKSITEALRRQEQNIKSFEETYDRKLKNELLKYQLELKDDYIIRTNRLIEDERKNKEKAVHLQEELIAINSKKEELNQSVNRVKELELELESVKAQSLAITKQNHMLNEKVKEMSDYSLLKEEKLELLAQNKLLKQQLEESRNENLRLLNRLAQPAPELAVFQKELRKAEKAIVVEHEEFESCRQALHKQLQDEIEHSAQLKAQILGYKASVKSLTTQVADLKLQLKQTQTALENEVYCNPKQSVIDRSVNGLINGNVVPCNGEISGDFLNNPFKQENVLARMVASRITNYPTAWVEGSSPDSDLEFVANTKARVKELQQEAERLEKAFRSYHRRVIKNSAKSPLAAKSPPSLHLLEAFKNITSSSPERHIFGEDRVVSEQPQVGTLEERNDVVEALTGSAASRLRGGTSSRRLSSTPLPKAKRSLESEMYLEGLGRSHIASPSPCPDRMPLPSPTESRHSLSIPPVSSPPEQKVGLYRRQTELQDKSEFSDVDKLAFKDNEEFESSFESAGNMPRQLEMGGLSPAGDMSHVDAAAAAVPLSYQHPSVDQKQIEEQKEEEKIREQQVKERRQREERRQSNLQEVLERERRELEKLYQERKMIEESLKIKIKKELEMENELEMSNQEIKDKSAHSENPLEKYMKIIQQEQDQESADKSSKKMVQEGSLVDTLQSSDKVESLTGFSHEELDDSW
| null | null |
axoneme assembly [GO:0035082]; cilium assembly [GO:0060271]; embryonic body morphogenesis [GO:0010172]; epithelial cilium movement involved in determination of left/right asymmetry [GO:0060287]; negative regulation of fibroblast growth factor receptor signaling pathway involved in neural plate anterior/posterior pattern formation [GO:2000314]
|
centriolar satellite [GO:0034451]; centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytosol [GO:0005829]; extracellular region [GO:0005576]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; motile cilium [GO:0031514]; nucleus [GO:0005634]
|
alpha-tubulin binding [GO:0043014]; gamma-tubulin binding [GO:0043015]; identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090]
|
PF16045;
| null |
OFD1 family
|
PTM: Phosphorylated. Phosphorylation at Ser-735, by the cAMP-dependent protein kinase PKA, triggers ubiquitination and proteasomal degradation of OFD1. Also increases its interaction with TBC1D31 and regulates its function in ciliogenesis. {ECO:0000269|PubMed:33934390}.; PTM: Ubiquitinated by PJA2, upon phosphorylation at Ser-735 by PKA, leads to the proteasomal degradation of OFD1. {ECO:0000269|PubMed:33934390}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:12595504, ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:20230748, ECO:0000269|PubMed:26643951}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17761535}. Nucleus {ECO:0000269|PubMed:17761535}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:24121310, ECO:0000269|PubMed:26643951}. Note=Localizes to centriole distal ends and to centriolar satellites (PubMed:20230748, PubMed:24121310). Localization to centrioles and pericentriolar satellites may be mediated by KIAA0753/OFIP (PubMed:26643951). {ECO:0000269|PubMed:26643951}.
| null | null | null | null | null |
FUNCTION: Component of the centrioles controlling mother and daughter centrioles length. Recruits to the centriole IFT88 and centriole distal appendage-specific proteins including CEP164 (By similarity). Involved in the biogenesis of the cilium, a centriole-associated function. The cilium is a cell surface projection found in many vertebrate cells required to transduce signals important for development and tissue homeostasis (PubMed:33934390). Plays an important role in development by regulating Wnt signaling and the specification of the left-right axis. Only OFD1 localized at the centriolar satellites is removed by autophagy, which is an important step in the ciliogenesis regulation (By similarity). {ECO:0000250|UniProtKB:Q80Z25, ECO:0000269|PubMed:33934390}.
|
Homo sapiens (Human)
|
O75674
|
TM1L1_HUMAN
|
MAFGKSHRDPYATSVGHLIEKATFAGVQTEDWGQFMHICDIINTTQDGPKDAVKALKKRISKNYNHKEIQLTLSLIDMCVQNCGPSFQSLIVKKEFVKENLVKLLNPRYNLPLDIQNRILNFIKTWSQGFPGGVDVSEVKEVYLDLVKKGVQFPPSEAEAETARQETAQISSNPPTSVPTAPALSSVIAPKNSTVTLVPEQIGKLHSELDMVKMNVRVMSAILMENTPGSENHEDIELLQKLYKTGREMQERIMDLLVVVENEDVTVELIQVNEDLNNAILGYERFTRNQQRILEQNKNQKEATNTTSEPSAPSQDLLDLSPSPRMPRATLGELNTMNNQLSGLNFSLPSSDVTNNLKPSLHPQMNLLALENTEIPPFAQRTSQNLTSSHAYDNFLEHSNSVFLQPVSLQTIAAAPSNQSLPPLPSNHPAMTKSDLQPPNYYEVMEFDPLAPAVTTEAIYEEIDAHQHKGAQNDGD
| null | null |
activation of protein kinase activity [GO:0032147]; negative regulation of mitotic nuclear division [GO:0045839]; positive regulation of protein autophosphorylation [GO:0031954]; protein transport [GO:0015031]; signal transduction [GO:0007165]; ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043162]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome [GO:0005768]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; Golgi stack [GO:0005795]; lysosome [GO:0005764]; membrane [GO:0016020]
|
clathrin binding [GO:0030276]; phosphatidylinositol binding [GO:0035091]; protein kinase activator activity [GO:0030295]; protein kinase binding [GO:0019901]; SH3 domain binding [GO:0017124]; ubiquitin binding [GO:0043130]
|
PF03127;PF00790;
|
1.20.58.160;1.25.40.90;
|
TOM1 family
|
PTM: Phosphorylated on tyrosines by FYN and LYN. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack. Endosome membrane {ECO:0000305}. Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=A small proportion is membrane-associated. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Probable adapter protein involved in signaling pathways. Interacts with the SH2 and SH3 domains of various signaling proteins when it is phosphorylated. May promote FYN activation, possibly by disrupting intramolecular SH3-dependent interactions (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O75676
|
KS6A4_HUMAN
|
MGDEDDDESCAVELRITEANLTGHEEKVSVENFELLKVLGTGAYGKVFLVRKAGGHDAGKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQAPFLVTLHYAFQTDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTFSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPVAQDLLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRLEPVYSPPGSPPPGDPRIFQGYSFVAPSILFDHNNAVMTDGLEAPGAGDRPGRAAVARSAMMQDSPFFQQYELDLREPALGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAGVVHRDLKPENILYADDTPGAPVKIIDFGFARLRPQSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEIMCKIREGRFSLDGEAWQGVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWLQDGSARSSPPLRTPDVLESSGPAVRSGLNATFMAFNRGKREGFFLKSVENAPLAKRRKQKLRSATASRRGSPAPANPGRAPVASKGAPRRANGPLPPS
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9792677};
|
inflammatory response [GO:0006954]; interleukin-1-mediated signaling pathway [GO:0070498]; intracellular signal transduction [GO:0035556]; negative regulation of cytokine production [GO:0001818]; positive regulation of CREB transcription factor activity [GO:0032793]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of transcription by RNA polymerase II [GO:0045944]; post-translational protein modification [GO:0043687]; protein phosphorylation [GO:0006468]; regulation of DNA-templated transcription [GO:0006355]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; synapse [GO:0045202]
|
ATP binding [GO:0005524]; histone H3S10 kinase activity [GO:0035175]; histone H3S28 kinase activity [GO:0044022]; magnesium ion binding [GO:0000287]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; ribosomal protein S6 kinase activity [GO:0004711]
|
PF00069;PF00433;
|
1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family, S6 kinase subfamily
|
PTM: Ser-343 and Thr-568 phosphorylation is required for kinase activity. Ser-343 and Ser-196 are autophosphorylated by the C-terminal kinase domain, and their phosphorylation is essential for the catalytic activity of the N-terminal kinase domain. Phosphorylated at Ser-343, Thr-568 and Thr-687 by MAPK1/ERK2, MAPK3/ERK1 and MAPK14/p38-alpha. Autophosphorylated at Ser-737 and Ser-745 by the N-terminal kinase domain (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11035004, ECO:0000269|PubMed:9792677}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:9792677}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:9792677};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase that is required for the mitogen or stress-induced phosphorylation of the transcription factors CREB1 and ATF1 and for the regulation of the transcription factor RELA, and that contributes to gene activation by histone phosphorylation and functions in the regulation of inflammatory genes. Phosphorylates CREB1 and ATF1 in response to mitogenic or stress stimuli such as UV-C irradiation, epidermal growth factor (EGF) and anisomycin. Plays an essential role in the control of RELA transcriptional activity in response to TNF. Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and EGF, which results in the transcriptional activation of several immediate early genes, including proto-oncogenes c-fos/FOS and c-jun/JUN. May also phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14). In lipopolysaccharide-stimulated primary macrophages, acts downstream of the Toll-like receptor TLR4 to limit the production of pro-inflammatory cytokines. Functions probably by inducing transcription of the MAP kinase phosphatase DUSP1 and the anti-inflammatory cytokine interleukin 10 (IL10), via CREB1 and ATF1 transcription factors. {ECO:0000269|PubMed:11035004, ECO:0000269|PubMed:12773393, ECO:0000269|PubMed:9792677}.
|
Homo sapiens (Human)
|
O75677
|
RFPL1_HUMAN
|
MKRLSLVTTNRLSPHGNFLPLCTFPLAVDMAALFQEASSCPVCSDYLEKPMSLECGCAVCFKCINSLQKEPHGEDLLCCCCSMVSQKNKIRPSWQLERLASHIKELEPKLKKILQMNPRMRKFQVDMTLDADTANNFLLISDDLRSVRSGCITQNRQDLAERFDVSICILGSPRFTCGRHYWEVDVGTSTEWDLGVCRESVHRKGRIHLTTERGFWTVSLRDGSRLSASTVPLTFLFVDRKLQRVGIFLDMGMQNVSFFDAEGGSHVYTFRSVSAEEPLHLFFAPPSPPNGDKSVLSICPVINPGTTDAPVHPGEAK
| null | null |
cell cycle [GO:0007049]; innate immune response [GO:0045087]; negative regulation of cell division [GO:0051782]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of G2/M transition of mitotic cell cycle [GO:0010972]; negative regulation of mitotic cell cycle [GO:0045930]; positive regulation of apoptotic process [GO:0043065]; positive regulation of autophagy [GO:0010508]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis [GO:2001272]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; protein polyubiquitination [GO:0000209]; regulation of protein localization [GO:0032880]; regulation of viral entry into host cell [GO:0046596]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]
|
metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; ubiquitin protein ligase activity [GO:0061630]
|
PF13765;PF11002;PF00622;PF15227;
|
2.60.120.920;3.30.40.10;
| null |
PTM: Phosphorylated by PKC and CDK1 (PubMed:20725088). The antiproliferative effect seems to be positively regulated by PKC phosphorylation and negatively by CDK1 phosphorylation (PubMed:20725088). {ECO:0000269|PubMed:20725088}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20725088}. Nucleus {ECO:0000269|PubMed:20725088}. Note=A higher concentration is observed in the cytoplasm compared to the nucleus. {ECO:0000269|PubMed:20725088}.
| null | null | null | null | null |
FUNCTION: Negatively regulates the G2-M phase transition, possibly by promoting cyclin B1/CCNB1 and CDK1 proteasomal degradation and thereby preventing their accumulation during interphase. {ECO:0000269|PubMed:20725088}.
|
Homo sapiens (Human)
|
O75678
|
RFPL2_HUMAN
|
MEVAELGFPETAVSQSRICLCAVLCGHWDFADMMVIRSLSLIRLEGVEGRDPVGGGNLTNKRPSCAPSPQDLSAQWKQLEDRGASSRRVDMAALFQEASSCPVCSDYLEKPMSLECGCAVCLKCINSLQKEPHGEDLLCCCSSMVSRKNKIRRNRQLERLASHIKELEPKLKKILQMNPRMRKFQVDMTLDANTANNFLLISDDLRSVRSGRIRQNRQDLAERFDVSVCILGSPRFTCGRHCWEVDVGTSTEWDLGVCRESVHRKGRIQLTTELGFWTVSLRDGGRLSATTVPLTFLFVDRKLQRVGIFLDMGMQNVSFFDAESGSHVYTFRSVSAEEPLRPFLAPSVPPNGDQGVLSICPLMNSGTTDAPVRPGEAK
| null | null |
innate immune response [GO:0045087]; positive regulation of autophagy [GO:0010508]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; protein polyubiquitination [GO:0000209]; regulation of gene expression [GO:0010468]; regulation of protein localization [GO:0032880]; regulation of viral entry into host cell [GO:0046596]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]
|
metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; ubiquitin protein ligase activity [GO:0061630]
|
PF13765;PF11002;PF00622;PF15227;
|
2.60.120.920;3.30.40.10;
| null | null | null | null | null | null | null | null | null |
Homo sapiens (Human)
|
O75679
|
RFPL3_HUMAN
|
MKRLSLVTTNRLSPQGNFLPLCTFPLAVDMAALFQEASSCPVCSDYLEKPMSLECGCTVCLKCINSLQKEPHGEDLLCCCCSMVSQRNKIRPNRQLERLVSHIKELEPKLKKILQMNPRMRKFQVDMTLDADTANNFLLISDDLRSVRSGLITQNRQDLAERFDVSVCILGSPRFTCGRHYWEVDVGTSTEWDLGVCRESVHCKGKIQLTTELGFWTVSLRDGSRLSASTVPLTFLLVDRKLQRVGIFLDMGMQNVSFFDAESGSHVYTFRSVSAEEPLRPFLAPSIPPNGDQGVLSICPLMNSGTTDAPVRPGEAK
| null | null |
innate immune response [GO:0045087]; positive regulation of autophagy [GO:0010508]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; protein polyubiquitination [GO:0000209]; regulation of gene expression [GO:0010468]; regulation of protein localization [GO:0032880]; regulation of viral entry into host cell [GO:0046596]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]
|
metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; ubiquitin protein ligase activity [GO:0061630]
|
PF13765;PF11002;PF00622;PF15227;
|
2.60.120.920;3.30.40.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25107902}. Nucleus {ECO:0000269|PubMed:25107902}. Note=A higher concentration of RFPL3 is observed in the cytoplasm compared to the nucleus. {ECO:0000269|PubMed:25107902}.
| null | null | null | null | null |
FUNCTION: (Microbial infection) Stimulates the activity of Human Immunodeficiency Virus 1/HIV-1 pre-integration complex. {ECO:0000269|PubMed:25107902}.
|
Homo sapiens (Human)
|
O75683
|
SURF6_HUMAN
|
MASLLAKDAYLQSLAKKICSHSAPEQQARTRAGKTQGSETAGPPKKKRKKTQKKFRKREEKAAEHKAKSLGEKSPAASGARRPEAAKEEAAWASSSAGNPADGLATEPESVFALDVLRQRLHEKIQEARGQGSAKELSPAALEKRRRRKQERDRKKRKRKELRAKEKARKAEEATEAQEVVEATPEGACTEPREPPGLIFNKVEVSEDEPASKAQRRKEKRQRVKGNLTPLTGRNYRQLLERLQARQSRLDELRGQDEGKAQELEAKMKWTNLLYKAEGVKIRDDERLLQEALKRKEKRRAQRQRRWEKRTAGVVEKMQQRQDRRRQNLRRKKAARAERRLLRARKKGRILPQDLERAGLV
| null | null |
ribosomal large subunit biogenesis [GO:0042273]; ribosomal small subunit biogenesis [GO:0042274]
|
chromosome [GO:0005694]; granular component [GO:0001652]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]
|
DNA binding [GO:0003677]; molecular condensate scaffold activity [GO:0140693]; RNA binding [GO:0003723]
|
PF04935;
| null |
SURF6 family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Granular component of the nucleolus. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Binds to both DNA and RNA in vitro, with a stronger binding capacity for RNA. May represent a nucleolar constitutive protein involved in ribosomal biosynthesis or assembly (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O75688
|
PPM1B_HUMAN
|
MGAFLDKPKTEKHNAHGAGNGLRYGLSSMQGWRVEMEDAHTAVVGIPHGLEDWSFFAVYDGHAGSRVANYCSTHLLEHITTNEDFRAAGKSGSALELSVENVKNGIRTGFLKIDEYMRNFSDLRNGMDRSGSTAVGVMISPKHIYFINCGDSRAVLYRNGQVCFSTQDHKPCNPREKERIQNAGGSVMIQRVNGSLAVSRALGDYDYKCVDGKGPTEQLVSPEPEVYEILRAEEDEFIILACDGIWDVMSNEELCEYVKSRLEVSDDLENVCNWVVDTCLHKGSRDNMSIVLVCFSNAPKVSDEAVKKDSELDKHLESRVEEIMEKSGEEGMPDLAHVMRILSAENIPNLPPGGGLAGKRNVIEAVYSRLNPHRESDGASDEAEESGSQGKLVEALRQMRINHRGNYRQLLEEMLTSYRLAKVEGEESPAEPAATATSSNSDAGNPVTMQESHTESESGLAELDSSNEDAGTKMSGEKI
|
3.1.3.16
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
|
N-terminal protein myristoylation [GO:0006499]; negative regulation of canonical NF-kappaB signal transduction [GO:0043124]; negative regulation of defense response to virus [GO:0050687]; negative regulation of interferon-beta production [GO:0032688]; negative regulation of non-canonical NF-kappaB signal transduction [GO:1901223]; peptidyl-threonine dephosphorylation [GO:0035970]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; protein dephosphorylation [GO:0006470]
|
cytosol [GO:0005829]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]
|
magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]
|
PF00481;PF07830;
|
1.10.10.430;3.60.40.10;
|
PP2C family
|
PTM: Isgylation negatively regulates its activity. {ECO:0000269|PubMed:16872604}.; PTM: N-myristoylation is essential for the recognition of its substrates for dephosphorylation. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22781750}. Membrane {ECO:0000250|UniProtKB:P36993}; Lipid-anchor {ECO:0000250|UniProtKB:P36993}. Note=Weakly associates at the membrane and N-myristoylation mediates the membrane localization. {ECO:0000250|UniProtKB:P36993}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16;
| null | null | null | null |
FUNCTION: Enzyme with a broad specificity. Dephosphorylates CDK2 and CDK6 in vitro. Dephosphorylates PRKAA1 and PRKAA2. Inhibits TBK1-mediated antiviral signaling by dephosphorylating it at 'Ser-172'. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB. {ECO:0000269|PubMed:18930133, ECO:0000269|PubMed:22750291}.
|
Homo sapiens (Human)
|
O75689
|
ADAP1_HUMAN
|
MAKERRRAVLELLQRPGNARCADCGAPDPDWASYTLGVFICLSCSGIHRNIPQVSKVKSVRLDAWEEAQVEFMASHGNDAARARFESKVPSFYYRPTPSDCQLLREQWIRAKYERQEFIYPEKQEPYSAGYREGFLWKRGRDNGQFLSRKFVLTEREGALKYFNRNDAKEPKAVMKIEHLNATFQPAKIGHPHGLQVTYLKDNSTRNIFIYHEDGKEIVDWFNALRAARFHYLQVAFPGAGDADLVPKLSRNYLKEGYMEKTGPKQTEGFRKRWFTMDDRRLMYFKDPLDAFARGEVFIGSKESGYTVLHGFPPSTQGHHWPHGITIVTPDRKFLFACETESDQREWVAAFQKAVDRPMLPQEYAVEAHFKHKP
| null | null |
cell surface receptor signaling pathway [GO:0007166]; regulation of GTPase activity [GO:0043087]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
GTPase activator activity [GO:0005096]; inositol 1,3,4,5 tetrakisphosphate binding [GO:0043533]; metal ion binding [GO:0046872]; phosphatidylinositol bisphosphate binding [GO:1902936]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]
|
PF01412;PF00169;
|
1.10.220.150;2.30.29.30;
| null |
PTM: Phosphorylated by PRKCA, PRKCI, PRKCZ and PRKD1 in vitro. {ECO:0000269|PubMed:12893243}.
|
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Recruited to the plasma membrane upon epidermal growth factor-dependent activation of phosphatidylinositol 4,5-diphosphate (PtdInsP2) 3-kinase.
| null | null | null | null | null |
FUNCTION: GTPase-activating protein for the ADP ribosylation factor family (Probable). Binds phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and inositol 1,3,4,5-tetrakisphosphate (InsP4). {ECO:0000269|PubMed:10448098, ECO:0000303|PubMed:10333475, ECO:0000305}.
|
Homo sapiens (Human)
|
O75691
|
UTP20_HUMAN
|
MKTKPVSHKTENTYRFLTFAERLGNVNIDIIHRIDRTASYEEEVETYFFEGLLKWRELNLTEHFGKFYKEVIDKCQSFNQLVYHQNEIVQSLKTHLQVKNSFAYQPLLDLVVQLARDLQMDFYPHFPEFFLTITSILETQDTELLEWAFTSLSYLYKYLWRLMVKDMSSIYSMYSTLLAHKKLHIRNFAAESFTFLMRKVSDKNALFNLMFLDLDKHPEKVEGVGQLLFEMCKGVRNMFHSCTGQAVKLILRKLGPVTETETQLPWMLIGETLKNMVKSTVSYISKEHFGTFFECLQESLLDLHTKVTKTNCCESSEQIKRLLETYLILVKHGSGTKIPTPADVCKVLSQTLQVASLSTSCWETLLDVISALILGENVSLPETLIKETIEKIFESRFEKRLIFSFSEVMFAMKQFEQLFLPSFLSYIVNCFLIDDAVVKDEALAILAKLILNKAAPPTAGSMAIEKYPLVFSPQMVGFYIKQKKTRSKGRNEQFPVLDHLLSIIKLPPNKDTTYLSQSWAALVVLPHIRPLEKEKVIPLVTGFIEALFMTVDKGSFGKGNLFVLCQAVNTLLSLEESSELLHLVPVERVKNLVLTFPLEPSVLLLTDLYYQRLALCGCKGPLSQEALMELFPKLQANISTGVSKIRLLTIRILNHFDVQLPESMEDDGLSERQSVFAILRQAELVPATVNDYREKLLHLRKLRHDVVQTAVPDGPLQEVPLRYLLGMLYINFSALWDPVIELISSHAHEMENKQFWKVYYEHLEKAATHAEKELQNDMTDEKSVGDESWEQTQEGDVGALYHEQLALKTDCQERLDHTNFRFLLWRALTKFPERVEPRSRELSPLFLRFINNEYYPADLQVAPTQDLRRKGKGMVAEEIEEEPAAGDDEELEEEAVPQDESSQKKKTRRAAAKQLIAHLQVFSKFSNPRALYLESKLYELYLQLLLHQDQMVQKITLDCIMTYKHPHVLPYRENLQRLLEDRSFKEEIVHFSISEDNAVVKTAHRADLFPILMRILYGRMKNKTGSKTQGKSASGTRMAIVLRFLAGTQPEEIQIFLDLLFEPVRHFKNGECHSAVIQAVEDLDLSKVLPLGRQHGILNSLEIVLKNISHLISAYLPKILQILLCMTATVSHILDQREKIQLRFINPLKNLRRLGIKMVTDIFLDWESYQFRTEEIDAVFHGAVWPQISRLGSESQYSPTPLLKLISIWSRNARYFPLLAKQKPGHPECDILTNVFAILSAKNLSDATASIVMDIVDDLLNLPDFEPTETVLNLLVTGCVYPGIAENIGESITIGGRLILPHVPAILQYLSKTTISAEKVKKKKNRAQVSKELGILSKISKFMKDKEQSSVLITLLLPFLHRGNIAEDTEVDILVTVQNLLKHCVDPTSFLKPIAKLFSVIKNKLSRKLLCTVFETLSDFESGLKYITDVVKLNAFDQRHLDDINFDVRFETFQTITSYIKEMQIVDVNYLIPVMHNCFYNLELGDMSLSDNASMCLMSIIKKLAALNVTEKDYREIIHRSLLEKLRKGLKSQTESIQQDYTTILSCLIQTFPNQLEFKDLVQLTHYHDPEMDFFENMKHIQIHRRARALKKLAKQLMEGKVVLSSKSLQNYIMPYAMTPIFDEKMLKHENITTAATEIIGAICKHLSWSAYMYYLKHFIHVLQTGQINQKLGVSLLVIVLEAFHFDHKTLEEQMGKIENEENAIEAIELPEPEAMELERVDEEEKEYTCKSLSDNGQPGTPDPADSGGTSAKESECITKPVSFLPQNKEEIERTIKNIQGTITGDILPRLHKCLASTTKREEEHKLVKSKVVNDEEVVRVPLAFAMVKLMQSLPQEVMEANLPSILLKVCALLKNRAQEIRDIARSTLAKIIEDLGVHFLLYVLKELQTTLVRGYQVHVLTFTVHMLLQGLTNKLQVGDLDSCLDIMIEIFNHELFGAVAEEKEVKQILSKVMEARRSKSYDSYEILGKFVGKDQVTKLILPLKEILQNTTSLKLARKVHETLRRITVGLIVNQEMTAESILLLSYGLISENLPLLTEKEKNPVAPAPDPRLPPQSCLLLPPTPVRGGQKAVVSRKTNMHIFIESGLRLLHLSLKTSKIKSSGECVLEMLDPFVSLLIDCLGSMDVKVITGALQCLIWVLRFPLPSIETKAEQLTKHLFLLLKDYAKLGAARGQNFHLVVNCFKCVTILVKKVKSYQITEKQLQVLLAYAEEDIYDTSRQATAFGLLKAILSRKLLVPEIDEVMRKVSKLAVSAQSEPARVQCRQVFLKYILDYPLGDKLRPNLEFMLAQLNYEHETGRESTLEMIAYLFDTFPQGLLHENCGMFFIPLCLMTINDDSATCKKMASMTIKSLLGKISLEKKDWLFDMVTTWFGAKKRLNRQLAALICGLFVESEGVDFEKRLGTVLPVIEKEIDPENFKDIMEETEEKAADRLLFSFLTLITKLIKECNIIQFTKPAETLSKIWSHVHSHLRHPHNWVWLTAAQIFGLLFASCQPEELIQKWNTKKTKKHLPEPVAIKFLASDLDQKMKSISLASCHQLHSKFLDQSLGEQVVKNLLFAAKVLYLLELYCEDKQSKIKEDLEEQEALEDGVACADEKAESDGEEKEEVKEELGRPATLLWLIQKLSRIAKLEAAYSPRNPLKRTCIFKFLGAVAMDLGIDKVKPYLPMIIAPLFRELNSTYSEQDPLLKNLSQEIIELLKKLVGLESFSLAFASVQKQANEKRALRKKRKALEFVTNPDIAAKKKMKKHKNKSEAKKRKIEFLRPGYKAKRQKSHSLKDLAMVE
| null | null |
endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000480]; endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000447]; endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000472]; negative regulation of cell population proliferation [GO:0008285]; ribosomal small subunit biogenesis [GO:0042274]; rRNA processing [GO:0006364]
|
90S preribosome [GO:0030686]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; preribosome, small subunit precursor [GO:0030688]; small-subunit processome [GO:0032040]
|
RNA binding [GO:0003723]
|
PF20416;PF07539;
| null |
UTP20 family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11790298, ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:16458307, ECO:0000269|PubMed:34516797}. Note=Colocalizes with NCL in the nucleolus.
| null | null | null | null | null |
FUNCTION: Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome. Involved in 18S pre-rRNA processing. Associates with U3 snoRNA. {ECO:0000269|PubMed:17498821, ECO:0000269|PubMed:34516797}.
|
Homo sapiens (Human)
|
O75694
|
NU155_HUMAN
|
MPSSLLGAAMPASTSAAALQEALENAGRLIDRQLQEDRMYPDLSELLMVSAPNNPTVSGMSDMDYPLQGPGLLSVPNLPEISSIRRVPLPPELVEQFGHMQCNCMMGVFPPISRAWLTIDSDIFMWNYEDGGDLAYFDGLSETILAVGLVKPKAGIFQPHVRHLLVLATPVDIVILGLSYANLQTGSGVLNDSLSGGMQLLPDPLYSLPTDNTYLLTITSTDNGRIFLAGKDGCLYEVAYQAEAGWFSQRCRKINHSKSSLSFLVPSLLQFTFSEDDPILQIAIDNSRNILYTRSEKGVIQVYDLGQDGQGMSRVASVSQNAIVSAAGNIARTIDRSVFKPIVQIAVIENSESLDCQLLAVTHAGVRLYFSTCPFRQPLARPNTLTLVHVRLPPGFSASSTVEKPSKVHRALYSKGILLMAASENEDNDILWCVNHDTFPFQKPMMETQMTAGVDGHSWALSAIDELKVDKIITPLNKDHIPITDSPVVVQQHMLPPKKFVLLSAQGSLMFHKLRPVDQLRHLLVSNVGGDGEEIERFFKLHQEDQACATCLILACSTAACDREVSAWATRAFFRYGGEAQMRFPTTLPPPSNVGPILGSPVYSSSPVPSGSPYPNPSFLGTPSHGIQPPAMSTPVCALGNPATQATNMSCVTGPEIVYSGKHNGICIYFSRIMGNIWDASLVVERIFKSGNREITAIESSVPCQLLESVLQELKGLQEFLDRNSQFAGGPLGNPNTTAKVQQRLIGFMRPENGNPQQMQQELQRKFHEAQLSEKISLQAIQQLVRKSYQALALWKLLCEHQFTIIVAELQKELQEQLKITTFKDLVIRDKELTGALIASLINCYIRDNAAVDGISLHLQDICPLLYSTDDAICSKANELLQRSRQVQNKTEKERMLRESLKEYQKISNQVDLSNVCAQYRQVRFYEGVVELSLTAAEKKDPQGLGLHFYKHGEPEEDIVGLQAFQERLNSYKCITDTLQELVNQSKAAPQSPSVPKKPGPPVLSSDPNMLSNEEAGHHFEQMLKLSQRSKDELFSIALYNWLIQVDLADKLLQVASPFLEPHLVRMAKVDQNRVRYMDLLWRYYEKNRSFSNAARVLSRLADMHSTEISLQQRLEYIARAILSAKSSTAISSIAADGEFLHELEEKMEVARIQLQIQETLQRQYSHHSSVQDAVSQLDSELMDITKLYGEFADPFKLAECKLAIIHCAGYSDPILVQTLWQDIIEKELSDSVTLSSSDRMHALSLKIVLLGKIYAGTPRFFPLDFIVQFLEQQVCTLNWDVGFVIQTMNEIGVPLPRLLEVYDQLFKSRDPFWNRMKKPLHLLDCIHVLLIRYVENPSQVLNCERRRFTNLCLDAVCGYLVELQSMSSSVAVQAITGNFKSLQAKLERLH
| null | null |
atrial cardiac muscle cell action potential [GO:0086014]; miRNA processing [GO:0035196]; mRNA export from nucleus [GO:0006406]; nuclear envelope organization [GO:0006998]; nucleocytoplasmic transport [GO:0006913]; protein import into nucleus [GO:0006606]; protein localization to nuclear inner membrane [GO:0036228]; RNA export from nucleus [GO:0006405]; transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery [GO:0000972]
|
cytosol [GO:0005829]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nuclear pore inner ring [GO:0044611]
|
structural constituent of nuclear pore [GO:0017056]
|
PF08801;
|
1.20.58.1780;1.20.120.1880;1.25.40.440;1.25.40.450;
|
Non-repetitive/WGA-negative nucleoporin family
|
PTM: Phosphorylated. Phosphorylation and dephosphorylation may be important for the function of NUP155 and may play a role in the reversible disassembly of the nuclear pore complex during mitosis (By similarity). {ECO:0000250}.; PTM: Disulfide-linked to NUP62. The inner channel of the NPC has a different redox environment from the cytoplasm and allows the formation of interchain disulfide bonds between some nucleoporins, the significant increase of these linkages upon oxidative stress reduces the permeability of the NPC (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P37199}. Nucleus membrane {ECO:0000250|UniProtKB:P37199}; Peripheral membrane protein {ECO:0000250|UniProtKB:P37199}; Cytoplasmic side {ECO:0000250|UniProtKB:P37199}. Nucleus membrane {ECO:0000250|UniProtKB:P37199}; Peripheral membrane protein {ECO:0000250|UniProtKB:P37199}; Nucleoplasmic side {ECO:0000250|UniProtKB:P37199}. Note=In mitosis, assumes a diffuse cytoplasmic distribution probably as a monomer, before reversing back into a punctate nuclear surface localization at the end of mitosis. {ECO:0000250|UniProtKB:P37199}.
| null | null | null | null | null |
FUNCTION: Essential component of nuclear pore complex. Could be essessential for embryogenesis. Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport. {ECO:0000250|UniProtKB:Q99P88}.
|
Homo sapiens (Human)
|
O75695
|
XRP2_HUMAN
|
MGCFFSKRRKADKESRPENEEERPKQYSWDQREKVDPKDYMFSGLKDETVGRLPGTVAGQQFLIQDCENCNIYIFDHSATVTIDDCTNCIIFLGPVKGSVFFRNCRDCKCTLACQQFRVRDCRKLEVFLCCATQPIIESSSNIKFGCFQWYYPELAFQFKDAGLSIFNNTWSNIHDFTPVSGELNWSLLPEDAVVQDYVPIPTTEELKAVRVSTEANRSIVPISRGQRQKSSDESCLVVLFAGDYTIANARKLIDEMVGKGFFLVQTKEVSMKAEDAQRVFREKAPDFLPLLNKGPVIALEFNGDGAVEVCQLIVNEIFNGTKMFVSESKETASGDVDSFYNFADIQMGI
| null | null |
cilium assembly [GO:0060271]; post-Golgi vesicle-mediated transport [GO:0006892]; protein folding [GO:0006457]; protein transport [GO:0015031]; visual perception [GO:0007601]
|
centriole [GO:0005814]; ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; periciliary membrane compartment [GO:1990075]; plasma membrane [GO:0005886]
|
GTP binding [GO:0005525]; GTPase activator activity [GO:0005096]; magnesium ion binding [GO:0000287]; unfolded protein binding [GO:0051082]
|
PF07986;
|
2.160.20.70;3.30.70.141;
|
TBCC family
|
PTM: Myristoylated on Gly-2; which may be required for membrane targeting. {ECO:0000305|PubMed:10942419}.; PTM: Palmitoylated on Cys-3; which may be required for plasma membrane targeting (Probable). Mutation of Cys-3 targets the protein to internal membranes. {ECO:0000269|PubMed:10942419, ECO:0000305}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10942419, ECO:0000269|PubMed:12417528}; Lipid-anchor {ECO:0000269|PubMed:10942419}; Cytoplasmic side {ECO:0000269|PubMed:10942419}. Cell projection, cilium {ECO:0000269|PubMed:20106869}. Note=Detected predominantly at the plasma membrane of rod and cone photoreceptors. Not detected in the nucleus. {ECO:0000269|PubMed:12417528}.
| null | null | null | null | null |
FUNCTION: Acts as a GTPase-activating protein (GAP) involved in trafficking between the Golgi and the ciliary membrane. Involved in localization of proteins, such as NPHP3, to the cilium membrane by inducing hydrolysis of GTP ARL3, leading to the release of UNC119 (or UNC119B). Acts as a GTPase-activating protein (GAP) for tubulin in concert with tubulin-specific chaperone C, but does not enhance tubulin heterodimerization. Acts as a guanine nucleotide dissociation inhibitor towards ADP-ribosylation factor-like proteins. {ECO:0000269|PubMed:11847227, ECO:0000269|PubMed:18376416, ECO:0000269|PubMed:20106869, ECO:0000269|PubMed:22085962}.
|
Homo sapiens (Human)
|
O75712
|
CXB3_HUMAN
|
MDWKTLQALLSGVNKYSTAFGRIWLSVVFVFRVLVYVVAAERVWGDEQKDFDCNTKQPGCTNVCYDNYFPISNIRLWALQLIFVTCPSLLVILHVAYREERERRHRQKHGDQCAKLYDNAGKKHGGLWWTYLFSLIFKLIIEFLFLYLLHTLWHGFNMPRLVQCANVAPCPNIVDCYIARPTEKKIFTYFMVGASAVCIVLTICELCYLICHRVLRGLHKDKPRGGCSPSSSASRASTCRCHHKLVEAGEVDPDPGNNKLQASAPNLTPI
| null | null |
cell-cell signaling [GO:0007267]; cellular response to retinoic acid [GO:0071300]; in utero embryonic development [GO:0001701]; placenta development [GO:0001890]; skin development [GO:0043588]; spermatogenesis [GO:0007283]
|
cell junction [GO:0030054]; connexin complex [GO:0005922]; cytoplasm [GO:0005737]; gap junction [GO:0005921]; intracellular membrane-bounded organelle [GO:0043231]
|
gap junction channel activity [GO:0005243]
|
PF00029;
|
1.20.1440.80;
|
Connexin family, Beta-type (group I) subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction.
| null | null | null | null | null |
FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
|
Homo sapiens (Human)
|
O75716
|
STK16_HUMAN
|
MGHALCVCSRGTVIIDNKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERGAKHEAWLLLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGSRQALTLQDWAAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEALQPPAPGQHTTQI
|
2.7.10.2; 2.7.11.1
| null |
cellular response to transforming growth factor beta stimulus [GO:0071560]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein autophosphorylation [GO:0046777]; regulation of vacuole fusion, non-autophagic [GO:0032889]; vacuolar protein processing [GO:0006624]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi-associated vesicle [GO:0005798]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
|
PTM: Mainly autophosphorylated on serine/threonine residues. Also autophosphorylated on Tyr-198. {ECO:0000269|PubMed:18184589}.; PTM: It is uncertain whether palmitoylation is on Cys-6 and/or Cys-8. {ECO:0000269|PubMed:10364453}.
|
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Associates with Golgi and Golgi-derived vesicles. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};
| null | null | null | null |
FUNCTION: Membrane-associated protein kinase that phosphorylates on serine and threonine residues. In vitro substrates include DRG1, ENO1 and EIF4EBP1. Also autophosphorylates. May be involved in secretory vesicle trafficking or intracellular signaling. May have a role in regulating stromal-epithelial interactions that occur during ductal morphogenesis in the mammary gland. May be involved in TGF-beta signaling. Able to autophosphorylate on Tyr residue; it is however unclear whether it has tyrosine-protein kinase toward other proteins. {ECO:0000269|PubMed:10364453}.
|
Homo sapiens (Human)
|
O75717
|
WDHD1_HUMAN
|
MPATRKPMRYGHTEGHTEVCFDDSGSFIVTCGSDGDVRIWEDLDDDDPKFINVGEKAYSCALKSGKLVTAVSNNTIQVHTFPEGVPDGILTRFTTNANHVVFNGDGTKIAAGSSDFLVKIVDVMDSSQQKTFRGHDAPVLSLSFDPKDIFLASASCDGSVRVWQISDQTCAISWPLLQKCNDVINAKSICRLAWQPKSGKLLAIPVEKSVKLYRRESWSHQFDLSDNFISQTLNIVTWSPCGQYLAAGSINGLIIVWNVETKDCMERVKHEKGYAICGLAWHPTCGRISYTDAEGNLGLLENVCDPSGKTSSSKVSSRVEKDYNDLFDGDDMSNAGDFLNDNAVEIPSFSKGIINDDEDDEDLMMASGRPRQRSHILEDDENSVDISMLKTGSSLLKEEEEDGQEGSIHNLPLVTSQRPFYDGPMPTPRQKPFQSGSTPLHLTHRFMVWNSIGIIRCYNDEQDNAIDVEFHDTSIHHATHLSNTLNYTIADLSHEAILLACESTDELASKLHCLHFSSWDSSKEWIIDLPQNEDIEAICLGQGWAAAATSALLLRLFTIGGVQKEVFSLAGPVVSMAGHGEQLFIVYHRGTGFDGDQCLGVQLLELGKKKKQILHGDPLPLTRKSYLAWIGFSAEGTPCYVDSEGIVRMLNRGLGNTWTPICNTREHCKGKSDHYWVVGIHENPQQLRCIPCKGSRFPPTLPRPAVAILSFKLPYCQIATEKGQMEEQFWRSVIFHNHLDYLAKNGYEYEESTKNQATKEQQELLMKMLALSCKLEREFRCVELADLMTQNAVNLAIKYASRSRKLILAQKLSELAVEKAAELTATQVEEEEEEEDFRKKLNAGYSNTATEWSQPRFRNQVEEDAEDSGEADDEEKPEIHKPGQNSFSKSTNSSDVSAKSGAVTFSSQGRVNPFKVSASSKEPAMSMNSARSTNILDNMGKSSKKSTALSRTTNNEKSPIIKPLIPKPKPKQASAASYFQKRNSQTNKTEEVKEENLKNVLSETPAICPPQNTENQRPKTGFQMWLEENRSNILSDNPDFSDEADIIKEGMIRFRVLSTEERKVWANKAKGETASEGTEAKKRKRVVDESDETENQEEKAKENLNLSKKQKPLDFSTNQKLSAFAFKQE
| null | null |
DNA repair [GO:0006281]; DNA-templated DNA replication [GO:0006261]; mitotic cell cycle [GO:0000278]
|
cytoplasm [GO:0005737]; nuclear replication fork [GO:0043596]; nucleoplasm [GO:0005654]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]
|
PF12894;PF20946;PF12341;PF00400;
|
1.10.30.10;2.130.10.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000305|PubMed:34694004, ECO:0000305|PubMed:35585232}.
| null | null | null | null | null |
FUNCTION: Core replisome component that acts as a replication initiation factor. Binds directly to the CMG complex and functions as a hub to recruit additional proteins to the replication fork. {ECO:0000269|PubMed:19805216, ECO:0000269|PubMed:34694004, ECO:0000269|PubMed:35585232}.
|
Homo sapiens (Human)
|
O75718
|
CRTAP_HUMAN
|
MEPGRRGAAALLALLCVACALRAGRAQYERYSFRSFPRDELMPLESAYRHALDKYSGEHWAESVGYLEISLRLHRLLRDSEAFCHRNCSAAPQPEPAAGLASYPELRLFGGLLRRAHCLKRCKQGLPAFRQSQPSREVLADFQRREPYKFLQFAYFKANNLPKAIAAAHTFLLKHPDDEMMKRNMAYYKSLPGAEDYIKDLETKSYESLFIRAVRAYNGENWRTSITDMELALPDFFKAFYECLAACEGSREIKDFKDFYLSIADHYVEVLECKIQCEENLTPVIGGYPVEKFVATMYHYLQFAYYKLNDLKNAAPCAVSYLLFDQNDKVMQQNLVYYQYHRDTWGLSDEHFQPRPEAVQFFNVTTLQKELYDFAKENIMDDDEGEVVEYVDDLLELEETS
| null | null |
chaperone-mediated protein folding [GO:0061077]; collagen fibril organization [GO:0030199]; negative regulation of post-translational protein modification [GO:1901874]; protein stabilization [GO:0050821]; spermatogenesis [GO:0007283]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; extracellular space [GO:0005615]; protein-containing complex [GO:0032991]
|
collagen binding [GO:0005518]
| null |
1.25.40.10;
|
Leprecan family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues. {ECO:0000269|PubMed:17055431}.
|
Homo sapiens (Human)
|
O75746
|
S2512_HUMAN
|
MAVKVQTTKRGDPHELRNIFLQYASTEVDGERYMTPEDFVQRYLGLYNDPNSNPKIVQLLAGVADQTKDGLISYQEFLAFESVLCAPDSMFIVAFQLFDKSGNGEVTFENVKEIFGQTIIHHHIPFNWDCEFIRLHFGHNRKKHLNYTEFTQFLQELQLEHARQAFALKDKSKSGMISGLDFSDIMVTIRSHMLTPFVEENLVSAAGGSISHQVSFSYFNAFNSLLNNMELVRKIYSTLAGTRKDVEVTKEEFAQSAIRYGQVTPLEIDILYQLADLYNASGRLTLADIERIAPLAEGALPYNLAELQRQQSPGLGRPIWLQIAESAYRFTLGSVAGAVGATAVYPIDLVKTRMQNQRGSGSVVGELMYKNSFDCFKKVLRYEGFFGLYRGLIPQLIGVAPEKAIKLTVNDFVRDKFTRRDGSVPLPAEVLAGGCAGGSQVIFTNPLEIVKIRLQVAGEITTGPRVSALNVLRDLGIFGLYKGAKACFLRDIPFSAIYFPVYAHCKLLLADENGHVGGLNLLAAGAMAGVPAASLVTPADVIKTRLQVAARAGQTTYSGVIDCFRKILREEGPSAFWKGTAARVFRSSPQFGVTLVTYELLQRWFYIDFGGLKPAGSEPTPKSRIADLPPANPDHIGGYRLATATFAGIENKFGLYLPKFKSPSVAVVQPKAAVAATQ
| null | null |
aspartate family amino acid metabolic process [GO:0009066]; aspartate transmembrane transport [GO:0015810]; gluconeogenesis [GO:0006094]; L-glutamate transmembrane transport [GO:0015813]; malate-aspartate shuttle [GO:0043490]; response to calcium ion [GO:0051592]
|
membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]
|
3-sulfino-L-alanine: proton, glutamate antiporter activity [GO:0000514]; acidic amino acid transmembrane transporter activity [GO:0015172]; aspartate:glutamate, proton antiporter activity [GO:0000515]; calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; L-aspartate transmembrane transporter activity [GO:0015183]; L-glutamate transmembrane transporter activity [GO:0005313]
|
PF00153;
|
1.10.238.10;1.50.40.10;
|
Mitochondrial carrier (TC 2.A.29) family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:11566871, ECO:0000269|PubMed:19641205, ECO:0000269|PubMed:24515575, ECO:0000269|PubMed:9722566}; Multi-pass membrane protein {ECO:0000269|PubMed:11566871}.
|
CATALYTIC ACTIVITY: Reaction=H(+)(out) + L-aspartate(in) + L-glutamate(out) = H(+)(in) + L-aspartate(out) + L-glutamate(in); Xref=Rhea:RHEA:70783, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; Evidence={ECO:0000269|PubMed:11566871, ECO:0000269|PubMed:19641205, ECO:0000269|PubMed:24515575}; CATALYTIC ACTIVITY: Reaction=3-sulfino-L-alanine(out) + H(+)(in) + L-glutamate(in) = 3-sulfino-L-alanine(in) + H(+)(out) + L-glutamate(out); Xref=Rhea:RHEA:70967, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:61085; Evidence={ECO:0000269|PubMed:11566871}; CATALYTIC ACTIVITY: Reaction=3-sulfino-L-alanine(out) + L-aspartate(in) = 3-sulfino-L-alanine(in) + L-aspartate(out); Xref=Rhea:RHEA:70975, ChEBI:CHEBI:29991, ChEBI:CHEBI:61085; Evidence={ECO:0000250|UniProtKB:F1LX07};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=24.7 umol/min/g enzyme toward L-aspartate {ECO:0000269|PubMed:11566871};
| null | null | null |
FUNCTION: Mitochondrial electrogenic aspartate/glutamate antiporter that favors efflux of aspartate and entry of glutamate and proton within the mitochondria as part of the malate-aspartate shuttle (PubMed:11566871, PubMed:19641205, PubMed:24515575). Also mediates the uptake of L-cysteinesulfinate by mitochondria in exchange of L-glutamate and proton. Can also exchange L-cysteinesulfinate with aspartate in their anionic form without any proton translocation (PubMed:11566871). {ECO:0000269|PubMed:11566871, ECO:0000269|PubMed:19641205, ECO:0000269|PubMed:24515575}.
|
Homo sapiens (Human)
|
O75747
|
P3C2G_HUMAN
|
MAYSWQTDPNPNESHEKQYEHQEFLFVNQPHSSSQVSLGFDQIVDEISGKIPHYESEIDENTFFVPTAPKWDSTGHSLNEAHQISLNEFTSKSRELSWHQVSKAPAIGFSPSVLPKPQNTNKECSWGSPIGKHHGADDSRFSILAPSFTSLDKINLEKELENENHNYHIGFESSIPPTNSSFSSDFMPKEENKRSGHVNIVEPSLMLLKGSLQPGMWESTWQKNIESIGCSIQLVEVPQSSNTSLASFCNKVKKIRERYHAADVNFNSGKIWSTTTAFPYQLFSKTKFNIHIFIDNSTQPLHFMPCANYLVKDLIAEILHFCTNDQLLPKDHILSVCGSEEFLQNDHCLGSHKMFQKDKSVIQLHLQKSREAPGKLSRKHEEDHSQFYLNQLLEFMHIWKVSRQCLLTLIRKYDFHLKYLLKTQENVYNIIEEVKKICSVLGCVETKQITDAVNELSLILQRKGENFYQSSETSAKGLIEKVTTELSTSIYQLINVYCNSFYADFQPVNVPRCTSYLNPGLPSHLSFTVYAAHNIPETWVHSYKAFSFTCWLTYAGKKLCQVRNYRNIPDKKLFFFLVNWNETINFPLEIKSLPRESMLTVKLFGIACATNNANLLAWTCLPLFPKEKSILGSMLFSMTLQSEPPVEMITPGVWDVSQPSPVTLQIDFPATGWEYMKPDSEENRSNLEEPLKECIKHIARLSQKQTPLLLSEEKKRYLWFYRFYCNNENCSLPLVLGSAPGWDERTVSEMHTILRRWTFSQPLEALGLLTSSFPDQEIRKVAVQQLDNLLNDELLEYLPQLVQAVKFEWNLESPLVQLLLHRSLQSIQVAHRLYWLLKNAENEAYFKSWYQKLLAALQFCAGKALNDEFSKEQKLIKILGDIGERVKSASDHQRQEVLKKEIGRLEEFFQDVNTCHLPLNPALCIKGIDHDACSYFTSNALPLKITFINANPMGKNISIIFKAGDDLRQDMLVLQLIQVMDNIWLQEGLDMQMIIYRCLSTGKDQGLVQMVPDAVTLAKIHRHSGLIGPLKENTIKKWFSQHNHLKADYEKALRNFFYSCAGWCVVTFILGVCDRHNDNIMLTKSGHMFHIDFGKFLGHAQTFGGIKRDRAPFIFTSEMEYFITEGGKNPQHFQDFVELCCRAYNIIRKHSQLLLNLLEMMLYAGLPELSGIQDLKYVYNNLRPQDTDLEATSHFTKKIKESLECFPVKLNNLIHTLAQMSAISPAKSTSQTFPQESCLLSTTRSIERATILGFSKKSSNLYLIQVTHSNNETSLTEKSFEQFSKLHSQLQKQFASLTLPEFPHWWHLPFTNSDHRRFRDLNHYMEQILNVSHEVTNSDCVLSFFLSEAVQQTVEESSPVYLGEKFPDKKPKVQLVISYEDVKLTILVKHMKNIHLPDGSAPSAHVEFYLLPYPSEVRRRKTKSVPKCTDPTYNEIVVYDEVTELQGHVLMLIVKSKTVFVGAINIRLCSVPLDKEKWYPLGNSII
|
2.7.1.137; 2.7.1.154
| null |
cell migration [GO:0016477]; chemotaxis [GO:0006935]; modulation by host of viral process [GO:0044788]; phosphatidylinositol-3-phosphate biosynthetic process [GO:0036092]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; phosphatidylinositol 3-kinase complex [GO:0005942]; plasma membrane [GO:0005886]
|
1-phosphatidylinositol-3-kinase activity [GO:0016303]; 1-phosphatidylinositol-4-phosphate 3-kinase activity [GO:0035005]; ATP binding [GO:0005524]; phosphatidylinositol binding [GO:0035091]; phosphatidylinositol kinase activity [GO:0052742]
|
PF00168;PF00454;PF00792;PF00794;PF00613;PF00787;
|
2.60.40.150;1.10.1070.11;1.25.40.70;3.30.1520.10;
|
PI3/PI4-kinase family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O70167}; Peripheral membrane protein {ECO:0000250|UniProtKB:O70167}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154; Evidence={ECO:0000250|UniProtKB:O70173}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18374; Evidence={ECO:0000250|UniProtKB:O70173}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.137; Evidence={ECO:0000250|UniProtKB:O70173}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710; Evidence={ECO:0000250|UniProtKB:O70173};
| null | null | null | null |
FUNCTION: Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers (By similarity). May play a role in SDF1A-stimulated chemotaxis (By similarity). {ECO:0000250|UniProtKB:O70167, ECO:0000250|UniProtKB:O70173}.
|
Homo sapiens (Human)
|
O75751
|
S22A3_HUMAN
|
MPSFDEALQRVGEFGRFQRRVFLLLCLTGVTFAFLFVGVVFLGTQPDHYWCRGPSAAALAERCGWSPEEEWNRTAPASRGPEPPERRGRCQRYLLEAANDSASATSALSCADPLAAFPNRSAPLVPCRGGWRYAQAHSTIVSEFDLVCVNAWMLDLTQAILNLGFLTGAFTLGYAADRYGRIVIYLLSCLGVGVTGVVVAFAPNFPVFVIFRFLQGVFGKGTWMTCYVIVTEIVGSKQRRIVGIVIQMFFTLGIIILPGIAYFIPNWQGIQLAITLPSFLFLLYYWVVPESPRWLITRKKGDKALQILRRIAKCNGKYLSSNYSEITVTDEEVSNPSFLDLVRTPQMRKCTLILMFAWFTSAVVYQGLVMRLGIIGGNLYIDFFISGVVELPGALLILLTIERLGRRLPFAASNIVAGVACLVTAFLPEGIAWLRTTVATLGRLGITMAFEIVYLVNSELYPTTLRNFGVSLCSGLCDFGGIIAPFLLFRLAAVWLELPLIIFGILASICGGLVMLLPETKGIALPETVDDVEKLGSPHSCKCGRNKKTPVSRSHL
| null | null |
cellular detoxification [GO:1990748]; dopamine transport [GO:0015872]; dopamine uptake [GO:0090494]; epinephrine transport [GO:0048241]; epinephrine uptake [GO:0051625]; histamine metabolic process [GO:0001692]; histamine transport [GO:0051608]; histamine uptake [GO:0051615]; monoamine transport [GO:0015844]; monoatomic ion transport [GO:0006811]; monocarboxylic acid transport [GO:0015718]; neurotransmitter transport [GO:0006836]; norepinephrine transport [GO:0015874]; norepinephrine uptake [GO:0051620]; organic anion transport [GO:0015711]; organic cation transport [GO:0015695]; purine-containing compound transmembrane transport [GO:0072530]; quaternary ammonium group transport [GO:0015697]; regulation of appetite [GO:0032098]; serotonin transport [GO:0006837]; serotonin uptake [GO:0051610]; spermidine transport [GO:0015848]; transport across blood-brain barrier [GO:0150104]; xenobiotic transport [GO:0042908]
|
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; endomembrane system [GO:0012505]; membrane [GO:0016020]; mitochondrial membrane [GO:0031966]; neuronal cell body [GO:0043025]; nuclear outer membrane [GO:0005640]; plasma membrane [GO:0005886]; presynapse [GO:0098793]
|
monoamine transmembrane transporter activity [GO:0008504]; neurotransmitter transmembrane transporter activity [GO:0005326]; organic anion transmembrane transporter activity [GO:0008514]; organic cation transmembrane transporter activity [GO:0015101]; quaternary ammonium group transmembrane transporter activity [GO:0015651]; spermidine transmembrane transporter activity [GO:0015606]; toxin transmembrane transporter activity [GO:0019534]
|
PF07690;
|
1.20.1250.20;
|
Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15817714, ECO:0000269|PubMed:20858707}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:15817714, ECO:0000269|PubMed:16263091}; Multi-pass membrane protein {ECO:0000305}. Basolateral cell membrane {ECO:0000269|PubMed:15817714}; Multi-pass membrane protein {ECO:0000305}. Mitochondrion membrane {ECO:0000250|UniProtKB:O88446}. Endomembrane system {ECO:0000250|UniProtKB:O88446}. Nucleus membrane {ECO:0000250|UniProtKB:O88446}. Nucleus outer membrane {ECO:0000250|UniProtKB:O88446}. Note=Localized to the apical/brush border membrane of enterocytes (PubMed:16263091). Localized to the luminal/apical membrane of ciliated epithelial cells in bronchi (PubMed:15817714). Localized to the basolateral membrane of intermediate cells in bronchi (PubMed:15817714). Localized to the entire plasma membrane of basal cells in bronchi (PubMed:15817714). {ECO:0000269|PubMed:15817714, ECO:0000269|PubMed:16263091}.
|
CATALYTIC ACTIVITY: Reaction=(R)-noradrenaline(out) = (R)-noradrenaline(in); Xref=Rhea:RHEA:73871, ChEBI:CHEBI:72587; Evidence={ECO:0000269|PubMed:10196521, ECO:0000269|PubMed:16581093, ECO:0000269|PubMed:20858707}; CATALYTIC ACTIVITY: Reaction=(R)-adrenaline(out) = (R)-adrenaline(in); Xref=Rhea:RHEA:73875, ChEBI:CHEBI:71406; Evidence={ECO:0000269|PubMed:10196521, ECO:0000269|PubMed:16581093, ECO:0000269|PubMed:20858707}; CATALYTIC ACTIVITY: Reaction=serotonin(out) = serotonin(in); Xref=Rhea:RHEA:73867, ChEBI:CHEBI:350546; Evidence={ECO:0000269|PubMed:10196521, ECO:0000269|PubMed:20858707}; CATALYTIC ACTIVITY: Reaction=dopamine(out) = dopamine(in); Xref=Rhea:RHEA:73863, ChEBI:CHEBI:59905; Evidence={ECO:0000269|PubMed:20858707}; CATALYTIC ACTIVITY: Reaction=histamine(out) = histamine(in); Xref=Rhea:RHEA:73879, ChEBI:CHEBI:58432; Evidence={ECO:0000269|PubMed:16581093, ECO:0000269|PubMed:20858707}; CATALYTIC ACTIVITY: Reaction=tyramine(in) = tyramine(out); Xref=Rhea:RHEA:74783, ChEBI:CHEBI:327995; Evidence={ECO:0000269|PubMed:10196521}; CATALYTIC ACTIVITY: Reaction=guanidine(out) = guanidine(in); Xref=Rhea:RHEA:73883, ChEBI:CHEBI:30087; Evidence={ECO:0000269|PubMed:10966924}; CATALYTIC ACTIVITY: Reaction=agmatine(out) = agmatine(in); Xref=Rhea:RHEA:72131, ChEBI:CHEBI:58145; Evidence={ECO:0000269|PubMed:12538837}; CATALYTIC ACTIVITY: Reaction=spermidine(in) = spermidine(out); Xref=Rhea:RHEA:35039, ChEBI:CHEBI:57834; Evidence={ECO:0000250|UniProtKB:O88446}; CATALYTIC ACTIVITY: Reaction=L-histidyl-L-proline diketopiperazine(in) = L-histidyl-L-proline diketopiperazine(out); Xref=Rhea:RHEA:74787, ChEBI:CHEBI:90039; Evidence={ECO:0000269|PubMed:17460754}; CATALYTIC ACTIVITY: Reaction=(R)-salsolinol(in) = (R)-salsolinol(out); Xref=Rhea:RHEA:74791, ChEBI:CHEBI:194082; Evidence={ECO:0000269|PubMed:17460754};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=126 uM for cyclo(his-pro) {ECO:0000269|PubMed:17460754}; KM=139 uM for salsolinol {ECO:0000269|PubMed:17460754}; KM=220 uM for histamine {ECO:0000269|PubMed:16581093}; KM=641 uM for histamine {ECO:0000269|PubMed:20858707}; KM=240 uM for adrenaline {ECO:0000269|PubMed:16581093}; KM=458 uM for adrenaline {ECO:0000269|PubMed:20858707}; KM=923 uM for noradrenaline {ECO:0000269|PubMed:20858707}; KM=2630 uM for noradrenaline {ECO:0000269|PubMed:16581093}; KM=988 uM for serotonin {ECO:0000269|PubMed:20858707}; KM=1033 uM for dopamine {ECO:0000269|PubMed:20858707}; KM=2500 uM for agmatine {ECO:0000269|PubMed:12538837}; Vmax=0.4 nmol/min/mg enzyme for cyclo(his-pro) uptake {ECO:0000269|PubMed:17460754}; Vmax=0.5 nmol/min/mg enzyme for salsolinol uptake {ECO:0000269|PubMed:17460754}; Vmax=34.6 nmol/min/mg enzyme for histamine uptake {ECO:0000269|PubMed:20858707}; Vmax=12.76 nmol/min/mg enzyme for adrenaline uptake {ECO:0000269|PubMed:20858707}; Vmax=30.13 nmol/min/mg enzyme for noradrenaline uptake {ECO:0000269|PubMed:20858707}; Vmax=11.56 nmol/min/mg enzyme for serotonin uptake {ECO:0000269|PubMed:20858707}; Vmax=22.68 nmol/min/mg enzyme for dopamine uptake {ECO:0000269|PubMed:20858707}; Vmax=15.9 nmol/min/mg enzyme for agmatine uptake {ECO:0000269|PubMed:12538837};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 for agmatine and MPP(+) transport. {ECO:0000269|PubMed:12538837};
| null |
FUNCTION: Electrogenic voltage-dependent transporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics (PubMed:10196521, PubMed:10966924, PubMed:12538837, PubMed:17460754, PubMed:20858707). Cation cellular uptake or release is driven by the electrochemical potential, i.e. membrane potential and concentration gradient (PubMed:10966924). Functions as a Na(+)- and Cl(-)-independent, bidirectional uniporter (PubMed:12538837). Implicated in monoamine neurotransmitters uptake such as dopamine, adrenaline/epinephrine, noradrenaline/norepinephrine, histamine, serotonin and tyramine, thereby supporting a role in homeostatic regulation of aminergic neurotransmission in the brain (PubMed:10196521, PubMed:16581093, PubMed:20858707). Transports dopaminergic neuromodulators cyclo(his-pro) and salsolinol with low efficiency (PubMed:17460754). May be involved in the uptake and disposition of cationic compounds by renal clearance from the blood flow (PubMed:10966924). May contribute to regulate the transport of cationic compounds in testis across the blood-testis-barrier (Probable). Mediates the transport of polyamine spermidine and putrescine (By similarity). Mediates the bidirectional transport of polyamine agmatine (PubMed:12538837). Also transports guanidine (PubMed:10966924). May also mediate intracellular transport of organic cations, thereby playing a role in amine metabolism and intracellular signaling (By similarity). {ECO:0000250|UniProtKB:O88446, ECO:0000269|PubMed:10196521, ECO:0000269|PubMed:10966924, ECO:0000269|PubMed:12538837, ECO:0000269|PubMed:16581093, ECO:0000269|PubMed:17460754, ECO:0000269|PubMed:20858707, ECO:0000305|PubMed:35307651}.
|
Homo sapiens (Human)
|
O75752
|
B3GL1_HUMAN
|
MASALWTVLPSRMSLRSLKWSLLLLSLLSFFVMWYLSLPHYNVIERVNWMYFYEYEPIYRQDFHFTLREHSNCSHQNPFLVILVTSHPSDVKARQAIRVTWGEKKSWWGYEVLTFFLLGQEAEKEDKMLALSLEDEHLLYGDIIRQDFLDTYNNLTLKTIMAFRWVTEFCPNAKYVMKTDTDVFINTGNLVKYLLNLNHSEKFFTGYPLIDNYSYRGFYQKTHISYQEYPFKVFPPYCSGLGYIMSRDLVPRIYEMMGHVKPIKFEDVYVGICLNLLKVNIHIPEDTNLFFLYRIHLDVCQLRRVIAAHGFSSKEIITFWQVMLRNTTCHY
|
2.4.1.79
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10993897, ECO:0000269|PubMed:9582303};
|
glycosphingolipid biosynthetic process [GO:0006688]; oligosaccharide biosynthetic process [GO:0009312]; protein O-linked glycosylation [GO:0006493]
|
Golgi membrane [GO:0000139]
|
galactosylgalactosylglucosylceramide beta-D-acetylgalactosaminyltransferase activity [GO:0047273]; UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity [GO:0008499]
|
PF01762;
|
3.90.550.50;
|
Glycosyltransferase 31 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein.
|
CATALYTIC ACTIVITY: Reaction=a globoside Gb3Cer (d18:1(4E)) + UDP-N-acetyl-alpha-D-galactosamine = a globoside Gb4Cer (d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:22252, ChEBI:CHEBI:15378, ChEBI:CHEBI:18259, ChEBI:CHEBI:18313, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.79; Evidence={ECO:0000269|PubMed:10993897}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22253; Evidence={ECO:0000269|PubMed:10993897};
| null |
PATHWAY: Protein modification; protein glycosylation.
| null | null |
FUNCTION: Transfers N-acetylgalactosamine onto globotriaosylceramide (PubMed:10993897). Plays a critical role in preimplantation stage embryonic development (By similarity). {ECO:0000250|UniProtKB:Q920V1, ECO:0000269|PubMed:10993897}.
|
Homo sapiens (Human)
|
O75762
|
TRPA1_HUMAN
|
MKRSLRKMWRPGEKKEPQGVVYEDVPDDTEDFKESLKVVFEGSAYGLQNFNKQKKLKRCDDMDTFFLHYAAAEGQIELMEKITRDSSLEVLHEMDDYGNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHRTIDVNLEGENGNTAVIIACTTNNSEALQILLKKGAKPCKSNKWGCFPIHQAAFSGSKECMEIILRFGEEHGYSRQLHINFMNNGKATPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMISSYSGSVDIVNTTDGCHETMLHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQVDIKDNFGRNFLHLTVQQPYGLKNLRPEFMQMQQIKELVMDEDNDGCTPLHYACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLQDISDTRLLNEGDLHGMTPLHLAAKNGHDKVVQLLLKKGALFLSDHNGWTALHHASMGGYTQTMKVILDTNLKCTDRLDEDGNTALHFAAREGHAKAVALLLSHNADIVLNKQQASFLHLALHNKRKEVVLTIIRSKRWDECLKIFSHNSPGNKCPITEMIEYLPECMKVLLDFCMLHSTEDKSCRDYYIEYNFKYLQCPLEFTKKTPTQDVIYEPLTALNAMVQNNRIELLNHPVCKEYLLMKWLAYGFRAHMMNLGSYCLGLIPMTILVVNIKPGMAFNSTGIINETSDHSEILDTTNSYLIKTCMILVFLSSIFGYCKEAGQIFQQKRNYFMDISNVLEWIIYTTGIIFVLPLFVEIPAHLQWQCGAIAVYFYWMNFLLYLQRFENCGIFIVMLEVILKTLLRSTVVFIFLLLAFGLSFYILLNLQDPFSSPLLSIIQTFSMMLGDINYRESFLEPYLRNELAHPVLSFAQLVSFTIFVPIVLMNLLIGLAVGDIAEVQKHASLKRIAMQVELHTSLEKKLPLWFLRKVDQKSTIVYPNKPRSGGMLFHIFCFLFCTGEIRQEIPNADKSLEMEILKQKYRLKDLTFLLEKQHELIKLIIQKMEIISETEDDDSHCSFQDRFKKEQMEQRNSRWNTVLRAVKAKTHHLEP
| null | null |
calcium ion transmembrane transport [GO:0070588]; cell surface receptor signaling pathway [GO:0007166]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to organic substance [GO:0071310]; detection of chemical stimulus involved in sensory perception of pain [GO:0050968]; detection of mechanical stimulus involved in sensory perception of pain [GO:0050966]; intracellular calcium ion homeostasis [GO:0006874]; monoatomic ion transport [GO:0006811]; protein homotetramerization [GO:0051289]; response to cold [GO:0009409]; response to organic cyclic compound [GO:0014070]; response to organic substance [GO:0010033]; response to pain [GO:0048265]; response to xenobiotic stimulus [GO:0009410]; sensory perception of pain [GO:0019233]; thermoception [GO:0050955]
|
plasma membrane [GO:0005886]; stereocilium bundle [GO:0032421]
|
calcium channel activity [GO:0005262]; channel activity [GO:0015267]; identical protein binding [GO:0042802]; intracellularly gated calcium channel activity [GO:0015278]; temperature-gated cation channel activity [GO:0097604]
|
PF00023;PF12796;PF00520;
|
1.25.40.20;
|
Transient receptor (TC 1.A.4) family
|
PTM: TRPA1 activation by electrophiles occurs though covalent modification of specific cysteine residues in the N-terminal cytoplasmic domain (PubMed:25389312). {ECO:0000305|PubMed:25389312}.; PTM: Hydroxylation is required for TRPA1 activity inhibition in normoxia. In hypoxia, the decrease in oxygen concentration diminishes the activity of the hydroxylase EGLN1, thus relieving TRPA1 from inhibition and ultimately leading to channel activation. {ECO:0000269|PubMed:21873995}.; PTM: Oxidation of Cys-633 and Cys-856 in hyperoxia may override the hydroxylase EGLN1-mediated inhibition, causing TRPA1 activation. {ECO:0000269|PubMed:21873995}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20547126, ECO:0000269|PubMed:21873995, ECO:0000269|PubMed:25389312, ECO:0000269|PubMed:25855297}; Multi-pass membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Receptor-activated non-selective cation channel involved in pain detection and possibly also in cold perception, oxygen concentration perception, cough, itch, and inner ear function (PubMed:21873995, PubMed:23199233, PubMed:25389312, PubMed:25855297). Shows 8-fold preference for divalent over monovalent cations (PubMed:31447178). Has a central role in the pain response to endogenous inflammatory mediators and to a diverse array of irritants, such as allylthiocyanate (AITC) from mustard oil or wasabi, cinnamaldehyde, diallyl disulfide (DADS) from garlic, and acrolein, an irritant from tears gas and vehicle exhaust fumes (PubMed:20547126, PubMed:25389312, PubMed:27241698, PubMed:30878828). Acts also as an ionotropic cannabinoid receptor by being activated by delta(9)-tetrahydrocannabinol (THC), the psychoactive component of marijuana (PubMed:25389312). Is activated by a large variety of structurally unrelated electrophilic and non-electrophilic chemical compounds. Electrophilic ligands activate TRPA1 by interacting with critical N-terminal Cys residues in a covalent manner, whereas mechanisms of non-electrophilic ligands are not well determined. May be a component for the mechanosensitive transduction channel of hair cells in inner ear, thereby participating in the perception of sounds. Probably operated by a phosphatidylinositol second messenger system (By similarity). {ECO:0000250|UniProtKB:Q8BLA8, ECO:0000269|PubMed:20547126, ECO:0000269|PubMed:21873995, ECO:0000269|PubMed:25389312, ECO:0000269|PubMed:25855297, ECO:0000269|PubMed:27241698, ECO:0000269|PubMed:30878828, ECO:0000269|PubMed:31447178, ECO:0000305|PubMed:23199233}.
|
Homo sapiens (Human)
|
O75771
|
RA51D_HUMAN
|
MGVLRVGLCPGLTEEMIQLLRSHRIKTVVDLVSADLEEVAQKCGLSYKALVALRRVLLAQFSAFPVNGADLYEELKTSTAILSTGIGSLDKLLDAGLYTGEVTEIVGGPGSGKTQVCLCMAANVAHGLQQNVLYVDSNGGLTASRLLQLLQAKTQDEEEQAEALRRIQVVHAFDIFQMLDVLQELRGTVAQQVTGSSGTVKVVVVDSVTAVVSPLLGGQQREGLALMMQLARELKTLARDLGMAVVVTNHITRDRDSGRLKPALGRSWSFVPSTRILLDTIEGAGASGGRRMACLAKSSRQPTGFQEMVDIGTWGTSEQSATLQGDQT
| null | null |
DNA repair [GO:0006281]; DNA strand invasion [GO:0042148]; double-strand break repair via homologous recombination [GO:0000724]; interstrand cross-link repair [GO:0036297]; reciprocal meiotic recombination [GO:0007131]; regulation of cell cycle [GO:0051726]; telomere maintenance [GO:0000723]; telomere maintenance via recombination [GO:0000722]
|
centrosome [GO:0005813]; chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Rad51B-Rad51C-Rad51D-XRCC2 complex [GO:0033063]; replication fork [GO:0005657]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent DNA damage sensor activity [GO:0140664]; DNA binding [GO:0003677]; four-way junction DNA binding [GO:0000400]; gamma-tubulin binding [GO:0043015]; single-stranded DNA binding [GO:0003697]
|
PF08423;PF21794;
|
3.40.50.300;
|
RecA family, RAD51 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome, telomere.
| null | null | null | null | null |
FUNCTION: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. Bind to single-stranded DNA (ssDNA) and has DNA-dependent ATPase activity. Part of the RAD51 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. Involved in telomere maintenance. The BCDX2 subcomplex XRCC2:RAD51D can stimulate Holliday junction resolution by BLM. {ECO:0000269|PubMed:10871607, ECO:0000269|PubMed:11751635, ECO:0000269|PubMed:11834724, ECO:0000269|PubMed:11842113, ECO:0000269|PubMed:12975363, ECO:0000269|PubMed:15109494, ECO:0000269|PubMed:23149936}.
|
Homo sapiens (Human)
|
O75781
|
PALM_HUMAN
|
MEVLAAETTSQQERLQAIAEKRKRQAEIENKRRQLEDERRQLQHLKSKALRERWLLEGTPSSASEGDEDLRRQMQDDEQKTRLLEDSVSRLEKEIEVLERGDSAPATAKENAAAPSPVRAPAPSPAKEERKTEVVMNSQQTPVGTPKDKRVSNTPLRTVDGSPMMKAAMYSVEITVEKDKVTGETRVLSSTTLLPRQPLPLGIKVYEDETKVVHAVDGTAENGIHPLSSSEVDELIHKADEVTLSEAGSTAGAAETRGAVEGAARTTPSRREITGVQAQPGEATSGPPGIQPGQEPPVTMIFMGYQNVEDEAETKKVLGLQDTITAELVVIEDAAEPKEPAPPNGSAAEPPTEAASREENQAGPEATTSDPQDLDMKKHRCKCCSIM
| null | null |
adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; cellular response to electrical stimulus [GO:0071257]; cytoskeleton organization [GO:0007010]; negative regulation of dopamine receptor signaling pathway [GO:0060160]; positive regulation of filopodium assembly [GO:0051491]; protein localization to plasma membrane [GO:0072659]; regulation of cell shape [GO:0008360]; synapse maturation [GO:0060074]
|
apicolateral plasma membrane [GO:0016327]; axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; cytoplasmic side of plasma membrane [GO:0009898]; cytoplasmic vesicle [GO:0031410]; dendritic spine [GO:0043197]; filopodium membrane [GO:0031527]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]
|
D3 dopamine receptor binding [GO:0031750]
|
PF03285;
| null |
Paralemmin family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14978216}; Lipid-anchor {ECO:0000269|PubMed:14978216}; Cytoplasmic side {ECO:0000269|PubMed:14978216}. Cell projection, filopodium membrane {ECO:0000269|PubMed:14978216}; Lipid-anchor {ECO:0000269|PubMed:14978216}. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Basolateral cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Apicolateral cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Translocation to the plasma membrane is enhanced upon stimulation of neuronal activity.
| null | null | null | null | null |
FUNCTION: Involved in plasma membrane dynamics and cell process formation. Isoform 1 and isoform 2 are necessary for axonal and dendritic filopodia induction, for dendritic spine maturation and synapse formation in a palmitoylation-dependent manner. {ECO:0000269|PubMed:14978216}.
|
Homo sapiens (Human)
|
O75783
|
RHBL1_HUMAN
|
MGRVEDGGTTEELEDWDPGTSALPAPGIKQGPREQTGTGPLSQKCWEPEPDAPSQPGPALWSRGRARTQALAGGSSLQQLDPENTGFIGADTFTGLVHSHELPLDPAKLDMLVALAQSNEQGQVCYQELVDLISSKRSSSFKRAIANGQRALPRDGPLDEPGLGVYKRFVRYVAYEILPCEVDRRWYFYRHRSCPPPVFMASVTLAQIIVFLCYGARLNKWVLQTYHPEYMKSPLVYHPGHRARAWRFLTYMFMHVGLEQLGFNALLQLMIGVPLEMVHGLLRISLLYLAGVLAGSLTVSITDMRAPVVGGSGGVYALCSAHLANVVMNWAGMRCPYKLLRMVLALVCMSSEVGRAVWLRFSPPLPASGPQPSFMAHLAGAVVGVSMGLTILRSYEERLRDQCGWWVVLLAYGTFLLFAVFWNVFAYDLLGAHIPPPP
|
3.4.21.105
| null |
proteolysis [GO:0006508]; signal transduction [GO:0007165]
|
membrane [GO:0016020]; plasma membrane [GO:0005886]
|
serine-type endopeptidase activity [GO:0004252]
|
PF01694;
|
1.10.238.10;1.20.1540.10;
|
Peptidase S54 family
| null |
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
|
CATALYTIC ACTIVITY: Reaction=Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.; EC=3.4.21.105;
| null | null | null | null |
FUNCTION: May be involved in regulated intramembrane proteolysis and the subsequent release of functional polypeptides from their membrane anchors. {ECO:0000250}.
|
Homo sapiens (Human)
|
O75787
|
RENR_HUMAN
|
MAVFVVLLALVAGVLGNEFSILKSPGSVVFRNGNWPIPGERIPDVAALSMGFSVKEDLSWPGLAVGNLFHRPRATVMVMVKGVNKLALPPGSVISYPLENAVPFSLDSVANSIHSLFSEETPVVLQLAPSEERVYMVGKANSVFEDLSVTLRQLRNRLFQENSVLSSLPLNSLSRNNEVDLLFLSELQVLHDISSLLSRHKHLAKDHSPDLYSLELAGLDEIGKRYGEDSEQFRDASKILVDALQKFADDMYSLYGGNAVVELVTVKSFDTSLIRKTRTILEAKQAKNPASPYNLAYKYNFEYSVVFNMVLWIMIALALAVIITSYNIWNMDPGYDSIIYRMTNQKIRMD
| null | null |
angiotensin maturation [GO:0002003]; central nervous system maturation [GO:0021626]; endosomal lumen acidification [GO:0048388]; eye pigmentation [GO:0048069]; Golgi lumen acidification [GO:0061795]; head morphogenesis [GO:0060323]; intracellular pH reduction [GO:0051452]; lysosomal lumen acidification [GO:0007042]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of transforming growth factor beta1 production [GO:0032914]; positive regulation of Wnt signaling pathway [GO:0030177]; proton transmembrane transport [GO:1902600]; regulation of MAPK cascade [GO:0043408]; rostrocaudal neural tube patterning [GO:0021903]; synaptic vesicle lumen acidification [GO:0097401]; vacuolar acidification [GO:0007035]
|
autophagosome membrane [GO:0000421]; axon [GO:0030424]; clathrin-coated vesicle membrane [GO:0030665]; dendritic spine membrane [GO:0032591]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; ficolin-1-rich granule membrane [GO:0101003]; Golgi membrane [GO:0000139]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; proton-transporting V-type ATPase complex [GO:0033176]; synaptic vesicle membrane [GO:0030672]; tertiary granule membrane [GO:0070821]; vacuolar proton-transporting V-type ATPase complex [GO:0016471]; vacuolar proton-transporting V-type ATPase, V0 domain [GO:0000220]
|
signaling receptor activity [GO:0038023]
|
PF07850;
| null | null |
PTM: Phosphorylated. {ECO:0000269|PubMed:12045255}.; PTM: Proteolytically cleaved by a furin-like convertase in the trans-Golgi network to generate N- and C-terminal fragments. {ECO:0000269|PubMed:29127204}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29127204}; Single-pass type I membrane protein {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:29127204}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, dendritic spine membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000250|UniProtKB:Q9CYN9}. Endosome membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:Q6AXS4}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q6AXS4}; Single-pass type I membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Multifunctional protein which functions as a renin, prorenin cellular receptor and is involved in the assembly of the lysosomal proton-transporting V-type ATPase (V-ATPase) and the acidification of the endo-lysosomal system (PubMed:12045255, PubMed:29127204, PubMed:30374053, PubMed:32276428). May mediate renin-dependent cellular responses by activating ERK1 and ERK2 (PubMed:12045255). By increasing the catalytic efficiency of renin in AGT/angiotensinogen conversion to angiotensin I, may also play a role in the renin-angiotensin system (RAS) (PubMed:12045255). Through its function in V-type ATPase (v-ATPase) assembly and acidification of the lysosome it regulates protein degradation and may control different signaling pathways important for proper brain development, synapse morphology and synaptic transmission (By similarity). {ECO:0000250|UniProtKB:Q9CYN9, ECO:0000269|PubMed:12045255, ECO:0000269|PubMed:29127204, ECO:0000269|PubMed:30374053, ECO:0000269|PubMed:32276428}.
|
Homo sapiens (Human)
|
O75791
|
GRAP2_HUMAN
|
MEAVAKFDFTASGEDELSFHTGDVLKILSNQEEWFKAELGSQEGYVPKNFIDIQFPKWFHEGLSRHQAENLLMGKEVGFFIIRASQSSPGDFSISVRHEDDVQHFKVMRDNKGNYFLWTEKFPSLNKLVDYYRTNSISRQKQIFLRDRTREDQGHRGNSLDRRSQGGPHLSGAVGEEIRPSMNRKLSDHPPTLPLQQHQHQPQPPQYAPAPQQLQQPPQQRYLQHHHFHQERRGGSLDINDGHCGTGLGSEMNAALMHRRHTDPVQLQAAGRVRWARALYDFEALEDDELGFHSGEVVEVLDSSNPSWWTGRLHNKLGLFPANYVAPMTR
| null | null |
cell-cell signaling [GO:0007267]; Ras protein signal transduction [GO:0007265]; regulation of MAPK cascade [GO:0043408]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome [GO:0005768]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
phosphotyrosine residue binding [GO:0001784]
|
PF00017;PF00018;
|
3.30.505.10;2.30.30.40;
|
GRB2/sem-5/DRK family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21179510}. Cytoplasm {ECO:0000269|PubMed:21179510}. Endosome {ECO:0000269|PubMed:21179510}.
| null | null | null | null | null |
FUNCTION: Interacts with SLP-76 to regulate NF-AT activation. Binds to tyrosine-phosphorylated shc.
|
Homo sapiens (Human)
|
O75792
|
RNH2A_HUMAN
|
MDLSELERDNTGRCRLSSPVPAVCRKEPCVLGVDEAGRGPVLGPMVYAICYCPLPRLADLEALKVADSKTLLESERERLFAKMEDTDFVGWALDVLSPNLISTSMLGRVKYNLNSLSHDTATGLIQYALDQGVNVTQVFVDTVGMPETYQARLQQSFPGIEVTVKAKADALYPVVSAASICAKVARDQAVKKWQFVEKLQDLDTDYGSGYPNDPKTKAWLKEHVEPVFGFPQFVRFSWRTAQTILEKEAEDVIWEDSASENQEGLRKITSYFLNEGSQARPRSSHRYFLERGLESATSL
|
3.1.26.4
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding. {ECO:0000250};
|
DNA replication [GO:0006260]; DNA replication, removal of RNA primer [GO:0043137]; mismatch repair [GO:0006298]; RNA catabolic process [GO:0006401]
|
cytosol [GO:0005829]; nucleoplasm [GO:0005654]; ribonuclease H2 complex [GO:0032299]
|
metal ion binding [GO:0046872]; RNA binding [GO:0003723]; RNA nuclease activity [GO:0004540]; RNA-DNA hybrid ribonuclease activity [GO:0004523]
|
PF01351;
|
3.30.420.10;1.10.10.460;
|
RNase HII family, Eukaryotic subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence={ECO:0000269|PubMed:21177858};
| null | null | null | null |
FUNCTION: Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes. {ECO:0000269|PubMed:16845400, ECO:0000269|PubMed:21177858}.
|
Homo sapiens (Human)
|
O75794
|
CD123_HUMAN
|
MKKEHVLHCQFSAWYPFFRGVTIKSVILPLPQNVKDYLLDDGTLVVSGRDDPPTHSQPDSDDEAEEIQWSDDENTATLTAPEFPEFATKVQEAINSLGGSVFPKLNWSAPRDAYWIAMNSSLKCKTLSDIFLLFKSSDFITRDFTQPFIHCTDDSPDPCIEYELVLRKWCELIPGAEFRCFVKENKLIGISQRDYTQYYDHISKQKEEIRRCIQDFFKKHIQYKFLDEDFVFDIYRDSRGKVWLIDFNPFGEVTDSLLFTWEELISENNLNGDFSEVDAQEQDSPAFRCTNSEVTVQPSPYLSYRLPKDFVDLSTGEDAHKLIDFLKLKRNQQEDD
| null | null |
eukaryotic translation initiation factor 2 complex assembly [GO:1905143]
|
cytoplasm [GO:0005737]
|
ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; protein folding chaperone [GO:0044183]
|
PF07065;
| null |
CDC123 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q62834}.
| null | null | null | null | null |
FUNCTION: ATP-dependent protein-folding chaperone for the eIF2 complex (PubMed:35031321, PubMed:37507029). Binds to the gamma subunit of the eIF2 complex which allows the subunit to assemble with the alpha and beta subunits (By similarity). {ECO:0000250|UniProtKB:Q05791, ECO:0000269|PubMed:35031321, ECO:0000269|PubMed:37507029}.
|
Homo sapiens (Human)
|
O75795
|
UDB17_HUMAN
|
MSLKWMSVFLLMQLSCYFSSGSCGKVLVWPTEYSHWINMKTILEELVQRGHEVIVLTSSASILVNASKSSAIKLEVYPTSLTKNDLEDFFMKMFDRWTYSISKNTFWSYFSQLQELCWEYSDYNIKLCEDAVLNKKLMRKLQESKFDVLLADAVNPCGELLAELLNIPFLYSLRFSVGYTVEKNGGGFLFPPSYVPVVMSELSDQMIFMERIKNMIYMLYFDFWFQAYDLKKWDQFYSEVLGRPTTLFETMGKAEMWLIRTYWDFEFPRPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSSGENGIVVFSLGSMISNMSEESANMIASALAQIPQKVLWRFDGKKPNTLGSNTRLYKWLPQNDLLGHPKTKAFITHGGTNGIYEAIYHGIPMVGIPLFADQHDNIAHMKAKGAALSVDIRTMSSRDLLNALKSVINDPIYKENIMKLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHNLTWIQYHSLDVIAFLLACVATMIFMITKCCLFCFRKLAKTGKKKKRD
|
2.4.1.17
| null |
cellular glucuronidation [GO:0052695]; estrogen metabolic process [GO:0008210]; steroid metabolic process [GO:0008202]; xenobiotic metabolic process [GO:0006805]
|
endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]
|
glucuronosyltransferase activity [GO:0015020]
|
PF00201;
|
3.40.50.2000;
|
UDP-glycosyltransferase family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:23288867}; Single-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP; Xref=Rhea:RHEA:21032, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:132367, ChEBI:CHEBI:132368; EC=2.4.1.17; Evidence={ECO:0000269|PubMed:16595710, ECO:0000269|PubMed:18719240, ECO:0000269|PubMed:19022937, ECO:0000269|PubMed:23288867, ECO:0000269|PubMed:8798464}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21033; Evidence={ECO:0000305|PubMed:16595710, ECO:0000305|PubMed:18719240, ECO:0000305|PubMed:19022937, ECO:0000305|PubMed:23288867, ECO:0000305|PubMed:8798464}; CATALYTIC ACTIVITY: Reaction=17alpha-estradiol + UDP-alpha-D-glucuronate = 17alpha-estradiol 3-O-(beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:52868, ChEBI:CHEBI:15378, ChEBI:CHEBI:17160, ChEBI:CHEBI:57529, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223; Evidence={ECO:0000269|PubMed:23288867}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52869; Evidence={ECO:0000305|PubMed:23288867}; CATALYTIC ACTIVITY: Reaction=17alpha-estradiol + UDP-alpha-D-glucuronate = 17alpha-estradiol 17-O-(beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:52872, ChEBI:CHEBI:15378, ChEBI:CHEBI:17160, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136642; Evidence={ECO:0000269|PubMed:23288867}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52873; Evidence={ECO:0000305|PubMed:23288867}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + UDP-alpha-D-glucuronate = 17beta-estradiol 17-O-(beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:52464, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:82961; Evidence={ECO:0000269|PubMed:18719240, ECO:0000269|PubMed:23288867}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52465; Evidence={ECO:0000305|PubMed:18719240, ECO:0000305|PubMed:23288867}; CATALYTIC ACTIVITY: Reaction=17beta-hydroxy-5alpha-androstan-3-one + UDP-alpha-D-glucuronate = 5alpha-dihydrotestosterone 17-O-(beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:53000, ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136914; Evidence={ECO:0000269|PubMed:16595710}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53001; Evidence={ECO:0000305|PubMed:16595710}; CATALYTIC ACTIVITY: Reaction=testosterone + UDP-alpha-D-glucuronate = H(+) + testosterone 17-O-(beta-D-glucuronate) + UDP; Xref=Rhea:RHEA:52456, ChEBI:CHEBI:15378, ChEBI:CHEBI:17347, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136639; Evidence={ECO:0000269|PubMed:19022937}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52457; Evidence={ECO:0000305|PubMed:19022937};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.4 uM for 17beta-estradiol/estradiol (when assaying glucuronidation at position 17) {ECO:0000269|PubMed:18719240}; KM=10 uM for testosterone (when assaying glucuronidation at position 17) {ECO:0000269|PubMed:19022937}; KM=3.4 uM for testosterone {ECO:0000269|PubMed:8798464}; KM=0.7 uM for dihydrotestosterone {ECO:0000269|PubMed:8798464}; KM=1 uM for androstane-3alpha,17beta-diol {ECO:0000269|PubMed:8798464}; Vmax=327 pmol/min/mg enzyme for the formation of 17beta-estradiol 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:18719240}; Vmax=3.8 pmol/min/mg enzyme for the formation of 16alpha,17beta-estriol 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867}; Vmax=5.4 pmol/min/mg enzyme for the formation of 16beta,17beta-estriol 16-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867}; Vmax=5.9 pmol/min/mg enzyme for the formation of 16beta,17beta-estriol 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867}; Vmax=38.2 pmol/min/mg enzyme for the formation of 17beta-estradiol 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867}; Vmax=59.8 pmol/min/mg enzyme for the formation of 17alpha-estradiol 3-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867}; Vmax=32.7 pmol/min/mg enzyme for the formation of 17alpha-estradiol 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867}; Vmax=1626 pmol/min/mg enzyme for the formation of 5alpha-dihydrotestosterone 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:16595710}; Vmax=1002 pmol/min/mg enzyme for the formation of testosterone 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:19022937}; Vmax=50 pmol/min/mg enzyme for the formation of testosterone {ECO:0000269|PubMed:8798464}; Vmax=51.7 pmol/min/mg enzyme for the formation of dihydrotestosterone {ECO:0000269|PubMed:8798464}; Vmax=36.7 pmol/min/mg enzyme for the formation of androstane-3alpha,17beta-diol glucuronide {ECO:0000269|PubMed:8798464}; Note=Some kinetic parameters were assessed using commercial enzymes, which may represent a mix of both active and inactive protein forms, and therefore modify the kinetic values. {ECO:0000305|PubMed:16595710};
| null | null | null |
FUNCTION: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile (PubMed:16595710, PubMed:18719240, PubMed:19022937, PubMed:23288867, PubMed:8798464). Catalyzes the glucuronidation of endogenous steroid hormones such as androgens (epitestosterone, androsterone) and estrogens (estradiol, epiestradiol) (PubMed:16595710, PubMed:18719240, PubMed:19022937, PubMed:23288867, PubMed:8798464). {ECO:0000269|PubMed:16595710, ECO:0000269|PubMed:18719240, ECO:0000269|PubMed:19022937, ECO:0000269|PubMed:23288867, ECO:0000269|PubMed:8798464}.
|
Homo sapiens (Human)
|
O75800
|
ZMY10_HUMAN
|
MGDLELLLPGEAEVLVRGLRSFPLREMGSEGWNQQHENLEKLNMQAILDATVSQGEPIQELLVTHGKVPTLVEELIAVEMWKQKVFPVFCRVEDFKPQNTFPIYMVVHHEASIINLLETVFFHKEVCESAEDTVLDLVDYCHRKLTLLVAQSGCGGPPEGEGSQDSNPMQELQKQAELMEFEIALKALSVLRYITDCVDSLSLSTLSRMLSTHNLPCLLVELLEHSPWSRREGGKLQQFEGSRWHTVAPSEQQKLSKLDGQVWIALYNLLLSPEAQARYCLTSFAKGRLLKLRAFLTDTLLDQLPNLAHLQSFLAHLTLTETQPPKKDLVLEQIPEIWERLERENRGKWQAIAKHQLQHVFSPSEQDLRLQARRWAETYRLDVLEAVAPERPRCAYCSAEASKRCSRCQNEWYCCRECQVKHWEKHGKTCVLAAQGDRAK
| null | null |
cilium movement [GO:0003341]; inner dynein arm assembly [GO:0036159]; motile cilium assembly [GO:0044458]; outer dynein arm assembly [GO:0036158]; positive regulation of motile cilium assembly [GO:1905505]; protein localization to cilium [GO:0061512]
|
apical plasma membrane [GO:0016324]; centriolar satellite [GO:0034451]; cytoplasm [GO:0005737]; dynein axonemal particle [GO:0120293]
|
metal ion binding [GO:0046872]; molecular adaptor activity [GO:0060090]; protein folding chaperone [GO:0044183]
|
PF01753;
|
6.10.140.2220;
|
ZMYND10 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6AXZ5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q6AXZ5}. Apical cell membrane {ECO:0000250|UniProtKB:Q99ML0}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q5FWU8}.
| null | null | null | null | null |
FUNCTION: Plays a role in axonemal structure organization and motility (PubMed:23891469, PubMed:23891471). Involved in axonemal pre-assembly of inner and outer dynein arms (IDA and ODA, respectively) for proper axoneme building for cilia motility (By similarity). May act by indirectly regulating transcription of dynein proteins (By similarity). {ECO:0000250|UniProtKB:Q99ML0, ECO:0000269|PubMed:23891469, ECO:0000269|PubMed:23891471}.
|
Homo sapiens (Human)
|
O75807
|
PR15A_HUMAN
|
MAPGQAPHQATPWRDAHPFFLLSPVMGLLSRAWSRLRGLGPLEPWLVEAVKGAALVEAGLEGEARTPLAIPHTPWGRRPEEEAEDSGGPGEDRETLGLKTSSSLPEAWGLLDDDDGMYGEREATSVPRGQGSQFADGQRAPLSPSLLIRTLQGSDKNPGEEKAEEEGVAEEEGVNKFSYPPSHRECCPAVEEEDDEEAVKKEAHRTSTSALSPGSKPSTWVSCPGEEENQATEDKRTERSKGARKTSVSPRSSGSDPRSWEYRSGEASEEKEEKAHKETGKGEAAPGPQSSAPAQRPQLKSWWCQPSDEEEGEVKALGAAEKDGEAECPPCIPPPSAFLKAWVYWPGEDTEEEEDEEEDEDSDSGSDEEEGEAEASSSTPATGVFLKSWVYQPGEDTEEEEDEDSDTGSAEDEREAETSASTPPASAFLKAWVYRPGEDTEEEEDEDVDSEDKEDDSEAALGEAESDPHPSHPDQRAHFRGWGYRPGKETEEEEAAEDWGEAEPCPFRVAIYVPGEKPPPPWAPPRLPLRLQRRLKRPETPTHDPDPETPLKARKVRFSEKVTVHFLAVWAGPAQAARQGPWEQLARDRSRFARRITQAQEELSPCLTPAARARAWARLRNPPLAPIPALTQTLPSSSVPSSPVQTTPLSQAVATPSRSSAAAAAALDLSGRRG
| null | null |
apoptotic process [GO:0006915]; DNA damage response [GO:0006974]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; negative regulation of PERK-mediated unfolded protein response [GO:1903898]; negative regulation of phosphoprotein phosphatase activity [GO:0032515]; negative regulation of protein dephosphorylation [GO:0035308]; positive regulation of endoplasmic reticulum stress-induced eIF2 alpha dephosphorylation [GO:1903917]; positive regulation of peptidyl-serine dephosphorylation [GO:1902310]; positive regulation of phosphoprotein phosphatase activity [GO:0032516]; positive regulation of translational initiation in response to stress [GO:0032058]; protein localization to endoplasmic reticulum [GO:0070972]; regulation of cell cycle [GO:0051726]; regulation of translational initiation by eIF2 alpha dephosphorylation [GO:0036496]; response to endoplasmic reticulum stress [GO:0034976]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; protein phosphatase type 1 complex [GO:0000164]
|
protein kinase binding [GO:0019901]; protein phosphatase 1 binding [GO:0008157]; protein phosphatase activator activity [GO:0072542]; protein phosphatase regulator activity [GO:0019888]
|
PF10488;
| null |
PPP1R15 family
|
PTM: Phosphorylated at multiple Ser/Thr residues. Phosphorylated on tyrosine by LYN; which impairs its antiproliferative activity. Phosphorylation at Tyr-262 enhances proteasomal degradation, this position is dephosphorylated by PTPN2. {ECO:0000269|PubMed:11517336, ECO:0000269|PubMed:24092754}.; PTM: Polyubiquitinated. Exhibits a rapid proteasomal degradation with a half-life under 1 hour, ubiquitination depends on endoplasmic reticulum association. {ECO:0000269|PubMed:24092754}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:12556489, ECO:0000269|PubMed:21518769, ECO:0000269|PubMed:26742780}. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:21518769}. Note=Associates with membranes via an N-terminal amphipathic intramembrane region. {ECO:0000269|PubMed:21518769}.
| null | null | null | null | null |
FUNCTION: Recruits the serine/threonine-protein phosphatase PPP1CA to prevents excessive phosphorylation of the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress (PubMed:26095357, PubMed:26742780). Down-regulates the TGF-beta signaling pathway by promoting dephosphorylation of TGFB1 by PP1 (PubMed:14718519). May promote apoptosis by inducing p53/TP53 phosphorylation on 'Ser-15' (PubMed:14635196). Plays an essential role in autophagy by tuning translation during starvation, thus enabling lysosomal biogenesis and a sustained autophagic flux (PubMed:32978159). Acts also a viral restriction factor by attenuating HIV-1 replication (PubMed:31778897). Mechanistically, mediates the inhibition of HIV-1 TAR RNA-mediated translation (PubMed:31778897). {ECO:0000269|PubMed:11564868, ECO:0000269|PubMed:12556489, ECO:0000269|PubMed:14635196, ECO:0000269|PubMed:14718519, ECO:0000269|PubMed:26095357, ECO:0000269|PubMed:31778897, ECO:0000269|PubMed:8139541}.; FUNCTION: (Microbial infection) Promotes enterovirus 71 replication by mediating the internal ribosome entry site (IRES) activity of viral 5'-UTR. {ECO:0000269|PubMed:34985336}.
|
Homo sapiens (Human)
|
O75808
|
CAN15_HUMAN
|
MATVGEWSCVRCTFLNPAGQRQCSICEAPRHKPDLNHILRLSVEEQKWPCARCTFRNFLGKEACEVCGFTPEPAPGAAFLPVLNGVLPKPPAILGEPKGSCQEEAGPVRTAGLVATEPARGQCEDKDEEEKEEQEEEEGAAEPRGGWACPRCTLHNTPVASSCSVCGGPRRLSLPRIPPEALVVPEVVAPAGFHVVPAAPPPGLPGEGAEANPPATSQGPAAEPEPPRVPPFSPFSSTLQNNPVPRSRREVPPQLQPPVPEAAQPSPSAGCRGAPQGSGWAGASRLAELLSGKRLSVLEEEATEGGTSRVEAGSSTSGSDIIDLAGDTVRYTPASPSSPDFTTWSCAKCTLRNPTVAPRCSACGCSKLHGFQEHGEPPTHCPDCGADKPSPCGRSCGRVSSAQKAARVLPERPGQWACPACTLLNALRAKHCAACHTPQLLVAQRRGAAPLRRRESMHVEQRRQTDEGEAKALWENIVAFCRENNVSFVDDSFPPGPESVGFPAGDSVQQRVRQWLRPQEINCSVFRDHRATWSVFHTLRPSDILQGLLGNCWFLSALAVLAERPDLVERVMVTRSLCAEGAYQVRLCKDGTWTTVLVDDMLPCDEAGCLLFSQAQRKQLWVALIEKALAKLHGSYFALQAGRAIEGLATLTGAPCESLALQLSSTNPREEPVDTDLIWAKMLSSKEAGFLMGASCGGGNMKVDDSAYESLGLRPRHAYSILDVRDVQGTRLLRLRNPWGRFSWNGSWSDEWPHWPGHLRGELMPHGSSEGVFWMEYGDFVRYFDSVDICKVHSDWQEARVQGCFPSSASAPVGVTALTVLERASLEFALFQEGSRRSDAVDSHLLDLCILVFRATFGSGGHLSLGRLLAHSKRAVKKFVSCDVMLEPGEYAVVCCAFNHWGPPLPGTPAPQASSPSAGVPRASPEPPGHVLAVYSSRLVMVEPVEAQPTTLADAIILLTESRGERHEGREGMTCYYLTHGWAGLIVVVENRHPKAYLHVQCDCTDSFNVVSTRGSLRTQDSVPPLHRQVLVILSQLEGNAGFSITHRLAHRKAAQAFLSDWTASKGTHSPPLTPEVAGLHGPRPL
|
3.4.22.-
| null |
proteolysis [GO:0006508]
|
cytoplasm [GO:0005737]
|
calcium-dependent cysteine-type endopeptidase activity [GO:0004198]; metal ion binding [GO:0046872]
|
PF00648;PF00641;
|
3.90.70.10;4.10.1060.10;2.30.30.380;
|
Peptidase C2 family
| null | null | null | null | null | null | null | null |
Homo sapiens (Human)
|
O75815
|
BCAR3_HUMAN
|
MAAGKFASLPRNMPVNHQFPLASSMDLLSSRSPLAEHRPDAYQDVSIHGTLPRKKKGPPPIRSCDDFSHMGTLPHSKSPRQNSPVTQDGIQESPWQDRHGETFTFRDPHLLDPTVEYVKFSKERHIMDRTPEKLKKELEEELLLSSEDLRSHAWYHGRIPRQVSENLVQRDGDFLVRDSLSSPGNFVLTCQWKNLAQHFKINRTVLRLSEAYSRVQYQFEMESFDSIPGLVRCYVGNRRPISQQSGAIIFQPINRTVPLRCLEEHYGTSPGQAREGSLTKGRPDVAKRLSLTMGGVQAREQNLPRGNLLRNKEKSGSQPACLDHMQDRRALSLKAHQSESYLPIGCKLPPQSSGVDTSPCPNSPVFRTGSEPALSPAVVRRVSSDARAGEALRGSDSQLCPKPPPKPCKVPFLKVPSSPSAWLNSEANYCELNPAFATGCGRGAKLPSCAQGSHTELLTAKQNEAPGPRNSGVNYLILDDDDRERPWEPAAAQMEKGQWDKGEFVTPLLETVSSFRPNEFESKFLPPENKPLETAMLKRAKELFTNNDPKVIAQHVLSMDCRVARILGVSEEMRRNMGVSSGLELITLPHGHQLRLDIIERHNTMAIGIAVDILGCTGTLEDRAATLSKIIQVAVELKDSMGDLYSFSALMKALEMPQITRLEKTWTALRHQYTQTAILYEKQLKPFSKLLHEGRESTCVPPNNVSVPLLMPLVTLMERQAVTFEGTDMWEKNDQSCEIMLNHLATARFMAEAADSYRMNAERILAGFQPDEEMNEICKTEFQMRLLWGSKGAQVNQTERYEKFNQILTALSRKLEPPPVKQAEL
| null | null |
endothelin receptor signaling pathway [GO:0086100]; epidermal growth factor receptor signaling pathway [GO:0007173]; insulin receptor signaling pathway [GO:0008286]; lens morphogenesis in camera-type eye [GO:0002089]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of GTPase activity [GO:0043547]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; response to xenobiotic stimulus [GO:0009410]; signal transduction [GO:0007165]; small GTPase-mediated signal transduction [GO:0007264]
|
cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; membrane [GO:0016020]
|
guanyl-nucleotide exchange factor activity [GO:0005085]; kinase binding [GO:0019900]; phosphotyrosine residue binding [GO:0001784]
|
PF00617;PF00017;
|
1.10.840.10;3.30.505.10;
| null |
PTM: Phosphorylated on tyrosine residues. {ECO:0000250|UniProtKB:Q9QZK2}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9QZK2}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q9QZK2}. Note=Localization to focal adhesions depends on interaction with PTPRA. {ECO:0000250|UniProtKB:Q9QZK2}.
| null | null | null | null | null |
FUNCTION: Acts as an adapter protein downstream of several growth factor receptors to promote cell proliferation, migration, and redistribution of actin fibers (PubMed:24216110). Specifically involved in INS/insulin signaling pathway by mediating MAPK1/ERK2-MAPK3/ERK1 activation and DNA synthesis (PubMed:24216110). Promotes insulin-mediated membrane ruffling (By similarity). In response to vasoconstrictor peptide EDN1, involved in the activation of RAP1 downstream of PTK2B via interaction with phosphorylated BCAR1 (PubMed:19086031). Inhibits cell migration and invasion via regulation of TGFB-mediated matrix digestion, actin filament rearrangement, and inhibition of invadopodia activity (By similarity). May inhibit TGFB-SMAD signaling, via facilitating BCAR1 and SMAD2 and/or SMAD3 interaction (By similarity). Regulates EGF-induced DNA synthesis (PubMed:18722344). Required for the maintenance of ocular lens morphology and structural integrity, potentially via regulation of focal adhesion complex signaling (By similarity). Acts upstream of PTPRA to regulate the localization of BCAR1 and PTPRA to focal adhesions, via regulation of SRC-mediated phosphorylation of PTPRA (By similarity). Positively regulates integrin-induced tyrosine phosphorylation of BCAR1 (By similarity). Acts as a guanine nucleotide exchange factor (GEF) for small GTPases RALA, RAP1A and RRAS (By similarity). However, in a contrasting study, lacks GEF activity towards RAP1 (PubMed:22081014). {ECO:0000250|UniProtKB:D3ZAZ5, ECO:0000250|UniProtKB:Q9QZK2, ECO:0000269|PubMed:18722344, ECO:0000269|PubMed:19086031, ECO:0000269|PubMed:22081014, ECO:0000269|PubMed:24216110}.
|
Homo sapiens (Human)
|
O75817
|
POP7_HUMAN
|
MAENREPRGAVEAELDPVEYTLRKRLPSRLPRRPNDIYVNMKTDFKAQLARCQKLLDGGARGQNACSEIYIHGLGLAINRAINIALQLQAGSFGSLQVAANTSTVELVDELEPETDTREPLTRIRNNSAIHIRVFRVTPK
| null | null |
rRNA processing [GO:0006364]; tRNA 5'-leader removal [GO:0001682]; tRNA processing [GO:0008033]
|
cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; multimeric ribonuclease P complex [GO:0030681]; nucleolar ribonuclease P complex [GO:0005655]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonuclease MRP complex [GO:0000172]
|
ribonuclease P activity [GO:0004526]; ribonuclease P RNA binding [GO:0033204]; RNA binding [GO:0003723]
|
PF12328;
|
3.30.110.20;
|
Histone-like Alba family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14715275, ECO:0000269|PubMed:20215441}. Cytoplasm {ECO:0000269|PubMed:14715275}. Cytoplasmic granule {ECO:0000269|PubMed:14715275}. Note=Under stress conditions colocalizes with SMN1 in punctuated cytoplasmic granules. {ECO:0000269|PubMed:14715275}.
| null | null | null | null | null |
FUNCTION: Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends (PubMed:30454648, PubMed:9630247). Also a component of the MRP ribonuclease complex, which cleaves pre-rRNA sequences (PubMed:28115465). {ECO:0000269|PubMed:28115465, ECO:0000269|PubMed:30454648, ECO:0000269|PubMed:9630247}.
|
Homo sapiens (Human)
|
O75818
|
RPP40_HUMAN
|
MATLRRLREAPRHLLVCEKSNFGNHKSRHRHLVQTHYYNYRVSFLIPECGILSEELKNLVMNTGPYYFVKNLPLHELITPEFISTFIKKGSCYALTYNTHIDEDNTVALLPNGKLILSLDKDTYEETGLQGHPSQFSGRKIMKFIVSIDLMELSLNLDSKKYERISWSFKEKKPLKFDFLLAWHKTGSEESTMMSYFSKYQIQEHQPKVALSTLRDLQCPVLQSSELEGTPEVSCRALELFDWLGAVFSNVDLNNEPNNFISTYCCPEPSTVVAKAYLCTITGFILPEKICLLLEHLCHYFDEPKLAPWVTLSVQGFADSPVSWEKNEHGFRKGGEHLYNFVIFNNQDYWLQMAVGANDHCPP
| null | null |
endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000447]; tRNA 5'-leader removal [GO:0001682]
|
multimeric ribonuclease P complex [GO:0030681]; nucleolar ribonuclease P complex [GO:0005655]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonuclease MRP complex [GO:0000172]
|
ribonuclease MRP activity [GO:0000171]; ribonuclease P activity [GO:0004526]; ribonuclease P RNA binding [GO:0033204]
|
PF08584;
| null | null | null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends (PubMed:30454648, PubMed:9630247). Also a component of the MRP ribonuclease complex, which cleaves pre-rRNA sequences (PubMed:28115465). {ECO:0000269|PubMed:28115465, ECO:0000269|PubMed:30454648, ECO:0000269|PubMed:9630247}.
|
Homo sapiens (Human)
|
O75821
|
EIF3G_HUMAN
|
MPTGDFDSKPSWADQVEEEGEDDKCVTSELLKGIPLATGDTSPEPELLPGAPLPPPKEVINGNIKTVTEYKIDEDGKKFKIVRTFRIETRKASKAVARRKNWKKFGNSEFDPPGPNVATTTVSDDVSMTFITSKEDLNCQEEEDPMNKLKGQKIVSCRICKGDHWTTRCPYKDTLGPMQKELAEQLGLSTGEKEKLPGELEPVQATQNKTGKYVPPSLRDGASRRGESMQPNRRADDNATIRVTNLSEDTRETDLQELFRPFGSISRIYLAKDKTTGQSKGFAFISFHRREDAARAIAGVSGFGYDHLILNVEWAKPSTN
| null | null |
formation of cytoplasmic translation initiation complex [GO:0001732]; translational initiation [GO:0006413]; viral translational termination-reinitiation [GO:0075525]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; perinuclear region of cytoplasm [GO:0048471]
|
RNA binding [GO:0003723]; translation initiation factor activity [GO:0003743]
|
PF12353;PF00076;
|
3.30.70.330;
|
EIF-3 subunit G family
|
PTM: Phosphorylated. Phosphorylation is enhanced upon serum stimulation. {ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:17322308}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03006}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:17094969}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:17094969}. Note=Colocalizes with AIFM1 in the nucleus and perinuclear region.
| null | null | null | null | null |
FUNCTION: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). This subunit can bind 18S rRNA. {ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}.; FUNCTION: (Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426). {ECO:0000269|PubMed:18056426}.
|
Homo sapiens (Human)
|
O75822
|
EIF3J_HUMAN
|
MAAAAAAAGDSDSWDADAFSVEDPVRKVGGGGTAGGDRWEGEDEDEDVKDNWDDDDDEKKEEAEVKPEVKISEKKKIAEKIKEKERQQKKRQEEIKKRLEEPEEPKVLTPEEQLADKLRLKKLQEESDLELAKETFGVNNAVYGIDAMNPSSRDDFTEFGKLLKDKITQYEKSLYYASFLEVLVRDVCISLEIDDLKKITNSLTVLCSEKQKQEKQSKAKKKKKGVVPGGGLKATMKDDLADYGGYDGGYVQDYEDFM
| null | null |
formation of cytoplasmic translation initiation complex [GO:0001732]; translational initiation [GO:0006413]
|
cytosol [GO:0005829]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]
|
identical protein binding [GO:0042802]; translation initiation factor activity [GO:0003743]
|
PF08597;
|
1.10.246.60;
|
EIF-3 subunit J family
|
PTM: Phosphorylated. Phosphorylation is enhanced upon serum stimulation. {ECO:0000255|HAMAP-Rule:MF_03009, ECO:0000269|PubMed:17322308}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03009}.
| null | null | null | null | null |
FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). {ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}.
|
Homo sapiens (Human)
|
O75828
|
CBR3_HUMAN
|
MSSCSRVALVTGANRGIGLAIARELCRQFSGDVVLTARDVARGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLNVLVNNAAVAFKSDDPMPFDIKAEMTLKTNFFATRNMCNELLPIMKPHGRVVNISSLQCLRAFENCSEDLQERFHSETLTEGDLVDLMKKFVEDTKNEVHEREGWPNSPYGVSKLGVTVLSRILARRLDEKRKADRILVNACCPGPVKTDMDGKDSIRTVEEGAETPVYLALLPPDATEPQGQLVHDKVVQNW
|
1.1.1.184; 1.6.5.10
| null |
cognition [GO:0050890]; phylloquinone catabolic process [GO:0042376]; xenobiotic metabolic process [GO:0006805]
|
cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]
|
3-keto sterol reductase activity [GO:0000253]; carbonyl reductase (NADPH) activity [GO:0004090]; NADPH binding [GO:0070402]; NADPH dehydrogenase (quinone) activity [GO:0008753]
|
PF00106;
|
3.40.50.720;
|
Short-chain dehydrogenases/reductases (SDR) family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18493841}.
|
CATALYTIC ACTIVITY: Reaction=a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH; Xref=Rhea:RHEA:19257, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087, ChEBI:CHEBI:35681, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.184; Evidence={ECO:0000269|PubMed:18493841}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19259; Evidence={ECO:0000305|PubMed:18493841}; CATALYTIC ACTIVITY: Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+); Xref=Rhea:RHEA:46164, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124; EC=1.6.5.10; Evidence={ECO:0000269|PubMed:15537833, ECO:0000269|PubMed:18493841, ECO:0000269|PubMed:19841672}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46165; Evidence={ECO:0000305|PubMed:19841672};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=25 uM for menadione {ECO:0000269|PubMed:15537833}; KM=43 uM for menadione {ECO:0000269|PubMed:18493841}; KM=300 uM for 4-benzoylpyridine {ECO:0000269|PubMed:18493841}; KM=130 uM for 4-nitorobenzaldehyde {ECO:0000269|PubMed:18493841}; KM=420 uM for 1,2-naphthoquinone {ECO:0000269|PubMed:19841672}; KM=14630 uM for isatin {ECO:0000269|PubMed:19841672}; KM=140 uM for oracin {ECO:0000269|PubMed:19841672}; KM=90 uM for NADPH {ECO:0000269|PubMed:15537833}; KM=38 uM for NADPH {ECO:0000269|PubMed:18493841}; Vmax=6 umol/min/mg enzyme with 1,2-naphthoquinone as substrate {ECO:0000269|PubMed:19841672}; Vmax=0.1 umol/min/mg enzyme with oracin as substrate {ECO:0000269|PubMed:19841672}; Vmax=15 umol/min/mg enzyme with isatin as substrate {ECO:0000269|PubMed:19841672}; Note=kcat is 0.55 min(-1) with menadione as substrate (PubMed:18493841). kcat is 0.70 min(-1) with 4-benzoylpyridine as substrate (PubMed:18493841). kcat is 0.59 min(-1) with 4-nitorobenzaldehyde as substrate (PubMed:18493841). {ECO:0000269|PubMed:18493841};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5-7. {ECO:0000269|PubMed:15537833, ECO:0000269|PubMed:18493841};
| null |
FUNCTION: Catalyzes the NADPH-dependent reduction of carbonyl compounds to their corresponding alcohols (PubMed:18493841). Has low NADPH-dependent oxidoreductase activity. Acts on several orthoquinones, acts as well on non-quinone compounds, such as isatin or on the anticancer drug oracin (PubMed:15537833, PubMed:18493841, PubMed:19841672). Best substrates for CBR3 is 1,2- naphthoquinone, hence could play a role in protection against cytotoxicity of exogenous quinones (PubMed:19841672). Exerts activity toward ortho-quinones but not paraquinones. No endogenous substrate for CBR3 except isatin has been identified (PubMed:19841672). {ECO:0000269|PubMed:15537833, ECO:0000269|PubMed:18493841, ECO:0000269|PubMed:19841672}.
|
Homo sapiens (Human)
|
O75829
|
CNMD_HUMAN
|
MTENSDKVPIALVGPDDVEFCSPPAYATLTVKPSSPARLLKVGAVVLISGAVLLLFGAIGAFYFWKGSDSHIYNVHYTMSINGKLQDGSMEIDAGNNLETFKMGSGAEEAIAVNDFQNGITGIRFAGGEKCYIKAQVKARIPEVGAVTKQSISSKLEGKIMPVKYEENSLIWVAVDQPVKDNSFLSSKVLELCGDLPIFWLKPTYPKEIQRERREVVRKIVPTTTKRPHSGPRSNPGAGRLNNETRPSVQEDSQAFNPDNPYHQQEGESMTFDPRLDHEGICCIECRRSYTHCQKICEPLGGYYPWPYNYQGCRSACRVIMPCSWWVARILGMV
| null | null |
cartilage development [GO:0051216]; cell differentiation [GO:0030154]; negative regulation of angiogenesis [GO:0016525]; negative regulation of endothelial cell proliferation [GO:0001937]; proteoglycan metabolic process [GO:0006029]; skeletal system development [GO:0001501]
|
endomembrane system [GO:0012505]; extracellular region [GO:0005576]; membrane [GO:0016020]
| null |
PF04089;
|
3.30.390.150;
|
Chondromodulin-1 family
|
PTM: After cleavage, the post-translationally modified ChM-I is secreted as a glycoprotein.
|
SUBCELLULAR LOCATION: [Chondromodulin-1]: Secreted, extracellular space, extracellular matrix. Note=Accumulated in the inter-territorial matrix of cartilage.; SUBCELLULAR LOCATION: [Chondrosurfactant protein]: Endomembrane system {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Bifunctional growth regulator that stimulates the growth of cultured chondrocytes in the presence of basic fibroblast growth factor (FGF) but inhibits the growth of cultured vascular endothelial cells. May contribute to the rapid growth of cartilage and vascular invasion prior to the replacement of cartilage by bone during endochondral bone development. Inhibits in vitro tube formation and mobilization of endothelial cells. Plays a role as antiangiogenic factor in cardiac valves to suppress neovascularization. {ECO:0000269|PubMed:16980969}.
|
Homo sapiens (Human)
|
O75832
|
PSD10_HUMAN
|
MEGCVSNLMVCNLAYSGKLEELKESILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKALLGKGAQVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKGNLKMIHILLYYKASTNIQDTEGNTPLHLACDEERVEEAKLLVSQGASIYIENKEEKTPLQVAKGGLGLILKRMVEG
| null | null |
apoptotic process [GO:0006915]; cytoplasmic sequestering of NF-kappaB [GO:0007253]; negative regulation of apoptotic process [GO:0043066]; negative regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043518]; negative regulation of MAPK cascade [GO:0043409]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell growth [GO:0030307]; positive regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045737]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of telomere capping [GO:1904355]; proteasome regulatory particle assembly [GO:0070682]; protein localization to chromosome, telomeric region [GO:0070198]; protein localization to plasma membrane [GO:0072659]; regulation of transcription by RNA polymerase II [GO:0006357]
|
cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; intermediate filament cytoskeleton [GO:0045111]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; proteasome complex [GO:0000502]
|
cytoskeletal protein binding [GO:0008092]; NAD+ ADP-ribosyltransferase activity [GO:0003950]; protein-macromolecule adaptor activity [GO:0030674]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription factor binding [GO:0008134]; transmembrane transporter binding [GO:0044325]
|
PF00023;PF12796;
|
1.25.40.20;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18040287}. Nucleus {ECO:0000269|PubMed:18040287}.
| null | null | null | null | null |
FUNCTION: Acts as a chaperone during the assembly of the 26S proteasome, specifically of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD10:PSMC4:PSMC5:PAAF1 module which probably assembles with a PSMD5:PSMC2:PSMC1:PSMD2 module. Independently of the proteasome, regulates EGF-induced AKT activation through inhibition of the RHOA/ROCK/PTEN pathway, leading to prolonged AKT activation. Plays an important role in RAS-induced tumorigenesis.; FUNCTION: Acts as an proto-oncoprotein by being involved in negative regulation of tumor suppressors RB1 and p53/TP53. Overexpression is leading to phosphorylation of RB1 and proteasomal degradation of RB1. Regulates CDK4-mediated phosphorylation of RB1 by competing with CDKN2A for binding with CDK4. Facilitates binding of MDM2 to p53/TP53 and the mono- and polyubiquitination of p53/TP53 by MDM2 suggesting a function in targeting the TP53:MDM2 complex to the 26S proteasome. Involved in p53-independent apoptosis. Involved in regulation of NF-kappa-B by retaining it in the cytoplasm. Binds to the NF-kappa-B component RELA and accelerates its XPO1/CRM1-mediated nuclear export.
|
Homo sapiens (Human)
|
O75838
|
CIB2_HUMAN
|
MGNKQTIFTEEQLDNYQDCTFFNKKDILKLHSRFYELAPNLVPMDYRKSPIVHVPMSLIIQMPELRENPFKERIVAAFSEDGEGNLTFNDFVDMFSVLCESAPRELKANYAFKIYDFNTDNFICKEDLELTLARLTKSELDEEEVVLVCDKVIEEADLDGDGKLGFADFEDMIAKAPDFLSTFHIRI
| null | null |
calcium ion homeostasis [GO:0055074]; cellular response to ATP [GO:0071318]; photoreceptor cell maintenance [GO:0045494]; positive regulation of cytosolic calcium ion concentration [GO:0007204]
|
blood microparticle [GO:0072562]; cell periphery [GO:0071944]; cuticular plate [GO:0032437]; cytoplasm [GO:0005737]; muscle tendon junction [GO:0005927]; neuromuscular junction [GO:0031594]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750]; sarcolemma [GO:0042383]; stereocilium [GO:0032420]
|
calcium ion binding [GO:0005509]; integrin binding [GO:0005178]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803]
|
PF13499;
|
1.10.238.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Z309}. Cell projection, stereocilium {ECO:0000269|PubMed:26173970, ECO:0000269|PubMed:26426422}. Photoreceptor inner segment {ECO:0000250|UniProtKB:Q9Z309}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:Q9Z309}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q9Z309}. Note=Colocalizes with ITGA7 at the myotendinous junctions (MTJ) and at the neuromuscular junctions (NMJ) (By similarity). Located mainly in stereocilia and at the apical surface of hair cells of the cochlea (By similarity). Localizes in the cuticular plate along and at the tip of the stereocilia of vestibular sensory hair cells (PubMed:26173970, PubMed:26426422). {ECO:0000250|UniProtKB:Q9Z309, ECO:0000269|PubMed:26173970, ECO:0000269|PubMed:26426422}.
| null | null | null | null | null |
FUNCTION: Calcium- and integrin-binding protein that plays a role in intracellular calcium homeostasis (By similarity). Acts as an auxiliary subunit of the sensory mechanoelectrical transduction (MET) channel in hair cells (By similarity). Essential for mechanoelectrical transduction (MET) currents in auditory hair cells and thereby required for hearing (By similarity). Regulates the function of hair cell mechanotransduction by controlling the distribution of transmembrane channel-like proteins TMC1 and TMC2, and by regulating the function of the MET channels in hair cells (By similarity). Required for the maintenance of auditory hair cell stereocilia bundle morphology and function and for hair-cell survival in the cochlea (By similarity). Critical for proper photoreceptor cell maintenance and function (By similarity). Plays a role in intracellular calcium homeostasis by decreasing ATP-induced calcium release (PubMed:23023331, PubMed:26173970, PubMed:26426422). {ECO:0000250|UniProtKB:Q9Z309, ECO:0000269|PubMed:23023331, ECO:0000269|PubMed:26173970, ECO:0000269|PubMed:26426422}.
|
Homo sapiens (Human)
|
O75840
|
KLF7_HUMAN
|
MDVLASYSIFQELQLVHDTGYFSALPSLEETWQQTCLELERYLQTEPRRISETFGEDLDCFLHASPPPCIEESFRRLDPLLLPVEAAICEKSSAVDILLSRDKLLSETCLSLQPASSSLDSYTAVNQAQLNAVTSLTPPSSPELSRHLVKTSQTLSAVDGTVTLKLVAKKAALSSVKVGGVATAAAAVTAAGAVKSGQSDSDQGGLGAEACPENKKRVHRCQFNGCRKVYTKSSHLKAHQRTHTGEKPYKCSWEGCEWRFARSDELTRHYRKHTGAKPFKCNHCDRCFSRSDHLALHMKRHI
| null | null |
axon guidance [GO:0007411]; axonogenesis [GO:0007409]; dendrite morphogenesis [GO:0048813]; glucose homeostasis [GO:0042593]; negative regulation of adipose tissue development [GO:1904178]; negative regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061179]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of epidermal cell differentiation [GO:0045604]; regulation of transcription by RNA polymerase II [GO:0006357]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270]
|
PF00096;
|
3.30.160.60;
|
Krueppel C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9774444}.
| null | null | null | null | null |
FUNCTION: Transcriptional factor (PubMed:16339272, PubMed:9774444). Plays a critical role in neuronal morphogenesis and survival of sensory neurons (By similarity). Represses the corneal epithelium differentiation (PubMed:28916725). Acts also as a metabolic regulator, by modulating insulin sensitivity in pancreatic beta cells and skeletal muscle cells (PubMed:16339272). Inhibits transcriptional inducers of adipogenesis and has a repressive role in the expression of several adipokines, including leptin (PubMed:16339272). {ECO:0000250|UniProtKB:Q99JB0, ECO:0000269|PubMed:16339272, ECO:0000269|PubMed:28916725, ECO:0000269|PubMed:9774444}.
|
Homo sapiens (Human)
|
O75841
|
UPK1B_HUMAN
|
MAKDNSTVRCFQGLLIFGNVIIGCCGIALTAECIFFVSDQHSLYPLLEATDNDDIYGAAWIGIFVGICLFCLSVLGIVGIMKSSRKILLAYFILMFIVYAFEVASCITAATQQDFFTPNLFLKQMLERYQNNSPPNNDDQWKNNGVTKTWDRLMLQDNCCGVNGPSDWQKYTSAFRTENNDADYPWPRQCCVMNNLKEPLNLEACKLGVPGFYHNQGCYELISGPMNRHAWGVAWFGFAILCWTFWVLLGTMFYWSRIEY
| null | null |
epithelial cell differentiation [GO:0030855]; response to bacterium [GO:0009617]
|
apical plasma membrane urothelial plaque [GO:0120001]; extracellular exosome [GO:0070062]; membrane [GO:0016020]
|
structural molecule activity [GO:0005198]
|
PF00335;
|
1.10.1450.10;
|
Tetraspanin (TM4SF) family
|
PTM: N-glycosylated with high-mannose oligosaccharides. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in normal bladder epithelial physiology, possibly in regulating membrane permeability of superficial umbrella cells or in stabilizing the apical membrane through AUM/cytoskeletal interactions (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O75843
|
AP1G2_HUMAN
|
MVVPSLKLQDLIEEIRGAKTQAQEREVIQKECAHIRASFRDGDPVHRHRQLAKLLYVHMLGYPAHFGQMECLKLIASSRFTDKRVGYLGAMLLLDERHDAHLLITNSIKNDLSQGIQPVQGLALCTLSTMGSAEMCRDLAPEVEKLLLQPSPYVRKKAILTAVHMIRKVPELSSVFLPPCAQLLHERHHGILLGTITLITELCERSPAALRHFRKVVPQLVHILRTLVTMGYSTEHSISGVSDPFLQVQILRLLRILGRNHEESSETMNDLLAQVATNTDTSRNAGNAVLFETVLTIMDIRSAAGLRVLAVNILGRFLLNSDRNIRYVALTSLLRLVQSDHSAVQRHRPTVVECLRETDASLSRRALELSLALVNSSNVRAMMQELQAFLESCPPDLRADCASGILLAAERFAPTKRWHIDTILHVLTTAGTHVRDDAVANLTQLIGGAQELHAYSVRRLYNALAEDISQQPLVQVAAWCIGEYGDLLLAGNCEEIEPLQVDEEEVLALLEKVLQSHMSLPATRGYALTALMKLSTRLCGDNNRIRQVVSIYGSCLDVELQQRAVEYDTLFRKYDHMRAAILEKMPLVERDGPQADEEAKESKEAAQLSEAAPVPTEPQASQLLDLLDLLDGASGDVQHPPHLDPSPGGALVHLLDLPCVPPPPAPIPDLKVFEREGVQLNLSFIRPPENPALLLITITATNFSEGDVTHFICQAAVPKSLQLQLQAPSGNTVPARGGLPITQLFRILNPNKAPLRLKLRLTYDHFHQSVQEIFEVNNLPVESWQ
| null | null |
Golgi to vacuole transport [GO:0006896]; intracellular protein transport [GO:0006886]; vesicle-mediated transport [GO:0016192]
|
AP-1 adaptor complex [GO:0030121]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi-associated vesicle [GO:0005798]; membrane [GO:0016020]; transport vesicle [GO:0030133]
|
clathrin adaptor activity [GO:0035615]
|
PF01602;PF02883;
|
2.60.40.1230;1.25.10.10;
|
Adaptor complexes large subunit family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:11333915, ECO:0000269|PubMed:9762922}; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:11333915}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:9733768}; Peripheral membrane protein. Endosome membrane {ECO:0000269|PubMed:16867982}; Peripheral membrane protein. Note=Mainly localized to perinuclear vesicular structures (PubMed:9733768). Colocalizes with HBV major surface antigen L and HBV core protein C in CD63-containing compartments (PubMed:16867982). Colocalizes with HBV major surface antigen L to cis-Golgi-like structures (PubMed:11333915).
| null | null | null | null | null |
FUNCTION: May function in protein sorting in late endosomes or multivesucular bodies (MVBs). {ECO:0000269|PubMed:9733768}.; FUNCTION: (Microbial infection) Involved in MVB-assisted maturation of hepatitis B virus (HBV). {ECO:0000269|PubMed:16867982, ECO:0000269|PubMed:17553870}.
|
Homo sapiens (Human)
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.