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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O95613
|
PCNT_HUMAN
|
MEVEQEQRRRKVEAGRTKLAHFRQRKTKGDSSHSEKKTAKRKGSAVDASVQEESPVTKEDSALCGGGDICKSTSCDDTPDGAGGAFAAQPEDCDGEKREDLEQLQQKQVNDHPPEQCGMFTVSDHPPEQHGMFTVGDHPPEQRGMFTVSDHPPEQHGMFTVSDHPPEQRGMFTISDHQPEQRGMFTVSDHTPEQRGIFTISDHPAEQRGMFTKECEQECELAITDLESGREDEAGLHQSQAVHGLELEALRLSLSNMHTAQLELTQANLQKEKETALTELREMLNSRRAQELALLQSRQQHELELLREQHAREKEEVVLRCGQEAAELKEKLQSEMEKNAQIVKTLKEDWESEKDLCLENLRKELSAKHQSEMEDLQNQFQKELAEQRAELEKIFQDKNQAERALRNLESHHQAAIEKLREDLQSEHGRCLEDLEFKFKESEKEKQLELENLQASYEDLKAQSQEEIRRLWSQLDSARTSRQELSELHEQLLARTSRVEDLEQLKQREKTQHESELEQLRIYFEKKLRDAEKTYQEDLTLLQQRLQGAREDALLDSVEVGLSCVGLEEKPEKGRKDHVDELEPERHKESLPRFQAELEESHRHQLEALESPLCIQHEGHVSDRCCVETSALGHEWRLEPSEGHSQELPWVHLQGVQDGDLEADTERAARVLGLETEHKVQLSLLQTELKEEIELLKIENRNLYGKLQHETRLKDDLEKVKHNLIEDHQKELNNAKQKTELMKQEFQRKETDWKVMKEELQREAEEKLTLMLLELREKAESEKQTIINKFELREAEMRQLQDQQAAQILDLERSLTEQQGRLQQLEQDLTSDDALHCSQCGREPPTAQDGELAALHVKEDCALQLMLARSRFLEERKEITEKFSAEQDAFLQEAQEQHARELQLLQERHQQQLLSVTAELEARHQAALGELTASLESKQGALLAARVAELQTKHAADLGALETRHLSSLDSLESCYLSEFQTIREEHRQALELLRADFEEQLWKKDSLHQTILTQELEKLKRKHEGELQSVRDHLRTEVSTELAGTVAHELQGVHQGEFGSEKKTALHEKEETLRLQSAQAQPFHQEEKESLSLQLQKKNHQVQQLKDQVLSLSHEIEECRSELEVLQQRRERENREGANLLSMLKADVNLSHSERGALQDALRRLLGLFGETLRAAVTLRSRIGERVGLCLDDAGAGLALSTAPALEETWSDVALPELDRTLSECAEMSSVAEISSHMRESFLMSPESVRECEQPIRRVFQSLSLAVDGLMEMALDSSRQLEEARQIHSRFEKEFSFKNEETAQVVRKHQELLECLKEESAAKAELALELHKTQGTLEGFKVETADLKEVLAGKEDSEHRLVLELESLRRQLQQAAQEQAALREECTRLWSRGEATATDAEAREAALRKEVEDLTKEQSETRKQAEKDRSALLSQMKILESELEEQLSQHRGCAKQAEAVTALEQQVASLDKHLRNQRQFMDEQAAEREHEREEFQQEIQRLEGQLRQAAKPQPWGPRDSQQAPLDGEVELLQQKLREKLDEFNELAIQKESADRQVLMQEEEIKRLEEMNINIRKKVAQLQEEVEKQKNIVKGLEQDKEVLKKQQMSSLLLASTLQSTLDAGRCPEPPSGSPPEGPEIQLEVTQRALLRRESEVLDLKEQLEKMKGDLESKNEEILHLNLKLDMQNSQTAVSLRELEEENTSLKVIYTRSSEIEELKATIENLQENQKRLQKEKAEEIEQLHEVIEKLQHELSLMGPVVHEVSDSQAGSLQSELLCSQAGGPRGQALQGELEAALEAKEALSRLLADQERRHSQALEALQQRLQGAEEAAELQLAELERNVALREAEVEDMASRIQEFEAALKAKEATIAERNLEIDALNQRKAAHSAELEAVLLALARIRRALEQQPLAAGAAPPELQWLRAQCARLSRQLQVLHQRFLRCQVELDRRQARRATAHTRVPGAHPQPRMDGGAKAQVTGDVEASHDAALEPVVPDPQGDLQPVLVTLKDAPLCKQEGVMSVLTVCQRQLQSELLLVKNEMRLSLEDGGKGKEKVLEDCQLPKVDLVAQVKQLQEKLNRLLYSMTFQNVDAADTKSLWPMASAHLLESSWSDDSCDGEEPDISPHIDTCDANTATGGVTDVIKNQAIDACDANTTPGGVTDVIKNWDSLIPDEMPDSPIQEKSECQDMSLSSPTSVLGGSRHQSHTAEAGPRKSPVGMLDLSSWSSPEVLRKDWTLEPWPSLPVTPHSGALSLCSADTSLGDRADTSLPQTQGPGLLCSPGVSAAALALQWAESPPADDHHVQRTAVEKDVEDFITTSFDSQETLSSPPPGLEGKADRSEKSDGSGFGARLSPGSGGPEAQTAGPVTPASISGRFQPLPEAMKEKEVRPKHVKALLQMVRDESHQILALSEGLAPPSGEPHPPRKEDEIQDISLHGGKTQEVPTACPDWRGDLLQVVQEAFEKEQEMQGVELQPRLSGSDLGGHSSLLERLEKIIREQGDLQEKSLEHLRLPDRSSLLSEIQALRAQLRMTHLQNQEKLQHLRTALTSAEARGSQQEHQLRRQVELLAYKVEQEKCIAGDLQKTLSEEQEKANSVQKLLAAEQTVVRDLKSDLCESRQKSEQLSRSLCEVQQEVLQLRSMLSSKENELKAALQELESEQGKGRALQSQLEEEQLRHLQRESQSAKALEELRASLETQRAQSSRLCVALKHEQTAKDNLQKELRIEHSRCEALLAQERSQLSELQKDLAAEKSRTLELSEALRHERLLTEQLSQRTQEACVHQDTQAHHALLQKLKEEKSRVVDLQAMLEKVQQQALHSQQQLEAEAQKHCEALRREKEVSATLKSTVEALHTQKRELRCSLEREREKPAWLQAELEQSHPRLKEQEGRKAARRSAEARQSPAAAEQWRKWQRDKEKLRELELQRQRDLHKIKQLQQTVRDLESKDEVPGSRLHLGSARRAAGSDADHLREQQRELEAMRQRLLSAARLLTSFTSQAVDRTVNDWTSSNEKAVMSLLHTLEELKSDLSRPTSSQKKMAAELQFQFVDVLLKDNVSLTKALSTVTQEKLELSRAVSKLEKLLKHHLQKGCSPSRSERSAWKPDETAPQSSLRRPDPGRLPPAASEEAHTSNVKMEKLYLHYLRAESFRKALIYQKKYLLLLIGGFQDSEQETLSMIAHLGVFPSKAERKITSRPFTRFRTAVRVVIAILRLRFLVKKWQEVDRKGALAQGKAPRPGPRARQPQSPPRTRESPPTRDVPSGHTRDPARGRRLAAAASPHSGGRATPSPNSRLERSLTASQDPEHSLTEYIHHLEVIQQRLGGVLPDSTSKKSCHPMIKQ
| null | null |
cilium assembly [GO:0060271]; microtubule cytoskeleton organization [GO:0000226]; mitotic spindle organization [GO:0007052]; positive regulation of intracellular protein transport [GO:0090316]; signal transduction [GO:0007165]
|
centriolar satellite [GO:0034451]; centriole [GO:0005814]; centrosome [GO:0005813]; cytosol [GO:0005829]; membrane [GO:0016020]; microtubule [GO:0005874]
|
calmodulin binding [GO:0005516]; molecular adaptor activity [GO:0060090]
|
PF10495;
| null | null |
PTM: Cleaved during mitotis which leads to removal of CDK5RAP2 from the centrosome and promotes centriole disengagement and subsequent centriole separation (PubMed:22722493, PubMed:25503564). The C-terminal fragment is rapidly degraded following cleavage (PubMed:22722493). {ECO:0000269|PubMed:22722493, ECO:0000269|PubMed:25503564}.; PTM: Ubiquitinated by TRIM43; leading to proteasomal degradation. {ECO:0000269|PubMed:30420784}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:10823944, ECO:0000269|PubMed:11171385, ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:18955030, ECO:0000269|PubMed:22797915, ECO:0000269|PubMed:27137183, ECO:0000269|PubMed:30420784}. Note=Centrosomal at all stages of the cell cycle. Remains associated with centrosomes following microtubule depolymerization. Colocalized with DISC1 at the centrosome.
| null | null | null | null | null |
FUNCTION: Integral component of the filamentous matrix of the centrosome involved in the initial establishment of organized microtubule arrays in both mitosis and meiosis. Plays a role, together with DISC1, in the microtubule network formation. Is an integral component of the pericentriolar material (PCM). May play an important role in preventing premature centrosome splitting during interphase by inhibiting NEK2 kinase activity at the centrosome. {ECO:0000269|PubMed:10823944, ECO:0000269|PubMed:11171385, ECO:0000269|PubMed:18955030, ECO:0000269|PubMed:20599736, ECO:0000269|PubMed:30420784}.
|
Homo sapiens (Human)
|
O95619
|
YETS4_HUMAN
|
MFKRMAEFGPDSGGRVKGVTIVKPIVYGNVARYFGKKREEDGHTHQWTVYVKPYRNEDMSAYVKKIQFKLHESYGNPLRVVTKPPYEITETGWGEFEIIIKIFFIDPNERPVTLYHLLKLFQSDTNAMLGKKTVVSEFYDEMIFQDPTAMMQQLLTTSRQLTLGAYKHETEFAELEVKTREKLEAAKKKTSFEIAELKERLKASRETINCLKNEIRKLEEDDQAKDI
| null | null |
chromatin remodeling [GO:0006338]; mitotic cell cycle [GO:0000278]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of double-strand break repair via homologous recombination [GO:1905168]; regulation of apoptotic process [GO:0042981]; regulation of cell cycle [GO:0051726]; regulation of DNA-templated transcription [GO:0006355]; regulation of double-strand break repair [GO:2000779]; regulation of transcription by RNA polymerase II [GO:0006357]
|
NuA4 histone acetyltransferase complex [GO:0035267]; nuclear matrix [GO:0016363]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634]
|
histone binding [GO:0042393]; lysine-acetylated histone binding [GO:0070577]; modification-dependent protein binding [GO:0140030]; structural constituent of cytoskeleton [GO:0005200]
|
PF03366;
|
2.60.40.1970;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00376, ECO:0000269|PubMed:10913114, ECO:0000269|PubMed:18445686}.
| null | null | null | null | null |
FUNCTION: Chromatin reader component of the NuA4 histone acetyltransferase (HAT) complex, a complex involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A (PubMed:12963728, PubMed:14966270). Specifically recognizes and binds acylated histone H3, with a preference for histone H3 diacetylated at 'Lys-18' and 'Lys-27' (H3K18ac and H3K27ac) or histone H3 diacetylated at 'Lys-14' and 'Lys-27' (H3K14ac and H3K27ac) (PubMed:29437725, PubMed:29900004, PubMed:30071723). Also able to recognize and bind crotonylated histone H3 (PubMed:30071723). May also recognize and bind histone H3 succinylated at 'Lys-122' (H3K122succ); additional evidences are however required to confirm this result in vivo (PubMed:29463709). Plays a key role in histone variant H2AZ1/H2A.Z deposition into specific chromatin regions: recognizes and binds H3K14ac and H3K27ac on the promoters of actively transcribed genes and recruits NuA4-related complex to deposit H2AZ1/H2A.Z (PubMed:29437725). H2AZ1/H2A.Z deposition is required for maintenance of embryonic stem cell (By similarity). {ECO:0000250|UniProtKB:Q9CR11, ECO:0000269|PubMed:12963728, ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:29437725, ECO:0000269|PubMed:29463709, ECO:0000269|PubMed:29900004, ECO:0000269|PubMed:30071723}.
|
Homo sapiens (Human)
|
O95622
|
ADCY5_HUMAN
|
MSGSKSVSPPGYAAQKTAAPAPRGGPEHRSAWGEADSRANGYPHAPGGSARGSTKKPGGAVTPQQQQRLASRWRSDDDDDPPLSGDDPLAGGFGFSFRSKSAWQERGGDDCGRGSRRQRRGAASGGSTRAPPAGGGGGSAAAAASAGGTEVRPRSVEVGLEERRGKGRAADELEAGAVEGGEGSGDGGSSADSGSGAGPGAVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQSSLTMLMAVLVLVCLVMLAFHAARPPLQLPYLAVLAAAVGVILIMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSALHLAIALRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYEVEPGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAKMNRQRTNSIGHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDKNAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLTFREPDLEKKYSKQVDDRFGAYVACASLVFLFICFVQITIVPHSIFMLSFYLTCSLLLTLVVFVSVIYSCVKLFPSPLQTLSRKIVRSKMNSTLVGVFTITLVFLAAFVNMFTCNSRDLLGCLAQEHNISASQVNACHVAESAVNYSLGDEQGFCGSPWPNCNFPEYFTYSVLLSLLACSVFLQISCIGKLVLMLAIELIYVLIVEVPGVTLFDNADLLVTANAIDFFNNGTSQCPEHATKVALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKLQATEEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIISEDRFRQLEKIKTIGSTYMAASGLNDSTYDKVGKTHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNGGPPLS
|
4.6.1.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15385642}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:15385642}; Note=Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). {ECO:0000250|UniProtKB:P30803};
|
adenylate cyclase-activating dopamine receptor signaling pathway [GO:0007191]; adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adenylate cyclase-inhibiting dopamine receptor signaling pathway [GO:0007195]; adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; cAMP biosynthetic process [GO:0006171]; cellular response to forskolin [GO:1904322]; G protein-coupled adenosine receptor signaling pathway [GO:0001973]; intracellular signal transduction [GO:0035556]; locomotory behavior [GO:0007626]; neuromuscular process controlling balance [GO:0050885]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061178]
|
cilium [GO:0005929]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
adenylate cyclase activity [GO:0004016]; adenylate cyclase binding [GO:0008179]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; scaffold protein binding [GO:0097110]
|
PF16214;PF06327;PF00211;
|
3.30.70.1230;
|
Adenylyl cyclase class-4/guanylyl cyclase family
|
PTM: Phosphorylated by RAF1. {ECO:0000269|PubMed:15385642}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15385642, ECO:0000305|PubMed:26206488}; Multi-pass membrane protein. Cell projection, cilium {ECO:0000250|UniProtKB:P84309}.
|
CATALYTIC ACTIVITY: Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1; Evidence={ECO:0000269|PubMed:15385642, ECO:0000269|PubMed:24700542, ECO:0000269|PubMed:26206488};
| null | null | null | null |
FUNCTION: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling (PubMed:15385642, PubMed:24700542, PubMed:26206488). Mediates signaling downstream of ADRB1 (PubMed:24700542). Regulates the increase of free cytosolic Ca(2+) in response to increased blood glucose levels and contributes to the regulation of Ca(2+)-dependent insulin secretion (PubMed:24740569). {ECO:0000269|PubMed:15385642, ECO:0000269|PubMed:24700542, ECO:0000269|PubMed:24740569, ECO:0000269|PubMed:26206488}.
|
Homo sapiens (Human)
|
O95628
|
CNOT4_HUMAN
|
MSRSPDAKEDPVECPLCMEPLEIDDINFFPCTCGYQICRFCWHRIRTDENGLCPACRKPYPEDPAVYKPLSQEELQRIKNEKKQKQNERKQKISENRKHLASVRVVQKNLVFVVGLSQRLADPEVLKRPEYFGKFGKIHKVVINNSTSYAGSQGPSASAYVTYIRSEDALRAIQCVNNVVVDGRTLKASLGTTKYCSYFLKNMQCPKPDCMYLHELGDEAASFTKEEMQAGKHQEYEQKLLQELYKLNPNFLQLSTGSVDKNKNKVTPLQRYDTPIDKPSDSLSIGNGDNSQQISNSDTPSPPPGLSKSNPVIPISSSNHSARSPFEGAVTESQSLFSDNFRHPNPIPSGLPPFPSSPQTSSDWPTAPEPQSLFTSETIPVSSSTDWQAAFGFGSSKQPEDDLGFDPFDVTRKALADLIEKELSVQDQPSLSPTSLQNSSSHTTTAKGPGSGFLHPAAATNANSLNSTFSVLPQRFPQFQQHRAVYNSFSFPGQAARYPWMAFPRNSIMHLNHTANPTSNSNFLDLNLPPQHNTGLGGIPVAGEEEVKVSTMPLSTSSHSLQQGQQPTSLHTTVA
|
2.3.2.27
| null |
nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; protein autoubiquitination [GO:0051865]; protein ubiquitination [GO:0016567]; regulation of megakaryocyte differentiation [GO:0045652]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
CCR4-NOT complex [GO:0030014]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; RNA binding [GO:0003723]; ubiquitin-protein transferase activity [GO:0004842]
|
PF00076;PF14570;
|
3.30.70.330;3.30.40.10;
| null |
PTM: Autoubiquitinated. {ECO:0000269|PubMed:11823428, ECO:0000269|PubMed:15001359}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000269|PubMed:11823428, ECO:0000269|PubMed:26575292, ECO:0000269|PubMed:29861391};
| null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:26575292}.
| null | null |
FUNCTION: Has E3 ubiquitin ligase activity, promoting ubiquitination and degradation of target proteins (PubMed:11823428, PubMed:22159038, PubMed:26575292). Involved in activation of the JAK/STAT pathway (PubMed:11823428, PubMed:22159038). Catalyzes ubiquitination of methylated RBM15 (PubMed:26575292). Plays a role in quality control of translation of mitochondrial outer membrane-localized mRNA (PubMed:29861391). As part of the PINK1-regulated signaling, upon mitochondria damage, ubiquitinates ABCE1 and thereby recruits autophagy receptors to the mitochondrial outer membrane to initiate mitophagy (PubMed:29861391). {ECO:0000269|PubMed:11823428, ECO:0000269|PubMed:22159038, ECO:0000269|PubMed:26575292, ECO:0000269|PubMed:29861391}.
|
Homo sapiens (Human)
|
O95630
|
STABP_HUMAN
|
MSDHGDVSLPPEDRVRALSQLGSAVEVNEDIPPRRYFRSGVEIIRMASIYSEEGNIEHAFILYNKYITLFIEKLPKHRDYKSAVIPEKKDTVKKLKEIAFPKAEELKAELLKRYTKEYTEYNEEKKKEAEELARNMAIQQELEKEKQRVAQQKQQQLEQEQFHAFEEMIRNQELEKERLKIVQEFGKVDPGLGGPLVPDLEKPSLDVFPTLTVSSIQPSDCHTTVRPAKPPVVDRSLKPGALSNSESIPTIDGLRHVVVPGRLCPQFLQLASANTARGVETCGILCGKLMRNEFTITHVLIPKQSAGSDYCNTENEEELFLIQDQQGLITLGWIHTHPTQTAFLSSVDLHTHCSYQMMLPESVAIVCSPKFQETGFFKLTDHGLEEISSCRQKGFHPHSKDPPLFCSCSHVTVVDRAVTITDLR
|
3.4.19.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O35864}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:O35864};
|
hippocampal neuron apoptotic process [GO:0110088]; mitotic cytokinesis [GO:0000281]; negative regulation of hippocampal neuron apoptotic process [GO:0110091]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative regulation of Ras protein signal transduction [GO:0046580]; positive regulation of cell population proliferation [GO:0008284]; protein deubiquitination [GO:0016579]; proteolysis [GO:0006508]; receptor signaling pathway via JAK-STAT [GO:0007259]
|
cleavage furrow [GO:0032154]; cytosol [GO:0005829]; early endosome [GO:0005769]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
deubiquitinase activity [GO:0101005]; K63-linked deubiquitinase activity [GO:0061578]; metal ion binding [GO:0046872]; metal-dependent deubiquitinase activity [GO:0140492]; protein domain specific binding [GO:0019904]
|
PF01398;PF08969;
|
3.40.140.10;1.20.58.80;
|
Peptidase M67C family
|
PTM: Phosphorylated after BMP type I receptor activation. {ECO:0000269|PubMed:11483516}.; PTM: Ubiquitinated by SMURF2 in the presence of RNF11. {ECO:0000269|PubMed:14755250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17261583, ECO:0000305|PubMed:10383417}. Membrane {ECO:0000269|PubMed:17261583}; Peripheral membrane protein {ECO:0000269|PubMed:17261583}. Cytoplasm {ECO:0000269|PubMed:17261583}. Early endosome {ECO:0000269|PubMed:15314065, ECO:0000269|PubMed:17261583}.
| null | null | null | null | null |
FUNCTION: Zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains (PubMed:15314065, PubMed:23542699, PubMed:34425109). Does not cleave 'Lys-48'-linked polyubiquitin chains (PubMed:15314065). Plays a role in signal transduction for cell growth and MYC induction mediated by IL-2 and GM-CSF (PubMed:10383417). Potentiates BMP (bone morphogenetic protein) signaling by antagonizing the inhibitory action of SMAD6 and SMAD7 (PubMed:11483516). Has a key role in regulation of cell surface receptor-mediated endocytosis and ubiquitin-dependent sorting of receptors to lysosomes (PubMed:15314065, PubMed:17261583). Endosomal localization of STAMBP is required for efficient EGFR degradation but not for its internalization (PubMed:15314065, PubMed:17261583). Involved in the negative regulation of PI3K-AKT-mTOR and RAS-MAP signaling pathways (PubMed:23542699). {ECO:0000269|PubMed:10383417, ECO:0000269|PubMed:11483516, ECO:0000269|PubMed:15314065, ECO:0000269|PubMed:17261583, ECO:0000269|PubMed:23542699, ECO:0000269|PubMed:34425109}.
|
Homo sapiens (Human)
|
O95631
|
NET1_HUMAN
|
MMRAVWEALAALAAVACLVGAVRGGPGLSMFAGQAAQPDPCSDENGHPRRCIPDFVNAAFGKDVRVSSTCGRPPARYCVVSERGEERLRSCHLCNASDPKKAHPPAFLTDLNNPHNLTCWQSENYLQFPHNVTLTLSLGKKFEVTYVSLQFCSPRPESMAIYKSMDYGRTWVPFQFYSTQCRKMYNRPHRAPITKQNEQEAVCTDSHTDMRPLSGGLIAFSTLDGRPSAHDFDNSPVLQDWVTATDIRVAFSRLHTFGDENEDDSELARDSYFYAVSDLQVGGRCKCNGHAARCVRDRDDSLVCDCRHNTAGPECDRCKPFHYDRPWQRATAREANECVACNCNLHARRCRFNMELYKLSGRKSGGVCLNCRHNTAGRHCHYCKEGYYRDMGKPITHRKACKACDCHPVGAAGKTCNQTTGQCPCKDGVTGITCNRCAKGYQQSRSPIAPCIKIPVAPPTTAASSVEEPEDCDSYCKASKGKLKINMKKYCKKDYAVQIHILKADKAGDWWKFTVNIISVYKQGTSRIRRGDQSLWIRSRDIACKCPKIKPLKKYLLLGNAEDSPDQSGIVADKSSLVIQWRDTWARRLRKFQQREKKGKCKKA
| null | null |
anterior/posterior axon guidance [GO:0033564]; apoptotic process [GO:0006915]; Cdc42 protein signal transduction [GO:0032488]; cell-cell adhesion [GO:0098609]; chemorepulsion of axon [GO:0061643]; glial cell proliferation [GO:0014009]; inner ear morphogenesis [GO:0042472]; mammary gland duct morphogenesis [GO:0060603]; motor neuron migration [GO:0097475]; negative regulation of axon extension [GO:0030517]; nuclear migration [GO:0007097]; positive regulation of axon extension [GO:0045773]; positive regulation of cell motility [GO:2000147]; positive regulation of glial cell proliferation [GO:0060252]; Ras protein signal transduction [GO:0007265]; regulation of glial cell migration [GO:1903975]; regulation of synapse assembly [GO:0051963]; regulation of transcription by RNA polymerase II [GO:0006357]; substrate adhesion-dependent cell spreading [GO:0034446]; substrate-dependent cell migration, cell extension [GO:0006930]
|
actin cytoskeleton [GO:0015629]; basement membrane [GO:0005604]; cytosol [GO:0005829]; extracellular region [GO:0005576]; nucleoplasm [GO:0005654]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00053;PF00055;PF01759;
|
2.40.50.120;2.60.120.260;2.10.25.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28945198}. Cytoplasm {ECO:0000269|PubMed:28945198}. Note=Mainly secreted. {ECO:0000269|PubMed:28945198}.
| null | null | null | null | null |
FUNCTION: Netrins control guidance of CNS commissural axons and peripheral motor axons. Its association with either DCC or some UNC5 receptors will lead to axon attraction or repulsion, respectively. Binding to UNC5C might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased microtubule dynamics and axon repulsion (PubMed:28483977). Involved in dorsal root ganglion axon projection towards the spinal cord (PubMed:28483977). It also serves as a survival factor via its association with its receptors which prevent the initiation of apoptosis. Involved in tumorigenesis by regulating apoptosis (PubMed:15343335). {ECO:0000269|PubMed:15343335, ECO:0000269|PubMed:28483977}.
|
Homo sapiens (Human)
|
O95633
|
FSTL3_HUMAN
|
MRPGAPGPLWPLPWGALAWAVGFVSSMGSGNPAPGGVCWLQQGQEATCSLVLQTDVTRAECCASGNIDTAWSNLTHPGNKINLLGFLGLVHCLPCKDSCDGVECGPGKACRMLGGRPRCECAPDCSGLPARLQVCGSDGATYRDECELRAARCRGHPDLSVMYRGRCRKSCEHVVCPRPQSCVVDQTGSAHCVVCRAAPCPVPSSPGQELCGNNNVTYISSCHMRQATCFLGRSIGVRHAGSCAGTPEEPPGGESAEEEENFV
| null | null |
cell differentiation [GO:0030154]; hematopoietic progenitor cell differentiation [GO:0002244]; negative regulation of activin receptor signaling pathway [GO:0032926]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of osteoclast differentiation [GO:0045671]; negative regulation of transmembrane receptor protein serine/threonine kinase signaling pathway [GO:0090101]; ossification [GO:0001503]; positive regulation of cell-cell adhesion [GO:0022409]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of BMP signaling pathway [GO:0030510]; regulation of transcription by RNA polymerase II [GO:0006357]
|
endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
activin binding [GO:0048185]; fibronectin binding [GO:0001968]
|
PF09289;PF21333;PF07648;
|
3.30.60.30;3.90.290.10;
| null | null |
SUBCELLULAR LOCATION: [Isoform 1]: Secreted.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. Note=Although alternative initiation has been demonstrated and resulted in different localization, the major source of nuclear FSTL3 appears not to depend on translation initiation at Met-27 according to. {ECO:0000269|PubMed:16150905}.
| null | null | null | null | null |
FUNCTION: Isoform 1 or the secreted form is a binding and antagonizing protein for members of the TGF-beta family, such as activin, BMP2 and MSTN. Inhibits activin A-, activin B-, BMP2- and MSDT-induced cellular signaling; more effective on activin A than on activin B. Involved in bone formation; inhibits osteoclast differentiation. Involved in hematopoiesis; involved in differentiation of hemopoietic progenitor cells, increases hematopoietic cell adhesion to fibronectin and seems to contribute to the adhesion of hematopoietic precursor cells to the bone marrow stroma. Isoform 2 or the nuclear form is probably involved in transcriptional regulation via interaction with MLLT10. {ECO:0000269|PubMed:11948405, ECO:0000269|PubMed:15451575, ECO:0000269|PubMed:15574124, ECO:0000269|PubMed:16336961, ECO:0000269|PubMed:17868029, ECO:0000269|PubMed:17878677}.
|
Homo sapiens (Human)
|
O95639
|
CPSF4_HUMAN
|
MQEIIASVDHIKFDLEIAVEQQLGAQPLPFPGMDKSGAAVCEFFLKAACGKGGMCPFRHISGEKTVVCKHWLRGLCKKGDQCEFLHEYDMTKMPECYFYSKFGECSNKECPFLHIDPESKIKDCPWYDRGFCKHGPLCRHRHTRRVICVNYLVGFCPEGPSCKFMHPRFELPMGTTEQPPLPQQTQPPAKQSNNPPLQRSSSLIQLTSQNSSPNQQRTPQVIGVMQSQNSSAGNRGPRPLEQVTCYKCGEKGHYANRCTKGHLAFLSGQ
| null | null |
mRNA processing [GO:0006397]
|
intracellular membrane-bounded organelle [GO:0043231]; mRNA cleavage and polyadenylation specificity factor complex [GO:0005847]; nucleoplasm [GO:0005654]
|
RNA binding [GO:0003723]; sequence-specific double-stranded DNA binding [GO:1990837]; zinc ion binding [GO:0008270]
|
PF00642;PF15663;PF00098;
|
4.10.1000.10;4.10.60.10;
|
CPSF4/YTH1 family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. CPSF4 binds RNA polymers with a preference for poly(U). {ECO:0000269|PubMed:14749727, ECO:0000269|PubMed:9224719}.
|
Homo sapiens (Human)
|
O95644
|
NFAC1_HUMAN
|
MPSTSFPVPSKFPLGPAAAVFGRGETLGPAPRAGGTMKSAEEEHYGYASSNVSPALPLPTAHSTLPAPCHNLQTSTPGIIPPADHPSGYGAALDGGPAGYFLSSGHTRPDGAPALESPRIEITSCLGLYHNNNQFFHDVEVEDVLPSSKRSPSTATLSLPSLEAYRDPSCLSPASSLSSRSCNSEASSYESNYSYPYASPQTSPWQSPCVSPKTTDPEEGFPRGLGACTLLGSPRHSPSTSPRASVTEESWLGARSSRPASPCNKRKYSLNGRQPPYSPHHSPTPSPHGSPRVSVTDDSWLGNTTQYTSSAIVAAINALTTDSSLDLGDGVPVKSRKTTLEQPPSVALKVEPVGEDLGSPPPPADFAPEDYSSFQHIRKGGFCDQYLAVPQHPYQWAKPKPLSPTSYMSPTLPALDWQLPSHSGPYELRIEVQPKSHHRAHYETEGSRGAVKASAGGHPIVQLHGYLENEPLMLQLFIGTADDRLLRPHAFYQVHRITGKTVSTTSHEAILSNTKVLEIPLLPENSMRAVIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQPSGRTLSLQVASNPIECSQRSAQELPLVEKQSTDSYPVVGGKKMVLSGHNFLQDSKVIFVEKAPDGHHVWEMEAKTDRDLCKPNSLVVEIPPFRNQRITSPVHVSFYVCNGKRKRSQYQRFTYLPANVPIIKTEPTDDYEPAPTCGPVSQGLSPLPRPYYSQQLAMPPDPSSCLVAGFPPCPQRSTLMPAAPGVSPKLHDLSPAAYTKGVASPGHCHLGLPQPAGEAPAVQDVPRPVATHPGSPGQPPPALLPQQVSAPPSSSCPPGLEHSLCPSSPSPPLPPATQEPTCLQPCSPACPPATGRPQHLPSTVRRDESPTAGPRLLPEVHEDGSPNLAPIPVTVKREPEELDQLYLDDVNEIIRNDLSSTSTHS
| null | null |
aortic valve morphogenesis [GO:0003180]; calcineurin-NFAT signaling cascade [GO:0033173]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular response to tumor necrosis factor [GO:0071356]; intracellular signal transduction [GO:0035556]; mononuclear cell differentiation [GO:1903131]; negative regulation of vascular associated smooth muscle cell differentiation [GO:1905064]; negative regulation of Wnt signaling pathway [GO:0030178]; positive regulation of DNA biosynthetic process [GO:2000573]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; pulmonary valve morphogenesis [GO:0003184]; regulation of transcription by RNA polymerase II [GO:0006357]; response to muscle activity [GO:0014850]; skeletal muscle adaptation [GO:0043501]; wound healing [GO:0042060]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; sarcoplasm [GO:0016528]; transcription regulator complex [GO:0005667]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; FK506 binding [GO:0005528]; mitogen-activated protein kinase p38 binding [GO:0048273]; nucleic acid binding [GO:0003676]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific double-stranded DNA binding [GO:1990837]; transcription coactivator binding [GO:0001223]
|
PF16179;PF00554;
|
2.60.40.10;2.60.40.340;
| null |
PTM: Phosphorylated by NFATC-kinase and GSK3B; phosphorylation induces NFATC1 nuclear exit and dephosphorylation by calcineurin promotes nuclear import. Phosphorylation by PKA and DYRK2 negatively modulates nuclear accumulation, and promotes subsequent phosphorylation by GSK3B or casein kinase 1. {ECO:0000269|PubMed:12351631, ECO:0000269|PubMed:16511445, ECO:0000269|PubMed:9072970}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16511445}. Nucleus {ECO:0000269|PubMed:16511445}. Note=Cytoplasmic for the phosphorylated form and nuclear after activation that is controlled by calcineurin-mediated dephosphorylation. Rapid nuclear exit of NFATC is thought to be one mechanism by which cells distinguish between sustained and transient calcium signals. Translocation to the nucleus is increased in the presence of calcium in pre-osteoblasts (By similarity). The subcellular localization of NFATC plays a key role in the regulation of gene transcription (PubMed:16511445). Nuclear translocation of NFATC1 is enhanced in the presence of TNFSF11. Nuclear translocation is decreased in the presence of FBN1 which can bind and sequester TNFSF11 (By similarity). {ECO:0000250|UniProtKB:O88942, ECO:0000269|PubMed:16511445}.
| null | null | null | null | null |
FUNCTION: Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2 or IL-4 gene transcription. Also controls gene expression in embryonic cardiac cells. Could regulate not only the activation and proliferation but also the differentiation and programmed death of T-lymphocytes as well as lymphoid and non-lymphoid cells (PubMed:10358178). Required for osteoclastogenesis and regulates many genes important for osteoclast differentiation and function (By similarity). {ECO:0000250|UniProtKB:O88942, ECO:0000269|PubMed:10358178}.
|
Homo sapiens (Human)
|
O95670
|
VATG2_HUMAN
|
MASQSQGIQQLLQAEKRAAEKVADARKRKARRLKQAKEEAQMEVEQYRREREHEFQSKQQAAMGSQGNLSAEVEQATRRQVQGMQSSQQRNRERVLAQLLGMVCDVRPQVHPNYRISA
| null | null |
regulation of macroautophagy [GO:0016241]; synaptic vesicle lumen acidification [GO:0097401]
|
clathrin-coated vesicle membrane [GO:0030665]; cytosol [GO:0005829]; extrinsic component of synaptic vesicle membrane [GO:0098850]; melanosome [GO:0042470]; synaptic vesicle membrane [GO:0030672]; vacuolar proton-transporting V-type ATPase, V1 domain [GO:0000221]
|
ATP hydrolysis activity [GO:0016887]; proton-transporting ATPase activity, rotational mechanism [GO:0046961]
|
PF03179;
|
1.20.5.2950;
|
V-ATPase G subunit family
| null |
SUBCELLULAR LOCATION: Melanosome {ECO:0000269|PubMed:17081065}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:Q0VCV6}; Peripheral membrane protein {ECO:0000305}. Note=Highly enriched in late-stage melanosomes. {ECO:0000269|PubMed:17081065}.
| null | null | null | null | null |
FUNCTION: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. {ECO:0000250|UniProtKB:O75348}.
|
Homo sapiens (Human)
|
O95671
|
ASML_HUMAN
|
MVLCPVIGKLLHKRVVLASASPRRQEILSNAGLRFEVVPSKFKEKLDKASFATPYGYAMETAKQKALEVANRLYQKDLRAPDVVIGADTIVTVGGLILEKPVDKQDAYRMLSRLSGREHSVFTGVAIVHCSSKDHQLDTRVSEFYEETKVKFSELSEELLWEYVHSGEPMDKAGGYGIQALGGMLVESVHGDFLNVVGFPLNHFCKQLVKLYYPPRPEDLRRSVKHDSIPAADTFEDLSDVEGGGSEPTQRDAGSRDEKAEAGEAGQATAEAECHRTRETLPPFPTRLLELIEGFMLSKGLLTACKLKVFDLLKDEAPQKAADIASKVDASACGMERLLDICAAMGLLEKTEQGYSNTETANVYLASDGEYSLHGFIMHNNDLTWNLFTYLEFAIREGTNQHHRALGKKAEDLFQDAYYQSPETRLRFMRAMHGMTKLTACQVATAFNLSRFSSACDVGGCTGALARELAREYPRMQVTVFDLPDIIELAAHFQPPGPQAVQIHFAAGDFFRDPLPSAELYVLCRILHDWPDDKVHKLLSRVAESCKPGAGLLLVETLLDEEKRVAQRALMQSLNMLVQTEGKERSLGEYQCLLELHGFHQVQVVHLGGVLDAILATKVAP
|
2.1.1.-; 3.6.1.9
|
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:24210219}; Note=Pyrophosphatase activity requires a divalent metal cation. {ECO:0000269|PubMed:24210219};
|
methylation [GO:0032259]; nucleotide metabolic process [GO:0009117]
|
cytosol [GO:0005829]
|
dTTP diphosphatase activity [GO:0036218]; nucleoside triphosphate diphosphatase activity [GO:0047429]; O-methyltransferase activity [GO:0008171]; UTP diphosphatase activity [GO:0036221]
|
PF16864;PF02545;PF00891;
|
3.90.950.10;3.40.50.150;1.10.10.10;
|
Maf family, YhdE subfamily; Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family
| null | null |
CATALYTIC ACTIVITY: Reaction=dTTP + H2O = diphosphate + dTMP + H(+); Xref=Rhea:RHEA:28534, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:63528; EC=3.6.1.9; Evidence={ECO:0000269|PubMed:24210219}; CATALYTIC ACTIVITY: Reaction=H2O + UTP = diphosphate + H(+) + UMP; Xref=Rhea:RHEA:29395, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:57865; EC=3.6.1.9; Evidence={ECO:0000269|PubMed:24210219}; CATALYTIC ACTIVITY: Reaction=CTP + H2O = CMP + diphosphate + H(+); Xref=Rhea:RHEA:27762, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:60377; EC=3.6.1.9; Evidence={ECO:0000269|PubMed:24210219}; CATALYTIC ACTIVITY: Reaction=H2O + psi-UTP = diphosphate + H(+) + psi-UMP; Xref=Rhea:RHEA:58740, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58380, ChEBI:CHEBI:142798; Evidence={ECO:0000269|PubMed:24210219}; CATALYTIC ACTIVITY: Reaction=H2O + TTP = 5-methyl-UMP + diphosphate + H(+); Xref=Rhea:RHEA:58736, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:63527, ChEBI:CHEBI:142797; Evidence={ECO:0000269|PubMed:24210219}; CATALYTIC ACTIVITY: Reaction=5-methyl-CTP + H2O = 5-methyl-CMP + diphosphate + H(+); Xref=Rhea:RHEA:58732, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:142795, ChEBI:CHEBI:142796; Evidence={ECO:0000269|PubMed:24210219};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=32.7 uM for dTTP {ECO:0000269|PubMed:24210219}; KM=41.2 uM for UTP {ECO:0000269|PubMed:24210219}; KM=17.4 uM for CTP {ECO:0000269|PubMed:24210219}; KM=22.8 uM for dCTP {ECO:0000269|PubMed:24210219}; KM=16.1 uM for m(5)UTP {ECO:0000269|PubMed:24210219}; KM=39.4 uM for m(5)CTP {ECO:0000269|PubMed:24210219}; KM=18.7 uM for pseudo-UTP {ECO:0000269|PubMed:24210219}; KM=10.7 uM for 8-oxo-GTP {ECO:0000269|PubMed:24210219}; KM=10.3 uM for N(4)-methyl-dCTP {ECO:0000269|PubMed:24210219}; Note=kcat is 0.7 sec(-1) with dTTP as substrate. kcat is 0.7 sec(-1) with UTP as substrate. kcat is 0.8 sec(-1) with CTP as substrate. kcat is 0.3 sec(-1) with dCTP as substrate. kcat is 1.5 sec(-1) with m(5)UTP as substrate. kcat is 3.7 sec(-1) with m(5)CTP as substrate. kcat is 2.5 sec(-1) with pseudo-UTP as substrate. kcat is 0.2 sec(-1) with 8-oxo-GTP as substrate. kcat is 0.3 sec(-1) with N(4)-methyl-dCTP as substrate. {ECO:0000269|PubMed:24210219};
| null | null | null |
FUNCTION: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. Can also hydrolyze CTP and the modified nucleotides pseudo-UTP, 5-methyl-UTP (m(5)UTP) and 5-methyl-CTP (m(5)CTP). Has weak activity with dCTP, 8-oxo-GTP and N(4)-methyl-dCTP (PubMed:24210219). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids (PubMed:24210219). In addition, the presence of the putative catalytic domain of S-adenosyl-L-methionine binding in the C-terminal region argues for a methyltransferase activity (Probable). {ECO:0000269|PubMed:24210219, ECO:0000305}.
|
Homo sapiens (Human)
|
O95672
|
ECEL1_HUMAN
|
MEPPYSLTAHYDEFQEVKYVSRCGAGGARGASLPPGFPLGAARSATGARSGLPRWNRREVCLLSGLVFAAGLCAILAAMLALKYLGPVAAGGGACPEGCPERKAFARAARFLAANLDASIDPCQDFYSFACGGWLRRHAIPDDKLTYGTIAAIGEQNEERLRRLLARPGGGPGGAAQRKVRAFFRSCLDMREIERLGPRPMLEVIEDCGGWDLGGAEERPGVAARWDLNRLLYKAQGVYSAAALFSLTVSLDDRNSSRYVIRIDQDGLTLPERTLYLAQDEDSEKILAAYRVFMERVLSLLGADAVEQKAQEILQVEQQLANITVSEHDDLRRDVSSMYNKVTLGQLQKITPHLRWKWLLDQIFQEDFSEEEEVVLLATDYMQQVSQLIRSTPHRVLHNYLVWRVVVVLSEHLSPPFREALHELAQEMEGSDKPQELARVCLGQANRHFGMALGALFVHEHFSAASKAKVQQLVEDIKYILGQRLEELDWMDAETRAAARAKLQYMMVMVGYPDFLLKPDAVDKEYEFEVHEKTYFKNILNSIRFSIQLSVKKIRQEVDKSTWLLPPQALNAYYLPNKNQMVFPAGILQPTLYDPDFPQSLNYGGIGTIIGHELTHGYDDWGGQYDRSGNLLHWWTEASYSRFLRKAECIVRLYDNFTVYNQRVNGKHTLGENIADMGGLKLAYHAYQKWVREHGPEHPLPRLKYTHDQLFFIAFAQNWCIKRRSQSIYLQVLTDKHAPEHYRVLGSVSQFEEFGRAFHCPKDSPMNPAHKCSVW
|
3.4.24.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion. {ECO:0000250};
|
neuropeptide signaling pathway [GO:0007218]; protein processing [GO:0016485]; respiratory system process [GO:0003016]
|
plasma membrane [GO:0005886]
|
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]
|
PF01431;PF05649;
|
3.40.390.10;1.10.1380.10;
|
Peptidase M13 family
|
PTM: N-glycosylated.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May contribute to the degradation of peptide hormones and be involved in the inactivation of neuronal peptides.
|
Homo sapiens (Human)
|
O95674
|
CDS2_HUMAN
|
MTELRQRVAHEPVAPPEDKESESEAKVDGETASDSESRAESAPLPVSADDTPEVLNRALSNLSSRWKNWWVRGILTLAMIAFFFIIIYLGPMVLMIIVMCVQIKCFHEIITIGYNVYHSYDLPWFRTLSWYFLLCVNYFFYGETVTDYFFTLVQREEPLRILSKYHRFISFTLYLIGFCMFVLSLVKKHYRLQFYMFGWTHVTLLIVVTQSHLVIHNLFEGMIWFIVPISCVICNDIMAYMFGFFFGRTPLIKLSPKKTWEGFIGGFFATVVFGLLLSYVMSGYRCFVCPVEYNNDTNSFTVDCEPSDLFRLQEYNIPGVIQSVIGWKTVRMYPFQIHSIALSTFASLIGPFGGFFASGFKRAFKIKDFANTIPGHGGIMDRFDCQYLMATFVNVYIASFIRGPNPSKLIQQFLTLRPDQQLHIFNTLRSHLIDKGMLTSTTEDE
|
2.7.7.41
| null |
CDP-diacylglycerol biosynthetic process [GO:0016024]; lipid droplet formation [GO:0140042]; phosphatidylglycerol biosynthetic process [GO:0006655]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]
|
phosphatidate cytidylyltransferase activity [GO:0004605]
|
PF01148;
| null |
CDS family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:25375833, ECO:0000269|PubMed:26946540, ECO:0000269|PubMed:31548309}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41; Evidence={ECO:0000269|PubMed:25375833}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16230; Evidence={ECO:0000305|PubMed:25375833}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + CTP + H(+) = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphate; Xref=Rhea:RHEA:45648, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:77091, ChEBI:CHEBI:85349; Evidence={ECO:0000269|PubMed:25375833}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45649; Evidence={ECO:0000305|PubMed:25375833}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + CTP + H(+) = 1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphate; Xref=Rhea:RHEA:45660, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:77098, ChEBI:CHEBI:85352; Evidence={ECO:0000269|PubMed:25375833}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45661; Evidence={ECO:0000305|PubMed:25375833}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + CTP + H(+) = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphate; Xref=Rhea:RHEA:45652, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:72864, ChEBI:CHEBI:85350; Evidence={ECO:0000269|PubMed:25375833}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45653; Evidence={ECO:0000305|PubMed:25375833}; CATALYTIC ACTIVITY: Reaction=1,2-di-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate + CTP + H(+) = 1,2-di-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphate; Xref=Rhea:RHEA:45656, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:77126, ChEBI:CHEBI:85351; Evidence={ECO:0000269|PubMed:25375833}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45657; Evidence={ECO:0000305|PubMed:25375833}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CTP + H(+) = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphate; Xref=Rhea:RHEA:45664, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:74560, ChEBI:CHEBI:85353; Evidence={ECO:0000269|PubMed:25375833}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45665; Evidence={ECO:0000305|PubMed:25375833}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphate + CTP + H(+) = 1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphate; Xref=Rhea:RHEA:45668, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:77130, ChEBI:CHEBI:85354; Evidence={ECO:0000269|PubMed:25375833}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45669; Evidence={ECO:0000305|PubMed:25375833}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + CTP + H(+) = 1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphate; Xref=Rhea:RHEA:45672, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:77128, ChEBI:CHEBI:85355; Evidence={ECO:0000269|PubMed:25375833}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45673; Evidence={ECO:0000305|PubMed:25375833}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CTP + H(+) = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphate; Xref=Rhea:RHEA:45676, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:74546, ChEBI:CHEBI:85356; Evidence={ECO:0000269|PubMed:25375833}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45677; Evidence={ECO:0000305|PubMed:25375833};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 uM for 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid {ECO:0000269|PubMed:25375833}; KM=0.9 uM for 1-stearoyl-2-linoleoyl-sn-phosphatidic acid {ECO:0000269|PubMed:25375833}; Vmax=9.3 umol/min/mg enzyme for 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid {ECO:0000269|PubMed:25375833}; Vmax=3.5 umol/min/mg enzyme for 1-stearoyl-2-linoleoyl-sn-phosphatidic acid {ECO:0000269|PubMed:25375833};
|
PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
| null | null |
FUNCTION: Catalyzes the conversion of phosphatidic acid (PA) to CDP-diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of phosphatidylglycerol, cardiolipin and phosphatidylinositol (PubMed:25375833). Exhibits specificity for the nature of the acyl chains at the sn-1 and sn-2 positions in the substrate, PA and the preferred acyl chain composition is 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid (PubMed:25375833). Plays an important role in regulating the growth and maturation of lipid droplets which are storage organelles at the center of lipid and energy homeostasis (PubMed:26946540, PubMed:31548309). {ECO:0000269|PubMed:25375833, ECO:0000269|PubMed:26946540, ECO:0000269|PubMed:31548309}.
|
Homo sapiens (Human)
|
O95677
|
EYA4_HUMAN
|
MEDSQDLNEQSVKKTCTESDVSQSQNSRSMEMQDLASPHTLVGGGDTPGSSKLEKSNLSSTSVTTNGTGGENMTVLNTADWLLSCNTPSSATMSLLAVKTEPLNSSETTATTGDGALDTFTGSVITSSGYSPRSAHQYSPQLYPSKPYPHILSTPAAQTMSAYAGQTQYSGMQQPAVYTAYSQTGQPYSLPTYDLGVMLPAIKTESGLSQTQSPLQSGCLSYSPGFSTPQPGQTPYSYQMPGSSFAPSSTIYANNSVSNSTNFSGSQQDYPSYTAFGQNQYAQYYSASTYGAYMTSNNTADGTPSSTSTYQLQESLPGLTNQPGEFDTMQSPSTPIKDLDERTCRSSGSKSRGRGRKNNPSPPPDSDLERVFVWDLDETIIVFHSLLTGSYAQKYGKDPPMAVTLGLRMEEMIFNLADTHLFFNDLEECDQVHIDDVSSDDNGQDLSTYSFATDGFHAAASSANLCLPTGVRGGVDWMRKLAFRYRRVKELYNTYKNNVGGLLGPAKRDAWLQLRAEIEGLTDSWLTNALKSLSIISTRSNCINVLVTTTQLIPALAKVLLYSLGGAFPIENIYSATKIGKESCFERIMQRFGRKVVYVVIGDGVEEEQAAKKHNMPFWRISSHSDLLALHQALELEYL
|
3.1.3.48
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O00167}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:O00167};
|
anatomical structure morphogenesis [GO:0009653]; cell differentiation [GO:0030154]; chromatin organization [GO:0006325]; DNA repair [GO:0006281]; inner ear development [GO:0048839]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; positive regulation of DNA repair [GO:0045739]; visual perception [GO:0007601]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; protein tyrosine phosphatase activity [GO:0004725]
|
PF00702;
|
3.40.50.12350;
|
HAD-like hydrolase superfamily, EYA family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99502}. Nucleus {ECO:0000250|UniProtKB:Q99502}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000250|UniProtKB:Q99502};
| null | null | null | null |
FUNCTION: Tyrosine phosphatase that specifically dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph). 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Promotes efficient DNA repair by dephosphorylating H2AX, promoting the recruitment of DNA repair complexes containing MDC1. Its function as histone phosphatase probably explains its role in transcription regulation during organogenesis. May be involved in development of the eye (By similarity). {ECO:0000250|UniProtKB:Q99502}.
|
Homo sapiens (Human)
|
O95678
|
K2C75_HUMAN
|
MSRQSSITFQSGSRRGFSTTSAITPAAGRSRFSSVSVARSAAGSGGLGRISSAGASFGSRSLYNLGGAKRVSINGCGSSCRSGFGGRASNRFGVNSGFGYGGGVGGGFSGPSFPVCPPGGIQEVTVNQSLLTPLHLQIDPTIQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQGSRTVRQNLEPLFDSYTSELRRQLESITTERGRLEAELRNMQDVVEDFKVRYEDEINKRTAAENEFVALKKDVDAAYMNKVELEAKVKSLPEEINFIHSVFDAELSQLQTQVGDTSVVLSMDNNRNLDLDSIIAEVKAQYEDIANRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEISEMNRMIQRLRAEIDSVKKQCSSLQTAIADAEQRGELALKDARAKLVDLEEALQKAKQDMARLLREYQELMNIKLALDVEIATYRKLLEGEECRLSGEGVSPVNISVVTSTLSSGYGSGSSIGGGNLGLGGGSGYSFTTSGGHSLGAGLGGSGFSATSNRGLGGSGSSVKFVSTTSSSQKSYTH
| null | null |
hematopoietic progenitor cell differentiation [GO:0002244]; intermediate filament organization [GO:0045109]; keratinization [GO:0031424]
|
cornified envelope [GO:0001533]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intermediate filament [GO:0005882]; keratin filament [GO:0045095]
|
structural constituent of skin epidermis [GO:0030280]; structural molecule activity [GO:0005198]
|
PF00038;PF16208;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
| null | null | null | null | null | null | null |
FUNCTION: Plays a central role in hair and nail formation. Essential component of keratin intermediate filaments in the companion layer of the hair follicle.
|
Homo sapiens (Human)
|
O95684
|
CEP43_HUMAN
|
MAATAAAVVAEEDTELRDLLVQTLENSGVLNRIKAELRAAVFLALEEQEKVENKTPLVNESLKKFLNTKDGRLVASLVAEFLQFFNLDFTLAVFQPETSTLQGLEGRENLARDLGIIEAEGTVGGPLLLEVIRRCQQKEKGPTTGEGALDLSDVHSPPKSPEGKTSAQTTPSKIPRYKGQGKKKTSGQKAGDKKANDEANQSDTSVSLSEPKSKSSLHLLSHETKIGSFLSNRTLDGKDKAGLCPDEDDMEGDSFFDDPIPKPEKTYGLRKEPRKQAGSLASLSDAPPLKSGLSSLAGAPSLKDSESKRGNTVLKDLKLISDKIGSLGLGTGEDDDYVDDFNSTSHRSEKSEISIGEEIEEDLSVEIDDINTSDKLDDLTQDLTVSQLSDVADYLEDVA
| null | null |
cell projection organization [GO:0030030]; microtubule anchoring [GO:0034453]; negative regulation of protein kinase activity [GO:0006469]; positive regulation of cell growth [GO:0030307]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]
|
cell projection [GO:0042995]; centriole [GO:0005814]; centrosome [GO:0005813]; cytosol [GO:0005829]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
|
protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein tyrosine kinase inhibitor activity [GO:0030292]
|
PF09398;
|
1.20.960.40;
|
CEP43 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:16314388, ECO:0000269|PubMed:16690081, ECO:0000269|PubMed:28659385}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:28428259, ECO:0000269|PubMed:28625565, ECO:0000269|PubMed:28659385}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:28659385}. Note=Associated with gamma-tubulin (PubMed:16314388). Localizes on both mother and daughter centrioles (PubMed:28428259, PubMed:28625565). Localizes to an axial position on the mother centriole (PubMed:28625565). Localizes to the distal end of the centriole partly on the subdistal appendage region (PubMed:28659385). {ECO:0000269|PubMed:16314388, ECO:0000269|PubMed:28428259, ECO:0000269|PubMed:28625565, ECO:0000269|PubMed:28659385}.
| null | null | null | null | null |
FUNCTION: Required for anchoring microtubules to the centrosomes (PubMed:16314388, PubMed:28659385). Required for ciliation (PubMed:28625565, PubMed:28659385). {ECO:0000269|PubMed:16314388, ECO:0000269|PubMed:28625565, ECO:0000269|PubMed:28659385}.
|
Homo sapiens (Human)
|
O95696
|
BRD1_HUMAN
|
MRRKGRCHRGSAARHPSSPCSVKHSPTRETLTYAQAQRMVEIEIEGRLHRISIFDPLEIILEDDLTAQEMSECNSNKENSERPPVCLRTKRHKNNRVKKKNEALPSAHGTPASASALPEPKVRIVEYSPPSAPRRPPVYYKFIEKSAEELDNEVEYDMDEEDYAWLEIVNEKRKGDCVPAVSQSMFEFLMDRFEKESHCENQKQGEQQSLIDEDAVCCICMDGECQNSNVILFCDMCNLAVHQECYGVPYIPEGQWLCRHCLQSRARPADCVLCPNKGGAFKKTDDDRWGHVVCALWIPEVGFANTVFIEPIDGVRNIPPARWKLTCYLCKQKGVGACIQCHKANCYTAFHVTCAQKAGLYMKMEPVKELTGGGTTFSVRKTAYCDVHTPPGCTRRPLNIYGDVEMKNGVCRKESSVKTVRSTSKVRKKAKKAKKALAEPCAVLPTVCAPYIPPQRLNRIANQVAIQRKKQFVERAHSYWLLKRLSRNGAPLLRRLQSSLQSQRSSQQRENDEEMKAAKEKLKYWQRLRHDLERARLLIELLRKREKLKREQVKVEQVAMELRLTPLTVLLRSVLDQLQDKDPARIFAQPVSLKEVPDYLDHIKHPMDFATMRKRLEAQGYKNLHEFEEDFDLIIDNCMKYNARDTVFYRAAVRLRDQGGVVLRQARREVDSIGLEEASGMHLPERPAAAPRRPFSWEDVDRLLDPANRAHLGLEEQLRELLDMLDLTCAMKSSGSRSKRAKLLKKEIALLRNKLSQQHSQPLPTGPGLEGFEEDGAALGPEAGEEVLPRLETLLQPRKRSRSTCGDSEVEEESPGKRLDAGLTNGFGGARSEQEPGGGLGRKATPRRRCASESSISSSNSPLCDSSFNAPKCGRGKPALVRRHTLEDRSELISCIENGNYAKAARIAAEVGQSSMWISTDAAASVLEPLKVVWAKCSGYPSYPALIIDPKMPRVPGHHNGVTIPAPPLDVLKIGEHMQTKSDEKLFLVLFFDNKRSWQWLPKSKMVPLGIDETIDKLKMMEGRNSSIRKAVRIAFDRAMNHLSRVHGEPTSDLSDID
| null | null |
chromatin remodeling [GO:0006338]; erythrocyte maturation [GO:0043249]; positive regulation of erythrocyte differentiation [GO:0045648]; regulation of developmental process [GO:0050793]; regulation of DNA-templated transcription [GO:0006355]; regulation of hemopoiesis [GO:1903706]; regulation of transcription by RNA polymerase II [GO:0006357]; response to electrical stimulus [GO:0051602]; response to immobilization stress [GO:0035902]
|
dendrite [GO:0030425]; histone H3-K14 acetyltransferase complex [GO:0036409]; MOZ/MORF histone acetyltransferase complex [GO:0070776]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; perikaryon [GO:0043204]
|
histone binding [GO:0042393]; histone reader activity [GO:0140566]; metal ion binding [GO:0046872]
|
PF00439;PF10513;PF13831;PF00855;PF13832;
|
2.30.30.140;1.20.920.10;3.30.40.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21753189, ECO:0000269|PubMed:21880731, ECO:0000269|PubMed:25593309}. Chromosome {ECO:0000269|PubMed:21753189, ECO:0000269|PubMed:28334966}. Note=Localizes to transcription start sites. {ECO:0000269|PubMed:21753189, ECO:0000269|PubMed:28334966}.
| null | null | null | null | null |
FUNCTION: Scaffold subunit of various histone acetyltransferase (HAT) complexes, such as the MOZ/MORF and HBO1 complexes, that acts as a regulator of hematopoiesis (PubMed:16387653, PubMed:21753189, PubMed:21880731). Plays a key role in HBO1 complex by directing KAT7/HBO1 specificity towards histone H3 'Lys-14' acetylation (H3K14ac), thereby promoting erythroid differentiation (PubMed:21753189). {ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:21753189, ECO:0000269|PubMed:21880731}.
|
Homo sapiens (Human)
|
O95704
|
APBB3_HUMAN
|
MLGKDYMLAIILVNCDDDLWGDHSLEVEAGLPPGWRKIHDAAGTYYWHVPSGSTQWQRPTWELGDAEDPGTGTEGIWGLRPPKGRSFSSLESSLDRSNSLSWYGGESYIQSMEPGAKCFAVRSLGWVEVPEEDLAPGKSSIAVNNCIQQLAQTRSRSQPPDGAWGEGQNMLMILKKDAMSLVNPLDHSLIHCQPLVHIRVWGVGSSKGRDRDFAFVASDKDSCMLKCHVFCCDVPAKAIASALHGLCAQILSERVEVSGDASCCSPDPISPEDLPRQVELLDAVSQAAQKYEALYMGTLPVTKAMGMDVLNEAIGTLTARGDRNAWVPTMLSVSDSLMTAHPIQAEASTEEEPLWQCPVRLVTFIGVGRDPHTFGLIADLGRQSFQCAAFWCQPHAGGLSEAVQAACMVQYQKCLVASAARGKAWGAQARARLRLKRTSSMDSPGGPLPLPLLKGGVGGAGATPRKRGVFSFLDAFRLKPSLLHMP
| null | null |
positive regulation of protein secretion [GO:0050714]; regulation of DNA-templated transcription [GO:0006355]
|
actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nuclear body [GO:0016604]; nucleus [GO:0005634]
|
amyloid-beta binding [GO:0001540]; low-density lipoprotein particle receptor binding [GO:0050750]
|
PF00640;PF00397;
|
2.20.70.10;2.30.29.30;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12153398}. Nucleus {ECO:0000269|PubMed:12153398}.; SUBCELLULAR LOCATION: [Isoform I-214]: Nucleus.; SUBCELLULAR LOCATION: [Isoform I-245]: Nucleus.
| null | null | null | null | null |
FUNCTION: May modulate the internalization of amyloid-beta precursor protein.
|
Homo sapiens (Human)
|
O95707
|
RPP29_HUMAN
|
MKSVIYHALSQKEANDSDVQPSGAQRAEAFVRAFLKRSTPRMSPQAREDQLQRKAVVLEYFTRHKRKEKKKKAKGLSARQRRELRLFDIKPEQQRYSLFLPLHELWKQYIRDLCSGLKPDTQPQMIQAKLLKADLHGAIISVTKSKCPSYVGITGILLQETKHIFKIITKEDRLKVIPKLNCVFTVETDGFISYIYGSKFQLRSSERSAKKFKAKGTIDL
| null | null |
rRNA processing [GO:0006364]; tRNA 5'-leader removal [GO:0001682]
|
multimeric ribonuclease P complex [GO:0030681]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; ribonuclease MRP complex [GO:0000172]; ribonuclease P complex [GO:0030677]
|
ribonuclease P activity [GO:0004526]; ribonuclease P RNA binding [GO:0033204]
|
PF01868;
|
2.30.30.210;
|
Eukaryotic/archaeal RNase P protein component 1 family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10352175}.
| null | null | null | null | null |
FUNCTION: Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends. {ECO:0000269|PubMed:10024167, ECO:0000269|PubMed:10352175, ECO:0000269|PubMed:30454648}.
|
Homo sapiens (Human)
|
O95711
|
LY86_HUMAN
|
MKGFTATLFLWTLIFPSCSGGGGGKAWPTHVVCSDSGLEVLYQSCDPLQDFGFSVEKCSKQLKSNINIRFGIILREDIKELFLDLALMSQGSSVLNFSYPICEAALPKFSFCGRRKGEQIYYAGPVNNPEFTIPQGEYQVLLELYTEKRSTVACANATIMCS
| null | null |
inflammatory response [GO:0006954]; innate immune response [GO:0045087]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; positive regulation of lipopolysaccharide-mediated signaling pathway [GO:0031666]
|
extracellular region [GO:0005576]
| null |
PF02221;
|
2.60.40.770;
| null | null |
SUBCELLULAR LOCATION: Secreted, extracellular space. Note=Associated with CD180 at the cell surface.
| null | null | null | null | null |
FUNCTION: May cooperate with CD180 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) and cytokine production. Important for efficient CD180 cell surface expression (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O95714
|
HERC2_HUMAN
|
MPSESFCLAAQARLDSKWLKTDIQLAFTRDGLCGLWNEMVKDGEIVYTGTESTQNGELPPRKDDSVEPSGTKKEDLNDKEKKDEEETPAPIYRAKSILDSWVWGKQPDVNELKECLSVLVKEQQALAVQSATTTLSALRLKQRLVILERYFIALNRTVFQENVKVKWKSSGISLPPVDKKSSRPAGKGVEGLARVGSRAALSFAFAFLRRAWRSGEDADLCSELLQESLDALRALPEASLFDESTVSSVWLEVVERATRFLRSVVTGDVHGTPATKGPGSIPLQDQHLALAILLELAVQRGTLSQMLSAILLLLQLWDSGAQETDNERSAQGTSAPLLPLLQRFQSIICRKDAPHSEGDMHLLSGPLSPNESFLRYLTLPQDNELAIDLRQTAVVVMAHLDRLATPCMPPLCSSPTSHKGSLQEVIGWGLIGWKYYANVIGPIQCEGLANLGVTQIACAEKRFLILSRNGRVYTQAYNSDTLAPQLVQGLASRNIVKIAAHSDGHHYLALAATGEVYSWGCGDGGRLGHGDTVPLEEPKVISAFSGKQAGKHVVHIACGSTYSAAITAEGELYTWGRGNYGRLGHGSSEDEAIPMLVAGLKGLKVIDVACGSGDAQTLAVTENGQVWSWGDGDYGKLGRGGSDGCKTPKLIEKLQDLDVVKVRCGSQFSIALTKDGQVYSWGKGDNQRLGHGTEEHVRYPKLLEGLQGKKVIDVAAGSTHCLALTEDSEVHSWGSNDQCQHFDTLRVTKPEPAALPGLDTKHIVGIACGPAQSFAWSSCSEWSIGLRVPFVVDICSMTFEQLDLLLRQVSEGMDGSADWPPPQEKECVAVATLNLLRLQLHAAISHQVDPEFLGLGLGSILLNSLKQTVVTLASSAGVLSTVQSAAQAVLQSGWSVLLPTAEERARALSALLPCAVSGNEVNISPGRRFMIDLLVGSLMADGGLESALHAAITAEIQDIEAKKEAQKEKEIDEQEANASTFHRSRTPLDKDLINTGICESSGKQCLPLVQLIQQLLRNIASQTVARLKDVARRISSCLDFEQHSRERSASLDLLLRFQRLLISKLYPGESIGQTSDISSPELMGVGSLLKKYTALLCTHIGDILPVAASIASTSWRHFAEVAYIVEGDFTGVLLPELVVSIVLLLSKNAGLMQEAGAVPLLGGLLEHLDRFNHLAPGKERDDHEELAWPGIMESFFTGQNCRNNEEVTLIRKADLENHNKDGGFWTVIDGKVYDIKDFQTQSLTGNSILAQFAGEDPVVALEAALQFEDTRESMHAFCVGQYLEPDQEIVTIPDLGSLSSPLIDTERNLGLLLGLHASYLAMSTPLSPVEIECAKWLQSSIFSGGLQTSQIHYSYNEEKDEDHCSSPGGTPASKSRLCSHRRALGDHSQAFLQAIADNNIQDHNVKDFLCQIERYCRQCHLTTPIMFPPEHPVEEVGRLLLCCLLKHEDLGHVALSLVHAGALGIEQVKHRTLPKSVVDVCRVVYQAKCSLIKTHQEQGRSYKEVCAPVIERLRFLFNELRPAVCNDLSIMSKFKLLSSLPRWRRIAQKIIRERRKKRVPKKPESTDDEEKIGNEESDLEEACILPHSPINVDKRPIAIKSPKDKWQPLLSTVTGVHKYKWLKQNVQGLYPQSPLLSTIAEFALKEEPVDVEKMRKCLLKQLERAEVRLEGIDTILKLASKNFLLPSVQYAMFCGWQRLIPEGIDIGEPLTDCLKDVDLIPPFNRMLLEVTFGKLYAWAVQNIRNVLMDASAKFKELGIQPVPLQTITNENPSGPSLGTIPQARFLLVMLSMLTLQHGANNLDLLLNSGMLALTQTALRLIGPSCDNVEEDMNASAQGASATVLEETRKETAPVQLPVSGPELAAMMKIGTRVMRGVDWKWGDQDGPPPGLGRVIGELGEDGWIRVQWDTGSTNSYRMGKEGKYDLKLAELPAAAQPSAEDSDTEDDSEAEQTERNIHPTAMMFTSTINLLQTLCLSAGVHAEIMQSEATKTLCGLLRMLVESGTTDKTSSPNRLVYREQHRSWCTLGFVRSIALTPQVCGALSSPQWITLLMKVVEGHAPFTATSLQRQILAVHLLQAVLPSWDKTERARDMKCLVEKLFDFLGSLLTTCSSDVPLLRESTLRRRRVRPQASLTATHSSTLAEEVVALLRTLHSLTQWNGLINKYINSQLRSITHSFVGRPSEGAQLEDYFPDSENPEVGGLMAVLAVIGGIDGRLRLGGQVMHDEFGEGTVTRITPKGKITVQFSDMRTCRVCPLNQLKPLPAVAFNVNNLPFTEPMLSVWAQLVNLAGSKLEKHKIKKSTKQAFAGQVDLDLLRCQQLKLYILKAGRALLSHQDKLRQILSQPAVQETGTVHTDDGAVVSPDLGDMSPEGPQPPMILLQQLLASATQPSPVKAIFDKQELEAAALAVCQCLAVESTHPSSPGFEDCSSSEATTPVAVQHIRPARVKRRKQSPVPALPIVVQLMEMGFSRRNIEFALKSLTGASGNASSLPGVEALVGWLLDHSDIQVTELSDADTVSDEYSDEEVVEDVDDAAYSMSTGAVVTESQTYKKRADFLSNDDYAVYVRENIQVGMMVRCCRAYEEVCEGDVGKVIKLDRDGLHDLNVQCDWQQKGGTYWVRYIHVELIGYPPPSSSSHIKIGDKVRVKASVTTPKYKWGSVTHQSVGVVKAFSANGKDIIVDFPQQSHWTGLLSEMELVPSIHPGVTCDGCQMFPINGSRFKCRNCDDFDFCETCFKTKKHNTRHTFGRINEPGQSAVFCGRSGKQLKRCHSSQPGMLLDSWSRMVKSLNVSSSVNQASRLIDGSEPCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVDPADSSYMPSLVVVSGGNSLNNLIELKTININPSDTTVPLLNDCTEYHRYIEIAIKQCRSSGIDCKIHGLILLGRIRAEEEDLAAVPFLASDNEEEEDEKGNSGSLIRKKAAGLESAATIRTKVFVWGLNDKDQLGGLKGSKIKVPSFSETLSALNVVQVAGGSKSLFAVTVEGKVYACGEATNGRLGLGISSGTVPIPRQITALSSYVVKKVAVHSGGRHATALTVDGKVFSWGEGDDGKLGHFSRMNCDKPRLIEALKTKRIRDIACGSSHSAALTSSGELYTWGLGEYGRLGHGDNTTQLKPKMVKVLLGHRVIQVACGSRDAQTLALTDEGLVFSWGDGDFGKLGRGGSEGCNIPQNIERLNGQGVCQIECGAQFSLALTKSGVVWTWGKGDYFRLGHGSDVHVRKPQVVEGLRGKKIVHVAVGALHCLAVTDSGQVYAWGDNDHGQQGNGTTTVNRKPTLVQGLEGQKITRVACGSSHSVAWTTVDVATPSVHEPVLFQTARDPLGASYLGVPSDADSSAASNKISGASNSKPNRPSLAKILLSLDGNLAKQQALSHILTALQIMYARDAVVGALMPAAMIAPVECPSFSSAAPSDASAMASPMNGEECMLAVDIEDRLSPNPWQEKREIVSSEDAVTPSAVTPSAPSASARPFIPVTDDLGAASIIAETMTKTKEDVESQNKAAGPEPQALDEFTSLLIADDTRVVVDLLKLSVCSRAGDRGRDVLSAVLSGMGTAYPQVADMLLELCVTELEDVATDSQSGRLSSQPVVVESSHPYTDDTSTSGTVKIPGAEGLRVEFDRQCSTERRHDPLTVMDGVNRIVSVRSGREWSDWSSELRIPGDELKWKFISDGSVNGWGWRFTVYPIMPAAGPKELLSDRCVLSCPSMDLVTCLLDFRLNLASNRSIVPRLAASLAACAQLSALAASHRMWALQRLRKLLTTEFGQSININRLLGENDGETRALSFTGSALAALVKGLPEALQRQFEYEDPIVRGGKQLLHSPFFKVLVALACDLELDTLPCCAETHKWAWFRRYCMASRVAVALDKRTPLPRLFLDEVAKKIRELMADSENMDVLHESHDIFKREQDEQLVQWMNRRPDDWTLSAGGSGTIYGWGHNHRGQLGGIEGAKVKVPTPCEALATLRPVQLIGGEQTLFAVTADGKLYATGYGAGGRLGIGGTESVSTPTLLESIQHVFIKKVAVNSGGKHCLALSSEGEVYSWGEAEDGKLGHGNRSPCDRPRVIESLRGIEVVDVAAGGAHSACVTAAGDLYTWGKGRYGRLGHSDSEDQLKPKLVEALQGHRVVDIACGSGDAQTLCLTDDDTVWSWGDGDYGKLGRGGSDGCKVPMKIDSLTGLGVVKVECGSQFSVALTKSGAVYTWGKGDYHRLGHGSDDHVRRPRQVQGLQGKKVIAIATGSLHCVCCTEDGEVYTWGDNDEGQLGDGTTNAIQRPRLVAALQGKKVNRVACGSAHTLAWSTSKPASAGKLPAQVPMEYNHLQEIPIIALRNRLLLLHHLSELFCPCIPMFDLEGSLDETGLGPSVGFDTLRGILISQGKEAAFRKVVQATMVRDRQHGPVVELNRIQVKRSRSKGGLAGPDGTKSVFGQMCAKMSSFGPDSLLLPHRVWKVKFVGESVDDCGGGYSESIAEICEELQNGLTPLLIVTPNGRDESGANRDCYLLSPAARAPVHSSMFRFLGVLLGIAIRTGSPLSLNLAEPVWKQLAGMSLTIADLSEVDKDFIPGLMYIRDNEATSEEFEAMSLPFTVPSASGQDIQLSSKHTHITLDNRAEYVRLAINYRLHEFDEQVAAVREGMARVVPVPLLSLFTGYELETMVCGSPDIPLHLLKSVATYKGIEPSASLIQWFWEVMESFSNTERSLFLRFVWGRTRLPRTIADFRGRDFVIQVLDKYNPPDHFLPESYTCFFLLKLPRYSCKQVLEEKLKYAIHFCKSIDTDDYARIALTGEPAADDSSDDSDNEDVDSFASDSTQDYLTGH
|
2.3.2.26
| null |
DNA damage response [GO:0006974]; DNA repair [GO:0006281]; intracellular protein transport [GO:0006886]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ubiquitination [GO:0016567]; spermatogenesis [GO:0007283]
|
centriole [GO:0005814]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
guanyl-nucleotide exchange factor activity [GO:0005085]; SUMO binding [GO:0032183]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase binding [GO:0031625]; zinc ion binding [GO:0008270]
|
PF03256;PF11515;PF00173;PF00632;PF06701;PF00415;PF00569;
|
2.30.30.30;3.30.60.90;3.10.120.10;2.60.120.260;3.30.2160.10;3.30.2410.10;3.90.1750.10;2.130.10.30;2.30.30.40;
| null |
PTM: Phosphorylation at Thr-4827 is required for interaction with RNF8. {ECO:0000269|PubMed:20023648}.; PTM: Sumoylated with SUMO1 by PIAS4 in response to double-strand breaks (DSBs), promoting the interaction with RNF8. {ECO:0000269|PubMed:22508508}.
|
SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Nucleus. Note=Recruited to sites of DNA damage in response to ionizing radiation (IR) via its interaction with RNF8. May loose association with centrosomes during mitosis.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26; Evidence={ECO:0000269|PubMed:20304803};
| null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase that regulates ubiquitin-dependent retention of repair proteins on damaged chromosomes. Recruited to sites of DNA damage in response to ionizing radiation (IR) and facilitates the assembly of UBE2N and RNF8 promoting DNA damage-induced formation of 'Lys-63'-linked ubiquitin chains. Acts as a mediator of binding specificity between UBE2N and RNF8. Involved in the maintenance of RNF168 levels. E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of XPA which influences the circadian oscillation of DNA excision repair activity. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (PubMed:26692333). Modulates also iron metabolism by regulating the basal turnover of FBXL5 (PubMed:24778179). {ECO:0000269|PubMed:20023648, ECO:0000269|PubMed:20304803, ECO:0000269|PubMed:22508508, ECO:0000269|PubMed:24778179, ECO:0000269|PubMed:26692333}.
|
Homo sapiens (Human)
|
O95715
|
CXL14_HUMAN
|
MSLLPRRAPPVSMRLLAAALLLLLLALYTARVDGSKCKCSRKGPKIRYSDVKKLEMKPKYPHCEEKMVIITTKSVSRYRGQEHCLHPKLQSTKRFIKWYNAWNEKRRVYEE
| null | null |
antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cell-cell signaling [GO:0007267]; chemotaxis [GO:0006935]; signal transduction [GO:0007165]
|
extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]
|
chemokine activity [GO:0008009]
|
PF00048;
|
2.40.50.40;
|
Intercrine alpha (chemokine CxC) family
|
PTM: Ubiquitinated, followed by degradation by the proteasome. {ECO:0000269|PubMed:16987528}.
|
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Potent chemoattractant for neutrophils, and weaker for dendritic cells. Not chemotactic for T-cells, B-cells, monocytes, natural killer cells or granulocytes. Does not inhibit proliferation of myeloid progenitors in colony formation assays. {ECO:0000269|PubMed:10049774, ECO:0000269|PubMed:10946286}.
|
Homo sapiens (Human)
|
O95716
|
RAB3D_HUMAN
|
MASAGDTQAGPRDAADQNFDYMFKLLLIGNSSVGKTSFLFRYADDSFTPAFVSTVGIDFKVKTVYRHDKRIKLQIWDTAGQERYRTITTAYYRGAMGFLLMYDIANQESFAAVQDWATQIKTYSWDNAQVILVGNKCDLEDERVVPAEDGRRLADDLGFEFFEASAKENINVKQVFERLVDVICEKMNESLEPSSSSGSNGKGPAVGDAPAPQPSSCSC
| null | null |
bone resorption [GO:0045453]; positive regulation of regulated secretory pathway [GO:1903307]; protein localization to plasma membrane [GO:0072659]; protein secretion [GO:0009306]; regulation of exocytosis [GO:0017157]; vesicle docking involved in exocytosis [GO:0006904]
|
azurophil granule membrane [GO:0035577]; cytoplasmic microtubule [GO:0005881]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]; secretory vesicle [GO:0099503]; synaptic vesicle [GO:0008021]; zymogen granule [GO:0042588]
|
GTP binding [GO:0005525]; GTP-dependent protein binding [GO:0030742]; GTPase activity [GO:0003924]; myosin V binding [GO:0031489]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Rab family
|
PTM: Phosphorylation of Thr-86 in the switch II region by LRRK2 prevents the association of RAB regulatory proteins, including CHM and CHML. {ECO:0000269|PubMed:29125462}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Protein transport. Probably involved in regulated exocytosis (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O95718
|
ERR2_HUMAN
|
MSSDDRHLGSSCGSFIKTEPSSPSSGIDALSHHSPSGSSDASGGFGLALGTHANGLDSPPMFAGAGLGGTPCRKSYEDCASGIMEDSAIKCEYMLNAIPKRLCLVCGDIASGYHYGVASCEACKAFFKRTIQGNIEYSCPATNECEITKRRRKSCQACRFMKCLKVGMLKEGVRLDRVRGGRQKYKRRLDSESSPYLSLQISPPAKKPLTKIVSYLLVAEPDKLYAMPPPGMPEGDIKALTTLCDLADRELVVIIGWAKHIPGFSSLSLGDQMSLLQSAWMEILILGIVYRSLPYDDKLVYAEDYIMDEEHSRLAGLLELYRAILQLVRRYKKLKVEKEEFVTLKALALANSDSMYIEDLEAVQKLQDLLHEALQDYELSQRHEEPWRTGKLLLTLPLLRQTAAKAVQHFYSVKLQGKVPMHKLFLEMLEAKV
| null | null |
cell dedifferentiation [GO:0043697]; cell population proliferation [GO:0008283]; inner ear development [GO:0048839]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; negative regulation of stem cell differentiation [GO:2000737]; photoreceptor cell maintenance [GO:0045494]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of stem cell population maintenance [GO:1902459]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of stem cell division [GO:2000035]; regulation of transcription by RNA polymerase II [GO:0006357]; stem cell division [GO:0017145]; stem cell population maintenance [GO:0019827]
|
chromatin [GO:0000785]; condensed chromosome [GO:0000793]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; estrogen response element binding [GO:0034056]; nuclear receptor activity [GO:0004879]; nuclear steroid receptor activity [GO:0003707]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II complex binding [GO:0000993]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]; steroid binding [GO:0005496]; zinc ion binding [GO:0008270]
|
PF00104;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family, NR3 subfamily
|
PTM: Acetylated by PCAF/KAT2 (in vitro). {ECO:0000269|PubMed:20484414}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18775884}. Cytoplasm {ECO:0000250|UniProtKB:Q61539}. Chromosome {ECO:0000250|UniProtKB:Q61539}.
| null | null | null | null | null |
FUNCTION: [Isoform 3]: Transcription factor that binds a canonical ESRRB recognition (ERRE) sequence 5'TCAAGGTCA-3' localized on promoter and enhancer of targets genes regulating their expression or their transcription activity (PubMed:17920186, PubMed:19755138). Plays a role, in a LIF-independent manner, in maintainance of self-renewal and pluripotency of embryonic and trophoblast stem cells through different signaling pathways including FGF signaling pathway and Wnt signaling pathways. Upon FGF signaling pathway activation, interacts with KDM1A by directly binding to enhancer site of ELF5 and EOMES and activating their transcription leading to self-renewal of trophoblast stem cells. Also regulates expression of multiple rod-specific genes and is required for survival of this cell type (By similarity). Plays a role as transcription factor activator of GATA6, NR0B1, POU5F1 and PERM1 (PubMed:23836911). Plays a role as transcription factor repressor of NFE2L2 transcriptional activity and ESR1 transcriptional activity (PubMed:17920186, PubMed:19755138). During mitosis remains bound to a subset of interphase target genes, including pluripotency regulators, through the canonical ESRRB recognition (ERRE) sequence, leading to their transcriptional activation in early G1 phase. Can coassemble on structured DNA elements with other transcription factors like SOX2, POU5F1, KDM1A and NCOA3 to trigger ESRRB-dependent gene activation. This mechanism, in the case of SOX2 corecruitment prevents the embryonic stem cells (ESCs) to epiblast stem cells (EpiSC) transition through positive regulation of NR0B1 that inhibits the EpiSC transcriptional program. Also plays a role inner ear development by controlling expression of ion channels and transporters and in early placentation (By similarity). {ECO:0000250|UniProtKB:Q61539, ECO:0000269|PubMed:17920186, ECO:0000269|PubMed:19755138, ECO:0000269|PubMed:23836911}.; FUNCTION: [Isoform 1]: Transcription factor that binds a canonical ESRRB recognition (ERRE) sequence 5'TCAAGGTCA-3' localized on promoter and enhancer of targets genes regulating their expression or their transcription activity. Positively regulates ESR1 transcriptional activity upon E2 stimulation. {ECO:0000269|PubMed:19755138}.
|
Homo sapiens (Human)
|
O95721
|
SNP29_HUMAN
|
MSAYPKSYNPFDDDGEDEGARPAPWRDARDLPDGPDAPADRQQYLRQEVLRRAEATAASTSRSLALMYESEKVGVASSEELARQRGVLERTEKMVDKMDQDLKISQKHINSIKSVFGGLVNYFKSKPVETPPEQNGTLTSQPNNRLKEAISTSKEQEAKYQASHPNLRKLDDTDPVPRGAGSAMSTDAYPKNPHLRAYHQKIDSNLDELSMGLGRLKDIALGMQTEIEEQDDILDRLTTKVDKLDVNIKSTERKVRQL
| null | null |
autophagosome maturation [GO:0097352]; autophagosome membrane docking [GO:0016240]; cilium assembly [GO:0060271]; exocytosis [GO:0006887]; membrane fusion [GO:0061025]; protein transport [GO:0015031]; synaptic vesicle fusion to presynaptic active zone membrane [GO:0031629]; synaptic vesicle priming [GO:0016082]; vesicle targeting [GO:0006903]
|
autophagosome [GO:0005776]; autophagosome membrane [GO:0000421]; azurophil granule membrane [GO:0035577]; centrosome [GO:0005813]; ciliary pocket membrane [GO:0020018]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]; presynapse [GO:0098793]; SNARE complex [GO:0031201]
|
SNAP receptor activity [GO:0005484]; syntaxin binding [GO:0019905]
| null |
1.20.5.110;
|
SNAP-25 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23217709}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Z2P6}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:25686604}; Peripheral membrane protein {ECO:0000305}. Cell projection, cilium membrane {ECO:0000269|PubMed:25686250}; Peripheral membrane protein {ECO:0000305}. Note=Appears to be mostly membrane-bound, probably via interaction with syntaxins, but a significant portion is cytoplasmic. Localizes to the ciliary pocket from where the cilium protrudes. {ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:25686250}.
| null | null | null | null | null |
FUNCTION: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. SNAP29 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane. Also plays a role in ciliogenesis by regulating membrane fusions. {ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:25686250, ECO:0000269|PubMed:25686604}.
|
Homo sapiens (Human)
|
O95727
|
CRTAM_HUMAN
|
MWWRVLSLLAWFPLQEASLTNHTETITVEEGQTLTLKCVTSLRKNSSLQWLTPSGFTIFLNEYPALKNSKYQLLHHSANQLSITVPNVTLQDEGVYKCLHYSDSVSTKEVKVIVLATPFKPILEASVIRKQNGEEHVVLMCSTMRSKPPPQITWLLGNSMEVSGGTLHEFETDGKKCNTTSTLIIHTYGKNSTVDCIIRHRGLQGRKLVAPFRFEDLVTDEETASDALERNSLSSQDPQQPTSTVSVTEDSSTSEIDKEEKEQTTQDPDLTTEANPQYLGLARKKSGILLLTLVSFLIFILFIIVQLFIMKLRKAHVIWKKENEVSEHTLESYRSRSNNEETSSEEKNGQSSHPMRCMNYITKLYSEAKTKRKENVQHSKLEEKHIQVPESIV
| null | null |
adaptive immune response [GO:0002250]; cell recognition [GO:0008037]; detection of stimulus [GO:0051606]; detection of tumor cell [GO:0002355]; establishment of T cell polarity [GO:0001768]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; lymphocyte migration into lymphoid organs [GO:0097021]; negative regulation of activated T cell proliferation [GO:0046007]; positive regulation of cytokine production [GO:0001819]; positive regulation of natural killer cell mediated cytotoxicity [GO:0045954]; positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target [GO:0002860]; positive regulation of type II interferon production [GO:0032729]; regulation of CD8-positive, alpha-beta T cell activation [GO:2001185]; regulation of T cell activation [GO:0050863]; regulation of T cell differentiation [GO:0045580]
|
immunological synapse [GO:0001772]; plasma membrane [GO:0005886]
|
identical protein binding [GO:0042802]; signaling receptor binding [GO:0005102]
|
PF08205;PF07686;
|
2.60.40.10;
|
Nectin family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q149L7}; Single-pass type I membrane protein {ECO:0000255}. Note=In a subset of CD4+ T-cells, colocalizes with SCRIB at the immunological synapse during the late phase of T-cell activation. {ECO:0000250|UniProtKB:Q149L7}.
| null | null | null | null | null |
FUNCTION: Mediates heterophilic cell-cell adhesion which regulates the activation, differentiation and tissue retention of various T-cell subsets (By similarity). Interaction with CADM1 promotes natural killer (NK) cell cytotoxicity and IFNG/interferon-gamma secretion by CD8+ T-cells in vitro as well as NK cell-mediated rejection of tumors expressing CADM1 in vivo (PubMed:15811952). Regulates CD8+ T-cell proliferation in response to T-cell receptor (TCR) activation (By similarity). Appears to be dispensable for CD8+ T-cell-mediated cytotoxicity (By similarity). Interaction with SCRIB promotes the late phase of cellular polarization of a subset of CD4+ T-cells, which in turn regulates TCR-mediated proliferation and IFNG, IL17 and IL22 production (By similarity). By interacting with CADM1 on CD8+ dendritic cells, regulates the retention of activated CD8+ T-cells within the draining lymph node (By similarity). Required for the intestinal retention of intraepithelial CD4+ CD8+ T-cells and, to a lesser extent, intraepithelial and lamina propria CD8+ T-cells and CD4+ T-cells (By similarity). Interaction with CADM1 promotes the adhesion to gut-associated CD103+ dendritic cells, which may facilitate the expression of gut-homing and adhesion molecules on T-cells and the conversion of CD4+ T-cells into CD4+ CD8+ T-cells (By similarity). {ECO:0000250|UniProtKB:Q149L7, ECO:0000269|PubMed:15811952}.
|
Homo sapiens (Human)
|
O95741
|
CPNE6_HUMAN
|
MSDPEMGWVPEPPTMTLGASRVELRVSCHGLLDRDTLTKPHPCVLLKLYSDEQWVEVERTEVLRSCSSPVFSRVLALEYFFEEKQPLQFHVFDAEDGATSPRNDTFLGSTECTLGQIVSQTKVTKPLLLKNGKTAGKSTITIVAEEVSGTNDYVQLTFRAYKLDNKDLFSKSDPFMEIYKTNEDQSDQLVWRTEVVKNNLNPSWEPFRLSLHSLCSCDVHRPLKFLVYDYDSSGKHDFIGEFTSTFQEMQEGTANPGQEMQWDCINPKYRDKKKNYKSSGTVVLAQCTVEKVHTFLDYIMGGCQISFTVAIDFTASNGDPRSSQSLHCLSPRQPNHYLQALRAVGGICQDYDSDKRFPAFGFGARIPPNFEVSHDFAINFDPENPECEEISGVIASYRRCLPQIQLYGPTNVAPIINRVAEPAQREQSTGQATKYSVLLVLTDGVVSDMAETRTAIVRASRLPMSIIIVGVGNADFSDMRLLDGDDGPLRCPRGVPAARDIVQFVPFRDFKDAAPSALAKCVLAEVPRQVVEYYASQGISPGAPRPCTLATTPSPSP
| null |
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
|
cell differentiation [GO:0030154]; cellular response to calcium ion [GO:0071277]; positive regulation of dendrite extension [GO:1903861]; postsynaptic actin cytoskeleton organization [GO:0098974]
|
axon [GO:0030424]; clathrin-coated endocytic vesicle [GO:0045334]; dendrite [GO:0030425]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; phosphatidylserine binding [GO:0001786]
|
PF00168;PF07002;
|
2.60.40.150;
|
Copine family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Z140}. Cell membrane {ECO:0000250|UniProtKB:Q9Z140}. Endosome {ECO:0000250|UniProtKB:Q9Z140}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q9Z140}. Perikaryon {ECO:0000250|UniProtKB:Q9Z140}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9Z140}. Note=Mainly cytoplasmic in absence of calcium. Associated predominantly with membranes in presence of calcium. Translocates to the cell membrane in a calcium-dependent manner. Colocalized with transferrin in intracellular clathrin-coated membrane vesicles in a calcium-dependent manner. {ECO:0000250|UniProtKB:Q9Z140}.
| null | null | null | null | null |
FUNCTION: Calcium-dependent phospholipid-binding protein that plays a role in calcium-mediated intracellular processes. Binds phospholipid membranes in a calcium-dependent manner (By similarity). Plays a role in dendrite formation by melanocytes (PubMed:23999003). {ECO:0000250|UniProtKB:Q9Z140, ECO:0000269|PubMed:23999003}.
|
Homo sapiens (Human)
|
O95747
|
OXSR1_HUMAN
|
MSEDSSALPWSINRDDYELQEVIGSGATAVVQAAYCAPKKEKVAIKRINLEKCQTSMDELLKEIQAMSQCHHPNIVSYYTSFVVKDELWLVMKLLSGGSVLDIIKHIVAKGEHKSGVLDESTIATILREVLEGLEYLHKNGQIHRDVKAGNILLGEDGSVQIADFGVSAFLATGGDITRNKVRKTFVGTPCWMAPEVMEQVRGYDFKADIWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPSLETGVQDKEMLKKYGKSFRKMISLCLQKDPEKRPTAAELLRHKFFQKAKNKEFLQEKTLQRAPTISERAKKVRRVPGSSGRLHKTEDGGWEWSDDEFDEESEEGKAAISQLRSPRVKESISNSELFPTTDPVGTLLQVPEQISAHLPQPAGQIATQPTQVSLPPTAEPAKTAQALSSGSGSQETKIPISLVLRLRNSKKELNDIRFEFTPGRDTAEGVSQELISAGLVDGRDLVIVAANLQKIVEEPQSNRSVTFKLASGVEGSDIPDDGKLIGFAQLSIS
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:14707132};
|
cell volume homeostasis [GO:0006884]; cellular hyperosmotic response [GO:0071474]; cellular hypotonic response [GO:0071476]; cellular response to chemokine [GO:1990869]; chemokine (C-C motif) ligand 21 signaling pathway [GO:0038116]; chemokine (C-X-C motif) ligand 12 signaling pathway [GO:0038146]; intracellular signal transduction [GO:0035556]; negative regulation of potassium ion transmembrane transport [GO:1901380]; osmosensory signaling pathway [GO:0007231]; peptidyl-threonine phosphorylation [GO:0018107]; positive regulation of T cell chemotaxis [GO:0010820]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; renal sodium ion absorption [GO:0070294]; response to oxidative stress [GO:0006979]; response to xenobiotic stimulus [GO:0009410]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]
|
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF12202;PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
|
PTM: Phosphorylation at Thr-185 by WNK kinases (WNK1, WNK2, WNK3 or WNK4) is required for activation (PubMed:16669787, PubMed:16832045, PubMed:17190791, PubMed:21321328, PubMed:22989884, PubMed:29581290). Autophosphorylated; promoting its activity (PubMed:14707132, PubMed:22052202). {ECO:0000269|PubMed:14707132, ECO:0000269|PubMed:16669787, ECO:0000269|PubMed:16832045, ECO:0000269|PubMed:17190791, ECO:0000269|PubMed:21321328, ECO:0000269|PubMed:22052202, ECO:0000269|PubMed:22989884, ECO:0000269|PubMed:29581290}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22361696, ECO:0000269|PubMed:22989884}.
|
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:14707132, ECO:0000269|PubMed:21321328}; 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:14707132, ECO:0000269|PubMed:16669787, ECO:0000269|PubMed:18270262, ECO:0000269|PubMed:21321328};
| null | null | null | null |
FUNCTION: Effector serine/threonine-protein kinase component of the WNK-SPAK/OSR1 kinase cascade, which is involved in various processes, such as ion transport, response to hypertonic stress and blood pressure (PubMed:16669787, PubMed:18270262, PubMed:21321328, PubMed:34289367). Specifically recognizes and binds proteins with a RFXV motif (PubMed:16669787, PubMed:17721439, PubMed:21321328). Acts downstream of WNK kinases (WNK1, WNK2, WNK3 or WNK4): following activation by WNK kinases, catalyzes phosphorylation of ion cotransporters, such as SLC12A1/NKCC2, SLC12A2/NKCC1, SLC12A3/NCC, SLC12A5/KCC2 or SLC12A6/KCC3, regulating their activity (PubMed:17721439). Mediates regulatory volume increase in response to hyperosmotic stress by catalyzing phosphorylation of ion cotransporters SLC12A1/NKCC2, SLC12A2/NKCC1 and SLC12A6/KCC3 downstream of WNK1 and WNK3 kinases (PubMed:16669787, PubMed:21321328). Phosphorylation of Na-K-Cl cotransporters SLC12A2/NKCC1 and SLC12A2/NKCC1 promote their activation and ion influx; simultaneously, phosphorylation of K-Cl cotransporters SLC12A5/KCC2 and SLC12A6/KCC3 inhibit their activity, blocking ion efflux (PubMed:16669787, PubMed:19665974, PubMed:21321328). Acts as a regulator of NaCl reabsorption in the distal nephron by mediating phosphorylation and activation of the thiazide-sensitive Na-Cl cotransporter SLC12A3/NCC in distal convoluted tubule cells of kidney downstream of WNK4 (PubMed:18270262). Also acts as a regulator of angiogenesis in endothelial cells downstream of WNK1 (PubMed:23386621, PubMed:25362046). Acts as an activator of inward rectifier potassium channels KCNJ2/Kir2.1 and KCNJ4/Kir2.3 downstream of WNK1: recognizes and binds the RXFXV/I variant motif on KCNJ2/Kir2.1 and KCNJ4/Kir2.3 and regulates their localization to the cell membrane without mediating their phosphorylation (PubMed:29581290). Phosphorylates RELL1, RELL2 and RELT (PubMed:16389068, PubMed:28688764). Phosphorylates PAK1 (PubMed:14707132). Phosphorylates PLSCR1 in the presence of RELT (PubMed:22052202). {ECO:0000269|PubMed:14707132, ECO:0000269|PubMed:16389068, ECO:0000269|PubMed:16669787, ECO:0000269|PubMed:17721439, ECO:0000269|PubMed:18270262, ECO:0000269|PubMed:19665974, ECO:0000269|PubMed:21321328, ECO:0000269|PubMed:22052202, ECO:0000269|PubMed:23386621, ECO:0000269|PubMed:25362046, ECO:0000269|PubMed:28688764, ECO:0000269|PubMed:29581290, ECO:0000269|PubMed:34289367}.
|
Homo sapiens (Human)
|
O95749
|
GGPPS_HUMAN
|
MEKTQETVQRILLEPYKYLLQLPGKQVRTKLSQAFNHWLKVPEDKLQIIIEVTEMLHNASLLIDDIEDNSKLRRGFPVAHSIYGIPSVINSANYVYFLGLEKVLTLDHPDAVKLFTRQLLELHQGQGLDIYWRDNYTCPTEEEYKAMVLQKTGGLFGLAVGLMQLFSDYKEDLKPLLNTLGLFFQIRDDYANLHSKEYSENKSFCEDLTEGKFSFPTIHAIWSRPESTQVQNILRQRTENIDIKKYCVHYLEDVGSFEYTRNTLKELEAKAYKQIDARGGNPELVALVKHLSKMFKEENE
|
2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; Note=Binds 3 Mg(2+) ions. {ECO:0000305};
|
farnesyl diphosphate biosynthetic process [GO:0045337]; geranyl diphosphate biosynthetic process [GO:0033384]; geranylgeranyl diphosphate biosynthetic process [GO:0033386]; isoprenoid biosynthetic process [GO:0008299]; isoprenoid metabolic process [GO:0006720]; plastoquinone biosynthetic process [GO:0010236]; ubiquinone biosynthetic process [GO:0006744]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; transferase complex [GO:1990234]; Z disc [GO:0030018]
|
dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; prenyltransferase activity [GO:0004659]
|
PF00348;
|
1.10.600.10;
|
FPP/GGPP synthase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32403198}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:32403198}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:32403198}.
|
CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000269|PubMed:16698791}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.10; Evidence={ECO:0000269|PubMed:16698791}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; Evidence={ECO:0000269|PubMed:16698791};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3 uM for isopentenyl diphosphate {ECO:0000269|PubMed:16698791}; KM=4.2 uM for farnesyl diphosphate {ECO:0000269|PubMed:16698791};
|
PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1.; PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1.; PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and isopentenyl diphosphate: step 1/1.
| null | null |
FUNCTION: Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins. {ECO:0000269|PubMed:32403198}.
|
Homo sapiens (Human)
|
O95750
|
FGF19_HUMAN
|
MRSGCVVVHVWILAGLWLAVAGRPLAFSDAGPHVHYGWGDPIRLRHLYTSGPHGLSSCFLRIRADGVVDCARGQSAHSLLEIKAVALRTVAIKGVHSVRYLCMGADGKMQGLLQYSEEDCAFEEEIRPDGYNVYRSEKHRLPVSLSSAKQRQLYKNRGFLPLSHFLPMLPMVPEEPEDLRGHLESDMFSSPLETDSMDPFGLVTGLEAVRSPSFEK
| null | null |
animal organ morphogenesis [GO:0009887]; cell differentiation [GO:0030154]; fibroblast growth factor receptor signaling pathway [GO:0008543]; negative regulation of bile acid biosynthetic process [GO:0070858]; negative regulation of gene expression [GO:0010629]; nervous system development [GO:0007399]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of gene expression [GO:0010628]; positive regulation of glucose import [GO:0046326]; positive regulation of JNK cascade [GO:0046330]; positive regulation of protein phosphorylation [GO:0001934]; regulation of cell migration [GO:0030334]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083]
|
PF00167;
|
2.80.10.50;
|
Heparin-binding growth factors family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Involved in the suppression of bile acid biosynthesis through down-regulation of CYP7A1 expression, following positive regulation of the JNK and ERK1/2 cascades. Stimulates glucose uptake in adipocytes. Activity requires the presence of KLB and FGFR4. {ECO:0000269|PubMed:12815072, ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:17623664, ECO:0000269|PubMed:19085950}.
|
Homo sapiens (Human)
|
O95751
|
LDOC1_HUMAN
|
MVDELVLLLHALLMRHRALSIENSQLMEQLRLLVCERASLLRQVRPPSCPVPFPETFNGESSRLPEFIVQTASYMLVNENRFCNDAMKVAFLISLLTGEAEEWVVPYIEMDSPILGDYRAFLDEMKQCFGWDDDEDDDDEEEEDDY
| null | null |
cellular response to lipopolysaccharide [GO:0071222]; cellular response to muramyl dipeptide [GO:0071225]; maternal placenta development [GO:0001893]; maternal process involved in parturition [GO:0060137]; negative regulation of cell population proliferation [GO:0008285]
|
nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
| null |
PF16297;
| null |
LDOC1 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10403563}.
| null | null | null | null | null |
FUNCTION: May have an important role in the development and/or progression of some cancers.
|
Homo sapiens (Human)
|
O95754
|
SEM4F_HUMAN
|
MPASAARPRPGPGQPTASPFPLLLLAVLSGPVSGRVPRSVPRTSLPISEADSCLTRFAVPHTYNYSVLLVDPASHTLYVGARDTIFALSLPFSGERPRRIDWMVPEAHRQNCRKKGKKEDECHNFVQILAIANASHLLTCGTFAFDPKCGVIDVSRFQQVERLESGRGKCPFEPAQRSAAVMAGGVLYAATVKNYLGTEPIITRAVGRAEDWIRTDTLPSWLNAPAFVAAVALSPAEWGDEDGDDEIYFFFTETSRAFDSYERIKVPRVARVCAGDLGGRKTLQQRWTTFLKADLLCPGPEHGRASSVLQDVAVLRPELGAGTPIFYGIFSSQWEGATISAVCAFRPQDIRTVLNGPFRELKHDCNRGLPVVDNDVPQPRPGECITNNMKLRHFGSSLSLPDRVLTFIRDHPLMDRPVFPADGHPLLVTTDTAYLRVVAHRVTSLSGKEYDVLYLGTEDGHLHRAVRIGAQLSVLEDLALFPEPQPVENMKLYHSWLLVGSRTEVTQVNTTNCGRLQSCSECILAQDPVCAWSFRLDECVAHAGEHRGLVQDIESADVSSLCPKEPGERPVVFEVPVATAAHVVLPCSPSSAWASCVWHQPSGVTALTPRRDGLEVVVTPGAMGAYACECQEGGAAHVVAAYSLVWGSQRDAPSRAHTVGAGLAGFFLGILAASLTLILIGRRQQRRRQRELLARDKVGLDLGAPPSGTTSYSQDPPSPSPEDERLPLALAKRGSGFGGFSPPFLLDPCPSPAHIRLTGAPLATCDETSI
| null | null |
axon guidance [GO:0007411]; cell-cell signaling [GO:0007267]; negative chemotaxis [GO:0050919]; negative regulation of axon extension involved in axon guidance [GO:0048843]; nervous system development [GO:0007399]; neural crest cell migration [GO:0001755]; positive regulation of cell migration [GO:0030335]; retinal ganglion cell axon guidance [GO:0031290]; semaphorin-plexin signaling pathway [GO:0071526]
|
dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]
|
chemorepellent activity [GO:0045499]; semaphorin receptor binding [GO:0030215]
|
PF01437;PF01403;PF19428;
|
3.30.1680.10;2.130.10.10;
|
Semaphorin family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}. Postsynaptic density {ECO:0000250|UniProtKB:Q9Z143}. Perikaryon {ECO:0000250|UniProtKB:Q9Z123}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9Z123}. Note=Colocalizes with DLG4 at synapses. {ECO:0000250|UniProtKB:Q9Z123}.
| null | null | null | null | null |
FUNCTION: Probable cell surface receptor that regulates oligodendroglial precursor cell migration (By similarity). Might also regulate differentiation of oligodendroglial precursor cells (By similarity). Has growth cone collapse activity against retinal ganglion-cell axons (By similarity). {ECO:0000250|UniProtKB:Q9Z123, ECO:0000250|UniProtKB:Q9Z143}.
|
Homo sapiens (Human)
|
O95758
|
PTBP3_HUMAN
|
MDGVVTDLITVGLKRGSDELLSSGIINGPFTMNSSTPSTANGNDSKKFKRDRPPCSPSRVLHLRKIPCDVTEAEIISLGLPFGKVTNLLMLKGKSQAFLEMASEEAAVTMVNYYTPITPHLRSQPVYIQYSNHRELKTDNLPNQARAQAALQAVSAVQSGSLALSGGPSNEGTVLPGQSPVLRIIIENLFYPVTLEVLHQIFSKFGTVLKIITFTKNNQFQALLQYADPVNAHYAKMALDGQNIYNACCTLRIDFSKLTSLNVKYNNDKSRDFTRLDLPTGDGQPSLEPPMAAAFGAPGIISSPYAGAAGFAPAIGFPQATGLSVPAVPGALGPLTITSSAVTGRMAIPGASGIPGNSVLLVTNLNPDLITPHGLFILFGVYGDVHRVKIMFNKKENALVQMADANQAQLAMNHLSGQRLYGKVLRATLSKHQAVQLPREGQEDQGLTKDFSNSPLHRFKKPGSKNFQNIFPPSATLHLSNIPPSVTVDDLKNLFIEAGCSVKAFKFFQKDRKMALIQLGSVEEAIQALIELHNHDLGENHHLRVSFSKSTI
| null | null |
anatomical structure morphogenesis [GO:0009653]; erythrocyte maturation [GO:0043249]; mRNA processing [GO:0006397]; negative regulation of RNA splicing [GO:0033119]; regulation of cell differentiation [GO:0045595]; regulation of RNA splicing [GO:0043484]; RNA splicing [GO:0008380]
|
nucleus [GO:0005634]
|
mRNA binding [GO:0003729]; RNA binding [GO:0003723]
|
PF13893;PF11835;
|
3.30.70.330;
| null | null | null | null | null | null | null | null |
FUNCTION: RNA-binding protein that mediates pre-mRNA alternative splicing regulation. Plays a role in the regulation of cell proliferation, differentiation and migration. Positive regulator of EPO-dependent erythropoiesis. Participates in cell differentiation regulation by repressing tissue-specific exons. Promotes FAS exon 6 skipping. Binds RNA, preferentially to both poly(G) and poly(U). {ECO:0000269|PubMed:10207106, ECO:0000269|PubMed:18335065, ECO:0000269|PubMed:19441079, ECO:0000269|PubMed:20937273}.
|
Homo sapiens (Human)
|
O95760
|
IL33_HUMAN
|
MKPKMKYSTNKISTAKWKNTASKALCFKLGKSQQKAKEVCPMYFMKLRSGLMIKKEACYFRRETTKRPSLKTGRKHKRHLVLAACQQQSTVECFAFGISGVQKYTRALHDSSITGISPITEYLASLSTYNDQSITFALEDESYEIYVEDLKKDEKKDKVLLSYYESQHPSNESGDGVDGKMLMVTLSPTKDFWLHANNKEHSVELHKCEKPLPDQAFFVLHNMHSNCVSFECKTDPGVFIGVKDNHLALIKVDSSENLCTENILFKLSET
| null | null |
cellular response to mechanical stimulus [GO:0071260]; defense response to virus [GO:0051607]; extrinsic apoptotic signaling pathway [GO:0097191]; gene expression [GO:0010467]; interleukin-33-mediated signaling pathway [GO:0038172]; macrophage differentiation [GO:0030225]; microglial cell activation involved in immune response [GO:0002282]; microglial cell proliferation [GO:0061518]; negative regulation of immunoglobulin production [GO:0002638]; negative regulation of inflammatory response to wounding [GO:0106015]; negative regulation of leukocyte migration [GO:0002686]; negative regulation of macrophage proliferation [GO:0120042]; negative regulation of T-helper 1 type immune response [GO:0002826]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of type II interferon production [GO:0032689]; positive regulation of CD80 production [GO:0150145]; positive regulation of CD86 production [GO:0150142]; positive regulation of cellular defense response [GO:0010186]; positive regulation of chemokine production [GO:0032722]; positive regulation of cytokine production [GO:0001819]; positive regulation of gene expression [GO:0010628]; positive regulation of immunoglobulin production [GO:0002639]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interleukin-13 production [GO:0032736]; positive regulation of interleukin-4 production [GO:0032753]; positive regulation of interleukin-5 production [GO:0032754]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of macrophage activation [GO:0043032]; positive regulation of MHC class I biosynthetic process [GO:0045345]; positive regulation of MHC class II biosynthetic process [GO:0045348]; positive regulation of neuroinflammatory response [GO:0150078]; positive regulation of nitric-oxide synthase biosynthetic process [GO:0051770]; positive regulation of oligodendrocyte differentiation [GO:0048714]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of type 2 immune response [GO:0002830]; protein import into nucleus [GO:0006606]; type 2 immune response [GO:0042092]
|
chromosome [GO:0005694]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transport vesicle [GO:0030133]
|
cytokine activity [GO:0005125]; interleukin-33 receptor binding [GO:0002112]
|
PF15095;
|
2.80.10.50;
|
IL-1 family
|
PTM: The full-length protein can be released from cells and is able to signal via the IL1RL1/ST2 receptor. However, proteolytic processing by CELA1, CSTG/cathepsin G and ELANE/neutrophil elastase produces C-terminal peptides that are more active than the unprocessed full length protein (PubMed:22307629, PubMed:35794369). May also be proteolytically processed by calpains (PubMed:19596270, PubMed:22307629). Proteolytic cleavage mediated by apoptotic caspases including CASP3 and CASP7 results in IL33 inactivation (PubMed:19559631). In vitro proteolytic cleavage by CASP1 was reported (PubMed:16286016, PubMed:19439663) but could not be confirmed in vivo (PubMed:19465481) suggesting that IL33 is probably not a direct substrate for that caspase (PubMed:19439663, PubMed:19465481). {ECO:0000269|PubMed:16286016, ECO:0000269|PubMed:19439663, ECO:0000269|PubMed:19465481, ECO:0000269|PubMed:19559631, ECO:0000269|PubMed:19596270, ECO:0000269|PubMed:22307629, ECO:0000269|PubMed:35794369}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12819012, ECO:0000269|PubMed:17185418, ECO:0000269|PubMed:18787100, ECO:0000269|PubMed:18836528, ECO:0000269|PubMed:21734074}. Chromosome {ECO:0000269|PubMed:17185418}. Cytoplasm {ECO:0000269|PubMed:32272059}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:22215666}. Secreted {ECO:0000269|PubMed:19465481, ECO:0000269|PubMed:35794369}. Note=Secreted and released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore following cleavage by CELA1 (PubMed:35794369). Associates with heterochromatin and mitotic chromosomes (PubMed:17185418). The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (PubMed:32272059). {ECO:0000269|PubMed:32272059, ECO:0000269|PubMed:35794369}.
| null | null | null | null | null |
FUNCTION: Cytokine that binds to and signals through the IL1RL1/ST2 receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells (PubMed:16286016, PubMed:19841166). Involved in the maturation of Th2 cells inducing the secretion of T-helper type 2-associated cytokines (PubMed:17853410, PubMed:18836528). Also involved in activation of mast cells, basophils, eosinophils and natural killer cells (PubMed:17853410, PubMed:18836528). Acts as an enhancer of polarization of alternatively activated macrophages (PubMed:19841166). Acts as a chemoattractant for Th2 cells, and may function as an 'alarmin', that amplifies immune responses during tissue injury (PubMed:17853410, PubMed:18836528). Induces rapid UCP2-dependent mitochondrial rewiring that attenuates the generation of reactive oxygen species and preserves the integrity of Krebs cycle required for persistent production of itaconate and subsequent GATA3-dependent differentiation of inflammation-resolving alternatively activated macrophages (By similarity). {ECO:0000250|UniProtKB:Q8BVZ5, ECO:0000269|PubMed:16286016, ECO:0000269|PubMed:17853410, ECO:0000269|PubMed:18836528, ECO:0000269|PubMed:19841166}.; FUNCTION: In quiescent endothelia the uncleaved form is constitutively and abundantly expressed, and acts as a chromatin-associated nuclear factor with transcriptional repressor properties, it may sequester nuclear NF-kappaB/RELA, lowering expression of its targets (PubMed:21734074). This form is rapidely lost upon angiogenic or pro-inflammatory activation (PubMed:18787100). {ECO:0000269|PubMed:18787100, ECO:0000269|PubMed:21734074}.
|
Homo sapiens (Human)
|
O95772
|
STR3N_HUMAN
|
MNHLPEDMENALTGSQSSHASLRNIHSINPTQLMARIESYEGREKKGISDVRRTFCLFVTFDLLFVTLLWIIELNVNGGIENTLEKEVMQYDYYSSYFDIFLLAVFRFKVLILAYAVCRLRHWWAIALTTAVTSAFLLAKVILSKLFSQGAFGYVLPIISFILAWIETWFLDFKVLPQEAEEENRLLIVQDASERAALIPGGLSDGQFYSPPESEAGSEEAEEKQDSEKPLLEL
| null | null |
cholesterol transport [GO:0030301]; vesicle tethering to endoplasmic reticulum [GO:0099044]
|
cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-endosome membrane contact site [GO:0140284]; endosome [GO:0005768]; intracellular membrane-bounded organelle [GO:0043231]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; organelle membrane contact site [GO:0044232]
|
cholesterol binding [GO:0015485]; protein homodimerization activity [GO:0042803]
|
PF10457;
| null |
STARD3 family
| null |
SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:24105263, ECO:0000269|PubMed:29858488}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to contact sites between the endoplasmic reticulum and late endosomes: associates with the endoplasmic reticulum membrane via interaction with VAPA, VAPB or MOSPD2. {ECO:0000269|PubMed:24105263}.
| null | null | null | null | null |
FUNCTION: Tethering protein that creates contact site between the endoplasmic reticulum and late endosomes: localizes to late endosome membranes and contacts the endoplasmic reticulum via interaction with VAPA and VAPB (PubMed:24105263). {ECO:0000269|PubMed:24105263}.
|
Homo sapiens (Human)
|
O95777
|
LSM8_HUMAN
|
MTSALENYINRTVAVITSDGRMIVGTLKGFDQTINLILDESHERVFSSSQGVEQVVLGLYIVRGDNVAVIGEIDEETDSALDLGNIRAEPLNSVAH
| null | null |
mRNA splicing, via spliceosome [GO:0000398]
|
Lsm2-8 complex [GO:0120115]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; precatalytic spliceosome [GO:0071011]; U2-type precatalytic spliceosome [GO:0071005]; U4/U6 x U5 tri-snRNP complex [GO:0046540]; U6 snRNP [GO:0005688]
|
mRNA binding [GO:0003729]; RNA binding [GO:0003723]; U6 snRNA binding [GO:0017070]
|
PF01423;
|
2.30.30.100;
|
SnRNP Sm proteins family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10523320, ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166}.
| null | null | null | null | null |
FUNCTION: Plays a role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex) (PubMed:28781166). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA (PubMed:10523320). {ECO:0000269|PubMed:10523320, ECO:0000269|PubMed:28781166}.
|
Homo sapiens (Human)
|
O95782
|
AP2A1_HUMAN
|
MPAVSKGDGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNKYTEKQIGYLFISVLVNSNSELIRLINNAIKNDLASRNPTFMCLALHCIANVGSREMGEAFAADIPRILVAGDSMDSVKQSAALCLLRLYKASPDLVPMGEWTARVVHLLNDQHMGVVTAAVSLITCLCKKNPDDFKTCVSLAVSRLSRIVSSASTDLQDYTYYFVPAPWLSVKLLRLLQCYPPPEDAAVKGRLVECLETVLNKAQEPPKSKKVQHSNAKNAILFETISLIIHYDSEPNLLVRACNQLGQFLQHRETNLRYLALESMCTLASSEFSHEAVKTHIDTVINALKTERDVSVRQRAADLLYAMCDRSNAKQIVSEMLRYLETADYAIREEIVLKVAILAEKYAVDYSWYVDTILNLIRIAGDYVSEEVWYRVLQIVTNRDDVQGYAAKTVFEALQAPACHENMVKVGGYILGEFGNLIAGDPRSSPPVQFSLLHSKFHLCSVATRALLLSTYIKFINLFPETKATIQGVLRAGSQLRNADVELQQRAVEYLTLSSVASTDVLATVLEEMPPFPERESSILAKLKRKKGPGAGSALDDGRRDPSSNDINGGMEPTPSTVSTPSPSADLLGLRAAPPPAAPPASAGAGNLLVDVFDGPAAQPSLGPTPEEAFLSELEPPAPESPMALLADPAPAADPGPEDIGPPIPEADELLNKFVCKNNGVLFENQLLQIGVKSEFRQNLGRMYLFYGNKTSVQFQNFSPTVVHPGDLQTQLAVQTKRVAAQVDGGAQVQQVLNIECLRDFLTPPLLSVRFRYGGAPQALTLKLPVTINKFFQPTEMAAQDFFQRWKQLSLPQQEAQKIFKANHPMDAEVTKAKLLGFGSALLDNVDPNPENFVGAGIIQTKALQVGCLLRLEPNAQAQMYRLTLRTSKEPVSRHLCELLAQQF
| null | null |
clathrin-dependent endocytosis [GO:0072583]; endocytosis [GO:0006897]; Golgi to endosome transport [GO:0006895]; intracellular protein transport [GO:0006886]; negative regulation of hyaluronan biosynthetic process [GO:1900126]; positive regulation of neuron projection development [GO:0010976]; positive regulation of receptor-mediated endocytosis [GO:0048260]; postsynaptic neurotransmitter receptor internalization [GO:0098884]; vesicle-mediated transport [GO:0016192]
|
AP-2 adaptor complex [GO:0030122]; apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; clathrin coat of trans-Golgi network vesicle [GO:0030130]; clathrin-coated endocytic vesicle [GO:0045334]; clathrin-coated endocytic vesicle membrane [GO:0030669]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; endocytic vesicle membrane [GO:0030666]; endolysosome membrane [GO:0036020]; filopodium tip [GO:0032433]; membrane [GO:0016020]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]
|
clathrin adaptor activity [GO:0035615]; low-density lipoprotein particle receptor binding [GO:0050750]; protein kinase binding [GO:0019901]; protein-containing complex binding [GO:0044877]
|
PF01602;PF02296;PF02883;
|
2.60.40.1230;1.25.10.10;3.30.310.10;
|
Adaptor complexes large subunit family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16262731}. Membrane, coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. During long-term potentiation in hippocampal neurons, AP-2 is responsible for the endocytosis of ADAM10 (PubMed:23676497). The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif (By similarity). {ECO:0000250, ECO:0000269|PubMed:14745134, ECO:0000269|PubMed:15473838, ECO:0000269|PubMed:19033387, ECO:0000269|PubMed:23676497}.
|
Homo sapiens (Human)
|
O95785
|
WIZ_HUMAN
|
MEGSLAGSLAAPDRPQGPERLPGPAPRENIEGGAEAAEGEGGIFRSTRYLPVTKEGPRDILDGRGGISGTPDGRGPWEHPLVQEAGEGILSERRFEDSVIVRTMKPHAELEGSRRFLHHRGEPRLLEKHAQGRPRFDWLQDEDEQGSPQDAGLHLDLPAQPPPLAPFRRVFVPVEDTPKTLDMAVVGGREDLEDLEGLAQPSEWGLPTSASEVATQTWTVNSEASVERLQPLLPPIRTGPYLCELLEEVAEGVASPDEDEDEEPAVFPCIECSIYFKQKEHLLEHMSQHRRAPGQEPPADLAPLACGECGWAFADPTALEQHRQLHQASREKIIEEIQKLKQVPGDEGREARLQCPKCVFGTNSSRAYVQHAKLHMREPPGQTTKEPFGGSSGAGSPSPEASALLYQPYGAAVGLSACVFCGFPAPSESLLREHVRLVHAHPHWEEDGEAYEEDPASQPGTSQDAHACFPDTAVDYFGKAEPSLAPMWRENPAGYDPSLAFGPGCQQLSIRDFPLSKPLLHGTGQRPLGRLAFPSTLASTPYSLQLGRNKSTVHPQGLGERRRPWSEEEEEEEEEEDVVLTSEMDFSPENGVFSPLATPSLIPQAALELKQAFREALQAVEATQGQQQQLRGMVPIVLVAKLGPQVMAAARVPPRLQPEELGLAGAHPLDFLLLDAPLGGPLGLDTLLDGDPAMALKHEERKCPYCPDRFHNGIGLANHVRGHLNRVGVSYNVRHFISAEEVKAIERRFSFQKKKKKVANFDPGTFSLMRCDFCGAGFDTRAGLSSHARAHLRDFGITNWELTVSPINILQELLATSAAEQPPSPLGREPGGPPGSFLTSRRPRLPLTVPFPPTWAEDPGPAYGDAQSLTTCEVCGACFETRKGLSSHARSHLRQLGVAESESSGAPIDLLYELVKQKGLPDAHLGLPPGLAKKSSSLKEVVAGAPRPGLLSLAKPLDAPAVNKAIKSPPGFSAKGLGHPPSSPLLKKTPLALAGSPTPKNPEDKSPQLSLSPRPASPKAQWPQSEDEGPLNLTSGPEPARDIRCEFCGEFFENRKGLSSHARSHLRQMGVTEWYVNGSPIDTLREILKRRTQSRPGGPPNPPGPSPKALAKMMGGAGPGSSLEARSPSDLHISPLAKKLPPPPGSPLGHSPTASPPPTARKMFPGLAAPSLPKKLKPEQIRVEIKREMLPGALHGELHPSEGPWGAPREDMTPLNLSSRAEPVRDIRCEFCGEFFENRKGLSSHARSHLRQMGVTEWSVNGSPIDTLREILKKKSKPCLIKKEPPAGDLAPALAEDGPPTVAPGPVQSPLPLSPLAGRPGKPGAGPAQVPRELSLTPITGAKPSATGYLGSVAAKRPLQEDRLLPAEVKAKTYIQTELPFKAKTLHEKTSHSSTEACCELCGLYFENRKALASHARAHLRQFGVTEWCVNGSPIETLSEWIKHRPQKVGAYRSYIQGGRPFTKKFRSAGHGRDSDKRPSLGLAPGGLAVVGRSAGGEPGPEAGRAADGGERPLAASPPGTVKAEEHQRQNINKFERRQARPPDASAARGGEDTNDLQQKLEEVRQPPPRVRPVPSLVPRPPQTSLVKFVGNIYTLKCRFCEVEFQGPLSIQEEWVRHLQRHILEMNFSKADPPPEESQAPQAQTAAAEAP
| null | null |
positive regulation of nuclear cell cycle DNA replication [GO:0010571]; protein stabilization [GO:0050821]; regulation of transcription by RNA polymerase II [GO:0006357]
|
extracellular exosome [GO:0070062]; midbody [GO:0030496]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; histone methyltransferase binding [GO:1990226]; metal ion binding [GO:0046872]; protein-containing complex binding [GO:0044877]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription corepressor binding [GO:0001222]
| null |
3.30.160.60;
|
Krueppel C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May link EHMT1 and EHMT2 histone methyltransferases to the CTBP corepressor machinery. May be involved in EHMT1-EHMT2 heterodimer formation and stabilization (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O95786
|
RIGI_HUMAN
|
MTTEQRRSLQAFQDYIRKTLDPTYILSYMAPWFREEEVQYIQAEKNNKGPMEAATLFLKFLLELQEEGWFRGFLDALDHAGYSGLYEAIESWDFKKIEKLEEYRLLLKRLQPEFKTRIIPTDIISDLSECLINQECEEILQICSTKGMMAGAEKLVECLLRSDKENWPKTLKLALEKERNKFSELWIVEKGIKDVETEDLEDKMETSDIQIFYQEDPECQNLSENSCPPSEVSDTNLYSPFKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGKVVFFANQIPVYEQQKSVFSKYFERHGYRVTGISGATAENVPVEQIVENNDIIILTPQILVNNLKKGTIPSLSIFTLMIFDECHNTSKQHPYNMIMFNYLDQKLGGSSGPLPQVIGLTASVGVGDAKNTDEALDYICKLCASLDASVIATVKHNLEELEQVVYKPQKFFRKVESRISDKFKYIIAQLMRDTESLAKRICKDLENLSQIQNREFGTQKYEQWIVTVQKACMVFQMPDKDEESRICKALFLYTSHLRKYNDALIISEHARMKDALDYLKDFFSNVRAAGFDEIEQDLTQRFEEKLQELESVSRDPSNENPKLEDLCFILQEEYHLNPETITILFVKTRALVDALKNWIEGNPKLSFLKPGILTGRGKTNQNTGMTLPAQKCILDAFKASGDHNILIATSVADEGIDIAQCNLVILYEYVGNVIKMIQTRGRGRARGSKCFLLTSNAGVIEKEQINMYKEKMMNDSILRLQTWDEAVFREKILHIQTHEKFIRDSQEKPKPVPDKENKKLLCRKCKALACYTADVRVIEECHYTVLGDAFKECFVSRPHPKPKQFSSFEKRAKIFCARQNCSHDWGIHVKYKTFEIPVIKIESFVVEDIATGVQTLYSKWKDFHFEKIPFDPAEMSK
|
3.6.4.13
| null |
antiviral innate immune response [GO:0140374]; cellular response to exogenous dsRNA [GO:0071360]; cytoplasmic pattern recognition receptor signaling pathway [GO:0002753]; defense response to virus [GO:0051607]; detection of virus [GO:0009597]; gene expression [GO:0010467]; innate immune response [GO:0045087]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of gene expression [GO:0010628]; positive regulation of granulocyte macrophage colony-stimulating factor production [GO:0032725]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of myeloid dendritic cell cytokine production [GO:0002735]; positive regulation of response to cytokine stimulus [GO:0060760]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; regulation of cell migration [GO:0030334]; regulation of type III interferon production [GO:0034344]; response to exogenous dsRNA [GO:0043330]; response to virus [GO:0009615]; RIG-I signaling pathway [GO:0039529]
|
actin cytoskeleton [GO:0015629]; bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; ribonucleoprotein complex [GO:1990904]; ruffle membrane [GO:0032587]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded DNA binding [GO:0003690]; double-stranded RNA binding [GO:0003725]; GTP binding [GO:0005525]; identical protein binding [GO:0042802]; pattern recognition receptor activity [GO:0038187]; RNA helicase activity [GO:0003724]; single-stranded RNA binding [GO:0003727]; ubiquitin protein ligase binding [GO:0031625]; zinc ion binding [GO:0008270]
|
PF16739;PF00270;PF00271;PF18119;PF11648;
|
1.20.1320.30;1.10.533.10;3.40.50.300;2.170.150.30;
|
Helicase family, RLR subfamily
|
PTM: Phosphorylated in resting cells and dephosphorylated in RNA virus-infected cells. Phosphorylation at Thr-770, Ser-854 and Ser-855 results in inhibition of its activity while dephosphorylation at these sites results in its activation. {ECO:0000269|PubMed:21068236}.; PTM: Ubiquitinated. 'Lys-63' ubiquitination by RNF135, which occurs after RNA-binding and homodimerization, releases the autoinhibition of the CARD domains by the RLR CTR domain, an essential step in the activation of the RIG-I signaling pathway (PubMed:23950712, PubMed:28469175, PubMed:31006531). Lys-172 is the critical site of ubiquitination for MAVS/IPS1 binding and to induce anti-viral signal transduction (PubMed:17392790, PubMed:30193849). Lys-154, Lys-164 and Lys-172 are shared sites for RNF135-mediated and TRIM4-mediated ubiquitination (PubMed:19017631, PubMed:19484123, PubMed:24755855). Also undergoes 'Lys-48' ubiquitination at Lys-181 by RNF125 that leads to proteasomal degradation (PubMed:17460044, PubMed:26471729). 'Lys-48' ubiquitination follows viral infection and is enhanced by 'Lys-63'-linked ubiquitination of the CARD domains that promotes interaction with VCP/p97 and subsequent recruitment of RNF125 (PubMed:17460044, PubMed:26471729). Within a negative feedback loop involving SIGLEC10 and PTPN11, 'Lys-48' ubiquitination at Lys-812 by CBL also elicits the proteasomal degradation of RIGI (By similarity). Deubiquitinated by CYLD, a protease that selectively cleaves 'Lys-63'-linked ubiquitin chains (PubMed:18636086). Also probably deubiquitinated by USP17L2/USP17 that cleaves 'Lys-48'- and 'Lys-63'-linked ubiquitin chains and positively regulates the receptor (PubMed:20368735). Ubiquitinated by TRIM40 via 'Lys-48'-linked ubiquitination; leading to proteasomal degradation (PubMed:29117565). Deubiquitinated by USP27X that cleaves 'Lys-63'-linked ubiquitin chains and inhibits the innate immune receptor activity (PubMed:32027733). Deubiquitinated by USP3 that also cleaves 'Lys-63'-linked ubiquitin chains and inhibits the innate immune receptor activity (PubMed:24366338). {ECO:0000250|UniProtKB:Q6Q899, ECO:0000269|PubMed:17392790, ECO:0000269|PubMed:17460044, ECO:0000269|PubMed:18636086, ECO:0000269|PubMed:19017631, ECO:0000269|PubMed:19484123, ECO:0000269|PubMed:20368735, ECO:0000269|PubMed:23950712, ECO:0000269|PubMed:24366338, ECO:0000269|PubMed:24755855, ECO:0000269|PubMed:26471729, ECO:0000269|PubMed:29117565, ECO:0000269|PubMed:30193849, ECO:0000269|PubMed:31006531, ECO:0000269|PubMed:32027733}.; PTM: ISGylated. Conjugated to ubiquitin-like protein ISG15 upon IFN-beta stimulation. ISGylation negatively regulates its function in antiviral signaling response. {ECO:0000269|PubMed:16009940, ECO:0000269|PubMed:18057259, ECO:0000269|PubMed:20368735}.; PTM: Sumoylated, probably by MUL1; inhibiting its polyubiquitination. {ECO:0000269|PubMed:20368735, ECO:0000269|PubMed:23399697}.; PTM: (Microbial infection) Deamidated on Asn-495 and Asn-549 by herpes simplex virus 1 protein UL37. These modifications eliminate RIGI detection of viral RNA and restriction of viral replication. {ECO:0000269|PubMed:27866900}.; PTM: Degraded via selective autophagy following interaction with IRGM (PubMed:32715615). IRGM promotes RIGI recruitment to autophagosome membranes, promoting its SQSTM1/p62-dependent autophagic degradation (PubMed:32715615). {ECO:0000269|PubMed:32715615}.; PTM: (Microbial infection) Cleaved by the protease 3C of coxsackievirus B3, poliovirus and enterovirus 71 allowing the virus to disrupt the host type I interferon production. {ECO:0000269|PubMed:24390337}.; PTM: (Microbial infection) Phosphorylated at Ser-8 by herpes simplex virus 1 protein US3 leading to inhibition of critical RIGI activation steps. {ECO:0000269|PubMed:34935440}.
|
SUBCELLULAR LOCATION: Cytoplasm. Cell projection, ruffle membrane. Cytoplasm, cytoskeleton. Cell junction, tight junction. Note=Colocalized with TRIM25 at cytoplasmic perinuclear bodies. Associated with the actin cytoskeleton at membrane ruffles.
|
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:19211564}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000305|PubMed:19211564};
| null | null | null | null |
FUNCTION: Innate immune receptor that senses cytoplasmic viral nucleic acids and activates a downstream signaling cascade leading to the production of type I interferons and pro-inflammatory cytokines (PubMed:15208624, PubMed:15708988, PubMed:16125763, PubMed:16127453, PubMed:16153868, PubMed:17190814, PubMed:18636086, PubMed:19122199, PubMed:19211564, PubMed:24366338, PubMed:28469175, PubMed:29117565, PubMed:31006531, PubMed:34935440, PubMed:35263596, PubMed:36793726). Forms a ribonucleoprotein complex with viral RNAs on which it homooligomerizes to form filaments (PubMed:15208624, PubMed:15708988). The homooligomerization allows the recruitment of RNF135 an E3 ubiquitin-protein ligase that activates and amplifies the RIG-I-mediated antiviral signaling in an RNA length-dependent manner through ubiquitination-dependent and -independent mechanisms (PubMed:28469175, PubMed:31006531). Upon activation, associates with mitochondria antiviral signaling protein (MAVS/IPS1) that activates the IKK-related kinases TBK1 and IKBKE which in turn phosphorylate the interferon regulatory factors IRF3 and IRF7, activating transcription of antiviral immunological genes including the IFN-alpha and IFN-beta interferons (PubMed:28469175, PubMed:31006531). Ligands include 5'-triphosphorylated ssRNAs and dsRNAs but also short dsRNAs (<1 kb in length) (PubMed:15208624, PubMed:15708988, PubMed:19576794, PubMed:19609254, PubMed:21742966). In addition to the 5'-triphosphate moiety, blunt-end base pairing at the 5'-end of the RNA is very essential (PubMed:15208624, PubMed:15708988, PubMed:19576794, PubMed:19609254, PubMed:21742966). Overhangs at the non-triphosphorylated end of the dsRNA RNA have no major impact on its activity (PubMed:15208624, PubMed:15708988, PubMed:19576794, PubMed:19609254, PubMed:21742966). A 3'overhang at the 5'triphosphate end decreases and any 5'overhang at the 5' triphosphate end abolishes its activity (PubMed:15208624, PubMed:15708988, PubMed:19576794, PubMed:19609254, PubMed:21742966). Detects both positive and negative strand RNA viruses including members of the families Paramyxoviridae: Human respiratory syncytial virus and measles virus (MeV), Rhabdoviridae: vesicular stomatitis virus (VSV), Orthomyxoviridae: influenza A and B virus, Flaviviridae: Japanese encephalitis virus (JEV), hepatitis C virus (HCV), dengue virus (DENV) and west Nile virus (WNV) (PubMed:21616437, PubMed:21884169). It also detects rotaviruses and reoviruses (PubMed:21616437, PubMed:21884169). Detects and binds to SARS-CoV-2 RNAs which is inhibited by m6A RNA modifications (Ref.70). Also involved in antiviral signaling in response to viruses containing a dsDNA genome such as Epstein-Barr virus (EBV) (PubMed:19631370). Detects dsRNA produced from non-self dsDNA by RNA polymerase III, such as Epstein-Barr virus-encoded RNAs (EBERs). May play important roles in granulocyte production and differentiation, bacterial phagocytosis and in the regulation of cell migration. {ECO:0000269|PubMed:15208624, ECO:0000269|PubMed:15708988, ECO:0000269|PubMed:16125763, ECO:0000269|PubMed:16127453, ECO:0000269|PubMed:16153868, ECO:0000269|PubMed:17190814, ECO:0000269|PubMed:18636086, ECO:0000269|PubMed:19122199, ECO:0000269|PubMed:19211564, ECO:0000269|PubMed:19576794, ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370, ECO:0000269|PubMed:21742966, ECO:0000269|PubMed:24366338, ECO:0000269|PubMed:28469175, ECO:0000269|PubMed:29117565, ECO:0000269|PubMed:31006531, ECO:0000269|PubMed:34935440, ECO:0000269|PubMed:35263596, ECO:0000269|PubMed:36793726, ECO:0000269|Ref.70, ECO:0000303|PubMed:21616437, ECO:0000303|PubMed:21884169}.
|
Homo sapiens (Human)
|
O95789
|
ZMYM6_HUMAN
|
MKEPLDGECGKAVVPQQELLDKIKEEPDNAQEYGCVQQPKTQESKLKIGGVSSVNERPIAQQLNPGFQLSFASSGPSVLLPSVPAVAIKVFCSGCKKMLYKGQTAYHKTGSTQLFCSTRCITRHSSPACLPPPPKKTCTNCSKDILNPKDVITTRFENSYPSKDFCSQSCLSSYELKKKPVVTIYTKSISTKCSMCQKNADTRFEVKYQNVVHGLCSDACFSKFHSTNNLTMNCCENCGSYCYSSSGPCQSQKVFSSTSVTAYKQNSAQIPPYALGKSLRPSAEMIETTNDSGKTELFCSINCLSAYRVKTVTSSGVQVSCHSCKTSAIPQYHLAMSNGTIYSFCSSSCVVAFQNVFSKPKGTNSSAVPLSQGQVVVSPPSSRSAVSIGGGNTSAVSPSSIRGSAAASLQPLAEQSQQVALTHTVVKLKCQHCNHLFATKPELLFYKGKMFLFCGKNCSDEYKKKNKVVAMCDYCKLQKIIKETVRFSGVDKPFCSEVCKFLSARDFGERWGNYCKMCSYCSQTSPNLVENRLEGKLEEFCCEDCMSKFTVLFYQMAKCDGCKRQGKLSESIKWRGNIKHFCNLFCVLEFCHQQIMNDCLPQNKVNISKAKTAVTELPSARTDTTPVITSVMSLAKIPATLSTGNTNSVLKGAVTKEAAKIIQDESTQEDAMKFPSSQSSQPSRLLKNKGISCKPVTQTKATSCKPHTQHKECQTDLPMPNEKNDAELDSPPSKKKRLGFFQTYDTEYLKVGFIICPGSKESSPRPQCVICGEILSSENMKPANLSHHLKTKHSELENKPVDFFEQKSLEMECQNSSLKKCLLVEKSLVKASYLIAFQTAASKKPFSIAEELIKPYLVEMCSEVLGSSAGDKMKTIPLSNVTIQHRIDELSADIEDQLIQKVRESKWFALQIDESSEISNITLLLCYIRFIDYDCRDVKEELLFCIEMPTQITGFEIFELINKYIDSKSLNWKHCVGLCTDGAASMTGRYSGLKAKIQEVAMNTAAFTHCFIHRERLVAEKLSPCLHKILLQSAQILSFIKSNALNSRMLTILCEEMGSEHVSLPLHAEVRWISRGRMLKRLFELRHEIEIFLSQKHSDLAKYFHDEEWVGKLAYLSDIFSLINELNLSLQGTLTTFFNLCNKIDVFKRKLKMWLKRTQENDYDMFPSFSEFSNSSGLNMTDITRIIFEHLEGLSQVFSDCFPPEQDLRSGNLWIIHPFMNHQNNNLTDFEEEKLTELSSDLGLQALFKSVSVTQFWINAKTSYPELHERAMKFLLPFSTVYLCDAAFSALTESKQKNLLGSGPALRLAVTSLIPRIEKLVKEKE
| null | null |
cytoskeleton organization [GO:0007010]; regulation of cell morphogenesis [GO:0022604]
|
nucleus [GO:0005634]
|
DNA binding [GO:0003677]; zinc ion binding [GO:0008270]
|
PF06467;
| null | null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Plays a role in the regulation of cell morphology and cytoskeletal organization. {ECO:0000269|PubMed:21834987}.
|
Homo sapiens (Human)
|
O95793
|
STAU1_HUMAN
|
MSQVQVQVQNPSAALSGSQILNKNQSLLSQPLMSIPSTTSSLPSENAGRPIQNSALPSASITSTSAAAESITPTVELNALCMKLGKKPMYKPVDPYSRMQSTYNYNMRGGAYPPRYFYPFPVPPLLYQVELSVGGQQFNGKGKTRQAAKHDAAAKALRILQNEPLPERLEVNGRESEEENLNKSEISQVFEIALKRNLPVNFEVARESGPPHMKNFVTKVSVGEFVGEGEGKSKKISKKNAAIAVLEELKKLPPLPAVERVKPRIKKKTKPIVKPQTSPEYGQGINPISRLAQIQQAKKEKEPEYTLLTERGLPRRREFVMQVKVGNHTAEGTGTNKKVAKRNAAENMLEILGFKVPQAQPTKPALKSEEKTPIKKPGDGRKVTFFEPGSGDENGTSNKEDEFRMPYLSHQQLPAGILPMVPEVAQAVGVSQGHHTKDFTRAAPNPAKATVTAMIARELLYGGTSPTAETILKNNISSGHVPHGPLTRPSEQLDYLSRVQGFQVEYKDFPKNNKNEFVSLINCSSQPPLISHGIGKDVESCHDMAALNILKLLSELDQQSTEMPRTGNGPMSVCGRC
| null | null |
anterograde dendritic transport of messenger ribonucleoprotein complex [GO:0098964]; cellular response to oxidative stress [GO:0034599]; germ cell development [GO:0007281]; intracellular mRNA localization [GO:0008298]; lncRNA-mediated post-transcriptional gene silencing [GO:0000512]; modification of postsynaptic structure [GO:0099010]; positive regulation by virus of viral protein levels in host cell [GO:0046726]; positive regulation of long-term synaptic potentiation [GO:1900273]; positive regulation of viral genome replication [GO:0045070]; protein localization to synapse [GO:0035418]
|
cell body [GO:0044297]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendrite cytoplasm [GO:0032839]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; messenger ribonucleoprotein complex [GO:1990124]; microtubule associated complex [GO:0005875]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; rough endoplasmic reticulum [GO:0005791]
|
double-stranded RNA binding [GO:0003725]; mRNA binding [GO:0003729]; protein phosphatase 1 binding [GO:0008157]; RNA binding [GO:0003723]
|
PF00035;PF16482;
|
3.30.160.20;6.10.250.1360;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19029303}. Rough endoplasmic reticulum {ECO:0000269|PubMed:19029303}. Note=Localizes exclusively with the rough reticulum endoplasmic (RER).
| null | null | null | null | null |
FUNCTION: Binds double-stranded RNA (regardless of the sequence) and tubulin. May play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site.; FUNCTION: (Microbial infection) Plays a role in virus particles production of many viruses including of HIV-1, HERV-K, ebola virus and influenza virus. Acts by interacting with various viral proteins involved in particle budding process. {ECO:0000269|PubMed:10325410, ECO:0000269|PubMed:18498651, ECO:0000269|PubMed:23926355, ECO:0000269|PubMed:30301857}.
|
Homo sapiens (Human)
|
O95801
|
TTC4_HUMAN
|
MEQPGQDPTSDDVMDSFLEKFQSQPYRGGFHEDQWEKEFEKVPLFMSRAPSEIDPRENPDLACLQSIIFDEERSPEEQAKTYKDEGNDYFKEKDYKKAVISYTEGLKKKCADPDLNAVLYTNRAAAQYYLGNFRSALNDVTAARKLKPCHLKAIIRGALCHLELKHFAEAVNWCDEGLQIDAKEKKLLEMRAKADKLKRIEQRDVRKANLKEKKERNQNEALLQAIKARNIRLSEAACEDEDSASEGLGELFLDGLSTENPHGARLSLDGQGRLSWPVLFLYPEYAQSDFISAFHEDSRFIDHLMVMFGETPSWDLEQKYCPDNLEVYFEDEDRAELYRVPAKSTLLQVLQHQRYFVKALTPAFLVCVGSSPFCKNFLRGRKVYQIR
| null | null |
defense response to virus [GO:0051607]; innate immune response [GO:0045087]; protein folding [GO:0006457]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]
|
PF18972;
|
1.25.40.10;
|
TTC4 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18320024, ECO:0000269|PubMed:29251827}. Nucleus, nucleoplasm {ECO:0000269|PubMed:18320024}. Cytoplasm {ECO:0000269|PubMed:29251827}. Note=Predominantly nuclear in the G1 and S phases of cell cycle and is evenly distributed between the nucleus and cytoplasm in the G2 phase (By similarity). MSL1 can promote its nuclear localization (By similarity). {ECO:0000250|UniProtKB:Q8R3H9}.
| null | null | null | null | null |
FUNCTION: May act as a co-chaperone for HSP90AB1 (PubMed:18320024). Promotes Sendai virus (SeV)-induced host cell innate immune responses (PubMed:29251827). {ECO:0000269|PubMed:18320024, ECO:0000269|PubMed:29251827}.
|
Homo sapiens (Human)
|
O95803
|
NDST3_HUMAN
|
MSFIMKLHRHFQRTVILLATFCMVSIIISAYYLYSGYKQENELSETASEVDCGDLQHLPYQLMEVKAMKLFDASRTDPTVLVFVESQYSSLGQDIIMILESSRFQYHIEIAPGKGDLPVLIDKMKGKYILIIYENILKYINMDSWNRSLLDKYCVEYGVGVIGFHKTSEKSVQSFQLKGFPFSIYGNLAVKDCCINPHSPLIRVTKSSKLEKGSLPGTDWTVFQINHSAYQPVIFAKVKTPENLSPSISKGAFYATIIHDLGLHDGIQRVLFGNNLNFWLHKLIFIDAISFLSGKRLTLSLDRYILVDIDDIFVGKEGTRMNTNDVKALLDTQNLLRAQITNFTFNLGFSGKFYHTGTEEEDEGDDCLLGSVDEFWWFPHMWSHMQPHLFHNESSLVEQMILNKKFALEHGIPTDMGYAVAPHHSGVYPVHVQLYEAWKKVWNIKITSTEEYPHLKPARYRRGFIHKNIMVLPRQTCGLFTHTIFYKEYPGGPKELDKSIQGGELFFTVVLNPISIFMTHLSNYGNDRLGLYTFVNLANFVKSWTNLRLQTLPPVQLAHKYFELFPDQKDPLWQNPCDDKRHRDIWSKEKTCDRLPKFLVIGPQKTGTTALYLFLVMHPSILSNSPSPKTFEEVQFFNRNNYHRGIDWYMDFFPVPSNVTTDFLFEKSANYFHSEEAPKRAASLVPKAKIITILIDPSDRAYSWYQHQRSHEDPAALKFSFYEVISAGPRAPSELRALQKRCLVPGWYASHIERWLVYFPPFQLLIIDGQQLRTDPATVMDEVQKFLGVLPHYNYSEALTFDSHKGFWCQLLEEGKTKCLGKSKGRKYPPMDSDSRTFLSSYYRDHNVELSKLLHKLGQPLPSWLRQELQKVR
|
2.8.2.8; 3.-.-.-
| null |
heparan sulfate proteoglycan biosynthetic process [GO:0015012]; heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process [GO:0015014]; heparin biosynthetic process [GO:0030210]
|
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
|
[heparan sulfate]-glucosamine N-sulfotransferase activity [GO:0015016]; deacetylase activity [GO:0019213]; heparan sulfate N-deacetylase activity [GO:0102140]
|
PF12062;PF00685;
|
3.40.50.300;
|
Sulfotransferase 1 family, NDST subfamily
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan sulfate](n) = adenosine 3',5'-bisphosphate + 2 H(+) + N-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n); Xref=Rhea:RHEA:21980, Rhea:RHEA-COMP:9830, Rhea:RHEA-COMP:14602, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:58388, ChEBI:CHEBI:140572; EC=2.8.2.8; Evidence={ECO:0000269|PubMed:9915799};
| null |
PATHWAY: Glycan metabolism; heparan sulfate biosynthesis. {ECO:0000269|PubMed:9915799}.; PATHWAY: Glycan metabolism; heparin biosynthesis. {ECO:0000269|PubMed:9915799}.
| null | null |
FUNCTION: Essential bifunctional enzyme that catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Has high deacetylase activity but low sulfotransferase activity. {ECO:0000269|PubMed:9915799}.
|
Homo sapiens (Human)
|
O95807
|
TM50A_HUMAN
|
MSGFLEGLRCSECIDWGEKRNTIASIAAGVLFFTGWWIIIDAAVIYPTMKDFNHSYHACGVIATIAFLMINAVSNGQVRGDSYSEGCLGQTGARIWLFVGFMLAFGSLIASMWILFGGYVAKEKDIVYPGIAVFFQNAFIFFGGLVFKFGRTEDLWQ
| null | null |
late endosome to vacuole transport via multivesicular body sorting pathway [GO:0032511]; protein targeting to vacuole [GO:0006623]
|
endoplasmic reticulum [GO:0005783]; glial cell projection [GO:0097386]; membrane [GO:0016020]; neuronal cell body [GO:0043025]
| null |
PF05255;
| null |
UPF0220 family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
| null | null | null | null | null | null |
Homo sapiens (Human)
|
O95810
|
CAVN2_HUMAN
|
MGEDAAQAEKFQHPGSDMRQEKPSSPSPMPSSTPSPSLNLGNTEEAIRDNSQVNAVTVLTLLDKLVNMLDAVQENQHKMEQRQISLEGSVKGIQNDLTKLSKYQASTSNTVSKLLEKSRKVSAHTRAVKERMDRQCAQVKRLENNHAQLLRRNHFKVLIFQEENEIPASVFVKQPVSGAVEGKEELPDENKSLEETLHTVDLSSDDDLPHDEEALEDSAEEKVEESRAEKIKRSSLKKVDSLKKAFSRQNIEKKMNKLGTKIVSVERREKIKKSLTSNHQKISSGKSSPFKVSPLTFGRKKVREGESHAENETKSEDLPSSEQMPNDQEEESFAEGHSEASLASALVEGEIAEEAAEKATSRGSNSGMDSNIDLTIVEDEEEESVALEQAQKVRYEGSYALTSEEAERSDGDPVQPAVLQVHQTS
| null | null |
plasma membrane tubulation [GO:0097320]
|
caveola [GO:0005901]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane raft [GO:0045121]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
|
phosphatidylserine binding [GO:0001786]; phospholipid binding [GO:0005543]; protein kinase C binding [GO:0005080]
|
PF15237;
| null |
CAVIN family
|
PTM: Phosphorylated on Ser residues. {ECO:0000269|PubMed:2390065}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10191091, ECO:0000269|PubMed:2390065}. Membrane, caveola {ECO:0000269|PubMed:19262564, ECO:0000269|PubMed:19525939}. Note=Localizes in the caveolae in a caveolin-dependent manner. {ECO:0000269|PubMed:19262564}.
| null | null | null | null | null |
FUNCTION: Plays an important role in caveolar biogenesis and morphology. Regulates caveolae morphology by inducing membrane curvature within caveolae (PubMed:19525939). Plays a role in caveola formation in a tissue-specific manner. Required for the formation of caveolae in the lung and fat endothelia but not in the heart endothelia. Negatively regulates the size or stability of CAVIN complexes in the lung endothelial cells. May play a role in targeting PRKCA to caveolae (By similarity). {ECO:0000250|UniProtKB:Q66H98, ECO:0000269|PubMed:19525939}.
|
Homo sapiens (Human)
|
O95813
|
CER1_HUMAN
|
MHLLLFQLLVLLPLGKTTRHQDGRQNQSSLSPVLLPRNQRELPTGNHEEAEEKPDLFVAVPHLVATSPAGEGQRQREKMLSRFGRFWKKPEREMHPSRDSDSEPFPPGTQSLIQPIDGMKMEKSPLREEAKKFWHHFMFRKTPASQGVILPIKSHEVHWETCRTVPFSQTITHEGCEKVVVQNNLCFGKCGSVHFPGAAQHSHTSCSHCLPAKFTTMHLPLNCTELSSVIKVVMLVEECQCKVKTEHEDGHILHAGSQDSFIPGVSA
| null | null |
anterior/posterior axis specification [GO:0009948]; anterior/posterior pattern specification [GO:0009952]; bone mineralization [GO:0030282]; cell migration involved in gastrulation [GO:0042074]; cellular response to cadmium ion [GO:0071276]; determination of dorsal identity [GO:0048263]; determination of heart left/right asymmetry [GO:0061371]; gastrulation [GO:0007369]; growth plate cartilage chondrocyte proliferation [GO:0003419]; negative regulation of activin receptor signaling pathway [GO:0032926]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of mesoderm development [GO:2000381]; nervous system development [GO:0007399]; sequestering of BMP in extracellular matrix [GO:0035582]; signal transduction involved in regulation of gene expression [GO:0023019]; ureteric bud development [GO:0001657]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
BMP binding [GO:0036122]; cytokine activity [GO:0005125]; morphogen activity [GO:0016015]; protein homodimerization activity [GO:0042803]
|
PF03045;
|
2.10.90.10;
|
DAN family
|
PTM: N-glycosylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Cytokine that may play a role in anterior neural induction and somite formation during embryogenesis in part through a BMP-inhibitory mechanism. Can regulate Nodal signaling during gastrulation as well as the formation and patterning of the primitive streak (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O95816
|
BAG2_HUMAN
|
MAQAKINAKANEGRFCRSSSMADRSSRLLESLDQLELRVEALREAATAVEQEKEILLEMIHSIQNSQDMRQISDGEREELNLTANRLMGRTLTVEVSVETIRNPQQQESLKHATRIIDEVVNKFLDDLGNAKSHLMSLYSACSSEVPHGPVDQKFQSIVIGCALEDQKKIKRRLETLLRNIENSDKAIKLLEHSKGAGSKTLQQNAESRFN
| null | null |
negative regulation of protein binding [GO:0032091]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of ubiquitin protein ligase activity [GO:1904667]; positive regulation of proteasomal protein catabolic process [GO:1901800]; positive regulation of protein processing [GO:0010954]; protein folding [GO:0006457]; protein metabolic process [GO:0019538]; protein stabilization [GO:0050821]
|
axon [GO:0030424]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic microtubule [GO:1901588]; protein folding chaperone complex [GO:0101031]
|
adenyl-nucleotide exchange factor activity [GO:0000774]; heat shock protein binding [GO:0031072]; identical protein binding [GO:0042802]; protein-folding chaperone binding [GO:0051087]; tau protein binding [GO:0048156]; transmembrane transporter binding [GO:0044325]; ubiquitin protein ligase binding [GO:0031625]
| null |
1.20.58.890;
| null | null | null | null | null | null | null | null |
FUNCTION: Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release (PubMed:24318877, PubMed:9873016). {ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:9873016}.
|
Homo sapiens (Human)
|
O95817
|
BAG3_HUMAN
|
MSAATHSPMMQVASGNGDRDPLPPGWEIKIDPQTGWPFFVDHNSRTTTWNDPRVPSEGPKETPSSANGPSREGSRLPPAREGHPVYPQLRPGYIPIPVLHEGAENRQVHPFHVYPQPGMQRFRTEAAAAAPQRSQSPLRGMPETTQPDKQCGQVAAAAAAQPPASHGPERSQSPAASDCSSSSSSASLPSSGRSSLGSHQLPRGYISIPVIHEQNVTRPAAQPSFHQAQKTHYPAQQGEYQTHQPVYHKIQGDDWEPRPLRAASPFRSSVQGASSREGSPARSSTPLHSPSPIRVHTVVDRPQQPMTHRETAPVSQPENKPESKPGPVGPELPPGHIPIQVIRKEVDSKPVSQKPPPPSEKVEVKVPPAPVPCPPPSPGPSAVPSSPKSVATEERAAPSTAPAEATPPKPGEAEAPPKHPGVLKVEAILEKVQGLEQAVDNFEGKKTDKKYLMIEEYLTKELLALDSVDPEGRADVRQARRDGVRKVQTILEKLEQKAIDVPGQVQVYELQPSNLEADQPLQAIMEMGAVAADKGKKNAGNAEDPHTETQQPEATAAATSNPSSMTDTPGNPAAP
| null | null |
aggresome assembly [GO:0070842]; autophagosome assembly [GO:0000045]; cellular response to heat [GO:0034605]; cellular response to mechanical stimulus [GO:0071260]; cellular response to unfolded protein [GO:0034620]; chaperone-mediated autophagy [GO:0061684]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; muscle cell cellular homeostasis [GO:0046716]; negative regulation of apoptotic process [GO:0043066]; negative regulation of striated muscle cell apoptotic process [GO:0010664]; positive regulation of aggrephagy [GO:1905337]; positive regulation of protein export from nucleus [GO:0046827]; positive regulation of protein import into nucleus [GO:0042307]; protein folding [GO:0006457]; protein stabilization [GO:0050821]; protein transport along microtubule [GO:0098840]; striated muscle cell apoptotic process [GO:0010658]
|
aggresome [GO:0016235]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein folding chaperone complex [GO:0101031]; stress fiber [GO:0001725]; Z disc [GO:0030018]
|
adenyl-nucleotide exchange factor activity [GO:0000774]; cadherin binding [GO:0045296]; dynein intermediate chain binding [GO:0045505]; protein carrier chaperone [GO:0140597]; protein-containing complex binding [GO:0044877]; protein-folding chaperone binding [GO:0051087]
|
PF02179;PF00397;
|
2.20.70.10;1.20.58.120;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26159920}. Cytoplasm {ECO:0000269|PubMed:26159920}. Note=Colocalizes with HSF1 to the nucleus upon heat stress (PubMed:26159920). {ECO:0000269|PubMed:26159920}.
| null | null | null | null | null |
FUNCTION: Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSPA8/HSC70 (PubMed:27474739, PubMed:9873016). Has anti-apoptotic activity (PubMed:10597216). Plays a role in the HSF1 nucleocytoplasmic transport (PubMed:26159920). {ECO:0000269|PubMed:10597216, ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:26159920, ECO:0000269|PubMed:27474739, ECO:0000269|PubMed:9873016}.
|
Homo sapiens (Human)
|
O95819
|
M4K4_HUMAN
|
MANDSPAKSLVDIDLSSLRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKYSHHRNIATYYGAFIKKSPPGHDDQLWLVMEFCGAGSITDLVKNTKGNTLKEDWIAYISREILRGLAHLHIHHVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDLWSCGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSKKWSKKFFSFIEGCLVKNYMQRPSTEQLLKHPFIRDQPNERQVRIQLKDHIDRTRKKRGEKDETEYEYSGSEEEEEEVPEQEGEPSSIVNVPGESTLRRDFLRLQQENKERSEALRRQQLLQEQQLREQEEYKRQLLAERQKRIEQQKEQRRRLEEQQRREREARRQQEREQRRREQEEKRRLEELERRRKEEEERRRAEEEKRRVEREQEYIRRQLEEEQRHLEVLQQQLLQEQAMLLECRWREMEEHRQAERLQRQLQQEQAYLLSLQHDHRRPHPQHSQQPPPPQQERSKPSFHAPEPKAHYEPADRAREVEDRFRKTNHSSPEAQSKQTGRVLEPPVPSRSESFSNGNSESVHPALQRPAEPQVPVRTTSRSPVLSRRDSPLQGSGQQNSQAGQRNSTSIEPRLLWERVEKLVPRPGSGSSSGSSNSGSQPGSHPGSQSGSGERFRVRSSSKSEGSPSQRLENAVKKPEDKKEVFRPLKPADLTALAKELRAVEDVRPPHKVTDYSSSSEESGTTDEEDDDVEQEGADESTSGPEDTRAASSLNLSNGETESVKTMIVHDDVESEPAMTPSKEGTLIVRQTQSASSTLQKHKSSSSFTPFIDPRLLQISPSSGTTVTSVVGFSCDGMRPEAIRQDPTRKGSVVNVNPTNTRPQSDTPEIRKYKKRFNSEILCAALWGVNLLVGTESGLMLLDRSGQGKVYPLINRRRFQQMDVLEGLNVLVTISGKKDKLRVYYLSWLRNKILHNDPEVEKKQGWTTVGDLEGCVHYKVVKYERIKFLVIALKSSVEVYAWAPKPYHKFMAFKSFGELVHKPLLVDLTVEEGQRLKVIYGSCAGFHAVDVDSGSVYDIYLPTHIQCSIKPHAIIILPNTDGMELLVCYEDEGVYVNTYGRITKDVVLQWGEMPTSVAYIRSNQTMGWGEKAIEIRSVETGHLDGVFMHKRAQRLKFLCERNDKVFFASVRSGGSSQVYFMTLGRTSLLSW
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9890973};
|
intracellular signal transduction [GO:0035556]; MAPK cascade [GO:0000165]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell-matrix adhesion [GO:0001953]; neuron projection morphogenesis [GO:0048812]; positive regulation of ARF protein signal transduction [GO:0032014]; positive regulation of cell migration [GO:0030335]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of focal adhesion disassembly [GO:0120183]; positive regulation of GTPase activity [GO:0043547]; positive regulation of keratinocyte migration [GO:0051549]; protein phosphorylation [GO:0006468]; regulation of JNK cascade [GO:0046328]; regulation of MAPK cascade [GO:0043408]
|
cytoplasm [GO:0005737]; focal adhesion [GO:0005925]
|
ATP binding [GO:0005524]; creatine kinase activity [GO:0004111]; microtubule binding [GO:0008017]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00780;PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14966141}.
|
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:9890973}; 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:9890973};
| null | null | null | null |
FUNCTION: Serine/threonine kinase that plays a role in the response to environmental stress and cytokines such as TNF-alpha. Appears to act upstream of the JUN N-terminal pathway (PubMed:9890973). Activator of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. MAP4Ks act in parallel to and are partially redundant with STK3/MST2 and STK4/MST2 in the phosphorylation and activation of LATS1/2, and establish MAP4Ks as components of the expanded Hippo pathway (PubMed:26437443). Phosphorylates SMAD1 on Thr-322 (PubMed:21690388). {ECO:0000269|PubMed:21690388, ECO:0000269|PubMed:26437443, ECO:0000269|PubMed:9890973}.
|
Homo sapiens (Human)
|
O95822
|
DCMC_HUMAN
|
MRGFGPGLTARRLLPLRLPPRPPGPRLASGQAAGALERAMDELLRRAVPPTPAYELREKTPAPAEGQCADFVSFYGGLAETAQRAELLGRLARGFGVDHGQVAEQSAGVLHLRQQQREAAVLLQAEDRLRYALVPRYRGLFHHISKLDGGVRFLVQLRADLLEAQALKLVEGPDVREMNGVLKGMLSEWFSSGFLNLERVTWHSPCEVLQKISEAEAVHPVKNWMDMKRRVGPYRRCYFFSHCSTPGEPLVVLHVALTGDISSNIQAIVKEHPPSETEEKNKITAAIFYSISLTQQGLQGVELGTFLIKRVVKELQREFPHLGVFSSLSPIPGFTKWLLGLLNSQTKEHGRNELFTDSECKEISEITGGPINETLKLLLSSSEWVQSEKLVRALQTPLMRLCAWYLYGEKHRGYALNPVANFHLQNGAVLWRINWMADVSLRGITGSCGLMANYRYFLEETGPNSTSYLGSKIIKASEQVLSLVAQFQKNSKL
|
4.1.1.9
| null |
acetyl-CoA biosynthetic process [GO:0006085]; acyl-CoA metabolic process [GO:0006637]; fatty acid biosynthetic process [GO:0006633]; fatty acid oxidation [GO:0019395]; malonyl-CoA catabolic process [GO:2001294]; positive regulation of fatty acid oxidation [GO:0046321]; regulation of fatty acid beta-oxidation [GO:0031998]; regulation of glucose metabolic process [GO:0010906]; response to ischemia [GO:0002931]; response to nutrient [GO:0007584]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]
|
identical protein binding [GO:0042802]; malonyl-CoA decarboxylase activity [GO:0050080]
|
PF05292;PF17408;
|
3.40.630.150;1.20.140.90;
| null |
PTM: Acetylation at Lys-472 activates malonyl-CoA decarboxylase activity. Deacetylation at Lys-472 by SIRT4 represses activity, leading to promote lipogenesis (By similarity). {ECO:0000250|UniProtKB:Q99J39}.; PTM: Interchain disulfide bonds may form in peroxisomes (Potential). Interchain disulfide bonds are not expected to form in the reducing environment of the cytoplasm and mitochondria. {ECO:0000305}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10417274}. Mitochondrion matrix {ECO:0000269|PubMed:10417274}. Peroxisome {ECO:0000269|PubMed:10417274}. Peroxisome matrix {ECO:0000250|UniProtKB:Q920F5}. Note=Enzymatically active in all three subcellular compartments. {ECO:0000250|UniProtKB:Q920F5}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + malonyl-CoA = acetyl-CoA + CO2; Xref=Rhea:RHEA:18781, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384; EC=4.1.1.9; Evidence={ECO:0000269|PubMed:10417274, ECO:0000269|PubMed:10455107, ECO:0000269|PubMed:15003260, ECO:0000269|PubMed:23482565, ECO:0000269|PubMed:9869665}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18782; Evidence={ECO:0000305|PubMed:23482565};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.36 mM for malonyl-CoA (Malonyl-CoA decarboxylase mitochondrial form) {ECO:0000269|PubMed:15003260}; KM=0.83 mM for malonyl-CoA (Malonyl-CoA decarboxylase mitochondrial form) {ECO:0000269|PubMed:23482565}; KM=0.22 mM for malonyl-CoA (Malonyl-CoA decarboxylase cytoplasmic+peroxisomal form) {ECO:0000269|PubMed:10455107}; KM=0.33 mM for malonyl-CoA (Malonyl-CoA decarboxylase cytoplasmic+peroxisomal form) {ECO:0000269|PubMed:15003260}; Note=kcat is 19 sec(-1) with malonyl-CoA for malonyl-CoA decarboxylase mitochondrial form (PubMed:15003260). kcat is 28 sec(-1) with malonyl-CoA for Malonyl-CoA decarboxylase cytoplasmic+peroxisomal form (PubMed:15003260). The catalytic efficiency for malonyl-CoA is at least 1.09-fold higher with the malonyl-CoA decarboxylase cytoplasmic+peroxisomal form (PubMed:15003260). {ECO:0000269|PubMed:15003260};
|
PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from malonyl-CoA: step 1/1.
| null | null |
FUNCTION: Catalyzes the conversion of malonyl-CoA to acetyl-CoA. In the fatty acid biosynthesis MCD selectively removes malonyl-CoA and thus assures that methyl-malonyl-CoA is the only chain elongating substrate for fatty acid synthase and that fatty acids with multiple methyl side chains are produced. In peroxisomes it may be involved in degrading intraperoxisomal malonyl-CoA, which is generated by the peroxisomal beta-oxidation of odd chain-length dicarboxylic fatty acids. Plays a role in the metabolic balance between glucose and lipid oxidation in muscle independent of alterations in insulin signaling. May play a role in controlling the extent of ischemic injury by promoting glucose oxidation. {ECO:0000269|PubMed:10455107, ECO:0000269|PubMed:15003260, ECO:0000269|PubMed:18314420, ECO:0000269|PubMed:23482565}.
|
Homo sapiens (Human)
|
O95825
|
QORL1_HUMAN
|
MKGLYFQQSSTDEEITFVFQEKEDLPVTEDNFVKLQVKACALSQINTKLLAEMKMKKDLFPVGREIAGIVLDVGSKVSFFQPDDEVVGILPLDSEDPGLCEVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHYLSHLSPGKSVLIMDGASAFGTIAIQLAHHRGAKVISTACSLEDKQCLERFRPPIARVIDVSNGKVHVAESCLEETGGLGVDIVLDAGVRLYSKDDEPAVKLQLLPHKHDIITLLGVGGHWVTTEENLQLDPPDSHCLFLKGATLAFLNDEVWNLSNVQQGKYLCILKDVMEKLSTGVFRPQLDEPIPLYEAKVSMEAVQKNQGRKKQVVQF
|
1.-.-.-
| null |
quinone metabolic process [GO:1901661]
|
cytosol [GO:0005829]; early endosome [GO:0005769]
|
NADP binding [GO:0050661]; NADPH:quinone reductase activity [GO:0003960]
| null |
3.90.180.10;
|
Zinc-containing alcohol dehydrogenase family, Quinone oxidoreductase subfamily
| null |
SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:37267905}.
| null | null | null | null | null |
FUNCTION: Component of the FERRY complex (Five-subunit Endosomal Rab5 and RNA/ribosome intermediary) (PubMed:37267905, PubMed:37267906). The FERRY complex directly interacts with mRNAs and RAB5A, and functions as a RAB5A effector involved in the localization and the distribution of specific mRNAs most likely by mediating their endosomal transport. The complex recruits mRNAs and ribosomes to early endosomes through direct mRNA-interaction (PubMed:37267905). {ECO:0000269|PubMed:37267905, ECO:0000269|PubMed:37267906}.
|
Homo sapiens (Human)
|
O95831
|
AIFM1_HUMAN
|
MFRCGGLAAGALKQKLVPLVRTVCVRSPRQRNRLPGNLFQRWHVPLELQMTRQMASSGASGGKIDNSVLVLIVGLSTVGAGAYAYKTMKEDEKRYNERISGLGLTPEQKQKKAALSASEGEEVPQDKAPSHVPFLLIGGGTAAFAAARSIRARDPGARVLIVSEDPELPYMRPPLSKELWFSDDPNVTKTLRFKQWNGKERSIYFQPPSFYVSAQDLPHIENGGVAVLTGKKVVQLDVRDNMVKLNDGSQITYEKCLIATGGTPRSLSAIDRAGAEVKSRTTLFRKIGDFRSLEKISREVKSITIIGGGFLGSELACALGRKARALGTEVIQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVGVSSGKLLIKLKDGRKVETDHIVAAVGLEPNVELAKTGGLEIDSDFGGFRVNAELQARSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRLAGENMTGAAKPYWHQSMFWSDLGPDVGYEAIGLVDSSLPTVGVFAKATAQDNPKSATEQSGTGIRSESETESEASEITIPPSTPAVPQAPVQGEDYGKGVIFYLRDKVVVGIVLWNIFNRMPIARKIIKDGEQHEDLNEVAKLFNIHED
|
1.6.99.-
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:23217327, ECO:0000269|PubMed:24914854, ECO:0000269|PubMed:27178839, ECO:0000269|PubMed:27818101};
|
activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; apoptotic process [GO:0006915]; cellular response to aldosterone [GO:1904045]; cellular response to estradiol stimulus [GO:0071392]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to hypoxia [GO:0071456]; cellular response to nitric oxide [GO:0071732]; chromosome condensation [GO:0030261]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; mitochondrial respiratory chain complex assembly [GO:0033108]; mitochondrial respiratory chain complex I assembly [GO:0032981]; neuron apoptotic process [GO:0051402]; neuron differentiation [GO:0030182]; positive regulation of apoptotic process [GO:0043065]; positive regulation of necroptotic process [GO:0060545]; positive regulation of neuron apoptotic process [GO:0043525]; protein import into mitochondrial intermembrane space [GO:0045041]; regulation of apoptotic DNA fragmentation [GO:1902510]; response to ischemia [GO:0002931]; response to L-glutamate [GO:1902065]; response to toxic substance [GO:0009636]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
|
DNA binding [GO:0003677]; FAD binding [GO:0071949]; NAD(P)H oxidase H2O2-forming activity [GO:0016174]; NADH dehydrogenase activity [GO:0003954]; oxidoreductase activity, acting on NAD(P)H [GO:0016651]; poly-ADP-D-ribose binding [GO:0072572]; protein dimerization activity [GO:0046983]
|
PF14721;PF07992;
|
3.30.390.30;3.50.50.60;
|
FAD-dependent oxidoreductase family
|
PTM: Under normal conditions, a 54-residue N-terminal segment is first proteolytically removed during or just after translocation into the mitochondrial intermembrane space (IMS) by the mitochondrial processing peptidase (MPP) to form the inner-membrane-anchored mature form (AIFmit). During apoptosis, it is further proteolytically processed at amino-acid position 101 leading to the generation of the mature form, which is confined to the mitochondrial IMS in a soluble form (AIFsol). AIFsol is released to the cytoplasm in response to specific death signals, and translocated to the nucleus, where it induces nuclear apoptosis in a caspase-independent manner. {ECO:0000269|PubMed:15775970}.; PTM: Ubiquitination by XIAP/BIRC4 does not lead to proteasomal degradation. Ubiquitination at Lys-255 by XIAP/BIRC4 blocks its ability to bind DNA and induce chromatin degradation, thereby inhibiting its ability to induce cell death. {ECO:0000269|PubMed:17967870, ECO:0000269|PubMed:22103349}.
|
SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000269|PubMed:15775970, ECO:0000269|PubMed:24914854, ECO:0000269|PubMed:26004228}. Mitochondrion inner membrane. Cytoplasm {ECO:0000269|PubMed:15775970, ECO:0000269|PubMed:33168626}. Nucleus {ECO:0000269|PubMed:15775970, ECO:0000269|PubMed:17094969, ECO:0000269|PubMed:33168626}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17094969}. Note=Proteolytic cleavage during or just after translocation into the mitochondrial intermembrane space (IMS) results in the formation of an inner-membrane-anchored mature form (AIFmit). During apoptosis, further proteolytic processing leads to a mature form, which is confined to the mitochondrial IMS in a soluble form (AIFsol). AIFsol is released to the cytoplasm in response to specific death signals, and translocated to the nucleus, where it induces nuclear apoptosis (PubMed:15775970). Release into the cytoplasm is mediated upon binding to poly-ADP-ribose chains (By similarity). Translocation into the nucleus is promoted by interaction with (auto-poly-ADP-ribosylated) processed form of PARP1 (PubMed:33168626). Colocalizes with EIF3G in the nucleus and perinuclear region (PubMed:17094969). {ECO:0000250|UniProtKB:Q9Z0X1, ECO:0000269|PubMed:15775970, ECO:0000269|PubMed:17094969, ECO:0000269|PubMed:33168626}.; SUBCELLULAR LOCATION: [Isoform 3]: Mitochondrion intermembrane space {ECO:0000269|PubMed:20111043}. Mitochondrion inner membrane {ECO:0000269|PubMed:20111043}. Note=Has a stronger membrane anchorage than isoform 1. {ECO:0000269|PubMed:20111043}.; SUBCELLULAR LOCATION: [Isoform 4]: Mitochondrion {ECO:0000269|PubMed:16644725}. Cytoplasm, cytosol {ECO:0000269|PubMed:16644725}. Note=In pro-apoptotic conditions, is released from mitochondria to cytosol in a calpain/cathepsin-dependent manner. {ECO:0000269|PubMed:16644725}.; SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm {ECO:0000269|PubMed:16365034}.
|
CATALYTIC ACTIVITY: Reaction=A + H(+) + NADH = AH2 + NAD(+); Xref=Rhea:RHEA:11356, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:23217327, ECO:0000269|PubMed:24914854, ECO:0000269|PubMed:27178839}; CATALYTIC ACTIVITY: [Isoform 4]: Reaction=A + H(+) + NADH = AH2 + NAD(+); Xref=Rhea:RHEA:11356, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:16644725};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.53 mM for NADH {ECO:0000269|PubMed:23217327}; KM=26 uM for cytochrome c (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:23217327, ECO:0000269|PubMed:27178839}; KM=138 uM for dichlorophenolindophenol (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:27178839}; KM=0.51 mM for NADH (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:27178839}; KM=896 uM for NADPH {ECO:0000269|PubMed:24914854}; Note=kcat is 86 min(-1) for dichlorophenolindophenol reduction and 24 min(-1) for cytochrome c reduction (PubMed:27178839). kcat is 1.5 sec(-1) for dichlorophenolindophenol reduction, 3.1 sec(-1) for ferricyanide and 0.6 sec(-1) for cytochrome c reduction (PubMed:24914854). {ECO:0000269|PubMed:24914854, ECO:0000269|PubMed:27178839}; Kinetic parameters: KM=102.6 uM for NADH {ECO:0000269|PubMed:16644725}; KM=45.3 uM for NADPH {ECO:0000269|PubMed:16644725};
| null | null | null |
FUNCTION: Functions both as NADH oxidoreductase and as regulator of apoptosis (PubMed:17094969, PubMed:20362274, PubMed:23217327, PubMed:33168626). In response to apoptotic stimuli, it is released from the mitochondrion intermembrane space into the cytosol and to the nucleus, where it functions as a proapoptotic factor in a caspase-independent pathway (PubMed:20362274). Release into the cytoplasm is mediated upon binding to poly-ADP-ribose chains (By similarity). The soluble form (AIFsol) found in the nucleus induces 'parthanatos' i.e. caspase-independent fragmentation of chromosomal DNA (PubMed:20362274). Binds to DNA in a sequence-independent manner (PubMed:27178839). Interacts with EIF3G, and thereby inhibits the EIF3 machinery and protein synthesis, and activates caspase-7 to amplify apoptosis (PubMed:17094969). Plays a critical role in caspase-independent, pyknotic cell death in hydrogen peroxide-exposed cells (PubMed:19418225). In contrast, participates in normal mitochondrial metabolism. Plays an important role in the regulation of respiratory chain biogenesis by interacting with CHCHD4 and controlling CHCHD4 mitochondrial import (PubMed:26004228). {ECO:0000250|UniProtKB:Q9Z0X1, ECO:0000269|PubMed:17094969, ECO:0000269|PubMed:19418225, ECO:0000269|PubMed:20362274, ECO:0000269|PubMed:23217327, ECO:0000269|PubMed:26004228, ECO:0000269|PubMed:27178839, ECO:0000269|PubMed:33168626}.; FUNCTION: [Isoform 4]: Has NADH oxidoreductase activity. Does not induce nuclear apoptosis. {ECO:0000269|PubMed:16644725}.; FUNCTION: [Isoform 5]: Pro-apoptotic isoform. {ECO:0000269|PubMed:16365034}.
|
Homo sapiens (Human)
|
O95832
|
CLD1_HUMAN
|
MANAGLQLLGFILAFLGWIGAIVSTALPQWRIYSYAGDNIVTAQAMYEGLWMSCVSQSTGQIQCKVFDSLLNLSSTLQATRALMVVGILLGVIAIFVATVGMKCMKCLEDDEVQKMRMAVIGGAIFLLAGLAILVATAWYGNRIVQEFYDPMTPVNARYEFGQALFTGWAAASLCLLGGALLCCSCPRKTTSYPTPRPYPKPAPSSGKDYV
| null | null |
bicellular tight junction assembly [GO:0070830]; calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules [GO:0016338]; cell adhesion [GO:0007155]; cell junction maintenance [GO:0034331]; cell-cell junction organization [GO:0045216]; cellular response to butyrate [GO:1903545]; cellular response to lead ion [GO:0071284]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interferon [GO:0071346]; establishment of blood-nerve barrier [GO:0008065]; establishment of endothelial intestinal barrier [GO:0090557]; establishment of skin barrier [GO:0061436]; liver regeneration [GO:0097421]; maintenance of blood-brain barrier [GO:0035633]; positive regulation of bicellular tight junction assembly [GO:1903348]; positive regulation of cell migration [GO:0030335]; positive regulation of epithelial cell proliferation involved in wound healing [GO:0060054]; positive regulation of wound healing [GO:0090303]; protein complex oligomerization [GO:0051259]; response to dexamethasone [GO:0071548]; response to ethanol [GO:0045471]; response to interleukin-18 [GO:0070673]; response to lipopolysaccharide [GO:0032496]; response to toxic substance [GO:0009636]; xenobiotic transport across blood-nerve barrier [GO:0061772]
|
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; bicellular tight junction [GO:0005923]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; tight junction [GO:0070160]
|
identical protein binding [GO:0042802]; structural molecule activity [GO:0005198]; virus receptor activity [GO:0001618]
|
PF00822;
|
1.20.140.150;
|
Claudin family
| null |
SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:20375010, ECO:0000269|PubMed:23407391}. Cell membrane {ECO:0000269|PubMed:23704991}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:20375010}. Note=Associates with CD81 and the CLDN1-CD81 complex localizes to the basolateral cell membrane. {ECO:0000269|PubMed:20375010}.
| null | null | null | null | null |
FUNCTION: Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia. While some claudin family members play essential roles in the formation of impermeable barriers, others mediate the permeability to ions and small molecules. Often, several claudin family members are coexpressed and interact with each other, and this determines the overall permeability. CLDN1 is required to prevent the paracellular diffusion of small molecules through tight junctions in the epidermis and is required for the normal barrier function of the skin. Required for normal water homeostasis and to prevent excessive water loss through the skin, probably via an indirect effect on the expression levels of other proteins, since CLDN1 itself seems to be dispensable for water barrier formation in keratinocyte tight junctions (PubMed:23407391). {ECO:0000269|PubMed:23407391}.; FUNCTION: (Microbial infection) Acts as a co-receptor for hepatitis C virus (HCV) in hepatocytes (PubMed:17325668, PubMed:20375010, PubMed:24038151). Associates with CD81 and the CLDN1-CD81 receptor complex is essential for HCV entry into host cell (PubMed:20375010). Acts as a receptor for dengue virus (PubMed:24074594). {ECO:0000269|PubMed:17325668, ECO:0000269|PubMed:20375010, ECO:0000269|PubMed:24038151, ECO:0000269|PubMed:24074594}.
|
Homo sapiens (Human)
|
O95833
|
CLIC3_HUMAN
|
MAETKLQLFVKASEDGESVGHCPSCQRLFMVLLLKGVPFTLTTVDTRRSPDVLKDFAPGSQLPILLYDSDAKTDTLQIEDFLEETLGPPDFPSLAPRYRESNTAGNDVFHKFSAFIKNPVPAQDEALYQQLLRALARLDSYLRAPLEHELAGEPQLRESRRRFLDGDRLTLADCSLLPKLHIVDTVCAHFRQAPIPAELRGVRRYLDSAMQEKEFKYTCPHSAEILAAYRPAVHPR
| null | null |
chloride transport [GO:0006821]; signal transduction [GO:0007165]
|
chloride channel complex [GO:0034707]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nuclear body [GO:0016604]; nucleus [GO:0005634]
|
chloride channel activity [GO:0005254]
|
PF13410;PF13409;
|
1.20.1050.10;3.40.30.10;
|
Chloride channel CLIC family
| null |
SUBCELLULAR LOCATION: Nucleus. Membrane; Single-pass membrane protein. Cytoplasm. Note=Predominantly nuclear. Some protein was found in the cytoplasm. Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Can insert into membranes and form chloride ion channels. May participate in cellular growth control. {ECO:0000269|PubMed:9880541}.
|
Homo sapiens (Human)
|
O95834
|
EMAL2_HUMAN
|
MSSFGAGKTKEVIFSVEDGSVKMFLRGRPVPMMIPDELAPTYSLDTRSELPSCRLKLEWVYGYRGRDCRANLYLLPTGEIVYFVASVAVLYSVEEQRQRHYLGHNDDIKCLAIHPDMVTIATGQVAGTTKEGKPLPPHVRIWDSVSLSTLHVLGLGVFDRAVCCVGFSKSNGGNLLCAVDESNDHMLSVWDWAKETKVVDVKCSNEAVLVATFHPTDPTVLITCGKSHIYFWTLEGGSLSKRQGLFEKHEKPKYVLCVTFLEGGDVVTGDSGGNLYVWGKGGNRITQAVLGAHDGGVFGLCALRDGTLVSGGGRDRRVVLWGSDYSKLQEVEVPEDFGPVRTVAEGHGDTLYVGTTRNSILQGSVHTGFSLLVQGHVEELWGLATHPSRAQFVTCGQDKLVHLWSSDSHQPLWSRIIEDPARSAGFHPSGSVLAVGTVTGRWLLLDTETHDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVYTVDQGGRKVSRLGKCSGHSSFITHLDWAQDSSCFVTNSGDYEILYWDPATCKQITSADAVRNMEWATATCVLGFGVFGIWSEGADGTDINAVARSHDGKLLASADDFGKVHLFSYPCCQPRALSHKYGGHSSHVTNVAFLWDDSMALTTGGKDTSVLQWRVV
| null | null |
microtubule cytoskeleton organization [GO:0000226]; negative regulation of microtubule polymerization [GO:0031115]; regulation of microtubule nucleation [GO:0010968]; sensory perception of sound [GO:0007605]; visual perception [GO:0007601]
|
cytoplasm [GO:0005737]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875]; mitotic spindle [GO:0072686]
|
microtubule binding [GO:0008017]; protein self-association [GO:0043621]; tubulin binding [GO:0015631]
|
PF03451;PF00400;
|
2.130.10.10;
|
WD repeat EMAP family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11694528}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11694528}. Note=Colocalizes with the microtubule cytoskeleton. Colocalizes with the mitotic spindle. {ECO:0000269|PubMed:11694528}.
| null | null | null | null | null |
FUNCTION: Tubulin binding protein that inhibits microtubule nucleation and growth, resulting in shorter microtubules. {ECO:0000269|PubMed:11694528}.
|
Homo sapiens (Human)
|
O95835
|
LATS1_HUMAN
|
MKRSEKPEGYRQMRPKTFPASNYTVSSRQMLQEIRESLRNLSKPSDAAKAEHNMSKMSTEDPRQVRNPPKFGTHHKALQEIRNSLLPFANETNSSRSTSEVNPQMLQDLQAAGFDEDMVIQALQKTNNRSIEAAIEFISKMSYQDPRREQMAAAAARPINASMKPGNVQQSVNRKQSWKGSKESLVPQRHGPPLGESVAYHSESPNSQTDVGRPLSGSGISAFVQAHPSNGQRVNPPPPPQVRSVTPPPPPRGQTPPPRGTTPPPPSWEPNSQTKRYSGNMEYVISRISPVPPGAWQEGYPPPPLNTSPMNPPNQGQRGISSVPVGRQPIIMQSSSKFNFPSGRPGMQNGTGQTDFMIHQNVVPAGTVNRQPPPPYPLTAANGQSPSALQTGGSAAPSSYTNGSIPQSMMVPNRNSHNMELYNISVPGLQTNWPQSSSAPAQSSPSSGHEIPTWQPNIPVRSNSFNNPLGNRASHSANSQPSATTVTAITPAPIQQPVKSMRVLKPELQTALAPTHPSWIPQPIQTVQPSPFPEGTASNVTVMPPVAEAPNYQGPPPPYPKHLLHQNPSVPPYESISKPSKEDQPSLPKEDESEKSYENVDSGDKEKKQITTSPITVRKNKKDEERRESRIQSYSPQAFKFFMEQHVENVLKSHQQRLHRKKQLENEMMRVGLSQDAQDQMRKMLCQKESNYIRLKRAKMDKSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKYYQSGDHPRQDSMDFSNEWGDPSSCRCGDRLKPLERRAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKNGADEIKAHPFFKTIDFSSDLRQQSASYIPKITHPTDTSNFDPVDPDKLWSDDNEEENVNDTLNGWYKNGKHPEHAFYEFTFRRFFDDNGYPYNYPKPIEYEYINSQGSEQQSDEDDQNTGSEIKNRDLVYV
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
|
cell division [GO:0051301]; cytoplasmic sequestering of protein [GO:0051220]; G1/S transition of mitotic cell cycle [GO:0000082]; G2/M transition of mitotic cell cycle [GO:0000086]; hippo signaling [GO:0035329]; hormone-mediated signaling pathway [GO:0009755]; inner cell mass cell fate commitment [GO:0001827]; inner cell mass cellular morphogenesis [GO:0001828]; keratinocyte differentiation [GO:0030216]; mammary gland epithelial cell differentiation [GO:0060644]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045736]; negative regulation of protein localization to nucleus [GO:1900181]; positive regulation of apoptotic process [GO:0043065]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; protein phosphorylation [GO:0006468]; regulation of actin filament polymerization [GO:0030833]; regulation of intracellular estrogen receptor signaling pathway [GO:0033146]; regulation of organ growth [GO:0046620]; regulation of protein-containing complex assembly [GO:0043254]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]; regulation of ubiquitin-dependent protein catabolic process [GO:2000058]; sister chromatid segregation [GO:0000819]
|
centrosome [GO:0005813]; cytosol [GO:0005829]; midbody [GO:0030496]; nucleus [GO:0005634]; spindle pole [GO:0000922]
|
ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; nuclear estrogen receptor binding [GO:0030331]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;PF00433;PF00627;
|
1.10.8.10;1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family
|
PTM: Autophosphorylated and phosphorylated during M-phase of the cell cycle (PubMed:10518011, PubMed:15122335, PubMed:9988268). Phosphorylated by STK3/MST2 at Ser-909 and Thr-1079, which results in its activation (PubMed:15688006). Phosphorylated by MAP4Ks; in parallel to STK3/MST2 and resulting to its activation (PubMed:26437443). Phosphorylation at Ser-464 by NUAK1 and NUAK2 leads to decreased protein level and is required to regulate cellular senescence and cellular ploidy (PubMed:19927127). {ECO:0000269|PubMed:10518011, ECO:0000269|PubMed:15122335, ECO:0000269|PubMed:15688006, ECO:0000269|PubMed:19927127, ECO:0000269|PubMed:26437443, ECO:0000269|PubMed:9988268}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:10518011}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:10518011}. Midbody {ECO:0000269|PubMed:10518011}. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:10518011}. Note=Localizes to the centrosomes throughout interphase but migrates to the mitotic apparatus, including spindle pole bodies, mitotic spindle, and midbody, during mitosis. {ECO:0000269|PubMed:10518011}.
|
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:10518011, ECO:0000269|PubMed:15122335}; 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:10518011, ECO:0000269|PubMed:15122335};
| null | null | null | null |
FUNCTION: Negative regulator of YAP1 in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Acts as a tumor suppressor which plays a critical role in maintenance of ploidy through its actions in both mitotic progression and the G1 tetraploidy checkpoint. Negatively regulates G2/M transition by down-regulating CDK1 kinase activity. Involved in the control of p53 expression. Affects cytokinesis by regulating actin polymerization through negative modulation of LIMK1. May also play a role in endocrine function. Plays a role in mammary gland epithelial cell differentiation, both through the Hippo signaling pathway and the intracellular estrogen receptor signaling pathway by promoting the degradation of ESR1 (PubMed:28068668). {ECO:0000269|PubMed:10518011, ECO:0000269|PubMed:10831611, ECO:0000269|PubMed:15122335, ECO:0000269|PubMed:15220930, ECO:0000269|PubMed:18158288, ECO:0000269|PubMed:19927127, ECO:0000269|PubMed:26437443, ECO:0000269|PubMed:28068668}.
|
Homo sapiens (Human)
|
O95837
|
GNA14_HUMAN
|
MAGCCCLSAEEKESQRISAEIERQLRRDKKDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDRKGFTKLVYQNIFTAMQAMIRAMDTLRIQYVCEQNKENAQIIREVEVDKVSMLSREQVEAIKQLWQDPGIQECYDRRREYQLSDSAKYYLTDIDRIATPSFVPTQQDVLRVRVPTTGIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFESVTSIIFLVALSEYDQVLAECDNENRMEESKALFKTIITYPWFLNSSVILFLNKKDLLEEKIMYSHLISYFPEYTGPKQDVRAARDFILKLYQDQNPDKEKVIYSHFTCATDTDNIRFVFAAVKDTILQLNLREFNLV
| null | null |
action potential [GO:0001508]; adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; phospholipase C-activating dopamine receptor signaling pathway [GO:0060158]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; heterotrimeric G-protein complex [GO:0005834]; plasma membrane [GO:0005886]
|
G protein-coupled receptor binding [GO:0001664]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]
|
PF00503;
|
1.10.400.10;3.40.50.300;
|
G-alpha family, G(q) subfamily
| null | null | null | null | null | null | null |
FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
|
Homo sapiens (Human)
|
O95843
|
GUC1C_HUMAN
|
MGNGKSIAGDQKAVPTQETHVWYRTFMMEYPSGLQTLHEFKTLLGLQGLNQKANKHIDQVYNTFDTNKDGFVDFLEFIAAVNLIMQEKMEQKLKWYFKLYDADGNGSIDKNELLDMFMAVQALNGQQTLSPEEFINLVFHKIDINNDGELTLEEFINGMAKDQDLLEIVYKSFDFSNVLRVICNGKQPDMETDSSKSPDKAGLGKVKMK
| null | null |
signal transduction [GO:0007165]; visual perception [GO:0007601]
|
photoreceptor disc membrane [GO:0097381]
|
calcium ion binding [GO:0005509]; calcium sensitive guanylate cyclase activator activity [GO:0008048]
|
PF13202;PF13499;
|
1.10.238.10;
| null | null | null | null | null | null | null | null |
FUNCTION: Stimulates guanylyl cyclase 1 (GC1) and GC2 when free calcium ions concentration is low and inhibits guanylyl cyclases when free calcium ions concentration is elevated. This Ca(2+)-sensitive regulation of guanylyl cyclase (GC) is a key event in recovery of the dark state of rod photoreceptors following light exposure.
|
Homo sapiens (Human)
|
O95847
|
UCP4_HUMAN
|
MSVPEEEERLLPLTQRWPRASKFLLSGCAATVAELATFPLDLTKTRLQMQGEAALARLGDGARESAPYRGMVRTALGIIEEEGFLKLWQGVTPAIYRHVVYSGGRMVTYEHLREVVFGKSEDEHYPLWKSVIGGMMAGVIGQFLANPTDLVKVQMQMEGKRKLEGKPLRFRGVHHAFAKILAEGGIRGLWAGWVPNIQRAALVNMGDLTTYDTVKHYLVLNTPLEDNIMTHGLSSLCSGLVASILGTPADVIKSRIMNQPRDKQGRGLLYKSSTDCLIQAVQGEGFMSLYKGFLPSWLRMTPWSMVFWLTYEKIREMSGVSPF
| null | null |
inner ear development [GO:0048839]; intracellular triglyceride homeostasis [GO:0035356]; negative regulation of mitochondrial calcium ion concentration [GO:0051562]; negative regulation of mitochondrial membrane potential [GO:0010917]; negative regulation of neuron apoptotic process [GO:0043524]; positive regulation of cell population proliferation [GO:0008284]; regulation of glucose import [GO:0046324]; response to cold [GO:0009409]
|
apical part of cell [GO:0045177]; mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]
|
chloride transmembrane transporter activity [GO:0015108]; protein homodimerization activity [GO:0042803]; proton transmembrane transporter activity [GO:0015078]; transmembrane transporter activity [GO:0022857]
|
PF00153;
|
1.50.40.10;
|
Mitochondrial carrier (TC 2.A.29) family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:10025957}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to neuronal cell body and processes. Within mitochondrial inner membrane, it is mainly observed in the inner boundary membrane locally separated from F(1)F(0) ATP synthase, which is preferentially localized in cristae. {ECO:0000250|UniProtKB:Q9D6D0}.
|
CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000269|PubMed:22524567, ECO:0000269|PubMed:26182433}; CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:22524567, ECO:0000269|PubMed:26182433};
| null | null | null | null |
FUNCTION: Facilitates proton transport across the inner mitochondrial membrane and may dissipate excessive proton gradient associated with oxidative and metabolic stress at neuronal synapses. Regulates glutamate-induced proton conductance in astrocytes, shifting the energy metabolism toward aerobic glycolysis and lactate transfer to neurons for ATP synthesis. Can transport chloride ions with lower efficiency. The transport mechanism remains to be elucidated. {ECO:0000250|UniProtKB:Q9D6D0, ECO:0000269|PubMed:10025957, ECO:0000269|PubMed:22524567, ECO:0000269|PubMed:26182433}.
|
Homo sapiens (Human)
|
O95848
|
NUD14_HUMAN
|
MERIEGASVGRCAASPYLRPLTLHYRQNGAQKSWDFMKTHDSVTVLLFNSSRRSLVLVKQFRPAVYAGEVERRFPGSLAAVDQDGPRELQPALPGSAGVTVELCAGLVDQPGLSLEEVACKEAWEECGYHLAPSDLRRVATYWSGVGLTGSRQTMFYTEVTDAQRSGPGGGLVEEGELIEVVHLPLEGAQAFADDPDIPKTLGVIFGVSWFLSQVAPNLDLQ
|
3.6.1.45
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
|
nucleoside phosphate metabolic process [GO:0006753]; protein N-linked glycosylation via asparagine [GO:0018279]; ribose phosphate metabolic process [GO:0019693]
|
cytosol [GO:0005829]
|
ADP-ribose diphosphatase activity [GO:0047631]; ADP-sugar diphosphatase activity [GO:0019144]; bis(5'-adenosyl)-pentaphosphatase activity [GO:0034432]; guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity [GO:0008893]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; UDP-sugar diphosphatase activity [GO:0008768]
| null |
3.90.79.10;
|
Nudix hydrolase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12429023}.
|
CATALYTIC ACTIVITY: Reaction=UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate.; EC=3.6.1.45;
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-9.5.;
| null |
FUNCTION: Hydrolyzes UDP-glucose to glucose 1-phosphate and UMP and ADP-ribose to ribose 5-phosphate and AMP. The physiological substrate is probably UDP-glucose. Poor activity on other substrates such as ADP-glucose, CDP-glucose, GDP-glucose and GDP-mannose.
|
Homo sapiens (Human)
|
O95858
|
TSN15_HUMAN
|
MPRGDSEQVRYCARFSYLWLKFSLIIYSTVFWLIGALVLSVGIYAEVERQKYKTLESAFLAPAIILILLGVVMFMVSFIGVLASLRDNLYLLQAFMYILGICLIMELIGGVVALTFRNQTIDFLNDNIRRGIENYYDDLDFKNIMDFVQKKFKCCGGEDYRDWSKNQYHDCSAPGPLACGVPYTCCIRNTTEVVNTMCGYKTIDKERFSVQDVIYVRGCTNAVIIWFMDNYTIMAGILLGILLPQFLGVLLTLLYITRVEDIIMEHSVTDGLLGPGAKPSVEAAGTGCCLCYPN
| null | null |
negative regulation of Notch signaling pathway [GO:0045746]; protein localization to plasma membrane [GO:0072659]; protein maturation [GO:0051604]; regulation of membrane protein ectodomain proteolysis [GO:0051043]
|
cell junction [GO:0030054]; cell surface [GO:0009986]; cytosol [GO:0005829]; endoplasmic reticulum lumen [GO:0005788]; intracellular membrane-bounded organelle [GO:0043231]; late endosome membrane [GO:0031902]; nuclear body [GO:0016604]; plasma membrane [GO:0005886]; tetraspanin-enriched microdomain [GO:0097197]
|
enzyme binding [GO:0019899]
|
PF00335;
|
1.10.1450.10;
|
Tetraspanin (TM4SF) family
|
PTM: Palmitoylated. {ECO:0000269|PubMed:31792032}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26686862, ECO:0000269|PubMed:30463011, ECO:0000269|PubMed:31792032}; Multi-pass membrane protein {ECO:0000305}. Late endosome membrane {ECO:0000269|PubMed:26686862}.
| null | null | null | null | null |
FUNCTION: Part of TspanC8 subgroup, composed of 6 members that interact with the transmembrane metalloprotease ADAM10. This interaction is required for ADAM10 exit from the endoplasmic reticulum and for enzymatic maturation and trafficking to the cell surface as well as substrate specificity. Different TspanC8/ADAM10 complexes have distinct substrates (PubMed:26686862, PubMed:30463011, PubMed:31792032, PubMed:34739841). Promotes ADAM10-mediated cleavage of CDH2 (PubMed:34739841). Negatively regulates ligand-induced Notch activity probably by regulating ADAM10 activity (PubMed:26686862, PubMed:31792032). {ECO:0000269|PubMed:26686862, ECO:0000269|PubMed:30463011, ECO:0000269|PubMed:31792032, ECO:0000269|PubMed:34739841}.
|
Homo sapiens (Human)
|
O95859
|
TSN12_HUMAN
|
MAREDSVKCLRCLLYALNLLFWLMSISVLAVSAWMRDYLNNVLTLTAETRVEEAVILTYFPVVHPVMIAVCCFLIIVGMLGYCGTVKRNLLLLAWYFGSLLVIFCVELACGVWTYEQELMVPVQWSDMVTLKARMTNYGLPRYRWLTHAWNFFQREFKCCGVVYFTDWLEMTEMDWPPDSCCVREFPGCSKQAHQEDLSDLYQEGCGKKMYSFLRGTKQLQVLRFLGISIGVTQILAMILTITLLWALYYDRREPGTDQMMSLKNDNSQHLSCPSVELLKPSLSRIFEHTSMANSFNTHFEMEEL
| null | null |
angiogenesis [GO:0001525]; cell surface receptor signaling pathway [GO:0007166]; maintenance of blood-brain barrier [GO:0035633]; Norrin signaling pathway [GO:0110135]; regulation of angiogenesis [GO:0045765]; retina layer formation [GO:0010842]
|
membrane [GO:0016020]; plasma membrane [GO:0005886]
| null |
PF00335;
|
1.10.1450.10;
|
Tetraspanin (TM4SF) family
|
PTM: Palmitoylated; required for interaction with ADAM10. The precise position of palmitoylated residues is unclear and occurs either on Cys-9, Cys-12 and/or Cys-83. {ECO:0000269|PubMed:19587294}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Regulator of cell surface receptor signal transduction. Plays a central role in retinal vascularization by regulating norrin (NDP) signal transduction. Acts in concert with norrin (NDP) to promote FZD4 multimerization and subsequent activation of FZD4, leading to promote accumulation of beta-catenin (CTNNB1) and stimulate LEF/TCF-mediated transcriptional programs. Suprisingly, it only activates the norrin (NDP)-dependent activation of FZD4, while it does not activate the Wnt-dependent activation of FZD4, suggesting the existence of a Wnt-independent signaling that also promote accumulation the beta-catenin (CTNNB1) (By similarity). Acts as a regulator of membrane proteinases such as ADAM10 and MMP14/MT1-MMP. Activates ADAM10-dependent cleavage activity of amyloid precursor protein (APP). Activates MMP14/MT1-MMP-dependent cleavage activity. {ECO:0000250, ECO:0000269|PubMed:19211836, ECO:0000269|PubMed:19587294}.
|
Homo sapiens (Human)
|
O95861
|
BPNT1_HUMAN
|
MASSNTVLMRLVASAYSIAQKAGMIVRRVIAEGDLGIVEKTCATDLQTKADRLAQMSICSSLARKFPKLTIIGEEDLPSEEVDQELIEDSQWEEILKQPCPSQYSAIKEEDLVVWVDPLDGTKEYTEGLLDNVTVLIGIAYEGKAIAGVINQPYYNYEAGPDAVLGRTIWGVLGLGAFGFQLKEVPAGKHIITTTRSHSNKLVTDCVAAMNPDAVLRVGGAGNKIIQLIEGKASAYVFASPGCKKWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMNSAGVLATLRNYDYYASRVPESIKNALVP
|
3.1.3.57; 3.1.3.7
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10675562}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000269|Ref.14};
|
3'-phosphoadenosine 5'-phosphosulfate metabolic process [GO:0050427]; nervous system development [GO:0007399]; nucleobase-containing compound metabolic process [GO:0006139]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; sulfate assimilation [GO:0000103]
|
cytosol [GO:0005829]
|
3'(2'),5'-bisphosphate nucleotidase activity [GO:0008441]; inositol-1,4-bisphosphate 1-phosphatase activity [GO:0004441]; metal ion binding [GO:0046872]
|
PF00459;
|
3.40.190.80;3.30.540.10;
|
Inositol monophosphatase superfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate; Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7; Evidence={ECO:0000269|PubMed:10675562}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10041; Evidence={ECO:0000305|PubMed:10675562}; CATALYTIC ACTIVITY: Reaction=adenosine 2',5'-bisphosphate + H2O = AMP + phosphate; Xref=Rhea:RHEA:77643, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:194156, ChEBI:CHEBI:456215; EC=3.1.3.7; Evidence={ECO:0000269|PubMed:10675562}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77644; Evidence={ECO:0000305|PubMed:10675562}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + H2O = adenosine 5'-phosphosulfate + phosphate; Xref=Rhea:RHEA:77639, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339; EC=3.1.3.7; Evidence={ECO:0000250|UniProtKB:Q9Z1N4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77640; Evidence={ECO:0000250|UniProtKB:Q9Z1N4}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate; Xref=Rhea:RHEA:15553, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58282, ChEBI:CHEBI:58469; EC=3.1.3.57; Evidence={ECO:0000269|PubMed:10675562}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15554; Evidence={ECO:0000305|PubMed:10675562}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4-trisphosphate + H2O = 1D-myo-inositol 3,4-bisphosphate + phosphate; Xref=Rhea:RHEA:70319, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58414, ChEBI:CHEBI:83241; Evidence={ECO:0000250|UniProtKB:Q9Z1N4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70320; Evidence={ECO:0000250|UniProtKB:Q9Z1N4};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.4 uM for 1D-myo-inositol 1,4-bisphosphate {ECO:0000269|PubMed:10675562}; Vmax=1.1 umol/min/mg enzyme with adenosine 3',5'-bisphosphate as substrate {ECO:0000269|PubMed:10675562}; Vmax=0.2 umol/min/mg enzyme with 1D-myo-inositol 1,4-bisphosphate as substrate {ECO:0000269|PubMed:10675562}; Note=KM for adenosine 3',5'-bisphosphate is below 1 uM. {ECO:0000269|PubMed:10675562};
| null | null | null |
FUNCTION: Phosphatase that converts 3'(2')-phosphoadenosine 5'-phosphate (PAP) to AMP and inositol 1,4-bisphosphate (Ins(1,4)P2) to inositol 4-phosphate (PubMed:10675562). Is also able to hydrolyze adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) (By similarity). Probably prevents the toxic accumulation of PAP, a compound which inhibits a variety of proteins, including PAPS-utilizing enzymes such as sulfotransferases, and RNA processing enzymes. Could also play a role in inositol recycling and phosphoinositide metabolism. Is not active on 3'-AMP, inositol-1-phosphate and inositol-1,4,5-triphosphate (PubMed:10675562). {ECO:0000250|UniProtKB:Q9Z1N4, ECO:0000269|PubMed:10675562}.
|
Homo sapiens (Human)
|
O95863
|
SNAI1_HUMAN
|
MPRSFLVRKPSDPNRKPNYSELQDSNPEFTFQQPYDQAHLLAAIPPPEILNPTASLPMLIWDSVLAPQAQPIAWASLRLQESPRVAELTSLSDEDSGKGSQPPSPPSPAPSSFSSTSVSSLEAEAYAAFPGLGQVPKQLAQLSEAKDLQARKAFNCKYCNKEYLSLGALKMHIRSHTLPCVCGTCGKAFSRPWLLQGHVRTHTGEKPFSCPHCSRAFADRSNLRAHLQTHSDVKKYQCQACARTFSRMSLLHKHQESGCSGCPR
| null | null |
aortic valve morphogenesis [GO:0003180]; canonical Wnt signaling pathway [GO:0060070]; cartilage morphogenesis [GO:0060536]; epithelial cell migration [GO:0010631]; epithelial to mesenchymal transition [GO:0001837]; epithelial to mesenchymal transition involved in endocardial cushion formation [GO:0003198]; hair follicle morphogenesis [GO:0031069]; heterochromatin organization [GO:0070828]; left/right pattern formation [GO:0060972]; mesoderm formation [GO:0001707]; negative regulation of cell differentiation involved in embryonic placenta development [GO:0060806]; negative regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043518]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage [GO:1902230]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of vitamin D biosynthetic process [GO:0010957]; Notch signaling pathway [GO:0007219]; osteoblast differentiation [GO:0001649]; positive regulation of cell migration [GO:0030335]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; regulation of bicellular tight junction assembly [GO:2000810]; regulation of DNA-templated transcription [GO:0006355]; roof of mouth development [GO:0060021]; trophoblast giant cell differentiation [GO:0060707]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; fibrillar center [GO:0001650]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]
|
DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; kinase binding [GO:0019900]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00096;PF13912;
|
3.30.160.60;
|
Snail C2H2-type zinc-finger protein family
|
PTM: Phosphorylated by GSK3B. Once phosphorylated, it becomes a target for BTRC ubiquitination. Phosphorylation by CSNK1E, probably at Ser-104, provides the priming site for the subsequent phosphorylation by GSK3B, probably at Ser-100 and Ser-96. Phosphorylation by PAK1 may modulate its transcriptional activity by promoting increased accumulation in the nucleus. Phosphorylation at Ser-11 and Ser-92 positively regulates its functions in induction of EMT and cell survival, respectively. Phosphorylation by LATS2, upon mitotic stress, oncogenic stress or Hippo pathway activation, occurs in the nucleus and promotes nuclear retention and stabilization of total cellular protein level (PubMed:24157836). {ECO:0000269|PubMed:15647282, ECO:0000269|PubMed:19923321, ECO:0000269|PubMed:20305697, ECO:0000269|PubMed:24157836, ECO:0000305|PubMed:15448698}.; PTM: Ubiquitinated on Lys-98, Lys-137 and Lys-146 by FBXL14 and BTRC leading to degradation (PubMed:19955572). BTRC-triggered ubiquitination requires previous GSK3B-mediated SNAI1 phosphorylation. Ubiquitination induced upon interaction with NOTCH1 or TP53/p53 is mediated by MDM2 (PubMed:20385133). Ubiquitinated in a FBXL5-dependent manner; preventing interaction with DNA and promoting its degradation (PubMed:24157836). Deubiquitinated by USP37; leading to stabilization (PubMed:31911859). {ECO:0000269|PubMed:19955572, ECO:0000269|PubMed:20385133, ECO:0000269|PubMed:24157836, ECO:0000269|PubMed:31911859}.; PTM: O-GlcNAcylation at Ser-112 is enhanced in hyperglycaemic conditions, it opposes phosphorylation by GSK3B, and stabilizes the protein.; PTM: ADP-ribosylation by PARP1 increases protein half-life and may be involved in TGFB-induced SNAI1 up-regulation.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15448698, ECO:0000269|PubMed:15833848, ECO:0000269|PubMed:20389281, ECO:0000269|PubMed:24157836, ECO:0000269|PubMed:24699649, ECO:0000269|PubMed:25893292}. Cytoplasm {ECO:0000269|PubMed:15448698, ECO:0000269|PubMed:15833848}. Note=Once phosphorylated (probably on Ser-107, Ser-111, Ser-115 and Ser-119) it is exported from the nucleus to the cytoplasm where subsequent phosphorylation of the destruction motif and ubiquitination involving BTRC occurs. {ECO:0000269|PubMed:15448698}.
| null | null | null | null | null |
FUNCTION: Involved in induction of the epithelial to mesenchymal transition (EMT), formation and maintenance of embryonic mesoderm, growth arrest, survival and cell migration. Binds to 3 E-boxes of the E-cadherin/CDH1 gene promoter and to the promoters of CLDN7 and KRT8 and, in association with histone demethylase KDM1A which it recruits to the promoters, causes a decrease in dimethylated H3K4 levels and represses transcription (PubMed:20389281, PubMed:20562920). The N-terminal SNAG domain competes with histone H3 for the same binding site on the histone demethylase complex formed by KDM1A and RCOR1, and thereby inhibits demethylation of histone H3 at 'Lys-4' (in vitro) (PubMed:20389281, PubMed:21300290, PubMed:23721412). During EMT, involved with LOXL2 in negatively regulating pericentromeric heterochromatin transcription (By similarity). SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits (By similarity). Associates with EGR1 and SP1 to mediate tetradecanoyl phorbol acetate (TPA)-induced up-regulation of CDKN2B, possibly by binding to the CDKN2B promoter region 5'-TCACA-3. In addition, may also activate the CDKN2B promoter by itself. {ECO:0000250|UniProtKB:Q02085, ECO:0000269|PubMed:10655587, ECO:0000269|PubMed:15647282, ECO:0000269|PubMed:16096638, ECO:0000269|PubMed:20121949, ECO:0000269|PubMed:20389281, ECO:0000269|PubMed:20562920, ECO:0000269|PubMed:21300290, ECO:0000269|PubMed:21952048, ECO:0000269|PubMed:23721412}.
|
Homo sapiens (Human)
|
O95864
|
FADS2_HUMAN
|
MGKGGNQGEGAAEREVSVPTFSWEEIQKHNLRTDRWLVIDRKVYNITKWSIQHPGGQRVIGHYAGEDATDAFRAFHPDLEFVGKFLKPLLIGELAPEEPSQDHGKNSKITEDFRALRKTAEDMNLFKTNHVFFLLLLAHIIALESIAWFTVFYFGNGWIPTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGHLKGASANWWNHRHFQHHAKPNIFHKDPDVNMLHVFVLGEWQPIEYGKKKLKYLPYNHQHEYFFLIGPPLLIPMYFQYQIIMTMIVHKNWVDLAWAVSYYIRFFITYIPFYGILGALLFLNFIRFLESHWFVWVTQMNHIVMEIDQEAYRDWFSSQLTATCNVEQSFFNDWFSGHLNFQIEHHLFPTMPRHNLHKIAPLVKSLCAKHGIEYQEKPLLRALLDIIRSLKKSGKLWLDAYLHK
|
1.14.19.3
| null |
alpha-linolenic acid metabolic process [GO:0036109]; arachidonic acid metabolite production involved in inflammatory response [GO:0002538]; linoleic acid metabolic process [GO:0043651]; lipid metabolic process [GO:0006629]; positive regulation of cellular response to oxidative stress [GO:1900409]; unsaturated fatty acid biosynthetic process [GO:0006636]
|
endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
linoleoyl-CoA desaturase activity [GO:0016213]; oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water [GO:0016717]; stearoyl-CoA 9-desaturase activity [GO:0004768]
|
PF00173;PF00487;
|
3.10.120.10;
|
Fatty acid desaturase type 1 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (6Z,9Z,12Z)-octadecatrienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:47140, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57363, ChEBI:CHEBI:57383; EC=1.14.19.3; Evidence={ECO:0000269|PubMed:12713571}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47141; Evidence={ECO:0000269|PubMed:12713571}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:47144, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:71489, ChEBI:CHEBI:74034; EC=1.14.19.3; Evidence={ECO:0000250|UniProtKB:Q9Z0R9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47145; Evidence={ECO:0000250|UniProtKB:Q9Z0R9}; CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + hexadecanoyl-CoA + O2 = (6Z)-hexadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:37023, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57379, ChEBI:CHEBI:74339; Evidence={ECO:0000269|PubMed:12713571}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37024; Evidence={ECO:0000269|PubMed:12713571}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z,18Z,21Z)-tetracosapentaenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (6Z,9Z,12Z,15Z,18Z,21Z)-tetracosahexaenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:36999, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:74083, ChEBI:CHEBI:74086; Evidence={ECO:0000250|UniProtKB:Q9Z122}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37000; Evidence={ECO:0000250|UniProtKB:Q9Z122}; CATALYTIC ACTIVITY: Reaction=(11E)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (6Z,11E)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46064, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:74296, ChEBI:CHEBI:85652; Evidence={ECO:0000250|UniProtKB:Q9Z122}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46065; Evidence={ECO:0000250|UniProtKB:Q9Z122}; CATALYTIC ACTIVITY: Reaction=(11Z,14Z)-eicosadienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (8Z,11Z,14Z)-eicosatrienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:39567, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:74264, ChEBI:CHEBI:76410; Evidence={ECO:0000250|UniProtKB:B8R1K0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39568; Evidence={ECO:0000250|UniProtKB:B8R1K0}; CATALYTIC ACTIVITY: Reaction=(11Z,14Z,17Z)-eicosatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (8Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:39571, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:74265, ChEBI:CHEBI:74328; Evidence={ECO:0000250|UniProtKB:B8R1K0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39572; Evidence={ECO:0000250|UniProtKB:B8R1K0};
| null |
PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis. {ECO:0000305|PubMed:9867867}.
| null | null |
FUNCTION: Involved in the biosynthesis of highly unsaturated fatty acids (HUFA) from the essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3) precursors, acting as a fatty acyl-coenzyme A (CoA) desaturase that introduces a cis double bond at carbon 6 of the fatty acyl chain. Catalyzes the first and rate limiting step in this pathway which is the desaturation of LA (18:2n-6) and ALA (18:3n-3) into gamma-linoleate (GLA) (18:3n-6) and stearidonate (18:4n-3), respectively (PubMed:12713571). Subsequently, in the biosynthetic pathway of HUFA n-3 series, it desaturates tetracosapentaenoate (24:5n-3) to tetracosahexaenoate (24:6n-3), which is then converted to docosahexaenoate (DHA)(22:6n-3), an important lipid for nervous system function (By similarity). Desaturates hexadecanate (palmitate) to produce 6Z-hexadecenoate (sapienate), a fatty acid unique to humans and major component of human sebum, that has been implicated in the development of acne and may have potent antibacterial activity (PubMed:12713571). It can also desaturate (11E)-octadecenoate (trans-vaccenoate, the predominant trans fatty acid in human milk) at carbon 6 generating (6Z,11E)-octadecadienoate (By similarity). In addition to Delta-6 activity, this enzyme exhibits Delta-8 activity with slight biases toward n-3 fatty acyl-CoA substrates (By similarity). {ECO:0000250|UniProtKB:B8R1K0, ECO:0000250|UniProtKB:Q9Z122, ECO:0000269|PubMed:12713571}.
|
Homo sapiens (Human)
|
O95865
|
DDAH2_HUMAN
|
MGTPGEGLGRCSHALIRGVPESLASGEGAGAGLPALDLAKAQREHGVLGGKLRQRLGLQLLELPPEESLPLGPLLGDTAVIQGDTALITRPWSPARRPEVDGVRKALQDLGLRIVEIGDENATLDGTDVLFTGREFFVGLSKWTNHRGAEIVADTFRDFAVSTVPVSGPSHLRGLCGMGGPRTVVAGSSDAAQKAVRAMAVLTDHPYASLTLPDDAAADCLFLRPGLPGVPPFLLHRGGGDLPNSQEALQKLSDVTLVPVSCSELEKAGAGLSSLCLVLSTRPHS
|
3.-.-.-
| null |
arginine metabolic process [GO:0006525]; negative regulation of apoptotic process [GO:0043066]; positive regulation of nitric oxide biosynthetic process [GO:0045429]
|
extracellular exosome [GO:0070062]; mitochondrion [GO:0005739]
|
amino acid binding [GO:0016597]; hydrolase activity [GO:0016787]
| null | null |
DDAH family
|
PTM: Phosphorylated by TBK1. Phosphorylation inhibits the translocation into the mitochondrion upon Sendai viral infection. {ECO:0000269|PubMed:33850055}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21898353, ECO:0000269|PubMed:33850055}. Mitochondrion {ECO:0000269|PubMed:21898353, ECO:0000269|PubMed:33850055}. Note=Translocates from cytosol to mitochondrion upon IL1B stimulation in chondrocytes.; SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:33850055}. Note=(Microbial infection) Translocates to the mitochondrion upon Sendai viral infection. {ECO:0000269|PubMed:33850055}.
| null | null | null | null | null |
FUNCTION: Putative hydrolase with unknown substrate (Probable). Does not hydrolyze N(G),N(G)-dimethyl-L-arginine (ADMA) which acts as an inhibitor of NOS (PubMed:21493890, PubMed:37296100). In endothelial cells, induces expression of vascular endothelial growth factor (VEGF) via phosphorylation of the transcription factor SP1 by PKA in a process that is independent of NO and NO synthase (By similarity). Similarly, enhances pancreatic insulin secretion through SP1-mediated transcriptional up-regulation of secretagogin/SCGN, an insulin vesicle docking protein (By similarity). Upon viral infection, relocates to mitochondria where it promotes mitochondrial fission through activation of DNM1L leading to the inhibition of innate response activation mediated by MAVS (PubMed:33850055). {ECO:0000250|UniProtKB:Q99LD8, ECO:0000269|PubMed:21493890, ECO:0000269|PubMed:33850055, ECO:0000269|PubMed:37296100, ECO:0000305|PubMed:10493931, ECO:0000305|PubMed:21493890, ECO:0000305|PubMed:37296100}.
|
Homo sapiens (Human)
|
O95866
|
G6B_HUMAN
|
MAVFLQLLPLLLSRAQGNPGASLDGRPGDRVNLSCGGVSHPIRWVWAPSFPACKGLSKGRRPILWASSSGTPTVPPLQPFVGRLRSLDSGIRRLELLLSAGDSGTFFCKGRHEDESRTVLHVLGDRTYCKAPGPTHGSVYPQLLIPLLGAGLVLGLGALGLVWWLHRRLPPQPIRPLPRFAPLVKTEPQRPVKEEEPKIPGDLDQEPSLLYADLDHLALSRPRRLSTADPADASTIYAVVV
| null | null |
blood coagulation [GO:0007596]; erythrocyte differentiation [GO:0030218]; integrin-mediated signaling pathway [GO:0007229]; megakaryocyte development [GO:0035855]; megakaryocyte differentiation [GO:0030219]; negative regulation of signal transduction [GO:0009968]; platelet formation [GO:0030220]
|
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
|
heparin binding [GO:0008201]
|
PF15096;
| null | null |
PTM: All isoforms are N-glycosylated. {ECO:0000269|PubMed:11544253, ECO:0000269|PubMed:23112346}.; PTM: Isoform E is O-glycosylated. {ECO:0000269|PubMed:11544253}.; PTM: Phosphorylated. {ECO:0000269|PubMed:11544253, ECO:0000269|PubMed:23112346}.
|
SUBCELLULAR LOCATION: [Isoform E]: Endoplasmic reticulum {ECO:0000269|PubMed:11544253}. Golgi apparatus {ECO:0000269|PubMed:11544253}.; SUBCELLULAR LOCATION: [Isoform D]: Endoplasmic reticulum {ECO:0000269|PubMed:11544253}. Golgi apparatus {ECO:0000269|PubMed:11544253}.; SUBCELLULAR LOCATION: [Isoform B]: Cell membrane {ECO:0000269|PubMed:11544253}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform A]: Cell membrane {ECO:0000269|PubMed:11544253}; Single-pass type I membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Inhibitory receptor that acts as a critical regulator of hematopoietic lineage differentiation, megakaryocyte function and platelet production (PubMed:12665801, PubMed:17311996, PubMed:27743390). Inhibits platelet aggregation and activation by agonists such as ADP and collagen-related peptide (PubMed:12665801). This regulation of megakaryocate function as well as platelet production ann activation is done through the inhibition (via the 2 ITIM motifs) of the receptors CLEC1B and GP6:FcRgamma signaling (PubMed:17311996). Appears to operate in a calcium-independent manner (PubMed:12665801). {ECO:0000269|PubMed:12665801, ECO:0000269|PubMed:17311996, ECO:0000269|PubMed:27743390}.; FUNCTION: Isoform B, displayed in this entry, is the only isoform to contain both a transmembrane region and 2 immunoreceptor tyrosine-based inhibitor motifs (ITIMs) and, thus, the only one which probably has a role of inhibitory receptor. Isoform A may be the activating counterpart of isoform B. {ECO:0000305|PubMed:11544253}.
|
Homo sapiens (Human)
|
O95867
|
LY66C_HUMAN
|
MKALMLLTLSVLLCWVSADIRCHSCYKVPVLGCVDRQSCRLEPGQQCLTTHAYLGKMWVFSNLRCGTPEEPCQEAFNQTNRKLGLTYNTTCCNKDNCNSAGPRPTPALGLVFLTSLAGLGLWLLH
| null | null | null |
external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
|
identical protein binding [GO:0042802]
| null | null | null |
PTM: N-glycosylated. {ECO:0000269|PubMed:17008713}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17008713}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:17008713}.
| null | null | null | null | null | null |
Homo sapiens (Human)
|
O95868
|
LY66D_HUMAN
|
MKPQFVGILLSSLLGAALGNRMRCYNCGGSPSSSCKEAVTTCGEGRPQPGLEQIKLPGNPPVTLIHQHPACVAAHHCNQVETESVGDVTYPAHRDCYLGDLCNSAVASHVAPAGILAAAATALTCLLPGLWSG
| null | null |
acetylcholine receptor signaling pathway [GO:0095500]
|
external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; filopodium [GO:0030175]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; synapse [GO:0045202]
|
acetylcholine receptor inhibitor activity [GO:0030550]; identical protein binding [GO:0042802]
| null | null | null |
PTM: O-glycosylated. {ECO:0000269|PubMed:17008713}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17008713}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:17008713}. Cell projection, filopodium {ECO:0000269|PubMed:17008713}.
| null | null | null | null | null | null |
Homo sapiens (Human)
|
O95870
|
ABHGA_HUMAN
|
MAKLLSCVLGPRLYKIYRERDSERAPASVPETPTAVTAPHSSSWDTYYQPRALEKHADSILALASVFWSISYYSSPFAFFYLYRKGYLSLSKVVPFSHYAGTLLLLLAGVACLRGIGRWTNPQYRQFITILEATHRNQSSENKRQLANYNFDFRSWPVDFHWEEPSSRKESRGGPSRRGVALLRPEPLHRGTADTLLNRVKKLPCQITSYLVAHTLGRRMLYPGSVYLLQKALMPVLLQGQARLVEECNGRRAKLLACDGNEIDTMFVDRRGTAEPQGQKLVICCEGNAGFYEVGCVSTPLEAGYSVLGWNHPGFAGSTGVPFPQNEANAMDVVVQFAIHRLGFQPQDIIIYAWSIGGFTATWAAMSYPDVSAMILDASFDDLVPLALKVMPDSWRGLVTRTVRQHLNLNNAEQLCRYQGPVLLIRRTKDEIITTTVPEDIMSNRGNDLLLKLLQHRYPRVMAEEGLRVVRQWLEASSQLEEASIYSRWEVEEDWCLSVLRSYQAEHGPDFPWSVGEDMSADGRRQLALFLARKHLHNFEATHCTPLPAQNFQMPWHL
|
3.1.-.-; 3.1.1.23
| null |
monoacylglycerol catabolic process [GO:0052651]; phosphatidylserine catabolic process [GO:0006660]; prostaglandin catabolic process [GO:1905344]
|
endomembrane system [GO:0012505]; membrane [GO:0016020]
|
acylglycerol lipase activity [GO:0047372]; phospholipase activity [GO:0004620]
|
PF00561;
|
3.40.50.1820;
|
AB hydrolase superfamily, ABHD16 family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9Z1Q2}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=1-heptadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoserine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-heptadecanoyl-sn-glycero-3-phosphoserine + H(+); Xref=Rhea:RHEA:44500, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:84461, ChEBI:CHEBI:84462; Evidence={ECO:0000250|UniProtKB:Q9Z1Q2}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phospho-L-serine + H(+); Xref=Rhea:RHEA:41752, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:75020, ChEBI:CHEBI:75029; Evidence={ECO:0000250|UniProtKB:Q9Z1Q2}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoserine + H2O = (9Z,12Z)-octadecadienoate + 1-octadecanoyl-sn-glycero-3-phosphoserine + H(+); Xref=Rhea:RHEA:44516, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:84466, ChEBI:CHEBI:84467; Evidence={ECO:0000250|UniProtKB:Q9Z1Q2}; CATALYTIC ACTIVITY: Reaction=1-heptadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-heptadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:44520, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:74340, ChEBI:CHEBI:84470; Evidence={ECO:0000250|UniProtKB:Q9Z1Q2}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoglycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phosphoglycerol + H(+); Xref=Rhea:RHEA:44524, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:84472, ChEBI:CHEBI:84475; Evidence={ECO:0000250|UniProtKB:Q9Z1Q2}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + H(+); Xref=Rhea:RHEA:44528, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72833, ChEBI:CHEBI:72837; Evidence={ECO:0000250|UniProtKB:Q9Z1Q2}; CATALYTIC ACTIVITY: Reaction=1-heptadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-heptadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:44540, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:84489, ChEBI:CHEBI:84490; Evidence={ECO:0000250|UniProtKB:Q9Z1Q2}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72841, ChEBI:CHEBI:75158; Evidence={ECO:0000250|UniProtKB:Q9Z1Q2}; CATALYTIC ACTIVITY: Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.; EC=3.1.1.23; Evidence={ECO:0000269|PubMed:25290914}; CATALYTIC ACTIVITY: Reaction=1-tetradecanoylglycerol + H2O = glycerol + H(+) + tetradecanoate; Xref=Rhea:RHEA:44312, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30807, ChEBI:CHEBI:75562; Evidence={ECO:0000269|PubMed:25290914}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44313; Evidence={ECO:0000269|PubMed:25290914}; CATALYTIC ACTIVITY: Reaction=2-hexadecanoylglycerol + H2O = glycerol + H(+) + hexadecanoate; Xref=Rhea:RHEA:39963, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:75455; Evidence={ECO:0000269|PubMed:25290914}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39964; Evidence={ECO:0000269|PubMed:25290914}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:75342; Evidence={ECO:0000269|PubMed:25290914}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488; Evidence={ECO:0000269|PubMed:25290914}; CATALYTIC ACTIVITY: Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:73990; Evidence={ECO:0000269|PubMed:25290914}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492; Evidence={ECO:0000269|PubMed:25290914}; CATALYTIC ACTIVITY: Reaction=2-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-octadecadienoate + glycerol + H(+); Xref=Rhea:RHEA:44732, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30245, ChEBI:CHEBI:75457; Evidence={ECO:0000269|PubMed:25290914}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44733; Evidence={ECO:0000269|PubMed:25290914}; CATALYTIC ACTIVITY: Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+); Xref=Rhea:RHEA:44728, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:75612; Evidence={ECO:0000269|PubMed:25290914}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44729; Evidence={ECO:0000269|PubMed:25290914}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+); Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392; Evidence={ECO:0000269|PubMed:25290914}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133; Evidence={ECO:0000269|PubMed:25290914}; CATALYTIC ACTIVITY: Reaction=H2O + prostaglandin D2-1-glycerol ester = glycerol + H(+) + prostaglandin D2; Xref=Rhea:RHEA:45412, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:57406, ChEBI:CHEBI:85232; Evidence={ECO:0000269|PubMed:25290914}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45413; Evidence={ECO:0000269|PubMed:25290914}; CATALYTIC ACTIVITY: Reaction=2-glyceryl-15-deoxy-Delta(12,14)-prostaglandin J2 + H2O = 15-deoxy-Delta(12,14)-prostaglandin J2 + glycerol + H(+); Xref=Rhea:RHEA:45416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:85236, ChEBI:CHEBI:85238; Evidence={ECO:0000269|PubMed:25290914}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45417; Evidence={ECO:0000269|PubMed:25290914}; CATALYTIC ACTIVITY: Reaction=1-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-octadecadienoate + glycerol + H(+); Xref=Rhea:RHEA:48428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30245, ChEBI:CHEBI:75568; Evidence={ECO:0000269|PubMed:25290914}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48429; Evidence={ECO:0000269|PubMed:25290914};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.9 uM for 1-(9Z,12Z-octadecadienoyl)-glycerol (1-LG) (in absence of BSA) {ECO:0000269|PubMed:25290914}; KM=137.8 uM for 1-(9Z,12Z-octadecadienoyl)-glycerol (1-LG) (in presence of BSA) {ECO:0000269|PubMed:25290914}; KM=20.9 uM for 2-glyceryl-15-deoxy-Delta(12,14)-prostaglandin J2 (15d-PGJ(2)-G) (in presence of BSA) {ECO:0000269|PubMed:25290914}; Vmax=7.3 nmol/min/mg enzyme with 1-(9Z,12Z-octadecadienoyl)-glycerol (1-LG) as substrate (in absence of BSA) {ECO:0000269|PubMed:25290914}; Vmax=13.2 nmol/min/mg enzyme with 1-(9Z,12Z-octadecadienoyl)-glycerol (1-LG) as substrate (in presence of BSA) {ECO:0000269|PubMed:25290914};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2-8.0. {ECO:0000269|PubMed:25290914};
| null |
FUNCTION: Phosphatidylserine (PS) lipase that mediates the hydrolysis of phosphatidylserine to generate lysophosphatidylserine (LPS) (By similarity). LPS constitutes a class of signaling lipids that regulates immunological and neurological processes (By similarity). Has no activity towards diacylglycerol, triacylglycerol or lysophosphatidylserine lipase (PubMed:25290914). Also has monoacylglycerol lipase activity, with preference for 1-(9Z,12Z-octadecadienoyl)-glycerol (1-LG) and 2-glyceryl-15-deoxy-Delta(12,14)-prostaglandin J2 (15d-PGJ(2)-G) (PubMed:25290914). {ECO:0000250|UniProtKB:Q9Z1Q2, ECO:0000269|PubMed:25290914}.
|
Homo sapiens (Human)
|
O95872
|
GPAN1_HUMAN
|
MSRPLLITFTPATDPSDLWKDGQQQPQPEKPESTLDGAAARAFYEALIGDESSAPDSQRSQTEPARERKRKKRRIMKAPAAEAVAEGASGRHGQGRSLEAEDKMTHRILRAAQEGDLPELRRLLEPHEAGGAGGNINARDAFWWTPLMCAARAGQGAAVSYLLGRGAAWVGVCELSGRDAAQLAEEAGFPEVARMVRESHGETRSPENRSPTPSLQYCENCDTHFQDSNHRTSTAHLLSLSQGPQPPNLPLGVPISSPGFKLLLRGGWEPGMGLGPRGEGRANPIPTVLKRDQEGLGYRSAPQPRVTHFPAWDTRAVAGRERPPRVATLSWREERRREEKDRAWERDLRTYMNLEF
| null | null | null | null |
nucleic acid binding [GO:0003676]
|
PF13637;PF01585;
|
1.25.40.20;
| null | null | null | null | null | null | null | null | null |
Homo sapiens (Human)
|
O95876
|
FRITZ_HUMAN
|
MRREFCWDAYSKAAGSRASSPLPRQDRDSFCHQMSFCLTELHLWSLKNTLHIADRDIGIYQYYDKKDPPATEHGNLEKKQKLAESRDYPWTLKNRRPEKLRDSLKELEELMQNSRCVLSKWKNKYVCQLLFGSGVLVSLSLSGPQLEKVVIDRSLVGKLISDTISDALLTDSFIILSFLAQNKLCFIQFTKKMESSDVNKRLEKLSALDYKIFYYEIPGPINKTTERHLAINCVHDRVVCWWPLVNDDAWPWAPISSEKDRANLLLLGYAQGRLEVLSSVRTEWDPLDVRFGTKQPYQVFTVEHSVSVDKEPMADSCIYECIRNKIQCVSVTRIPLKSKAISCCRNVTEDKLILGCEDSSLILYETHRRVTLLAQTELLPSLISCHPSGAILLVGSNQGELQIFDMALSPINIQLLAEDRLPRETLQFSKLFDASSSLVQMQWIAPQVVSQKGEGSDIYDLLFLRFERGPLGVLLFKLGVFTRGQLGLIDIIFQYIHCDEIYEAINILSSMNWDTLGHQCFISMSAIVNHLLRQKLTPEREAQLETSLGTFYAPTRPLLDSTILEYRDQISKYARRFFHHLLRYQRFEKAFLLAVDVGARDLFMDIHYLALDKGELALAEVARKRASDIDAESITSGVELLGPLDRGDMLNEAFIGLSLAPQGEDSFPDNLPPSCPTHRHILQQRILNGSSNRQIIDRRNELEKDICSGFLMTNTCNAEDGELREDGREQEIRDGGSLKMIHFGLV
| null | null |
auditory receptor cell morphogenesis [GO:0002093]; camera-type eye development [GO:0043010]; cilium assembly [GO:0060271]; cilium organization [GO:0044782]; circulatory system development [GO:0072359]; digestive system development [GO:0055123]; embryonic digit morphogenesis [GO:0042733]; establishment of planar polarity [GO:0001736]; establishment of protein localization [GO:0045184]; intraciliary transport [GO:0042073]; kidney development [GO:0001822]; nervous system development [GO:0007399]; neural tube development [GO:0021915]; podocyte cell migration [GO:0090521]; regulation of cilium assembly [GO:1902017]; regulation of embryonic cell shape [GO:0016476]; regulation of establishment of cell polarity [GO:2000114]; regulation of fibroblast migration [GO:0010762]; regulation of focal adhesion assembly [GO:0051893]; regulation of protein localization [GO:0032880]; regulation of ruffle assembly [GO:1900027]; respiratory system development [GO:0060541]; roof of mouth development [GO:0060021]; septin cytoskeleton organization [GO:0032185]; smoothened signaling pathway [GO:0007224]; tongue morphogenesis [GO:0043587]
|
axonemal basal plate [GO:0097541]; axoneme [GO:0005930]; cilium [GO:0005929]; plasma membrane [GO:0005886]
| null |
PF11768;
|
2.130.10.10;
|
WD repeat fritz family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q32NR9}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q32NR9}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q32NR9}.
| null | null | null | null | null |
FUNCTION: Probable effector of the planar cell polarity signaling pathway which regulates the septin cytoskeleton in both ciliogenesis and collective cell movements. Together with FUZ and WDPCP proposed to function as core component of the CPLANE (ciliogenesis and planar polarity effectors) complex involved in the recruitment of peripheral IFT-A proteins to basal bodies (By similarity). {ECO:0000250|UniProtKB:Q32NR9, ECO:0000250|UniProtKB:Q8C456}.
|
Homo sapiens (Human)
|
O95881
|
TXD12_HUMAN
|
METRPRLGATCLLGFSFLLLVISSDGHNGLGKGFGDHIHWRTLEDGKKEAAASGLPLMVIIHKSWCGACKALKPKFAESTEISELSHNFVMVNLEDEEEPKDEDFSPDGGYIPRILFLDPSGKVHPEIINENGNPSYKYFYVSAEQVVQGMKEAQERLTGDAFRKKHLEDEL
|
1.8.4.2
| null |
negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902236]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]
|
protein-disulfide reductase (glutathione) activity [GO:0019153]; protein-disulfide reductase activity [GO:0015035]
|
PF13899;
|
3.40.30.10;
| null | null |
SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:12761212}.
|
CATALYTIC ACTIVITY: Reaction=[protein]-disulfide + 2 glutathione = [protein]-dithiol + glutathione disulfide; Xref=Rhea:RHEA:21064, Rhea:RHEA-COMP:10593, Rhea:RHEA-COMP:10594, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.8.4.2; Evidence={ECO:0000269|PubMed:12761212}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21066; Evidence={ECO:0000305|PubMed:12761212};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=25 uM for Asn-Arg-Cys-Ser-Gln-Gly-Ser-Cys-Trp-Asn {ECO:0000269|PubMed:12761212};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:12761212};
| null |
FUNCTION: Protein-disulfide reductase of the endoplasmic reticulum that promotes disulfide bond formation in client proteins through its thiol-disulfide oxidase activity. {ECO:0000269|PubMed:12761212}.
|
Homo sapiens (Human)
|
O95886
|
DLGP3_HUMAN
|
MRGYHGDRGSHPRPARFADQQHMDVGPAARAPYLLGSREAFSTEPRFCAPRAGLGHISPEGPLSLSEGPSVGPEGGPAGAGVGGGSSTFPRMYPGQGPFDTCEDCVGHPQGKGAPRLPPTLLDQFEKQLPVQQDGFHTLPYQRGPAGAGPGPAPGTGTAPEPRSESPSRIRHLVHSVQKLFAKSHSLEAPGKRDYNGPKAEGRGGSGGDSYPGPGSGGPHTSHHHHHHHHHHHHQSRHGKRSKSKDRKGDGRHQAKSTGWWSSDDNLDSDSGFLAGGRPPGEPGGPFCLEGPDGSYRDLSFKGRSGGSEGRCLACTGMSMSLDGQSVKRSAWHTMMVSQGRDGYPGAGPGKGLLGPETKAKARTYHYLQVPQDDWGGYPTGGKDGEIPCRRMRSGSYIKAMGDEESGDSDGSPKTSPKAVARRFTTRRSSSVDQARINCCVPPRIHPRSSIPGYSRSLTTGQLSDELNQQLEAVCGSVFGELESQAVDALDLPGCFRMRSHSYLRAIQAGCSQDDDCLPLLATPAAVSGRPGSSFNFRKAPPPIPPGSQAPPRISITAQSSTDSAHESFTAAEGPARRCSSADGLDGPAMGARTLELAPVPPRASPKPPTLIIKTIPGREELRSLARQRKWRPSIGVQVETISDSDTENRSRREFHSIGVQVEEDKRRARFKRSNSVTAGVQADLELEGLAGLATVATEDKALQFGRSFQRHASEPQPGPRAPTYSVFRTVHTQGQWAYREGYPLPYEPPATDGSPGPAPAPTPGPGAGRRDSWIERGSRSLPDSGRASPCPRDGEWFIKMLRAEVEKLEHWCQQMEREAEDYELPEEILEKIRSAVGSTQLLLSQKVQQFFRLCQQSMDPTAFPVPTFQDLAGFWDLLQLSIEDVTLKFLELQQLKANSWKLLEPKEEKKVPPPIPKKPLRGRGVPVKERSLDSVDRQRQEARKRLLAAKRAASFRHSSATESADSIEIYIPEAQTRL
| null | null |
modification of synaptic structure [GO:0099563]; modulation of chemical synaptic transmission [GO:0050804]; signaling [GO:0023052]
|
cholinergic synapse [GO:0098981]; glutamatergic synapse [GO:0098978]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic specialization [GO:0099572]
|
amyloid-beta binding [GO:0001540]; molecular adaptor activity [GO:0060090]
|
PF03359;
| null |
SAPAP family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Postsynaptic density {ECO:0000250}. Synapse {ECO:0000250}. Note=Postsynaptic density of neuronal cells. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May play a role in the molecular organization of synapses and neuronal cell signaling. Could be an adapter protein linking ion channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-95/SAP90 at the plasma membrane.
|
Homo sapiens (Human)
|
O95897
|
NOE2_HUMAN
|
MWPLTVPPPLLLLLCSGLAGQTLFQNPEEGWQLYTSAQAPDGKCICTAVIPAQSTCSRDGRSRELRQLMEKVQNVSQSMEVLELRTYRDLQYVRGMETLMRSLDARLRAADGSLSAKSFQELKDRMTELLPLSSVLEQYKADTRTIVRLREEVRNLSGSLAAIQEEMGAYGYEDLQQRVMALEARLHACAQKLGCGKLTGVSNPITVRAMGSRFGSWMTDTMAPSADSRVWYMDGYYKGRRVLEFRTLGDFIKGQNFIQHLLPQPWAGTGHVVYNGSLFYNKYQSNVVVKYHFRSRSVLVQRSLPGAGYNNTFPYSWGGFSDMDFMVDESGLWAVYTTNQNAGNIVVSRLDPHTLEVMRSWDTGYPKRSAGEAFMICGVLYVTNSHLAGAKVYFAYFTNTSSYEYTDVPFHNQYSHISMLDYNPRERALYTWNNGHQVLYNVTLFHVISTSGDP
| null | null |
positive regulation of smooth muscle cell differentiation [GO:0051152]; protein secretion [GO:0009306]; regulation of vascular associated smooth muscle cell dedifferentiation [GO:1905174]; signal transduction [GO:0007165]
|
AMPA glutamate receptor complex [GO:0032281]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; synapse [GO:0045202]
| null |
PF12308;PF02191;
| null | null |
PTM: N-glycosylated. {ECO:0000269|PubMed:21228389}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21228389}. Synapse {ECO:0000250|UniProtKB:Q8BM13}. Membrane {ECO:0000250|UniProtKB:Q8BM13}. Nucleus {ECO:0000269|PubMed:25298399}. Cytoplasm {ECO:0000269|PubMed:25298399}. Note=Nuclear localization is induced by TGF-beta. {ECO:0000269|PubMed:25298399}.
| null | null | null | null | null |
FUNCTION: Involved in transforming growth factor beta (TGF-beta)-induced smooth muscle differentiation. TGF-beta induces expression and translocation of OLFM2 to the nucleus where it binds to SRF, causing its dissociation from the transcriptional repressor HEY2/HERP1 and facilitating binding of SRF to target genes (PubMed:25298399). Plays a role in AMPAR complex organization (By similarity). Is a regulator of vascular smooth-muscle cell (SMC) phenotypic switching, that acts by promoting RUNX2 and inhibiting MYOCD binding to SRF. SMC phenotypic switching is the process through which vascular SMCs undergo transition between a quiescent contractile phenotype and a proliferative synthetic phenotype in response to pathological stimuli. SMC phenotypic plasticity is essential for vascular development and remodeling (By similarity). {ECO:0000250|UniProtKB:Q568Y7, ECO:0000250|UniProtKB:Q8BM13, ECO:0000269|PubMed:25298399}.
|
Homo sapiens (Human)
|
O95900
|
TRUB2_HUMAN
|
MGSAGLSRLHGLFAVYKPPGLKWKHLRDTVELQLLKGLNARKPPAPKQRVRFLLGPMEGSEEKELTLTATSVPSFINHPLVCGPAFAHLKVGVGHRLDAQASGVLVLGVGHGCRLLTDMYNAHLTKDYTVRGLLGKATDDFREDGRLVEKTTYDHVTREKLDRILAVIQGSHQKALVMYSNLDLKTQEAYEMAVRGLIRPMNKSPMLITGIRCLYFAPPEFLLEVQCMHETQKELRKLVHEIGLELKTTAVCTQVRRTRDGFFTLDSALLRTQWDLTNIQDAIRAATPQVAAELEKSLSPGLDTKQLPSPGWSWDSQGPSSTLGLERGAGQ
|
5.4.99.-; 5.4.99.25
| null |
mRNA processing [GO:0006397]; mRNA pseudouridine synthesis [GO:1990481]; positive regulation of mitochondrial translation [GO:0070131]; tRNA processing [GO:0008033]
|
mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; ribonucleoprotein granule [GO:0035770]
|
pseudouridine synthase activity [GO:0009982]; RNA binding [GO:0003723]
|
PF01509;
|
3.30.2350.10;
|
Pseudouridine synthase TruB family
| null |
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:27974379, ECO:0000269|PubMed:33023933}. Note=Localizes to mitochondrial RNA granules, platforms for post-transcriptional RNA modification and ribosome assembly. {ECO:0000269|PubMed:27974379, ECO:0000269|PubMed:28082677}.
|
CATALYTIC ACTIVITY: Reaction=a uridine in mRNA = a pseudouridine in mRNA; Xref=Rhea:RHEA:56644, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:14659, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; Evidence={ECO:0000269|PubMed:31477916, ECO:0000305|PubMed:27974379}; CATALYTIC ACTIVITY: Reaction=uridine(55) in tRNA = pseudouridine(55) in tRNA; Xref=Rhea:RHEA:42532, Rhea:RHEA-COMP:10101, Rhea:RHEA-COMP:10102, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.25; Evidence={ECO:0000269|PubMed:33023933}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42533; Evidence={ECO:0000269|PubMed:33023933};
| null | null | null | null |
FUNCTION: Minor enzyme contributing to the isomerization of uridine to pseudouridine (pseudouridylation) of specific mitochondrial mRNAs (mt-mRNAs) such as COXI and COXIII mt-mRNAs (PubMed:27974379, PubMed:31477916). As a component of a functional protein-RNA module, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mitochondrial ribosomal RNA (16S mt-rRNA), controls 16S mt-rRNA abundance and is required for intra-mitochondrial translation (PubMed:27667664). Also catalyzes pseudouridylation of some tRNAs, including synthesis of pseudouridine(55) from uracil-55, in the psi GC loop of a subset of tRNAs (PubMed:33023933). {ECO:0000269|PubMed:27667664, ECO:0000269|PubMed:27974379, ECO:0000269|PubMed:31477916, ECO:0000269|PubMed:33023933}.
|
Homo sapiens (Human)
|
O95905
|
ECD_HUMAN
|
MEETMKLATMEDTVEYCLFLIPDESRDSDKHKEILQKYIERIITRFAPMLVPYIWQNQPFNLKYKPGKGGVPAHMFGVTKFGDNIEDEWFIVYVIKQITKEFPELVARIEDNDGEFLLIEAADFLPKWLDPENSTNRVFFCHGELCIIPAPRKSGAESWLPTTPPTIPQALNIITAHSEKILASESIRAAVNRRIRGYPEKIQASLHRAHCFLPAGIVAVLKQRPRLVAAAVQAFYLRDPIDLRACRVFKTFLPETRIMTSVTFTKCLYAQLVQQRFVPDRRSGYRLPPPSDPQYRAHELGMKLAHGFEILCSKCSPHFSDCKKSLVTASPLWASFLESLKKNDYFKGLIEGSAQYRERLEMAENYFQLSVDWPESSLAMSPGEEILTLLQTIPFDIEDLKKEAANLPPEDDDQWLDLSPDQLDQLLQEAVGKKESESVSKEEKEQNYDLTEVSESMKAFISKVSTHKGAELPREPSEAPITFDADSFLNYFDKILGPRPNESDSDDLDDEDFECLDSDDDLDFETHEPGEEASLKGTLDNLKSYMAQMDQELAHTCISKSFTTRNQVEPVSQTTDNNSDEEDSGTGESVMAPVDVDLNLVSNILESYSSQAGLAGPASNLLQSMGVQLPDNTDHRPTSKPTKN
| null | null |
fibroblast proliferation [GO:0048144]; mRNA processing [GO:0006397]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of G1/S transition of mitotic cell cycle [GO:2000045]; RNA splicing [GO:0008380]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
histone acetyltransferase binding [GO:0035035]
|
PF07093;
| null |
ECD family
|
PTM: Phosphorylated predominantly by CK2 on two serine-containing clusters; involved in cell cycle regulation activity. {ECO:0000269|PubMed:26711270}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16849563, ECO:0000269|PubMed:19919181, ECO:0000269|PubMed:26711270}. Nucleus {ECO:0000269|PubMed:16849563, ECO:0000269|PubMed:19919181, ECO:0000269|PubMed:26711270}. Note=Predominantly is located in the cytoplasm. {ECO:0000269|PubMed:16849563, ECO:0000269|PubMed:19919181, ECO:0000269|PubMed:26711270}.
| null | null | null | null | null |
FUNCTION: Regulator of p53/TP53 stability and function. Inhibits MDM2-mediated degradation of p53/TP53 possibly by cooperating in part with TXNIP (PubMed:16849563, PubMed:23880345). May be involved transcriptional regulation. In vitro has intrinsic transactivation activity enhanced by EP300. May be a transcriptional activator required for the expression of glycolytic genes (PubMed:19919181, PubMed:9928932). Involved in regulation of cell cycle progression. Proposed to disrupt Rb-E2F binding leading to transcriptional activation of E2F proteins (PubMed:19640839). The cell cycle -regulating function may depend on its RUVBL1-mediated association with the R2TP complex (PubMed:26711270). May play a role in regulation of pre-mRNA splicing (PubMed:24722212). {ECO:0000269|PubMed:16849563, ECO:0000269|PubMed:19640839, ECO:0000269|PubMed:19919181, ECO:0000269|PubMed:23880345, ECO:0000269|PubMed:26711270, ECO:0000305|PubMed:24722212, ECO:0000305|PubMed:9928932}.
|
Homo sapiens (Human)
|
O95907
|
MOT3_HUMAN
|
MGAGGPRRGEGPPDGGWGWVVLGACFVVTGFAYGFPKAVSVFFRALMRDFDAGYSDTAWVSSIMLAMLYGTGPVSSILVTRFGCRPVMLAGGLLASAGMILASFATRLLELYLTAGVLTGLGLALNFQPSLIMLGLYFERRRPLANGLAAAGSPVFLSALSPLGQQLLERFGWRGGFLLLGGLLLHCCACGAVMRPPPGPGPRPRRDSAGDRAGDAPGEAEADGAGLQLREASPRVRPRRRLLDLAVCTDRAFAVYAVTKFLMALGLFVPAILLVNYAKDAGVPDTDAAFLLSIVGFVDIVARPACGALAGLARLRPHVPYLFSLALLANGLTDLSSARARSYGALVAFCVAFGLSYGMVGALQFEVLMAAVGAPRFPSALGLVLLVEAAAVLIGPPSAGRLVDVLKNYEIIFYLAGSEVALAGVFMAVATNCCLRCAKAAPSGPGTEGGASDTEDAEAEGDSEPLPVVAEEPGNLEALEVLSARGEPTEPEIEARPRLAAESV
| null | null |
lactate transport [GO:0015727]; monocarboxylic acid transport [GO:0015718]
|
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
lactate transmembrane transporter activity [GO:0015129]; monocarboxylic acid transmembrane transporter activity [GO:0008028]; symporter activity [GO:0015293]
|
PF07690;
|
1.20.1250.20;
|
Major facilitator superfamily, Monocarboxylate porter (TC 2.A.1.13) family
| null |
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:21199217}; Multi-pass membrane protein {ECO:0000255}. Note=Basolateral sorting signals (BLSS) in C-terminal cytoplasmic tail ensure its basolateral expression (PubMed:21199217). Colocalizes with BSG in basolateral cell membrane of the retinal pigment epithelium (By similarity). {ECO:0000250|UniProtKB:O35308, ECO:0000269|PubMed:21199217}.
|
CATALYTIC ACTIVITY: Reaction=(S)-lactate(in) + H(+)(in) = (S)-lactate(out) + H(+)(out); Xref=Rhea:RHEA:29415, ChEBI:CHEBI:15378, ChEBI:CHEBI:16651; Evidence={ECO:0000250|UniProtKB:Q90632};
| null | null | null | null |
FUNCTION: Probable retinal pigment epithelium (RPE)-specific proton-coupled L-lactate transporter (By similarity). May facilitate transport of lactate and H(+) out of the retina and could therefore play a role in pH and ion homeostasis of the outer retina (By similarity). {ECO:0000250|UniProtKB:O35308, ECO:0000250|UniProtKB:Q90632}.
|
Homo sapiens (Human)
|
O95922
|
TTLL1_HUMAN
|
MAGKVKWVTDIEKSVLINNFEKRGWVQVTENEDWNFYWMSVQTIRNVFSVEAGYRLSDDQIVNHFPNHYELTRKDLMVKNIKRYRKELEKEGSPLAEKDENGKYLYLDFVPVTYMLPADYNLFVEEFRKSPSSTWIMKPCGKAQGKGIFLINKLSQIKKWSRDSKTSSFVSQSNKEAYVISLYINNPLLIGGRKFDLRLYVLVSTYRPLRCYMYKLGFCRFCTVKYTPSTSELDNMFVHLTNVAIQKHGEDYNHIHGGKWTVSNLRLYLESTRGKEVTSKLFDEIHWIIVQSLKAVAPVMNNDKHCFECYGYDIIIDDKLKPWLIEVNASPSLTSSTANDRILKYNLINDTLNIAVPNGEIPDCKWNKSPPKEVLGNYEILYDEELAQGDGADRELRSRQGQSLGPRAGRSRDSGRAVLTTWK
|
6.3.2.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A4Q9E8};
|
cerebellar Purkinje cell differentiation [GO:0021702]; immune response in nasopharyngeal-associated lymphoid tissue [GO:0002395]; microtubule cytoskeleton organization [GO:0000226]; mucociliary clearance [GO:0120197]; protein polyglutamylation [GO:0018095]; regulation of blastocyst development [GO:0120222]; sperm axoneme assembly [GO:0007288]
|
ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; microtubule [GO:0005874]; motile cilium [GO:0031514]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; tubulin binding [GO:0015631]; tubulin-glutamic acid ligase activity [GO:0070740]
|
PF03133;
|
3.30.470.20;
|
Tubulin polyglutamylase family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q91V51}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q91V51}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q91V51}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q91V51}.
|
CATALYTIC ACTIVITY: Reaction=(L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + ATP + L-glutamate = (L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60148, Rhea:RHEA-COMP:15519, Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143623, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q91V51}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60149; Evidence={ECO:0000250|UniProtKB:Q91V51};
| null | null | null | null |
FUNCTION: Catalytic subunit of a polyglutamylase complex which modifies tubulin, generating side chains of glutamate on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin (PubMed:34782749). Probably involved in the side-chain elongation step of the polyglutamylation reaction rather than the initiation step. Modifies both alpha- and beta-tubulins with a preference for the alpha-tail. Unlike most polyglutamylases of the tubulin--tyrosine ligase family, only displays a catalytic activity when in complex with other proteins as it is most likely lacking domains important for autonomous activity. Part of the neuronal tubulin polyglutamylase complex. Mediates cilia and flagella polyglutamylation which is essential for their biogenesis and motility. Involved in respiratory motile cilia function through the regulation of beating asymmetry. Essential for sperm flagella biogenesis, motility and male fertility. Involved in KLF4 glutamylation which impedes its ubiquitination, thereby leading to somatic cell reprogramming, pluripotency maintenance and embryogenesis. {ECO:0000250|UniProtKB:Q91V51, ECO:0000269|PubMed:34782749}.
|
Homo sapiens (Human)
|
O95925
|
EPPI_HUMAN
|
MGSSGLLSLLVLFVLLANVQGPGLTDWLFPRRCPKIREECEFQERDVCTKDRQCQDNKKCCVFSCGKKCLDLKQDVCEMPKETGPCLAYFLHWWYDKKDNTCSMFVYGGCQGNNNNFQSKANCLNTCKNKRFP
| null | null |
defense response to bacterium [GO:0042742]; negative regulation of calcium ion import [GO:0090281]; negative regulation of flagellated sperm motility [GO:1901318]; negative regulation of peptidase activity [GO:0010466]
|
acrosomal vesicle [GO:0001669]; cell surface [GO:0009986]; extracellular space [GO:0005615]; protein-containing complex [GO:0032991]; sperm plasma membrane [GO:0097524]
|
serine-type endopeptidase inhibitor activity [GO:0004867]
|
PF00014;PF00095;
|
4.10.75.10;4.10.410.10;
| null | null |
SUBCELLULAR LOCATION: [Isoform 1]: Secreted. Cell surface. Note=Bound to the surface of testicular and on the head and tail of ejaculate spermatozoa.
| null | null | null | null | null |
FUNCTION: Serine protease inhibitor that plays an essential role in male reproduction and fertility. Modulates the hydrolysis of SEMG1 by KLK3/PSA (a serine protease), provides antimicrobial protection for spermatozoa in the ejaculate coagulum, and binds SEMG1 thereby inhibiting sperm motility. {ECO:0000269|PubMed:15229136, ECO:0000269|PubMed:17644992}.
|
Homo sapiens (Human)
|
O95926
|
SYF2_HUMAN
|
MAAIAASEVLVDSAEEGSLAAAAELAAQKREQRLRKFRELHLMRNEARKLNHQEVVEEDKRLKLPANWEAKKARLEWELKEEEKKKECAARGEDYEKVKLLEISAEDAERWERKKKRKNPDLGFSDYAAAQLRQYHRLTKQIKPDMETYERLREKHGEEFFPTSNSLLHGTHVPSTEEIDRMVIDLEKQIEKRDKYSRRRPYNDDADIDYINERNAKFNKKAERFYGKYTAEIKQNLERGTAV
| null | null |
embryonic organ development [GO:0048568]; gastrulation [GO:0007369]; in utero embryonic development [GO:0001701]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; mRNA splicing, via spliceosome [GO:0000398]; positive regulation of cell population proliferation [GO:0008284]
|
catalytic step 2 spliceosome [GO:0071013]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; post-mRNA release spliceosomal complex [GO:0071014]; Prp19 complex [GO:0000974]; U2-type catalytic step 2 spliceosome [GO:0071007]
|
RNA binding [GO:0003723]
|
PF08231;
| null |
SYF2 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11118353, ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}.
| null | null | null | null | null |
FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:28076346, PubMed:28502770). {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}.
|
Homo sapiens (Human)
|
O95931
|
CBX7_HUMAN
|
MELSAIGEQVFAVESIRKKRVRKGKVEYLVKWKGWPPKYSTWEPEEHILDPRLVMAYEEKEERDRASGYRKRGPKPKRLLLQRLYSMDLRSSHKAKGKEKLCFSLTCPLGSGSPEGVVKAGAPELVDKGPLVPTLPFPLRKPRKAHKYLRLSRKKFPPRGPNLESHSHRRELFLQEPPAPDVLQAAGEWEPAAQPPEEEADADLAEGPPPWTPALPSSEVTVTDITANSITVTFREAQAAEGFFRDRSGKF
| null | null |
chromatin organization [GO:0006325]; negative regulation of transcription by RNA polymerase II [GO:0000122]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PcG protein complex [GO:0031519]; PRC1 complex [GO:0035102]
| null |
PF17218;PF00385;
|
2.40.50.40;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14647293, ECO:0000269|PubMed:21060834, ECO:0000269|PubMed:21282530}.
| null | null | null | null | null |
FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Promotes histone H3 trimethylation at 'Lys-9' (H3K9me3). Binds to trimethylated lysine residues in histones, and possibly also other proteins. Regulator of cellular lifespan by maintaining the repression of CDKN2A, but not by inducing telomerase activity. {ECO:0000269|PubMed:19636380, ECO:0000269|PubMed:21047797, ECO:0000269|PubMed:21060834, ECO:0000269|PubMed:21282530}.
|
Homo sapiens (Human)
|
O95932
|
TGM3L_HUMAN
|
MAGIRVTKVDWQRSRNGAAHHTQEYPCPELVVRRGQSFSLTLELSRALDCEEILIFTMETGPRASEALHTKAVFQTSELERGEGWTAAREAQMEKTLTVSLASPPSAVIGRYLLSIRLSSHRKHSNRRLGEFVLLFNPWCAEDDVFLASEEERQEYVLSDSGIIFRGVEKHIRAQGWNYGQFEEDILNICLSILDRSPGHQNNPATDVSCRHNPIYVTRVISAMVNSNNDRGVVQGQWQGKYGGGTSPLHWRGSVAILQKWLKGRYKPVKYGQCWVFAGVLCTVLRCLGIATRVVSNFNSAHDTDQNLSVDKYVDSFGRTLEDLTEDSMWNFHVWNESWFARQDLGPSYNGWQVLDATPQEESEGVFRCGPASVTAIREGDVHLAHDGPFVFAEVNADYITWLWHEDESRERVYSNTKKIGRCISTKAVGSDSRVDITDLYKYPEGSRKERQVYSKAVNRLFGVEASGRRIWIRRAGGRCLWRDDLLEPATKPSIAGKFKVLEPPMLGHDLRLALCLANLTSRAQRVRVNLSGATILYTRKPVAEILHESHAVRLGPQEEKRIPITISYSKYKEDLTEDKKILLAAMCLVTKGEKLLVEKDITLEDFITIKVLGPAMVGVAVTVEVTVVNPLIERVKDCALMVEGSGLLQEQLSIDVPTLEPQERASVQFDITPSKSGPRQLQVDLVSPHFPDIKGFVIVHVATAK
|
2.3.2.13
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds up to 3 Ca(2+) cations per subunit. {ECO:0000250};
| null |
cytoplasm [GO:0005737]
|
metal ion binding [GO:0046872]; protein-glutamine gamma-glutamyltransferase activity [GO:0003810]
|
PF00927;PF01841;PF00868;
|
2.60.40.10;3.90.260.10;
|
Transglutaminase superfamily, Transglutaminase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23206699, ECO:0000269|PubMed:25253745, ECO:0000269|PubMed:29053796}.
|
CATALYTIC ACTIVITY: Reaction=L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:54816, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14005, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:30011, ChEBI:CHEBI:138370; EC=2.3.2.13; Evidence={ECO:0000255|PROSITE-ProRule:PRU10024};
| null | null | null | null |
FUNCTION: Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. {ECO:0000250}.
|
Homo sapiens (Human)
|
O95935
|
TBX18_HUMAN
|
MAEKRRGSPCSMLSLKAHAFSVEALIGAEKQQQLQKKRRKLGAEEAAGAVDDGGCSRGGGAGEKGSSEGDEGAALPPPAGATSGPARSGADLERGAAGGCEDGFQQGASPLASPGGSPKGSPARSLARPGTPLPSPQAPRVDLQGAELWKRFHEIGTEMIITKAGRRMFPAMRVKISGLDPHQQYYIAMDIVPVDNKRYRYVYHSSKWMVAGNADSPVPPRVYIHPDSPASGETWMRQVISFDKLKLTNNELDDQGHIILHSMHKYQPRVHVIRKDCGDDLSPIKPVPSGEGVKAFSFPETVFTTVTAYQNQQITRLKIDRNPFAKGFRDSGRNRMGLEALVESYAFWRPSLRTLTFEDIPGIPKQGNASSSTLLQGTGNGVPATHPHLLSGSSCSSPAFHLGPNTSQLCSLAPADYSACARSGLTLNRYSTSLAETYNRLTNQAGETFAPPRTPSYVGVSSSTSVNMSMGGTDGDTFSCPQTSLSMQISGMSPQLQYIMPSPSSNAFATNQTHQGSYNTFRLHSPCALYGYNFSTSPKLAASPEKIVSSQGSFLGSSPSGTMTDRQMLPPVEGVHLLSSGGQQSFFDSRTLGSLTLSSSQVSAHMV
| null | null |
cell fate specification [GO:0001708]; cochlea morphogenesis [GO:0090103]; morphogenesis of embryonic epithelium [GO:0016331]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neural plate anterior/posterior regionalization [GO:0021999]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of SA node cell action potential [GO:0098907]; regulation of transcription by RNA polymerase II [GO:0006357]; sinoatrial node cell development [GO:0060931]; sinoatrial node cell fate commitment [GO:0060930]; sinoatrial node development [GO:0003163]; smooth muscle cell differentiation [GO:0051145]; somitogenesis [GO:0001756]; ureter development [GO:0072189]
|
chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription repressor complex [GO:0090571]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00907;
|
2.60.40.820;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201, ECO:0000269|PubMed:26235987}.
| null | null | null | null | null |
FUNCTION: Acts as a transcriptional repressor involved in developmental processes of a variety of tissues and organs, including the heart and coronary vessels, the ureter and the vertebral column. Required for embryonic development of the sino atrial node (SAN) head area. {ECO:0000250|UniProtKB:Q9EPZ6, ECO:0000269|PubMed:26235987}.
|
Homo sapiens (Human)
|
O95936
|
EOMES_HUMAN
|
MQLGEQLLVSSVNLPGAHFYPLESARGGSGGSAGHLPSAAPSPQKLDLDKASKKFSGSLSCEAVSGEPAAASAGAPAAMLSDTDAGDAFASAAAVAKPGPPDGRKGSPCGEEELPSAAAAAAAAAAAAAATARYSMDSLSSERYYLQSPGPQGSELAAPCSLFPYQAAAGAPHGPVYPAPNGARYPYGSMLPPGGFPAAVCPPGRAQFGPGAGAGSGAGGSSGGGGGPGTYQYSQGAPLYGPYPGAAAAGSCGGLGGLGVPGSGFRAHVYLCNRPLWLKFHRHQTEMIITKQGRRMFPFLSFNINGLNPTAHYNVFVEVVLADPNHWRFQGGKWVTCGKADNNMQGNKMYVHPESPNTGSHWMRQEISFGKLKLTNNKGANNNNTQMIVLQSLHKYQPRLHIVEVTEDGVEDLNEPSKTQTFTFSETQFIAVTAYQNTDITQLKIDHNPFAKGFRDNYDSSHQIVPGGRYGVQSFFPEPFVNTLPQARYYNGERTVPQTNGLLSPQQSEEVANPPQRWLVTPVQQPGTNKLDISSYESEYTSSTLLPYGIKSLPLQTSHALGYYPDPTFPAMAGWGGRGSYQRKMAAGLPWTSRTSPTVFSEDQLSKEKVKEEIGSSWIETPPSIKSLDSNDSGVYTSACKRRRLSPSNSSNENSPSIKCEDINAEEYSKDTSKGMGGYYAFYTTP
| null | null |
adaptive immune response [GO:0002250]; astrocyte differentiation [GO:0048708]; brain development [GO:0007420]; cardioblast differentiation [GO:0010002]; CD8-positive, alpha-beta T cell differentiation involved in immune response [GO:0002302]; cell differentiation involved in embryonic placenta development [GO:0060706]; cerebral cortex neuron differentiation [GO:0021895]; cerebral cortex regionalization [GO:0021796]; chromatin remodeling [GO:0006338]; DNA demethylation [GO:0080111]; endoderm formation [GO:0001706]; endodermal cell fate specification [GO:0001714]; gene expression [GO:0010467]; mesendoderm development [GO:0048382]; mesoderm formation [GO:0001707]; mesodermal to mesenchymal transition involved in gastrulation [GO:0060809]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron migration [GO:0001764]; olfactory bulb development [GO:0021772]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; skeletal muscle cell differentiation [GO:0035914]; stem cell population maintenance [GO:0019827]; trophectodermal cell differentiation [GO:0001829]
|
chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
chromatin DNA binding [GO:0031490]; DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00907;PF16176;
|
2.60.40.820;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Functions as a transcriptional activator playing a crucial role during development. Functions in trophoblast differentiation and later in gastrulation, regulating both mesoderm delamination and endoderm specification. Plays a role in brain development being required for the specification and the proliferation of the intermediate progenitor cells and their progeny in the cerebral cortex. Also involved in the differentiation of CD8+ T-cells during immune response regulating the expression of lytic effector genes. {ECO:0000269|PubMed:17353897, ECO:0000269|PubMed:17566017}.
|
Homo sapiens (Human)
|
O95944
|
NCTR2_HUMAN
|
MAWRALHPLLLLLLLFPGSQAQSKAQVLQSVAGQTLTVRCQYPPTGSLYEKKGWCKEASALVCIRLVTSSKPRTMAWTSRFTIWDDPDAGFFTVTMTDLREEDSGHYWCRIYRPSDNSVSKSVRFYLVVSPASASTQTSWTPRDLVSSQTQTQSCVPPTAGARQAPESPSTIPVPSQPQNSTLRPGPAAPIALVPVFCGLLVAKSLVLSALLVWWGDIWWKTMMELRSLDTQKATCHLQQVTDLPWTSVSSPVEREILYHTVARTKISDDDDEHTL
| null | null |
cellular defense response [GO:0006968]; signal transduction [GO:0007165]
|
cell surface [GO:0009986]; plasma membrane [GO:0005886]
|
signaling receptor activity [GO:0038023]; transmembrane signaling receptor activity [GO:0004888]
|
PF07686;
|
2.60.40.10;
|
Natural cytotoxicity receptor (NCR) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Cytotoxicity-activating receptor that may contribute to the increased efficiency of activated natural killer (NK) cells to mediate tumor cell lysis. {ECO:0000269|PubMed:10049942}.
|
Homo sapiens (Human)
|
O95947
|
TBX6_HUMAN
|
MYHPRELYPSLGAGYRLGPAQPGADSSFPPALAEGYRYPELDTPKLDCFLSGMEAAPRTLAAHPPLPLLPPAMGTEPAPSAPEALHSLPGVSLSLENRELWKEFSSVGTEMIITKAGRRMFPACRVSVTGLDPEARYLFLLDVIPVDGARYRWQGRRWEPSGKAEPRLPDRVYIHPDSPATGAHWMRQPVSFHRVKLTNSTLDPHGHLILHSMHKYQPRIHLVRAAQLCSQHWGGMASFRFPETTFISVTAYQNPQITQLKIAANPFAKGFRENGRNCKRERDARVKRKLRGPEPAATEAYGSGDTPGGPCDSTLGGDIRESDPEQAPAPGEATAAPAPLCGGPSAEAYLLHPAAFHGAPSHLPTRSPSFPEAPDSGRSAPYSAAFLELPHGSGGSGYPAAPPAVPFAPHFLQGGPFPLPYTAPGGYLDVGSKPMY
| null | null |
anatomical structure morphogenesis [GO:0009653]; cell fate specification [GO:0001708]; heart looping [GO:0001947]; mesoderm development [GO:0007498]; mesodermal cell fate specification [GO:0007501]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; negative regulation of neuron maturation [GO:0014043]; negative regulation of neuron projection development [GO:0010977]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; signal transduction involved in regulation of gene expression [GO:0023019]; somite rostral/caudal axis specification [GO:0032525]; vasculogenesis [GO:0001570]
|
chromatin [GO:0000785]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00907;
|
2.60.40.820;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}.
| null | null | null | null | null |
FUNCTION: T-box transcription factor that plays an essential role in the determination of the fate of axial stem cells: neural vs mesodermal. Acts in part by down-regulating, a specific enhancer (N1) of SOX2, to inhibit neural development. Seems to play also an essential role in left/right axis determination and acts through effects on Notch signaling around the node as well as through an effect on the morphology and motility of the nodal cilia (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O95948
|
ONEC2_HUMAN
|
MKAAYTAYRCLTKDLEGCAMNPELTMESLGTLHGPAGGGSGGGGGGGGGGGGGGPGHEQELLASPSPHHAGRGAAGSLRGPPPPPTAHQELGTAAAAAAAASRSAMVTSMASILDGGDYRPELSIPLHHAMSMSCDSSPPGMGMSNTYTTLTPLQPLPPISTVSDKFHHPHPHHHPHHHHHHHHQRLSGNVSGSFTLMRDERGLPAMNNLYSPYKEMPGMSQSLSPLAATPLGNGLGGLHNAQQSLPNYGPPGHDKMLSPNFDAHHTAMLTRGEQHLSRGLGTPPAAMMSHLNGLHHPGHTQSHGPVLAPSRERPPSSSSGSQVATSGQLEEINTKEVAQRITAELKRYSIPQAIFAQRVLCRSQGTLSDLLRNPKPWSKLKSGRETFRRMWKWLQEPEFQRMSALRLAACKRKEQEPNKDRNNSQKKSRLVFTDLQRRTLFAIFKENKRPSKEMQITISQQLGLELTTVSNFFMNARRRSLEKWQDDLSTGGSSSTSSTCTKA
| null | null |
animal organ morphogenesis [GO:0009887]; cell fate commitment [GO:0045165]; cilium assembly [GO:0060271]; endocrine pancreas development [GO:0031018]; epithelial cell development [GO:0002064]; liver development [GO:0001889]; mesenchymal stem cell migration [GO:1905319]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; peripheral nervous system neuron development [GO:0048935]; positive regulation of mesenchymal stem cell migration [GO:1905322]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cell-matrix adhesion [GO:0001952]; regulation of transcription by RNA polymerase II [GO:0006357]; transforming growth factor beta receptor signaling pathway [GO:0007179]
|
actin cytoskeleton [GO:0015629]; chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF02376;PF00046;
|
1.10.10.60;1.10.260.40;
|
CUT homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Transcriptional activator. Activates the transcription of a number of liver genes such as HNF3B.
|
Homo sapiens (Human)
|
O95954
|
FTCD_HUMAN
|
MSQLVECVPNFSEGKNQEVIDAISGAITQTPGCVLLDVDAGPSTNRTVYTFVGPPECVVEGALNAARVASRLIDMSRHQGEHPRMGALDVCPFIPVRGVSVDECVLCAQAFGQRLAEELDVPVYLYGEAARMDSRRTLPAIRAGEYEALPKKLQQADWAPDFGPSSFVPSWGATATGARKFLIAFNINLLGTKEQAHRIALNLREQGRGKDQPGRLKKVQGIGWYLDEKNLAQVSTNLLDFEVTALHTVYEETCREAQELSLPVVGSQLVGLVPLKALLDAAAFYCEKENLFILEEEQRIRLVVSRLGLDSLCPFSPKERIIEYLVPERGPERGLGSKSLRAFVGEVGARSAAPGGGSVAAAAAAMGAALGSMVGLMTYGRRQFQSLDTTMRRLIPPFREASAKLTTLVDADAEAFTAYLEAMRLPKNTPEEKDRRTAALQEGLRRAVSVPLTLAETVASLWPALQELARCGNLACRSDLQVAAKALEMGVFGAYFNVLINLRDITDEAFKDQIHHRVSSLLQEAKTQAALVLDCLETRQE
|
2.1.2.5; 4.3.1.4
| null |
cytoskeleton organization [GO:0007010]; folic acid-containing compound metabolic process [GO:0006760]; histidine catabolic process to glutamate and formamide [GO:0019556]; histidine catabolic process to glutamate and formate [GO:0019557]
|
centriole [GO:0005814]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]; smooth endoplasmic reticulum membrane [GO:0030868]
|
folic acid binding [GO:0005542]; formimidoyltetrahydrofolate cyclodeaminase activity [GO:0030412]; glutamate formimidoyltransferase activity [GO:0030409]; microtubule binding [GO:0008017]
|
PF02971;PF04961;PF07837;
|
1.20.120.680;3.30.70.670;3.30.990.10;
|
Cyclodeaminase/cyclohydrolase family; Formiminotransferase family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9YH58}. Golgi apparatus {ECO:0000250|UniProtKB:Q9YH58}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:16534631}. Note=More abundantly located around the mother centriole. {ECO:0000269|PubMed:16534631}.
|
CATALYTIC ACTIVITY: Reaction=5-formimidoyltetrahydrofolate + L-glutamate = (6S)-5,6,7,8-tetrahydrofolate + N-formimidoyl-L-glutamate; Xref=Rhea:RHEA:15097, ChEBI:CHEBI:29985, ChEBI:CHEBI:57453, ChEBI:CHEBI:57456, ChEBI:CHEBI:58928; EC=2.1.2.5; Evidence={ECO:0000269|PubMed:12815595}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15099; Evidence={ECO:0000305|PubMed:12815595}; CATALYTIC ACTIVITY: Reaction=5-formimidoyltetrahydrofolate + 2 H(+) = (6R)-5,10-methenyltetrahydrofolate + NH4(+); Xref=Rhea:RHEA:22736, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57455, ChEBI:CHEBI:57456; EC=4.3.1.4; Evidence={ECO:0000250|UniProtKB:P53603}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22737; Evidence={ECO:0000250|UniProtKB:P53603};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=10.2 umol/min/mg enzyme for the glutamate formimidoyltransferase activity {ECO:0000269|PubMed:12815595};
|
PATHWAY: Amino-acid degradation; L-histidine degradation into L-glutamate; L-glutamate from N-formimidoyl-L-glutamate (transferase route): step 1/1. {ECO:0000269|PubMed:12815595}.
| null | null |
FUNCTION: Folate-dependent enzyme, that displays both transferase and deaminase activity. Serves to channel one-carbon units from formiminoglutamate to the folate pool. {ECO:0000269|PubMed:12815595}.; FUNCTION: Binds and promotes bundling of vimentin filaments originating from the Golgi. {ECO:0000250|UniProtKB:O88618}.
|
Homo sapiens (Human)
|
O95965
|
ITGBL_HUMAN
|
MRPPGFRNFLLLASSLLFAGLSAVPQSFSPSLRSWPGAACRLSRAESERRCRAPGQPPGAALCHGRGRCDCGVCICHVTEPGMFFGPLCECHEWVCETYDGSTCAGHGKCDCGKCKCDQGWYGDACQYPTNCDLTKKKSNQMCKNSQDIICSNAGTCHCGRCKCDNSDGSGLVYGKFCECDDRECIDDETEEICGGHGKCYCGNCYCKAGWHGDKCEFQCDITPWESKRRCTSPDGKICSNRGTCVCGECTCHDVDPTGDWGDIHGDTCECDERDCRAVYDRYSDDFCSGHGQCNCGRCDCKAGWYGKKCEHPQSCTLSAEESIRKCQGSSDLPCSGRGKCECGKCTCYPPGDRRVYGKTCECDDRRCEDLDGVVCGGHGTCSCGRCVCERGWFGKLCQHPRKCNMTEEQSKNLCESADGILCSGKGSCHCGKCICSAEEWYISGEFCDCDDRDCDKHDGLICTGNGICSCGNCECWDGWNGNACEIWLGSEYP
| null | null |
cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell migration [GO:0016477]; cell-cell adhesion [GO:0098609]; cell-matrix adhesion [GO:0007160]; integrin-mediated signaling pathway [GO:0007229]
|
cell surface [GO:0009986]; extracellular region [GO:0005576]; focal adhesion [GO:0005925]; integrin complex [GO:0008305]; plasma membrane [GO:0005886]
|
integrin binding [GO:0005178]
|
PF07974;
|
2.10.25.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
| null | null | null | null | null | null |
Homo sapiens (Human)
|
O95967
|
FBLN4_HUMAN
|
MLPCASCLPGSLLLWALLLLLLGSASPQDSEEPDSYTECTDGYEWDPDSQHCRDVNECLTIPEACKGEMKCINHYGGYLCLPRSAAVINDLHGEGPPPPVPPAQHPNPCPPGYEPDDQDSCVDVDECAQALHDCRPSQDCHNLPGSYQCTCPDGYRKIGPECVDIDECRYRYCQHRCVNLPGSFRCQCEPGFQLGPNNRSCVDVNECDMGAPCEQRCFNSYGTFLCRCHQGYELHRDGFSCSDIDECSYSSYLCQYRCINEPGRFSCHCPQGYQLLATRLCQDIDECESGAHQCSEAQTCVNFHGGYRCVDTNRCVEPYIQVSENRCLCPASNPLCREQPSSIVHRYMTITSERSVPADVFQIQATSVYPGAYNAFQIRAGNSQGDFYIRQINNVSAMLVLARPVTGPREYVLDLEMVTMNSLMSYRASSVLRLTVFVGAYTF
| null | null |
aorta development [GO:0035904]; aorta smooth muscle tissue morphogenesis [GO:0060414]; elastic fiber assembly [GO:0048251]; negative regulation of vascular associated smooth muscle cell proliferation [GO:1904706]; positive regulation of aortic smooth muscle cell differentiation [GO:1904831]; positive regulation of collagen fibril organization [GO:1904028]; positive regulation of smooth muscle cell-matrix adhesion [GO:1905609]; regulation of collagen fibril organization [GO:1904026]; vascular associated smooth muscle cell development [GO:0097084]
|
basement membrane [GO:0005604]; collagen-containing extracellular matrix [GO:0062023]; elastic fiber [GO:0071953]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular vesicle [GO:1903561]; microfibril [GO:0001527]
|
calcium ion binding [GO:0005509]; extracellular matrix structural constituent [GO:0005201]; heparin binding [GO:0008201]; protein homodimerization activity [GO:0042803]
|
PF12662;PF07645;PF12661;
|
2.10.25.10;
|
Fibulin family
|
PTM: N-glycosylated; contains mostly complex-type glycans (PubMed:23782690, PubMed:27339457). Not O-glycosylated (PubMed:27339457). {ECO:0000269|PubMed:23782690, ECO:0000269|PubMed:27339457}.; PTM: Cleaved by ELANE; produces a 50-55 kDa fragment (PubMed:27339457). Cleaved by MMP2 and MMP9; produces several fragments (PubMed:27339457). {ECO:0000269|PubMed:27339457}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:20389311, ECO:0000269|PubMed:27339457}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:Q9WVJ9}. Note=Localizes on the microfibrils surrounding ELN cores. {ECO:0000250|UniProtKB:Q9WVJ9}.
| null | null | null | null | null |
FUNCTION: Plays a crucial role in elastic fiber formation in tissue, and in the formation of ultrastructural connections between elastic laminae and smooth muscle cells in the aorta, therefore participates in terminal differentiation and maturation of smooth muscle cell (SMC) and in the mechanical properties and wall integrity maintenance of the aorta (PubMed:27339457). In addition, is involved in the control of collagen fibril assembly in tissue throught proteolytic activation of LOX leading to cross- linking of collagen and elastin (By similarity). Also promotes ELN coacervation and participates in the deposition of ELN coacervates on to microfibrils but also regulates ELN cross- linking through LOX interaction (PubMed:18973305, PubMed:19570982). Moreover adheres to the cells through heparin binding in a calcium-dependent manner and regulates vascularlar smooth muscle cells proliferation through angiotensin signaling (PubMed:23782690). {ECO:0000250|UniProtKB:Q9WVJ9, ECO:0000269|PubMed:18973305, ECO:0000269|PubMed:19570982, ECO:0000269|PubMed:23782690, ECO:0000269|PubMed:27339457}.
|
Homo sapiens (Human)
|
O95968
|
SG1D1_HUMAN
|
MRLSVCLLLLTLALCCYRANAVVCQALGSEITGFLLAGKPVFKFQLAKFKAPLEAVAAKMEVKKCVDTMAYEKRVLITKTLGKIAEKCDR
| null | null | null |
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)
|
O95970
|
LGI1_HUMAN
|
MESERSKRMGNACIPLKRIAYFLCLLSALLLTEGKKPAKPKCPAVCTCTKDNALCENARSIPRTVPPDVISLSFVRSGFTEISEGSFLFTPSLQLLLFTSNSFDVISDDAFIGLPHLEYLFIENNNIKSISRHTFRGLKSLIHLSLANNNLQTLPKDIFKGLDSLTNVDLRGNSFNCDCKLKWLVEWLGHTNATVEDIYCEGPPEYKKRKINSLSSKDFDCIITEFAKSQDLPYQSLSIDTFSYLNDEYVVIAQPFTGKCIFLEWDHVEKTFRNYDNITGTSTVVCKPIVIETQLYVIVAQLFGGSHIYKRDSFANKFIKIQDIEILKIRKPNDIETFKIENNWYFVVADSSKAGFTTIYKWNGNGFYSHQSLHAWYRDTDVEYLEIVRTPQTLRTPHLILSSSSQRPVIYQWNKATQLFTNQTDIPNMEDVYAVKHFSVKGDVYICLTRFIGDSKVMKWGGSSFQDIQRMPSRGSMVFQPLQINNYQYAILGSDYSFTQVYNWDAEKAKFVKFQELNVQAPRSFTHVSINKRNFLFASSFKGNTQIYKHVIVDLSA
| null | null |
axon guidance [GO:0007411]; myelination [GO:0042552]; nervous system development [GO:0007399]; neuron projection development [GO:0031175]; neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0099645]; positive regulation of cell growth [GO:0030307]; positive regulation of synaptic transmission [GO:0050806]
|
axon initial segment [GO:0043194]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; synaptic cleft [GO:0043083]
|
signaling receptor binding [GO:0005102]
|
PF03736;PF13855;
|
3.80.10.10;
| null |
PTM: Glycosylated. {ECO:0000269|PubMed:17067999}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16787412, ECO:0000269|PubMed:17067999, ECO:0000269|PubMed:17296837}. Synapse {ECO:0000250|UniProtKB:Q8K4Y5}. Cytoplasm {ECO:0000250|UniProtKB:Q9JIA1}.; SUBCELLULAR LOCATION: [Isoform 1]: Golgi apparatus {ECO:0000269|PubMed:17067999}. Secreted {ECO:0000269|PubMed:9879993}. Cytoplasm {ECO:0000250|UniProtKB:Q9JIA1}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum {ECO:0000269|PubMed:17067999}. Cytoplasm {ECO:0000250|UniProtKB:Q9JIA1}.
| null | null | null | null | null |
FUNCTION: Regulates voltage-gated potassium channels assembled from KCNA1, KCNA4 and KCNAB1. It slows down channel inactivation by precluding channel closure mediated by the KCNAB1 subunit. Ligand for ADAM22 that positively regulates synaptic transmission mediated by AMPA-type glutamate receptors (By similarity). Plays a role in suppressing the production of MMP1/3 through the phosphatidylinositol 3-kinase/ERK pathway. May play a role in the control of neuroblastoma cell survival. {ECO:0000250, ECO:0000269|PubMed:15047712, ECO:0000269|PubMed:16518856}.
|
Homo sapiens (Human)
|
O95971
|
BY55_HUMAN
|
MLLEPGRGCCALAILLAIVDIQSGGCINITSSASQEGTRLNLICTVWHKKEEAEGFVVFLCKDRSGDCSPETSLKQLRLKRDPGIDGVGEISSQLMFTISQVTPLHSGTYQCCARSQKSGIRLQGHFFSILFTETGNYTVTGLKQRQHLEFSHNEGTLSSGFLQEKVWVMLVTSLVALQAL
| null | null |
adaptive immune response [GO:0002250]; angiogenesis [GO:0001525]; defense response to Gram-negative bacterium [GO:0050829]; innate immune response [GO:0045087]; mucosal immune response [GO:0002385]; negative regulation of adaptive immune memory response [GO:1905675]; negative regulation of angiogenesis [GO:0016525]; negative regulation of CD4-positive, alpha-beta T cell costimulation [GO:1900280]; negative regulation of T cell receptor signaling pathway [GO:0050860]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; positive regulation of endothelial cell apoptotic process [GO:2000353]; positive regulation of natural killer cell cytokine production [GO:0002729]; positive regulation of natural killer cell degranulation [GO:0043323]; positive regulation of natural killer cell mediated cytotoxicity [GO:0045954]; positive regulation of natural killer cell mediated immune response to tumor cell [GO:0002857]; positive regulation of type II interferon production [GO:0032729]; T cell costimulation [GO:0031295]
|
extracellular region [GO:0005576]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
|
activating MHC class I receptor activity [GO:0032397]; kinase binding [GO:0019900]; MHC class I protein complex binding [GO:0023024]; MHC class I receptor activity [GO:0032393]; MHC class Ib receptor activity [GO:0032394]; signaling receptor binding [GO:0005102]
| null |
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: [CD160 antigen]: Cell membrane {ECO:0000269|PubMed:12486241, ECO:0000269|PubMed:18193050, ECO:0000269|PubMed:9973372}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:23761635, ECO:0000269|PubMed:9743336}.; SUBCELLULAR LOCATION: [CD160 antigen, soluble form]: Secreted. Note=Released from the cell membrane by GPI cleavage. {ECO:0000269|PubMed:17237375, ECO:0000269|PubMed:23761635, ECO:0000269|PubMed:9743336}.
| null | null | null | null | null |
FUNCTION: [CD160 antigen]: Receptor on immune cells capable to deliver stimulatory or inhibitory signals that regulate cell activation and differentiation. Exists as a GPI-anchored and as a transmembrane form, each likely initiating distinct signaling pathways via phosphoinositol 3-kinase in activated NK cells and via LCK and CD247/CD3 zeta chain in activated T cells (PubMed:11978774, PubMed:17307798, PubMed:19109136). Receptor for both classical and non-classical MHC class I molecules (PubMed:12486241, PubMed:9973372). In the context of acute viral infection, recognizes HLA-C and triggers NK cell cytotoxic activity, likely playing a role in anti-viral innate immune response (PubMed:12486241). On CD8+ T cells, binds HLA-A2-B2M in complex with a viral peptide and provides a costimulatory signal to activated/memory T cells (PubMed:9973372). Upon persistent antigen stimulation, such as occurs during chronic viral infection, may progressively inhibit TCR signaling in memory CD8+ T cells, contributing to T cell exhaustion (PubMed:25255144). On endothelial cells, recognizes HLA-G and controls angiogenesis in immune privileged sites (PubMed:16809620). Receptor or ligand for TNF superfamily member TNFRSF14, participating in bidirectional cell-cell contact signaling between antigen presenting cells and lymphocytes. Upon ligation of TNFRSF14, provides stimulatory signal to NK cells enhancing IFNG production and anti-tumor immune response (By similarity). On activated CD4+ T cells, interacts with TNFRSF14 and down-regulates CD28 costimulatory signaling, restricting memory and alloantigen-specific immune response (PubMed:18193050). In the context of bacterial infection, acts as a ligand for TNFRSF14 on epithelial cells, triggering the production of antimicrobial proteins and pro-inflammatory cytokines (By similarity). {ECO:0000250|UniProtKB:O88875, ECO:0000269|PubMed:11978774, ECO:0000269|PubMed:12486241, ECO:0000269|PubMed:16809620, ECO:0000269|PubMed:17307798, ECO:0000269|PubMed:18193050, ECO:0000269|PubMed:19109136, ECO:0000269|PubMed:25255144, ECO:0000269|PubMed:9973372}.; FUNCTION: [CD160 antigen, soluble form]: The soluble GPI-cleaved form, usually released by activated lymphocytes, might play an immune regulatory role by limiting lymphocyte effector functions. {ECO:0000269|PubMed:17237375}.
|
Homo sapiens (Human)
|
O95972
|
BMP15_HUMAN
|
MVLLSILRILFLCELVLFMEHRAQMAEGGQSSIALLAEAPTLPLIEELLEESPGEQPRKPRLLGHSLRYMLELYRRSADSHGHPRENRTIGATMVRLVKPLTNVARPHRGTWHIQILGFPLRPNRGLYQLVRATVVYRHHLQLTRFNLSCHVEPWVQKNPTNHFPSSEGDSSKPSLMSNAWKEMDITQLVQQRFWNNKGHRILRLRFMCQQQKDSGGLELWHGTSSLDIAFLLLYFNDTHKSIRKAKFLPRGMEEFMERESLLRRTRQADGISAEVTASSSKHSGPENNQCSLHPFQISFRQLGWDHWIIAPPFYTPNYCKGTCLRVLRDGLNSPNHAIIQNLINQLVDQSVPRPSCVPYKYVPISVLMIEANGSILYKEYEGMIAESCTCR
| null | null |
female gamete generation [GO:0007292]
|
endoplasmic reticulum lumen [GO:0005788]; extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; growth factor activity [GO:0008083]
|
PF00019;
|
2.10.90.10;
|
TGF-beta family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: May be involved in follicular development. Oocyte-specific growth/differentiation factor that stimulates folliculogenesis and granulosa cell (GC) growth. {ECO:0000269|PubMed:18227435}.
|
Homo sapiens (Human)
|
O95977
|
S1PR4_HUMAN
|
MNATGTPVAPESCQQLAAGGHSRLIVLHYNHSGRLAGRGGPEDGGLGALRGLSVAASCLVVLENLLVLAAITSHMRSRRWVYYCLVNITLSDLLTGAAYLANVLLSGARTFRLAPAQWFLREGLLFTALAASTFSLLFTAGERFATMVRPVAESGATKTSRVYGFIGLCWLLAALLGMLPLLGWNCLCAFDRCSSLLPLYSKRYILFCLVIFAGVLATIMGLYGAIFRLVQASGQKAPRPAARRKARRLLKTVLMILLAFLVCWGPLFGLLLADVFGSNLWAQEYLRGMDWILALAVLNSAVNPIIYSFRSREVCRAVLSFLCCGCLRLGMRGPGDCLARAVEAHSGASTTDSSLRPRDSFRGSRSLSFRMREPLSSISSVRSI
| null | null |
activation of phospholipase C activity [GO:0007202]; adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; G protein-coupled receptor signaling pathway [GO:0007186]; immune response [GO:0006955]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; regulation of metabolic process [GO:0019222]
|
cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
|
G protein-coupled receptor activity [GO:0004930]; lipid binding [GO:0008289]; sphingosine-1-phosphate receptor activity [GO:0038036]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. May be involved in cell migration processes that are specific for lymphocytes. {ECO:0000269|PubMed:10679247, ECO:0000269|PubMed:10753843}.
|
Homo sapiens (Human)
|
O95980
|
RECK_HUMAN
|
MATVRASLRGALLLLLAVAGVAEVAGGLAPGSAGALCCNHSKDNQMCRDVCEQIFSSKSESRLKHLLQRAPDYCPETMVEIWNCMNSSLPGVFKKSDGWVGLGCCELAIALECRQACKQASSKNDISKVCRKEYENALFSCISRNEMGSVCCSYAGHHTNCREYCQAIFRTDSSPGPSQIKAVENYCASISPQLIHCVNNYTQSYPMRNPTDSLYCCDRAEDHACQNACKRILMSKKTEMEIVDGLIEGCKTQPLPQDPLWQCFLESSQSVHPGVTVHPPPSTGLDGAKLHCCSKANTSTCRELCTKLYSMSWGNTQSWQEFDRFCEYNPVEVSMLTCLADVREPCQLGCRNLTYCTNFNNRPTELFRSCNAQSDQGAMNDMKLWEKGSIKMPFINIPVLDIKKCQPEMWKAIACSLQIKPCHSKSRGSIICKSDCVEILKKCGDQNKFPEDHTAESICELLSPTDDLKNCIPLDTYLRPSTLGNIVEEVTHPCNPNPCPANELCEVNRKGCPSGDPCLPYFCVQGCKLGEASDFIVRQGTLIQVPSSAGEVGCYKICSCGQSGLLENCMEMHCIDLQKSCIVGGKRKSHGTSFSIDCNVCSCFAGNLVCSTRLCLSEHSSEDDRRTFTGLPCNCADQFVPVCGQNGRTYPSACIARCVGLQDHQFEFGSCMSKDPCNPNPCQKNQRCIPKPQVCLTTFDKFGCSQYECVPRQLACDQVQDPVCDTDHMEHNNLCTLYQRGKSLSYKGPCQPFCRATEPVCGHNGETYSSVCAAYSDRVAVDYYGDCQAVGVLSEHSSVAECASVKCPSLLAAGCKPIIPPGACCPLCAGMLRVLFDKEKLDTIAKVTNKKPITVLEILQKIRMHVSVPQCDVFGYFSIESEIVILIIPVDHYPKALQIEACNKEAEKIESLINSDSPTLASHVPLSALIISQVQVSSSVPSAGVRARPSCHSLLLPLSLGLALHLLWTYN
| null | null |
blood vessel maturation [GO:0001955]; canonical Wnt signaling pathway [GO:0060070]; embryo implantation [GO:0007566]; embryonic forelimb morphogenesis [GO:0035115]; extracellular matrix organization [GO:0030198]; negative regulation of cell migration [GO:0030336]; negative regulation of metalloendopeptidase activity [GO:1904684]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; regulation of angiogenesis [GO:0045765]; regulation of establishment of blood-brain barrier [GO:0090210]; sprouting angiogenesis [GO:0002040]
|
extracellular region [GO:0005576]; membrane [GO:0016020]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; Wnt signalosome [GO:1990909]
|
coreceptor activity [GO:0015026]; endopeptidase inhibitor activity [GO:0004866]; metalloendopeptidase inhibitor activity [GO:0008191]; serine-type endopeptidase inhibitor activity [GO:0004867]; Wnt-protein binding [GO:0017147]
|
PF07648;
|
3.30.60.30;
|
RECK family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:9789069}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30026314, ECO:0000269|PubMed:9789069}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:9789069}.
| null | null | null | null | null |
FUNCTION: Functions together with ADGRA2 to enable brain endothelial cells to selectively respond to Wnt7 signals (WNT7A or WNT7B) (PubMed:28289266, PubMed:30026314). Plays a key role in Wnt7-specific responses: required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation (By similarity). Acts as a Wnt7-specific coactivator of canonical Wnt signaling by decoding Wnt ligands: acts by interacting specifically with the disordered linker region of Wnt7, thereby conferring ligand selectivity for Wnt7 (PubMed:30026314). ADGRA2 is then required to deliver RECK-bound Wnt7 to frizzled by assembling a higher-order RECK-ADGRA2-Fzd-LRP5-LRP6 complex (PubMed:30026314). Also acts as a serine protease inhibitor: negatively regulates matrix metalloproteinase-9 (MMP9) by suppressing MMP9 secretion and by direct inhibition of its enzymatic activity (PubMed:18194466, PubMed:9789069). Also inhibits metalloproteinase activity of MMP2 and MMP14 (MT1-MMP) (PubMed:9789069). {ECO:0000250|UniProtKB:Q9Z0J1, ECO:0000269|PubMed:18194466, ECO:0000269|PubMed:28289266, ECO:0000269|PubMed:30026314, ECO:0000269|PubMed:9789069}.
|
Homo sapiens (Human)
|
O95983
|
MBD3_HUMAN
|
MERKRWECPALPQGWEREEVPRRSGLSAGHRDVFYYSPSGKKFRSKPQLARYLGGSMDLSTFDFRTGKMLMSKMNKSRQRVRYDSSNQVKGKPDLNTALPVRQTASIFKQPVTKITNHPSNKVKSDPQKAVDQPRQLFWEKKLSGLNAFDIAEELVKTMDLPKGLQGVGPGCTDETLLSAIASALHTSTMPITGQLSAAVEKNPGVWLNTTQPLCKAFMVTDEDIRKQEELVQQVRKRLEEALMADMLAHVEELARDGEAPLDKACAEDDDEEDEEEEEEEPDPDPEMEHV
| null | null |
chromatin remodeling [GO:0006338]; DNA methylation-dependent heterochromatin formation [GO:0006346]; embryonic organ development [GO:0048568]; in utero embryonic development [GO:0001701]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of cell fate specification [GO:0042659]; regulation of stem cell differentiation [GO:2000736]; response to estradiol [GO:0032355]; response to nutrient levels [GO:0031667]; ventricular cardiac muscle tissue development [GO:0003229]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; heterochromatin [GO:0000792]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; NuRD complex [GO:0016581]; protein-containing complex [GO:0032991]
|
DNA binding [GO:0003677]; methyl-CpG binding [GO:0008327]
|
PF01429;PF14048;PF16564;
| null | null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15701600, ECO:0000269|PubMed:16428440, ECO:0000269|PubMed:20523938, ECO:0000269|PubMed:28977666, ECO:0000269|PubMed:33283408}. Chromosome {ECO:0000269|PubMed:27732854}. Note=Nuclear, in discrete foci. Detected on chromatin, at promoter regions of active genes. {ECO:0000269|PubMed:27732854}.
| null | null | null | null | null |
FUNCTION: Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:12124384, PubMed:16428440, PubMed:28977666). Acts as transcriptional repressor and plays a role in gene silencing (PubMed:10947852, PubMed:18644863). Does not bind to methylated DNA by itself (PubMed:12124384, PubMed:16428440). Binds to a lesser degree DNA containing unmethylated CpG dinucleotides (PubMed:24307175). Recruits histone deacetylases and DNA methyltransferases. {ECO:0000269|PubMed:10947852, ECO:0000269|PubMed:12124384, ECO:0000269|PubMed:16428440, ECO:0000269|PubMed:18644863, ECO:0000269|PubMed:23361464, ECO:0000269|PubMed:24307175, ECO:0000269|PubMed:28977666, ECO:0000269|PubMed:9774669}.
|
Homo sapiens (Human)
|
O95985
|
TOP3B_HUMAN
|
MKTVLMVAEKPSLAQSIAKILSRGSLSSHKGLNGACSVHEYTGTFAGQPVRFKMTSVCGHVMTLDFLGKYNKWDKVDPAELFSQAPTEKKEANPKLNMVKFLQVEGRGCDYIVLWLDCDKEGENICFEVLDAVLPVMNKAHGGEKTVFRARFSSITDTDICNAMACLGEPDHNEALSVDARQELDLRIGCAFTRFQTKYFQGKYGDLDSSLISFGPCQTPTLGFCVERHDKIQSFKPETYWVLQAKVNTDKDRSLLLDWDRVRVFDREIAQMFLNMTKLEKEAQVEATSRKEKAKQRPLALNTVEMLRVASSSLGMGPQHAMQTAERLYTQGYISYPRTETTHYPENFDLKGSLRQQANHPYWADTVKRLLAEGINRPRKGHDAGDHPPITPMKSATEAELGGDAWRLYEYITRHFIATVSHDCKYLQSTISFRIGPELFTCSGKTVLSPGFTEVMPWQSVPLEESLPTCQRGDAFPVGEVKMLEKQTNPPDYLTEAELITLMEKHGIGTDASIPVHINNICQRNYVTVESGRRLKPTNLGIVLVHGYYKIDAELVLPTIRSAVEKQLNLIAQGKADYRQVLGHTLDVFKRKFHYFVDSIAGMDELMEVSFSPLAATGKPLSRCGKCHRFMKYIQAKPSRLHCSHCDETYTLPQNGTIKLYKELRCPLDDFELVLWSSGSRGKSYPLCPYCYNHPPFRDMKKGMGCNECTHPSCQHSLSMLGIGQCVECESGVLVLDPTSGPKWKVACNKCNVVAHCFENAHRVRVSADTCSVCEAALLDVDFNKAKSPLPGDETQHMGCVFCDPVFQELVELKHAASCHPMHRGGPGRRQGRGRGRARRPPGKPNPRRPKDKMSALAAYFV
|
5.6.2.1
| null |
chromosome segregation [GO:0007059]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; DNA topological change [GO:0006265]
|
condensed chromosome [GO:0000793]; DNA topoisomerase III-beta-TDRD3 complex [GO:0140225]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA topoisomerase activity [GO:0003916]; DNA topoisomerase type I (single strand cut, ATP-independent) activity [GO:0003917]; RNA binding [GO:0003723]
|
PF01131;PF01751;
|
3.40.50.140;1.10.460.10;2.70.20.10;1.10.290.10;
|
Type IA topoisomerase family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10131};
| null | null | null | null |
FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand than undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). Possesses negatively supercoiled DNA relaxing activity. {ECO:0000250}.
|
Homo sapiens (Human)
|
O95988
|
TCL1B_HUMAN
|
MASEASVRLGVPPGRLWIQRPGIYEDEEGRTWVTVVVRFNPSRREWARASQGSRYEPSITVHLWQMAVHTRELLSSGQMPFSQLPAVWQLYPGRKYRAADSSFWEIADHGQIDSMEQLVLTYQPERKD
| null | null |
intracellular signal transduction [GO:0035556]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]
| null |
protein kinase binding [GO:0019901]; protein serine/threonine kinase activator activity [GO:0043539]
|
PF01840;
|
2.40.15.10;
|
TCL1 family
| null | null | null | null | null | null | null |
FUNCTION: Enhances the phosphorylation and activation of AKT1 and AKT2. {ECO:0000269|PubMed:10983986}.
|
Homo sapiens (Human)
|
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