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 | MEVEQEQRRRKVEAGRTKLAHFRQRKTKGDSSHSEKKTAKRKGSAVDASVQEESPVTKEDSALCGGGDICKSTSCDDTPDGAGGAFAAQPEDCDGEKREDLEQLQQKQVNDHPPEQCGMFTVSDHPPEQHGMFTVGDHPPEQRGMFTVSDHPPEQHGMFTVSDHPPEQRGMFTISDHQPEQRGMFTVSDHTPEQRGIFTISDHPAEQRGMFTKECEQECELAITDLESGREDEAGLHQSQAVHGLELEALRLSLSNMHTAQLELTQANLQKEKETALTELREMLNSRRAQELALLQSRQQHELELLREQHAREKEEVVLR... | 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|PubM... | 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 st... | 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 ... | 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]; regulatio... | 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 prefe... | Homo sapiens (Human) |
O95622 | ADCY5_HUMAN | MSGSKSVSPPGYAAQKTAAPAPRGGPEHRSAWGEADSRANGYPHAPGGSARGSTKKPGGAVTPQQQQRLASRWRSDDDDDPPLSGDDPLAGGFGFSFRSKSAWQERGGDDCGRGSRRQRRGAASGGSTRAPPAGGGGGSAAAAASAGGTEVRPRSVEVGLEERRGKGRAADELEAGAVEGGEGSGDGGSSADSGSGAGPGAVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQSSLTMLMAVLVLVCLVMLAFHAARPPLQLPYLAVLAAAVGVILIMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLP... | 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 ... | 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... | Homo sapiens (Human) |
O95628 | CNOT4_HUMAN | MSRSPDAKEDPVECPLCMEPLEIDDINFFPCTCGYQICRFCWHRIRTDENGLCPACRKPYPEDPAVYKPLSQEELQRIKNEKKQKQNERKQKISENRKHLASVRVVQKNLVFVVGLSQRLADPEVLKRPEYFGKFGKIHKVVINNSTSYAGSQGPSASAYVTYIRSEDALRAIQCVNNVVVDGRTLKASLGTTKYCSYFLKNMQCPKPDCMYLHELGDEAASFTKEEMQAGKHQEYEQKLLQELYKLNPNFLQLSTGSVDKNKNKVTPLQRYDTPIDKPSDSLSIGNGDNSQQISNSDTPSPPPGLSKSNPVIPISSSNH... | 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:298613... | 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 ... | Homo sapiens (Human) |
O95630 | STABP_HUMAN | MSDHGDVSLPPEDRVRALSQLGSAVEVNEDIPPRRYFRSGVEIIRMASIYSEEGNIEHAFILYNKYITLFIEKLPKHRDYKSAVIPEKKDTVKKLKEIAFPKAEELKAELLKRYTKEYTEYNEEKKKEAEELARNMAIQQELEKEKQRVAQQKQQQLEQEQFHAFEEMIRNQELEKERLKIVQEFGKVDPGLGGPLVPDLEKPSLDVFPTLTVSSIQPSDCHTTVRPAKPPVVDRSLKPGALSNSESIPTIDGLRHVVVPGRLCPQFLQLASANTARGVETCGILCGKLMRNEFTITHVLIPKQSAGSDYCNTENEEELF... | 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 [G... | 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 (Pu... | Homo sapiens (Human) |
O95631 | NET1_HUMAN | MMRAVWEALAALAAVACLVGAVRGGPGLSMFAGQAAQPDPCSDENGHPRRCIPDFVNAAFGKDVRVSSTCGRPPARYCVVSERGEERLRSCHLCNASDPKKAHPPAFLTDLNNPHNLTCWQSENYLQFPHNVTLTLSLGKKFEVTYVSLQFCSPRPESMAIYKSMDYGRTWVPFQFYSTQCRKMYNRPHRAPITKQNEQEAVCTDSHTDMRPLSGGLIAFSTLDGRPSAHDFDNSPVLQDWVTATDIRVAFSRLHTFGDENEDDSELARDSYFYAVSDLQVGGRCKCNGHAARCVRDRDDSLVCDCRHNTAGPECDRCKP... | 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];... | 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 ... | 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 transme... | 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:16150... | 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 di... | 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 pref... | Homo sapiens (Human) |
O95644 | NFAC1_HUMAN | MPSTSFPVPSKFPLGPAAAVFGRGETLGPAPRAGGTMKSAEEEHYGYASSNVSPALPLPTAHSTLPAPCHNLQTSTPGIIPPADHPSGYGAALDGGPAGYFLSSGHTRPDGAPALESPRIEITSCLGLYHNNNQFFHDVEVEDVLPSSKRSPSTATLSLPSLEAYRDPSCLSPASSLSSRSCNSEASSYESNYSYPYASPQTSPWQSPCVSPKTTDPEEGFPRGLGACTLLGSPRHSPSTSPRASVTEESWLGARSSRPASPCNKRKYSLNGRQPPYSPHHSPTPSPHGSPRVSVTDDSWLGNTTQYTSSAIVAAINALT... | 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]; ne... | 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]; nuclei... | 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:12... | 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 distingu... | 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-l... | 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 c... | Homo sapiens (Human) |
O95671 | ASML_HUMAN | MVLCPVIGKLLHKRVVLASASPRRQEILSNAGLRFEVVPSKFKEKLDKASFATPYGYAMETAKQKALEVANRLYQKDLRAPDVVIGADTIVTVGGLILEKPVDKQDAYRMLSRLSGREHSVFTGVAIVHCSSKDHQLDTRVSEFYEETKVKFSELSEELLWEYVHSGEPMDKAGGYGIQALGGMLVESVHGDFLNVVGFPLNHFCKQLVKLYYPPRPEDLRRSVKHDSIPAADTFEDLSDVEGGGSEPTQRDAGSRDEKAEAGEAGQATAEAECHRTRETLPPFPTRLLELIEGFMLSKGLLTACKLKVFDLLKDEAPQK... | 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:... | 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 f... | 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 a... | Homo sapiens (Human) |
O95672 | ECEL1_HUMAN | MEPPYSLTAHYDEFQEVKYVSRCGAGGARGASLPPGFPLGAARSATGARSGLPRWNRREVCLLSGLVFAAGLCAILAAMLALKYLGPVAAGGGACPEGCPERKAFARAARFLAANLDASIDPCQDFYSFACGGWLRRHAIPDDKLTYGTIAAIGEQNEERLRRLLARPGGGPGGAAQRKVRAFFRSCLDMREIERLGPRPMLEVIEDCGGWDLGGAEERPGVAARWDLNRLLYKAQGVYSAAALFSLTVSLDDRNSSRYVIRIDQDGLTLPERTLYLAQDEDSEKILAAYRVFMERVLSLLGADAVEQKAQEILQVEQQL... | 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 | MTELRQRVAHEPVAPPEDKESESEAKVDGETASDSESRAESAPLPVSADDTPEVLNRALSNLSSRWKNWWVRGILTLAMIAFFFIIIYLGPMVLMIIVMCVQIKCFHEIITIGYNVYHSYDLPWFRTLSWYFLLCVNYFFYGETVTDYFFTLVQREEPLRILSKYHRFISFTLYLIGFCMFVLSLVKKHYRLQFYMFGWTHVTLLIVVTQSHLVIHNLFEGMIWFIVPISCVICNDIMAYMFGFFFGRTPLIKLSPKKTWEGFIGGFFATVVFGLLLSYVMSGYRCFVCPVEYNNDTNSFTVDCEPSDLFRLQEYNIPGV... | 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=lef... | 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:000... | 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... | Homo sapiens (Human) |
O95677 | EYA4_HUMAN | MEDSQDLNEQSVKKTCTESDVSQSQNSRSMEMQDLASPHTLVGGGDTPGSSKLEKSNLSSTSVTTNGTGGENMTVLNTADWLLSCNTPSSATMSLLAVKTEPLNSSETTATTGDGALDTFTGSVITSSGYSPRSAHQYSPQLYPSKPYPHILSTPAAQTMSAYAGQTQYSGMQQPAVYTAYSQTGQPYSLPTYDLGVMLPAIKTESGLSQTQSPLQSGCLSYSPGFSTPQPGQTPYSYQMPGSSFAPSSTIYANNSVSNSTNFSGSQQDYPSYTAFGQNQYAQYYSASTYGAYMTSNNTADGTPSSTSTYQLQESLPGLT... | 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:0045... | 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 dephos... | Homo sapiens (Human) |
O95678 | K2C75_HUMAN | MSRQSSITFQSGSRRGFSTTSAITPAAGRSRFSSVSVARSAAGSGGLGRISSAGASFGSRSLYNLGGAKRVSINGCGSSCRSGFGGRASNRFGVNSGFGYGGGVGGGFSGPSFPVCPPGGIQEVTVNQSLLTPLHLQIDPTIQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWALLQEQGSRTVRQNLEPLFDSYTSELRRQLESITTERGRLEAELRNMQDVVEDFKVRYEDEINKRTAAENEFVALKKDVDAAYMNKVELEAKVKSLPEEINFIHSVFDAELSQLQTQVGDTSVVLSMDNNRNLDLDSII... | 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 | MAATAAAVVAEEDTELRDLLVQTLENSGVLNRIKAELRAAVFLALEEQEKVENKTPLVNESLKKFLNTKDGRLVASLVAEFLQFFNLDFTLAVFQPETSTLQGLEGRENLARDLGIIEAEGTVGGPLLLEVIRRCQQKEKGPTTGEGALDLSDVHSPPKSPEGKTSAQTTPSKIPRYKGQGKKKTSGQKAGDKKANDEANQSDTSVSLSEPKSKSSLHLLSHETKIGSFLSNRTLDGKDKAGLCPDEDDMEGDSFFDDPIPKPEKTYGLRKEPRKQAGSLASLSDAPPLKSGLSSLAGAPSLKDSESKRGNTVLKDLKLI... | 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:0... | 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 | MRRKGRCHRGSAARHPSSPCSVKHSPTRETLTYAQAQRMVEIEIEGRLHRISIFDPLEIILEDDLTAQEMSECNSNKENSERPPVCLRTKRHKNNRVKKKNEALPSAHGTPASASALPEPKVRIVEYSPPSAPRRPPVYYKFIEKSAEELDNEVEYDMDEEDYAWLEIVNEKRKGDCVPAVSQSMFEFLMDRFEKESHCENQKQGEQQSLIDEDAVCCICMDGECQNSNVILFCDMCNLAVHQECYGVPYIPEGQWLCRHCLQSRARPADCVLCPNKGGAFKKTDDDRWGHVVCALWIPEVGFANTVFIEPIDGVRNIPP... | 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 po... | 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' acetyla... | Homo sapiens (Human) |
O95704 | APBB3_HUMAN | MLGKDYMLAIILVNCDDDLWGDHSLEVEAGLPPGWRKIHDAAGTYYWHVPSGSTQWQRPTWELGDAEDPGTGTEGIWGLRPPKGRSFSSLESSLDRSNSLSWYGGESYIQSMEPGAKCFAVRSLGWVEVPEEDLAPGKSSIAVNNCIQQLAQTRSRSQPPDGAWGEGQNMLMILKKDAMSLVNPLDHSLIHCQPLVHIRVWGVGSSKGRDRDFAFVASDKDSCMLKCHVFCCDVPAKAIASALHGLCAQILSERVEVSGDASCCSPDPISPEDLPRQVELLDAVSQAAQKYEALYMGTLPVTKAMGMDVLNEAIGTLTAR... | 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 | MPSESFCLAAQARLDSKWLKTDIQLAFTRDGLCGLWNEMVKDGEIVYTGTESTQNGELPPRKDDSVEPSGTKKEDLNDKEKKDEEETPAPIYRAKSILDSWVWGKQPDVNELKECLSVLVKEQQALAVQSATTTLSALRLKQRLVILERYFIALNRTVFQENVKVKWKSSGISLPPVDKKSSRPAGKGVEGLARVGSRAALSFAFAFLRRAWRSGEDADLCSELLQESLDALRALPEASLFDESTVSSVWLEVVERATRFLRSVVTGDVHGTPATKGPGSIPLQDQHLALAILLELAVQRGTLSQMLSAILLLLQLWDSG... | 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.... | 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 | MSSDDRHLGSSCGSFIKTEPSSPSSGIDALSHHSPSGSSDASGGFGLALGTHANGLDSPPMFAGAGLGGTPCRKSYEDCASGIMEDSAIKCEYMLNAIPKRLCLVCGDIASGYHYGVASCEACKAFFKRTIQGNIEYSCPATNECEITKRRRKSCQACRFMKCLKVGMLKEGVRLDRVRGGRQKYKRRLDSESSPYLSLQISPPAKKPLTKIVSYLLVAEPDKLYAMPPPGMPEGDIKALTTLCDLADRELVVIIGWAKHIPGFSSLSLGDQMSLLQSAWMEILILGIVYRSLPYDDKLVYAEDYIMDEEHSRLAGLLEL... | 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 D... | 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 b... | 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 maintainan... | 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]; vesicl... | 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:003... | 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:0... | 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... | Homo sapiens (Human) |
O95727 | CRTAM_HUMAN | MWWRVLSLLAWFPLQEASLTNHTETITVEEGQTLTLKCVTSLRKNSSLQWLTPSGFTIFLNEYPALKNSKYQLLHHSANQLSITVPNVTLQDEGVYKCLHYSDSVSTKEVKVIVLATPFKPILEASVIRKQNGEEHVVLMCSTMRSKPPPQITWLLGNSMEVSGGTLHEFETDGKKCNTTSTLIIHTYGKNSTVDCIIRHRGLQGRKLVAPFRFEDLVTDEETASDALERNSLSSQDPQQPTSTVSVTEDSSTSEIDKEEKEQTTQDPDLTTEANPQYLGLARKKSGILLLTLVSFLIFILFIIVQLFIMKLRKAHVIWK... | 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 orga... | 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-mediate... | Homo sapiens (Human) |
O95741 | CPNE6_HUMAN | MSDPEMGWVPEPPTMTLGASRVELRVSCHGLLDRDTLTKPHPCVLLKLYSDEQWVEVERTEVLRSCSSPVFSRVLALEYFFEEKQPLQFHVFDAEDGATSPRNDTFLGSTECTLGQIVSQTKVTKPLLLKNGKTAGKSTITIVAEEVSGTNDYVQLTFRAYKLDNKDLFSKSDPFMEIYKTNEDQSDQLVWRTEVVKNNLNPSWEPFRLSLHSLCSCDVHRPLKFLVYDYDSSGKHDFIGEFTSTFQEMQEGTANPGQEMQWDCINPKYRDKKKNYKSSGTVVLAQCTVEKVHTFLDYIMGGCQISFTVAIDFTASNGDP... | 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:... | 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:23999... | Homo sapiens (Human) |
O95747 | OXSR1_HUMAN | MSEDSSALPWSINRDDYELQEVIGSGATAVVQAAYCAPKKEKVAIKRINLEKCQTSMDELLKEIQAMSQCHHPNIVSYYTSFVVKDELWLVMKLLSGGSVLDIIKHIVAKGEHKSGVLDESTIATILREVLEGLEYLHKNGQIHRDVKAGNILLGEDGSVQIADFGVSAFLATGGDITRNKVRKTFVGTPCWMAPEVMEQVRGYDFKADIWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPSLETGVQDKEMLKKYGKSFRKMISLCLQKDPEKRPTAAELLRHKFFQKAKNKEFLQEKTLQRAPTISERAKKVRR... | 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... | 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:00... | 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:000026... | 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 protei... | 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]; ubiquinon... | 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 diph... | 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.; PATHWA... | 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 regulat... | 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,... | 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 | MPASAARPRPGPGQPTASPFPLLLLAVLSGPVSGRVPRSVPRTSLPISEADSCLTRFAVPHTYNYSVLLVDPASHTLYVGARDTIFALSLPFSGERPRRIDWMVPEAHRQNCRKKGKKEDECHNFVQILAIANASHLLTCGTFAFDPKCGVIDVSRFQQVERLESGRGKCPFEPAQRSAAVMAGGVLYAATVKNYLGTEPIITRAVGRAEDWIRTDTLPSWLNAPAFVAAVALSPAEWGDEDGDDEIYFFFTETSRAFDSYERIKVPRVARVCAGDLGGRKTLQQRWTTFLKADLLCPGPEHGRASSVLQDVAVLRPELG... | 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 gan... | 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:Q... | 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... | Homo sapiens (Human) |
O95758 | PTBP3_HUMAN | MDGVVTDLITVGLKRGSDELLSSGIINGPFTMNSSTPSTANGNDSKKFKRDRPPCSPSRVLHLRKIPCDVTEAEIISLGLPFGKVTNLLMLKGKSQAFLEMASEEAAVTMVNYYTPITPHLRSQPVYIQYSNHRELKTDNLPNQARAQAALQAVSAVQSGSLALSGGPSNEGTVLPGQSPVLRIIIENLFYPVTLEVLHQIFSKFGTVLKIITFTKNNQFQALLQYADPVNAHYAKMALDGQNIYNACCTLRIDFSKLTSLNVKYNNDKSRDFTRLDLPTGDGQPSLEPPMAAAFGAPGIISSPYAGAAGFAPAIGFPQA... | 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... | 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 ... | 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... | 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:2... | 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:... | 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 membr... | 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 ... | 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... | Homo sapiens (Human) |
O95782 | AP2A1_HUMAN | MPAVSKGDGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNKYTEKQIGYLFISVLVNSNSELIRLINNAIKNDLASRNPTFMCLALHCIANVGSREMGEAFAADIPRILVAGDSMDSVKQSAALCLLRLYKASPDLVPMGEWTARVVHLLNDQHMGVVTAAVSLITCLCKKNPDDFKTCVSLAVSRLSRIVSSASTDLQDYTYYFVPAPWLSVKLLRLLQCYPPPEDAAVKGRLVECLETVLNKAQEPPKSKKVQHSNAKNAILFETISLIIHY... | 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 re... | 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:00... | 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 nasc... | 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 i... | Homo sapiens (Human) |
O95785 | WIZ_HUMAN | MEGSLAGSLAAPDRPQGPERLPGPAPRENIEGGAEAAEGEGGIFRSTRYLPVTKEGPRDILDGRGGISGTPDGRGPWEHPLVQEAGEGILSERRFEDSVIVRTMKPHAELEGSRRFLHHRGEPRLLEKHAQGRPRFDWLQDEDEQGSPQDAGLHLDLPAQPPPLAPFRRVFVPVEDTPKTLDMAVVGGREDLEDLEGLAQPSEWGLPTSASEVATQTWTVNSEASVERLQPLLPPIRTGPYLCELLEEVAEGVASPDEDEDEEPAVFPCIECSIYFKQKEHLLEHMSQHRRAPGQEPPADLAPLACGECGWAFADPTALE... | 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 corepress... | 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 | MTTEQRRSLQAFQDYIRKTLDPTYILSYMAPWFREEEVQYIQAEKNNKGPMEAATLFLKFLLELQEEGWFRGFLDALDHAGYSGLYEAIESWDFKKIEKLEEYRLLLKRLQPEFKTRIIPTDIISDLSECLINQECEEILQICSTKGMMAGAEKLVECLLRSDKENWPKTLKLALEKERNKFSELWIVEKGIKDVETEDLEDKMETSDIQIFYQEDPECQNLSENSCPPSEVSDTNLYSPFKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGKVVFFANQIPVYEQQKSVFSKYFERHGYR... | 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 ... | 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 RN... | 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 RN... | 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|Pu... | 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,... | Homo sapiens (Human) |
O95789 | ZMYM6_HUMAN | MKEPLDGECGKAVVPQQELLDKIKEEPDNAQEYGCVQQPKTQESKLKIGGVSSVNERPIAQQLNPGFQLSFASSGPSVLLPSVPAVAIKVFCSGCKKMLYKGQTAYHKTGSTQLFCSTRCITRHSSPACLPPPPKKTCTNCSKDILNPKDVITTRFENSYPSKDFCSQSCLSSYELKKKPVVTIYTKSISTKCSMCQKNADTRFEVKYQNVVHGLCSDACFSKFHSTNNLTMNCCENCGSYCYSSSGPCQSQKVFSSTSVTAYKQNSAQIPPYALGKSLRPSAEMIETTNDSGKTELFCSINCLSAYRVKTVTSSGVQVS... | 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 | MSQVQVQVQNPSAALSGSQILNKNQSLLSQPLMSIPSTTSSLPSENAGRPIQNSALPSASITSTSAAAESITPTVELNALCMKLGKKPMYKPVDPYSRMQSTYNYNMRGGAYPPRYFYPFPVPPLLYQVELSVGGQQFNGKGKTRQAAKHDAAAKALRILQNEPLPERLEVNGRESEEENLNKSEISQVFEIALKRNLPVNFEVARESGPPHMKNFVTKVSVGEFVGEGEGKSKKISKKNAAIAVLEELKKLPPLPAVERVKPRIKKKTKPIVKPQTSPEYGQGINPISRLAQIQQAKKEKEPEYTLLTERGLPRRREFV... | 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 struct... | 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:009... | 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 p... | Homo sapiens (Human) |
O95801 | TTC4_HUMAN | MEQPGQDPTSDDVMDSFLEKFQSQPYRGGFHEDQWEKEFEKVPLFMSRAPSEIDPRENPDLACLQSIIFDEERSPEEQAKTYKDEGNDYFKEKDYKKAVISYTEGLKKKCADPDLNAVLYTNRAAAQYYLGNFRSALNDVTAARKLKPCHLKAIIRGALCHLELKHFAEAVNWCDEGLQIDAKEKKLLEMRAKADKLKRIEQRDVRKANLKEKKERNQNEALLQAIKARNIRLSEAACEDEDSASEGLGELFLDGLSTENPHGARLSLDGQGRLSWPVLFLYPEYAQSDFISAFHEDSRFIDHLMVMFGETPSWDLEQKY... | 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 pha... | 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 | MSFIMKLHRHFQRTVILLATFCMVSIIISAYYLYSGYKQENELSETASEVDCGDLQHLPYQLMEVKAMKLFDASRTDPTVLVFVESQYSSLGQDIIMILESSRFQYHIEIAPGKGDLPVLIDKMKGKYILIIYENILKYINMDSWNRSLLDKYCVEYGVGVIGFHKTSEKSVQSFQLKGFPFSIYGNLAVKDCCINPHSPLIRVTKSSKLEKGSLPGTDWTVFQINHSAYQPVIFAKVKTPENLSPSISKGAFYATIIHDLGLHDGIQRVLFGNNLNFWLHKLIFIDAISFLSGKRLTLSLDRYILVDIDDIFVGKEGTR... | 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... | 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 hepari... | 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 | MGEDAAQAEKFQHPGSDMRQEKPSSPSPMPSSTPSPSLNLGNTEEAIRDNSQVNAVTVLTLLDKLVNMLDAVQENQHKMEQRQISLEGSVKGIQNDLTKLSKYQASTSNTVSKLLEKSRKVSAHTRAVKERMDRQCAQVKRLENNHAQLLRRNHFKVLIFQEENEIPASVFVKQPVSGAVEGKEELPDENKSLEETLHTVDLSSDDDLPHDEEALEDSAEEKVEESRAEKIKRSSLKKVDSLKKAFSRQNIEKKMNKLGTKIVSVERREKIKKSLTSNHQKISSGKSSPFKVSPLTFGRKKVREGESHAENETKSEDLPS... | 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 hea... | 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/rig... | 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]; prote... | 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 | MSAATHSPMMQVASGNGDRDPLPPGWEIKIDPQTGWPFFVDHNSRTTTWNDPRVPSEGPKETPSSANGPSREGSRLPPAREGHPVYPQLRPGYIPIPVLHEGAENRQVHPFHVYPQPGMQRFRTEAAAAAPQRSQSPLRGMPETTQPDKQCGQVAAAAAAQPPASHGPERSQSPAASDCSSSSSSASLPSSGRSSLGSHQLPRGYISIPVIHEQNVTRPAAQPSFHQAQKTHYPAQQGEYQTHQPVYHKIQGDDWEPRPLRAASPFRSSVQGASSREGSPARSSTPLHSPSPIRVHTVVDRPQQPMTHRETAPVSQPENK... | 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 [... | 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/HSC... | Homo sapiens (Human) |
O95819 | M4K4_HUMAN | MANDSPAKSLVDIDLSSLRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKYSHHRNIATYYGAFIKKSPPGHDDQLWLVMEFCGAGSITDLVKNTKGNTLKEDWIAYISREILRGLAHLHIHHVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDLWSCGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSKKWSKKFFSFIEGCLVKNYMQRPSTEQLLKHPFIRDQPNERQVRIQLKDHIDRTRKKRGEKDETE... | 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 regulati... | 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 ... | 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 restrict... | Homo sapiens (Human) |
O95822 | DCMC_HUMAN | MRGFGPGLTARRLLPLRLPPRPPGPRLASGQAAGALERAMDELLRRAVPPTPAYELREKTPAPAEGQCADFVSFYGGLAETAQRAELLGRLARGFGVDHGQVAEQSAGVLHLRQQQREAAVLLQAEDRLRYALVPRYRGLFHHISKLDGGVRFLVQLRADLLEAQALKLVEGPDVREMNGVLKGMLSEWFSSGFLNLERVTWHSPCEVLQKISEAEAVHPVKNWMDMKRRVGPYRRCYFFSHCSTPGEPLVVLHVALTGDISSNIQAIVKEHPPSETEEKNKITAAIFYSISLTQQGLQGVELGTFLIKRVVKELQREFP... | 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:003199... | 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 expecte... | 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|PubM... | 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 cyto... | 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 i... | Homo sapiens (Human) |
O95825 | QORL1_HUMAN | MKGLYFQQSSTDEEITFVFQEKEDLPVTEDNFVKLQVKACALSQINTKLLAEMKMKKDLFPVGREIAGIVLDVGSKVSFFQPDDEVVGILPLDSEDPGLCEVVRVHEHYLVHKPEKVTWTEAAGSIRDGVRAYTALHYLSHLSPGKSVLIMDGASAFGTIAIQLAHHRGAKVISTACSLEDKQCLERFRPPIARVIDVSNGKVHVAESCLEETGGLGVDIVLDAGVRLYSKDDEPAVKLQLLPHKHDIITLLGVGGHWVTTEENLQLDPPDSHCLFLKGATLAFLNDEVWNLSNVQQGKYLCILKDVMEKLSTGVFRPQL... | 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 mediati... | Homo sapiens (Human) |
O95831 | AIFM1_HUMAN | MFRCGGLAAGALKQKLVPLVRTVCVRSPRQRNRLPGNLFQRWHVPLELQMTRQMASSGASGGKIDNSVLVLIVGLSTVGAGAYAYKTMKEDEKRYNERISGLGLTPEQKQKKAALSASEGEEVPQDKAPSHVPFLLIGGGTAAFAAARSIRARDPGARVLIVSEDPELPYMRPPLSKELWFSDDPNVTKTLRFKQWNGKERSIYFQPPSFYVSAQDLPHIENGGVAVLTGKKVVQLDVRDNMVKLNDGSQITYEKCLIATGGTPRSLSAIDRAGAEVKSRTTLFRKIGDFRSLEKISREVKSITIIGGGFLGSELACALG... | 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:007145... | 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 pro... | 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:0000... | 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 ... | 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:27... | 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... | 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 respons... | 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 ... | 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 membe... | 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 | MSSFGAGKTKEVIFSVEDGSVKMFLRGRPVPMMIPDELAPTYSLDTRSELPSCRLKLEWVYGYRGRDCRANLYLLPTGEIVYFVASVAVLYSVEEQRQRHYLGHNDDIKCLAIHPDMVTIATGQVAGTTKEGKPLPPHVRIWDSVSLSTLHVLGLGVFDRAVCCVGFSKSNGGNLLCAVDESNDHMLSVWDWAKETKVVDVKCSNEAVLVATFHPTDPTVLITCGKSHIYFWTLEGGSLSKRQGLFEKHEKPKYVLCVTFLEGGDVVTGDSGGNLYVWGKGGNRITQAVLGAHDGGVFGLCALRDGTLVSGGGRDRRVVL... | 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 | MKRSEKPEGYRQMRPKTFPASNYTVSSRQMLQEIRESLRNLSKPSDAAKAEHNMSKMSTEDPRQVRNPPKFGTHHKALQEIRNSLLPFANETNSSRSTSEVNPQMLQDLQAAGFDEDMVIQALQKTNNRSIEAAIEFISKMSYQDPRREQMAAAAARPINASMKPGNVQQSVNRKQSWKGSKESLVPQRHGPPLGESVAYHSESPNSQTDVGRPLSGSGISAFVQAHPSNGQRVNPPPPPQVRSVTPPPPPRGQTPPPRGTTPPPPSWEPNSQTKRYSGNMEYVISRISPVPPGAWQEGYPPPPLNTSPMNPPNQGQRGI... | 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 ce... | 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 (PubM... | 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:105... | 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:000026... | 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... | Homo sapiens (Human) |
O95837 | GNA14_HUMAN | MAGCCCLSAEEKESQRISAEIERQLRRDKKDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDRKGFTKLVYQNIFTAMQAMIRAMDTLRIQYVCEQNKENAQIIREVEVDKVSMLSREQVEAIKQLWQDPGIQECYDRRREYQLSDSAKYYLTDIDRIATPSFVPTQQDVLRVRVPTTGIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFESVTSIIFLVALSEYDQVLAECDNENRMEESKALFKTIITYPWFLNSSVILFLNKKDLLEEKIMYSHLISYFPEYTGPKQDVRAARDFILKLYQDQNPDKEKVI... | 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 ... | Homo sapiens (Human) |
O95847 | UCP4_HUMAN | MSVPEEEERLLPLTQRWPRASKFLLSGCAATVAELATFPLDLTKTRLQMQGEAALARLGDGARESAPYRGMVRTALGIIEEEGFLKLWQGVTPAIYRHVVYSGGRMVTYEHLREVVFGKSEDEHYPLWKSVIGGMMAGVIGQFLANPTDLVKVQMQMEGKRKLEGKPLRFRGVHHAFAKILAEGGIRGLWAGWVPNIQRAALVNMGDLTTYDTVKHYLVLNTPLEDNIMTHGLSSLCSGLVASILGTPADVIKSRIMNQPRDKQGRGLLYKSSTDCLIQAVQGEGFMSLYKGFLPSWLRMTPWSMVFWLTYEKIREMSGV... | 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... | 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 i... | 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:2... | 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 lacta... | 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... | 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 c... | 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) ... | 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|PubM... | 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:... | 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 th... | 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 follic... | 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-s... | 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 prom... | 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-10... | 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 KDM1... | Homo sapiens (Human) |
O95864 | FADS2_HUMAN | MGKGGNQGEGAAEREVSVPTFSWEEIQKHNLRTDRWLVIDRKVYNITKWSIQHPGGQRVIGHYAGEDATDAFRAFHPDLEFVGKFLKPLLIGELAPEEPSQDHGKNSKITEDFRALRKTAEDMNLFKTNHVFFLLLLAHIIALESIAWFTVFYFGNGWIPTLITAFVLATSQAQAGWLQHDYGHLSVYRKPKWNHLVHKFVIGHLKGASANWWNHRHFQHHAKPNIFHKDPDVNMLHVFVLGEWQPIEYGKKKLKYLPYNHQHEYFFLIGPPLLIPMYFQYQIIMTMIVHKNWVDLAWAVSYYIRFFITYIPFYGILGAL... | 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 aci... | 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:C... | 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 ... | 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}.... | 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 fac... | 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... | 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... | 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 | MAKLLSCVLGPRLYKIYRERDSERAPASVPETPTAVTAPHSSSWDTYYQPRALEKHADSILALASVFWSISYYSSPFAFFYLYRKGYLSLSKVVPFSHYAGTLLLLLAGVACLRGIGRWTNPQYRQFITILEATHRNQSSENKRQLANYNFDFRSWPVDFHWEEPSSRKESRGGPSRRGVALLRPEPLHRGTADTLLNRVKKLPCQITSYLVAHTLGRRMLYPGSVYLLQKALMPVLLQGQARLVEECNGRRAKLLACDGNEIDTMFVDRRGTAEPQGQKLVICCEGNAGFYEVGCVSTPLEAGYSVLGWNHPGFAGSTG... | 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; E... | 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)-p... | 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, triacylglycer... | Homo sapiens (Human) |
O95872 | GPAN1_HUMAN | MSRPLLITFTPATDPSDLWKDGQQQPQPEKPESTLDGAAARAFYEALIGDESSAPDSQRSQTEPARERKRKKRRIMKAPAAEAVAEGASGRHGQGRSLEAEDKMTHRILRAAQEGDLPELRRLLEPHEAGGAGGNINARDAFWWTPLMCAARAGQGAAVSYLLGRGAAWVGVCELSGRDAAQLAEEAGFPEVARMVRESHGETRSPENRSPTPSLQYCENCDTHFQDSNHRTSTAHLLSLSQGPQPPNLPLGVPISSPGFKLLLRGGWEPGMGLGPRGEGRANPIPTVLKRDQEGLGYRSAPQPRVTHFPAWDTRAVAGR... | 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 | MRREFCWDAYSKAAGSRASSPLPRQDRDSFCHQMSFCLTELHLWSLKNTLHIADRDIGIYQYYDKKDPPATEHGNLEKKQKLAESRDYPWTLKNRRPEKLRDSLKELEELMQNSRCVLSKWKNKYVCQLLFGSGVLVSLSLSGPQLEKVVIDRSLVGKLISDTISDALLTDSFIILSFLAQNKLCFIQFTKKMESSDVNKRLEKLSALDYKIFYYEIPGPINKTTERHLAINCVHDRVVCWWPLVNDDAWPWAPISSEKDRANLLLLGYAQGRLEVLSSVRTEWDPLDVRFGTKQPYQVFTVEHSVSVDKEPMADSCIYE... | 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 polarit... | 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 recr... | 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}; PhysiologicalDir... | 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 | MRGYHGDRGSHPRPARFADQQHMDVGPAARAPYLLGSREAFSTEPRFCAPRAGLGHISPEGPLSLSEGPSVGPEGGPAGAGVGGGSSTFPRMYPGQGPFDTCEDCVGHPQGKGAPRLPPTLLDQFEKQLPVQQDGFHTLPYQRGPAGAGPGPAPGTGTAPEPRSESPSRIRHLVHSVQKLFAKSHSLEAPGKRDYNGPKAEGRGGSGGDSYPGPGSGGPHTSHHHHHHHHHHHHQSRHGKRSKSKDRKGDGRHQAKSTGWWSSDDNLDSDSGFLAGGRPPGEPGGPFCLEGPDGSYRDLSFKGRSGGSEGRCLACTGMSM... | 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 | MWPLTVPPPLLLLLCSGLAGQTLFQNPEEGWQLYTSAQAPDGKCICTAVIPAQSTCSRDGRSRELRQLMEKVQNVSQSMEVLELRTYRDLQYVRGMETLMRSLDARLRAADGSLSAKSFQELKDRMTELLPLSSVLEQYKADTRTIVRLREEVRNLSGSLAAIQEEMGAYGYEDLQQRVMALEARLHACAQKLGCGKLTGVSNPITVRAMGSRFGSWMTDTMAPSADSRVWYMDGYYKGRRVLEFRTLGDFIKGQNFIQHLLPQPWAGTGHVVYNGSLFYNKYQSNVVVKYHFRSRSVLVQRSLPGAGYNNTFPYSWGGF... | 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 (Pub... | Homo sapiens (Human) |
O95900 | TRUB2_HUMAN | MGSAGLSRLHGLFAVYKPPGLKWKHLRDTVELQLLKGLNARKPPAPKQRVRFLLGPMEGSEEKELTLTATSVPSFINHPLVCGPAFAHLKVGVGHRLDAQASGVLVLGVGHGCRLLTDMYNAHLTKDYTVRGLLGKATDDFREDGRLVEKTTYDHVTREKLDRILAVIQGSHQKALVMYSNLDLKTQEAYEMAVRGLIRPMNKSPMLITGIRCLYFAPPEFLLEVQCMHETQKELRKLVHEIGLELKTTAVCTQVRRTRDGFFTLDSALLRTQWDLTNIQDAIRAATPQVAAELEKSLSPGLDTKQLPSPGWSWDSQGPS... | 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 t... | 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, FA... | Homo sapiens (Human) |
O95905 | ECD_HUMAN | MEETMKLATMEDTVEYCLFLIPDESRDSDKHKEILQKYIERIITRFAPMLVPYIWQNQPFNLKYKPGKGGVPAHMFGVTKFGDNIEDEWFIVYVIKQITKEFPELVARIEDNDGEFLLIEAADFLPKWLDPENSTNRVFFCHGELCIIPAPRKSGAESWLPTTPPTIPQALNIITAHSEKILASESIRAAVNRRIRGYPEKIQASLHRAHCFLPAGIVAVLKQRPRLVAAAVQAFYLRDPIDLRACRVFKTFLPETRIMTSVTFTKCLYAQLVQQRFVPDRRSGYRLPPPSDPQYRAHELGMKLAHGFEILCSKCSPHFS... | 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:19919... | 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 ac... | Homo sapiens (Human) |
O95907 | MOT3_HUMAN | MGAGGPRRGEGPPDGGWGWVVLGACFVVTGFAYGFPKAVSVFFRALMRDFDAGYSDTAWVSSIMLAMLYGTGPVSSILVTRFGCRPVMLAGGLLASAGMILASFATRLLELYLTAGVLTGLGLALNFQPSLIMLGLYFERRRPLANGLAAAGSPVFLSALSPLGQQLLERFGWRGGFLLLGGLLLHCCACGAVMRPPPGPGPRPRRDSAGDRAGDAPGEAEADGAGLQLREASPRVRPRRRLLDLAVCTDRAFAVYAVTKFLMALGLFVPAILLVNYAKDAGVPDTDAAFLLSIVGFVDIVARPACGALAGLARLRPHVP... | 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 e... | 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|UniP... | Homo sapiens (Human) |
O95922 | TTLL1_HUMAN | MAGKVKWVTDIEKSVLINNFEKRGWVQVTENEDWNFYWMSVQTIRNVFSVEAGYRLSDDQIVNHFPNHYELTRKDLMVKNIKRYRKELEKEGSPLAEKDENGKYLYLDFVPVTYMLPADYNLFVEEFRKSPSSTWIMKPCGKAQGKGIFLINKLSQIKKWSRDSKTSSFVSQSNKEAYVISLYINNPLLIGGRKFDLRLYVLVSTYRPLRCYMYKLGFCRFCTVKYTPSTSELDNMFVHLTNVAIQKHGEDYNHIHGGKWTVSNLRLYLESTRGKEVTSKLFDEIHWIIVQSLKAVAPVMNNDKHCFECYGYDIIIDDKL... | 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 axone... | 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:CHEB... | 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 r... | 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:1522... | 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 monoubiquitinatio... | Homo sapiens (Human) |
O95932 | TGM3L_HUMAN | MAGIRVTKVDWQRSRNGAAHHTQEYPCPELVVRRGQSFSLTLELSRALDCEEILIFTMETGPRASEALHTKAVFQTSELERGEGWTAAREAQMEKTLTVSLASPPSAVIGRYLLSIRLSSHRKHSNRRLGEFVLLFNPWCAEDDVFLASEEERQEYVLSDSGIIFRGVEKHIRAQGWNYGQFEEDILNICLSILDRSPGHQNNPATDVSCRHNPIYVTRVISAMVNSNNDRGVVQGQWQGKYGGGTSPLHWRGSVAILQKWLKGRYKPVKYGQCWVFAGVLCTVLRCLGIATRVVSNFNSAHDTDQNLSVDKYVDSFGRT... | 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... | 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 | MAEKRRGSPCSMLSLKAHAFSVEALIGAEKQQQLQKKRRKLGAEEAAGAVDDGGCSRGGGAGEKGSSEGDEGAALPPPAGATSGPARSGADLERGAAGGCEDGFQQGASPLASPGGSPKGSPARSLARPGTPLPSPQAPRVDLQGAELWKRFHEIGTEMIITKAGRRMFPAMRVKISGLDPHQQYYIAMDIVPVDNKRYRYVYHSSKWMVAGNADSPVPPRVYIHPDSPASGETWMRQVISFDKLKLTNNELDDQGHIILHSMHKYQPRVHVIRKDCGDDLSPIKPVPSGEGVKAFSFPETVFTTVTAYQNQQITRLKID... | 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:0... | 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... | 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|PubM... | Homo sapiens (Human) |
O95936 | EOMES_HUMAN | MQLGEQLLVSSVNLPGAHFYPLESARGGSGGSAGHLPSAAPSPQKLDLDKASKKFSGSLSCEAVSGEPAAASAGAPAAMLSDTDAGDAFASAAAVAKPGPPDGRKGSPCGEEELPSAAAAAAAAAAAAAATARYSMDSLSSERYYLQSPGPQGSELAAPCSLFPYQAAAGAPHGPVYPAPNGARYPYGSMLPPGGFPAAVCPPGRAQFGPGAGAGSGAGGSSGGGGGPGTYQYSQGAPLYGPYPGAAAAGSCGGLGGLGVPGSGFRAHVYLCNRPLWLKFHRHQTEMIITKQGRRMFPFLSFNINGLNPTAHYNVFVEVV... | 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];... | 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... | 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... | 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 | MYHPRELYPSLGAGYRLGPAQPGADSSFPPALAEGYRYPELDTPKLDCFLSGMEAAPRTLAAHPPLPLLPPAMGTEPAPSAPEALHSLPGVSLSLENRELWKEFSSVGTEMIITKAGRRMFPACRVSVTGLDPEARYLFLLDVIPVDGARYRWQGRRWEPSGKAEPRLPDRVYIHPDSPATGAHWMRQPVSFHRVKLTNSTLDPHGHLILHSMHKYQPRIHLVRAAQLCSQHWGGMASFRFPETTFISVTAYQNPQITQLKIAANPFAKGFRENGRNCKRERDARVKRKLRGPEPAATEAYGSGDTPGGPCDSTLGGDIR... | 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 [... | 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 bindin... | 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 t... | Homo sapiens (Human) |
O95948 | ONEC2_HUMAN | MKAAYTAYRCLTKDLEGCAMNPELTMESLGTLHGPAGGGSGGGGGGGGGGGGGGPGHEQELLASPSPHHAGRGAAGSLRGPPPPPTAHQELGTAAAAAAAASRSAMVTSMASILDGGDYRPELSIPLHHAMSMSCDSSPPGMGMSNTYTTLTPLQPLPPISTVSDKFHHPHPHHHPHHHHHHHHQRLSGNVSGSFTLMRDERGLPAMNNLYSPYKEMPGMSQSLSPLAATPLGNGLGGLHNAQQSLPNYGPPGHDKMLSPNFDAHHTAMLTRGEQHLSRGLGTPPAAMMSHLNGLHHPGHTQSHGPVLAPSRERPPSSSS... | 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... | 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 | MSQLVECVPNFSEGKNQEVIDAISGAITQTPGCVLLDVDAGPSTNRTVYTFVGPPECVVEGALNAARVASRLIDMSRHQGEHPRMGALDVCPFIPVRGVSVDECVLCAQAFGQRLAEELDVPVYLYGEAARMDSRRTLPAIRAGEYEALPKKLQQADWAPDFGPSSFVPSWGATATGARKFLIAFNINLLGTKEQAHRIALNLREQGRGKDQPGRLKKVQGIGWYLDEKNLAQVSTNLLDFEVTALHTVYEETCREAQELSLPVVGSQLVGLVPLKALLDAAAFYCEKENLFILEEEQRIRLVVSRLGLDSLCPFSPKER... | 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 ret... | 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... | 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 | MRPPGFRNFLLLASSLLFAGLSAVPQSFSPSLRSWPGAACRLSRAESERRCRAPGQPPGAALCHGRGRCDCGVCICHVTEPGMFFGPLCECHEWVCETYDGSTCAGHGKCDCGKCKCDQGWYGDACQYPTNCDLTKKKSNQMCKNSQDIICSNAGTCHCGRCKCDNSDGSGLVYGKFCECDDRECIDDETEEICGGHGKCYCGNCYCKAGWHGDKCEFQCDITPWESKRRCTSPDGKICSNRGTCVCGECTCHDVDPTGDWGDIHGDTCECDERDCRAVYDRYSDDFCSGHGQCNCGRCDCKAGWYGKKCEHPQSCTLSA... | 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 | MLPCASCLPGSLLLWALLLLLLGSASPQDSEEPDSYTECTDGYEWDPDSQHCRDVNECLTIPEACKGEMKCINHYGGYLCLPRSAAVINDLHGEGPPPPVPPAQHPNPCPPGYEPDDQDSCVDVDECAQALHDCRPSQDCHNLPGSYQCTCPDGYRKIGPECVDIDECRYRYCQHRCVNLPGSFRCQCEPGFQLGPNNRSCVDVNECDMGAPCEQRCFNSYGTFLCRCHQGYELHRDGFSCSDIDECSYSSYLCQYRCINEPGRFSCHCPQGYQLLATRLCQDIDECESGAHQCSEAQTCVNFHGGYRCVDTNRCVEPYI... | 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 coll... | 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 (P... | 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:Q9... | 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 i... | 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 | MESERSKRMGNACIPLKRIAYFLCLLSALLLTEGKKPAKPKCPAVCTCTKDNALCENARSIPRTVPPDVISLSFVRSGFTEISEGSFLFTPSLQLLLFTSNSFDVISDDAFIGLPHLEYLFIENNNIKSISRHTFRGLKSLIHLSLANNNLQTLPKDIFKGLDSLTNVDLRGNSFNCDCKLKWLVEWLGHTNATVEDIYCEGPPEYKKRKINSLSSKDFDCIITEFAKSQDLPYQSLSIDTFSYLNDEYVVIAQPFTGKCIFLEWDHVEKTFRNYDNITGTSTVVCKPIVIETQLYVIVAQLFGGSHIYKRDSFANKFIK... | 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 transmi... | 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:987999... | 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... | 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]; ne... | 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 mem... | 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 ... | Homo sapiens (Human) |
O95972 | BMP15_HUMAN | MVLLSILRILFLCELVLFMEHRAQMAEGGQSSIALLAEAPTLPLIEELLEESPGEQPRKPRLLGHSLRYMLELYRRSADSHGHPRENRTIGATMVRLVKPLTNVARPHRGTWHIQILGFPLRPNRGLYQLVRATVVYRHHLQLTRFNLSCHVEPWVQKNPTNHFPSSEGDSSKPSLMSNAWKEMDITQLVQQRFWNNKGHRILRLRFMCQQQKDSGGLELWHGTSSLDIAFLLLYFNDTHKSIRKAKFLPRGMEEFMERESLLRRTRQADGISAEVTASSSKHSGPENNQCSLHPFQISFRQLGWDHWIIAPPFYTPNYC... | 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 | MNATGTPVAPESCQQLAAGGHSRLIVLHYNHSGRLAGRGGPEDGGLGALRGLSVAASCLVVLENLLVLAAITSHMRSRRWVYYCLVNITLSDLLTGAAYLANVLLSGARTFRLAPAQWFLREGLLFTALAASTFSLLFTAGERFATMVRPVAESGATKTSRVYGFIGLCWLLAALLGMLPLLGWNCLCAFDRCSSLLPLYSKRYILFCLVIFAGVLATIMGLYGAIFRLVQASGQKAPRPAARRKARRLLKTVLMILLAFLVCWGPLFGLLLADVFGSNLWAQEYLRGMDWILALAVLNSAVNPIIYSFRSREVCRAVLS... | 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 met... | 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:107... | Homo sapiens (Human) |
O95980 | RECK_HUMAN | MATVRASLRGALLLLLAVAGVAEVAGGLAPGSAGALCCNHSKDNQMCRDVCEQIFSSKSESRLKHLLQRAPDYCPETMVEIWNCMNSSLPGVFKKSDGWVGLGCCELAIALECRQACKQASSKNDISKVCRKEYENALFSCISRNEMGSVCCSYAGHHTNCREYCQAIFRTDSSPGPSQIKAVENYCASISPQLIHCVNNYTQSYPMRNPTDSLYCCDRAEDHACQNACKRILMSKKTEMEIVDGLIEGCKTQPLPQDPLWQCFLESSQSVHPGVTVHPPPSTGLDGAKLHCCSKANTSTCRELCTKLYSMSWGNTQSWQ... | 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 [G... | 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). A... | 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:00001... | 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:0000... | 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 ... | Homo sapiens (Human) |
O95985 | TOP3B_HUMAN | MKTVLMVAEKPSLAQSIAKILSRGSLSSHKGLNGACSVHEYTGTFAGQPVRFKMTSVCGHVMTLDFLGKYNKWDKVDPAELFSQAPTEKKEANPKLNMVKFLQVEGRGCDYIVLWLDCDKEGENICFEVLDAVLPVMNKAHGGEKTVFRARFSSITDTDICNAMACLGEPDHNEALSVDARQELDLRIGCAFTRFQTKYFQGKYGDLDSSLISFGPCQTPTLGFCVERHDKIQSFKPETYWVLQAKVNTDKDRSLLLDWDRVRVFDREIAQMFLNMTKLEKEAQVEATSRKEKAKQRPLALNTVEMLRVASSSLGMGPQH... | 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... | 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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