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
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O00159 | MYO1C_HUMAN | MALQVELVPTGEIIRVVHPHRPCKLALGSDGVRVTMESALTARDRVGVQDFVLLENFTSEAAFIENLRRRFRENLIYTYIGPVLVSVNPYRDLQIYSRQHMERYRGVSFYEVPPHLFAVADTVYRALRTERRDQAVMISGESGAGKTEATKRLLQFYAETCPAPERGGAVRDRLLQSNPVLEAFGNAKTLRNDNSSRFGKYMDVQFDFKGAPVGGHILSYLLEKSRVVHQNHGERNFHIFYQLLEGGEEETLRRLGLERNPQSYLYLVKGQCAKVSSINDKSDWKVVRKALTVIDFTEDEVEDLLSIVASVLHLGNIHFAANEESNAQVTTENQLKYLTRLLSVEGSTLREALTHRKIIAKGEELLSPLNLEQAAYARDALAKAVYSRTFTWLVGKINRSLASKDVESPSWRSTTVLGLLDIYGFEVFQHNSFEQFCINYCNEKLQQLFIELTLKSEQEEYEAEGIAWEPVQYFNNKIICDLVEEKFKGIISILDEECLRPGEATDLTFLEKLEDTVKHHPHFLTHKLADQRTRKSLGRGEFRLLHYAGEVTYSVTGFLDKNNDLLFRNLKETMCSSKNPIMSQCFDRSELSDKKRPETVATQFKMSLLQLVEILQSKEPAYVRCIKPNDAKQPGRFDEVLIRHQVKYLGLLENLRVRRAGFAYRRKYEAFLQRYKSLCPETWPTWAGRPQDGVAVLVRHLGYKPEEYKMGRTKIFIRFPKTLFATEDALEVRRQSLATKIQAAWRGFHWRQKFLRVKRSAICIQSWWRGTLGRRKAAKRKWAAQTIRRLIRGFVLRHAPRCPENAFFLDHVRTSFLLNLRRQLPQNVLDTSWPTPPPALREASELLRELCIKNMVWKYCRSISPEWKQQLQQKAVASEIFKGKKDNYPQSVPRLFISTRLGTDEISPRVLQALGSEPIQYAVPVVKYDRKGYKPRSRQLLLTPNAVVIVEDAKVKQRIDYANLTGISVSSLSDSLFVLHVQRADNKQKGDVVLQSDHVIETLTKTALSANRVNSININQGSITFAGGPGRDGTIDFTPGSELLITKAKNGHLAVVAPRLNSR | null | null | actin filament organization [GO:0007015]; actin filament-based movement [GO:0030048]; cellular response to type II interferon [GO:0071346]; chromatin remodeling [GO:0006338]; endocytosis [GO:0006897]; positive regulation of cell migration [GO:0030335]; positive regulation of cellular response to insulin stimulus [GO:1900078]; positive regulation of protein targeting to membrane [GO:0090314]; positive regulation of transcription by RNA polymerase I [GO:0045943]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription by RNA polymerase III [GO:0045945]; protein targeting to membrane [GO:0006612]; regulation of bicellular tight junction assembly [GO:2000810]; vascular endothelial growth factor signaling pathway [GO:0038084]; vesicle transport along actin filament [GO:0030050] | actin cytoskeleton [GO:0015629]; B-WICH complex [GO:0110016]; basal plasma membrane [GO:0009925]; brush border [GO:0005903]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; filamentous actin [GO:0031941]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; membrane raft [GO:0045121]; microvillus [GO:0005902]; nuclear body [GO:0016604]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587]; stereocilium membrane [GO:0060171]; unconventional myosin complex [GO:0016461] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]; signaling receptor binding [GO:0005102]; small GTPase binding [GO:0031267] | PF00612;PF00063;PF06017; | 1.10.10.820;1.20.5.190;1.20.58.530;6.20.240.20;3.40.850.10;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | PTM: Isoform 2 contains a N-acetylmethionine at position 1. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22736583}. Nucleus {ECO:0000269|PubMed:22736583}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9WTI7}. Cell projection, stereocilium membrane {ECO:0000250|UniProtKB:Q92002}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q9WTI7}. Cell projection, ruffle membrane {ECO:0000269|PubMed:34380438}. Note=Colocalizes with CABP1 and CIB1 at cell margin, membrane ruffles and punctate regions on the cell membrane (By similarity). Colocalizes in adipocytes with GLUT4 at actin-based membranes (By similarity). Colocalizes with GLUT4 at insulin-induced ruffles at the cell membrane (By similarity). Localizes transiently at cell membrane to region known to be enriched in PIP2 (By similarity). Activation of phospholipase C results in its redistribution to the cytoplasm (By similarity). Colocalizes with RNA polymerase II (PubMed:22736583). Translocates to nuclear speckles upon exposure to inhibitors of RNA polymerase II transcription (PubMed:22736583). {ECO:0000250|UniProtKB:Q9WTI7, ECO:0000269|PubMed:22736583}.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus, nucleoplasm {ECO:0000269|PubMed:16133118}. Nucleus, nucleolus {ECO:0000269|PubMed:16133118, ECO:0000269|PubMed:16877530}. Note=Colocalizes with RNA polymerase II in the nucleus (By similarity). Colocalizes with RNA polymerase I in nucleoli (By similarity). In the nucleolus, is localized predominantly in dense fibrillar component (DFC) and in granular component (GC) (PubMed:16133118, PubMed:16877530). Accumulates strongly in DFC and GC during activation of transcription (PubMed:16133118). Colocalizes with transcription sites (By similarity). Colocalizes in the granular cortex at the periphery of the nucleolus with RPS6 (PubMed:16877530). Colocalizes in nucleoplasm with RPS6 and actin that are in contact with RNP particles (PubMed:16877530). Colocalizes with RPS6 at the nuclear pore level (PubMed:16877530). {ECO:0000250|UniProtKB:Q9WTI7, ECO:0000269|PubMed:16133118, ECO:0000269|PubMed:16877530}. | null | null | null | null | null | FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes. {ECO:0000269|PubMed:24636949}.; FUNCTION: [Isoform 3]: Involved in regulation of transcription. Associated with transcriptional active ribosomal genes. Appears to cooperate with the WICH chromatin-remodeling complex to facilitate transcription. Necessary for the formation of the first phosphodiester bond during transcription initiation. {ECO:0000250|UniProtKB:Q9WTI7}. | Homo sapiens (Human) |
O00160 | MYO1F_HUMAN | MGSKERFHWQSHNVKQSGVDDMVLLPQITEDAIAANLRKRFMDDYIFTYIGSVLISVNPFKQMPYFTDREIDLYQGAAQYENPPHIYALTDNMYRNMLIDCENQCVIISGESGAGKTVAAKYIMGYISKVSGGGEKVQHVKDIILQSNPLLEAFGNAKTVRNNNSSRFGKYFEIQFSRGGEPDGGKISNFLLEKSRVVMQNENERNFHIYYQLLEGASQEQRQNLGLMTPDYYYYLNQSDTYQVDGTDDRSDFGETLSAMQVIGIPPSIQQLVLQLVAGILHLGNISFCEDGNYARVESVDLLAFPAYLLGIDSGRLQEKLTSRKMDSRWGGRSESINVTLNVEQAAYTRDALAKGLYARLFDFLVEAINRAMQKPQEEYSIGVLDIYGFEIFQKNGFEQFCINFVNEKLQQIFIELTLKAEQEEYVQEGIRWTPIQYFNNKVVCDLIENKLSPPGIMSVLDDVCATMHATGGGADQTLLQKLQAAVGTHEHFNSWSAGFVIHHYAGKVSYDVSGFCERNRDVLFSDLIELMQTSEQAFLRMLFPEKLDGDKKGRPSTAGSKIKKQANDLVATLMRCTPHYIRCIKPNETKRPRDWEENRVKHQVEYLGLKENIRVRRAGFAYRRQFAKFLQRYAILTPETWPRWRGDERQGVQHLLRAVNMEPDQYQMGSTKVFVKNPESLFLLEEVRERKFDGFARTIQKAWRRHVAVRKYEEMREEASNILLNKKERRRNSINRNFVGDYLGLEERPELRQFLGKRERVDFADSVTKYDRRFKPIKRDLILTPKCVYVIGREKVKKGPEKGQVCEVLKKKVDIQALRGVSLSTRQDDFFILQEDAADSFLESVFKTEFVSLLCKRFEEATRRPLPLTFSDTLQFRVKKEGWGGGGTRSVTFSRGFGDLAVLKVGGRTLTVSVGDGLPKSSKPTRKGMAKGKPRRSSQAPTRAAPAPPRGMDRNGVPPSARGGPLPLEIMSGGGTHRPPRGPPSTSLGASRRPRARPPSEHNTEFLNVPDQGMAGMQRKRSVGQRPVPGVGRPKPQPRTHGPRCRALYQYVGQDVDELSFNVNEVIEILMEDPSGWWKGRLHGQEGLFPGNYVEKI | null | null | actin filament organization [GO:0007015]; endocytosis [GO:0006897]; vesicle transport along actin filament [GO:0030050] | actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; microvillus [GO:0005902]; plasma membrane [GO:0005886]; unconventional myosin complex [GO:0016461]; vesicle [GO:0031982] | actin binding [GO:0003779]; actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146] | PF00063;PF06017;PF00018; | 1.10.10.820;1.20.5.4820;1.20.58.530;3.40.850.10;1.20.120.720;2.30.30.40; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | null | null | null | null | null | null | FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
O00161 | SNP23_HUMAN | MDNLSSEEIQQRAHQITDESLESTRRILGLAIESQDAGIKTITMLDEQKEQLNRIEEGLDQINKDMRETEKTLTELNKCCGLCVCPCNRTKNFESGKAYKTTWGDGGENSPCNVVSKQPGPVTNGQLQQPTTGAASGGYIKRITNDAREDEMEENLTQVGSILGNLKDMALNIGNEIDAQNPQIKRITDKADTNRDRIDIANARAKKLIDS | null | null | exocytosis [GO:0006887]; histamine secretion by mast cell [GO:0002553]; membrane fusion [GO:0061025]; post-Golgi vesicle-mediated transport [GO:0006892]; protein transport [GO:0015031]; synaptic vesicle fusion to presynaptic active zone membrane [GO:0031629]; synaptic vesicle priming [GO:0016082]; vesicle targeting [GO:0006903] | adherens junction [GO:0005912]; azurophil granule [GO:0042582]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; presynapse [GO:0098793]; SNARE complex [GO:0031201]; specific granule [GO:0042581]; specific granule membrane [GO:0035579]; synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex [GO:0070032]; tertiary granule membrane [GO:0070821] | SNAP receptor activity [GO:0005484]; syntaxin binding [GO:0019905]; syntaxin-1 binding [GO:0017075] | PF00835; | 1.20.5.110; | SNAP-25 family | null | SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cell membrane; Lipid-anchor. Synapse, synaptosome. Note=Mainly localized to the plasma membrane. | null | null | null | null | null | FUNCTION: Essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion. | Homo sapiens (Human) |
O00165 | HAX1_HUMAN | MSLFDLFRGFFGFPGPRSHRDPFFGGMTRDEDDDEEEEEEGGSWGRGNPRFHSPQHPPEEFGFGFSFSPGGGIRFHDNFGFDDLVRDFNSIFSDMGAWTLPSHPPELPGPESETPGERLREGQTLRDSMLKYPDSHQPRIFGGVLESDARSESPQPAPDWGSQRPFHRFDDVWPMDPHPRTREDNDLDSQVSQEGLGPVLQPQPKSYFKSISVTKITKPDGIVEERRTVVDSEGRTETTVTRHEADSSPRGDPESPRPPALDDAFSILDLFLGRWFRSR | null | null | cellular response to cytokine stimulus [GO:0071345]; granulocyte colony-stimulating factor signaling pathway [GO:0038158]; negative regulation of apoptotic process [GO:0043066]; positive regulation of granulocyte differentiation [GO:0030854]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of actin filament organization [GO:0110053]; regulation of actin filament polymerization [GO:0030833]; regulation of apoptotic process [GO:0042981]; regulation of autophagy of mitochondrion [GO:1903146]; regulation of protein targeting to mitochondrion [GO:1903214] | actin cytoskeleton [GO:0015629]; apical plasma membrane [GO:0016324]; cell cortex [GO:0005938]; clathrin-coated vesicle [GO:0030136]; endoplasmic reticulum [GO:0005783]; lamellipodium [GO:0030027]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; P-body [GO:0000932]; sarcoplasmic reticulum [GO:0016529]; transcription regulator complex [GO:0005667] | interleukin-1 binding [GO:0019966]; signaling adaptor activity [GO:0035591] | null | null | HAX1 family | PTM: Proteolytically cleaved by caspase-3 during apoptosis. {ECO:0000269|PubMed:18319618}. | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:18971376, ECO:0000269|PubMed:9058808}. Endoplasmic reticulum {ECO:0000269|PubMed:18971376, ECO:0000269|PubMed:9058808}. Nucleus membrane {ECO:0000269|PubMed:9058808}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:O35387}. Cytoplasm, cell cortex {ECO:0000269|PubMed:26997484}. Cell membrane {ECO:0000269|PubMed:26997484}; Peripheral membrane protein {ECO:0000269|PubMed:26997484}; Cytoplasmic side {ECO:0000269|PubMed:26997484}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:Q7TSE9}. Cytoplasm, P-body {ECO:0000269|PubMed:23164465}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:23164465, ECO:0000269|PubMed:25298122}. Nucleus {ECO:0000269|PubMed:23164465}. Note=Predominantly cytoplasmic. Also detected in the nucleus when nuclear export is inhibited, and in response to cellular stress caused by arsenite (in vitro). {ECO:0000269|PubMed:23164465}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:23164465}. Nucleus {ECO:0000269|PubMed:23164465}. Note=Predominantly cytoplasmic. Also detected in the nucleus when nuclear export is inhibited (in vitro). {ECO:0000269|PubMed:23164465}.; SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm {ECO:0000269|PubMed:23164465}. Nucleus {ECO:0000269|PubMed:23164465}. Note=Shuttles between nucleus and cytoplasm. {ECO:0000269|PubMed:23164465}.; SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm {ECO:0000269|PubMed:23164465}. Note=Predominantly cytoplasmic. {ECO:0000269|PubMed:23164465}. | null | null | null | null | null | FUNCTION: Recruits the Arp2/3 complex to the cell cortex and regulates reorganization of the cortical actin cytoskeleton via its interaction with KCNC3 and the Arp2/3 complex (PubMed:26997484). Slows down the rate of inactivation of KCNC3 channels (PubMed:26997484). Promotes GNA13-mediated cell migration. Involved in the clathrin-mediated endocytosis pathway. May be involved in internalization of ABC transporters such as ABCB11. May inhibit CASP9 and CASP3. Promotes cell survival. May regulate intracellular calcium pools. {ECO:0000269|PubMed:15339924, ECO:0000269|PubMed:16857965, ECO:0000269|PubMed:17545607, ECO:0000269|PubMed:18319618, ECO:0000269|PubMed:18971376, ECO:0000269|PubMed:26997484, ECO:0000269|PubMed:9058808}. | Homo sapiens (Human) |
O00167 | EYA2_HUMAN | MVELVISPSLTVNSDCLDKLKFNRADAAVWTLSDRQGITKSAPLRVSQLFSRSCPRVLPRQPSTAMAAYGQTQYSAGIQQATPYTAYPPPAQAYGIPSYSIKTEDSLNHSPGQSGFLSYGSSFSTSPTGQSPYTYQMHGTTGFYQGGNGLGNAAGFGSVHQDYPSYPGFPQSQYPQYYGSSYNPPYVPASSICPSPLSTSTYVLQEASHNVPNQSSESLAGEYNTHNGPSTPAKEGDTDRPHRASDGKLRGRSKRSSDPSPAGDNEIERVFVWDLDETIIIFHSLLTGTFASRYGKDTTTSVRIGLMMEEMIFNLADTHLFFNDLEDCDQIHVDDVSSDDNGQDLSTYNFSADGFHSSAPGANLCLGSGVHGGVDWMRKLAFRYRRVKEMYNTYKNNVGGLIGTPKRETWLQLRAELEALTDLWLTHSLKALNLINSRPNCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKTGKESCFERIMQRFGRKAVYVVIGDGVEEEQGAKKHNMPFWRISCHADLEALRHALELEYL | 3.1.3.48 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19858093}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:19858093}; | cell differentiation [GO:0030154]; DNA repair [GO:0006281]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; mesodermal cell fate specification [GO:0007501]; mitochondrial outer membrane permeabilization [GO:0097345]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; positive regulation of DNA repair [GO:0045739]; striated muscle tissue development [GO:0014706] | cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | histone H2AXY142 phosphatase activity [GO:0140793]; magnesium ion binding [GO:0000287]; protein tyrosine phosphatase activity [GO:0004725] | PF00702; | 3.40.50.12350; | HAD-like hydrolase superfamily, EYA family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10906137, ECO:0000269|PubMed:12500905}. Nucleus {ECO:0000269|PubMed:10906137, ECO:0000269|PubMed:12500905, ECO:0000269|PubMed:19497856}. Note=Retained in the cytoplasm via interaction with GNAZ and GNAI2 (PubMed:10906137). Interaction with SIX1, SIX2, SIX4 or SIX5 is required for translocation to the nucleus (PubMed:10906137, PubMed:12500905). {ECO:0000269|PubMed:10906137, ECO:0000269|PubMed:12500905}. | 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:0000269|PubMed:19351884}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.9 uM for H2AXY142ph {ECO:0000269|PubMed:19351884}; KM=80 uM for H2AXS139ph {ECO:0000269|PubMed:19351884}; | null | null | null | FUNCTION: Functions both as protein phosphatase and as transcriptional coactivator for SIX1, and probably also for SIX2, SIX4 and SIX5 (PubMed:12500905, PubMed:23435380). Tyrosine phosphatase that dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph) and promotes efficient DNA repair via the recruitment of DNA repair complexes containing MDC1. '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 (PubMed:19351884). Its function as histone phosphatase may contribute to its function in transcription regulation during organogenesis. Plays an important role in hypaxial muscle development together with SIX1 and DACH2; in this it is functionally redundant with EYA1 (PubMed:12500905). {ECO:0000269|PubMed:12500905, ECO:0000269|PubMed:19351884, ECO:0000269|PubMed:21706047, ECO:0000269|PubMed:23435380}. | Homo sapiens (Human) |
O00168 | PLM_HUMAN | MASLGHILVFCVGLLTMAKAESPKEHDPFTYDYQSLQIGGLVIAGILFILGILIVLSRRCRCKFNQQQRTGEPDEEEGTFRSSIRRLSTRRR | null | null | chloride transport [GO:0006821]; muscle contraction [GO:0006936]; negative regulation of protein glutathionylation [GO:0010734]; positive regulation of sodium ion export across plasma membrane [GO:1903278]; potassium ion transport [GO:0006813]; regulation of cardiac muscle cell membrane potential [GO:0086036]; regulation of heart contraction [GO:0008016]; regulation of sodium ion transmembrane transporter activity [GO:2000649]; sodium ion transport [GO:0006814] | apical plasma membrane [GO:0016324]; caveola [GO:0005901]; intercalated disc [GO:0014704]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; sodium:potassium-exchanging ATPase complex [GO:0005890]; T-tubule [GO:0030315] | chloride channel activity [GO:0005254]; sodium channel regulator activity [GO:0017080]; transmembrane transporter binding [GO:0044325] | PF02038; | 1.20.5.780; | FXYD family | PTM: Major plasma membrane substrate for cAMP-dependent protein kinase (PKA) and protein kinase C (PKC) in several different tissues (By similarity). Phosphorylated in response to insulin and adrenergic stimulation (By similarity). Phosphorylation at Ser-88 stimulates sodium/potassium-transporting ATPase activity while the unphosphorylated form inhibits sodium/potassium-transporting ATPase activity (By similarity). Phosphorylation increases tetramerization, decreases binding to ATP1A1 and reduces inhibition of ATP1A1 activity (By similarity). Phosphorylation at Ser-83 leads to greatly reduced interaction with ATP1A1, ATP1A2 and ATP1A3 (By similarity). May be phosphorylated by DMPK (PubMed:10811636). {ECO:0000250|UniProtKB:O08589, ECO:0000250|UniProtKB:P56513, ECO:0000269|PubMed:10811636}.; PTM: Palmitoylation increases half-life and stability and is enhanced upon phosphorylation at Ser-88 by PKA. {ECO:0000269|PubMed:21868384}. | SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P56513}; Single-pass type I membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:O08589}; Single-pass type I membrane protein {ECO:0000255}. Membrane, caveola {ECO:0000250|UniProtKB:O08589}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:O08589}. Note=Detected in the apical cell membrane in brain. In myocytes, localizes to sarcolemma, t-tubules and intercalated disks. {ECO:0000250|UniProtKB:O08589}. | null | null | null | null | null | FUNCTION: Associates with and regulates the activity of the sodium/potassium-transporting ATPase (NKA) which transports Na(+) out of the cell and K(+) into the cell. Inhibits NKA activity in its unphosphorylated state and stimulates activity when phosphorylated. Reduces glutathionylation of the NKA beta-1 subunit ATP1B1, thus reversing glutathionylation-mediated inhibition of ATP1B1. Contributes to female sexual development by maintaining the excitability of neurons which secrete gonadotropin-releasing hormone. {ECO:0000250|UniProtKB:O08589, ECO:0000250|UniProtKB:P56513, ECO:0000250|UniProtKB:Q9Z239}. | Homo sapiens (Human) |
O00170 | AIP_HUMAN | MADIIARLREDGIQKRVIQEGRGELPDFQDGTKATFHYRTLHSDDEGTVLDDSRARGKPMELIIGKKFKLPVWETIVCTMREGEIAQFLCDIKHVVLYPLVAKSLRNIAVGKDPLEGQRHCCGVAQMREHSSLGHADLDALQQNPQPLIFHMEMLKVESPGTYQQDPWAMTDEEKAKAVPLIHQEGNRLYREGHVKEAAAKYYDAIACLKNLQMKEQPGSPEWIQLDQQITPLLLNYCQCKLVVEEYYEVLDHCSSILNKYDDNVKAYFKRGKAHAAVWNAQEAQADFAKVLELDPALAPVVSRELRALEARIRQKDEEDKARFRGIFSH | null | null | protein maturation by protein folding [GO:0022417]; protein targeting to mitochondrion [GO:0006626]; regulation of protein kinase A signaling [GO:0010738]; xenobiotic metabolic process [GO:0006805] | aryl hydrocarbon receptor complex [GO:0034751]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654] | aryl hydrocarbon receptor binding [GO:0017162]; GAF domain binding [GO:0036004]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; transcription coactivator activity [GO:0003713]; unfolded protein binding [GO:0051082] | PF00254; | 3.10.50.40;1.25.40.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: May play a positive role in AHR-mediated (aromatic hydrocarbon receptor) signaling, possibly by influencing its receptivity for ligand and/or its nuclear targeting.; FUNCTION: Cellular negative regulator of the hepatitis B virus (HBV) X protein. | Homo sapiens (Human) |
O00175 | CCL24_HUMAN | MAGLMTIVTSLLFLGVCAHHIIPTGSVVIPSPCCMFFVSKRIPENRVVSYQLSSRSTCLKAGVIFTTKKGQQFCGDPKQEWVQRYMKNLDAKQKKASPRARAVAVKGPVQRYPGNQTTC | null | null | cell-cell signaling [GO:0007267]; cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interferon [GO:0071346]; chemokine-mediated signaling pathway [GO:0070098]; chemotaxis [GO:0006935]; cytoskeleton organization [GO:0007010]; eosinophil chemotaxis [GO:0048245]; G protein-coupled receptor signaling pathway [GO:0007186]; immune response [GO:0006955]; inflammatory response [GO:0006954]; lymphocyte chemotaxis [GO:0048247]; monocyte chemotaxis [GO:0002548]; neutrophil chemotaxis [GO:0030593]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cell migration [GO:0030335]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of eosinophil migration [GO:2000418]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of GTPase activity [GO:0043547]; positive regulation of inflammatory response [GO:0050729]; regulation of cell shape [GO:0008360]; signal transduction [GO:0007165] | extracellular space [GO:0005615] | CCR chemokine receptor binding [GO:0048020]; CCR3 chemokine receptor binding [GO:0031728]; chemokine activity [GO:0008009]; receptor ligand activity [GO:0048018] | PF00048; | 2.40.50.40; | Intercrine beta (chemokine CC) family | PTM: N-glycosylated. {ECO:0000269|PubMed:9104803}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9104803, ECO:0000269|PubMed:9365122}. | null | null | null | null | null | FUNCTION: Chemotactic for resting T-lymphocytes, and eosinophils (PubMed:9104803, PubMed:9365122). Has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes (PubMed:9104803, PubMed:9365122). Is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line (PubMed:9104803, PubMed:9365122). Binds to CCR3 (PubMed:9104803, PubMed:9365122). {ECO:0000269|PubMed:9104803, ECO:0000269|PubMed:9365122}. | Homo sapiens (Human) |
O00178 | GTPB1_HUMAN | MATERSRSAMDSPVPASMFAPEPSSPGAARAAAAAARLHGGFDSDCSEDGEALNGEPELDLTSKLVLVSPTSEQYDSLLRQMWERMDEGCGETIYVIGQGSDGTEYGLSEADMEASYATVKSMAEQIEADVILLRERQEAGGRVRDYLVRKRVGDNDFLEVRVAVVGNVDAGKSTLLGVLTHGELDNGRGFARQKLFRHKHEIESGRTSSVGNDILGFDSEGNVVNKPDSHGGSLEWTKICEKSTKVITFIDLAGHEKYLKTTVFGMTGHLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPANILQETLKLLQRLLKSPGCRKIPVLVQSKDDVIVTASNFSSERMCPIFQISNVTGENLDLLKMFLNLLSPRTSYREEEPAEFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGPDPLGNFLSIAVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRKGMVMVSPRLNPQASWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMDKDCLRTGDKATVHFRFIKTPEYLHIDQRLVFREGRTKAVGTITKLLQTTNNSPMNSKPQQIKMQSTKKGPLTKRDEGGPSGGPAVGAPPPGDEASSVGAGQPAASSNLQPQPKPSSGGRRRGGQRHKVKSQGACVTPASGC | null | null | cytoplasmic translation [GO:0002181]; GTP metabolic process [GO:0046039]; immune response [GO:0006955]; positive regulation of mRNA catabolic process [GO:0061014]; signal transduction [GO:0007165]; translational elongation [GO:0006414] | cytoplasmic exosome (RNase complex) [GO:0000177]; cytosol [GO:0005829]; membrane [GO:0016020] | alpha-aminoacyl-tRNA binding [GO:1904678]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; RNA binding [GO:0003723]; translation elongation factor activity [GO:0003746]; tRNA binding [GO:0000049] | PF00009;PF03144; | 3.40.50.300;2.40.30.10; | TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, GTPBP1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Promotes degradation of target mRNA species. Plays a role in the regulation of circadian mRNA stability. Binds GTP and has GTPase activity (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
O00180 | KCNK1_HUMAN | MLQSLAGSSCVRLVERHRSAWCFGFLVLGYLLYLVFGAVVFSSVELPYEDLLRQELRKLKRRFLEEHECLSEQQLEQFLGRVLEASNYGVSVLSNASGNWNWDFTSALFFASTVLSTTGYGHTVPLSDGGKAFCIIYSVIGIPFTLLFLTAVVQRITVHVTRRPVLYFHIRWGFSKQVVAIVHAVLLGFVTVSCFFFIPAAVFSVLEDDWNFLESFYFCFISLSTIGLGDYVPGEGYNQKFRELYKIGITCYLLLGLIAMLVVLETFCELHELKKFRKMFYVKKDKDEDQVHIIEHDQLSFSSITDQAAGMKEDQKQNEPFVATQSSACVDGPANH | null | null | potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; regulation of resting membrane potential [GO:0060075]; response to nicotine [GO:0035094]; sodium ion transmembrane transport [GO:0035725]; stabilization of membrane potential [GO:0030322] | apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]; dendrite [GO:0030425]; intracellular membrane-bounded organelle [GO:0043231]; inward rectifier potassium channel complex [GO:1902937]; membrane [GO:0016020]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; potassium channel complex [GO:0034705]; recycling endosome [GO:0055037]; synaptic membrane [GO:0097060]; voltage-gated potassium channel complex [GO:0008076] | identical protein binding [GO:0042802]; inward rectifier potassium channel activity [GO:0005242]; outward rectifier potassium channel activity [GO:0015271]; potassium channel activity [GO:0005267]; potassium ion leak channel activity [GO:0022841]; sodium channel activity [GO:0005272] | PF07885; | 1.10.287.70; | Two pore domain potassium channel (TC 1.A.1.8) family | PTM: Sumoylation is controversial. Sumoylated by UBE2I (PubMed:15820677). Not sumoylated when expressed in xenopus oocytes or mammalian cells (PubMed:17693262). Sumoylation inactivates the channel, but does not interfere with expression at the cell membrane (PubMed:15820677). Sumoylation of a single subunit is sufficient to silence the dimeric channel (PubMed:20498050, PubMed:23169818). Sumoylation of KCNK1 is sufficient to silence heterodimeric channels formed by KCNK1 and KCNK3 or KCNK9 (PubMed:23169818). Desumoylated by SENP1; this activates the channel (PubMed:15820677, PubMed:20498050, PubMed:23169818). Desumoylated by SENP1; this strongly increases halothane-mediated activation of heterodimeric channels formed with KCNK9 (PubMed:23169818). SENP1 treatment has no effect (PubMed:17693262). {ECO:0000269|PubMed:15820677, ECO:0000269|PubMed:17693262, ECO:0000269|PubMed:20498050, ECO:0000269|PubMed:23169818}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15820677, ECO:0000269|PubMed:17693262, ECO:0000269|PubMed:20498050, ECO:0000269|PubMed:21653227, ECO:0000269|PubMed:22282804, ECO:0000269|PubMed:22431633, ECO:0000269|PubMed:23169818, ECO:0000269|PubMed:25001086, ECO:0000269|PubMed:8605869, ECO:0000269|PubMed:8978667}; Multi-pass membrane protein {ECO:0000269|PubMed:22282804, ECO:0000269|PubMed:8978667, ECO:0000305}. Recycling endosome {ECO:0000269|PubMed:19959478}. Synaptic cell membrane {ECO:0000250|UniProtKB:Q9Z2T2}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:O08581}. Perikaryon {ECO:0000250|UniProtKB:O08581}. Cell projection, dendrite {ECO:0000250|UniProtKB:O08581}. Cell projection {ECO:0000250|UniProtKB:O08581}. Apical cell membrane {ECO:0000269|PubMed:21964404}; Multi-pass membrane protein {ECO:0000305}. Note=The heterodimer with KCNK2 is detected at the astrocyte cell membrane. Not detected at the astrocyte cell membrane when KCNK2 is absent. Detected on neuronal cell bodies, and to a lesser degree on neuronal cell projections. Detected on hippocampus dentate gyrus granule cell bodies and to a lesser degree on proximal dendrites. Detected at the apical cell membrane in stria vascularis in the cochlea. Detected at the apical cell membrane of vestibular dark cells situated between the crista and the utricle in the inner ear. Detected at the apical cell membrane in kidney proximal tubule segment S1 and in subapical compartments in segments S1, S2 and S3. Predominantly in cytoplasmic structures in kidney distal convoluted tubules and collecting ducts (By similarity). Detected at the apical cell membrane of bronchial epithelial cells (PubMed:21964404). {ECO:0000250|UniProtKB:O08581, ECO:0000250|UniProtKB:Q9Z2T2, ECO:0000269|PubMed:21964404}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=Has a unit conductance of 34 pS. Both activation and channel closure are very rapid. Is not voltage-gated. The relationship between voltage and current is nearly linear. Has a mean open time of 0.3 msec at a membrane potential of -80 mV, and 1.9 msec at +80 mV (PubMed:8605869). {ECO:0000269|PubMed:19959478, ECO:0000269|PubMed:8605869}; | null | null | null | FUNCTION: Ion channel that contributes to passive transmembrane potassium transport and to the regulation of the resting membrane potential in brain astrocytes, but also in kidney and in other tissues (PubMed:15820677, PubMed:21653227). Forms dimeric channels through which potassium ions pass in accordance with their electrochemical gradient. The channel is selective for K(+) ions at physiological potassium concentrations and at neutral pH, but becomes permeable to Na(+) at subphysiological K(+) levels and upon acidification of the extracellular medium (PubMed:21653227, PubMed:22431633). The homodimer has very low potassium channel activity, when expressed in heterologous systems, and can function as weakly inward rectifying potassium channel (PubMed:15820677, PubMed:21653227, PubMed:22431633, PubMed:23169818, PubMed:25001086, PubMed:8605869, PubMed:8978667). Channel activity is modulated by activation of serotonin receptors (By similarity). Heterodimeric channels containing KCNK1 and KCNK2 have much higher activity, and may represent the predominant form in astrocytes (By similarity). Heterodimeric channels containing KCNK1 and KCNK3 or KCNK9 have much higher activity (PubMed:23169818). Heterodimeric channels formed by KCNK1 and KCNK9 may contribute to halothane-sensitive currents (PubMed:23169818). Mediates outward rectifying potassium currents in dentate gyrus granule cells and contributes to the regulation of their resting membrane potential (By similarity). Contributes to the regulation of action potential firing in dentate gyrus granule cells and down-regulates their intrinsic excitability (By similarity). In astrocytes, the heterodimer formed by KCNK1 and KCNK2 is required for rapid glutamate release in response to activation of G-protein coupled receptors, such as F2R and CNR1 (By similarity). Required for normal ion and water transport in the kidney (By similarity). Contributes to the regulation of the resting membrane potential of pancreatic beta cells (By similarity). The low channel activity of homodimeric KCNK1 may be due to sumoylation (PubMed:15820677, PubMed:20498050, PubMed:23169818). The low channel activity may be due to rapid internalization from the cell membrane and retention in recycling endosomes (PubMed:19959478). {ECO:0000250|UniProtKB:O08581, ECO:0000250|UniProtKB:Q9Z2T2, ECO:0000269|PubMed:15820677, ECO:0000269|PubMed:17693262, ECO:0000269|PubMed:19959478, ECO:0000269|PubMed:20498050, ECO:0000269|PubMed:21653227, ECO:0000269|PubMed:22282804, ECO:0000269|PubMed:22431633, ECO:0000269|PubMed:23169818, ECO:0000269|PubMed:25001086, ECO:0000269|PubMed:8605869, ECO:0000269|PubMed:8978667}. | Homo sapiens (Human) |
O00182 | LEG9_HUMAN | MAFSGSQAPYLSPAVPFSGTIQGGLQDGLQITVNGTVLSSSGTRFAVNFQTGFSGNDIAFHFNPRFEDGGYVVCNTRQNGSWGPEERKTHMPFQKGMPFDLCFLVQSSDFKVMVNGILFVQYFHRVPFHRVDTISVNGSVQLSYISFQNPRTVPVQPAFSTVPFSQPVCFPPRPRGRRQKPPGVWPANPAPITQTVIHTVQSAPGQMFSTPAIPPMMYPHPAYPMPFITTILGGLYPSKSILLSGTVLPSAQRFHINLCSGNHIAFHLNPRFDENAVVRNTQIDNSWGSEERSLPRKMPFVRGQSFSVWILCEAHCLKVAVDGQHLFEYYHRLRNLPTINRLEVGGDIQLTHVQT | null | null | cellular response to type II interferon [GO:0071346]; cellular response to virus [GO:0098586]; chemotaxis [GO:0006935]; ERK1 and ERK2 cascade [GO:0070371]; female pregnancy [GO:0007565]; inflammatory response [GO:0006954]; maternal process involved in female pregnancy [GO:0060135]; natural killer cell tolerance induction [GO:0002519]; negative regulation of activated T cell proliferation [GO:0046007]; negative regulation of CD4-positive, alpha-beta T cell proliferation [GO:2000562]; negative regulation of chemokine production [GO:0032682]; negative regulation of gene expression [GO:0010629]; negative regulation of mast cell degranulation [GO:0043305]; negative regulation of natural killer cell mediated cytotoxicity [GO:0045953]; negative regulation of tumor necrosis factor production [GO:0032720]; negative regulation of type II interferon production [GO:0032689]; p38MAPK cascade [GO:0038066]; positive regulation of activated T cell autonomous cell death [GO:0070241]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of CD4-positive, alpha-beta T cell proliferation [GO:2000563]; positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation involved in immune response [GO:0032834]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:2001269]; positive regulation of dendritic cell apoptotic process [GO:2000670]; positive regulation of dendritic cell chemotaxis [GO:2000510]; positive regulation of dendritic cell differentiation [GO:2001200]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of gene expression [GO:0010628]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of interleukin-10 production [GO:0032733]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of interleukin-13 production [GO:0032736]; positive regulation of interleukin-4 production [GO:0032753]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of monocyte chemotactic protein-1 production [GO:0071639]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell [GO:2001190]; positive regulation of transforming growth factor beta production [GO:0071636]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of type II interferon production [GO:0032729]; positive regulation of viral entry into host cell [GO:0046598]; response to interleukin-1 [GO:0070555]; response to lipopolysaccharide [GO:0032496] | collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleus [GO:0005634] | carbohydrate binding [GO:0030246]; disaccharide binding [GO:0048030]; enzyme binding [GO:0019899]; galactose binding [GO:0005534]; galactoside binding [GO:0016936] | PF00337; | 2.60.120.200; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23242525}. Nucleus {ECO:0000269|PubMed:23242525}. Secreted {ECO:0000269|PubMed:23817958, ECO:0000269|PubMed:25578313}. Note=May also be secreted by a non-classical secretory pathway (By similarity). Secreted by mesenchymal stromal cells upon IFNG stimulation (PubMed:23817958). {ECO:0000250|UniProtKB:O08573, ECO:0000269|PubMed:23817958}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:24333696}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000269|PubMed:24333696}. | null | null | null | null | null | FUNCTION: Binds galactosides (PubMed:18005988). Has high affinity for the Forssman pentasaccharide (PubMed:18005988). Ligand for HAVCR2/TIM3 (PubMed:16286920). Binding to HAVCR2 induces T-helper type 1 lymphocyte (Th1) death (PubMed:16286920). Also stimulates bactericidal activity in infected macrophages by causing macrophage activation and IL1B secretion which restricts intracellular bacterial growth (By similarity). Ligand for P4HB; the interaction retains P4HB at the cell surface of Th2 T-helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307). Ligand for CD44; the interaction enhances binding of SMAD3 to the FOXP3 promoter, leading to up-regulation of FOXP3 expression and increased induced regulatory T (iTreg) cell stability and suppressive function (By similarity). Promotes ability of mesenchymal stromal cells to suppress T-cell proliferation (PubMed:23817958). Expands regulatory T-cells and induces cytotoxic T-cell apoptosis following virus infection (PubMed:20209097). Activates ERK1/2 phosphorylation inducing cytokine (IL-6, IL-8, IL-12) and chemokine (CCL2) production in mast and dendritic cells (PubMed:16116184, PubMed:24465902). Inhibits degranulation and induces apoptosis of mast cells (PubMed:24465902). Induces maturation and migration of dendritic cells (PubMed:16116184, PubMed:25754930). Inhibits natural killer (NK) cell function (PubMed:23408620). Can transform NK cell phenotype from peripheral to decidual during pregnancy (PubMed:25578313). Astrocyte derived galectin-9 enhances microglial TNF production (By similarity). May play a role in thymocyte-epithelial interactions relevant to the biology of the thymus. May provide the molecular basis for urate flux across cell membranes, allowing urate that is formed during purine metabolism to efflux from cells and serving as an electrogenic transporter that plays an important role in renal and gastrointestinal urate excretion (By similarity). Highly selective to the anion urate (By similarity). {ECO:0000250|UniProtKB:O08573, ECO:0000250|UniProtKB:P97840, ECO:0000269|PubMed:16116184, ECO:0000269|PubMed:16286920, ECO:0000269|PubMed:18005988, ECO:0000269|PubMed:18977853, ECO:0000269|PubMed:20209097, ECO:0000269|PubMed:21670307, ECO:0000269|PubMed:23408620, ECO:0000269|PubMed:23817958, ECO:0000269|PubMed:24465902, ECO:0000269|PubMed:25578313, ECO:0000269|PubMed:25754930}.; FUNCTION: [Isoform 2]: Acts as an eosinophil chemoattractant (PubMed:9642261). It also inhibits angiogenesis (PubMed:24333696). Suppresses IFNG production by natural killer cells (By similarity). {ECO:0000250|UniProtKB:O08573, ECO:0000269|PubMed:24333696, ECO:0000269|PubMed:9642261}. | Homo sapiens (Human) |
O00186 | STXB3_HUMAN | MAPPVAERGLKSVVWQKIKATVFDDCKKEGEWKIMLLDEFTTKLLASCCKMTDLLEEGITVVENIYKNREPVRQMKALYFITPTSKSVDCFLHDFASKSENKYKAAYIYFTDFCPDNLFNKIKASCSKSIRRCKEINISFIPHESQVYTLDVPDAFYYCYSPDPGNAKGKDAIMETMADQIVTVCATLDENPGVRYKSKPLDNASKLAQLVEKKLEDYYKIDEKSLIKGKTHSQLLIIDRGFDPVSTVLHELTFQAMAYDLLPIENDTYKYKTDGKEKEAILEEEDDLWVRIRHRHIAVVLEEIPKLMKEISSTKKATEGKTSLSALTQLMKKMPHFRKQITKQVVHLNLAEDCMNKFKLNIEKLCKTEQDLALGTDAEGQKVKDSMRVLLPVLLNKNHDNCDKIRAILLYIFSINGTTEENLDRLIQNVKIENESDMIRNWSYLGVPIVPQSQQGKPLRKDRSAEETFQLSRWTPFIKDIMEDAIDNRLDSKEWPYCSQCPAVWNGSGAVSARQKPRANYLEDRKNGSKLIVFVIGGITYSEVRCAYEVSQAHKSCEVIIGSTHVLTPKKLLDDIKMLNKPKDKVSLIKDE | null | null | brain development [GO:0007420]; cellular response to type II interferon [GO:0071346]; insulin secretion [GO:0030073]; intracellular glucose homeostasis [GO:0001678]; intracellular protein transport [GO:0006886]; negative regulation of calcium ion-dependent exocytosis [GO:0045955]; negative regulation of glucose import [GO:0046325]; neurotransmitter secretion [GO:0007269]; neutrophil degranulation [GO:0043312]; platelet aggregation [GO:0070527]; protein to membrane docking [GO:0022615]; response to insulin [GO:0032868]; vesicle docking involved in exocytosis [GO:0006904]; vesicle-mediated transport [GO:0016192] | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; platelet alpha granule [GO:0031091]; presynapse [GO:0098793]; secretory granule [GO:0030141]; specific granule [GO:0042581]; tertiary granule [GO:0070820] | protein-containing complex binding [GO:0044877]; syntaxin binding [GO:0019905]; syntaxin-1 binding [GO:0017075] | PF00995; | 1.25.40.60;3.40.50.1910;3.40.50.2060; | STXBP/unc-18/SEC1 family | PTM: Phosphorylated by PKC in platelets in response to thrombin stimulation; phosphorylation inhibits binding to STX4. {ECO:0000269|PubMed:10194441}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10194441}. Cell membrane {ECO:0000269|PubMed:10194441}. Note=In platelets, predominantly cytosolic. Low amounts membrane-associated. | null | null | null | null | null | FUNCTION: Together with STX4 and VAMP2, may play a role in insulin-dependent movement of GLUT4 and in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes. {ECO:0000250}. | Homo sapiens (Human) |
O00187 | MASP2_HUMAN | MRLLTLLGLLCGSVATPLGPKWPEPVFGRLASPGFPGEYANDQERRWTLTAPPGYRLRLYFTHFDLELSHLCEYDFVKLSSGAKVLATLCGQESTDTERAPGKDTFYSLGSSLDITFRSDYSNEKPFTGFEAFYAAEDIDECQVAPGEAPTCDHHCHNHLGGFYCSCRAGYVLHRNKRTCSALCSGQVFTQRSGELSSPEYPRPYPKLSSCTYSISLEEGFSVILDFVESFDVETHPETLCPYDFLKIQTDREEHGPFCGKTLPHRIETKSNTVTITFVTDESGDHTGWKIHYTSTAQPCPYPMAPPNGHVSPVQAKYILKDSFSIFCETGYELLQGHLPLKSFTAVCQKDGSWDRPMPACSIVDCGPPDDLPSGRVEYITGPGVTTYKAVIQYSCEETFYTMKVNDGKYVCEADGFWTSSKGEKSLPVCEPVCGLSARTTGGRIYGGQKAKPGDFPWQVLILGGTTAAGALLYDNWVLTAAHAVYEQKHDASALDIRMGTLKRLSPHYTQAWSEAVFIHEGYTHDAGFDNDIALIKLNNKVVINSNITPICLPRKEAESFMRTDDIGTASGWGLTQRGFLARNLMYVDIPIVDHQKCTAAYEKPPYPRGSVTANMLCAGLESGGKDSCRGDSGGALVFLDSETERWFVGGIVSWGSMNCGEAGQYGVYTKVINYIPWIENIISDF | 3.4.21.104 | null | complement activation, classical pathway [GO:0006958]; complement activation, lectin pathway [GO:0001867]; proteolysis [GO:0006508] | extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; complement component C4b binding [GO:0001855]; identical protein binding [GO:0042802]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252] | PF00431;PF07645;PF00084;PF00089; | 2.10.70.10;2.10.25.10;2.60.120.290;2.40.10.10; | Peptidase S1 family | PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.; PTM: Activated by cleavage after Arg-444. The uncleaved zymogen is inactive towards synthetic substrates, but has sufficient activity to effect autocatalytic cleavage. | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Selective cleavage after Arg-223 in complement component C2 (-Ser-Leu-Gly-Arg-|-Lys-Ile-Gln-Ile) and after Arg-76 in complement component C4 (-Gly-Leu-Gln-Arg-|-Ala-Leu-Glu-Ile).; EC=3.4.21.104; | null | null | null | null | FUNCTION: Serum protease that plays an important role in the activation of the complement system via mannose-binding lectin. After activation by auto-catalytic cleavage it cleaves C2 and C4, leading to their activation and to the formation of C3 convertase. {ECO:0000269|PubMed:10946292}. | Homo sapiens (Human) |
O00189 | AP4M1_HUMAN | MISQFFILSSKGDPLIYKDFRGDSGGRDVAELFYRKLTGLPGDESPVVMHHHGRHFIHIRHSGLYLVVTTSENVSPFSLLELLSRLATLLGDYCGSLGEGTISRNVALVYELLDEVLDYGYVQTTSTEMLRNFIQTEAVVSKPFSLFDLSSVGLFGAETQQSKVAPSSAASRPVLSSRSDQSQKNEVFLDVVERLSVLIASNGSLLKVDVQGEIRLKSFLPSGSEMRIGLTEEFCVGKSELRGYGPGIRVDEVSFHSSVNLDEFESHRILRLQPPQGELTVMRYQLSDDLPSPLPFRLFPSVQWDRGSGRLQVYLKLRCDLLSKSQALNVRLHLPLPRGVVSLSQELSSPEQKAELAEGALRWDLPRVQGGSQLSGLFQMDVPGPPGPPSHGLSTSASPLGLGPASLSFELPRHTCSGLQVRFLRLAFRPCGNANPHKWVRHLSHSDAYVIRI | null | null | autophagosome assembly [GO:0000045]; Golgi to endosome transport [GO:0006895]; Golgi to lysosome transport [GO:0090160]; intracellular protein transport [GO:0006886]; post-Golgi vesicle-mediated transport [GO:0006892]; protein localization [GO:0008104]; protein localization to basolateral plasma membrane [GO:1903361]; protein targeting [GO:0006605]; protein targeting to lysosome [GO:0006622]; vesicle-mediated transport [GO:0016192] | AP-4 adaptor complex [GO:0030124]; clathrin adaptor complex [GO:0030131]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; early endosome [GO:0005769]; endosome lumen [GO:0031904]; extracellular exosome [GO:0070062]; trans-Golgi network [GO:0005802]; trans-Golgi network membrane [GO:0032588] | protein domain specific binding [GO:0019904]; protein transmembrane transporter activity [GO:0008320] | PF00928;PF01217; | 3.30.450.60;2.60.40.1170; | Adaptor complexes medium subunit family | null | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:20230749, ECO:0000269|PubMed:29180427, ECO:0000269|PubMed:32073997}; Peripheral membrane protein {ECO:0000305|PubMed:32073997}. Early endosome {ECO:0000269|PubMed:20230749}. Note=Found in soma and dendritic shafts of neuronal cells. {ECO:0000250|UniProtKB:Q2PWT8}. | null | null | null | null | null | FUNCTION: Component of the adaptor protein complex 4 (AP-4). Adaptor protein complexes are vesicle coat components involved both in vesicle formation and cargo selection. They control the vesicular transport of proteins in different trafficking pathways (PubMed:10066790, PubMed:10436028, PubMed:11139587, PubMed:11802162, PubMed:20230749). AP-4 forms a non clathrin-associated coat on vesicles departing the trans-Golgi network (TGN) and may be involved in the targeting of proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system (PubMed:11139587, PubMed:20230749). It is also involved in protein sorting to the basolateral membrane in epithelial cells and the proper asymmetric localization of somatodendritic proteins in neurons (By similarity). Within AP-4, the mu-type subunit AP4M1 is directly involved in the recognition and binding of tyrosine-based sorting signals found in the cytoplasmic part of cargos (PubMed:10436028, PubMed:11139587, PubMed:20230749, PubMed:26544806). The adaptor protein complex 4 (AP-4) may also recognize other types of sorting signal (By similarity). {ECO:0000250|UniProtKB:E2RED8, ECO:0000250|UniProtKB:Q2PWT8, ECO:0000250|UniProtKB:Q9JKC7, ECO:0000269|PubMed:10066790, ECO:0000269|PubMed:10436028, ECO:0000269|PubMed:11139587, ECO:0000269|PubMed:11802162, ECO:0000269|PubMed:20230749, ECO:0000269|PubMed:26544806}. | Homo sapiens (Human) |
O00192 | ARVC_HUMAN | MEDCNVHSAASILASVKEQEARFERLTRALEQERRHVALQLERAQQPGMVSGGMGSGQPLPMAWQQLVLQEQSPGSQASLATMPEAPDVLEETVTVEEDPGTPTSHVSIVTSEDGTTRRTETKVTKTVKTVTTRTVRQVPVGPDGLPLLDGGPPLGPFADGALDRHFLLRGGGPVATLSRAYLSSGGGFPEGPEPRDSPSYGSLSRGLGMRPPRAGPLGPGPGDGCFTLPGHREAFPVGPEPGPPGGRSLPERFQAEPYGLEDDTRSLAADDEGGPELEPDYGTATRRRPECGRGLHTRAYEDTADDGGELADERPAFPMVTAPLAQPERGSMGSLDRLVRRSPSVDSARKEPRWRDPELPEVLAMLRHPVDPVKANAAAYLQHLCFENEGVKRRVRQLRGLPLLVALLDHPRAEVRRRACGALRNLSYGRDTDNKAAIRDCGGVPALVRLLRAARDNEVRELVTGTLWNLSSYEPLKMVIIDHGLQTLTHEVIVPHSGWEREPNEDSKPRDAEWTTVFKNTSGCLRNVSSDGAEARRRLRECEGLVDALLHALQSAVGRKDTDNKSVENCVCIMRNLSYHVHKEVPGADRYQEAEPGPLGSAVGSQRRRRDDASCFGGKKAKEEWFHQGKKDGEMDRNFDTLDLPKRTEAAKGFELLYQPEVVRLYLSLLTESRNFNTLEAAAGALQNLSAGNWMWATYIRATVRKERGLPVLVELLQSETDKVVRAVAIALRNLSLDRRNKDLIGSYAMAELVRNVRNAQAPPRPGACLEEDTVVAVLNTIHEIVSDSLDNARSLLQARGVPALVALVASSQSVREAKAASHVLQTVWSYKELRGTLQKDGWTKARFQSAAATAKGPKGALSPGGFDDSTLPLVDKSLEGEKTGSRDVIPMDALGPDGYSTVDRRERRPRGASSAGEASEKEPLKLDPSRKAPPPGPSRPAVRLVDAVGDAKPQPVDSWV | null | null | cell adhesion [GO:0007155]; cell-cell adhesion [GO:0098609]; cell-cell junction assembly [GO:0007043]; mRNA processing [GO:0006397]; RNA splicing [GO:0008380] | adherens junction [GO:0005912]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | cadherin binding [GO:0045296] | PF00514; | 1.25.10.10; | Beta-catenin family | null | SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000269|PubMed:10725230, ECO:0000269|PubMed:24644279, ECO:0000305|PubMed:30479852}. Nucleus {ECO:0000269|PubMed:10725230, ECO:0000269|PubMed:24644279}. Cytoplasm {ECO:0000269|PubMed:24644279}. Note=In heart, localizes at area composita, the mixed-type junctional structure composed of both desmosomal and adherens junctional proteins. {ECO:0000250|UniProtKB:B4F7F3}. | null | null | null | null | null | FUNCTION: Contributes to the regulation of alternative splicing of pre-mRNAs. {ECO:0000269|PubMed:24644279}. | Homo sapiens (Human) |
O00194 | RB27B_HUMAN | MTDGDYDYLIKLLALGDSGVGKTTFLYRYTDNKFNPKFITTVGIDFREKRVVYNAQGPNGSSGKAFKVHLQLWDTAGQERFRSLTTAFFRDAMGFLLMFDLTSQQSFLNVRNWMSQLQANAYCENPDIVLIGNKADLPDQREVNERQARELADKYGIPYFETSAATGQNVEKAVETLLDLIMKRMEQCVEKTQIPDTVNGGNSGNLDGEKPPEKKCIC | 3.6.5.2 | null | anterograde axonal protein transport [GO:0099641]; exocytosis [GO:0006887]; multivesicular body sorting pathway [GO:0071985]; positive regulation of exocytosis [GO:0045921]; synaptic vesicle endocytosis [GO:0048488] | apical plasma membrane [GO:0016324]; axon cytoplasm [GO:1904115]; exocytic vesicle [GO:0070382]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi stack [GO:0005795]; late endosome [GO:0005770]; melanosome [GO:0042470]; multivesicular body membrane [GO:0032585]; plasma membrane [GO:0005886]; platelet dense granule membrane [GO:0031088]; secretory granule [GO:0030141]; synaptic vesicle membrane [GO:0030672]; trans-Golgi network transport vesicle [GO:0030140]; zymogen granule membrane [GO:0042589] | G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; myosin V binding [GO:0031489]; protein domain specific binding [GO:0019904] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | null | SUBCELLULAR LOCATION: Membrane; Lipid-anchor. Late endosome {ECO:0000269|PubMed:30771381}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000305|PubMed:30771381}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000305|PubMed:30771381}; | null | null | null | null | FUNCTION: Small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate homeostasis of late endocytic pathway, including endosomal positioning, maturation and secretion (PubMed:30771381). Plays a role in NTRK2/TRKB axonal anterograde transport by facilitating the association of NTRK2/TRKB with KLC1 (PubMed:21775604). May be involved in targeting uroplakins to urothelial apical membranes (By similarity). {ECO:0000250|UniProtKB:Q8HZJ5, ECO:0000269|PubMed:21775604, ECO:0000269|PubMed:30771381}. | Homo sapiens (Human) |
O00198 | HRK_HUMAN | MCPCPLHRGRGPPAVCACSAGRLGLRSSAAQLTAARLKALGDELHQRTMWRRRARSRRAPAPGALPTYWPWLCAAAQVAALAAWLLGRRNL | null | null | apoptotic process [GO:0006915]; positive regulation of apoptotic process [GO:0043065]; positive regulation of protein-containing complex assembly [GO:0031334]; positive regulation of release of cytochrome c from mitochondria [GO:0090200] | membrane [GO:0016020]; mitochondrion [GO:0005739] | null | PF15196; | null | null | null | SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. Mitochondrion. | null | null | null | null | null | FUNCTION: Promotes apoptosis. {ECO:0000269|PubMed:15031724, ECO:0000269|PubMed:9130713}. | Homo sapiens (Human) |
O00203 | AP3B1_HUMAN | MSSNSFPYNEQSGGGEATELGQEATSTISPSGAFGLFSSDLKKNEDLKQMLESNKDSAKLDAMKRIVGMIAKGKNASELFPAVVKNVASKNIEIKKLVYVYLVRYAEEQQDLALLSISTFQRALKDPNQLIRASALRVLSSIRVPIIVPIMMLAIKEASADLSPYVRKNAAHAIQKLYSLDPEQKEMLIEVIEKLLKDKSTLVAGSVVMAFEEVCPDRIDLIHKNYRKLCNLLVDVEEWGQVVIIHMLTRYARTQFVSPWKEGDELEDNGKNFYESDDDQKEKTDKKKKPYTMDPDHRLLIRNTKPLLQSRNAAVVMAVAQLYWHISPKSEAGIISKSLVRLLRSNREVQYIVLQNIATMSIQRKGMFEPYLKSFYVRSTDPTMIKTLKLEILTNLANEANISTLLREFQTYVKSQDKQFAAATIQTIGRCATNILEVTDTCLNGLVCLLSNRDEIVVAESVVVIKKLLQMQPAQHGEIIKHMAKLLDSITVPVARASILWLIGENCERVPKIAPDVLRKMAKSFTSEDDLVKLQILNLGAKLYLTNSKQTKLLTQYILNLGKYDQNYDIRDRTRFIRQLIVPNVKSGALSKYAKKIFLAQKPAPLLESPFKDRDHFQLGTLSHTLNIKATGYLELSNWPEVAPDPSVRNVEVIELAKEWTPAGKAKQENSAKKFYSESEEEEDSSDSSSDSESESGSESGEQGESGEEGDSNEDSSEDSSSEQDSESGRESGLENKRTAKRNSKAKGKSDSEDGEKENEKSKTSDSSNDESSSIEDSSSDSESESEPESESESRRVTKEKEKKTKQDRTPLTKDVSLLDLDDFNPVSTPVALPTPALSPSLMADLEGLHLSTSSSVISVSTPAFVPTKTHVLLHRMSGKGLAAHYFFPRQPCIFGDKMVSIQITLNNTTDRKIENIHIGEKKLPIGMKMHVFNPIDSLEPEGSITVSMGIDFCDSTQTASFQLCTKDDCFNVNIQPPVGELLLPVAMSEKDFKKEQGVLTGMNETSAVIIAAPQNFTPSVIFQKVVNVANVGAVPSGQDNIHRFAAKTVHSGSLMLVTVELKEGSTAQLIINTEKTVIGSVLLRELKPVLSQG | null | null | anterograde axonal transport [GO:0008089]; anterograde synaptic vesicle transport [GO:0048490]; antigen processing and presentation, exogenous lipid antigen via MHC class Ib [GO:0048007]; blood coagulation [GO:0007596]; cell morphogenesis [GO:0000902]; clathrin-coated vesicle cargo loading, AP-3-mediated [GO:0035654]; establishment of protein localization to mitochondrial membrane involved in mitochondrial fission [GO:0090152]; granulocyte differentiation [GO:0030851]; hematopoietic progenitor cell differentiation [GO:0002244]; homeostasis of number of cells [GO:0048872]; inflammatory response [GO:0006954]; intracellular protein transport [GO:0006886]; intracellular transport [GO:0046907]; intracellular zinc ion homeostasis [GO:0006882]; lung morphogenesis [GO:0060425]; lysosome organization [GO:0007040]; melanosome assembly [GO:1903232]; melanosome organization [GO:0032438]; mRNA transcription by RNA polymerase II [GO:0042789]; platelet dense granule organization [GO:0060155]; positive regulation of NK T cell differentiation [GO:0051138]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein localization to cell surface [GO:0034394]; protein modification process [GO:0036211]; protein targeting to lysosome [GO:0006622]; respiratory system process [GO:0003016]; single fertilization [GO:0007338]; skin epidermis development [GO:0098773]; spermatogenesis [GO:0007283]; toll-like receptor signaling pathway [GO:0002224]; vesicle-mediated transport [GO:0016192] | AP-3 adaptor complex [GO:0030123]; axon cytoplasm [GO:1904115]; clathrin adaptor complex [GO:0030131]; clathrin-coated vesicle membrane [GO:0030665]; early endosome [GO:0005769]; Golgi apparatus [GO:0005794]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; microvesicle [GO:1990742]; mitochondrion [GO:0005739] | GTP-dependent protein binding [GO:0030742]; protein phosphatase binding [GO:0019903] | PF01602;PF14796;PF14797; | 1.25.10.10; | Adaptor complexes large subunit family | PTM: Phosphorylated on serine residues. {ECO:0000269|PubMed:9182526}.; PTM: Pyrophosphorylation by 5-diphosphoinositol pentakisphosphate (5-IP7) impairs interaction with KIF3A (PubMed:19934039). Serine pyrophosphorylation is achieved by Mg(2+)-dependent, but enzyme independent transfer of a beta-phosphate from a inositol pyrophosphate to a pre-phosphorylated serine residue (PubMed:19934039). {ECO:0000269|PubMed:19934039}. | SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000305|PubMed:9151686}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus {ECO:0000305|PubMed:9151686}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000305|PubMed:9151686}. | null | null | null | null | null | FUNCTION: Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. {ECO:0000305|PubMed:9151686}. | Homo sapiens (Human) |
O00204 | ST2B1_HUMAN | MDGPAEPQIPGLWDTYEDDISEISQKLPGEYFRYKGVPFPVGLYSLESISLAENTQDVRDDDIFIITYPKSGTTWMIEIICLILKEGDPSWIRSVPIWERAPWCETIVGAFSLPDQYSPRLMSSHLPIQIFTKAFFSSKAKVIYMGRNPRDVVVSLYHYSKIAGQLKDPGTPDQFLRDFLKGEVQFGSWFDHIKGWLRMKGKDNFLFITYEELQQDLQGSVERICGFLGRPLGKEALGSVVAHSTFSAMKANTMSNYTLLPPSLLDHRRGAFLRKGVCGDWKNHFTVAQSEAFDRAYRKQMRGMPTFPWDEDPEEDGSPDPEPSPEPEPKPSLEPNTSLEREPRPNSSPSPSPGQASETPHPRPS | 2.8.2.2 | null | 3'-phosphoadenosine 5'-phosphosulfate metabolic process [GO:0050427]; cholesterol metabolic process [GO:0008203]; negative regulation of cell population proliferation [GO:0008285]; positive regulation of epidermal cell differentiation [GO:0045606]; steroid metabolic process [GO:0008202]; sulfation [GO:0051923] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; nucleus [GO:0005634] | cholesterol binding [GO:0015485]; cholesterol sulfotransferase activity [GO:0051922]; nucleic acid binding [GO:0003676]; small molecule binding [GO:0036094]; steroid hormone binding [GO:1990239]; steroid sulfotransferase activity [GO:0050294]; sulfotransferase activity [GO:0008146] | PF00685; | 3.40.50.300; | Sulfotransferase 1 family | PTM: Phosphorylated. {ECO:0000269|PubMed:16855051}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12923182, ECO:0000269|PubMed:16855051, ECO:0000269|PubMed:21855633, ECO:0000269|PubMed:28575648}. Microsome {ECO:0000269|PubMed:16855051, ECO:0000269|PubMed:21855633}. Nucleus {ECO:0000269|PubMed:16855051, ECO:0000269|PubMed:21855633}. Note=Phosphorylation of Ser-348 is required for translocation to the nucleus. {ECO:0000269|PubMed:21855633}. | CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate + H(+); Xref=Rhea:RHEA:22552, ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:83414; EC=2.8.2.2; Evidence={ECO:0000269|PubMed:12145317, ECO:0000269|PubMed:16855051, ECO:0000269|PubMed:19589875, ECO:0000269|PubMed:21855633, ECO:0000269|PubMed:9799594}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + 3beta-hydroxyandrost-5-en-17-one = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate + H(+); Xref=Rhea:RHEA:51216, ChEBI:CHEBI:15378, ChEBI:CHEBI:28689, ChEBI:CHEBI:57905, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343; Evidence={ECO:0000269|PubMed:12145317, ECO:0000269|PubMed:16855051, ECO:0000269|PubMed:21855633, ECO:0000269|PubMed:9799594}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51217; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=(24S)-hydroxycholesterol + 3'-phosphoadenylyl sulfate = (24S)-hydroxycholesterol 3-sulfate + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:52348, ChEBI:CHEBI:15378, ChEBI:CHEBI:34310, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136567; Evidence={ECO:0000269|PubMed:19589875}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52349; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + cholesterol = adenosine 3',5'-bisphosphate + cholesterol sulfate + H(+); Xref=Rhea:RHEA:52368, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136579; Evidence={ECO:0000269|PubMed:12145317, ECO:0000269|PubMed:12923182}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52369; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + pregnenolone = adenosine 3',5'-bisphosphate + H(+) + pregnenolone sulfate; Xref=Rhea:RHEA:52356, ChEBI:CHEBI:15378, ChEBI:CHEBI:16581, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:133000; Evidence={ECO:0000269|PubMed:12145317, ECO:0000269|PubMed:12923182, ECO:0000269|PubMed:21855633}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52357; Evidence={ECO:0000305}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=23.5 uM for (24S)-hydroxycholesterol {ECO:0000269|PubMed:19589875}; KM=10.9 uM for DHEA (at 37 degrees Celsius, in the presence of 1 mM MgCl2) {ECO:0000269|PubMed:21855633}; KM=3.8 uM for DHEA (at 37 degrees Celsius, in the presence of 10 mM MgCl2) {ECO:0000269|PubMed:16855051}; KM=11.8 uM for pregnenolone (at 37 degrees Celsius, in the presence of 1 mM MgCl2) {ECO:0000269|PubMed:21855633}; KM=0.6 uM for PAPS (at 37 degrees Celsius, in the presence of 1 mM MgCl2) {ECO:0000269|PubMed:21855633}; Vmax=1752 pmol/min/mg enzyme toward DHEA (at 37 degrees Celsius, in the presence of 10 mM MgCl2) {ECO:0000269|PubMed:16855051}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. Retains 70% and 20% of activity when incubated at 42 degrees Celsius for 45 and 120 minutes, respectively. Activity is lost after 200 minutes incubation at 42 degrees Celsius. {ECO:0000269|PubMed:16855051, ECO:0000269|PubMed:21855633}; | FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation. Responsible for the sulfation of cholesterol (PubMed:12145317, PubMed:19589875). Catalyzes sulfation of the 3beta-hydroxyl groups of steroids, such as, pregnenolone and dehydroepiandrosterone (DHEA) (PubMed:12145317, PubMed:16855051, PubMed:21855633, PubMed:9799594). Preferentially sulfonates cholesterol, while it has also significant activity with pregnenolone and DHEA (PubMed:12145317, PubMed:21855633). Plays a role in epidermal cholesterol metabolism and in the regulation of epidermal proliferation and differentiation (PubMed:28575648). {ECO:0000269|PubMed:12145317, ECO:0000269|PubMed:16855051, ECO:0000269|PubMed:19589875, ECO:0000269|PubMed:21855633, ECO:0000269|PubMed:28575648, ECO:0000269|PubMed:9799594}.; FUNCTION: [Isoform 2]: Sulfonates pregnenolone but not cholesterol. {ECO:0000269|PubMed:12145317}. | Homo sapiens (Human) |
O00206 | TLR4_HUMAN | MMSASRLAGTLIPAMAFLSCVRPESWEPCVEVVPNITYQCMELNFYKIPDNLPFSTKNLDLSFNPLRHLGSYSFFSFPELQVLDLSRCEIQTIEDGAYQSLSHLSTLILTGNPIQSLALGAFSGLSSLQKLVAVETNLASLENFPIGHLKTLKELNVAHNLIQSFKLPEYFSNLTNLEHLDLSSNKIQSIYCTDLRVLHQMPLLNLSLDLSLNPMNFIQPGAFKEIRLHKLTLRNNFDSLNVMKTCIQGLAGLEVHRLVLGEFRNEGNLEKFDKSALEGLCNLTIEEFRLAYLDYYLDDIIDLFNCLTNVSSFSLVSVTIERVKDFSYNFGWQHLELVNCKFGQFPTLKLKSLKRLTFTSNKGGNAFSEVDLPSLEFLDLSRNGLSFKGCCSQSDFGTTSLKYLDLSFNGVITMSSNFLGLEQLEHLDFQHSNLKQMSEFSVFLSLRNLIYLDISHTHTRVAFNGIFNGLSSLEVLKMAGNSFQENFLPDIFTELRNLTFLDLSQCQLEQLSPTAFNSLSSLQVLNMSHNNFFSLDTFPYKCLNSLQVLDYSLNHIMTSKKQELQHFPSSLAFLNLTQNDFACTCEHQSFLQWIKDQRQLLVEVERMECATPSDKQGMPVLSLNITCQMNKTIIGVSVLSVLVVSVVAVLVYKFYFHLMLLAGCIKYGRGENIYDAFVIYSSQDEDWVRNELVKNLEEGVPPFQLCLHYRDFIPGVAIAANIIHEGFHKSRKVIVVVSQHFIQSRWCIFEYEIAQTWQFLSSRAGIIFIVLQKVEKTLLRQQVELYRLLSRNTYLEWEDSVLGRHIFWRRLRKALLDGKSWNPEGTVGTGCNWQEATSI | null | null | astrocyte development [GO:0014002]; B cell proliferation involved in immune response [GO:0002322]; cellular response to amyloid-beta [GO:1904646]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to lipoteichoic acid [GO:0071223]; cellular response to mechanical stimulus [GO:0071260]; cellular response to oxidised low-density lipoprotein particle stimulus [GO:0140052]; cellular response to platelet-derived growth factor stimulus [GO:0036120]; cellular response to type II interferon [GO:0071346]; defense response to bacterium [GO:0042742]; defense response to Gram-negative bacterium [GO:0050829]; detection of fungus [GO:0016046]; detection of lipopolysaccharide [GO:0032497]; ERK1 and ERK2 cascade [GO:0070371]; gene expression [GO:0010467]; I-kappaB phosphorylation [GO:0007252]; immune response [GO:0006955]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; intestinal epithelial structure maintenance [GO:0060729]; JNK cascade [GO:0007254]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; macrophage activation [GO:0042116]; MHC class II biosynthetic process [GO:0045342]; microglia differentiation [GO:0014004]; MyD88-dependent toll-like receptor signaling pathway [GO:0002755]; negative regulation of cold-induced thermogenesis [GO:0120163]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of interleukin-17 production [GO:0032700]; negative regulation of interleukin-23 production [GO:0032707]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of osteoclast differentiation [GO:0045671]; negative regulation of tumor necrosis factor production [GO:0032720]; negative regulation of type II interferon production [GO:0032689]; nitric oxide biosynthetic process [GO:0006809]; nitric oxide production involved in inflammatory response [GO:0002537]; nucleotide-binding oligomerization domain containing 1 signaling pathway [GO:0070427]; nucleotide-binding oligomerization domain containing 2 signaling pathway [GO:0070431]; phagocytosis [GO:0006909]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cellular response to macrophage colony-stimulating factor stimulus [GO:1903974]; positive regulation of chemokine (C-X-C motif) ligand 2 production [GO:2000343]; positive regulation of chemokine production [GO:0032722]; positive regulation of cytokine production involved in inflammatory response [GO:1900017]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of gene expression [GO:0010628]; positive regulation of inflammatory response [GO:0050729]; positive regulation of interferon-alpha production [GO:0032727]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of interleukin-1 production [GO:0032732]; positive regulation of interleukin-10 production [GO:0032733]; positive regulation of interleukin-12 production [GO:0032735]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of JNK cascade [GO:0046330]; positive regulation of macrophage activation [GO:0043032]; positive regulation of macrophage cytokine production [GO:0060907]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of matrix metallopeptidase secretion [GO:1904466]; positive regulation of MHC class II biosynthetic process [GO:0045348]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of nitric-oxide synthase biosynthetic process [GO:0051770]; positive regulation of NLRP3 inflammasome complex assembly [GO:1900227]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway [GO:0070430]; positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway [GO:0070434]; positive regulation of platelet activation [GO:0010572]; positive regulation of reactive oxygen species biosynthetic process [GO:1903428]; positive regulation of smooth muscle cell migration [GO:0014911]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of stress-activated MAPK cascade [GO:0032874]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of type II interferon production [GO:0032729]; regulation of dendritic cell cytokine production [GO:0002730]; response to lipopolysaccharide [GO:0032496]; stress-activated MAPK cascade [GO:0051403]; T-helper 1 type immune response [GO:0042088]; toll-like receptor 4 signaling pathway [GO:0034142]; toll-like receptor signaling pathway [GO:0002224]; TRIF-dependent toll-like receptor signaling pathway [GO:0035666]; wound healing involved in inflammatory response [GO:0002246] | cell surface [GO:0009986]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; endosome membrane [GO:0010008]; external side of plasma membrane [GO:0009897]; lipopolysaccharide receptor complex [GO:0046696]; perinuclear region of cytoplasm [GO:0048471]; phagocytic cup [GO:0001891]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; ruffle [GO:0001726] | amyloid-beta binding [GO:0001540]; identical protein binding [GO:0042802]; lipopolysaccharide binding [GO:0001530]; lipopolysaccharide immune receptor activity [GO:0001875]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; protein heterodimerization activity [GO:0046982]; signaling receptor activity [GO:0038023]; signaling receptor binding [GO:0005102]; transmembrane signaling receptor activity [GO:0004888] | PF12799;PF13516;PF13855;PF01582; | 3.80.10.10;3.40.50.10140; | Toll-like receptor family | PTM: N-glycosylated. Glycosylation of Asn-526 and Asn-575 seems to be necessary for the expression of TLR4 on the cell surface and the LPS-response. Likewise, mutants lacking two or more of the other N-glycosylation sites were deficient in interaction with LPS. {ECO:0000269|PubMed:11706042, ECO:0000269|PubMed:17803912, ECO:0000269|PubMed:19252480, ECO:0000269|PubMed:22363519}.; PTM: Phosphorylated on tyrosine residues by LYN after binding lipopolysaccharide. {ECO:0000250|UniProtKB:Q9QUK6}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11274165, ECO:0000269|PubMed:17098818, ECO:0000269|PubMed:20037584, ECO:0000269|PubMed:21393102, ECO:0000269|PubMed:27022195, ECO:0000269|PubMed:36232715, ECO:0000269|PubMed:36945827, ECO:0000269|PubMed:9237759}; Single-pass type I membrane protein {ECO:0000269|PubMed:11274165}. Early endosome {ECO:0000269|PubMed:27022195}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q9QUK6}. Note=Upon complex formation with CD36 and TLR6, internalized through dynamin-dependent endocytosis (PubMed:20037584). Colocalizes with RFTN1 at cell membrane and then together with RFTN1 moves to endosomes, upon lipopolysaccharide stimulation. Co-localizes with ZG16B/PAUF at the cell membrane of pancreatic cancer cells (PubMed:36232715). {ECO:0000269|PubMed:20037584, ECO:0000269|PubMed:36232715}. | null | null | null | null | null | FUNCTION: Transmembrane receptor that functions as a pattern recognition receptor recognizing pathogen- and damage-associated molecular patterns (PAMPs and DAMPs) to induce innate immune responses via downstream signaling pathways (PubMed:10835634, PubMed:15809303, PubMed:16622205, PubMed:17292937, PubMed:17478729, PubMed:20037584, PubMed:20711192, PubMed:23880187, PubMed:27022195, PubMed:29038465). At the plasma membrane, cooperates with LY96 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) (PubMed:27022195). Also involved in LPS-independent inflammatory responses triggered by free fatty acids, such as palmitate, and Ni(2+) (PubMed:20711192). Mechanistically, acts via MYD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (PubMed:10835634, PubMed:21393102, PubMed:27022195, PubMed:36945827, PubMed:9237759). Alternatively, CD14-mediated TLR4 internalization via endocytosis is associated with the initiation of a MYD88-independent signaling via the TICAM1-TBK1-IRF3 axis leading to type I interferon production (PubMed:14517278). In addition to the secretion of proinflammatory cytokines, initiates the activation of NLRP3 inflammasome and formation of a positive feedback loop between autophagy and NF-kappa-B signaling cascade (PubMed:32894580). In complex with TLR6, promotes inflammation in monocytes/macrophages by associating with TLR6 and the receptor CD86 (PubMed:23880187). Upon ligand binding, such as oxLDL or amyloid-beta 42, the TLR4:TLR6 complex is internalized and triggers inflammatory response, leading to NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway (PubMed:23880187). In myeloid dendritic cells, vesicular stomatitis virus glycoprotein G but not LPS promotes the activation of IRF7, leading to type I IFN production in a CD14-dependent manner (PubMed:15265881, PubMed:23880187). Required for the migration-promoting effects of ZG16B/PAUF on pancreatic cancer cells. {ECO:0000269|PubMed:10835634, ECO:0000269|PubMed:14517278, ECO:0000269|PubMed:15265881, ECO:0000269|PubMed:15809303, ECO:0000269|PubMed:16622205, ECO:0000269|PubMed:17292937, ECO:0000269|PubMed:17478729, ECO:0000269|PubMed:20037584, ECO:0000269|PubMed:20711192, ECO:0000269|PubMed:23880187, ECO:0000269|PubMed:27022195, ECO:0000269|PubMed:29038465, ECO:0000269|PubMed:36945827, ECO:0000269|PubMed:9237759}. | Homo sapiens (Human) |
O00212 | RHOD_HUMAN | MTAAQAAGEEAPPGVRSVKVVLVGDGGCGKTSLLMVFADGAFPESYTPTVFERYMVNLQVKGKPVHLHIWDTAGQDDYDRLRPLFYPDASVLLLCFDVTSPNSFDNIFNRWYPEVNHFCKKVPIIVVGCKTDLRKDKSLVNKLRRNGLEPVTYHRGQEMARSVGAVAYLECSARLHDNVHAVFQEAAEVALSSRGRNFWRRITQGFCVVT | null | null | actin filament bundle assembly [GO:0051017]; actin filament organization [GO:0007015]; cell migration [GO:0016477]; focal adhesion assembly [GO:0048041]; lamellipodium assembly [GO:0030032]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell migration [GO:0030335]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of small GTPase mediated signal transduction [GO:0051056]; Rho protein signal transduction [GO:0007266]; signal transduction [GO:0007165] | cytosol [GO:0005829]; early endosome [GO:0005769]; endosome membrane [GO:0010008]; Golgi membrane [GO:0000139]; mitochondrial outer membrane [GO:0005741]; plasma membrane [GO:0005886] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; guanyl-nucleotide exchange factor activity [GO:0005085]; protein kinase binding [GO:0019901] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rho family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome {ECO:0000269|PubMed:24102721}. Note=Colocalizes with RAB5 to early endosomes (By similarity). {ECO:0000250|UniProtKB:P97348}. | null | null | null | null | null | FUNCTION: Involved in endosome dynamics. May coordinate membrane transport with the function of the cytoskeleton. Involved in the internalization and trafficking of activated tyrosine kinase receptors such as PDGFRB. Participates in the reorganization of actin cytoskeleton; the function seems to involve WHAMM and includes regulation of filopodia formation and actin filament bundling. Can modulate the effect of DAPK3 in reorganization of actin cytoskeleton and focal adhesion dissolution. {ECO:0000269|PubMed:23087206, ECO:0000269|PubMed:23454120, ECO:0000269|PubMed:24102721}. | Homo sapiens (Human) |
O00213 | APBB1_HUMAN | MSVPSSLSQSAINANSHGGPALSLPLPLHAAHNQLLNAKLQATAVGPKDLRSAMGEGGGPEPGPANAKWLKEGQNQLRRAATAHRDQNRNVTLTLAEEASQEPEMAPLGPKGLIHLYSELELSAHNAANRGLRGPGLIISTQEQGPDEGEEKAAGEAEEEEEDDDDEEEEEDLSSPPGLPEPLESVEAPPRPQALTDGPREHSKSASLLFGMRNSAASDEDSSWATLSQGSPSYGSPEDTDSFWNPNAFETDSDLPAGWMRVQDTSGTYYWHIPTGTTQWEPPGRASPSQGSSPQEESQLTWTGFAHGEGFEDGEFWKDEPSDEAPMELGLKEPEEGTLTFPAQSLSPEPLPQEEEKLPPRNTNPGIKCFAVRSLGWVEMTEEELAPGRSSVAVNNCIRQLSYHKNNLHDPMSGGWGEGKDLLLQLEDETLKLVEPQSQALLHAQPIISIRVWGVGRDSGRERDFAYVARDKLTQMLKCHVFRCEAPAKNIATSLHEICSKIMAERRNARCLVNGLSLDHSKLVDVPFQVEFPAPKNELVQKFQVYYLGNVPVAKPVGVDVINGALESVLSSSSREQWTPSHVSVAPATLTILHQQTEAVLGECRVRFLSFLAVGRDVHTFAFIMAAGPASFCCHMFWCEPNAASLSEAVQAACMLRYQKCLDARSQASTSCLPAPPAESVARRVGWTVRRGVQSLWGSLKPKRLGAHTP | null | null | apoptotic process [GO:0006915]; axonogenesis [GO:0007409]; chromatin organization [GO:0006325]; DNA damage response [GO:0006974]; negative regulation of cell cycle G1/S phase transition [GO:1902807]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of apoptotic process [GO:0043065]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of neuron projection development [GO:0010976]; positive regulation of protein secretion [GO:0050714]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; signal transduction [GO:0007165]; smooth muscle contraction [GO:0006939] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; synapse [GO:0045202] | amyloid-beta binding [GO:0001540]; chromatin binding [GO:0003682]; histone binding [GO:0042393]; low-density lipoprotein particle receptor binding [GO:0050750]; molecular adaptor activity [GO:0060090]; proline-rich region binding [GO:0070064]; transcription coactivator activity [GO:0003713]; ubiquitin protein ligase binding [GO:0031625] | PF00640;PF00397; | 2.20.70.10;2.30.29.30; | null | PTM: Phosphorylation at Ser-610 by SGK1 promotes its localization to the nucleus (By similarity). Phosphorylated following nuclear translocation (PubMed:15031292, PubMed:18922798). Phosphorylation at Tyr-547 by ABL1 enhances transcriptional activation activity and reduces the affinity for RASD1/DEXRAS1 (PubMed:15031292, PubMed:18922798). Phosphorylated at Ser-459 by PKC upon insulin activation (PubMed:36250347). {ECO:0000250|UniProtKB:P46933, ECO:0000269|PubMed:15031292, ECO:0000269|PubMed:18922798, ECO:0000269|PubMed:36250347}.; PTM: Acetylation at Lys-204 and Lys-701 by KAT5 promotes its transcription activator activity. {ECO:0000269|PubMed:33938178}.; PTM: Polyubiquitination by RNF157 leads to degradation by the proteasome (PubMed:25342469). {ECO:0000269|PubMed:25342469}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18468999}. Cytoplasm {ECO:0000269|PubMed:18468999}. Nucleus {ECO:0000269|PubMed:15031292, ECO:0000269|PubMed:18468999, ECO:0000269|PubMed:18922798, ECO:0000269|PubMed:19343227}. Cell projection, growth cone {ECO:0000250|UniProtKB:P46933}. Nucleus speckle {ECO:0000269|PubMed:17512906}. Note=Colocalizes with TSHZ3 in axonal growth cone (By similarity). Colocalizes with TSHZ3 in the nucleus (PubMed:19343227). In normal conditions, it mainly localizes to the cytoplasm, while a small fraction is tethered to the cell membrane via its interaction with APP (PubMed:18468999). Following exposure to DNA damaging agents, it is released from cell membrane and translocates to the nucleus (PubMed:18468999). Nuclear translocation is under the regulation of APP (PubMed:18468999). Colocalizes with NEK6 at the nuclear speckles (PubMed:17512906). Phosphorylation at Ser-610 by SGK1 promotes its localization to the nucleus (By similarity). {ECO:0000250|UniProtKB:P46933, ECO:0000269|PubMed:17512906, ECO:0000269|PubMed:18468999, ECO:0000269|PubMed:19343227}. | null | null | null | null | null | FUNCTION: Transcription coregulator that can have both coactivator and corepressor functions (PubMed:15031292, PubMed:18468999, PubMed:18922798, PubMed:25342469, PubMed:33938178). Adapter protein that forms a transcriptionally active complex with the gamma-secretase-derived amyloid precursor protein (APP) intracellular domain (PubMed:15031292, PubMed:18468999, PubMed:18922798, PubMed:25342469). Plays a central role in the response to DNA damage by translocating to the nucleus and inducing apoptosis (PubMed:15031292, PubMed:18468999, PubMed:18922798, PubMed:25342469). May act by specifically recognizing and binding histone H2AX phosphorylated on 'Tyr-142' (H2AXY142ph) at double-strand breaks (DSBs), recruiting other pro-apoptosis factors such as MAPK8/JNK1 (PubMed:19234442). Required for histone H4 acetylation at double-strand breaks (DSBs) (PubMed:19234442). Its ability to specifically bind modified histones and chromatin modifying enzymes such as KAT5/TIP60, probably explains its transcription activation activity (PubMed:33938178). Functions in association with TSHZ3, SET and HDAC factors as a transcriptional repressor, that inhibits the expression of CASP4 (PubMed:19343227). Associates with chromatin in a region surrounding the CASP4 transcriptional start site(s) (PubMed:19343227). Involved in hippocampal neurite branching and neuromuscular junction formation, as a result plays a role in spatial memory functioning (By similarity). Plays a role in the maintenance of lens transparency (By similarity). May play a role in muscle cell strength (By similarity). Acts as a molecular adapter that functions in neurite outgrowth by activating the RAC1-ARF6 axis upon insulin treatment (PubMed:36250347). {ECO:0000250|UniProtKB:Q9QXJ1, ECO:0000269|PubMed:15031292, ECO:0000269|PubMed:18468999, ECO:0000269|PubMed:18922798, ECO:0000269|PubMed:19234442, ECO:0000269|PubMed:19343227, ECO:0000269|PubMed:25342469, ECO:0000269|PubMed:33938178, ECO:0000269|PubMed:36250347}. | Homo sapiens (Human) |
O00214 | LEG8_HUMAN | MMLSLNNLQNIIYNPVIPFVGTIPDQLDPGTLIVIRGHVPSDADRFQVDLQNGSSMKPRADVAFHFNPRFKRAGCIVCNTLINEKWGREEITYDTPFKREKSFEIVIMVLKDKFQVAVNGKHTLLYGHRIGPEKIDTLGIYGKVNIHSIGFSFSSDLQSTQASSLELTEISRENVPKSGTPQLRLPFAARLNTPMGPGRTVVVKGEVNANAKSFNVDLLAGKSKDIALHLNPRLNIKAFVRNSFLQESWGEEERNITSFPFSPGMYFEMIIYCDVREFKVAVNGVHSLEYKHRFKELSSIDTLEINGDIHLLEVRSW | null | null | cellular response to virus [GO:0098586]; lymphatic endothelial cell migration [GO:1904977]; xenophagy [GO:0098792] | cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; extracellular space [GO:0005615]; membrane [GO:0016020] | carbohydrate binding [GO:0030246]; integrin binding [GO:0005178] | PF00337; | 2.60.120.200; | null | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000269|PubMed:22246324}. Cytoplasm, cytosol {ECO:0000269|PubMed:22246324}. | null | null | null | null | null | FUNCTION: Beta-galactoside-binding lectin that acts as a sensor of membrane damage caused by infection and restricts the proliferation of infecting pathogens by targeting them for autophagy (PubMed:22246324, PubMed:28077878). Detects membrane rupture by binding beta-galactoside ligands located on the lumenal side of the endosome membrane; these ligands becoming exposed to the cytoplasm following rupture (PubMed:22246324, PubMed:28077878). Restricts infection by initiating autophagy via interaction with CALCOCO2/NDP52 (PubMed:22246324, PubMed:28077878). Required to restrict infection of bacterial invasion such as S.typhimurium (PubMed:22246324). Also required to restrict infection of Picornaviridae viruses (PubMed:28077878). Has a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans (PubMed:21288902). {ECO:0000269|PubMed:21288902, ECO:0000269|PubMed:22246324, ECO:0000269|PubMed:28077878}. | Homo sapiens (Human) |
O00217 | NDUS8_HUMAN | MRCLTTPMLLRALAQAARAGPPGGRSLHSSAVAATYKYVNMQDPEMDMKSVTDRAARTLLWTELFRGLGMTLSYLFREPATINYPFEKGPLSPRFRGEHALRRYPSGEERCIACKLCEAICPAQAITIEAEPRADGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFSTETHEELLYNKEKLLNNGDKWEAEIAANIQADYLYR | 7.1.1.2 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:Q56224}; Note=Binds 2 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:Q56224}; | aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]; response to oxidative stress [GO:0006979] | mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739] | 4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872]; NADH dehydrogenase (ubiquinone) activity [GO:0008137] | PF12838; | 3.30.70.3270; | Complex I 23 kDa subunit family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891, ECO:0000305|PubMed:9666055}; Peripheral membrane protein {ECO:0000250|UniProtKB:P42028}; Matrix side {ECO:0000250|UniProtKB:P42028}. | CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000269|PubMed:22499348}; | null | null | null | null | FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:22499348). Essential for the catalytic activity and assembly of complex I (PubMed:22499348). {ECO:0000269|PubMed:22499348}. | Homo sapiens (Human) |
O00219 | HYAS3_HUMAN | MPVQLTTALRVVGTSLFALAVLGGILAAYVTGYQFIHTEKHYLSFGLYGAILGLHLLIQSLFAFLEHRRMRRAGQALKLPSPRRGSVALCIAAYQEDPDYLRKCLRSAQRISFPDLKVVMVVDGNRQEDAYMLDIFHEVLGGTEQAGFFVWRSNFHEAGEGETEASLQEGMDRVRDVVRASTFSCIMQKWGGKREVMYTAFKALGDSVDYIQVCDSDTVLDPACTIEMLRVLEEDPQVGGVGGDVQILNKYDSWISFLSSVRYWMAFNVERACQSYFGCVQCISGPLGMYRNSLLQQFLEDWYHQKFLGSKCSFGDDRHLTNRVLSLGYRTKYTARSKCLTETPTKYLRWLNQQTRWSKSYFREWLYNSLWFHKHHLWMTYESVVTGFFPFFLIATVIQLFYRGRIWNILLFLLTVQLVGIIKATYACFLRGNAEMIFMSLYSLLYMSSLLPAKIFAIATINKSGWGTSGRKTIVVNFIGLIPVSIWVAVLLGGLAYTAYCQDLFSETELAFLVSGAILYGCYWVALLMLYLAIIARRCGKKPEQYSLAFAEV | 2.4.1.212 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | carbohydrate metabolic process [GO:0005975]; extracellular matrix assembly [GO:0085029]; extracellular polysaccharide biosynthetic process [GO:0045226]; hyaluronan biosynthetic process [GO:0030213]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of hyaluranon cable assembly [GO:1900106] | early endosome [GO:0005769]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; hyaluranon cable [GO:0036117]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | hyaluronan synthase activity [GO:0050501]; identical protein binding [GO:0042802] | PF13641; | null | NodC/HAS family | PTM: O-GlcNAcylation increases the hyaluronan synthase activity, HAS3 stability and its plasma membrane residence. The concentration of UDP-GlcNAc controls the level of O-GlcNAc modification. {ECO:0000269|PubMed:26883802}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25795779, ECO:0000269|PubMed:26883802, ECO:0000269|PubMed:30394292}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:25795779}; Multi-pass membrane protein. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:O08650}; Multi-pass membrane protein {ECO:0000255}. Early endosome {ECO:0000269|PubMed:26883802}. Note=Travels from endoplasmic reticulum (ER), Golgi to plasma membrane (PubMed:26883802). Actives only when present in plasma membrane (By similarity). O-GlcNAcylation controls its membrane localization (PubMed:26883802). A rapid recycling of HAS3 between plasma membrane and endosomes is controlled by the cytosolic levels of UDP-GlcUA and UDP-GlcNAc (PubMed:26883802). {ECO:0000250|UniProtKB:O08650, ECO:0000269|PubMed:26883802}. | CATALYTIC ACTIVITY: Reaction=[hyaluronan](n) + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N-acetyl-beta-D-glucosaminyl-(1->4)-[hyaluronan](n) + UDP; Xref=Rhea:RHEA:20465, Rhea:RHEA-COMP:12583, Rhea:RHEA-COMP:12585, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:132153, ChEBI:CHEBI:132154; EC=2.4.1.212; Evidence={ECO:0000269|PubMed:23303191, ECO:0000269|PubMed:25795779, ECO:0000269|PubMed:26883802}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20466; Evidence={ECO:0000269|PubMed:26883802}; CATALYTIC ACTIVITY: Reaction=N-acetyl-beta-D-glucosaminyl-(1->4)-[hyaluronan](n) + UDP-alpha-D-glucuronate = [hyaluronan](n+1) + H(+) + UDP; Xref=Rhea:RHEA:12528, Rhea:RHEA-COMP:12585, Rhea:RHEA-COMP:12587, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:132153, ChEBI:CHEBI:132154; EC=2.4.1.212; Evidence={ECO:0000269|PubMed:23303191, ECO:0000269|PubMed:25795779, ECO:0000269|PubMed:26883802}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12529; Evidence={ECO:0000269|PubMed:26883802}; | null | PATHWAY: Glycan biosynthesis; hyaluronan biosynthesis. {ECO:0000269|PubMed:23303191}. | null | null | FUNCTION: Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. This is one of three isoenzymes responsible for cellular hyaluronan synthesis. {ECO:0000269|PubMed:23303191, ECO:0000269|PubMed:25795779, ECO:0000269|PubMed:26883802}. | Homo sapiens (Human) |
O00220 | TR10A_HUMAN | MAPPPARVHLGAFLAVTPNPGSAASGTEAAAATPSKVWGSSAGRIEPRGGGRGALPTSMGQHGPSARARAGRAPGPRPAREASPRLRVHKTFKFVVVGVLLQVVPSSAATIKLHDQSIGTQQWEHSPLGELCPPGSHRSEHPGACNRCTEGVGYTNASNNLFACLPCTACKSDEEERSPCTTTRNTACQCKPGTFRNDNSAEMCRKCSRGCPRGMVKVKDCTPWSDIECVHKESGNGHNIWVILVVTLVVPLLLVAVLIVCCCIGSGCGGDPKCMDRVCFWRLGLLRGPGAEDNAHNEILSNADSLSTFVSEQQMESQEPADLTGVTVQSPGEAQCLLGPAEAEGSQRRRLLVPANGADPTETLMLFFDKFANIVPFDSWDQLMRQLDLTKNEIDVVRAGTAGPGDALYAMLMKWVNKTGRNASIHTLLDALERMEERHAREKIQDLLVDSGKFIYLEDGTGSAVSLE | null | null | activation of NF-kappaB-inducing kinase activity [GO:0007250]; apoptotic process [GO:0006915]; cellular response to mechanical stimulus [GO:0071260]; extrinsic apoptotic signaling pathway [GO:0097191]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; positive regulation of apoptotic process [GO:0043065]; signal transduction [GO:0007165]; TRAIL-activated apoptotic signaling pathway [GO:0036462] | cell surface [GO:0009986]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; membrane raft [GO:0045121]; plasma membrane [GO:0005886] | death receptor activity [GO:0005035]; identical protein binding [GO:0042802]; protease binding [GO:0002020]; signaling receptor activity [GO:0038023]; TRAIL binding [GO:0045569] | PF00531;PF00020; | 1.10.533.10;2.10.50.10; | null | PTM: Palmitoylated (PubMed:19090789). Palmitoylation of TNFRSF10A is required for its association with lipid rafts, oligomerization and function in TRAIL-induced cell death (PubMed:19090789). Palmitoylated by ZDHHC3 (Probable). {ECO:0000269|PubMed:19090789, ECO:0000305|PubMed:22240897}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22240897}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000269|PubMed:19090789, ECO:0000269|PubMed:22240897}. Cytoplasm, cytosol {ECO:0000269|PubMed:22240897}. Note=Palmitoylation is required for association with membranes. {ECO:0000269|PubMed:22240897}. | null | null | null | null | null | FUNCTION: Receptor for the cytotoxic ligand TNFSF10/TRAIL (PubMed:26457518). The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis (PubMed:19090789). Promotes the activation of NF-kappa-B (PubMed:9430227). {ECO:0000269|PubMed:19090789, ECO:0000269|PubMed:9430227}. | Homo sapiens (Human) |
O00221 | IKBE_HUMAN | MNQRRSESRPGNHRLQAYAEPGKGDSGGAGPLSGSARRGRGGGGAIRVRRPCWSGGAGRGGGPAWAVRLPTVTAGWTWPALRTLSSLRAGPSEPHSPGRRPPRAGRPLCQADPQPGKAARRSLEPDPAQTGPRPARAAGMSEARKGPDEAEESQYDSGIESLRSLRSLPESTSAPASGPSDGSPQPCTHPPGPVKEPQEKEDADGERADSTYGSSSLTYTLSLLGGPEAEDPAPRLPLPHVGALSPQQLEALTYISEDGDTLVHLAVIHEAPAVLLCCLALLPQEVLDIQNNLYQTALHLAVHLDQPGAVRALVLKGASRALQDRHGDTALHVACQRQHLACARCLLEGRPEPGRGTSHSLDLQLQNWQGLACLHIATLQKNQPLMELLLRNGADIDVQEGTSGKTALHLAVETQERGLVQFLLQAGAQVDARMLNGCTPLHLAAGRGLMGISSTLCKAGADSLLRNVEDETPQDLTEESLVLLPFDDLKISGKLLLCTD | null | null | cellular response to tumor necrosis factor [GO:0071356]; cytoplasmic sequestering of transcription factor [GO:0042994] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; fibrillar center [GO:0001650]; nucleoplasm [GO:0005654] | NF-kappaB binding [GO:0051059] | PF12796; | 1.25.40.20; | NF-kappa-B inhibitor family | PTM: Serine phosphorylated; followed by proteasome-dependent degradation. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Inhibits NF-kappa-B by complexing with and trapping it in the cytoplasm. Inhibits DNA-binding of NF-kappa-B p50-p65 and p50-c-Rel complexes. {ECO:0000269|PubMed:9315679}. | Homo sapiens (Human) |
O00222 | GRM8_HUMAN | MVCEGKRSASCPCFFLLTAKFYWILTMMQRTHSQEYAHSIRVDGDIILGGLFPVHAKGERGVPCGELKKEKGIHRLEAMLYAIDQINKDPDLLSNITLGVRILDTCSRDTYALEQSLTFVQALIEKDASDVKCANGDPPIFTKPDKISGVIGAAASSVSIMVANILRLFKIPQISYASTAPELSDNTRYDFFSRVVPPDSYQAQAMVDIVTALGWNYVSTLASEGNYGESGVEAFTQISREIGGVCIAQSQKIPREPRPGEFEKIIKRLLETPNARAVIMFANEDDIRRILEAAKKLNQSGHFLWIGSDSWGSKIAPVYQQEEIAEGAVTILPKRASIDGFDRYFRSRTLANNRRNVWFAEFWEENFGCKLGSHGKRNSHIKKCTGLERIARDSSYEQEGKVQFVIDAVYSMAYALHNMHKDLCPGYIGLCPRMSTIDGKELLGYIRAVNFNGSAGTPVTFNENGDAPGRYDIFQYQITNKSTEYKVIGHWTNQLHLKVEDMQWAHREHTHPASVCSLPCKPGERKKTVKGVPCCWHCERCEGYNYQVDELSCELCPLDQRPNMNRTGCQLIPIIKLEWHSPWAVVPVFVAILGIIATTFVIVTFVRYNDTPIVRASGRELSYVLLTGIFLCYSITFLMIAAPDTIICSFRRVFLGLGMCFSYAALLTKTNRIHRIFEQGKKSVTAPKFISPASQLVITFSLISVQLLGVFVWFVVDPPHIIIDYGEQRTLDPEKARGVLKCDISDLSLICSLGYSILLMVTCTVYAIKTRGVPETFNEAKPIGFTMYTTCIIWLAFIPIFFGTAQSAEKMYIQTTTLTVSMSLSASVSLGMLYMPKVYIIIFHPEQNVQKRKRSFKAVVTAATMQSKLIQKGNDRPNGEVKSELCESLETNTSSTKTTYISYSNHSI | null | null | adenylate cyclase-inhibiting G protein-coupled glutamate receptor signaling pathway [GO:0007196]; adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; G protein-coupled glutamate receptor signaling pathway [GO:0007216]; regulation of synaptic transmission, glutamatergic [GO:0051966]; visual perception [GO:0007601] | plasma membrane [GO:0005886] | G protein-coupled receptor activity [GO:0004930]; glutamate receptor activity [GO:0008066]; group III metabotropic glutamate receptor activity [GO:0001642] | PF00003;PF01094;PF07562; | 3.40.50.2300;2.10.50.30; | G-protein coupled receptor 3 family | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. {ECO:0000269|PubMed:9473604}. | Homo sapiens (Human) |
O00231 | PSD11_HUMAN | MAAAAVVEFQRAQSLLSTDREASIDILHSIVKRDIQENDEEAVQVKEQSILELGSLLAKTGQAAELGGLLKYVRPFLNSISKAKAARLVRSLLDLFLDMEAATGQEVELCLECIEWAKSEKRTFLRQALEARLVSLYFDTKRYQEALHLGSQLLRELKKMDDKALLVEVQLLESKTYHALSNLPKARAALTSARTTANAIYCPPKLQATLDMQSGIIHAAEEKDWKTAYSYFYEAFEGYDSIDSPKAITSLKYMLLCKIMLNTPEDVQALVSGKLALRYAGRQTEALKCVAQASKNRSLADFEKALTDYRAELRDDPIISTHLAKLYDNLLEQNLIRVIEPFSRVQIEHISSLIKLSKADVERKLSQMILDKKFHGILDQGEGVLIIFDEPPVDKTYEAALETIQNMSKVVDSLYNKAKKLT | null | null | proteasome assembly [GO:0043248]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; stem cell differentiation [GO:0048863]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytosol [GO:0005829]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome accessory complex [GO:0022624]; proteasome complex [GO:0000502]; proteasome regulatory particle, lid subcomplex [GO:0008541]; secretory granule lumen [GO:0034774] | structural molecule activity [GO:0005198] | PF01399;PF18503;PF18055; | 1.25.40.570; | Proteasome subunit S9 family | PTM: Phosphorylated by AMPK. {ECO:0000269|PubMed:19616115}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. | null | null | null | null | null | FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. In the complex, PSMD11 is required for proteasome assembly. Plays a key role in increased proteasome activity in embryonic stem cells (ESCs): its high expression in ESCs promotes enhanced assembly of the 26S proteasome, followed by higher proteasome activity. {ECO:0000269|PubMed:1317798, ECO:0000269|PubMed:22972301}. | Homo sapiens (Human) |
O00232 | PSD12_HUMAN | MADGGSERADGRIVKMEVDYSATVDQRLPECAKLAKEGRLQEVIETLLSLEKQTRTASDMVSTSRILVAVVKMCYEAKEWDLLNENIMLLSKRRSQLKQAVAKMVQQCCTYVEEITDLPIKLRLIDTLRMVTEGKIYVEIERARLTKTLATIKEQNGDVKEAASILQELQVETYGSMEKKERVEFILEQMRLCLAVKDYIRTQIISKKINTKFFQEENTEKLKLKYYNLMIQLDQHEGSYLSICKHYRAIYDTPCIQAESEKWQQALKSVVLYVILAPFDNEQSDLVHRISGDKKLEEIPKYKDLLKLFTTMELMRWSTLVEDYGMELRKGSLESPATDVFGSTEEGEKRWKDLKNRVVEHNIRIMAKYYTRITMKRMAQLLDLSVDESEAFLSNLVVNKTIFAKVDRLAGIINFQRPKDPNNLLNDWSQKLNSLMSLVNKTTHLIAKEEMIHNLQ | null | null | proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; proteasome accessory complex [GO:0022624]; proteasome complex [GO:0000502]; proteasome regulatory particle [GO:0005838]; proteasome regulatory particle, lid subcomplex [GO:0008541]; secretory granule lumen [GO:0034774] | null | PF01399;PF18098; | 1.10.10.10; | Proteasome subunit p55 family | null | null | null | null | null | null | null | FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. {ECO:0000269|PubMed:1317798}. | Homo sapiens (Human) |
O00233 | PSMD9_HUMAN | MSDEEARQSGGSSQAGVVTVSDVQELMRRKEEIEAQIKANYDVLESQKGIGMNEPLVDCEGYPRSDVDLYQVRTARHNIICLQNDHKAVMKQVEEALHQLHARDKEKQARDMAEAHKEAMSRKLGQSESQGPPRAFAKVNSISPGSPASIAGLQVDDEIVEFGSVNTQNFQSLHNIGSVVQHSEGKPLNVTVIRRGEKHQLRLVPTRWAGKGLLGCNIIPLQR | null | null | negative regulation of insulin secretion [GO:0046676]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of insulin secretion [GO:0032024]; proteasome regulatory particle assembly [GO:0070682]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome regulatory particle [GO:0005838] | bHLH transcription factor binding [GO:0043425]; transcription coactivator activity [GO:0003713] | PF18265;PF17820; | 2.30.42.10;6.10.140.1710; | Proteasome subunit p27 family | null | null | null | null | null | null | null | FUNCTION: Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). During the base subcomplex assembly is part of an intermediate PSMD9:PSMC6:PSMC3 module, also known as modulator trimer complex; PSMD9 is released during the further base assembly process. {ECO:0000269|PubMed:19490896}. | Homo sapiens (Human) |
O00237 | RN103_HUMAN | MWLKLFFLLLYFLVLFVLARFFEAIVWYETGIFATQLVDPVALSFKKLKTILECRGLGYSGLPEKKDVRELVEKSGDLMEGELYSALKEEEASESVSSTNFSGEMHFYELVEDTKDGIWLVQVIANDRSPLVGKIHWEKMVKKVSRFGIRTGTFNCSSDPRYCRRRGWVRSTLIMSVPQTSTSKGKVMLKEYSGRKIEVEHIFKWITAHAASRIKTIYNAEHLKEEWNKSDQYWLKIYLFANLDQPPAFFSALSIKFTGRVEFIFVNVENWDNKSYMTDIGIYNMPSYILRTPEGIYRYGNHTGEFISLQAMDSFLRSLQPEVNDLFVLSLVLVNLMAWMDLFITQGATIKRFVVLISTLGTYNSLLIISWLPVLGFLQLPYLDSFYEYSLKLLRYSNTTTLASWVRADWMFYSSHPALFLSTYLGHGLLIDYFEKKRRRNNNNDEVNANNLEWLSSLWDWYTSYLFHPIASFQNFPVESDWDEDPDLFLERLAFPDLWLHPLIPTDYIKNLPMWRFKCLGVQSEEEMSEGSQDTENDSESENTDTLSSEKEVFEDKQSVLHNSPGTASHCDAEACSCANKYCQTSPCERKGRSYGSYNTNEDMEPDWLTWPADMLHCTECVVCLENFENGCLLMGLPCGHVFHQNCIVMWLAGGRHCCPVCRWPSYKKKQPYAQHQPLSNDVPS | 2.3.2.27 | null | central nervous system development [GO:0007417]; ERAD pathway [GO:0036503]; protein ubiquitination [GO:0016567] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842] | PF13639; | 3.30.40.10; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18675248}; Multi-pass membrane protein {ECO:0000269|PubMed:18675248}. | 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; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Acts as an E2-dependent E3 ubiquitin-protein ligase, probably involved in the ER-associated protein degradation pathway. {ECO:0000269|PubMed:10500182, ECO:0000269|PubMed:18675248}. | Homo sapiens (Human) |
O00238 | BMR1B_HUMAN | MLLRSAGKLNVGTKKEDGESTAPTPRPKVLRCKCHHHCPEDSVNNICSTDGYCFTMIEEDDSGLPVVTSGCLGLEGSDFQCRDTPIPHQRRSIECCTERNECNKDLHPTLPPLKNRDFVDGPIHHRALLISVTVCSLLLVLIILFCYFRYKRQETRPRYSIGLEQDETYIPPGESLRDLIEQSQSSGSGSGLPLLVQRTIAKQIQMVKQIGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYDYLKSTTLDAKSMLKLAYSSVSGLCHLHTEIFSTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVKFISDTNEVDIPPNTRVGTKRYMPPEVLDESLNRNHFQSYIMADMYSFGLILWEVARRCVSGGIVEEYQLPYHDLVPSDPSYEDMREIVCIKKLRPSFPNRWSSDECLRQMGKLMTECWAHNPASRLTALRVKKTLAKMSESQDIKL | 2.7.11.30 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; | BMP signaling pathway [GO:0030509]; cartilage condensation [GO:0001502]; cellular response to BMP stimulus [GO:0071773]; cellular response to growth factor stimulus [GO:0071363]; central nervous system neuron differentiation [GO:0021953]; chondrocyte development [GO:0002063]; dorsal/ventral pattern formation [GO:0009953]; endochondral bone morphogenesis [GO:0060350]; eye development [GO:0001654]; inflammatory response [GO:0006954]; negative regulation of chondrocyte proliferation [GO:1902731]; osteoblast differentiation [GO:0001649]; ovarian cumulus expansion [GO:0001550]; ovulation cycle [GO:0042698]; phosphorylation [GO:0016310]; positive regulation of bone mineralization [GO:0030501]; positive regulation of cartilage development [GO:0061036]; positive regulation of chondrocyte differentiation [GO:0032332]; positive regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902043]; positive regulation of gene expression [GO:0010628]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proteoglycan biosynthetic process [GO:0030166]; retina development in camera-type eye [GO:0060041]; retinal ganglion cell axon guidance [GO:0031290] | dendrite [GO:0030425]; HFE-transferrin receptor complex [GO:1990712]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; BMP binding [GO:0036122]; BMP receptor activity [GO:0098821]; metal ion binding [GO:0046872]; protein serine/threonine kinase activity [GO:0004674]; SMAD binding [GO:0046332]; transforming growth factor beta receptor activity, type I [GO:0005025]; transmembrane receptor protein serine/threonine kinase activity [GO:0004675]; transmembrane signaling receptor activity [GO:0004888] | PF01064;PF07714;PF08515; | 2.10.60.10;1.10.510.10; | Protein kinase superfamily, TKL Ser/Thr protein kinase family, TGFB receptor subfamily | PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P36898}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P36898}; Single-pass type I membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.30; Evidence={ECO:0000250|UniProtKB:P36898}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44881; Evidence={ECO:0000250|UniProtKB:P36898}; CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022, Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.30; Evidence={ECO:0000250|UniProtKB:P36898}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18674; Evidence={ECO:0000250|UniProtKB:P36898}; | null | null | null | null | FUNCTION: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP7/OP-1 and GDF5. Positively regulates chondrocyte differentiation through GDF5 interaction. {ECO:0000250|UniProtKB:P36898}. | Homo sapiens (Human) |
O00241 | SIRB1_HUMAN | MPVPASWPHLPSPFLLMTLLLGRLTGVAGEDELQVIQPEKSVSVAAGESATLRCAMTSLIPVGPIMWFRGAGAGRELIYNQKEGHFPRVTTVSELTKRNNLDFSISISNITPADAGTYYCVKFRKGSPDDVEFKSGAGTELSVRAKPSAPVVSGPAVRATPEHTVSFTCESHGFSPRDITLKWFKNGNELSDFQTNVDPAGDSVSYSIHSTARVVLTRGDVHSQVICEIAHITLQGDPLRGTANLSEAIRVPPTLEVTQQPMRAENQANVTCQVSNFYPRGLQLTWLENGNVSRTETASTLIENKDGTYNWMSWLLVNTCAHRDDVVLTCQVEHDGQQAVSKSYALEISAHQKEHGSDITHEAALAPTAPLLVALLLGPKLLLVVGVSAIYICWKQKA | null | null | cell surface receptor signaling pathway [GO:0007166]; positive regulation of phagocytosis [GO:0050766]; positive regulation of T cell activation [GO:0050870]; signal transduction [GO:0007165] | cell surface [GO:0009986]; plasma membrane [GO:0005886]; secretory granule membrane [GO:0030667] | null | PF07654;PF07686; | 2.60.40.10; | null | PTM: N-glycosylated. {ECO:0000269|PubMed:10604985, ECO:0000269|PubMed:16335952}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10604985}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Immunoglobulin-like cell surface receptor involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes. Participates also in the recruitment of tyrosine kinase SYK. Triggers activation of myeloid cells when associated with TYROBP (PubMed:10604985). {ECO:0000269|PubMed:10604985}. | Homo sapiens (Human) |
O00244 | ATOX1_HUMAN | MPKHEFSVDMTCGGCAEAVSRVLNKLGGVKYDIDLPNKKVCIESEHSMDTLLATLKKTGKTVSYLGLE | null | null | copper ion transport [GO:0006825]; intracellular copper ion homeostasis [GO:0006878]; response to oxidative stress [GO:0006979] | cytosol [GO:0005829] | copper chaperone activity [GO:0016531]; copper ion binding [GO:0005507]; copper-dependent protein binding [GO:0032767]; cuprous ion binding [GO:1903136]; metallochaperone activity [GO:0016530] | PF00403; | 3.30.70.100; | ATX1 family | null | null | null | null | null | null | null | FUNCTION: Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense. | Homo sapiens (Human) |
O00253 | AGRP_HUMAN | MLTAAVLSCALLLALPATRGAQMGLAPMEGIRRPDQALLPELPGLGLRAPLKKTTAEQAEEDLLQEAQALAEVLDLQDREPRSSRRCVRLHESCLGQQVPCCDPCATCYCRFFNAFCYCRKLGTAMNPCSRT | null | null | adult feeding behavior [GO:0008343]; circadian rhythm [GO:0007623]; eating behavior [GO:0042755]; feeding behavior [GO:0007631]; hormone-mediated signaling pathway [GO:0009755]; long-day photoperiodism [GO:0048571]; maternal process involved in female pregnancy [GO:0060135]; neuropeptide signaling pathway [GO:0007218]; positive regulation of feeding behavior [GO:2000253]; regulation of feeding behavior [GO:0060259]; response to insulin [GO:0032868] | extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; neuronal cell body [GO:0043025] | neuropeptide hormone activity [GO:0005184]; signaling receptor binding [GO:0005102]; type 1 melanocortin receptor binding [GO:0070996] | PF05039; | 4.10.760.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15927146}. Golgi apparatus lumen {ECO:0000269|PubMed:15927146}. | null | null | null | null | null | FUNCTION: Plays a role in weight homeostasis. Involved in the control of feeding behavior through the central melanocortin system. Acts as alpha melanocyte-stimulating hormone antagonist by inhibiting cAMP production mediated by stimulation of melanocortin receptors within the hypothalamus and adrenal gland. Has very low activity with MC5R (By similarity). Is an inverse agonist for MC3R and MC4R being able to suppress their constitutive activity. It promotes MC3R and MC4R endocytosis in an arrestin-dependent manner. {ECO:0000250, ECO:0000269|PubMed:10371151, ECO:0000269|PubMed:11145747, ECO:0000269|PubMed:15927146, ECO:0000269|PubMed:17041250, ECO:0000269|PubMed:9892020}. | Homo sapiens (Human) |
O00254 | PAR3_HUMAN | MKALIFAAAGLLLLLPTFCQSGMENDTNNLAKPTLPIKTFRGAPPNSFEEFPFSALEGWTGATITVKIKCPEESASHLHVKNATMGYLTSSLSTKLIPAIYLLVFVVGVPANAVTLWMLFFRTRSICTTVFYTNLAIADFLFCVTLPFKIAYHLNGNNWVFGEVLCRATTVIFYGNMYCSILLLACISINRYLAIVHPFTYRGLPKHTYALVTCGLVWATVFLYMLPFFILKQEYYLVQPDITTCHDVHNTCESSSPFQLYYFISLAFFGFLIPFVLIIYCYAAIIRTLNAYDHRWLWYVKASLLILVIFTICFAPSNIILIIHHANYYYNNTDGLYFIYLIALCLGSLNSCLDPFLYFLMSKTRNHSTAYLTK | null | null | blood coagulation [GO:0007596]; ligand-gated ion channel signaling pathway [GO:1990806]; platelet activation [GO:0030168]; positive regulation of insulin secretion [GO:0032024]; positive regulation of Rho protein signal transduction [GO:0035025]; response to wounding [GO:0009611] | apical plasma membrane [GO:0016324]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | G protein-coupled receptor activity [GO:0004930]; phosphatidylinositol phospholipase C activity [GO:0004435]; receptor ligand activity [GO:0048018]; thrombin-activated receptor activity [GO:0015057] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | PTM: A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand. | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. {ECO:0000269|PubMed:10079109}. | Homo sapiens (Human) |
O00255 | MEN1_HUMAN | MGLKAAQKTLFPLRSIDDVVRLFAAELGREEPDLVLLSLVLGFVEHFLAVNRVIPTNVPELTFQPSPAPDPPGGLTYFPVADLSIIAALYARFTAQIRGAVDLSLYPREGGVSSRELVKKVSDVIWNSLSRSYFKDRAHIQSLFSFITGTKLDSSGVAFAVVGACQALGLRDVHLALSEDHAWVVFGPNGEQTAEVTWHGKGNEDRRGQTVNAGVAERSWLYLKGSYMRCDRKMEVAFMVCAINPSIDLHTDSLELLQLQQKLLWLLYDLGHLERYPMALGNLADLEELEPTPGRPDPLTLYHKGIASAKTYYRDEHIYPYMYLAGYHCRNRNVREALQAWADTATVIQDYNYCREDEEIYKEFFEVANDVIPNLLKEAASLLEAGEERPGEQSQGTQSQGSALQDPECFAHLLRFYDGICKWEEGSPTPVLHVGWATFLVQSLGRFEGQVRQKVRIVSREAEAAEAEEPWGEEAREGRRRGPRRESKPEEPPPPKKPALDKGLGTGQGAVSGPPRKPPGTVAGTARGPEGGSTAQVPAPTASPPPEGPVLTFQSEKMKGMKELLVATKINSSAIKLQLTAQSQVQMKKQKVSTPSDYTLSFLKRQRKGL | null | null | DNA damage response [GO:0006974]; DNA repair [GO:0006281]; MAPK cascade [GO:0000165]; negative regulation of cell cycle [GO:0045786]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045736]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of JNK cascade [GO:0046329]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of telomerase activity [GO:0051974]; negative regulation of transcription by RNA polymerase II [GO:0000122]; osteoblast development [GO:0002076]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; regulation of transcription by RNA polymerase II [GO:0006357]; response to gamma radiation [GO:0010332]; response to UV [GO:0009411]; T-helper 2 cell differentiation [GO:0045064]; transcription initiation-coupled chromatin remodeling [GO:0045815] | chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum lumen [GO:0005788]; histone methyltransferase complex [GO:0035097]; MLL1 complex [GO:0071339]; MLL1/2 complex [GO:0044665]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; transcription repressor complex [GO:0017053] | chromatin binding [GO:0003682]; double-stranded DNA binding [GO:0003690]; four-way junction DNA binding [GO:0000400]; phosphoprotein binding [GO:0051219]; protein-macromolecule adaptor activity [GO:0030674]; R-SMAD binding [GO:0070412]; transcription cis-regulatory region binding [GO:0000976]; Y-form DNA binding [GO:0000403] | PF05053; | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12874027}. Note=Concentrated in nuclear body-like structures. Relocates to the nuclear matrix upon gamma irradiation. | null | null | null | null | null | FUNCTION: Essential component of a MLL/SET1 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3 (H3K4). Functions as a transcriptional regulator. Binds to the TERT promoter and represses telomerase expression. Plays a role in TGFB1-mediated inhibition of cell-proliferation, possibly regulating SMAD3 transcriptional activity. Represses JUND-mediated transcriptional activation on AP1 sites, as well as that mediated by NFKB subunit RELA. Positively regulates HOXC8 and HOXC6 gene expression. May be involved in normal hematopoiesis through the activation of HOXA9 expression (By similarity). May be involved in DNA repair. {ECO:0000250|UniProtKB:O88559, ECO:0000269|PubMed:11274402, ECO:0000269|PubMed:11526476, ECO:0000269|PubMed:12837246, ECO:0000269|PubMed:12874027, ECO:0000269|PubMed:14992727, ECO:0000269|PubMed:22327296}. | Homo sapiens (Human) |
O00257 | CBX4_HUMAN | MELPAVGEHVFAVESIEKKRIRKGRVEYLVKWRGWSPKYNTWEPEENILDPRLLIAFQNRERQEQLMGYRKRGPKPKPLVVQVPTFARRSNVLTGLQDSSTDNRAKLDLGAQGKGQGHQYELNSKKHHQYQPHSKERAGKPPPPGKSGKYYYQLNSKKHHPYQPDPKMYDLQYQGGHKEAPSPTCPDLGAKSHPPDKWAQGAGAKGYLGAVKPLAGAAGAPGKGSEKGPPNGMMPAPKEAVTGNGIGGKMKIVKNKNKNGRIVIVMSKYMENGMQAVKIKSGEVAEGEARSPSHKKRAADERHPPADRTFKKAAGAEEKKVEAPPKRREEEVSGVSDPQPQDAGSRKLSPTKEAFGEQPLQLTTKPDLLAWDPARNTHPPSHHPHPHPHHHHHHHHHHHHAVGLNLSHVRKRCLSETHGEREPCKKRLTARSISTPTCLGGSPAAERPADLPPAAALPQPEVILLDSDLDEPIDLRCVKTRSEAGEPPSSLQVKPETPASAAVAVAAAAAPTTTAEKPPAEAQDEPAESLSEFKPFFGNIIITDVTANCLTVTFKEYVTV | 2.3.2.- | null | chromatin organization [GO:0006325]; negative regulation of apoptotic process [GO:0043066]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; protein sumoylation [GO:0016925] | nuclear body [GO:0016604]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PcG protein complex [GO:0031519]; PRC1 complex [GO:0035102] | chromatin binding [GO:0003682]; enzyme binding [GO:0019899]; methylated histone binding [GO:0035064]; phosphoprotein binding [GO:0051219]; single-stranded RNA binding [GO:0003727]; SUMO binding [GO:0032183]; SUMO ligase activity [GO:0061665]; SUMO transferase activity [GO:0019789]; transcription cis-regulatory region binding [GO:0000976]; transcription corepressor activity [GO:0003714] | PF17218;PF00385; | 2.40.50.40; | null | PTM: Ubiquitinated. Ubiquitination regulates the function of the Polycomb group (PcG) multiprotein PRC1-like complex. Deubiquitinated by USP26. {ECO:0000269|PubMed:28839133}.; PTM: Phosphorylated on Thr-497 by HIPK2 upon DNA damage. This phosphorylation stimulates E3 SUMO-protein ligase activity and promotes sumoylation on Lys-494, as well as sumoylation of other target proteins, such as HNRNPK. {ECO:0000269|PubMed:12679040, ECO:0000269|PubMed:15592428, ECO:0000269|PubMed:17018294}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12679040, ECO:0000269|PubMed:17018294, ECO:0000269|PubMed:18927235, ECO:0000269|PubMed:21282530}. Nucleus speckle {ECO:0000269|PubMed:19266028}. Note=Localization to nuclear polycomb bodies is required for ZNF131 sumoylation (PubMed:22467880). Localized in distinct foci on chromatin (PubMed:18927235). {ECO:0000269|PubMed:18927235, ECO:0000269|PubMed:22467880}. | null | null | PATHWAY: Protein modification; protein sumoylation. | null | null | FUNCTION: E3 SUMO-protein ligase which facilitates SUMO1 conjugation by UBE2I (PubMed:12679040). Involved in the sumoylation of HNRNPK, a p53/TP53 transcriptional coactivator, hence indirectly regulates p53/TP53 transcriptional activation resulting in p21/CDKN1A expression. Monosumoylates ZNF131 (PubMed:22825850). {ECO:0000269|PubMed:12679040, ECO:0000269|PubMed:22825850}.; 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 (PubMed:12167701, PubMed:19636380, PubMed:21282530). PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (PubMed:12167701, PubMed:19636380, PubMed:21282530). Binds to histone H3 trimethylated at 'Lys-9' (H3K9me3) (By similarity). Plays a role in the lineage differentiation of the germ layers in embryonic development (By similarity). {ECO:0000250|UniProtKB:O55187, ECO:0000269|PubMed:12167701, ECO:0000269|PubMed:19636380, ECO:0000269|PubMed:21282530}. | Homo sapiens (Human) |
O00258 | GET1_HUMAN | MSSAAADHWAWLLVLSFVFGCNVLRILLPSFSSFMSRVLQKDAEQESQMRAEIQDMKQELSTVNMMDEFARYARLERKINKMTDKLKTHVKARTAQLAKIKWVISVAFYVLQAALMISLIWKYYSVPVAVVPSKWITPLDRLVAFPTRVAGGVGITCWILVCNKVVAIVLHPFS | null | null | protein insertion into ER membrane [GO:0045048]; protein stabilization [GO:0050821]; tail-anchored membrane protein insertion into ER membrane [GO:0071816] | endoplasmic reticulum membrane [GO:0005789]; GET complex [GO:0043529]; nucleus [GO:0005634] | protein-membrane adaptor activity [GO:0043495] | PF04420; | 1.10.287.660; | WRB/GET1 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21444755}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum (ER) (PubMed:21444755, PubMed:23041287, PubMed:24392163, PubMed:27226539). Together with CAMLG/GET2, acts as a membrane receptor for soluble GET3/TRC40, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol (PubMed:21444755, PubMed:23041287, PubMed:24392163, PubMed:27226539). Required to ensure correct topology and ER insertion of CAMLG (PubMed:31417168, PubMed:32187542). {ECO:0000269|PubMed:21444755, ECO:0000269|PubMed:23041287, ECO:0000269|PubMed:24392163, ECO:0000269|PubMed:27226539, ECO:0000269|PubMed:31417168, ECO:0000269|PubMed:32187542}. | Homo sapiens (Human) |
O00264 | PGRC1_HUMAN | MAAEDVVATGADPSDLESGGLLHEIFTSPLNLLLLGLCIFLLYKIVRGDQPAASGDSDDDEPPPLPRLKRRDFTPAELRRFDGVQDPRILMAINGKVFDVTKGRKFYGPEGPYGVFAGRDASRGLATFCLDKEALKDEYDDLSDLTAAQQETLSDWESQFTFKYHHVGKLLKEGEEPTVYSDEEEPKDESARKND | null | null | heme biosynthetic process [GO:0006783]; positive regulation of lipoprotein transport [GO:0140077]; positive regulation of protein localization to plasma membrane [GO:1903078] | cell body [GO:0044297]; endomembrane system [GO:0012505]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; smooth endoplasmic reticulum membrane [GO:0030868]; specific granule membrane [GO:0035579]; synapse [GO:0045202] | amyloid-beta binding [GO:0001540]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; steroid binding [GO:0005496] | PF00173; | 3.10.120.10; | Cytochrome b5 family, MAPR subfamily | PTM: O-glycosylated; contains chondroitin sulfate attached to Ser-54. Ser-54 is in the cytoplasmic domain but the glycosylated form was detected in urine, suggesting that the membrane-bound form is cleaved, allowing for production of a secreted form which is glycosylated. {ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}. | SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:Q95250}; Single-pass membrane protein {ECO:0000255}. Smooth endoplasmic reticulum membrane {ECO:0000303|PubMed:28396637}; Single-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:O55022}; Single-pass membrane protein {ECO:0000305}; Extracellular side {ECO:0000250|UniProtKB:O55022}. Secreted {ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}. Note=Localized at cell membrane, probably in lipid rafts, in serum-starved conditions. {ECO:0000269|PubMed:30443021}. | null | null | null | null | null | FUNCTION: Component of a progesterone-binding protein complex (PubMed:28396637). Binds progesterone (PubMed:25675345). Has many reported cellular functions (heme homeostasis, interaction with CYPs). Required for the maintenance of uterine histoarchitecture and normal female reproductive lifespan (By similarity). Intracellular heme chaperone. Regulates heme synthesis via interactions with FECH and acts as a heme donor for at least some hemoproteins (PubMed:27599036). Forms a ternary complex with TMEM97 receptor and low density lipid receptor/LDLR, which increases LDLR-mediated LDL lipoprotein internalization (PubMed:30443021). {ECO:0000250|UniProtKB:O55022, ECO:0000269|PubMed:25675345, ECO:0000269|PubMed:27599036, ECO:0000269|PubMed:30443021, ECO:0000303|PubMed:28396637}. | Homo sapiens (Human) |
O00267 | SPT5H_HUMAN | MSDSEDSNFSEEEDSERSSDGEEAEVDEERRSAAGSEKEEEPEDEEEEEEEEEYDEEEEEEDDDRPPKKPRHGGFILDEADVDDEYEDEDQWEDGAEDILEKEEIEASNIDNVVLDEDRSGARRLQNLWRDQREEELGEYYMKKYAKSSVGETVYGGSDELSDDITQQQLLPGVKDPNLWTVKCKIGEERATAISLMRKFIAYQFTDTPLQIKSVVAPEHVKGYIYVEAYKQTHVKQAIEGVGNLRLGYWNQQMVPIKEMTDVLKVVKEVANLKPKSWVRLKRGIYKDDIAQVDYVEPSQNTISLKMIPRIDYDRIKARMSLKDWFAKRKKFKRPPQRLFDAEKIRSLGGDVASDGDFLIFEGNRYSRKGFLFKSFAMSAVITEGVKPTLSELEKFEDQPEGIDLEVVTESTGKEREHNFQPGDNVEVCEGELINLQGKILSVDGNKITIMPKHEDLKDMLEFPAQELRKYFKMGDHVKVIAGRFEGDTGLIVRVEENFVILFSDLTMHELKVLPRDLQLCSETASGVDVGGQHEWGELVQLDPQTVGVIVRLERETFQVLNMYGKVVTVRHQAVTRKKDNRFAVALDSEQNNIHVKDIVKVIDGPHSGREGEIRHLFRSFAFLHCKKLVENGGMFVCKTRHLVLAGGSKPRDVTNFTVGGFAPMSPRISSPMHPSAGGQRGGFGSPGGGSGGMSRGRGRRDNELIGQTVRISQGPYKGYIGVVKDATESTARVELHSTCQTISVDRQRLTTVGSRRPGGMTSTYGRTPMYGSQTPMYGSGSRTPMYGSQTPLQDGSRTPHYGSQTPLHDGSRTPAQSGAWDPNNPNTPSRAEEEYEYAFDDEPTPSPQAYGGTPNPQTPGYPDPSSPQVNPQYNPQTPGTPAMYNTDQFSPYAAPSPQGSYQPSPSPQSYHQVAPSPAGYQNTHSPASYHPTPSPMAYQASPSPSPVGYSPMTPGAPSPGGYNPHTPGSGIEQNSSDWVTTDIQVKVRDTYLDTQVVGQTGVIRSVTGGMCSVYLKDSEKVVSISSEHLEPITPTKNNKVKVILGEDREATGVLLSIDGEDGIVRMDLDEQLKILNLRFLGKLLEA | null | null | negative regulation of DNA-templated transcription, elongation [GO:0032785]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; positive regulation of macroautophagy [GO:0016239]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription elongation by RNA polymerase II [GO:0034243]; transcription elongation by RNA polymerase II [GO:0006368]; transcription elongation-coupled chromatin remodeling [GO:0140673] | DSIF complex [GO:0032044]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; enzyme binding [GO:0019899]; mRNA binding [GO:0003729]; protein heterodimerization activity [GO:0046982]; RNA binding [GO:0003723] | PF00467;PF03439;PF11942; | 2.30.30.30;3.30.70.940; | SPT5 family | PTM: Methylated by PRMT1/HRMT1L2 and PRMT5/SKB1. Methylation negatively regulates interaction with P-TEFb and RNA polymerase II. {ECO:0000269|PubMed:12718890}.; PTM: Phosphorylated by CDK7 and CDK9. Phosphorylation by P-TEFb alleviates transcriptional pausing and can stimulate transcriptional elongation from the HIV-1 LTR. P-TEFb dependent phosphorylation is stimulated by the HIV-1 Tat protein. Phosphorylation may also stimulate interaction with PIN1. Bulk phosphorylation occurs predominantly in mitosis. {ECO:0000269|PubMed:10757782, ECO:0000269|PubMed:11112772, ECO:0000269|PubMed:11145967, ECO:0000269|PubMed:11575923, ECO:0000269|PubMed:11809800, ECO:0000269|PubMed:15564463, ECO:0000269|PubMed:16327805, ECO:0000269|PubMed:9199507}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10075709}. | null | null | null | null | null | FUNCTION: Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites. DSIF can also positively regulate transcriptional elongation and is required for the efficient activation of transcriptional elongation by the HIV-1 nuclear transcriptional activator, Tat. DSIF acts to suppress transcriptional pausing in transcripts derived from the HIV-1 LTR and blocks premature release of HIV-1 transcripts at terminator sequences. {ECO:0000269|PubMed:10075709, ECO:0000269|PubMed:10199401, ECO:0000269|PubMed:10393184, ECO:0000269|PubMed:10421630, ECO:0000269|PubMed:10454543, ECO:0000269|PubMed:10757782, ECO:0000269|PubMed:10912001, ECO:0000269|PubMed:11112772, ECO:0000269|PubMed:11553615, ECO:0000269|PubMed:11809800, ECO:0000269|PubMed:12653964, ECO:0000269|PubMed:12718890, ECO:0000269|PubMed:14701750, ECO:0000269|PubMed:15136722, ECO:0000269|PubMed:15380072, ECO:0000269|PubMed:16214896, ECO:0000269|PubMed:9450929, ECO:0000269|PubMed:9514752, ECO:0000269|PubMed:9857195}. | Homo sapiens (Human) |
O00268 | TAF4_HUMAN | MAAGSDLLDEVFFNSEVDEKVVSDLVGSLESQLAASAAHHHHLAPRTPEVRAAAAGALGNHVVSGSPAGAAGAGPAAPAEGAPGAAPEPPPAGRARPGGGGPQRPGPPSPRRPLVPAGPAPPAAKLRPPPEGSAGSCAPVPAAAAVAAGPEPAPAGPAKPAGPAALAARAGPGPGPGPGPGPGPGPGKPAGPGAAQTLNGSAALLNSHHAAAPAVSLVNNGPAALLPLPKPAAPGTVIQTPPFVGAAAPPAPAAPSPPAAPAPAAPAAAPPPPPPAPATLARPPGHPAGPPTAAPAVPPPAAAQNGGSAGAAPAPAPAAGGPAGVSGQPGPGAAAAAPAPGVKAESPKRVVQAAPPAAQTLAASGPASTAASMVIGPTMQGALPSPAAVPPPAPGTPTGLPKGAAGAVTQSLSRTPTATTSGIRATLTPTVLAPRLPQPPQNPTNIQNFQLPPGMVLVRSENGQLLMIPQQALAQMQAQAHAQPQTTMAPRPATPTSAPPVQISTVQAPGTPIIARQVTPTTIIKQVSQAQTTVQPSATLQRSPGVQPQLVLGGAAQTASLGTATAVQTGTPQRTVPGATTTSSAATETMENVKKCKNFLSTLIKLASSGKQSTETAANVKELVQNLLDGKIEAEDFTSRLYRELNSSPQPYLVPFLKRSLPALRQLTPDSAAFIQQSQQQPPPPTSQATTALTAVVLSSSVQRTAGKTAATVTSALQPPVLSLTQPTQVGVGKQGQPTPLVIQQPPKPGALIRPPQVTLTQTPMVALRQPHNRIMLTTPQQIQLNPLQPVPVVKPAVLPGTKALSAVSAQAAAAQKNKLKEPGGGSFRDDDDINDVASMAGVNLSEESARILATNSELVGTLTRSCKDETFLLQAPLQRRILEIGKKHGITELHPDVVSYVSHATQQRLQNLVEKISETAQQKNFSYKDDDRYEQASDVRAQLKFFEQLDQIEKQRKDEQEREILMRAAKSRSRQEDPEQLRLKQKAKEMQQQELAQMRQRDANLTALAAIGPRKKRKVDCPGPGSGAEGSGPGSVVPGSSGVGTPRQFTRQRITRVNLRDLIFCLENERETSHSLLLYKAFLK | null | null | DNA-templated transcription initiation [GO:0006352]; mRNA transcription by RNA polymerase II [GO:0042789]; ovarian follicle development [GO:0001541]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261]; regulation of DNA repair [GO:0006282]; regulation of transcription by RNA polymerase II [GO:0006357]; RNA polymerase II preinitiation complex assembly [GO:0051123]; transcription by RNA polymerase II [GO:0006366]; transcription initiation at RNA polymerase II promoter [GO:0006367] | chromatin [GO:0000785]; cytosol [GO:0005829]; male germ cell nucleus [GO:0001673]; MLL1 complex [GO:0071339]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; transcription factor TFIID complex [GO:0005669]; transcription factor TFTC complex [GO:0033276] | aryl hydrocarbon receptor binding [GO:0017162]; DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; RNA polymerase II general transcription initiation factor activity [GO:0016251] | PF05236;PF07531; | 1.10.20.10;1.20.120.1110; | TAF4 family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (PubMed:33795473). TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (PubMed:33795473). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:10594036, PubMed:33795473, PubMed:8942982). TAF4 may maintain an association between the TFIID and TFIIA complexes, while bound to the promoter, together with TBP, during PIC assembly (PubMed:33795473). Potentiates transcriptional activation by the AF-2S of the retinoic acid, vitamin D3 and thyroid hormone (PubMed:9192867). {ECO:0000269|PubMed:10594036, ECO:0000269|PubMed:33795473, ECO:0000269|PubMed:8942982, ECO:0000269|PubMed:9192867}. | Homo sapiens (Human) |
O00270 | GPR31_HUMAN | MPFPNCSAPSTVVATAVGVLLGLECGLGLLGNAVALWTFLFRVRVWKPYAVYLLNLALADLLLAACLPFLAAFYLSLQAWHLGRVGCWALHFLLDLSRSVGMAFLAAVALDRYLRVVHPRLKVNLLSPQAALGVSGLVWLLMVALTCPGLLISEAAQNSTRCHSFYSRADGSFSIIWQEALSCLQFVLPFGLIVFCNAGIIRALQKRLREPEKQPKLQRAQALVTLVVVLFALCFLPCFLARVLMHIFQNLGSCRALCAVAHTSDVTGSLTYLHSVLNPVVYCFSSPTFRSSYRRVFHTLRGKGQAAEPPDFNPRDSYS | null | null | G protein-coupled receptor signaling pathway [GO:0007186]; lipid metabolic process [GO:0006629]; negative regulation of inflammatory response [GO:0050728]; positive regulation of immune response [GO:0050778]; response to acidic pH [GO:0010447]; response to ischemia [GO:0002931]; response to molecule of bacterial origin [GO:0002237] | plasma membrane [GO:0005886] | arachidonic acid binding [GO:0050544]; bioactive lipid receptor activity [GO:0045125]; G protein-coupled receptor activity [GO:0004930] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21712392, ECO:0000269|PubMed:28619714, ECO:0000269|PubMed:31119277}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: High-affinity receptor for 12-(S)-hydroxy-5,8,10,14-eicosatetraenoic acid (12-S-HETE), with much lower affinities for other HETE isomers (PubMed:21712392, PubMed:29227475). 12-S-HETE is a eicosanoid, a 12-lipoxygenase (ALOX12) metabolite of arachidonic acid, involved in many physiologic and pathologic processes (PubMed:26965684, PubMed:28619714, PubMed:29227475). 12-S-HETE-binding leads to activation of ERK1/2 (MAPK3/MAPK1), MEK, and NF-kappa-B pathways leading to cell growth (PubMed:21712392, PubMed:29227475). Plays a crucial role for proliferation, survival and macropinocytosis of KRAS-dependent cancer cells by mediating the translocation of KRAS from the endoplasmic reticulum to the plasma membrane (PM) and its association with the PM (PubMed:28619714). Contributes to enhanced immune responses by inducing dendrite protrusion of small intestinal CX3CR1(+) phagocytes for the uptake of luminal antigens (By similarity). Acts also as a key receptor for 12-(S)-HETE-mediated liver ischemia reperfusion injury (PubMed:29227475). {ECO:0000250|UniProtKB:F8VQN3, ECO:0000269|PubMed:21712392, ECO:0000269|PubMed:26965684, ECO:0000269|PubMed:28619714, ECO:0000269|PubMed:29227475}.; FUNCTION: Proton-sensing G protein-coupled receptor. {ECO:0000269|PubMed:31119277}. | Homo sapiens (Human) |
O00273 | DFFA_HUMAN | MEVTGDAGVPESGEIRTLKPCLLRRNYSREQHGVAASCLEDLRSKACDILAIDKSLTPVTLVLAEDGTIVDDDDYFLCLPSNTKFVALASNEKWAYNNSDGGTAWISQESFDVDETDSGAGLKWKNVARQLKEDLSSIILLSEEDLQMLVDAPCSDLAQELRQSCATVQRLQHTLQQVLDQREEVRQSKQLLQLYLQALEKEGSLLSKQEESKAAFGEEVDAVDTGISRETSSDVALASHILTALREKQAPELSLSSQDLELVTKEDPKALAVALNWDIKKTETVQEACERELALRLQQTQSLHSLRSISASKASPPGDLQNPKRARQDPT | null | null | apoptotic DNA fragmentation [GO:0006309]; chaperone-mediated protein folding [GO:0061077]; negative regulation of apoptotic DNA fragmentation [GO:1902511]; negative regulation of deoxyribonuclease activity [GO:0032076]; negative regulation of execution phase of apoptosis [GO:1900118]; positive regulation of apoptotic process [GO:0043065]; thymocyte apoptotic process [GO:0070242] | chromatin [GO:0000785]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | deoxyribonuclease inhibitor activity [GO:0060703]; protein domain specific binding [GO:0019904]; protein folding chaperone [GO:0044183] | PF02017;PF09033; | 3.10.20.10;1.10.1490.10; | null | PTM: Caspase-3 cleaves DFF45 at 2 sites to generate an active factor. | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Inhibitor of the caspase-activated DNase (DFF40). | Homo sapiens (Human) |
O00287 | RFXAP_HUMAN | MEAQGVAEGAGPGAASGVPHPAALAPAAAPTLAPASVAAAASQFTLLVMQPCAGQDEAAAPGGSVGAGKPVRYLCEGAGDGEEEAGEDEADLLDTSDPPGGGESAASLEDLEDEETHSGGEGSSGGARRRGSGGGSMSKTCTYEGCSETTSQVAKQRKPWMCKKHRNKMYKDKYKKKKSDQALNCGGTASTGSAGNVKLEESADNILSIVKQRTGSFGDRPARPTLLEQVLNQKRLSLLRSPEVVQFLQKQQQLLNQQVLEQRQQQFPGTSM | null | null | positive regulation of MHC class II biosynthetic process [GO:0045348]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357] | nuclear speck [GO:0016607]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | DNA binding [GO:0003677] | PF15289; | 6.10.290.30; | null | PTM: Phosphorylated. | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Part of the RFX complex that binds to the X-box of MHC II promoters. | Homo sapiens (Human) |
O00291 | HIP1_HUMAN | MDRMASSMKQVPNPLPKVLSRRGVGAGLEAAERESFERTQTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRNELSDMSRMWGHLSEGYGQLCSIYLKLLRTKMEYHTKNPRFPGNLQMSDRQLDEAGESDVNNFFQLTVEMFDYLECELNLFQTVFNSLDMSRSVSVTAAGQCRLAPLIQVILDCSHLYDYTVKLLFKLHSCLPADTLQGHRDRFMEQFTKLKDLFYRSSNLQYFKRLIQIPQLPENPPNFLRASALSEHISPVVVIPAEASSPDSEPVLEKDDLMDMDASQQNLFDNKFDDIFGSSFSSDPFNFNSQNGVNKDEKDHLIERLYREISGLKAQLENMKTESQRVVLQLKGHVSELEADLAEQQHLRQQAADDCEFLRAELDELRRQREDTEKAQRSLSEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSMARQAQVDLEREKKELEDSLERISDQGQRKTQEQLEVLESLKQELATSQRELQVLQGSLETSAQSEANWAAEFAELEKERDSLVSGAAHREEELSALRKELQDTQLKLASTEESMCQLAKDQRKMLLVGSRKAAEQVIQDALNQLEEPPLISCAGSADHLLSTVTSISSCIEQLEKSWSQYLACPEDISGLLHSITLLAHLTSDAIAHGATTCLRAPPEPADSLTEACKQYGRETLAYLASLEEEGSLENADSTAMRNCLSKIKAIGEELLPRGLDIKQEELGDLVDKEMAATSAAIETATARIEEMLSKSRAGDTGVKLEVNERILGCCTSLMQAIQVLIVASKDLQREIVESGRGTASPKEFYAKNSRWTEGLISASKAVGWGATVMVDAADLVVQGRGKFEELMVCSHEIAASTAQLVAASKVKADKDSPNLAQLQQASRGVNQATAGVVASTISGKSQIEETDNMDFSSMTLTQIKRQEMDSQVRVLELENELQKERQKLGELRKKHYELAGVAEGWEEGTEASPPTLQEVVTEKE | null | null | actin filament organization [GO:0007015]; activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; cell differentiation [GO:0030154]; clathrin coat assembly [GO:0048268]; endocytosis [GO:0006897]; neurotransmitter receptor transport [GO:0099637]; positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of platelet-derived growth factor receptor-beta signaling pathway [GO:2000588]; positive regulation of receptor-mediated endocytosis [GO:0048260]; presynaptic modulation of chemical synaptic transmission [GO:0099171]; protein stabilization [GO:0050821]; regulation of apoptotic process [GO:0042981]; regulation of endocytosis [GO:0030100]; regulation of postsynaptic neurotransmitter receptor internalization [GO:0099149] | clathrin-coated vesicle [GO:0030136]; clathrin-coated vesicle membrane [GO:0030665]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleus [GO:0005634]; postsynapse [GO:0098794]; postsynaptic membrane [GO:0045211]; presynapse [GO:0098793]; presynaptic membrane [GO:0042734]; Schaffer collateral - CA1 synapse [GO:0098685] | actin filament binding [GO:0051015]; AP-2 adaptor complex binding [GO:0035612]; clathrin adaptor activity [GO:0035615]; clathrin binding [GO:0030276]; clathrin light chain binding [GO:0032051]; epidermal growth factor receptor binding [GO:0005154]; glutamate receptor binding [GO:0035254]; phosphatidylinositol binding [GO:0035091]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; phosphatidylinositol-3-phosphate binding [GO:0032266]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; structural constituent of cytoskeleton [GO:0005200] | PF07651;PF16515;PF01608; | 1.20.5.1700;1.25.40.90;6.10.250.920;1.20.1410.10; | SLA2 family | null | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Endomembrane system. Cytoplasmic vesicle, clathrin-coated vesicle membrane. Note=Shuttles between cytoplasm and nucleus. Nuclear translocation can be induced by AR. | null | null | null | null | null | FUNCTION: Plays a role in clathrin-mediated endocytosis and trafficking (PubMed:11532990, PubMed:11577110, PubMed:11889126). Involved in regulating AMPA receptor trafficking in the central nervous system in an NMDA-dependent manner (By similarity). Regulates presynaptic nerve terminal activity (By similarity). Enhances androgen receptor (AR)-mediated transcription (PubMed:16027218). May act as a proapoptotic protein that induces cell death by acting through the intrinsic apoptosis pathway (PubMed:11007801). Binds 3-phosphoinositides (via ENTH domain) (PubMed:14732715). May act through the ENTH domain to promote cell survival by stabilizing receptor tyrosine kinases following ligand-induced endocytosis (PubMed:14732715). May play a functional role in the cell filament networks (PubMed:18790740). May be required for differentiation, proliferation, and/or survival of somatic and germline progenitors (PubMed:11007801, PubMed:12163454). {ECO:0000250|UniProtKB:Q8VD75, ECO:0000269|PubMed:11007801, ECO:0000269|PubMed:11532990, ECO:0000269|PubMed:11577110, ECO:0000269|PubMed:11889126, ECO:0000269|PubMed:12163454, ECO:0000269|PubMed:14732715, ECO:0000269|PubMed:16027218, ECO:0000269|PubMed:18790740, ECO:0000269|PubMed:9147654}. | Homo sapiens (Human) |
O00292 | LFTY2_HUMAN | MWPLWLCWALWVLPLAGPGAALTEEQLLGSLLRQLQLSEVPVLDRADMEKLVIPAHVRAQYVVLLRRSHGDRSRGKRFSQSFREVAGRFLASEASTHLLVFGMEQRLPPNSELVQAVLRLFQEPVPKAALHRHGRLSPRSAQARVTVEWLRVRDDGSNRTSLIDSRLVSVHESGWKAFDVTEAVNFWQQLSRPRQPLLLQVSVQREHLGPLASGAHKLVRFASQGAPAGLGEPQLELHTLDLRDYGAQGDCDPEAPMTEGTRCCRQEMYIDLQGMKWAKNWVLEPPGFLAYECVGTCQQPPEALAFNWPFLGPRQCIASETASLPMIVSIKEGGRTRPQVVSLPNMRVQKCSCASDGALVPRRLQP | null | null | anterior/posterior axis specification [GO:0009948] | collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; platelet alpha granule lumen [GO:0031093] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; transforming growth factor beta receptor binding [GO:0005160] | PF00019;PF00688; | 2.60.120.970;2.10.90.10; | TGF-beta family | PTM: The processing of the protein may also occur at the second R-X-X-R site located at AA 132-135. Processing appears to be regulated in a cell-type specific manner. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Required for left-right (L-R) asymmetry determination of organ systems in mammals. May play a role in endometrial bleeding. | Homo sapiens (Human) |
O00294 | TULP1_HUMAN | MPLRDETLREVWASDSGHEEESLSPEAPRRPKQRPAPAQRLRKKRTEAPESPCPTGSKPRKPGAGRTGRPREEPSPDPAQARAPQTVYARFLRDPEAKKRDPRETFLVARAPDAEDEEEEEEEDEEDEEEEAEEKKEKILLPPKKPLREKSSADLKERRAKAQGPRGDLGSPDPPPKPLRVRNKEAPAGEGTKMRKTKKKGSGEADKDPSGSPASARKSPAAMFLVGEGSPDKKALKKKGTPKGARKEEEEEEEAATVIKKSNQKGKAKGKGKKKAKEERAPSPPVEVDEPREFVLRPAPQGRTVRCRLTRDKKGMDRGMYPSYFLHLDTEKKVFLLAGRKRKRSKTANYLISIDPTNLSRGGENFIGKLRSNLLGNRFTVFDNGQNPQRGYSTNVASLRQELAAVIYETNVLGFRGPRRMTVIIPGMSAENERVPIRPRNASDGLLVRWQNKTLESLIELHNKPPVWNDDSGSYTLNFQGRVTQASVKNFQIVHADDPDYIVLQFGRVAEDAFTLDYRYPLCALQAFAIALSSFDGKLACE | null | null | dendrite development [GO:0016358]; detection of light stimulus involved in visual perception [GO:0050908]; eye photoreceptor cell development [GO:0042462]; phagocytosis, recognition [GO:0006910]; photoreceptor cell maintenance [GO:0045494]; positive regulation of phagocytosis [GO:0050766]; protein localization to cilium [GO:0061512]; protein localization to photoreceptor outer segment [GO:1903546]; retina development in camera-type eye [GO:0060041]; retina homeostasis [GO:0001895]; visual perception [GO:0007601] | axon terminus [GO:0043679]; cell projection [GO:0042995]; cilium [GO:0005929]; cytosol [GO:0005829]; extracellular region [GO:0005576]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]; synapse [GO:0045202] | actin filament binding [GO:0051015]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546] | PF01167; | null | TUB family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16303976}. Cell membrane {ECO:0000269|PubMed:16303976}; Peripheral membrane protein {ECO:0000269|PubMed:16303976}; Cytoplasmic side {ECO:0000269|PubMed:16303976}. Secreted {ECO:0000250}. Synapse {ECO:0000250}. Note=Detected at synapses between photoreceptor cells and second-order neurons. Does not have a cleavable signal peptide and is secreted by an alternative pathway (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Required for normal development of photoreceptor synapses. Required for normal photoreceptor function and for long-term survival of photoreceptor cells. Interacts with cytoskeleton proteins and may play a role in protein transport in photoreceptor cells (By similarity). Binds lipids, especially phosphatidylinositol 3-phosphate, phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 3,4-bisphosphate, phosphatidylinositol 4,5-bisphosphate, phosphatidylinositol 3,4,5-bisphosphate, phosphatidylserine and phosphatidic acid (in vitro). Contribute to stimulation of phagocytosis of apoptotic retinal pigment epithelium (RPE) cells and macrophages. {ECO:0000250, ECO:0000269|PubMed:16303976, ECO:0000269|PubMed:19837063}. | Homo sapiens (Human) |
O00299 | CLIC1_HUMAN | MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKIEEFLEAVLCPPRYPKLAALNPESNTAGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDETSAEDEGVSQRKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVAKALK | null | null | chloride transport [GO:0006821]; platelet aggregation [GO:0070527]; positive regulation of osteoblast differentiation [GO:0045669]; regulation of mitochondrial membrane potential [GO:0051881]; signal transduction [GO:0007165] | blood microparticle [GO:0072562]; brush border [GO:0005903]; chloride channel complex [GO:0034707]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; vesicle [GO:0031982] | cadherin binding [GO:0045296]; chloride channel activity [GO:0005254] | PF13410;PF13409; | 1.20.1050.10;3.40.30.10; | Chloride channel CLIC family | PTM: Hydrogen peroxide treatment causes a conformation change, leading to dimerization and formation of an intramolecular disulfide bond between Cys-24 and Cys-59. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12681486, ECO:0000269|PubMed:9139710}. Nucleus membrane {ECO:0000269|PubMed:9139710}; Single-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:10793131, ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:12681486, ECO:0000269|PubMed:9139710, ECO:0000305|PubMed:11978800, ECO:0000305|PubMed:14613939}. Cell membrane {ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:11940526, ECO:0000269|PubMed:14613939, ECO:0000305|PubMed:11978800}; Single-pass membrane protein {ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:14613939}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q6MG61}. Note=Mostly in the nucleus including in the nuclear membrane (PubMed:12681486, PubMed:9139710). Small amount in the cytoplasm and the plasma membrane (PubMed:9139710). Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain (PubMed:11551966, PubMed:11940526, PubMed:12681486, PubMed:14613939, PubMed:9139710). Might not be present in the nucleus of cardiac cells (By similarity). {ECO:0000250|UniProtKB:Q6MG61, ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:11940526, ECO:0000269|PubMed:12681486, ECO:0000269|PubMed:14613939, ECO:0000269|PubMed:9139710}. | CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:11195932, ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:11978800, ECO:0000269|PubMed:14613939, ECO:0000269|PubMed:9139710}; | null | null | null | null | FUNCTION: Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Involved in regulation of the cell cycle. {ECO:0000269|PubMed:10834939, ECO:0000269|PubMed:11195932, ECO:0000269|PubMed:11551966, ECO:0000269|PubMed:11940526, ECO:0000269|PubMed:11978800, ECO:0000269|PubMed:14613939, ECO:0000269|PubMed:9139710}. | Homo sapiens (Human) |
O00300 | TR11B_HUMAN | MNNLLCCALVFLDISIKWTTQETFPPKYLHYDEETSHQLLCDKCPPGTYLKQHCTAKWKTVCAPCPDHYYTDSWHTSDECLYCSPVCKELQYVKQECNRTHNRVCECKEGRYLEIEFCLKHRSCPPGFGVVQAGTPERNTVCKRCPDGFFSNETSSKAPCRKHTNCSVFGLLLTQKGNATHDNICSGNSESTQKCGIDVTLCEEAFFRFAVPTKFTPNWLSVLVDNLPGTKVNAESVERIKRQHSSQEQTFQLLKLWKHQNKDQDIVKKIIQDIDLCENSVQRHIGHANLTFEQLRSLMESLPGKKVGAEDIEKTIKACKPSDQILKLLSLWRIKNGDQDTLKGLMHALKHSKTYHFPKTVTQSLKKTIRFLHSFTMYKLYQKLFLEMIGNQVQSVKISCL | null | null | apoptotic process [GO:0006915]; extracellular matrix organization [GO:0030198]; negative regulation of bone resorption [GO:0045779]; negative regulation of odontogenesis of dentin-containing tooth [GO:0042489]; negative regulation of osteoclast differentiation [GO:0045671]; negative regulation of tumor necrosis factor-mediated signaling pathway [GO:0010804]; response to arsenic-containing substance [GO:0046685]; response to estrogen [GO:0043627]; response to magnesium ion [GO:0032026]; response to nutrient [GO:0007584]; response to xenobiotic stimulus [GO:0009410]; signal transduction [GO:0007165]; skeletal system development [GO:0001501] | extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | cytokine activity [GO:0005125]; heparan sulfate binding [GO:1904399]; signaling receptor activity [GO:0038023] | PF00531;PF00020; | 1.10.533.10;2.10.50.10; | null | PTM: N-glycosylated. Contains sialic acid residues. {ECO:0000269|PubMed:22664871}.; PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Acts as a decoy receptor for TNFSF11/RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arterial calcification. May act as decoy receptor for TNFSF10/TRAIL and protect against apoptosis. TNFSF10/TRAIL binding blocks the inhibition of osteoclastogenesis. {ECO:0000269|PubMed:22664871, ECO:0000269|PubMed:9168977}. | Homo sapiens (Human) |
O00303 | EIF3F_HUMAN | MATPAVPVSAPPATPTPVPAAAPASVPAPTPAPAAAPVPAAAPASSSDPAAAAAATAAPGQTPASAQAPAQTPAPALPGPALPGPFPGGRVVRLHPVILASIVDSYERRNEGAARVIGTLLGTVDKHSVEVTNCFSVPHNESEDEVAVDMEFAKNMYELHKKVSPNELILGWYATGHDITEHSVLIHEYYSREAPNPIHLTVDTSLQNGRMSIKAYVSTLMGVPGRTMGVMFTPLTVKYAYYDTERIGVDLIMKTCFSPNRVIGLSSDLQQVGGASARIQDALSTVLQYAEDVLSGKVSADNTVGRFLMSLVNQVPKIVPDDFETMLNSNINDLLMVTYLANLTQSQIALNEKLVNL | 3.4.19.12 | null | formation of cytoplasmic translation initiation complex [GO:0001732]; IRES-dependent viral translational initiation [GO:0075522]; protein deubiquitination [GO:0016579]; proteolysis [GO:0006508]; translational initiation [GO:0006413] | cytosol [GO:0005829]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; eukaryotic translation initiation factor 3 complex, eIF3m [GO:0071541]; membrane [GO:0016020]; synapse [GO:0045202] | cysteine-type deubiquitinase activity [GO:0004843]; identical protein binding [GO:0042802]; metal-dependent deubiquitinase activity [GO:0140492]; translation initiation factor activity [GO:0003743]; translation initiation factor binding [GO:0031369] | PF01398;PF13012; | 3.40.140.10; | EIF-3 subunit F family | PTM: Phosphorylation is enhanced upon serum stimulation. Phosphorylated during apoptosis by caspase-processed CDK11. {ECO:0000269|PubMed:12446680, ECO:0000269|PubMed:17322308}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03005}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:21124883}; | null | null | null | null | FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). {ECO:0000255|HAMAP-Rule:MF_03005, ECO:0000269|PubMed:17581632, ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}.; FUNCTION: Deubiquitinates activated NOTCH1, promoting its nuclear import, thereby acting as a positive regulator of Notch signaling. {ECO:0000269|PubMed:21124883}. | Homo sapiens (Human) |
O00305 | CACB4_HUMAN | MSSSSYAKNGTADGPHSPTSQVARGTTTRRSRLKRSDGSTTSTSFILRQGSADSYTSRPSDSDVSLEEDREAIRQEREQQAAIQLERAKSKPVAFAVKTNVSYCGALDEDVPVPSTAISFDAKDFLHIKEKYNNDWWIGRLVKEGCEIGFIPSPLRLENIRIQQEQKRGRFHGGKSSGNSSSSLGEMVSGTFRATPTSTAKQKQKVTEHIPPYDVVPSMRPVVLVGPSLKGYEVTDMMQKALFDFLKHRFDGRISITRVTADISLAKRSVLNNPSKRAIIERSNTRSSLAEVQSEIERIFELARSLQLVVLDADTINHPAQLIKTSLAPIIVHVKVSSPKVLQRLIKSRGKSQSKHLNVQLVAADKLAQCPPEMFDVILDENQLEDACEHLGEYLEAYWRATHTTSSTPMTPLLGRNLGSTALSPYPTAISGLQSQRMRHSNHSTENSPIERRSLMTSDENYHNERARKSRNRLSSSSQHSRDHYPLVEEDYPDSYQDTYKPHRNRGSPGGYSHDSRHRL | null | null | adult walking behavior [GO:0007628]; cAMP metabolic process [GO:0046058]; cellular response to leukemia inhibitory factor [GO:1990830]; chemical synaptic transmission [GO:0007268]; detection of light stimulus involved in visual perception [GO:0050908]; gamma-aminobutyric acid secretion [GO:0014051]; gamma-aminobutyric acid signaling pathway [GO:0007214]; muscle cell development [GO:0055001]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; neuromuscular junction development [GO:0007528]; neuronal action potential propagation [GO:0019227]; Peyer's patch development [GO:0048541]; positive regulation of protein localization to nucleolus [GO:1904751]; regulation of synaptic vesicle exocytosis [GO:2000300]; regulation of voltage-gated calcium channel activity [GO:1901385]; spleen development [GO:0048536]; synaptic transmission, glutamatergic [GO:0035249]; T cell receptor signaling pathway [GO:0050852]; thymus development [GO:0048538] | cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; nuclear speck [GO:0016607]; plasma membrane [GO:0005886]; presynapse [GO:0098793]; synapse [GO:0045202]; voltage-gated calcium channel complex [GO:0005891] | protein kinase binding [GO:0019901]; voltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels [GO:0099626] | PF00625;PF12052; | 3.40.50.300;2.30.30.40; | Calcium channel beta subunit family | null | null | null | null | null | null | null | FUNCTION: The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting. {ECO:0000269|PubMed:11880487}. | Homo sapiens (Human) |
O00308 | WWP2_HUMAN | MASASSSRAGVALPFEKSQLTLKVVSAKPKVHNRQPRINSYVEVAVDGLPSETKKTGKRIGSSELLWNEIIILNVTAQSHLDLKVWSCHTLRNELLGTASVNLSNVLKNNGGKMENMQLTLNLQTENKGSVVSGGELTIFLDGPTVDLGNVPNGSALTDGSQLPSRDSSGTAVAPENRHQPPSTNCFGGRSRTHRHSGASARTTPATGEQSPGARSRHRQPVKNSGHSGLANGTVNDEPTTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAAQAPDALPAGWEQRELPNGRVYYVDHNTKTTTWERPLPPGWEKRTDPRGRFYYVDHNTRTTTWQRPTAEYVRNYEQWQSQRNQLQGAMQHFSQRFLYQSSSASTDHDPLGPLPPGWEKRQDNGRVYYVNHNTRTTQWEDPRTQGMIQEPALPPGWEMKYTSEGVRYFVDHNTRTTTFKDPRPGFESGTKQGSPGAYDRSFRWKYHQFRFLCHSNALPSHVKISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYFIQDMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKSTIYRHYTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELIGSNGPQKFCIDKVGKETWLPRSHTCFNRLDLPPYKSYEQLREKLLYAIEETEGFGQE | 2.3.2.26 | null | extracellular transport [GO:0006858]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression [GO:0010629]; negative regulation of Notch signaling pathway [GO:0045746]; negative regulation of protein transport [GO:0051224]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transporter activity [GO:0032410]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein autoubiquitination [GO:0051865]; protein K63-linked ubiquitination [GO:0070534]; protein modification process [GO:0036211]; protein ubiquitination [GO:0016567]; regulation of membrane potential [GO:0042391]; regulation of monoatomic ion transmembrane transport [GO:0034765]; regulation of potassium ion transmembrane transporter activity [GO:1901016]; symbiont entry into host cell [GO:0046718]; transcription by RNA polymerase II [GO:0006366] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151] | RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription factor binding [GO:0008134]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842] | PF00632;PF00397; | 2.20.70.10;2.60.40.150;3.30.2160.10;3.30.2410.10;3.90.1750.10; | null | PTM: Autoubiquitinated. Ubiquitinated by the SCF(FBXL15) complex, leading to its degradation by the proteasome. {ECO:0000269|PubMed:19343052, ECO:0000269|PubMed:21572392}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19274063, ECO:0000269|PubMed:20858735}. | 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:19274063, ECO:0000269|PubMed:19651900}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:19274063, ECO:0000269|PubMed:19651900}. | null | null | FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Polyubiquitinates POU5F1 by 'Lys-63'-linked conjugation and promotes it to proteasomal degradation; in embryonic stem cells (ESCs) the ubiquitination is proposed to regulate POU5F1 protein level. Ubiquitinates EGR2 and promotes it to proteasomal degradation; in T-cells the ubiquitination inhibits activation-induced cell death. Ubiquitinates SLC11A2; the ubiquitination is enhanced by presence of NDFIP1 and NDFIP2. Ubiquitinates RPB1 and promotes it to proteasomal degradation. {ECO:0000269|PubMed:19274063, ECO:0000269|PubMed:19651900}. | Homo sapiens (Human) |
O00311 | CDC7_HUMAN | MEASLGIQMDEPMAFSPQRDRFQAEGSLKKNEQNFKLAGVKKDIEKLYEAVPQLSNVFKIEDKIGEGTFSSVYLATAQLQVGPEEKIALKHLIPTSHPIRIAAELQCLTVAGGQDNVMGVKYCFRKNDHVVIAMPYLEHESFLDILNSLSFQEVREYMLNLFKALKRIHQFGIVHRDVKPSNFLYNRRLKKYALVDFGLAQGTHDTKIELLKFVQSEAQQERCSQNKSHIITGNKIPLSGPVPKELDQQSTTKASVKRPYTNAQIQIKQGKDGKEGSVGLSVQRSVFGERNFNIHSSISHESPAVKLMKQSKTVDVLSRKLATKKKAISTKVMNSAVMRKTASSCPASLTCDCYATDKVCSICLSRRQQVAPRAGTPGFRAPEVLTKCPNQTTAIDMWSAGVIFLSLLSGRYPFYKASDDLTALAQIMTIRGSRETIQAAKTFGKSILCSKEVPAQDLRKLCERLRGMDSSTPKLTSDIQGHASHQPAISEKTDHKASCLVQTPPGQYSGNSFKKGDSNSCEHCFDEYNTNLEGWNEVPDEAYDLLDKLLDLNPASRITAEEALLHPFFKDMSL | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | cell cycle phase transition [GO:0044770]; cell division [GO:0051301]; double-strand break repair via break-induced replication [GO:0000727]; G1/S transition of mitotic cell cycle [GO:0000082]; mitotic DNA damage checkpoint signaling [GO:0044773]; phosphorylation [GO:0016310]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; positive regulation of nuclear cell cycle DNA replication [GO:0010571]; signal transduction [GO:0007165] | cytoplasm [GO:0005737]; intercellular bridge [GO:0045171]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | ATP binding [GO:0005524]; kinase activity [GO:0016301]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, CDC7 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:27401717}. | 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:27401717}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000269|PubMed:27401717}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:27401717}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000269|PubMed:27401717}; | null | null | null | null | FUNCTION: Kinase involved in initiation of DNA replication. Phosphorylates critical substrates that regulate the G1/S phase transition and initiation of DNA replication, such as MCM proteins and CLASPIN. {ECO:0000269|PubMed:12065429, ECO:0000269|PubMed:27401717}. | Homo sapiens (Human) |
O00322 | UPK1A_HUMAN | MASAAAAEAEKGSPVVVGLLVVGNIIILLSGLSLFAETIWVTADQYRVYPLMGVSGKDDVFAGAWIAIFCGFSFFMVASFGVGAALCRRRSMVLTYLVLMLIVYIFECASCITSYTHRDYMVSNPSLITKQMLTFYSADTDQGQELTRLWDRVMIEQECCGTSGPMDWVNFTSAFRAATPEVVFPWPPLCCRRTGNFIPLNEEGCRLGHMDYLFTKGCFEHIGHAIDSYTWGISWFGFAILMWTLPVMLIAMYFYTML | null | null | epithelial cell differentiation [GO:0030855] | apical plasma membrane urothelial plaque [GO:0120001]; cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | null | PF00335; | 1.10.1450.10; | Tetraspanin (TM4SF) family | null | SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in normal bladder epithelial physiology, possibly in regulating membrane permeability of superficial umbrella cells or in stabilizing the apical membrane through AUM/cytoskeletal interactions (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
O00327 | BMAL1_HUMAN | MADQRMDISSTISDFMSPGPTDLLSSSLGTSGVDCNRKRKGSSTDYQESMDTDKDDPHGRLEYTEHQGRIKNAREAHSQIEKRRRDKMNSFIDELASLVPTCNAMSRKLDKLTVLRMAVQHMKTLRGATNPYTEANYKPTFLSDDELKHLILRAADGFLFVVGCDRGKILFVSESVFKILNYSQNDLIGQSLFDYLHPKDIAKVKEQLSSSDTAPRERLIDAKTGLPVKTDITPGPSRLCSGARRSFFCRMKCNRPSVKVEDKDFPSTCSKKKADRKSFCTIHSTGYLKSWPPTKMGLDEDNEPDNEGCNLSCLVAIGRLHSHVVPQPVNGEIRVKSMEYVSRHAIDGKFVFVDQRATAILAYLPQELLGTSCYEYFHQDDIGHLAECHRQVLQTREKITTNCYKFKIKDGSFITLRSRWFSFMNPWTKEVEYIVSTNTVVLANVLEGGDPTFPQLTASPHSMDSMLPSGEGGPKRTHPTVPGIPGGTRAGAGKIGRMIAEEIMEIHRIRGSSPSSCGSSPLNITSTPPPDASSPGGKKILNGGTPDIPSSGLLSGQAQENPGYPYSDSSSILGENPHIGIDMIDNDQGSSSPSNDEAAMAVIMSLLEADAGLGGPVDFSDLPWPL | null | null | circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; negative regulation of cold-induced thermogenesis [GO:0120163]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of glucocorticoid receptor signaling pathway [GO:2000323]; negative regulation of TOR signaling [GO:0032007]; oxidative stress-induced premature senescence [GO:0090403]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of circadian rhythm [GO:0042753]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of protein acetylation [GO:1901985]; positive regulation of skeletal muscle cell differentiation [GO:2001016]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; regulation of cell cycle [GO:0051726]; regulation of cellular senescence [GO:2000772]; regulation of DNA-templated transcription [GO:0006355]; regulation of hair cycle [GO:0042634]; regulation of insulin secretion [GO:0050796]; regulation of neurogenesis [GO:0050767]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of type B pancreatic cell development [GO:2000074]; response to redox state [GO:0051775]; spermatogenesis [GO:0007283] | aryl hydrocarbon receptor complex [GO:0034751]; chromatin [GO:0000785]; chromatoid body [GO:0033391]; CLOCK-BMAL transcription complex [GO:1990513]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605] | aryl hydrocarbon receptor binding [GO:0017162]; DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; E-box binding [GO:0070888]; Hsp90 protein binding [GO:0051879]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]; transcription cis-regulatory region binding [GO:0000976] | PF00010;PF00989;PF14598; | 4.10.280.10;3.30.450.20; | null | PTM: Ubiquitinated, leading to its proteasomal degradation (PubMed:24728990). Deubiquitinated by USP9X (PubMed:29626158). {ECO:0000269|PubMed:24728990, ECO:0000269|PubMed:29626158}.; PTM: O-glycosylated; contains O-GlcNAc. O-glycosylation by OGT prevents protein degradation by inhibiting ubiquitination. It also stabilizes the CLOCK-BMAL1 heterodimer thereby increasing CLOCK-BMAL1-mediated transcription of genes in the negative loop of the circadian clock such as PER1/2/3 and CRY1/2. {ECO:0000250|UniProtKB:Q9WTL8}.; PTM: Acetylated on Lys-538 by CLOCK during the repression phase of the circadian cycle. Acetylation facilitates recruitment of CRY1 protein and initiates the repression phase of the circadian cycle. Acetylated at Lys-538 by KAT5 during the activation phase of the cycle, leading to recruitment of the positive transcription elongation factor b (P-TEFb) and BRD4, followed by productive elongation of circadian transcripts. Deacetylated by SIRT1, which may result in decreased protein stability. {ECO:0000250|UniProtKB:Q9WTL8}.; PTM: Phosphorylated upon dimerization with CLOCK. Phosphorylation enhances the transcriptional activity, alters the subcellular localization and decreases the stability of the CLOCK-BMAL1 heterodimer by promoting its degradation. Phosphorylation shows circadian variations in the liver with a peak between CT10 to CT14. Phosphorylation at Ser-90 by CK2 is essential for its nuclear localization, its interaction with CLOCK and controls CLOCK nuclear entry (By similarity). Dephosphorylation at Ser-78 is important for dimerization with CLOCK and transcriptional activity (PubMed:23229515). {ECO:0000250|UniProtKB:Q9WTL8, ECO:0000269|PubMed:23229515}.; PTM: Sumoylated on Lys-259 upon dimerization with CLOCK. Predominantly conjugated to poly-SUMO2/3 rather than SUMO1 and the level of these conjugates undergo rhythmic variation, peaking at CT9-CT12. Sumoylation localizes it exclusively to the PML body and promotes its ubiquitination in the PML body, ubiquitin-dependent proteasomal degradation and the transcriptional activity of the CLOCK-BMAL1 heterodimer. {ECO:0000250|UniProtKB:Q9WTL8}.; PTM: Undergoes lysosome-mediated degradation in a time-dependent manner in the liver. {ECO:0000250|UniProtKB:Q9WTL8}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:24005054}. Cytoplasm {ECO:0000250|UniProtKB:Q9WTL8}. Nucleus, PML body {ECO:0000250|UniProtKB:Q9WTL8}. Note=Shuttles between the nucleus and the cytoplasm and this nucleocytoplasmic shuttling is essential for the nuclear accumulation of CLOCK, target gene transcription and the degradation of the CLOCK-BMAL1 heterodimer. The sumoylated form localizes in the PML body. Sequestered to the cytoplasm in the presence of ID2. {ECO:0000250|UniProtKB:Q9WTL8}. | null | null | null | null | null | FUNCTION: Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-BMAL1|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repressBMAL1 transcription, respectively.BMAL1 positively regulates myogenesis and negatively regulates adipogenesis via the transcriptional control of the genes of the canonical Wnt signaling pathway. Plays a role in normal pancreatic beta-cell function; regulates glucose-stimulated insulin secretion via the regulation of antioxidant genes NFE2L2/NRF2 and its targets SESN2, PRDX3, CCLC and CCLM. Negatively regulates the mTORC1 signaling pathway; regulates the expression of MTOR and DEPTOR. Controls diurnal oscillations of Ly6C inflammatory monocytes; rhythmic recruitment of the PRC2 complex imparts diurnal variation to chemokine expression that is necessary to sustain Ly6C monocyte rhythms. Regulates the expression of HSD3B2, STAR, PTGS2, CYP11A1, CYP19A1 and LHCGR in the ovary and also the genes involved in hair growth. Plays an important role in adult hippocampal neurogenesis by regulating the timely entry of neural stem/progenitor cells (NSPCs) into the cell cycle and the number of cell divisions that take place prior to cell-cycle exit. Regulates the circadian expression of CIART and KLF11. The CLOCK-BMAL1 heterodimer regulates the circadian expression of SERPINE1/PAI1, VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1, KLF10 and also genes implicated in glucose and lipid metabolism. Promotes rhythmic chromatin opening, regulating the DNA accessibility of other transcription factors. The NPAS2-BMAL1 heterodimer positively regulates the expression of MAOA, F7 and LDHA and modulates the circadian rhythm of daytime contrast sensitivity by regulating the rhythmic expression of adenylate cyclase type 1 (ADCY1) in the retina. The preferred binding motif for the CLOCK-BMAL1 heterodimer is 5'-CACGTGA-3', which contains a flanking adenine nucleotide at the 3-prime end of the canonical 6-nucleotide E-box sequence (PubMed:23229515). CLOCK specifically binds to the half-site 5'-CAC-3', while BMAL1 binds to the half-site 5'-GTGA-3' (PubMed:23229515). The CLOCK-BMAL1 heterodimer also recognizes the non-canonical E-box motifs 5'-AACGTGA-3' and 5'-CATGTGA-3' (PubMed:23229515). Essential for the rhythmic interaction of CLOCK with ASS1 and plays a critical role in positively regulating CLOCK-mediated acetylation of ASS1 (PubMed:28985504). Plays a role in protecting against lethal sepsis by limiting the expression of immune checkpoint protein CD274 in macrophages in a PKM2-dependent manner (By similarity). Regulates the diurnal rhythms of skeletal muscle metabolism via transcriptional activation of genes promoting triglyceride synthesis (DGAT2) and metabolic efficiency (COQ10B) (By similarity). {ECO:0000250|UniProtKB:Q9WTL8, ECO:0000269|PubMed:11441146, ECO:0000269|PubMed:12738229, ECO:0000269|PubMed:18587630, ECO:0000269|PubMed:23785138, ECO:0000269|PubMed:23955654, ECO:0000269|PubMed:24005054, ECO:0000269|PubMed:28985504}.; FUNCTION: (Microbial infection) Regulates SARS coronavirus-2/SARS-CoV-2 entry and replication in lung epithelial cells probably through the post-transcriptional regulation of ACE2 and interferon-stimulated gene expression. {ECO:0000269|PubMed:34545347}. | Homo sapiens (Human) |
O00329 | PK3CD_HUMAN | MPPGVDCPMEFWTKEENQSVVVDFLLPTGVYLNFPVSRNANLSTIKQLLWHRAQYEPLFHMLSGPEAYVFTCINQTAEQQELEDEQRRLCDVQPFLPVLRLVAREGDRVKKLINSQISLLIGKGLHEFDSLCDPEVNDFRAKMCQFCEEAAARRQQLGWEAWLQYSFPLQLEPSAQTWGPGTLRLPNRALLVNVKFEGSEESFTFQVSTKDVPLALMACALRKKATVFRQPLVEQPEDYTLQVNGRHEYLYGSYPLCQFQYICSCLHSGLTPHLTMVHSSSILAMRDEQSNPAPQVQKPRAKPPPIPAKKPSSVSLWSLEQPFRIELIQGSKVNADERMKLVVQAGLFHGNEMLCKTVSSSEVSVCSEPVWKQRLEFDINICDLPRMARLCFALYAVIEKAKKARSTKKKSKKADCPIAWANLMLFDYKDQLKTGERCLYMWPSVPDEKGELLNPTGTVRSNPNTDSAAALLICLPEVAPHPVYYPALEKILELGRHSECVHVTEEEQLQLREILERRGSGELYEHEKDLVWKLRHEVQEHFPEALARLLLVTKWNKHEDVAQMLYLLCSWPELPVLSALELLDFSFPDCHVGSFAIKSLRKLTDDELFQYLLQLVQVLKYESYLDCELTKFLLDRALANRKIGHFLFWHLRSEMHVPSVALRFGLILEAYCRGSTHHMKVLMKQGEALSKLKALNDFVKLSSQKTPKPQTKELMHLCMRQEAYLEALSHLQSPLDPSTLLAEVCVEQCTFMDSKMKPLWIMYSNEEAGSGGSVGIIFKNGDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLPTGDRTGLIEVVLRSDTIANIQLNKSNMAATAAFNKDALLNWLKSKNPGEALDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIMIRESGQLFHIDFGHFLGNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERFRGYCERAYTILRRHGLLFLHLFALMRAAGLPELSCSKDIQYLKDSLALGKTEEEALKHFRVKFNEALRESWKTKVNWLAHNVSKDNRQ | 2.7.1.137; 2.7.1.153 | null | adaptive immune response [GO:0002250]; B cell activation [GO:0042113]; B cell chemotaxis [GO:0035754]; B cell differentiation [GO:0030183]; B cell receptor signaling pathway [GO:0050853]; immune response [GO:0006955]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; mast cell chemotaxis [GO:0002551]; mast cell degranulation [GO:0043303]; mast cell differentiation [GO:0060374]; natural killer cell activation [GO:0030101]; natural killer cell chemotaxis [GO:0035747]; natural killer cell differentiation [GO:0001779]; neutrophil chemotaxis [GO:0030593]; neutrophil extravasation [GO:0072672]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; phosphatidylinositol-3-phosphate biosynthetic process [GO:0036092]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cell migration [GO:0030335]; positive regulation of cytokine production [GO:0001819]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of epithelial tube formation [GO:1905278]; positive regulation of gene expression [GO:0010628]; positive regulation of neutrophil apoptotic process [GO:0033031]; protein phosphorylation [GO:0006468]; respiratory burst involved in defense response [GO:0002679]; signal transduction [GO:0007165]; T cell activation [GO:0042110]; T cell chemotaxis [GO:0010818]; T cell differentiation [GO:0030217]; T cell receptor signaling pathway [GO:0050852]; vascular endothelial growth factor signaling pathway [GO:0038084] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; phosphatidylinositol 3-kinase complex [GO:0005942]; phosphatidylinositol 3-kinase complex, class IA [GO:0005943]; plasma membrane [GO:0005886] | 1-phosphatidylinositol-3-kinase activity [GO:0016303]; 1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity [GO:0046934]; 1-phosphatidylinositol-4-phosphate 3-kinase activity [GO:0035005]; ATP binding [GO:0005524]; kinase activity [GO:0016301] | PF00454;PF00792;PF02192;PF00794;PF00613; | 3.10.20.770;2.60.40.150;1.10.1070.11;1.25.40.70; | PI3/PI4-kinase family | PTM: Autophosphorylation on Ser-1039 results in the almost complete inactivation of the lipid kinase activity. {ECO:0000269|PubMed:10064595}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22020336}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + ADP + H(+); Xref=Rhea:RHEA:21292, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57836, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.153; Evidence={ECO:0000269|PubMed:15135396}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21293; Evidence={ECO:0000305|PubMed:15135396}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.137; Evidence={ECO:0000269|PubMed:9235916}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710; Evidence={ECO:0000305|PubMed:9235916}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 4,5-bisphosphate + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol 3,4,5-triphosphate) + ADP + H(+); Xref=Rhea:RHEA:43396, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77137, ChEBI:CHEBI:83243, ChEBI:CHEBI:456216; Evidence={ECO:0000305|PubMed:15135396}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43397; Evidence={ECO:0000305|PubMed:15135396}; | null | PATHWAY: Phospholipid metabolism; phosphatidylinositol phosphate biosynthesis. {ECO:0000305|PubMed:15135396, ECO:0000305|PubMed:9113989}. | null | null | FUNCTION: Phosphoinositide-3-kinase (PI3K) phosphorylates phosphatidylinositol (PI) and its phosphorylated derivatives at position 3 of the inositol ring to produce 3-phosphoinositides (PubMed:9235916). Uses ATP and PtdIns(4,5)P2 (phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3) (PubMed:15135396). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Mediates immune responses. Plays a role in B-cell development, proliferation, migration, and function. Required for B-cell receptor (BCR) signaling. Mediates B-cell proliferation response to anti-IgM, anti-CD40 and IL4 stimulation. Promotes cytokine production in response to TLR4 and TLR9. Required for antibody class switch mediated by TLR9. Involved in the antigen presentation function of B-cells. Involved in B-cell chemotaxis in response to CXCL13 and sphingosine 1-phosphate (S1P). Required for proliferation, signaling and cytokine production of naive, effector and memory T-cells. Required for T-cell receptor (TCR) signaling. Mediates TCR signaling events at the immune synapse. Activation by TCR leads to antigen-dependent memory T-cell migration and retention to antigenic tissues. Together with PIK3CG participates in T-cell development. Contributes to T-helper cell expansion and differentiation. Required for T-cell migration mediated by homing receptors SELL/CD62L, CCR7 and S1PR1 and antigen dependent recruitment of T-cells. Together with PIK3CG is involved in natural killer (NK) cell development and migration towards the sites of inflammation. Participates in NK cell receptor activation. Plays a role in NK cell maturation and cytokine production. Together with PIK3CG is involved in neutrophil chemotaxis and extravasation. Together with PIK3CG participates in neutrophil respiratory burst. Plays important roles in mast-cell development and mast cell mediated allergic response. Involved in stem cell factor (SCF)-mediated proliferation, adhesion and migration. Required for allergen-IgE-induced degranulation and cytokine release. The lipid kinase activity is required for its biological function. Isoform 2 may be involved in stabilizing total RAS levels, resulting in increased ERK phosphorylation and increased PI3K activity. {ECO:0000269|PubMed:15135396, ECO:0000269|PubMed:20081091, ECO:0000269|PubMed:22020336, ECO:0000269|PubMed:9235916}. | Homo sapiens (Human) |
O00330 | ODPX_HUMAN | MAASWRLGCDPRLLRYLVGFPGRRSVGLVKGALGWSVSRGANWRWFHSTQWLRGDPIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGSLIGLIVEEGEDWKHVEIPKDVGPPPPVSKPSEPRPSPEPQISIPVKKEHIPGTLRFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVQLKQTGKITESRPTPAPTATPTAPSPLQATAGPSYPRPVIPPVSTPGQPNAVGTFTEIPASNIRRVIAKRLTESKSTVPHAYATADCDLGAVLKVRQDLVKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRFRPVLKLTEDEEGNAKLQQRQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRLA | null | null | acetyl-CoA biosynthetic process from pyruvate [GO:0006086] | mitochondrial matrix [GO:0005759]; mitochondrial pyruvate dehydrogenase complex [GO:0005967]; mitochondrion [GO:0005739]; pyruvate dehydrogenase complex [GO:0045254] | acyltransferase activity [GO:0016746] | PF00198;PF00364;PF02817; | 2.40.50.100;3.30.559.10;4.10.320.10; | 2-oxoacid dehydrogenase family | PTM: Delipoylated at Lys-97 by SIRT4, delipoylation decreases the PHD complex activity. {ECO:0000269|PubMed:25525879}. | SUBCELLULAR LOCATION: Mitochondrion matrix. | null | null | null | null | null | FUNCTION: Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex. | Homo sapiens (Human) |
O00337 | S28A1_HUMAN | MENDPSRRRESISLTPVAKGLENMGADFLESLEEGQLPRSDLSPAEIRSSWSEAAPKPFSRWRNLQPALRARSFCREHMQLFRWIGTGLLCTGLSAFLLVACLLDFQRALALFVLTCVVLTFLGHRLLKRLLGPKLRRFLKPQGHPRLLLWFKRGLALAAFLGLVLWLSLDTSQRPEQLVSFAGICVFVALLFACSKHHCAVSWRAVSWGLGLQFVLGLLVIRTEPGFIAFEWLGEQIRIFLSYTKAGSSFVFGEALVKDVFAFQVLPIIVFFSCVISVLYHVGLMQWVILKIAWLMQVTMGTTATETLSVAGNIFVSQTEAPLLIRPYLADMTLSEVHVVMTGGYATIAGSLLGAYISFGIDATSLIAASVMAAPCALALSKLVYPEVEESKFRREEGVKLTYGDAQNLIEAASTGAAISVKVVANIAANLIAFLAVLDFINAALSWLGDMVDIQGLSFQLICSYILRPVAFLMGVAWEDCPVVAELLGIKLFLNEFVAYQDLSKYKQRRLAGAEEWVGDRKQWISVRAEVLTTFALCGFANFSSIGIMLGGLTSMVPQRKSDFSQIVLRALFTGACVSLVNACMAGILYMPRGAEVDCMSLLNTTLSSSSFEIYQCCREAFQSVNPEFSPEALDNCCRFYNHTICAQ | null | null | azole transmembrane transport [GO:0045117]; cytidine transport [GO:0015861]; nucleoside import across plasma membrane [GO:0180015]; nucleoside transmembrane transport [GO:1901642]; purine nucleobase transmembrane transport [GO:1904823]; pyrimidine nucleobase transport [GO:0015855]; pyrimidine-containing compound transmembrane transport [GO:0072531]; uridine transport [GO:0015862] | apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]; cytosol [GO:0005829]; nuclear speck [GO:0016607]; plasma membrane [GO:0005886] | azole transmembrane transporter activity [GO:1901474]; cytidine transmembrane transporter activity [GO:0015212]; nucleoside:sodium symporter activity [GO:0005415]; purine nucleobase transmembrane transporter activity [GO:0005345]; pyrimidine- and adenosine-specific:sodium symporter activity [GO:0015389]; uridine transmembrane transporter activity [GO:0015213] | PF07670;PF07662;PF01773; | null | Concentrative nucleoside transporter (CNT) (TC 2.A.41) family | PTM: N-glycosylated. N-glycosylation is required for localization to the plasma membrane and the transporter activity. {ECO:0000269|PubMed:30658162}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21998139}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q62674}. Apical cell membrane {ECO:0000269|PubMed:21998139}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q62674}. | CATALYTIC ACTIVITY: Reaction=Na(+)(out) + uridine(out) = Na(+)(in) + uridine(in); Xref=Rhea:RHEA:69887, ChEBI:CHEBI:16704, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:10455109, ECO:0000269|PubMed:14701834, ECO:0000269|PubMed:21795683, ECO:0000269|PubMed:21998139, ECO:0000269|PubMed:32126230, ECO:0000269|PubMed:9124315}; CATALYTIC ACTIVITY: Reaction=Na(+)(out) + thymidine(out) = Na(+)(in) + thymidine(in); Xref=Rhea:RHEA:69891, ChEBI:CHEBI:17748, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:10455109, ECO:0000269|PubMed:21998139, ECO:0000269|PubMed:9124315}; CATALYTIC ACTIVITY: Reaction=cytidine(out) + Na(+)(out) = cytidine(in) + Na(+)(in); Xref=Rhea:RHEA:69895, ChEBI:CHEBI:17562, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:10455109, ECO:0000269|PubMed:21998139, ECO:0000269|PubMed:30658162, ECO:0000269|PubMed:9124315}; CATALYTIC ACTIVITY: Reaction=adenosine(out) + Na(+)(out) = adenosine(in) + Na(+)(in); Xref=Rhea:RHEA:69927, ChEBI:CHEBI:16335, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:10455109, ECO:0000269|PubMed:15194733, ECO:0000269|PubMed:21998139, ECO:0000269|PubMed:32126230, ECO:0000269|PubMed:9124315}; | null | null | null | null | FUNCTION: Sodium and pyrimidine nucleoside symporter of the plasma membrane that imports uridine, thymidine and cytidine into cells by coupling their transport to the transmembrane sodium electrochemical gradient. Also transports adenosine, an atypical substrate transported with high apparent affinity, but low maximum velocity. Therefore, exhibits the transport characteristics of the nucleoside transport system cit or N2 subtype (N2/cit) (PubMed:10455109, PubMed:14701834, PubMed:15194733, PubMed:21795683, PubMed:21998139, PubMed:30658162, PubMed:32126230, PubMed:9124315). Involved in renal nucleoside (re)absorption (PubMed:30658162). {ECO:0000269|PubMed:10455109, ECO:0000269|PubMed:14701834, ECO:0000269|PubMed:15194733, ECO:0000269|PubMed:21795683, ECO:0000269|PubMed:21998139, ECO:0000269|PubMed:30658162, ECO:0000269|PubMed:32126230, ECO:0000269|PubMed:9124315}. | Homo sapiens (Human) |
O00338 | ST1C2_HUMAN | MALTSDLGKQIKLKEVEGTLLQPATVDNWSQIQSFEAKPDDLLICTYPKAGTTWIQEIVDMIEQNGDVEKCQRAIIQHRHPFIEWARPPQPSGVEKAKAMPSPRILKTHLSTQLLPPSFWENNCKFLYVARNAKDCMVSYYHFQRMNHMLPDPGTWEEYFETFINGKVVWGSWFDHVKGWWEMKDRHQILFLFYEDIKRDPKHEIRKVMQFMGKKVDETVLDKIVQETSFEKMKENPMTNRSTVSKSILDQSISSFMRKGTVGDWKNHFTVAQNERFDEIYRRKMEGTSINFCMEL | 2.8.2.1 | null | amine metabolic process [GO:0009308]; sulfation [GO:0051923] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; lysosome [GO:0005764] | aryl sulfotransferase activity [GO:0004062]; sulfotransferase activity [GO:0008146] | PF00685; | 3.40.50.300; | Sulfotransferase 1 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O46503}. Lysosome {ECO:0000250|UniProtKB:Q9WUW8}. | CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate + H(+); Xref=Rhea:RHEA:12164, ChEBI:CHEBI:15378, ChEBI:CHEBI:33853, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:140317; EC=2.8.2.1; Evidence={ECO:0000269|PubMed:10481272, ECO:0000269|PubMed:10783263, ECO:0000269|PubMed:9852044}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13.3 mM for p-nitrophenol {ECO:0000269|PubMed:10481272}; Vmax=0.005 nmol/min/mg enzyme with p-nitrophenol as substrate {ECO:0000269|PubMed:10481272}; | null | null | null | FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of phenolic compounds. Does not sulfonate steroids, dopamine, acetaminophen, or alpha-naphthol (PubMed:10481272, PubMed:10783263, PubMed:9852044). Catalyzes the sulfonation of the carcinogenic N-Hydroxy-2-acetylaminofluorene leading to highly reactive intermediates capable of forming DNA adducts, potentially resulting in mutagenesis (PubMed:9852044). {ECO:0000269|PubMed:10481272, ECO:0000269|PubMed:10783263, ECO:0000269|PubMed:9852044}. | Homo sapiens (Human) |
O00339 | MATN2_HUMAN | MEKMLAGCFLLILGQIVLLPAEARERSRGRSISRGRHARTHPQTALLESSCENKRADLVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHLSTGTMTGLAIQYALNIAFSEAEGARPLRENVPRVIMIVTDGRPQDSVAEVAAKARDTGILIFAIGVGQVDFNTLKSIGSEPHEDHVFLVANFSQIETLTSVFQKKLCTAHMCSTLEHNCAHFCINIPGSYVCRCKQGYILNSDQTTCRIQDLCAMEDHNCEQLCVNVPGSFVCQCYSGYALAEDGKRCVAVDYCASENHGCEHECVNADGSYLCQCHEGFALNPDKKTCTKIDYCASSNHGCQHECVNTDDSYSCHCLKGFTLNPDKKTCRRINYCALNKPGCEHECVNMEESYYCRCHRGYTLDPNGKTCSRVDHCAQQDHGCEQLCLNTEDSFVCQCSEGFLINEDLKTCSRVDYCLLSDHGCEYSCVNMDRSFACQCPEGHVLRSDGKTCAKLDSCALGDHGCEHSCVSSEDSFVCQCFEGYILREDGKTCRRKDVCQAIDHGCEHICVNSDDSYTCECLEGFRLAEDGKRCRRKDVCKSTHHGCEHICVNNGNSYICKCSEGFVLAEDGRRCKKCTEGPIDLVFVIDGSKSLGEENFEVVKQFVTGIIDSLTISPKAARVGLLQYSTQVHTEFTLRNFNSAKDMKKAVAHMKYMGKGSMTGLALKHMFERSFTQGEGARPLSTRVPRAAIVFTDGRAQDDVSEWASKAKANGITMYAVGVGKAIEEELQEIASEPTNKHLFYAEDFSTMDEISEKLKKGICEALEDSDGRQDSPAGELPKTVQQPTESEPVTINIQDLLSCSNFAVQHRYLFEEDNLLRSTQKLSHSTKPSGSPLEEKHDQCKCENLIMFQNLANEEVRKLTQRLEEMTQRMEALENRLRYR | null | null | axon guidance [GO:0007411]; dendrite regeneration [GO:0031104]; extracellular matrix organization [GO:0030198]; glial cell migration [GO:0008347]; neuron migration [GO:0001764]; response to axon injury [GO:0048678] | basement membrane [GO:0005604]; collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; matrilin complex [GO:0120216] | calcium ion binding [GO:0005509]; extracellular matrix structural constituent [GO:0005201] | PF12662;PF07645;PF14670;PF10393;PF00092; | 1.20.5.30;2.10.25.10;3.40.50.410; | null | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Involved in matrix assembly. {ECO:0000250}. | Homo sapiens (Human) |
O00341 | EAA5_HUMAN | MVPHAILARGRDVCRRNGLLILSVLSVIVGCLLGFFLRTRRLSPQEISYFQFPGELLMRMLKMMILPLVVSSLMSGLASLDAKTSSRLGVLTVAYYLWTTFMAVIVGIFMVSIIHPGSAAQKETTEQSGKPIMSSADALLDLIRNMFPANLVEATFKQYRTKTTPVVKSPKVAPEEAPPRRILIYGVQEENGSHVQNFALDLTPPPEVVYKSEPGTSDGMNVLGIVFFSATMGIMLGRMGDSGAPLVSFCQCLNESVMKIVAVAVWYFPFGIVFLIAGKILEMDDPRAVGKKLGFYSVTVVCGLVLHGLFILPLLYFFITKKNPIVFIRGILQALLIALATSSSSATLPITFKCLLENNHIDRRIARFVLPVGATINMDGTALYEAVAAIFIAQVNNYELDFGQIITISITATAASIGAAGIPQAGLVTMVIVLTSVGLPTDDITLIIAVDWALDRFRTMINVLGDALAAGIMAHICRKDFARDTGTEKLLPCETKPVSLQEIVAAQQNGCVKSVAEASELTLGPTCPHHVPVQVEQDEELPAASLNHCTIQISELETNV | null | null | chloride transmembrane transport [GO:1902476]; dicarboxylic acid transport [GO:0006835]; L-glutamate transmembrane transport [GO:0015813]; monoatomic ion transport [GO:0006811]; neurotransmitter transport [GO:0006836]; neurotransmitter uptake [GO:0001504] | plasma membrane [GO:0005886]; postsynapse [GO:0098794]; synaptic membrane [GO:0097060] | extracellularly glutamate-gated chloride channel activity [GO:0008068]; glutamate:sodium symporter activity [GO:0015501]; high-affinity L-glutamate transmembrane transporter activity [GO:0005314]; L-glutamate transmembrane transporter activity [GO:0005313]; neutral L-amino acid transmembrane transporter activity [GO:0015175] | PF00375; | 1.10.3860.10; | Dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family, SLC1A7 subfamily | null | SUBCELLULAR LOCATION: Photoreceptor inner segment membrane {ECO:0000250|UniProtKB:Q8JZR4}; Multi-pass membrane protein {ECO:0000255}. Synaptic cell membrane {ECO:0000250|UniProtKB:Q8JZR4}; Multi-pass membrane protein {ECO:0000255}. Note=Located in both cone and rod photoreceptor terminals and in axon terminals of rod bipolar cells. {ECO:0000250|UniProtKB:Q8JZR4}. | CATALYTIC ACTIVITY: Reaction=H(+)(out) + K(+)(in) + L-glutamate(out) + 3 Na(+)(out) = H(+)(in) + K(+)(out) + L-glutamate(in) + 3 Na(+)(in); Xref=Rhea:RHEA:70699, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:29985; Evidence={ECO:0000269|PubMed:9108121}; CATALYTIC ACTIVITY: Reaction=H(+)(out) + K(+)(in) + L-aspartate(out) + 3 Na(+)(out) = H(+)(in) + K(+)(out) + L-aspartate(in) + 3 Na(+)(in); Xref=Rhea:RHEA:70851, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:29991; Evidence={ECO:0000269|PubMed:9108121}; CATALYTIC ACTIVITY: Reaction=D-aspartate(out) + H(+)(out) + K(+)(in) + 3 Na(+)(out) = D-aspartate(in) + H(+)(in) + K(+)(out) + 3 Na(+)(in); Xref=Rhea:RHEA:71379, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:29990; Evidence={ECO:0000269|PubMed:9108121}; | null | null | null | null | FUNCTION: Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion (PubMed:9108121). Acts primarily as an inhibitory glutamate-gated chloride channel being a major inhibitory presynaptic receptor at mammalian rod bipolar cell axon terminals. Glutamate binding gates a large Cl(-) conductance that mediates inhibition, affecting visual processing in the retina (By similarity). {ECO:0000250|UniProtKB:Q8JZR4, ECO:0000269|PubMed:9108121}. | Homo sapiens (Human) |
O00358 | FOXE1_HUMAN | MTAESGPPPPQPEVLATVKEERGETAAGAGVPGEATGRGAGGRRRKRPLQRGKPPYSYIALIAMAIAHAPERRLTLGGIYKFITERFPFYRDNPKKWQNSIRHNLTLNDCFLKIPREAGRPGKGNYWALDPNAEDMFESGSFLRRRKRFKRSDLSTYPAYMHDAAAAAAAAAAAAAAAAIFPGAVPAARPPYPGAVYAGYAPPSLAAPPPVYYPAASPGPCRVFGLVPERPLSPELGPAPSGPGGSCAFASAGAPATTTGYQPAGCTGARPANPSAYAAAYAGPDGAYPQGAGSAIFAAAGRLAGPASPPAGGSSGGVETTVDFYGRTSPGQFGALGACYNPGGQLGGASAGAYHARHAAAYPGGIDRFVSAM | null | null | anatomical structure morphogenesis [GO:0009653]; cell differentiation [GO:0030154]; cell migration [GO:0016477]; chordate pharynx development [GO:0160093]; cranial skeletal system development [GO:1904888]; embryonic organ morphogenesis [GO:0048562]; hair follicle morphogenesis [GO:0031069]; hard palate development [GO:0060022]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of transcription by RNA polymerase II [GO:0006357]; soft palate development [GO:0060023]; thymus development [GO:0048538]; thyroid gland development [GO:0030878]; thyroid hormone generation [GO:0006590] | chromatin [GO:0000785]; nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837] | PF00250; | 1.10.10.10; | null | PTM: Phosphorylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21177256}. | null | null | null | null | null | FUNCTION: Transcription factor that binds consensus sites on a variety of gene promoters and activate their transcription. Involved in proper palate formation, most probably through the expression of MSX1 and TGFB3 genes which are direct targets of this transcription factor. Also implicated in thyroid gland morphogenesis. May indirectly play a role in cell growth and migration through the regulation of WNT5A expression. {ECO:0000269|PubMed:12165566, ECO:0000269|PubMed:16882747, ECO:0000269|PubMed:20094846, ECO:0000269|PubMed:20484477, ECO:0000269|PubMed:21177256, ECO:0000269|PubMed:24219130, ECO:0000269|PubMed:25381600, ECO:0000269|PubMed:9697705}. | Homo sapiens (Human) |
O00370 | LORF2_HUMAN | MTGSNSHITILTLNVNGLNSPIKRHRLASWIKSQDPSVCCIQETHLTCRDTHRLKIKGWRKIYQANGKQKKAGVAILVSDKTDFKPTKIKRDKEGHYIMVKGSIQQEELTILNIYAPNTGAPRFIKQVLSDLQRDLDSHTLIMGDFNTPLSILDRSTRQKVNKDTQELNSALHQTDLIDIYRTLHPKSTEYTFFSAPHHTYSKIDHIVGSKALLSKCKRTEIITNYLSDHSAIKLELRIKNLTQSRSTTWKLNNLLLNDYWVHNEMKAEIKMFFETNENKDTTYQNLWDAFKAVCRGKFIALNAYKRKQERSKIDTLTSQLKELEKQEQTHSKASRRQEITKIRAELKEIETQKTLQKINESRSWFFERINKIDRPLARLIKKKREKNQIDTIKNDKGDITTDPTEIQTTIREYYKHLYANKLENLEEMDTFLDTYTLPRLNQEEVESLNRPITGSEIVAIINSLPTKKSPGPDGFTAEFYQRYKEELVPFLLKLFQSIEKEGILPNSFYEASIILIPKPGRDTTKKENFRPISLMNIDAKILNKILANRIQQHIKKLIHHDQVGFIPGMQGWFNIRKSINVIQHINRAKDKNHVIISIDAEKAFDKIQQPFMLKTLNKLGIDGMYLKIIRAIYDKPTANIILNGQKLEAFPLKTGTRQGCPLSPLLFNIVLEVLARAIRQEKEIKGIQLGKEEVKLSLFADDMIVYLENPIVSAQNLLKLISNFSKVSGYKINVQKSQAFLYNNNRQTESQIMGELPFTIASKRIKYLGIQLTRDVKDLFKENYKPLLKEIKEDTNKWKNIPCSWVGRINIVKMAILPKVIYRFNAIPIKLPMTFFTELEKTTLKFIWNQKRARIAKSILSQKNKAGGITLPDFKLYYKATVTKTAWYWYQNRDIDQWNRTEPSEIMPHIYNYLIFDKPEKNKQWGKDSLLNKWCWENWLAICRKLKLDPFLTPYTKINSRWIKDLNVKPKTIKTLEENLGITIQDIGVGKDFMSKTPKAMATKDKIDKWDLIKLKSFCTAKETTIRVNRQPTTWEKIFATYSSDKGLISRIYNELKQIYKKKTNNPIKKWAKDMNRHFSKEDIYAAKKHMKKCSSSLAIREMQIKTTMRYHLTPVRMAIIKKSGNNRCWRGCGEIGTLVHCWWDCKLVQPLWKSVWRFLRDLELEIPFDPAIPLLGIYPKDYKSCCYKDTCTRMFIAALFTIAKTWNQPNCPTMIDWIKKMWHIYTMEYYAAIKNDEFISFVGTWMKLETIILSKLSQEQKTKHRIFSLIGGN | 2.7.7.49; 3.1.21.- | null | DNA recombination [GO:0006310]; nucleic acid metabolic process [GO:0090304]; retrotransposition [GO:0032197] | null | metal ion binding [GO:0046872]; RNA binding [GO:0003723]; RNA-directed DNA polymerase activity [GO:0003964]; type II site-specific deoxyribonuclease activity [GO:0009036] | PF03372;PF00078; | 3.60.10.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405, ECO:0000269|PubMed:9140393}; | null | null | null | null | FUNCTION: Has reverse transcriptase activity required for target-primed reverse transcription of the LINE-1 element mRNA, a crucial step in LINE-1 retrotransposition (PubMed:7516468, PubMed:9140393). Also has endonuclease activity that allows the introduction of nicks in the chromosomal target DNA (PubMed:17626046, PubMed:34554261, PubMed:8945517). Cleaves DNA in AT-rich regions between a 5' stretch of purines and a 3' stretch of pyrimidines, corresponding to sites of LINE-1 integration in the genome (PubMed:8945517). Conformational properties of the target DNA sequence rather than specific nucleotides are key determinants of the ORF2p capacity for sequence-specific DNA recognition (PubMed:17626046, PubMed:34554261). Unlike related endonucleases, does not bend the DNA helix but causes compression near the cleavage site (PubMed:34554261). {ECO:0000269|PubMed:17626046, ECO:0000269|PubMed:34554261, ECO:0000269|PubMed:7516468, ECO:0000269|PubMed:8945517, ECO:0000269|PubMed:9140393}. | Homo sapiens (Human) |
O00391 | QSOX1_HUMAN | MRRCNSGSGPPPSLLLLLLWLLAVPGANAAPRSALYSPSDPLTLLQADTVRGAVLGSRSAWAVEFFASWCGHCIAFAPTWKALAEDVKAWRPALYLAALDCAEETNSAVCRDFNIPGFPTVRFFKAFTKNGSGAVFPVAGADVQTLRERLIDALESHHDTWPPACPPLEPAKLEEIDGFFARNNEEYLALIFEKGGSYLGREVALDLSQHKGVAVRRVLNTEANVVRKFGVTDFPSCYLLFRNGSVSRVPVLMESRSFYTAYLQRLSGLTREAAQTTVAPTTANKIAPTVWKLADRSKIYMADLESALHYILRIEVGRFPVLEGQRLVALKKFVAVLAKYFPGRPLVQNFLHSVNEWLKRQKRNKIPYSFFKTALDDRKEGAVLAKKVNWIGCQGSEPHFRGFPCSLWVLFHFLTVQAARQNVDHSQEAAKAKEVLPAIRGYVHYFFGCRDCASHFEQMAAASMHRVGSPNAAVLWLWSSHNRVNARLAGAPSEDPQFPKVQWPPRELCSACHNERLDVPVWDVEATLNFLKAHFSPSNIILDFPAAGSAARRDVQNVAAAPELAMGALELESRNSTLDPGKPEMMKSPTNTTPHVPAEGPEASRPPKLHPGLRAAPGQEPPEHMAELQRNEQEQPLGQWHLSKRDTGAALLAESRAEKNRLWGPLEVRRVGRSSKQLVDIPEGQLEARAGRGRGQWLQVLGGGFSYLDISLCVGLYSLSFMGLLAMYTYFQAKIRALKGHAGHPAA | 1.8.3.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:18393449, ECO:0000269|PubMed:20211621}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:18393449, ECO:0000269|PubMed:20211621}; | extracellular matrix assembly [GO:0085029]; negative regulation of macroautophagy [GO:0016242]; protein folding [GO:0006457] | endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; intercellular bridge [GO:0045171]; intracellular membrane-bounded organelle [GO:0043231]; platelet alpha granule lumen [GO:0031093]; specific granule lumen [GO:0035580]; tertiary granule lumen [GO:1904724] | FAD binding [GO:0071949]; flavin-dependent sulfhydryl oxidase activity [GO:0016971]; protein disulfide isomerase activity [GO:0003756] | PF04777;PF18371;PF18108;PF00085; | 1.20.120.310;3.40.30.10;1.20.120.1960; | Quiescin-sulfhydryl oxidase (QSOX) family | PTM: N-glycosylated (PubMed:17331072, PubMed:29757379). O-glycosylated on Thr and Ser residues (PubMed:29757379). {ECO:0000269|PubMed:17331072, ECO:0000269|PubMed:29757379}. | SUBCELLULAR LOCATION: [Isoform 1]: Golgi apparatus membrane {ECO:0000269|PubMed:17331072, ECO:0000269|PubMed:23704371}; Single-pass membrane protein {ECO:0000305|PubMed:17331072}. Secreted {ECO:0000269|PubMed:29757379}. Note=A small proportion is secreted, probably via a proteolytic cleavage that removes the membrane anchor. {ECO:0000305|PubMed:29757379}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:10708601}. Note=Found in the extracellular medium of quiescent cells but is not found in proliferating cells. {ECO:0000269|PubMed:10708601}. | CATALYTIC ACTIVITY: Reaction=O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR'; Xref=Rhea:RHEA:17357, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16520, ChEBI:CHEBI:17412; EC=1.8.3.2; Evidence={ECO:0000269|PubMed:18393449, ECO:0000269|PubMed:22801504, ECO:0000269|PubMed:23704371, ECO:0000269|PubMed:23867277, ECO:0000269|PubMed:26819240, ECO:0000269|PubMed:29757379, ECO:0000269|PubMed:30367560}; | null | null | null | null | FUNCTION: Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide (PubMed:17331072, PubMed:18393449, PubMed:23704371, PubMed:23867277, PubMed:30367560). Plays a role in disulfide bond formation in a variety of extracellular proteins (PubMed:17331072, PubMed:22801504, PubMed:23867277, PubMed:30367560). In fibroblasts, required for normal incorporation of laminin into the extracellular matrix, and thereby for normal cell-cell adhesion and cell migration (PubMed:23704371, PubMed:23867277, PubMed:30367560). {ECO:0000269|PubMed:17331072, ECO:0000269|PubMed:18393449, ECO:0000269|PubMed:22801504, ECO:0000269|PubMed:23704371, ECO:0000269|PubMed:23867277, ECO:0000269|PubMed:30367560}. | Homo sapiens (Human) |
O00399 | DCTN6_HUMAN | MAEKTQKSVKIAPGAVVCVESEIRGDVTIGPRTVIHPKARIIAEAGPIVIGEGNLIEEQALIINAYPDNITPDTEDPEPKPMIIGTNNVFEVGCYSQAMKMGDNNVIESKAYVGRNVILTSGCIIGACCNLNTFEVIPENTVIYGADCLRRVQTERPQPQTLQLDFLMKILPNYHHLKKTMKGSSTPVKN | null | null | mitotic spindle organization [GO:0007052] | centrosome [GO:0005813]; cytosol [GO:0005829]; dynactin complex [GO:0005869]; kinetochore [GO:0000776] | dynein complex binding [GO:0070840] | null | 2.160.10.10; | Dynactin subunits 5/6 family, Dynactin subunit 6 subfamily | PTM: Phosphorylation at Thr-186 by CDK1 during mitotic prometaphase creates a binding site for PLK1 that facilitates its recruitment to kinetochores. {ECO:0000269|PubMed:23455152}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:D0G6S1}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:23455152}. | null | null | null | null | null | FUNCTION: Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules. {ECO:0000269|PubMed:23455152}. | Homo sapiens (Human) |
O00400 | ACATN_HUMAN | MSPTISHKDSSRQRRPGNFSHSLDMKSGPLPPGGWDDSHLDSAGREGDREALLGDTGTGDFLKAPQSFRAELSSILLLLFLYVLQGIPLGLAGSIPLILQSKNVSYTDQAFFSFVFWPFSLKLLWAPLVDAVYVKNFGRRKSWLVPTQYILGLFMIYLSTQVDRLLGNTDDRTPDVIALTVAFFLFEFLAATQDIAVDGWALTMLSRENVGYASTCNSVGQTAGYFLGNVLFLALESADFCNKYLRFQPQPRGIVTLSDFLFFWGTVFLITTTLVALLKKENEVSVVKEETQGITDTYKLLFAIIKMPAVLTFCLLILTAKIGFSAADAVTGLKLVEEGVPKEHLALLAVPMVPLQIILPLIISKYTAGPQPLNTFYKAMPYRLLLGLEYALLVWWTPKVEHQGGFPIYYYIVVLLSYALHQVTVYSMYVSIMAFNAKVSDPLIGGTYMTLLNTVSNLGGNWPSTVALWLVDPLTVKECVGASNQNCRTPDAVELCKKLGGSCVTALDGYYVESIICVFIGFGWWFFLGPKFKKLQDEGSSSWKCKRNN | null | null | acetyl-CoA transmembrane transport [GO:0035348]; transmembrane transport [GO:0055085] | endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; plasma membrane [GO:0005886] | acetyl-CoA transmembrane transporter activity [GO:0008521]; protein homodimerization activity [GO:0042803] | PF13000; | 1.20.1250.20; | SLC33A transporter family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20826464, ECO:0000269|PubMed:24828632}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA(in) = acetyl-CoA(out); Xref=Rhea:RHEA:75039, ChEBI:CHEBI:57288; Evidence={ECO:0000269|PubMed:20826464, ECO:0000269|PubMed:24828632}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75040; Evidence={ECO:0000269|PubMed:20826464, ECO:0000269|PubMed:24828632}; | null | null | null | null | FUNCTION: Acetyl-CoA transporter that mediates active acetyl-CoA import through the endoplasmic reticulum (ER) membrane into the ER lumen where specific ER-based acetyl-CoA:lysine acetyltransferases are responsible for the acetylation of ER-based protein substrates, such as BACE1 (PubMed:20826464, PubMed:24828632). Necessary for O-acetylation of gangliosides (PubMed:9096318). {ECO:0000269|PubMed:20826464, ECO:0000269|PubMed:24828632, ECO:0000269|PubMed:25402622, ECO:0000269|PubMed:9096318}. | Homo sapiens (Human) |
O00401 | WASL_HUMAN | MSSVQQQPPPPRRVTNVGSLLLTPQENESLFTFLGKKCVTMSSAVVQLYAADRNCMWSKKCSGVACLVKDNPQRSYFLRIFDIKDGKLLWEQELYNNFVYNSPRGYFHTFAGDTCQVALNFANEEEAKKFRKAVTDLLGRRQRKSEKRRDPPNGPNLPMATVDIKNPEITTNRFYGPQVNNISHTKEKKKGKAKKKRLTKADIGTPSNFQHIGHVGWDPNTGFDLNNLDPELKNLFDMCGISEAQLKDRETSKVIYDFIEKTGGVEAVKNELRRQAPPPPPPSRGGPPPPPPPPHNSGPPPPPARGRGAPPPPPSRAPTAAPPPPPPSRPSVAVPPPPPNRMYPPPPPALPSSAPSGPPPPPPSVLGVGPVAPPPPPPPPPPPGPPPPPGLPSDGDHQVPTTAGNKAALLDQIREGAQLKKVEQNSRPVSCSGRDALLDQIRQGIQLKSVADGQESTPPTPAPTSGIVGALMEVMQKRSKAIHSSDEDEDEDDEEDFEDDDEWED | null | null | actin filament polymerization [GO:0030041]; actin polymerization or depolymerization [GO:0008154]; cell division [GO:0051301]; dendritic spine morphogenesis [GO:0060997]; negative regulation of lymphocyte migration [GO:2000402]; negative regulation of membrane tubulation [GO:1903526]; positive regulation of clathrin-dependent endocytosis [GO:2000370]; positive regulation of filopodium assembly [GO:0051491]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein-containing complex assembly [GO:0065003]; protein-containing complex localization [GO:0031503]; regulation of postsynapse organization [GO:0099175]; regulation of protein localization [GO:0032880]; response to bacterium [GO:0009617]; spindle localization [GO:0051653]; vesicle budding from membrane [GO:0006900]; vesicle organization [GO:0016050]; vesicle transport along actin filament [GO:0030050] | actin cap [GO:0030478]; actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; endocytic vesicle membrane [GO:0030666]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; glutamatergic synapse [GO:0098978]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | actin binding [GO:0003779]; GTPase regulator activity [GO:0030695]; microtubule binding [GO:0008017] | PF00786;PF00568;PF02205; | 3.90.810.10;2.30.29.30; | null | PTM: Phosphorylation at Ser-242, Tyr-256, Ser-484 and Ser-485 enhances actin polymerization activity. {ECO:0000269|PubMed:16257963}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9422512}. Nucleus {ECO:0000269|PubMed:16767080}. Cytoplasm {ECO:0000250|UniProtKB:Q91YD9}. Note=Preferentially localized in the cytoplasm when phosphorylated and in the nucleus when unphosphorylated (By similarity). Exported from the nucleus by an nuclear export signal (NES)-dependent mechanism to the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q91YD9}. | null | null | null | null | null | FUNCTION: Regulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex (PubMed:16767080, PubMed:19366662, PubMed:19487689, PubMed:22847007, PubMed:22921828, PubMed:9422512). Involved in various processes, such as mitosis and cytokinesis, via its role in the regulation of actin polymerization (PubMed:19366662, PubMed:19487689, PubMed:22847007, PubMed:22921828, PubMed:9422512). Together with CDC42, involved in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia (PubMed:9422512). In addition to its role in the cytoplasm, also plays a role in the nucleus by regulating gene transcription, probably by promoting nuclear actin polymerization (PubMed:16767080). Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression (By similarity). Plays a role in dendrite spine morphogenesis (By similarity). Decreasing levels of DNMBP (using antisense RNA) alters apical junction morphology in cultured enterocytes, junctions curve instead of being nearly linear (PubMed:19767742). {ECO:0000250|UniProtKB:Q91YD9, ECO:0000269|PubMed:16767080, ECO:0000269|PubMed:19366662, ECO:0000269|PubMed:19487689, ECO:0000269|PubMed:19767742, ECO:0000269|PubMed:22847007, ECO:0000269|PubMed:22921828, ECO:0000269|PubMed:9422512}. | Homo sapiens (Human) |
O00408 | PDE2A_HUMAN | MGQACGHSILCRSQQYPAARPAEPRGQQVFLKPDEPPPPPQPCADSLQDALLSLGSVIDISGLQRAVKEALSAVLPRVETVYTYLLDGESQLVCEDPPHELPQEGKVREAIISQKRLGCNGLGFSDLPGKPLARLVAPLAPDTQVLVMPLADKEAGAVAAVILVHCGQLSDNEEWSLQAVEKHTLVALRRVQVLQQRGPREAPRAVQNPPEGTAEDQKGGAAYTDRDRKILQLCGELYDLDASSLQLKVLQYLQQETRASRCCLLLVSEDNLQLSCKVIGDKVLGEEVSFPLTGCLGQVVEDKKSIQLKDLTSEDVQQLQSMLGCELQAMLCVPVISRATDQVVALACAFNKLEGDLFTDEDEHVIQHCFHYTSTVLTSTLAFQKEQKLKCECQALLQVAKNLFTHLDDVSVLLQEIITEARNLSNAEICSVFLLDQNELVAKVFDGGVVDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFYRGVDDSTGFRTRNILCFPIKNENQEVIGVAELVNKINGPWFSKFDEDLATAFSIYCGISIAHSLLYKKVNEAQYRSHLANEMMMYHMKVSDDEYTKLLHDGIQPVAAIDSNFASFTYTPRSLPEDDTSMAILSMLQDMNFINNYKIDCPTLARFCLMVKKGYRDPPYHNWMHAFSVSHFCYLLYKNLELTNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYSSEGSVMERHHFAQAIAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDLQKMAEVGYDRNNKQHHRLLLCLLMTSCDLSDQTKGWKTTRKIAELIYKEFFSQGDLEKAMGNRPMEMMDREKAYIPELQISFMEHIAMPIYKLLQDLFPKAAELYERVASNREHWTKVSHKFTIRGLPSNNSLDFLDEEYEVPDLDGTRAPINGCCSLDAE | 3.1.4.17 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:15938621, ECO:0000269|PubMed:19828435, ECO:0000269|PubMed:23899287}; Note=Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions. {ECO:0000269|PubMed:15938621, ECO:0000269|PubMed:19828435, ECO:0000269|PubMed:23899287}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15938621, ECO:0000269|PubMed:19828435, ECO:0000269|PubMed:23899287}; Note=Binds 2 divalent metal cations per subunit. Site 2 has a preference for magnesium ions. {ECO:0000269|PubMed:15938621, ECO:0000269|PubMed:19828435, ECO:0000269|PubMed:23899287}; | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; aorta development [GO:0035904]; cAMP-mediated signaling [GO:0019933]; cellular response to 2,3,7,8-tetrachlorodibenzodioxine [GO:1904613]; cellular response to cAMP [GO:0071320]; cellular response to cGMP [GO:0071321]; cellular response to granulocyte macrophage colony-stimulating factor stimulus [GO:0097011]; cellular response to macrophage colony-stimulating factor stimulus [GO:0036006]; cellular response to mechanical stimulus [GO:0071260]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular response to xenobiotic stimulus [GO:0071466]; cGMP catabolic process [GO:0046069]; cGMP-mediated signaling [GO:0019934]; establishment of endothelial barrier [GO:0061028]; heart valve development [GO:0003170]; monocyte differentiation [GO:0030224]; negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0106072]; negative regulation of cAMP-mediated signaling [GO:0043951]; negative regulation of cGMP-mediated signaling [GO:0010754]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of vascular permeability [GO:0043116]; positive regulation of gene expression [GO:0010628]; positive regulation of inflammatory response [GO:0050729]; positive regulation of vascular permeability [GO:0043117]; regulation of cAMP-mediated signaling [GO:0043949]; regulation of cGMP-mediated signaling [GO:0010752]; regulation of mitochondrion organization [GO:0010821]; ventricular septum development [GO:0003281] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial outer membrane [GO:0005741]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]; synaptic membrane [GO:0097060] | 3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; cAMP binding [GO:0030552]; cGMP binding [GO:0030553]; cGMP-stimulated cyclic-nucleotide phosphodiesterase activity [GO:0004118]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; phosphate ion binding [GO:0042301]; protein homodimerization activity [GO:0042803]; TPR domain binding [GO:0030911]; zinc ion binding [GO:0008270] | PF01590;PF00233; | 3.30.450.40;1.10.1300.10; | Cyclic nucleotide phosphodiesterase family, PDE2 subfamily | null | SUBCELLULAR LOCATION: [Isoform PDE2A3]: Cell membrane {ECO:0000269|PubMed:19632989, ECO:0000269|PubMed:28463107}; Lipid-anchor {ECO:0000269|PubMed:19632989}.; SUBCELLULAR LOCATION: [Isoform PDE2A2]: Mitochondrion matrix {ECO:0000250|UniProtKB:Q922S4}. Mitochondrion inner membrane {ECO:0000269|PubMed:28463107}. Mitochondrion outer membrane {ECO:0000269|PubMed:28463107}.; SUBCELLULAR LOCATION: [Isoform PDE2A1]: Cytoplasm {ECO:0000269|PubMed:19632989, ECO:0000269|PubMed:28463107}.; SUBCELLULAR LOCATION: [Isoform 5]: Mitochondrion {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-phosphate + H(+); Xref=Rhea:RHEA:14653, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57867, ChEBI:CHEBI:58464; EC=3.1.4.17; Evidence={ECO:0000269|PubMed:15938621, ECO:0000269|PubMed:29392776, ECO:0000269|PubMed:9210593}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14654; Evidence={ECO:0000305|PubMed:9210593}; CATALYTIC ACTIVITY: Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746, ChEBI:CHEBI:58115; Evidence={ECO:0000269|PubMed:15938621, ECO:0000269|PubMed:29392776, ECO:0000269|PubMed:9210593}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958; Evidence={ECO:0000305|PubMed:9210593}; CATALYTIC ACTIVITY: Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15938621, ECO:0000269|PubMed:29392776, ECO:0000269|PubMed:9210593}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278; Evidence={ECO:0000305|PubMed:9210593}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=43.7 uM for 3',5'-cyclic GMP {ECO:0000269|PubMed:15938621}; KM=32 uM for 3',5'-cyclic AMP {ECO:0000269|PubMed:15938621}; Vmax=20.5 nmol/min/mg enzyme for 3',5'-cyclic AMP {ECO:0000269|PubMed:9210593}; Vmax=28.5 nmol/min/mg enzyme for 3',5'-cyclic GMP {ECO:0000269|PubMed:9210593}; Note=kcat is 0.6 sec(-1) with 3',5'-cyclic GMP as substrate (PubMed:15938621). kcat is 0.12 sec(-1) with 3',5'-cyclic AMP as substrate (PubMed:15938621). {ECO:0000269|PubMed:15938621}; | null | null | null | FUNCTION: cGMP-activated cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes (PubMed:15938621, PubMed:29392776, PubMed:9210593). Has a higher efficiency with cGMP compared to cAMP (PubMed:15938621). Plays a role in cell growth and migration (PubMed:24705027). {ECO:0000269|PubMed:15938621, ECO:0000269|PubMed:24705027, ECO:0000269|PubMed:29392776, ECO:0000269|PubMed:9210593}.; FUNCTION: [Isoform PDE2A2]: Regulates mitochondrial cAMP levels and respiration (By similarity). Involved in the regulation of mitochondria morphology/dynamics and apoptotic cell death via local modulation of cAMP/PKA signaling in the mitochondrion, including the monitoring of local cAMP levels at the outer mitochondrial membrane and of PKA-dependent phosphorylation of DNM1L (PubMed:28463107). {ECO:0000250|UniProtKB:Q922S4, ECO:0000269|PubMed:28463107}. | Homo sapiens (Human) |
O00409 | FOXN3_HUMAN | MGPVMPPSKKPESSGISVSSGLSQCYGGSGFSKALQEDDDLDFSLPDIRLEEGAMEDEELTNLNWLHESKNLLKSFGESVLRSVSPVQDLDDDTPPSPAHSDMPYDARQNPNCKPPYSFSCLIFMAIEDSPTKRLPVKDIYNWILEHFPYFANAPTGWKNSVRHNLSLNKCFKKVDKERSQSIGKGSLWCIDPEYRQNLIQALKKTPYHPHPHVFNTPPTCPQAYQSTSGPPIWPGSTFFKRNGALLQDPDIDAASAMMLLNTPPEIQAGFPPGVIQNGARVLSRGLFPGVRPLPITPIGVTAAMRNGITSCRMRTESEPSCGSPVVSGDPKEDHNYSSAKSSNARSTSPTSDSISSSSSSADDHYEFATKGSQEGSEGSEGSFRSHESPSDTEEDDRKHSQKEPKDSLGDSGYASQHKKRQHFAKARKVPSDTLPLKKRRTEKPPESDDEEMKEAAGSLLHLAGIRSCLNNITNRTAKGQKEQKETTKN | null | null | craniofacial suture morphogenesis [GO:0097094]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; negative regulation of DNA-templated transcription [GO:0045892]; regulation of DNA-templated transcription [GO:0006355] | chromatin [GO:0000785]; nucleus [GO:0005634] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981] | PF00250; | 1.10.10.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Acts as a transcriptional repressor. May be involved in DNA damage-inducible cell cycle arrests (checkpoints). {ECO:0000269|PubMed:16102918}. | Homo sapiens (Human) |
O00410 | IPO5_HUMAN | MAAAAAEQQQFYLLLGNLLSPDNVVRKQAEETYENIPGQSKITFLLQAIRNTTAAEEARQMAAVLLRRLLSSAFDEVYPALPSDVQTAIKSELLMIIQMETQSSMRKKVCDIAAELARNLIDEDGNNQWPEGLKFLFDSVSSQNVGLREAALHIFWNFPGIFGNQQQHYLDVIKRMLVQCMQDQEHPSIRTLSARATAAFILANEHNVALFKHFADLLPGFLQAVNDSCYQNDDSVLKSLVEIADTVPKYLRPHLEATLQLSLKLCGDTSLNNMQRQLALEVIVTLSETAAAMLRKHTNIVAQTIPQMLAMMVDLEEDEDWANADELEDDDFDSNAVAGESALDRMACGLGGKLVLPMIKEHIMQMLQNPDWKYRHAGLMALSAIGEGCHQQMEGILNEIVNFVLLFLQDPHPRVRYAACNAVGQMATDFAPGFQKKFHEKVIAALLQTMEDQGNQRVQAHAAAALINFTEDCPKSLLIPYLDNLVKHLHSIMVLKLQELIQKGTKLVLEQVVTSIASVADTAEEKFVPYYDLFMPSLKHIVENAVQKELRLLRGKTIECISLIGLAVGKEKFMQDASDVMQLLLKTQTDFNDMEDDDPQISYMISAWARMCKILGKEFQQYLPVVMGPLMKTASIKPEVALLDTQDMENMSDDDGWEFVNLGDQQSFGIKTAGLEEKSTACQMLVCYAKELKEGFVEYTEQVVKLMVPLLKFYFHDGVRVAAAESMPLLLECARVRGPEYLTQMWHFMCDALIKAIGTEPDSDVLSEIMHSFAKCIEVMGDGCLNNEHFEELGGILKAKLEEHFKNQELRQVKRQDEDYDEQVEESLQDEDDNDVYILTKVSDILHSIFSSYKEKVLPWFEQLLPLIVNLICPHRPWPDRQWGLCIFDDVIEHCSPASFKYAEYFLRPMLQYVCDNSPEVRQAAAYGLGVMAQYGGDNYRPFCTEALPLLVRVIQSADSKTKENVNATENCISAVGKIMKFKPDCVNVEEVLPHWLSWLPLHEDKEEAVQTFNYLCDLIESNHPIVLGPNNTNLPKIFSIIAEGEMHEAIKHEDPCAKRLANVVRQVQTSGGLWTECIAQLSPEQQAAIQELLNSA | null | null | cellular response to amino acid stimulus [GO:0071230]; cytoplasmic pattern recognition receptor signaling pathway [GO:0002753]; negative regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045736]; NLS-bearing protein import into nucleus [GO:0006607]; positive regulation of protein import into nucleus [GO:0042307]; protein import into nucleus [GO:0006606]; ribosomal protein import into nucleus [GO:0006610] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | GTPase inhibitor activity [GO:0005095]; nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139]; RNA binding [GO:0003723]; small GTPase binding [GO:0031267] | PF02985;PF13513;PF18808;PF18816;PF18829; | 1.25.10.10; | Importin beta family, Importin beta-3 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleolus. Note=Nucleus; nuclear rim. Found particularly in the nuclear rim and nucleolus. | null | null | null | null | null | FUNCTION: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5 (PubMed:11682607, PubMed:9687515). In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. Binds to CPEB3 and mediates its nuclear import following neuronal stimulation (By similarity). In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. {ECO:0000250|UniProtKB:Q8BKC5, ECO:0000269|PubMed:11682607, ECO:0000269|PubMed:9687515}. | Homo sapiens (Human) |
O00411 | RPOM_HUMAN | MSALCWGRGAAGLKRALRPCGRPGLPGKEGTAGGVCGPRRSSSASPQEQDQDRRKDWGHVELLEVLQARVRQLQAESVSEVVVNRVDVARLPECGSGDGSLQPPRKVQMGAKDATPVPCGRWAKILEKDKRTQQMRMQRLKAKLQMPFQSGEFKALTRRLQVEPRLLSKQMAGCLEDCTRQAPESPWEEQLARLLQEAPGKLSLDVEQAPSGQHSQAQLSGQQQRLLAFFKCCLLTDQLPLAHHLLVVHHGQRQKRKLLTLDMYNAVMLGWARQGAFKELVYVLFMVKDAGLTPDLLSYAAALQCMGRQDQDAGTIERCLEQMSQEGLKLQALFTAVLLSEEDRATVLKAVHKVKPTFSLPPQLPPPVNTSKLLRDVYAKDGRVSYPKLHLPLKTLQCLFEKQLHMELASRVCVVSVEKPTLPSKEVKHARKTLKTLRDQWEKALCRALRETKNRLEREVYEGRFSLYPFLCLLDEREVVRMLLQVLQALPAQGESFTTLARELSARTFSRHVVQRQRVSGQVQALQNHYRKYLCLLASDAEVPEPCLPRQYWEELGAPEALREQPWPLPVQMELGKLLAEMLVQATQMPCSLDKPHRSSRLVPVLYHVYSFRNVQQIGILKPHPAYVQLLEKAAEPTLTFEAVDVPMLCPPLPWTSPHSGAFLLSPTKLMRTVEGATQHQELLETCPPTALHGALDALTQLGNCAWRVNGRVLDLVLQLFQAKGCPQLGVPAPPSEAPQPPEAHLPHSAAPARKAELRRELAHCQKVAREMHSLRAEALYRLSLAQHLRDRVFWLPHNMDFRGRTYPCPPHFNHLGSDVARALLEFAQGRPLGPHGLDWLKIHLVNLTGLKKREPLRKRLAFAEEVMDDILDSADQPLTGRKWWMGAEEPWQTLACCMEVANAVRASDPAAYVSHLPVHQDGSCNGLQHYAALGRDSVGAASVNLEPSDVPQDVYSGVAAQVEVFRRQDAQRGMRVAQVLEGFITRKVVKQTVMTVVYGVTRYGGRLQIEKRLRELSDFPQEFVWEASHYLVRQVFKSLQEMFSGTRAIQHWLTESARLISHMGSVVEWVTPLGVPVIQPYRLDSKVKQIGGGIQSITYTHNGDISRKPNTRKQKNGFPPNFIHSLDSSHMMLTALHCYRKGLTFVSVHDCYWTHAADVSVMNQVCREQFVRLHSEPILQDLSRFLVKRFCSEPQKILEASQLKETLQAVPKPGAFDLEQVKRSTYFFS | 2.7.7.6 | null | mitochondrial transcription [GO:0006390]; transcription initiation at mitochondrial promoter [GO:0006391] | mitochondrial DNA-directed RNA polymerase complex [GO:0034245]; mitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; protein-containing complex [GO:0032991] | 3'-5'-RNA exonuclease activity [GO:0000175]; DNA primase activity [GO:0003896]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; mitochondrial promoter sequence-specific DNA binding [GO:0001018]; RNA binding [GO:0003723]; sequence-specific DNA binding [GO:0043565] | PF00940;PF14700; | 1.10.287.280;1.10.150.20;1.10.1320.10;1.25.40.10; | Phage and mitochondrial RNA polymerase family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23283301, ECO:0000269|PubMed:29445193}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10031, ECO:0000255|PROSITE-ProRule:PRU10032}; | null | null | null | null | FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of mitochondrial DNA into RNA using the four ribonucleoside triphosphates as substrates (PubMed:21278163, PubMed:33602924). Component of the mitochondrial transcription initiation complex, composed at least of TFB2M, TFAM and POLRMT that is required for basal transcription of mitochondrial DNA (PubMed:29149603). In this complex, TFAM recruits POLRMT to a specific promoter whereas TFB2M induces structural changes in POLRMT to enable promoter opening and trapping of the DNA non-template strand (PubMed:29149603). Has DNA primase activity (PubMed:18685103, PubMed:33602924). Catalyzes the synthesis of short RNA primers that are necessary for the initiation of lagging-strand DNA synthesis from the origin of light-strand DNA replication (OriL) (PubMed:18685103, PubMed:33602924). {ECO:0000269|PubMed:18685103, ECO:0000269|PubMed:21278163, ECO:0000269|PubMed:29149603, ECO:0000269|PubMed:33602924}. | Homo sapiens (Human) |
O00418 | EF2K_HUMAN | MADEDLIFRLEGVDGGQSPRAGHDGDSDGDSDDEEGYFICPITDDPSSNQNVNSKVNKYYSNLTKSERYSSSGSPANSFHFKEAWKHAIQKAKHMPDPWAEFHLEDIATERATRHRYNAVTGEWLDDEVLIKMASQPFGRGAMRECFRTKKLSNFLHAQQWKGASNYVAKRYIEPVDRDVYFEDVRLQMEAKLWGEEYNRHKPPKQVDIMQMCIIELKDRPGKPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTETGTDFGDGNLGVRGMALFFYSHACNRICESMGLAPFDLSPRERDAVNQNTKLLQSAKTILRGTEEKCGSPQVRTLSGSRPPLLRPLSENSGDENMSDVTFDSLPSSPSSATPHSQKLDHLHWPVFSDLDNMASRDHDHLDNHRESENSGDSGYPSEKRGELDDPEPREHGHSYSNRKYESDEDSLGSSGRVCVEKWNLLNSSRLHLPRASAVALEVQRLNALDLEKKIGKSILGKVHLAMVRYHEGGRFCEKGEEWDQESAVFHLEHAANLGELEAIVGLGLMYSQLPHHILADVSLKETEENKTKGFDYLLKAAEAGDRQSMILVARAFDSGQNLSPDRCQDWLEALHWYNTALEMTDCDEGGEYDGMQDEPRYMMLAREAEMLFTGGYGLEKDPQRSGDLYTQAAEAAMEAMKGRLANQYYQKAEEAWAQMEE | 2.7.11.20 | null | cellular response to anoxia [GO:0071454]; cellular response to brain-derived neurotrophic factor stimulus [GO:1990416]; cellular response to calcium ion [GO:0071277]; cellular response to cAMP [GO:0071320]; cellular response to insulin stimulus [GO:0032869]; myosin II filament disassembly [GO:0031037]; negative regulation of apoptotic process [GO:0043066]; positive regulation of dendritic spine morphogenesis [GO:0061003]; positive regulation of endocytosis [GO:0045807]; positive regulation of synapse assembly [GO:0051965]; protein autophosphorylation [GO:0046777]; regulation of protein autophosphorylation [GO:0031952]; regulation of translation at postsynapse [GO:0140245]; response to differentiation-inducing factor 1 [GO:1903013]; response to ischemia [GO:0002931]; response to prolactin [GO:1990637]; translational elongation [GO:0006414] | actomyosin contractile ring [GO:0005826]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; postsynaptic density [GO:0014069] | ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; elongation factor-2 kinase activity [GO:0004686]; myosin heavy chain kinase activity [GO:0016905]; protein kinase activity [GO:0004672]; translation factor activity, RNA binding [GO:0008135] | PF02816; | 3.20.200.10;1.25.40.10; | Protein kinase superfamily, Alpha-type protein kinase family | PTM: Autophosphorylated at multiple residues, Thr-348 being the major site. Phosphorylated by AMP-activated protein kinase AMPK at Ser-398 leading to EEF2K activation and protein synthesis inhibition. Phosphorylated by TRPM7 at Ser-78 resulting in improved protein stability, higher EE2F phosphorylated and subsequently reduced rate of protein synthesis. Phosphorylation by other kinases such as CDK1 and MAPK13 at Ser-359 or RPS6KA1 and RPS6KB1 at Ser-366 instead decrease EEF2K activity and promote protein synthesis. {ECO:0000269|PubMed:11015200, ECO:0000269|PubMed:11500363, ECO:0000269|PubMed:11500364, ECO:0000269|PubMed:14709557, ECO:0000269|PubMed:18337751, ECO:0000269|PubMed:21112387, ECO:0000269|PubMed:22216903}. | null | CATALYTIC ACTIVITY: Reaction=[translation elongation factor 2] + ATP = [translation elongation factor 2]-phosphate + ADP + H(+); Xref=Rhea:RHEA:21436, Rhea:RHEA-COMP:11268, Rhea:RHEA-COMP:11269, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.20; Evidence={ECO:0000269|PubMed:11015200, ECO:0000269|PubMed:9144159}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.2 uM for EEF2 {ECO:0000269|PubMed:11015200}; Vmax=4 nmol/min/mg enzyme {ECO:0000269|PubMed:11015200}; | null | null | null | FUNCTION: Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive. In turn, the rate of protein synthesis is reduced. {ECO:0000269|PubMed:14709557, ECO:0000269|PubMed:9144159}. | Homo sapiens (Human) |
O00421 | CCRL2_HUMAN | MANYTLAPEDEYDVLIEGELESDEAEQCDKYDAQALSAQLVPSLCSAVFVIGVLDNLLVVLILVKYKGLKRVENIYLLNLAVSNLCFLLTLPFWAHAGGDPMCKILIGLYFVGLYSETFFNCLLTVQRYLVFLHKGNFFSARRRVPCGIITSVLAWVTAILATLPEFVVYKPQMEDQKYKCAFSRTPFLPADETFWKHFLTLKMNISVLVLPLFIFTFLYVQMRKTLRFREQRYSLFKLVFAIMVVFLLMWAPYNIAFFLSTFKEHFSLSDCKSSYNLDKSVHITKLIATTHCCINPLLYAFLDGTFSKYLCRCFHLRSNTPLQPRGQSAQGTSREEPDHSTEV | null | null | calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; chemotaxis [GO:0006935]; G protein-coupled receptor signaling pathway [GO:0007186]; immune response [GO:0006955]; inflammatory response [GO:0006954]; positive regulation of cytosolic calcium ion concentration [GO:0007204] | cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886] | C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493]; CCR chemokine receptor binding [GO:0048020]; chemokine receptor activity [GO:0004950]; chemokine receptor binding [GO:0042379] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18397265, ECO:0000269|PubMed:20002784}; Multi-pass membrane protein {ECO:0000269|PubMed:18397265, ECO:0000269|PubMed:20002784}. | null | null | null | null | null | FUNCTION: Receptor for CCL19 and chemerin/RARRES2. Does not appear to be a signaling receptor, but may have a role in modulating chemokine-triggered immune responses by capturing and internalizing CCL19 or by presenting RARRES2 ligand to CMKLR1, a functional signaling receptors. Plays a critical role for the development of Th2 responses. | Homo sapiens (Human) |
O00422 | SAP18_HUMAN | MAVESRVTQEEIKKEPEKPIDREKTCPLLLRVFTTNNGRHHRMDEFSRGNVPSSELQIYTWMDATLKELTSLVKEVYPEARKKGTHFNFAIVFTDVKRPGYRVKEIGSTMSGRKGTDDSMTLQSQKFQIGDYLDIAITPPNRAPPPSGRMRPY | null | null | mRNA processing [GO:0006397]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; positive regulation of apoptotic process [GO:0043065]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of transcription by RNA polymerase II [GO:0006357]; RNA splicing [GO:0008380] | ASAP complex [GO:0061574]; cytosol [GO:0005829]; histone deacetylase complex [GO:0000118]; nuclear body [GO:0016604]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | RNA binding [GO:0003723]; transcription corepressor activity [GO:0003714] | PF06487; | 3.10.20.550; | SAP18 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16314458}. Cytoplasm {ECO:0000269|PubMed:16314458}. Nucleus speckle {ECO:0000269|PubMed:20966198}. Note=Shuttles between the nucleus and the cytoplasm (PubMed:16314458). Colocalizes with ACIN1 and SRSF2 in nuclear speckles (PubMed:20966198). {ECO:0000269|PubMed:16314458, ECO:0000269|PubMed:20966198}. | null | null | null | null | null | FUNCTION: Component of the SIN3-repressing complex. Enhances the ability of SIN3-HDAC1-mediated transcriptional repression. When tethered to the promoter, it can direct the formation of a repressive complex to core histone proteins. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP and PSAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. The ASAP complex can inhibit mRNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits the formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. {ECO:0000269|PubMed:12665594, ECO:0000269|PubMed:20966198, ECO:0000269|PubMed:22203037, ECO:0000269|PubMed:9150135}. | Homo sapiens (Human) |
O00423 | EMAL1_HUMAN | MEDGFSSYSSLYDTSSLLQFCNDDSASAASSMEVTDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRKGPTKARPLMQTLPLRTTVNNGTVLPKKPTGSLPSPSGVRKETAVPATKSNIKRTSSSERVSPGGRRESNGDSRGNRNRTGSTSSSSSGKKNSESKPKEPVFSAEEGYVKMFLRGRPVTMYMPKDQVDSYSLEAKVELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNVEEQLQRHYAGHNDDVKCLAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDSVTLNTLHVIGIGFFDRAVTCIAFSKSNGGTNLCAVDDSNDHVLSVWDWQKEEKLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTLEGSSLNKKQGLFEKQEKPKFVLCVTFSENGDTITGDSSGNILVWGKGTNRISYAVQGAHEGGIFALCMLRDGTLVSGGGKDRKLISWSGNYQKLRKTEIPEQFGPIRTVAEGKGDVILIGTTRNFVLQGTLSGDFTPITQGHTDELWGLAIHASKSQFLTCGHDKHATLWDAVGHRPVWDKIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVSDNGRKYTRVGKCSGHSSFITHLDWSVNSQFLVSNSGDYEILYWVPSACKQVVSVETTRDIEWATYTCTLGFHVFGVWPEGSDGTDINAVCRAHEKKLLSTGDDFGKVHLFSYPCSQFRAPSHIYGGHSSHVTNVDFLCEDSHLISTGGKDTSIMQWRVI | null | null | brain development [GO:0007420]; hematopoietic progenitor cell differentiation [GO:0002244]; microtubule cytoskeleton organization [GO:0000226]; mitotic spindle organization [GO:0007052]; neuroblast proliferation [GO:0007405] | cytosol [GO:0005829]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875]; mitotic spindle midzone [GO:1990023]; mitotic spindle pole [GO:0097431]; perinuclear region of cytoplasm [GO:0048471] | calcium ion binding [GO:0005509]; microtubule binding [GO:0008017]; tubulin binding [GO:0015631] | PF03451;PF00400; | 2.130.10.10; | WD repeat EMAP family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q05BC3}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q05BC3}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24859200, ECO:0000269|PubMed:25740311}. Note=Detected in cytoplasmic punctae. Co-localizes with microtubules (PubMed:24859200, PubMed:25740311). Enriched in perinuclear regions during interphase and in the region of spindle microtubules during metaphase. Enriched at the midzone during telophase and cytokinesis. Detected at growth cones in neurons (By similarity). {ECO:0000250|UniProtKB:Q05BC3, ECO:0000269|PubMed:24859200, ECO:0000269|PubMed:25740311}. | null | null | null | null | null | FUNCTION: Modulates the assembly and organization of the microtubule cytoskeleton, and probably plays a role in regulating the orientation of the mitotic spindle and the orientation of the plane of cell division. Required for normal proliferation of neuronal progenitor cells in the developing brain and for normal brain development. Does not affect neuron migration per se. {ECO:0000250|UniProtKB:Q05BC3}. | Homo sapiens (Human) |
O00425 | IF2B3_HUMAN | MNKLYIGNLSENAAPSDLESIFKDAKIPVSGPFLVKTGYAFVDCPDESWALKAIEALSGKIELHGKPIEVEHSVPKRQRIRKLQIRNIPPHLQWEVLDSLLVQYGVVESCEQVNTDSETAVVNVTYSSKDQARQALDKLNGFQLENFTLKVAYIPDEMAAQQNPLQQPRGRRGLGQRGSSRQGSPGSVSKQKPCDLPLRLLVPTQFVGAIIGKEGATIRNITKQTQSKIDVHRKENAGAAEKSITILSTPEGTSAACKSILEIMHKEAQDIKFTEEIPLKILAHNNFVGRLIGKEGRNLKKIEQDTDTKITISPLQELTLYNPERTITVKGNVETCAKAEEEIMKKIRESYENDIASMNLQAHLIPGLNLNALGLFPPTSGMPPPTSGPPSAMTPPYPQFEQSETETVHLFIPALSVGAIIGKQGQHIKQLSRFAGASIKIAPAEAPDAKVRMVIITGPPEAQFKAQGRIYGKIKEENFVSPKEEVKLEAHIRVPSFAAGRVIGKGGKTVNELQNLSSAEVVVPRDQTPDENDQVVVKITGHFYACQVAQRKIQEILTQVKQHQQQKALQSGPPQSRRK | null | null | anatomical structure morphogenesis [GO:0009653]; CRD-mediated mRNA stabilization [GO:0070934]; mRNA transport [GO:0051028]; negative regulation of translation [GO:0017148]; nervous system development [GO:0007399]; regulation of cytokine production [GO:0001817]; regulation of gene expression [GO:0010468]; translation [GO:0006412] | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; nucleus [GO:0005634]; P-body [GO:0000932] | mRNA 3'-UTR binding [GO:0003730]; mRNA 5'-UTR binding [GO:0048027]; N6-methyladenosine-containing RNA reader activity [GO:1990247]; RNA binding [GO:0003723]; translation regulator activity [GO:0045182] | PF00013;PF00076; | 3.30.310.210;3.30.70.330;3.30.1370.10; | RRM IMP/VICKZ family | null | SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, P-body {ECO:0000269|PubMed:29476152}. Cytoplasm, Stress granule {ECO:0000269|PubMed:29476152}. Note=Found in lamellipodia of the leading edge, in the perinuclear region, and beneath the plasma membrane. The subcytoplasmic localization is cell specific and regulated by cell contact and growth. Localized at the connecting piece and the tail of the spermatozoa. Colocalized with CD44 mRNA in RNP granules. In response to cellular stress, such as oxidative stress, recruited to stress granules. | null | null | null | null | null | FUNCTION: RNA-binding factor that may recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Preferentially binds to N6-methyladenosine (m6A)-containing mRNAs and increases their stability (PubMed:29476152). Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells. Binds to beta-actin/ACTB and MYC transcripts. Increases MYC mRNA stability by binding to the coding region instability determinant (CRD) and binding is enhanced by m6A-modification of the CRD (PubMed:29476152). Binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNAs. {ECO:0000269|PubMed:16541107, ECO:0000269|PubMed:23640942, ECO:0000269|PubMed:29476152}. | Homo sapiens (Human) |
O00429 | DNM1L_HUMAN | MEALIPVINKLQDVFNTVGADIIQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGIVTRRPLILQLVHVSQEDKRKTTGEENGVEAEEWGKFLHTKNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKIFSPNVVNLTLVDLPGMTKVPVGDQPKDIELQIRELILRFISNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKLDLMDAGTDAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKKYPSLANRNGTKYLARTLNRLLMHHIRDCLPELKTRINVLAAQYQSLLNSYGEPVDDKSATLLQLITKFATEYCNTIEGTAKYIETSELCGGARICYIFHETFGRTLESVDPLGGLNTIDILTAIRNATGPRPALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCSNYSTQELLRFPKLHDAIVEVVTCLLRKRLPVTNEMVHNLVAIELAYINTKHPDFADACGLMNNNIEEQRRNRLARELPSAVSRDKSSKVPSALAPASQEPSPAASAEADGKLIQDSRRETKNVASGGGGVGDGVQEPTTGNWRGMLKTSKAEELLAEEKSKPIPIMPASPQKGHAVNLLDVPVPVARKLSAREQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKALQGASQIIAEIRETHLW | 3.6.5.5 | null | calcium ion transport [GO:0006816]; endocytosis [GO:0006897]; heart contraction [GO:0060047]; intracellular distribution of mitochondria [GO:0048312]; membrane fusion [GO:0061025]; mitochondrial fission [GO:0000266]; mitochondrial fragmentation involved in apoptotic process [GO:0043653]; mitochondrial membrane fission [GO:0090149]; mitochondrion organization [GO:0007005]; mitocytosis [GO:0160040]; necroptotic process [GO:0070266]; peroxisome fission [GO:0016559]; positive regulation of apoptotic process [GO:0043065]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of mitochondrial fission [GO:0090141]; positive regulation of neutrophil chemotaxis [GO:0090023]; positive regulation of protein secretion [GO:0050714]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; protein complex oligomerization [GO:0051259]; protein localization to mitochondrion [GO:0070585]; protein-containing complex assembly [GO:0065003]; regulation of ATP metabolic process [GO:1903578]; regulation of gene expression [GO:0010468]; regulation of mitochondrion organization [GO:0010821]; regulation of mitophagy [GO:1901524]; regulation of peroxisome organization [GO:1900063]; release of cytochrome c from mitochondria [GO:0001836]; rhythmic process [GO:0048511] | brush border [GO:0005903]; clathrin-coated pit [GO:0005905]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; microtubule [GO:0005874]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; perinuclear region of cytoplasm [GO:0048471]; peroxisome [GO:0005777]; protein-containing complex [GO:0032991]; synaptic vesicle membrane [GO:0030672] | GTP binding [GO:0005525]; GTP-dependent protein binding [GO:0030742]; GTPase activator activity [GO:0005096]; GTPase activity [GO:0003924]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; microtubule binding [GO:0008017]; protein homodimerization activity [GO:0042803]; small GTPase binding [GO:0031267]; ubiquitin protein ligase binding [GO:0031625] | PF01031;PF00350;PF02212; | 1.20.120.1240;3.40.50.300; | TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family | PTM: Phosphorylation/dephosphorylation events on two sites near the GED domain regulate mitochondrial fission (PubMed:17301055, PubMed:17553808, PubMed:18695047, PubMed:18838687, PubMed:23283981, PubMed:29478834, PubMed:33850055). Phosphorylation on Ser-637 by CAMK1 and PKA inhibits the GTPase activity, leading to a defect in mitochondrial fission promoting mitochondrial elongation (PubMed:17553808, PubMed:18695047, PubMed:23283981, PubMed:29478834). Dephosphorylated on this site by PPP3CA which promotes mitochondrial fission (PubMed:18838687). Phosphorylation on Ser-616 by CDK1 and PINK1 activates the GTPase activity and promotes mitochondrial fission (PubMed:18838687, PubMed:21822277, PubMed:32484300). Phosphorylated in a circadian manner at Ser-637 (PubMed:29478834). Dephosphorylated by PGAM5 (PubMed:32439975). {ECO:0000269|PubMed:17301055, ECO:0000269|PubMed:17553808, ECO:0000269|PubMed:18695047, ECO:0000269|PubMed:18838687, ECO:0000269|PubMed:21822277, ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:29478834, ECO:0000269|PubMed:32439975, ECO:0000269|PubMed:32484300, ECO:0000269|PubMed:33850055}.; PTM: Sumoylated on various lysine residues within the B domain, probably by MUL1. Sumoylation positively regulates mitochondrial fission. Desumoylated by SENP5 during G2/M transition of mitosis. Appears to be linked to its catalytic activity. {ECO:0000269|PubMed:19407830, ECO:0000269|PubMed:19411255, ECO:0000269|PubMed:19638400}.; PTM: S-nitrosylation increases DNM1L dimerization, mitochondrial fission and causes neuronal damage. {ECO:0000269|PubMed:19342591}.; PTM: Ubiquitination by MARCHF5 affects mitochondrial morphology. {ECO:0000269|PubMed:16874301, ECO:0000269|PubMed:16936636}.; PTM: O-GlcNAcylation augments the level of the GTP-bound active form of DNM1L and induces translocation from the cytoplasm to mitochondria in cardiomyocytes. It also decreases phosphorylation at Ser-637 (By similarity). {ECO:0000250|UniProtKB:O35303}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11514614, ECO:0000269|PubMed:12618434, ECO:0000269|PubMed:9786947}. Golgi apparatus {ECO:0000269|PubMed:20688057, ECO:0000269|PubMed:9348079, ECO:0000269|PubMed:9570752}. Endomembrane system {ECO:0000269|PubMed:11514614, ECO:0000269|PubMed:9348079, ECO:0000269|PubMed:9472031, ECO:0000269|PubMed:9570752}; Peripheral membrane protein. Mitochondrion outer membrane {ECO:0000269|PubMed:26122121, ECO:0000269|PubMed:27145208, ECO:0000269|PubMed:27145933, ECO:0000269|PubMed:28969390}; Peripheral membrane protein. Peroxisome {ECO:0000269|PubMed:12499366, ECO:0000269|PubMed:12618434}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:O35303}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:O35303}. Note=Mainly cytosolic. Recruited by RALA and RALBP1 to mitochondrion during mitosis (PubMed:21822277). Translocated to the mitochondrial membrane through O-GlcNAcylation and interaction with FIS1. Colocalized with MARCHF5 at mitochondrial membrane (PubMed:17606867). Localizes to mitochondria at sites of division (PubMed:15208300). Localizes to mitochondria following necrosis induction. Recruited to the mitochondrial outer membrane by interaction with MIEF1. Mitochondrial recruitment is inhibited by C11orf65/MFI (By similarity). Associated with peroxisomal membranes, partly recruited there by PEX11B. May also be associated with endoplasmic reticulum tubules and cytoplasmic vesicles and found to be perinuclear (PubMed:9422767, PubMed:9570752). In some cell types, localizes to the Golgi complex (By similarity). Binds to phospholipid membranes (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q8K1M6, ECO:0000269|PubMed:15208300, ECO:0000269|PubMed:17606867, ECO:0000269|PubMed:21822277, ECO:0000269|PubMed:9422767, ECO:0000269|PubMed:9570752}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5; Evidence={ECO:0000269|PubMed:23977156, ECO:0000269|PubMed:9422767}; | null | null | null | null | FUNCTION: Functions in mitochondrial and peroxisomal division (PubMed:11514614, PubMed:12499366, PubMed:17301055, PubMed:17460227, PubMed:17553808, PubMed:18695047, PubMed:18838687, PubMed:19342591, PubMed:19411255, PubMed:19638400, PubMed:23283981, PubMed:23530241, PubMed:23921378, PubMed:26992161, PubMed:27145208, PubMed:27145933, PubMed:27301544, PubMed:27328748, PubMed:29478834, PubMed:32439975, PubMed:32484300, PubMed:9570752, PubMed:9786947). Mediates membrane fission through oligomerization into membrane-associated tubular structures that wrap around the scission site to constrict and sever the mitochondrial membrane through a GTP hydrolysis-dependent mechanism (PubMed:23530241, PubMed:23584531, PubMed:33850055). The specific recruitment at scission sites is mediated by membrane receptors like MFF, MIEF1 and MIEF2 for mitochondrial membranes (PubMed:23283981, PubMed:23921378, PubMed:29899447). While the recruitment by the membrane receptors is GTP-dependent, the following hydrolysis of GTP induces the dissociation from the receptors and allows DNM1L filaments to curl into closed rings that are probably sufficient to sever a double membrane (PubMed:29899447). Acts downstream of PINK1 to promote mitochondrial fission in a PRKN-dependent manner (PubMed:32484300). Plays an important role in mitochondrial fission during mitosis (PubMed:19411255, PubMed:26992161, PubMed:27301544, PubMed:27328748). Through its function in mitochondrial division, ensures the survival of at least some types of postmitotic neurons, including Purkinje cells, by suppressing oxidative damage (By similarity). Required for normal brain development, including that of cerebellum (PubMed:17460227, PubMed:26992161, PubMed:27145208, PubMed:27301544, PubMed:27328748). Facilitates developmentally regulated apoptosis during neural tube formation (By similarity). Required for a normal rate of cytochrome c release and caspase activation during apoptosis; this requirement may depend upon the cell type and the physiological apoptotic cues (By similarity). Required for formation of endocytic vesicles (PubMed:20688057, PubMed:23792689, PubMed:9570752). Proposed to regulate synaptic vesicle membrane dynamics through association with BCL2L1 isoform Bcl-X(L) which stimulates its GTPase activity in synaptic vesicles; the function may require its recruitment by MFF to clathrin-containing vesicles (PubMed:17015472, PubMed:23792689). Required for programmed necrosis execution (PubMed:22265414). Rhythmic control of its activity following phosphorylation at Ser-637 is essential for the circadian control of mitochondrial ATP production (PubMed:29478834). {ECO:0000250|UniProtKB:Q8K1M6, ECO:0000269|PubMed:11514614, ECO:0000269|PubMed:12499366, ECO:0000269|PubMed:17015472, ECO:0000269|PubMed:17301055, ECO:0000269|PubMed:17460227, ECO:0000269|PubMed:17553808, ECO:0000269|PubMed:18695047, ECO:0000269|PubMed:18838687, ECO:0000269|PubMed:19342591, ECO:0000269|PubMed:19411255, ECO:0000269|PubMed:19638400, ECO:0000269|PubMed:20688057, ECO:0000269|PubMed:22265414, ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:23530241, ECO:0000269|PubMed:23584531, ECO:0000269|PubMed:23792689, ECO:0000269|PubMed:23921378, ECO:0000269|PubMed:26992161, ECO:0000269|PubMed:27145208, ECO:0000269|PubMed:27145933, ECO:0000269|PubMed:27301544, ECO:0000269|PubMed:27328748, ECO:0000269|PubMed:29478834, ECO:0000269|PubMed:29899447, ECO:0000269|PubMed:32439975, ECO:0000269|PubMed:32484300, ECO:0000269|PubMed:33850055, ECO:0000269|PubMed:9570752, ECO:0000269|PubMed:9786947}.; FUNCTION: [Isoform 1]: Inhibits peroxisomal division when overexpressed. {ECO:0000269|PubMed:12618434}.; FUNCTION: [Isoform 4]: Inhibits peroxisomal division when overexpressed. {ECO:0000269|PubMed:12618434}. | Homo sapiens (Human) |
O00442 | RTCA_HUMAN | MAGPRVEVDGSIMEGGGQILRVSTALSCLLGLPLRVQKIRAGRSTPGLRPQHLSGLEMIRDLCDGQLEGAEIGSTEITFTPEKIKGGIHTADTKTAGSVCLLMQVSMPCVLFAASPSELHLKGGTNAEMAPQIDYTVMVFKPIVEKFGFIFNCDIKTRGYYPKGGGEVIVRMSPVKQLNPINLTERGCVTKIYGRAFVAGVLPFKVAKDMAAAAVRCIRKEIRDLYVNIQPVQEPKDQAFGNGNGIIIIAETSTGCLFAGSSLGKRGVNADKVGIEAAEMLLANLRHGGTVDEYLQDQLIVFMALANGVSRIKTGPVTLHTQTAIHFAEQIAKAKFIVKKSEDEEDAAKDTYIIECQGIGMTNPNL | 6.5.1.4 | null | negative regulation of optical nerve axon regeneration [GO:1905592]; RNA processing [GO:0006396] | nucleoplasm [GO:0005654]; nucleus [GO:0005634] | ATP binding [GO:0005524]; RNA binding [GO:0003723]; RNA-3'-phosphate cyclase activity [GO:0003963] | PF01137;PF05189; | 3.65.10.20;3.30.360.20; | RNA 3'-terminal cyclase family, Type 1 subfamily | null | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:9184239}. | CATALYTIC ACTIVITY: Reaction=a 3'-end 3'-phospho-ribonucleotide-RNA + ATP = a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + AMP + diphosphate; Xref=Rhea:RHEA:23976, Rhea:RHEA-COMP:10463, Rhea:RHEA-COMP:10464, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83062, ChEBI:CHEBI:83064, ChEBI:CHEBI:456215; EC=6.5.1.4; Evidence={ECO:0000269|PubMed:9184239}; | null | null | null | null | FUNCTION: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA (PubMed:9184239). The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product (PubMed:9184239). Likely functions in some aspects of cellular RNA processing (PubMed:25961792, PubMed:9184239). Function plays an important role in regulating axon regeneration by inhibiting central nervous system (CNS) axon regeneration following optic nerve injury (PubMed:25961792). {ECO:0000269|PubMed:25961792, ECO:0000269|PubMed:9184239}. | Homo sapiens (Human) |
O00443 | P3C2A_HUMAN | MAQISSNSGFKECPSSHPEPTRAKDVDKEEALQMEAEALAKLQKDRQVTDNQRGFELSSSTRKKAQVYNKQDYDLMVFPESDSQKRALDIDVEKLTQAELEKLLLDDSFETKKTPVLPVTPILSPSFSAQLYFRPTIQRGQWPPGLPGPSTYALPSIYPSTYSKQAAFQNGFNPRMPTFPSTEPIYLSLPGQSPYFSYPLTPATPFHPQGSLPIYRPVVSTDMAKLFDKIASTSEFLKNGKARTDLEITDSKVSNLQVSPKSEDISKFDWLDLDPLSKPKVDNVEVLDHEEEKNVSSLLAKDPWDAVLLEERSTANCHLERKVNGKSLSVATVTRSQSLNIRTTQLAKAQGHISQKDPNGTSSLPTGSSLLQEVEVQNEEMAAFCRSITKLKTKFPYTNHRTNPGYLLSPVTAQRNICGENASVKVSIDIEGFQLPVTFTCDVSSTVEIIIMQALCWVHDDLNQVDVGSYVLKVCGQEEVLQNNHCLGSHEHIQNCRKWDTEIRLQLLTFSAMCQNLARTAEDDETPVDLNKHLYQIEKPCKEAMTRHPVEELLDSYHNQVELALQIENQHRAVDQVIKAVRKICSALDGVETLAITESVKKLKRAVNLPRSKTADVTSLFGGEDTSRSSTRGSLNPENPVQVSINQLTAAIYDLLRLHANSGRSPTDCAQSSKSVKEAWTTTEQLQFTIFAAHGISSNWVSNYEKYYLICSLSHNGKDLFKPIQSKKVGTYKNFFYLIKWDELIIFPIQISQLPLESVLHLTLFGILNQSSGSSPDSNKQRKGPEALGKVSLPLFDFKRFLTCGTKLLYLWTSSHTNSVPGTVTKKGYVMERIVLQVDFPSPAFDIIYTTPQVDRSIIQQHNLETLENDIKGKLLDILHKDSSLGLSKEDKAFLWEKRYYCFKHPNCLPKILASAPNWKWVNLAKTYSLLHQWPALYPLIALELLDSKFADQEVRSLAVTWIEAISDDELTDLLPQFVQALKYEIYLNSSLVQFLLSRALGNIQIAHNLYWLLKDALHDVQFSTRYEHVLGALLSVGGKRLREELLKQTKLVQLLGGVAEKVRQASGSARQVVLQRSMERVQSFFQKNKCRLPLKPSLVAKELNIKSCSFFSSNAVPLKVTMVNADPMGEEINVMFKVGEDLRQDMLALQMIKIMDKIWLKEGLDLRMVIFKCLSTGRDRGMVELVPASDTLRKIQVEYGVTGSFKDKPLAEWLRKYNPSEEEYEKASENFIYSCAGCCVATYVLGICDRHNDNIMLRSTGHMFHIDFGKFLGHAQMFGSFKRDRAPFVLTSDMAYVINGGEKPTIRFQLFVDLCCQAYNLIRKQTNLFLNLLSLMIPSGLPELTSIQDLKYVRDALQPQTTDAEATIFFTRLIESSLGSIATKFNFFIHNLAQLRFSGLPSNDEPILSFSPKTYSFRQDGRIKEVSVFTYHKKYNPDKHYIYVVRILREGQIEPSFVFRTFDEFQELHNKLSIIFPLWKLPGFPNRMVLGRTHIKDVAAKRKIELNSYLQSLMNASTDVAECDLVCTFFHPLLRDEKAEGIARSADAGSFSPTPGQIGGAVKLSISYRNGTLFIMVMHIKDLVTEDGADPNPYVKTYLLPDNHKTSKRKTKISRKTRNPTFNEMLVYSGYSKETLRQRELQLSVLSAESLRENFFLGGVTLPLKDFNLSKETVKWYQLTAATYL | 2.7.1.137; 2.7.1.153; 2.7.1.154 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:9337861}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:9337861}; Note=Ca(2+) or Mg(2+). Mn(2+) cannot be used. {ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:9337861}; | cell migration [GO:0016477]; clathrin coat assembly [GO:0048268]; endocytosis [GO:0006897]; epidermal growth factor receptor signaling pathway [GO:0007173]; exocytosis [GO:0006887]; insulin receptor signaling pathway [GO:0008286]; membrane organization [GO:0061024]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol-3-phosphate biosynthetic process [GO:0036092]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of autophagy [GO:0010508]; positive regulation of cell migration involved in sprouting angiogenesis [GO:0090050]; vascular associated smooth muscle contraction [GO:0014829] | clathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; phosphatidylinositol 3-kinase complex [GO:0005942]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]; vesicle [GO:0031982] | 1-phosphatidylinositol-3-kinase activity [GO:0016303]; 1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity [GO:0046934]; 1-phosphatidylinositol-4-phosphate 3-kinase activity [GO:0035005]; ATP binding [GO:0005524]; clathrin binding [GO:0030276]; phosphatidylinositol binding [GO:0035091] | PF00168;PF00454;PF00792;PF00794;PF00613;PF00787; | 2.60.40.150;1.10.1070.11;1.25.40.70;3.30.1520.10; | PI3/PI4-kinase family | PTM: Phosphorylated upon insulin stimulation; which may lead to enzyme activation (By similarity). Phosphorylated on Ser-259 during mitosis and upon UV irradiation; which does not change enzymatic activity but leads to proteasomal degradation. Ser-259 phosphorylation may be mediated by CDK1 or JNK, depending on the physiological state of the cell. {ECO:0000250|UniProtKB:Q61194, ECO:0000269|PubMed:11606566, ECO:0000269|PubMed:12719431}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10766823, ECO:0000269|PubMed:11239472, ECO:0000269|PubMed:17038310}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:10766823, ECO:0000269|PubMed:11239472}. Nucleus {ECO:0000269|PubMed:11606566}. Cytoplasm {ECO:0000269|PubMed:11606566, ECO:0000269|PubMed:14563213}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:10766823, ECO:0000269|PubMed:11239472}. Note=Inserts preferentially into membranes containing PtdIns(4,5)P2 (PubMed:17038310). Associated with RNA-containing structures (PubMed:11606566). {ECO:0000269|PubMed:11606566, ECO:0000269|PubMed:17038310}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154; Evidence={ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11239472, ECO:0000269|PubMed:9337861}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18374; Evidence={ECO:0000305|PubMed:9337861}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.137; Evidence={ECO:0000269|PubMed:10766823, ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11239472, ECO:0000269|PubMed:9337861}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710; Evidence={ECO:0000305|PubMed:9337861}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + ADP + H(+); Xref=Rhea:RHEA:21292, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57836, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.153; Evidence={ECO:0000269|PubMed:11239472, ECO:0000269|PubMed:9337861}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21293; Evidence={ECO:0000305|PubMed:9337861}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=122 uM for PtdIns (in the absence of phosphatidylserine) {ECO:0000269|PubMed:9337861}; KM=64 uM for PtdIns (in the presence of phosphatidylserine) {ECO:0000269|PubMed:9337861}; KM=25 uM for PtdIns4P (in the presence of phosphatidylserine) {ECO:0000269|PubMed:9337861}; KM=15 uM for ATP (with PtdIns as substrate) (in the absence of phosphatidylserine) {ECO:0000269|PubMed:9337861}; KM=32 uM for ATP (with PtdIns as substrate) (in the presence of phosphatidylserine) {ECO:0000269|PubMed:9337861}; KM=54 uM for ATP (with PtdIns4P as substrate) (in the presence of phosphatidylserine) {ECO:0000269|PubMed:9337861}; Vmax=990 pmol/min/mg enzyme with PtdIns as substrate (in the absence of phosphatidylserine) {ECO:0000269|PubMed:9337861}; Vmax=200 pmol/min/mg enzyme with PtdIns as substrate (in the presence of phosphatidylserine) {ECO:0000269|PubMed:9337861}; Vmax=240 pmol/min/mg enzyme with PtdIns4P as substrate (in the presence of phosphatidylserine) {ECO:0000269|PubMed:9337861}; Vmax=6800 pmol/min/mg enzyme toward ATP with PtdIns as substrate (in the absence of phosphatidylserine) {ECO:0000269|PubMed:9337861}; Vmax=805 pmol/min/mg enzyme toward ATP with PtdIns as substrate (in the presence of phosphatidylserine) {ECO:0000269|PubMed:9337861}; Vmax=880 pmol/min/mg enzyme toward ATP with PtdIns4P as substrate (in the presence of phosphatidylserine) {ECO:0000269|PubMed:9337861}; Note=In the absence of the carrier phosphatidylserine, enzymatic kinetics toward PtdIns4P are non-linear.; | null | null | null | FUNCTION: Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers. Has a role in several intracellular trafficking events. Functions in insulin signaling and secretion. Required for translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane and glucose uptake in response to insulin-mediated RHOQ activation. Regulates insulin secretion through two different mechanisms: involved in glucose-induced insulin secretion downstream of insulin receptor in a pathway that involves AKT1 activation and TBC1D4/AS160 phosphorylation, and participates in the late step of insulin granule exocytosis probably in insulin granule fusion. Synthesizes PtdIns3P in response to insulin signaling. Functions in clathrin-coated endocytic vesicle formation and distribution. Regulates dynamin-independent endocytosis, probably by recruiting EEA1 to internalizing vesicles. In neurosecretory cells synthesizes PtdIns3P on large dense core vesicles. Participates in calcium induced contraction of vascular smooth muscle by regulating myosin light chain (MLC) phosphorylation through a mechanism involving Rho kinase-dependent phosphorylation of the MLCP-regulatory subunit MYPT1. May play a role in the EGF signaling cascade. May be involved in mitosis and UV-induced damage response. Required for maintenance of normal renal structure and function by supporting normal podocyte function. Involved in the regulation of ciliogenesis and trafficking of ciliary components (PubMed:31034465). {ECO:0000269|PubMed:10766823, ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11239472, ECO:0000269|PubMed:12719431, ECO:0000269|PubMed:16215232, ECO:0000269|PubMed:21081650, ECO:0000269|PubMed:31034465, ECO:0000269|PubMed:9337861}. | Homo sapiens (Human) |
O00444 | PLK4_HUMAN | MATCIGEKIEDFKVGNLLGKGSFAGVYRAESIHTGLEVAIKMIDKKAMYKAGMVQRVQNEVKIHCQLKHPSILELYNYFEDSNYVYLVLEMCHNGEMNRYLKNRVKPFSENEARHFMHQIITGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHEKHYTLCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLIGRPPFDTDTVKNTLNKVVLADYEMPSFLSIEAKDLIHQLLRRNPADRLSLSSVLDHPFMSRNSSTKSKDLGTVEDSIDSGHATISTAITASSSTSISGSLFDKRRLLIGQPLPNKMTVFPKNKSSTDFSSSGDGNSFYTQWGNQETSNSGRGRVIQDAEERPHSRYLRRAYSSDRSGTSNSQSQAKTYTMERCHSAEMLSVSKRSGGGENEERYSPTDNNANIFNFFKEKTSSSSGSFERPDNNQALSNHLCPGKTPFPFADPTPQTETVQQWFGNLQINAHLRKTTEYDSISPNRDFQGHPDLQKDTSKNAWTDTKVKKNSDASDNAHSVKQQNTMKYMTALHSKPEIIQQECVFGSDPLSEQSKTRGMEPPWGYQNRTLRSITSPLVAHRLKPIRQKTKKAVVSILDSEEVCVELVKEYASQEYVKEVLQISSDGNTITIYYPNGGRGFPLADRPPSPTDNISRYSFDNLPEKYWRKYQYASRFVQLVRSKSPKITYFTRYAKCILMENSPGADFEVWFYDGVKIHKTEDFIQVIEKTGKSYTLKSESEVNSLKEEIKMYMDHANEGHRICLALESIISEEERKTRSAPFFPIIIGRKPGSTSSPKALSPPPSVDSNYPTRERASFNRMVMHSAASPTQAPILNPSMVTNEGLGLTTTASGTDISSNSLKDCLPKSAQLLKSVFVKNVGWATQLTSGAVWVQFNDGSQLVVQAGVSSISYTSPNGQTTRYGENEKLPDYIKQKLQCLSSILLMFSNPTPNFH | 2.7.11.21 | null | centriole replication [GO:0007099]; cilium assembly [GO:0060271]; de novo centriole assembly involved in multi-ciliated epithelial cell differentiation [GO:0098535]; mitotic spindle organization [GO:0007052]; positive regulation of centriole replication [GO:0046601]; protein phosphorylation [GO:0006468]; trophoblast giant cell differentiation [GO:0060707] | centriole [GO:0005814]; centrosome [GO:0005813]; cleavage furrow [GO:0032154]; cytosol [GO:0005829]; deuterosome [GO:0098536]; kinetochore [GO:0000776]; nucleolus [GO:0005730]; procentriole [GO:0120098]; procentriole replication complex [GO:0120099]; spindle pole [GO:0000922]; XY body [GO:0001741] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069;PF18190;PF18409; | 2.40.50.930;3.30.1120.120;3.30.1120.130;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily | PTM: Acetylation by KAT2A and KAT2B impairs kinase activity by shifting the kinase to an inactive conformation. {ECO:0000269|PubMed:27796307}.; PTM: Ubiquitinated; leading to its degradation by the proteasome. {ECO:0000250}.; PTM: Tyrosine-phosphorylated by TEC. {ECO:0000269|PubMed:11489907}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:22020124, ECO:0000269|PubMed:27246242, ECO:0000269|PubMed:27796307}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q64702}. Cleavage furrow {ECO:0000250|UniProtKB:Q64702}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:30804208, ECO:0000269|PubMed:32433990}. Note=Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles. Associates with centrioles throughout the cell cycle. According to PubMed:16244668, it is not present at cleavage furrows. | 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=2.7.11.21; Evidence={ECO:0000269|PubMed:16244668, ECO:0000269|PubMed:18239451, ECO:0000269|PubMed:19164942}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.21; Evidence={ECO:0000269|PubMed:16244668, ECO:0000269|PubMed:18239451, ECO:0000269|PubMed:19164942}; | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as SASS6, CENPJ/CPAP, CCP110, CEP135 and gamma-tubulin. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Phosphorylates 'Ser-151' of FBXW5 during the G1/S transition, leading to inhibit FBXW5 ability to ubiquitinate SASS6. Its central role in centriole replication suggests a possible role in tumorigenesis, centrosome aberrations being frequently observed in tumors. Also involved in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles. Also involved in trophoblast differentiation by phosphorylating HAND1, leading to disrupt the interaction between HAND1 and MDFIC and activate HAND1. Phosphorylates CDC25C and CHEK2. Required for the recruitment of STIL to the centriole and for STIL-mediated centriole amplification (PubMed:22020124). Phosphorylates CEP131 at 'Ser-78' and PCM1 at 'Ser-372' which is essential for proper organization and integrity of centriolar satellites (PubMed:30804208). {ECO:0000269|PubMed:16244668, ECO:0000269|PubMed:16326102, ECO:0000269|PubMed:17681131, ECO:0000269|PubMed:18239451, ECO:0000269|PubMed:19164942, ECO:0000269|PubMed:21725316, ECO:0000269|PubMed:22020124, ECO:0000269|PubMed:27796307, ECO:0000269|PubMed:30804208}. | Homo sapiens (Human) |
O00445 | SYT5_HUMAN | MFPEPPTPGPPSPDTPPDSSRISHGPVPPWALATIVLVSGLLIFSCCFCLYRKSCRRRTGKKSQAQAQVHLQEVKGLGQSYIDKVQPEVEELEPAPSGPGQQVADKHELGRLQYSLDYDFQSGQLLVGILQAMGLAALDLGGSSDPYVRVYLLPDKRRRYETKVHRQTLNPHFGETFAFKVPYVELGGRVLVMAVYDFDRFSRNDAIGEVRVPMSSVDLGRPVQAWRELQAAPREEQEKLGDICFSLRYVPTAGKLTVIVLEAKNLKKMDVGGLSDPYVKVHLLQGGKKVRKKKTTIKKNTLNPYYNEAFSFEVPCDQVQKVQVELTVLDYDKLGKNEAIGRVAVGAAAGGAGLRHWADMLANPRRPIAQWHSLRPPDRVRLLPAP | null | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041, ECO:0000269|PubMed:27793683}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domains. {ECO:0000269|PubMed:15057824}; | calcium ion-regulated exocytosis of neurotransmitter [GO:0048791]; cellular response to calcium ion [GO:0071277]; chemical synaptic transmission [GO:0007268]; regulation of calcium ion-dependent exocytosis [GO:0017158]; regulation of dopamine secretion [GO:0014059]; synaptic vesicle endocytosis [GO:0048488] | axon [GO:0030424]; dense core granule [GO:0031045]; exocytic vesicle [GO:0070382]; neuronal cell body [GO:0043025]; neuronal dense core vesicle membrane [GO:0099012]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; proximal neuron projection [GO:1990769]; recycling endosome membrane [GO:0055038]; synaptic vesicle membrane [GO:0030672] | calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; clathrin binding [GO:0030276]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylserine binding [GO:0001786]; protein heterodimerization activity [GO:0046982]; syntaxin binding [GO:0019905] | PF00168; | 2.60.40.150; | Synaptotagmin family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Recycling endosome membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=In mast cells, localizes to the endocytic recycling compartment. {ECO:0000250}. | null | null | null | null | null | FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Regulates the Ca(2+)-dependent secretion of norepinephrine in PC12 cells. Required for export from the endocytic recycling compartment to the cell surface (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
O00451 | GFRA2_HUMAN | MILANVFCLFFFLDETLRSLASPSSLQGPELHGWRPPVDCVRANELCAAESNCSSRYRTLRQCLAGRDRNTMLANKECQAALEVLQESPLYDCRCKRGMKKELQCLQIYWSIHLGLTEGEEFYEASPYEPVTSRLSDIFRLASIFSGTGADPVVSAKSNHCLDAAKACNLNDNCKKLRSSYISICNREISPTERCNRRKCHKALRQFFDRVPSEYTYRMLFCSCQDQACAERRRQTILPSCSYEDKEKPNCLDLRGVCRTDHLCRSRLADFHANCRASYQTVTSCPADNYQACLGSYAGMIGFDMTPNYVDSSPTGIVVSPWCSCRGSGNMEEECEKFLRDFTENPCLRNAIQAFGNGTDVNVSPKGPSFQATQAPRVEKTPSLPDDLSDSTSLGTSVITTCTSVQEQGLKANNSKELSMCFTELTTNIIPGSNKVIKPNSGPSRARPSAALTVLSVLMLKLAL | null | null | glial cell-derived neurotrophic factor receptor signaling pathway [GO:0035860]; nervous system development [GO:0007399]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | external side of plasma membrane [GO:0009897]; extrinsic component of membrane [GO:0019898]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | glial cell-derived neurotrophic factor receptor activity [GO:0016167]; heparan sulfate binding [GO:1904399] | PF02351; | 1.10.220.110; | GDNFR family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O08842}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:O08842}. | null | null | null | null | null | FUNCTION: Receptor for neurturin (NRTN), a growth factor that supports the survival of sympathetic neurons (PubMed:10829012, PubMed:29414779, PubMed:31535977, PubMed:9182803). NRTN-binding leads to autophosphorylation and activation of the RET receptor (PubMed:31535977). Also able to mediate GDNF signaling through the RET tyrosine kinase receptor (PubMed:9182803). {ECO:0000269|PubMed:10829012, ECO:0000269|PubMed:29414779, ECO:0000269|PubMed:31535977, ECO:0000269|PubMed:9182803}.; FUNCTION: [Isoform 2]: Participates in NRTN-induced 'Ser-727' phosphorylation of STAT3. {ECO:0000250|UniProtKB:O08842}. | Homo sapiens (Human) |
O00453 | LST1_HUMAN | MLSRNDDICIYGGLGLGGLLLLAVVLLSACLCWLHRRVKRLERSWAQGSSEQELHYASLQRLPVPSSEGPDLRGRDKRGTKEDPRADYACIAENKPT | null | null | anatomical structure morphogenesis [GO:0009653]; cell morphogenesis [GO:0000902]; dendrite development [GO:0016358]; immune response [GO:0006955]; negative regulation of lymphocyte proliferation [GO:0050672]; regulation of cell shape [GO:0008360] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; plasma membrane [GO:0005886] | null | PF05083; | null | LST1 family | null | SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. Golgi apparatus membrane; Single-pass membrane protein. Endomembrane system; Single-pass membrane protein. Note=Also detected in a perinuclear region corresponding to the localization of the Golgi apparatus and throughout the cytoplasm. | null | null | null | null | null | FUNCTION: Possible role in modulating immune responses. Induces morphological changes including production of filopodia and microspikes when overexpressed in a variety of cell types and may be involved in dendritic cell maturation. Isoform 1 and isoform 2 have an inhibitory effect on lymphocyte proliferation. {ECO:0000269|PubMed:10706707, ECO:0000269|PubMed:11478849}. | Homo sapiens (Human) |
O00459 | P85B_HUMAN | MAGPEGFQYRALYPFRRERPEDLELLPGDVLVVSRAALQALGVAEGGERCPQSVGWMPGLNERTRQRGDFPGTYVEFLGPVALARPGPRPRGPRPLPARPRDGAPEPGLTLPDLPEQFSPPDVAPPLLVKLVEAIERTGLDSESHYRPELPAPRTDWSLSDVDQWDTAALADGIKSFLLALPAPLVTPEASAEARRALREAAGPVGPALEPPTLPLHRALTLRFLLQHLGRVASRAPALGPAVRALGATFGPLLLRAPPPPSSPPPGGAPDGSEPSPDFPALLVEKLLQEHLEEQEVAPPALPPKPPKAKPASTVLANGGSPPSLQDAEWYWGDISREEVNEKLRDTPDGTFLVRDASSKIQGEYTLTLRKGGNNKLIKVFHRDGHYGFSEPLTFCSVVDLINHYRHESLAQYNAKLDTRLLYPVSKYQQDQIVKEDSVEAVGAQLKVYHQQYQDKSREYDQLYEEYTRTSQELQMKRTAIEAFNETIKIFEEQGQTQEKCSKEYLERFRREGNEKEMQRILLNSERLKSRIAEIHESRTKLEQQLRAQASDNREIDKRMNSLKPDLMQLRKIRDQYLVWLTQKGARQKKINEWLGIKNETEDQYALMEDEDDLPHHEERTWYVGKINRTQAEEMLSGKRDGTFLIRESSQRGCYACSVVVDGDTKHCVIYRTATGFGFAEPYNLYGSLKELVLHYQHASLVQHNDALTVTLAHPVRAPGPGPPPAAR | null | null | B cell differentiation [GO:0030183]; cellular response to insulin stimulus [GO:0032869]; immune response [GO:0006955]; insulin receptor signaling pathway [GO:0008286]; intracellular glucose homeostasis [GO:0001678]; negative regulation of MAPK cascade [GO:0043409]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; positive regulation of cell adhesion [GO:0045785]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein transport [GO:0015031]; regulation of actin filament polymerization [GO:0030833]; regulation of autophagy [GO:0010506]; regulation of protein localization to plasma membrane [GO:1903076]; regulation of stress fiber assembly [GO:0051492]; response to endoplasmic reticulum stress [GO:0034976]; T cell differentiation [GO:0030217] | cytosol [GO:0005829]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; phosphatidylinositol 3-kinase complex [GO:0005942]; phosphatidylinositol 3-kinase complex, class IA [GO:0005943] | 1-phosphatidylinositol-3-kinase regulator activity [GO:0046935]; phosphatidylinositol 3-kinase regulatory subunit binding [GO:0036312]; phosphotyrosine residue binding [GO:0001784]; protein heterodimerization activity [GO:0046982]; protein phosphatase binding [GO:0019903]; receptor tyrosine kinase binding [GO:0030971] | PF16454;PF00620;PF00017; | 1.10.287.1490;1.10.555.10;3.30.505.10;2.30.30.40; | PI3K p85 subunit family | PTM: Phosphorylated in response to signaling from activated receptor-type protein kinases (PubMed:19690332, PubMed:20068231). Dephosphorylated by PTPRJ (PubMed:18348712). Dephosphorylated at Tyr-655 by PTPN13. Phosphorylation of Tyr-655 impairs while its dephosphorylation promotes interaction with FBXL2 and SCF(FBXL2)-mediated polyubiquitination (PubMed:23604317). {ECO:0000269|PubMed:18348712, ECO:0000269|PubMed:23604317}.; PTM: Ubiquitinated. Polyubiquitination by the SCF(FBXL2) complex probably promotes proteasomal degradation of PIK3R2. {ECO:0000303|PubMed:23604317}. | null | null | null | null | null | null | FUNCTION: Regulatory subunit of phosphoinositide-3-kinase (PI3K), a kinase that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Indirectly regulates autophagy (PubMed:23604317). Promotes nuclear translocation of XBP1 isoform 2 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement (By similarity). {ECO:0000250|UniProtKB:O08908, ECO:0000269|PubMed:23604317}. | Homo sapiens (Human) |
O00461 | GOLI4_HUMAN | MGNGMCSRKQKRIFQTLLLLTVVFGFLYGAMLYYELQTQLRKAEAVALKYQQHQESLSAQLQVVYEHRSRLEKSLQKERLEHKKAKEDFLVYKLEAQETLNKGRQDSNSRYSALNVQHQMLKSQHEELKKQHSDLEEEHRKQGEDFSRTFNDHKQKYLQLQQEKEQELSKLKETVYNLREENRQLRKAHQDIHTQLQDVKQQHKNLLSEHEQLVVTLEDHKSALAAAQTQVAEYKQLKDTLNRIPSLRKPDPAEQQNVTQVAHSPQGYNTAREKPTREVQEVSRNNDVWQNHEAVPGRAEDTKLYAPTHKEAEFQAPPEPIQQEVERREPEEHQVEEEHRKALEEEEMEQVGQAEHLEEEHDPSPEEQDREWKEQHEQREAANLLEGHARAEVYPSAKPMIKFQSPYEEQLEQQRLAVQQVEEAQQLREHQEALHQQRLQGHLLRQQEQQQQQVAREMALQRQAELEEGRPQHQEQLRQQAHYDAMDNDIVQGAEDQGIQGEEGAYERDNQHQDEAEGDPGNRHEPREQGPREADPESEADRAAVEDINPADDPNNQGEDEFEEAEQVREENLPDENEEQKQSNQKQENTEVEEHLVMAGNPDQQEDNVDEQYQEEAEEEVQEDLTEEKKRELEHNAEETYGENDENTDDKNNDGEEQEVRDDNRPKGREEHYEEEEEEEEDGAAVAEKSHRRAEM | null | null | null | cis-Golgi network [GO:0005801]; endocytic vesicle [GO:0030139]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; Golgi lumen [GO:0005796]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; transport vesicle [GO:0030133] | null | null | null | GOLIM4 family | PTM: Phosphorylated probably by c-AMP-dependent kinases in its lumenal part. {ECO:0000269|PubMed:9201717}.; PTM: O-glycosylated; modified by sialic acid residues. {ECO:0000250}.; PTM: N-glycosylated; N-glycans are probably of the complex type and modified by sialic acid residues. {ECO:0000269|PubMed:9201717}. | SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Endosome membrane; Single-pass type II membrane protein. Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Localizes to cis and medial Golgi cisternae. Probably cycles between early Golgi and distal compartments like endosome. | null | null | null | null | null | FUNCTION: Plays a role in endosome to Golgi protein trafficking; mediates protein transport along the late endosome-bypass pathway from the early endosome to the Golgi. {ECO:0000269|PubMed:15331763}. | Homo sapiens (Human) |
O00462 | MANBA_HUMAN | MRLHLLLLLALCGAGTTAAELSYSLRGNWSICNGNGSLELPGAVPGCVHSALFQQGLIQDSYYRFNDLNYRWVSLDNWTYSKEFKIPFEISKWQKVNLILEGVDTVSKILFNEVTIGETDNMFNRYSFDITNVVRDVNSIELRFQSAVLYAAQQSKAHTRYQVPPDCPPLVQKGECHVNFVRKEQCSFSWDWGPSFPTQGIWKDVRIEAYNICHLNYFTFSPIYDKSAQEWNLEIESTFDVVSSKPVGGQVIVAIPKLQTQQTYSIELQPGKRIVELFVNISKNITVETWWPHGHGNQTGYNMTVLFELDGGLNIEKSAKVYFRTVELIEEPIKGSPGLSFYFKINGFPIFLKGSNWIPADSFQDRVTSELLRLLLQSVVDANMNTLRVWGGGIYEQDEFYELCDELGIMVWQDFMFACALYPTDQGFLDSVTAEVAYQIKRLKSHPSIIIWSGNNENEEALMMNWYHISFTDRPIYIKDYVTLYVKNIRELVLAGDKSRPFITSSPTNGAETVAEAWVSQNPNSNYFGDVHFYDYISDCWNWKVFPKARFASEYGYQSWPSFSTLEKVSSTEDWSFNSKFSLHRQHHEGGNKQMLYQAGLHFKLPQSTDPLRTFKDTIYLTQVMQAQCVKTETEFYRRSRSEIVDQQGHTMGALYWQLNDIWQAPSWASLEYGGKWKMLHYFAQNFFAPLLPVGFENENTFYIYGVSDLHSDYSMTLSVRVHTWSSLEPVCSRVTERFVMKGGEAVCLYEEPVSELLRRCGNCTRESCVVSFYLSADHELLSPTNYHFLSSPKEAVGLCKAQITAIISQQGDIFVFDLETSAVAPFVWLDVGSIPGRFSDNGFLMTEKTRTILFYPWEPTSKNELEQSFHVTSLTDIY | 3.2.1.25 | null | glycoprotein catabolic process [GO:0006516]; oligosaccharide catabolic process [GO:0009313]; protein modification process [GO:0036211] | azurophil granule membrane [GO:0035577]; lysosomal lumen [GO:0043202]; plasma membrane [GO:0005886] | beta-mannosidase activity [GO:0004567]; mannose binding [GO:0005537] | PF02836;PF17753;PF17786; | 2.60.120.260;3.20.20.80;2.60.40.10; | Glycosyl hydrolase 2 family | null | SUBCELLULAR LOCATION: Lysosome {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.; EC=3.2.1.25; Evidence={ECO:0000305|PubMed:12890191, ECO:0000305|PubMed:16904924, ECO:0000305|PubMed:18565776, ECO:0000305|PubMed:30552791}; | null | PATHWAY: Glycan metabolism; N-glycan degradation. {ECO:0000269|PubMed:12890191, ECO:0000269|PubMed:30552791}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5-5. {ECO:0000269|PubMed:30552791}; | null | FUNCTION: Exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of all N-linked glycoprotein oligosaccharides. {ECO:0000305|PubMed:12890191, ECO:0000305|PubMed:30552791}. | Homo sapiens (Human) |
O00463 | TRAF5_HUMAN | MAYSEEHKGMPCGFIRQNSGNSISLDFEPSIEYQFVERLEERYKCAFCHSVLHNPHQTGCGHRFCQHCILSLRELNTVPICPVDKEVIKSQEVFKDNCCKREVLNLYVYCSNAPGCNAKVILGRYQDHLQQCLFQPVQCSNEKCREPVLRKDLKEHLSASCQFRKEKCLYCKKDVVVINLQNHEENLCPEYPVFCPNNCAKIILKTEVDEHLAVCPEAEQDCPFKHYGCAVTDKRRNLQQHEHSALREHMRLVLEKNVQLEEQISDLHKSLEQKESKIQQLAETIKKLEKEFKQFAQLFGKNGSFLPNIQVFASHIDKSAWLEAQVHQLLQMVNQQQNKFDLRPLMEAVDTVKQKITLLENNDQRLAVLEEETNKHDTHINIHKAQLSKNEERFKLLEGTCYNGKLIWKVTDYKMKKREAVDGHTVSIFSQSFYTSRCGYRLCARAYLNGDGSGRGSHLSLYFVVMRGEFDSLLQWPFRQRVTLMLLDQSGKKNIMETFKPDPNSSSFKRPDGEMNIASGCPRFVAHSVLENAKNAYIKDDTLFLKVAVDLTDLEDL | null | null | apoptotic process [GO:0006915]; interleukin-17-mediated signaling pathway [GO:0097400]; mRNA stabilization [GO:0048255]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of DNA-binding transcription factor activity [GO:0051091]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; protein K63-linked ubiquitination [GO:0070534]; regulation of apoptotic process [GO:0042981]; regulation of canonical NF-kappaB signal transduction [GO:0043122]; signal transduction [GO:0007165]; signal transduction involved in regulation of gene expression [GO:0023019]; tumor necrosis factor-mediated signaling pathway [GO:0033209] | CD40 receptor complex [GO:0035631]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829] | identical protein binding [GO:0042802]; thioesterase binding [GO:0031996]; tumor necrosis factor receptor binding [GO:0005164]; ubiquitin protein ligase binding [GO:0031625]; zinc ion binding [GO:0008270] | PF21355;PF21363;PF02176; | 3.30.40.10; | TNF receptor-associated factor family, A subfamily | PTM: Ubiquitinated at Lys-318 by the SCF(FBXL2) complex, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:P70191}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:15121867}. Cytoplasm, cytosol {ECO:0000269|PubMed:15121867}. | null | null | null | null | null | FUNCTION: Adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases. Mediates activation of NF-kappa-B and probably JNK. Seems to be involved in apoptosis. Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR. {ECO:0000269|PubMed:15121867}. | Homo sapiens (Human) |
O00468 | AGRIN_HUMAN | MAGRSHPGPLRPLLPLLVVAACVLPGAGGTCPERALERREEEANVVLTGTVEEILNVDPVQHTYSCKVRVWRYLKGKDLVARESLLDGGNKVVISGFGDPLICDNQVSTGDTRIFFVNPAPPYLWPAHKNELMLNSSLMRITLRNLEEVEFCVEDKPGTHFTPVPPTPPDACRGMLCGFGAVCEPNAEGPGRASCVCKKSPCPSVVAPVCGSDASTYSNECELQRAQCSQQRRIRLLSRGPCGSRDPCSNVTCSFGSTCARSADGLTASCLCPATCRGAPEGTVCGSDGADYPGECQLLRRACARQENVFKKFDGPCDPCQGALPDPSRSCRVNPRTRRPEMLLRPESCPARQAPVCGDDGVTYENDCVMGRSGAARGLLLQKVRSGQCQGRDQCPEPCRFNAVCLSRRGRPRCSCDRVTCDGAYRPVCAQDGRTYDSDCWRQQAECRQQRAIPSKHQGPCDQAPSPCLGVQCAFGATCAVKNGQAACECLQACSSLYDPVCGSDGVTYGSACELEATACTLGREIQVARKGPCDRCGQCRFGALCEAETGRCVCPSECVALAQPVCGSDGHTYPSECMLHVHACTHQISLHVASAGPCETCGDAVCAFGAVCSAGQCVCPRCEHPPPGPVCGSDGVTYGSACELREAACLQQTQIEEARAGPCEQAECGSGGSGSGEDGDCEQELCRQRGGIWDEDSEDGPCVCDFSCQSVPGSPVCGSDGVTYSTECELKKARCESQRGLYVAAQGACRGPTFAPLPPVAPLHCAQTPYGCCQDNITAARGVGLAGCPSACQCNPHGSYGGTCDPATGQCSCRPGVGGLRCDRCEPGFWNFRGIVTDGRSGCTPCSCDPQGAVRDDCEQMTGLCSCKPGVAGPKCGQCPDGRALGPAGCEADASAPATCAEMRCEFGARCVEESGSAHCVCPMLTCPEANATKVCGSDGVTYGNECQLKTIACRQGLQISIQSLGPCQEAVAPSTHPTSASVTVTTPGLLLSQALPAPPGALPLAPSSTAHSQTTPPPSSRPRTTASVPRTTVWPVLTVPPTAPSPAPSLVASAFGESGSTDGSSDEELSGDQEASGGGSGGLEPLEGSSVATPGPPVERASCYNSALGCCSDGKTPSLDAEGSNCPATKVFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFRSVRLRDLGPGKSVRAIVDVHFDPTTAFRAPDVARALLRQIQVSRRRSLGVRRPLQEHVRFMDFDWFPAFITGATSGAIAAGATARATTASRLPSSAVTPRAPHPSHTSQPVAKTTAAPTTRRPPTTAPSRVPGRRPPAPQQPPKPCDSQPCFHGGTCQDWALGGGFTCSCPAGRGGAVCEKVLGAPVPAFEGRSFLAFPTLRAYHTLRLALEFRALEPQGLLLYNGNARGKDFLALALLDGRVQLRFDTGSGPAVLTSAVPVEPGQWHRLELSRHWRRGTLSVDGETPVLGESPSGTDGLNLDTDLFVGGVPEDQAAVALERTFVGAGLRGCIRLLDVNNQRLELGIGPGAATRGSGVGECGDHPCLPNPCHGGAPCQNLEAGRFHCQCPPGRVGPTCADEKSPCQPNPCHGAAPCRVLPEGGAQCECPLGREGTFCQTASGQDGSGPFLADFNGFSHLELRGLHTFARDLGEKMALEVVFLARGPSGLLLYNGQKTDGKGDFVSLALRDRRLEFRYDLGKGAAVIRSREPVTLGAWTRVSLERNGRKGALRVGDGPRVLGESPKSRKVPHTVLNLKEPLYVGGAPDFSKLARAAAVSSGFDGAIQLVSLGGRQLLTPEHVLRQVDVTSFAGHPCTRASGHPCLNGASCVPREAAYVCLCPGGFSGPHCEKGLVEKSAGDVDTLAFDGRTFVEYLNAVTESELANEIPVPETLDSGALHSEKALQSNHFELSLRTEATQGLVLWSGKATERADYVALAIVDGHLQLSYNLGSQPVVLRSTVPVNTNRWLRVVAHREQREGSLQVGNEAPVTGSSPLGATQLDTDGALWLGGLPELPVGPALPKAYGTGFVGCLRDVVVGRHPLHLLEDAVTKPELRPCPTP | null | null | clustering of voltage-gated sodium channels [GO:0045162]; G protein-coupled acetylcholine receptor signaling pathway [GO:0007213]; neuromuscular junction development [GO:0007528]; positive regulation of filopodium assembly [GO:0051491]; positive regulation of GTPase activity [GO:0043547]; positive regulation of synaptic assembly at neuromuscular junction [GO:0045887]; positive regulation of transcription by RNA polymerase II [GO:0045944]; receptor clustering [GO:0043113]; signal transduction [GO:0007165]; synapse organization [GO:0050808] | basement membrane [GO:0005604]; collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; Golgi lumen [GO:0005796]; lysosomal lumen [GO:0043202]; plasma membrane [GO:0005886]; synapse [GO:0045202] | calcium ion binding [GO:0005509]; chondroitin sulfate binding [GO:0035374]; dystroglycan binding [GO:0002162]; heparan sulfate proteoglycan binding [GO:0043395]; laminin binding [GO:0043236]; sialic acid binding [GO:0033691]; structural constituent of cytoskeleton [GO:0005200] | PF00008;PF00050;PF07648;PF00053;PF00054;PF03146;PF01390; | 2.40.50.120;2.60.120.200;3.30.60.30;2.10.25.10;3.30.70.960; | null | PTM: Contains heparan and chondroitin sulfate chains and alpha-dystroglycan as well as N-linked and O-linked oligosaccharides. Glycosaminoglycans (GAGs), present in the N-terminal 110 kDa fragment, are required for induction of filopodia in hippocampal neurons. The first cluster (Gly/Ser-rich) for GAG attachment contains heparan sulfate (HS) chains and the second cluster (Ser/Thr-rich), contains chondroitin sulfate (CS) chains. Heparin and heparin sulfate binding in the G3 domain is independent of calcium ions. Binds heparin with a stoichiometry of 2:1. Binds sialic acid with a stoichiometry of 1:1 and binding requires calcium ions (By similarity). {ECO:0000250}.; PTM: At synaptic junctions, cleaved at two conserved sites, alpha and beta, by neurotrypsin. Cleavage at the alpha-site produces the agrin N-terminal 110-kDa subunit and the agrin C-terminal 110-kDa subunit. Further cleavage of agrin C-terminal 110-kDa subunit at the beta site produces the C-terminal fragments, agrin C-terminal 90 kDa fragment and agrin C-terminal 22 kDa fragment. Excessive cleavage at the beta-site releases large amounts of the agrin C-terminal 22 kDa fragment leading to destabilization at the neuromuscular junction (NMJ). | SUBCELLULAR LOCATION: [Isoform 1]: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:20551380}. Note=Synaptic basal lamina at the neuromuscular junction. {ECO:0000250|UniProtKB:P31696}.; SUBCELLULAR LOCATION: [Isoform 2]: Synapse {ECO:0000250|UniProtKB:A2ASQ1}. Cell membrane {ECO:0000250|UniProtKB:A2ASQ1}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:A2ASQ1}. | null | null | null | null | null | FUNCTION: [Isoform 1]: Heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. Component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Calcium ions are required for maximal AChR clustering. AGRN function in neurons is highly regulated by alternative splicing, glycan binding and proteolytic processing. Modulates calcium ion homeostasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha(3)-subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses. This secreted isoform forms a bridge, after release from motor neurons, to basal lamina through binding laminin via the NtA domain.; FUNCTION: [Isoform 2]: Transmembrane form that is the predominate form in neurons of the brain, induces dendritic filopodia and synapse formation in mature hippocampal neurons in large part due to the attached glycosaminoglycan chains and the action of Rho-family GTPases.; FUNCTION: Isoform 1, isoform 4 and isoform 5: neuron-specific (z+) isoforms that contain C-terminal insertions of 8-19 AA are potent activators of AChR clustering. Isoform 5, agrin (z+8), containing the 8-AA insert, forms a receptor complex in myotubules containing the neuronal AGRN, the muscle-specific kinase MUSK and LRP4, a member of the LDL receptor family. The splicing factors, NOVA1 and NOVA2, regulate AGRN splicing and production of the 'z' isoforms.; FUNCTION: Isoform 3 and isoform 6: lack any 'z' insert, are muscle-specific and may be involved in endothelial cell differentiation.; FUNCTION: [Agrin N-terminal 110 kDa subunit]: Is involved in regulation of neurite outgrowth probably due to the presence of the glycosaminoglcan (GAG) side chains of heparan and chondroitin sulfate attached to the Ser/Thr- and Gly/Ser-rich regions. Also involved in modulation of growth factor signaling (By similarity). {ECO:0000250, ECO:0000269|PubMed:19631309, ECO:0000269|PubMed:21969364}.; FUNCTION: [Agrin C-terminal 22 kDa fragment]: This released fragment is important for agrin signaling and to exert a maximal dendritic filopodia-inducing effect. All 'z' splice variants (z+) of this fragment also show an increase in the number of filopodia. | Homo sapiens (Human) |
O00469 | PLOD2_HUMAN | MGGCTVKPQLLLLALVLHPWNPCLGADSEKPSSIPTDKLLVITVATKESDGFHRFMQSAKYFNYTVKVLGQGEEWRGGDGINSIGGGQKVRLMKEVMEHYADQDDLVVMFTECFDVIFAGGPEEVLKKFQKANHKVVFAADGILWPDKRLADKYPVVHIGKRYLNSGGFIGYAPYVNRIVQQWNLQDNDDDQLFYTKVYIDPLKREAINITLDHKCKIFQTLNGAVDEVVLKFENGKARAKNTFYETLPVAINGNGPTKILLNYFGNYVPNSWTQDNGCTLCEFDTVDLSAVDVHPNVSIGVFIEQPTPFLPRFLDILLTLDYPKEALKLFIHNKEVYHEKDIKVFFDKAKHEIKTIKIVGPEENLSQAEARNMGMDFCRQDEKCDYYFSVDADVVLTNPRTLKILIEQNRKIIAPLVTRHGKLWSNFWGALSPDGYYARSEDYVDIVQGNRVGVWNVPYMANVYLIKGKTLRSEMNERNYFVRDKLDPDMALCRNAREMGVFMYISNRHEFGRLLSTANYNTSHYNNDLWQIFENPVDWKEKYINRDYSKIFTENIVEQPCPDVFWFPIFSEKACDELVEEMEHYGKWSGGKHHDSRISGGYENVPTDDIHMKQVDLENVWLHFIREFIAPVTLKVFAGYYTKGFALLNFVVKYSPERQRSLRPHHDASTFTINIALNNVGEDFQGGGCKFLRYNCSIESPRKGWSFMHPGRLTHLHEGLPVKNGTRYIAVSFIDP | 1.14.11.4 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:P24802}; COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250|UniProtKB:P24802}; | hydroxylysine biosynthetic process [GO:0046947]; peptidyl-lysine hydroxylation [GO:0017185]; protein modification process [GO:0036211]; response to hypoxia [GO:0001666] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; rough endoplasmic reticulum membrane [GO:0030867] | iron ion binding [GO:0005506]; L-ascorbic acid binding [GO:0031418]; procollagen-lysine 5-dioxygenase activity [GO:0008475] | PF03171; | 2.60.120.620; | null | null | SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-lysyl-[collagen] + O2 = (5R)-5-hydroxy-L-lysyl-[collagen] + CO2 + succinate; Xref=Rhea:RHEA:16569, Rhea:RHEA-COMP:12751, Rhea:RHEA-COMP:12752, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, ChEBI:CHEBI:133442; EC=1.14.11.4; Evidence={ECO:0000250|UniProtKB:P24802}; | null | null | null | null | FUNCTION: Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links. {ECO:0000250|UniProtKB:P24802}. | Homo sapiens (Human) |
O00470 | MEIS1_HUMAN | MAQRYDDLPHYGGMDGVGIPSTMYGDPHAARSMQPVHHLNHGPPLHSHQYPHTAHTNAMAPSMGSSVNDALKRDKDAIYGHPLFPLLALIFEKCELATCTPREPGVAGGDVCSSESFNEDIAVFAKQIRAEKPLFSSNPELDNLMIQAIQVLRFHLLELEKVHELCDNFCHRYISCLKGKMPIDLVIDDREGGSKSDSEDITRSANLTDQPSWNRDHDDTASTRSGGTPGPSSGGHTSHSGDNSSEQGDGLDNSVASPSTGDDDDPDKDKKRHKKRGIFPKVATNIMRAWLFQHLTHPYPSEEQKKQLAQDTGLTILQVNNWFINARRRIVQPMIDQSNRAVSQGTPYNPDGQPMGGFVMDGQQHMGIRAPGPMSGMGMNMGMEGQWHYM | null | null | angiogenesis [GO:0001525]; animal organ morphogenesis [GO:0009887]; brain development [GO:0007420]; cell growth involved in cardiac muscle cell development [GO:0061049]; definitive hemopoiesis [GO:0060216]; embryonic pattern specification [GO:0009880]; eye development [GO:0001654]; hemopoiesis [GO:0030097]; lens morphogenesis in camera-type eye [GO:0002089]; locomotory behavior [GO:0007626]; megakaryocyte development [GO:0035855]; negative regulation of myeloid cell differentiation [GO:0045638]; negative regulation of neuron differentiation [GO:0045665]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of transcription by RNA polymerase II [GO:0045944] | chromatin [GO:0000785]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF05920;PF16493; | 1.10.10.60; | TALE/MEIS homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. | null | null | null | null | null | FUNCTION: Acts as a transcriptional regulator of PAX6. Acts as a transcriptional activator of PF4 in complex with PBX1 or PBX2. Required for hematopoiesis, megakaryocyte lineage development and vascular patterning. May function as a cofactor for HOXA7 and HOXA9 in the induction of myeloid leukemias. {ECO:0000269|PubMed:12609849}. | Homo sapiens (Human) |
O00471 | EXOC5_HUMAN | MATTAELFEEPFVADEYIERLVWRTPGGGSRGGPEAFDPKRLLEEFVNHIQELQIMDERIQRKVEKLEQQCQKEAKEFAKKVQELQKSNQVAFQHFQELDEHISYVATKVCHLGDQLEGVNTPRQRAVEAQKLMKYFNEFLDGELKSDVFTNSEKIKEAADIIQKLHLIAQELPFDRFSEVKSKIASKYHDLECQLIQEFTSAQRRGEISRMREVAAVLLHFKGYSHCVDVYIKQCQEGAYLRNDIFEDAGILCQRVNKQVGDIFSNPETVLAKLIQNVFEIKLQSFVKEQLEECRKSDAEQYLKNLYDLYTRTTNLSSKLMEFNLGTDKQTFLSKLIKSIFISYLENYIEVETGYLKSRSAMILQRYYDSKNHQKRSIGTGGIQDLKERIRQRTNLPLGPSIDTHGETFLSQEVVVNLLQETKQAFERCHRLSDPSDLPRNAFRIFTILVEFLCIEHIDYALETGLAGIPSSDSRNANLYFLDVVQQANTIFHLFDKQFNDHLMPLISSSPKLSECLQKKKEIIEQMEMKLDTGIDRTLNCMIGQMKHILAAEQKKTDFKPEDENNVLIQYTNACVKVCAYVRKQVEKIKNSMDGKNVDTVLMELGVRFHRLIYEHLQQYSYSCMGGMLAICDVAEYRKCAKDFKIPMVLHLFDTLHALCNLLVVAPDNLKQVCSGEQLANLDKNILHSFVQLRADYRSARLARHFS | null | null | epithelial cell apoptotic process [GO:1904019]; establishment of planar polarity [GO:0001736]; exocytosis [GO:0006887]; Golgi to plasma membrane transport [GO:0006893]; membrane fission [GO:0090148]; mitotic cytokinesis [GO:0000281]; non-motile cilium assembly [GO:1905515]; post-Golgi vesicle-mediated transport [GO:0006892]; protein localization to plasma membrane [GO:0072659]; protein transport [GO:0015031]; vesicle docking involved in exocytosis [GO:0006904]; vesicle tethering involved in exocytosis [GO:0090522] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; exocyst [GO:0000145]; midbody [GO:0030496] | small GTPase binding [GO:0031267] | PF07393;PF20667; | null | SEC10 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9119050}. Midbody {ECO:0000269|PubMed:18756269}. Note=Localization at the midbody requires the presence of RALA, EXOC2 and EXOC3. {ECO:0000269|PubMed:18756269}. | null | null | null | null | null | FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. | Homo sapiens (Human) |
O00472 | ELL2_HUMAN | MAAGGTGGLREEQRYGLSCGRLGQDNITVLHVKLTETAIRALETYQSHKNLIPFRPSIQFQGLHGLVKIPKNDPLNEVHNFNFYLSNVGKDNPQGSFDCIQQTFSSSGASQLNCLGFIQDKITVCATNDSYQMTRERMTQAEEESRNRSTKVIKPGGPYVGKRVQIRKAPQAVSDTVPERKRSTPMNPANTIRKTHSSSTISQRPYRDRVIHLLALKAYKKPELLARLQKDGVNQKDKNSLGAILQQVANLNSKDLSYTLKDYVFKELQRDWPGYSEIDRRSLESVLSRKLNPSQNAAGTSRSESPVCSSRDAVSSPQKRLLDSEFIDPLMNKKARISHLTNRVPPTLNGHLNPTSEKSAAGLPLPPAAAAIPTPPPLPSTYLPISHPPQIVNSNSNSPSTPEGRGTQDLPVDSFSQNDSIYEDQQDKYTSRTSLETLPPGSVLLKCPKPMEENHSMSHKKSKKKSKKHKEKDQIKKHDIETIEEKEEDLKREEEIAKLNNSSPNSSGGVKEDCTASMEPSAIELPDYLIKYIAIVSYEQRQNYKDDFNAEYDEYRALHARMETVARRFIKLDAQRKRLSPGSKEYQNVHEEVLQEYQKIKQSSPNYHEEKYRCEYLHNKLAHIKRLIGEFDQQQAESWS | null | null | positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; snRNA transcription by RNA polymerase II [GO:0042795]; transcription elongation by RNA polymerase II [GO:0006368] | nucleoplasm [GO:0005654]; transcription elongation factor complex [GO:0008023] | cis-regulatory region sequence-specific DNA binding [GO:0000987] | PF10390;PF07303; | 6.10.140.340;1.10.10.2670; | ELL/occludin family | PTM: Ubiquitinated by SIAH1, leading to its degradation by the proteasome. Interaction with AFF4 stabilizes ELL2 and prevents ELL2 ubiquitination. {ECO:0000269|PubMed:22483617}. | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III (PubMed:22195968). Plays a role in immunoglobulin secretion in plasma cells: directs efficient alternative mRNA processing, influencing both proximal poly(A) site choice and exon skipping, as well as immunoglobulin heavy chain (IgH) alternative processing. Probably acts by regulating histone modifications accompanying transition from membrane-specific to secretory IgH mRNA expression. {ECO:0000269|PubMed:20159561, ECO:0000269|PubMed:20471948, ECO:0000269|PubMed:22195968, ECO:0000269|PubMed:23251033}. | Homo sapiens (Human) |
O00476 | NPT4_HUMAN | MATKTELSPTARESKNAQDMQVDETLIPRKVPSLCSARYGIALVLHFCNFTTIAQNVIMNITMVAMVNSTSPQSQLNDSSEVLPVDSFGGLSKAPKSLPAKSSILGGQFAIWEKWGPPQERSRLCSIALSGMLLGCFTAILIGGFISETLGWPFVFYIFGGVGCVCCLLWFVVIYDDPVSYPWISTSEKEYIISSLKQQVGSSKQPLPIKAMLRSLPIWSICLGCFSHQWLVSTMVVYIPTYISSVYHVNIRDNGLLSALPFIVAWVIGMVGGYLADFLLTKKFRLITVRKIATILGSLPSSALIVSLPYLNSGYITATALLTLSCGLSTLCQSGIYINVLDIAPRYSSFLMGASRGFSSIAPVIVPTVSGFLLSQDPEFGWRNVFFLLFAVNLLGLLFYLIFGEADVQEWAKERKLTRL | null | null | glucose-6-phosphate transport [GO:0015760]; monoatomic anion transport [GO:0006820]; monoatomic ion transmembrane transport [GO:0034220]; organic anion transport [GO:0015711]; phosphate ion transport [GO:0006817]; sodium ion transport [GO:0006814]; urate metabolic process [GO:0046415]; urate transport [GO:0015747]; xenobiotic detoxification by transmembrane export across the plasma membrane [GO:1990961] | apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]; cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886] | efflux transmembrane transporter activity [GO:0015562]; organic anion transmembrane transporter activity [GO:0008514]; sodium:phosphate symporter activity [GO:0005436]; toxin transmembrane transporter activity [GO:0019534]; urate transmembrane transporter activity [GO:0015143]; voltage-gated monoatomic anion channel activity [GO:0008308]; xenobiotic transmembrane transporter activity [GO:0042910] | PF07690; | 1.20.1250.20; | Major facilitator superfamily, Sodium/anion cotransporter family | null | SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15505377}; Multi-pass membrane protein {ECO:0000269|PubMed:15505377}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:20810651}; Multi-pass membrane protein {ECO:0000269|PubMed:20810651}. | CATALYTIC ACTIVITY: [Isoform 2]: Reaction=Na(+)(out) + urate(in) = Na(+)(in) + urate(out); Xref=Rhea:RHEA:72383, ChEBI:CHEBI:17775, ChEBI:CHEBI:29101; Evidence={ECO:0000305|PubMed:20810651}; | null | null | null | null | FUNCTION: [Isoform 2]: Transports organic anions in a voltage-driven, multispecific, manner, on the apical side of renal proximal tubule (PubMed:20810651). In particular, participates in the secretion of urate from the cell into the lumen (PubMed:20810651). Urate is the end product of purine metabolism (PubMed:20810651). May have roles in the metabolism and secretion of estrone sulfate, estradiol-17-beta-glucuronide, ochratoxin A, as wells as drugs such as bumetanide (PubMed:20810651). {ECO:0000269|PubMed:20810651, ECO:0000303|PubMed:20810651}. | Homo sapiens (Human) |
O00478 | BT3A3_HUMAN | MKMASSLAFLLLNFHVSLFLVQLLTPCSAQFSVLGPSGPILAMVGEDADLPCHLFPTMSAETMELRWVSSSLRQVVNVYADGKEVEDRQSAPYRGRTSILRDGITAGKAALRIHNVTASDSGKYLCYFQDGDFYEKALVELKVAALGSDLHIEVKGYEDGGIHLECRSTGWYPQPQIKWSDTKGENIPAVEAPVVADGVGLYAVAASVIMRGSSGGGVSCIIRNSLLGLEKTASISIADPFFRSAQPWIAALAGTLPISLLLLAGASYFLWRQQKEKIALSRETEREREMKEMGYAATEQEISLREKLQEELKWRKIQYMARGEKSLAYHEWKMALFKPADVILDPDTANAILLVSEDQRSVQRAEEPRDLPDNPERFEWRYCVLGCENFTSGRHYWEVEVGDRKEWHIGVCSKNVERKKGWVKMTPENGYWTMGLTDGNKYRALTEPRTNLKLPEPPRKVGIFLDYETGEISFYNATDGSHIYTFPHASFSEPLYPVFRILTLEPTALTICPIPKEVESSPDPDLVPDHSLETPLTPGLANESGEPQAEVTSLLLPAHPGAEVSPSATTNQNHKLQARTEALY | null | null | regulation of cytokine production [GO:0001817]; T cell mediated immunity [GO:0002456]; T cell receptor signaling pathway [GO:0050852] | external side of plasma membrane [GO:0009897]; membrane [GO:0016020]; plasma membrane [GO:0005886] | signaling receptor binding [GO:0005102] | PF13765;PF00622;PF07686; | 2.60.120.920;2.60.40.10; | Immunoglobulin superfamily, BTN/MOG family | PTM: N-glycosylated. {ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:20610803}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21918970, ECO:0000269|PubMed:22767497}; Single-pass type I membrane protein {ECO:0000269|PubMed:21918970, ECO:0000269|PubMed:22767497}. | null | null | null | null | null | FUNCTION: Plays a role in T-cell responses in the adaptive immune response. {ECO:0000269|PubMed:22767497}. | Homo sapiens (Human) |
O00481 | BT3A1_HUMAN | MKMASFLAFLLLNFRVCLLLLQLLMPHSAQFSVLGPSGPILAMVGEDADLPCHLFPTMSAETMELKWVSSSLRQVVNVYADGKEVEDRQSAPYRGRTSILRDGITAGKAALRIHNVTASDSGKYLCYFQDGDFYEKALVELKVAALGSDLHVDVKGYKDGGIHLECRSTGWYPQPQIQWSNNKGENIPTVEAPVVADGVGLYAVAASVIMRGSSGEGVSCTIRSSLLGLEKTASISIADPFFRSAQRWIAALAGTLPVLLLLLGGAGYFLWQQQEEKKTQFRKKKREQELREMAWSTMKQEQSTRVKLLEELRWRSIQYASRGERHSAYNEWKKALFKPADVILDPKTANPILLVSEDQRSVQRAKEPQDLPDNPERFNWHYCVLGCESFISGRHYWEVEVGDRKEWHIGVCSKNVQRKGWVKMTPENGFWTMGLTDGNKYRTLTEPRTNLKLPKPPKKVGVFLDYETGDISFYNAVDGSHIHTFLDVSFSEALYPVFRILTLEPTALTICPA | null | null | activated T cell proliferation [GO:0050798]; adaptive immune response [GO:0002250]; positive regulation of cytokine production [GO:0001819]; positive regulation of type II interferon production [GO:0032729]; regulation of cytokine production [GO:0001817]; T cell receptor signaling pathway [GO:0050852] | external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886] | signaling receptor binding [GO:0005102] | PF13765;PF00622;PF07686; | 2.60.120.920;2.60.40.10; | Immunoglobulin superfamily, BTN/MOG family | PTM: N-glycosylated. {ECO:0000269|PubMed:20610803, ECO:0000269|PubMed:22846996}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21113407, ECO:0000269|PubMed:21918970, ECO:0000269|PubMed:22767497}; Single-pass type I membrane protein {ECO:0000269|PubMed:21113407, ECO:0000269|PubMed:21918970, ECO:0000269|PubMed:22767497}. | null | null | null | null | null | FUNCTION: Plays a role in T-cell activation and in the adaptive immune response. Regulates the proliferation of activated T-cells. Regulates the release of cytokines and IFNG by activated T-cells. Mediates the response of T-cells toward infected and transformed cells that are characterized by high levels of phosphorylated metabolites, such as isopentenyl pyrophosphate. {ECO:0000269|PubMed:21113407, ECO:0000269|PubMed:21918970, ECO:0000269|PubMed:22767497, ECO:0000269|PubMed:22846996}. | Homo sapiens (Human) |
O00482 | NR5A2_HUMAN | MSSNSDTGDLQESLKHGLTPIGAGLPDRHGSPIPARGRLVMLPKVETEALGLARSHGEQGQMPENMQVSQFKMVNYSYDEDLEELCPVCGDKVSGYHYGLLTCESCKGFFKRTVQNNKRYTCIENQNCQIDKTQRKRCPYCRFQKCLSVGMKLEAVRADRMRGGRNKFGPMYKRDRALKQQKKALIRANGLKLEAMSQVIQAMPSDLTISSAIQNIHSASKGLPLNHAALPPTDYDRSPFVTSPISMTMPPHGSLQGYQTYGHFPSRAIKSEYPDPYTSSPESIMGYSYMDSYQTSSPASIPHLILELLKCEPDEPQVQAKIMAYLQQEQANRSKHEKLSTFGLMCKMADQTLFSIVEWARSSIFFRELKVDDQMKLLQNCWSELLILDHIYRQVVHGKEGSIFLVTGQQVDYSIIASQAGATLNNLMSHAQELVAKLRSLQFDQREFVCLKFLVLFSLDVKNLENFQLVEGVQEQVNAALLDYTMCNYPQQTEKFGQLLLRLPEIRAISMQAEEYLYYKHLNGDVPYNNLLIEMLHAKRA | null | null | acinar cell differentiation [GO:0090425]; bile acid metabolic process [GO:0008206]; calcineurin-mediated signaling [GO:0097720]; cellular response to leukemia inhibitory factor [GO:1990830]; cholesterol homeostasis [GO:0042632]; embryo development ending in birth or egg hatching [GO:0009792]; homeostatic process [GO:0042592]; hormone-mediated signaling pathway [GO:0009755]; pancreas morphogenesis [GO:0061113]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of viral genome replication [GO:0045070]; regulation of cell population proliferation [GO:0042127]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; tissue development [GO:0009888] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; nuclear receptor activity [GO:0004879]; phospholipid binding [GO:0005543]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]; transcription cis-regulatory region binding [GO:0000976]; transcription coregulator binding [GO:0001221]; zinc ion binding [GO:0008270] | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR5 subfamily | PTM: Sumoylated by SUMO1 at Lys-270 during the hepatic acute phase response, leading to promote interaction with GPS2 and prevent N-Cor corepressor complex dissociation. {ECO:0000269|PubMed:20159957}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Nuclear receptor that acts as a key metabolic sensor by regulating the expression of genes involved in bile acid synthesis, cholesterol homeostasis and triglyceride synthesis. Together with the oxysterol receptors NR1H3/LXR-alpha and NR1H2/LXR-beta, acts as an essential transcriptional regulator of lipid metabolism. Plays an anti-inflammatory role during the hepatic acute phase response by acting as a corepressor: inhibits the hepatic acute phase response by preventing dissociation of the N-Cor corepressor complex (PubMed:20159957). May be responsible for the liver-specific activity of enhancer II, probably in combination with other hepatocyte transcription factors. Key regulator of cholesterol 7-alpha-hydroxylase gene (CYP7A) expression in liver. May also contribute to the regulation of pancreas-specific genes and play important roles in embryonic development. Activates the transcription of CYP2C38 (By similarity). {ECO:0000250|UniProtKB:P45448, ECO:0000269|PubMed:15707893, ECO:0000269|PubMed:15723037, ECO:0000269|PubMed:15897460, ECO:0000269|PubMed:16289203, ECO:0000269|PubMed:20159957}.; FUNCTION: (Microbial infection) Plays a crucial role for hepatitis B virus gene transcription and DNA replication. Mechanistically, synergistically cooperates with HNF1A to up-regulate the activity of one of the critical cis-elements in the hepatitis B virus genome enhancer II (ENII). {ECO:0000269|PubMed:14728801, ECO:0000269|PubMed:9786908}. | Homo sapiens (Human) |
O00483 | NDUA4_HUMAN | MLRQIIGQAKKHPSLIPLFVFIGTGATGATLYLLRLALFNPDVCWDRNNPEPWNKLGPNDQYKFYSVNVDYSKLKKERPDF | null | null | cellular respiration [GO:0045333]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; positive regulation of cytochrome-c oxidase activity [GO:1904960] | mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739] | NADH dehydrogenase (ubiquinone) activity [GO:0008137]; protein-containing complex binding [GO:0044877] | PF06522; | null | Complex IV NDUFA4 subunit family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:23746447, ECO:0000269|PubMed:30030519}; Single-pass membrane protein {ECO:0000269|PubMed:30030519}. | null | null | null | null | null | FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules unsing 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix (PubMed:22902835). NDUFA4 is required for complex IV maintenance (PubMed:22902835). {ECO:0000269|PubMed:22902835}. | Homo sapiens (Human) |
O00487 | PSDE_HUMAN | MDRLLRLGGGMPGLGQGPPTDAPAVDTAEQVYISSLALLKMLKHGRAGVPMEVMGLMLGEFVDDYTVRVIDVFAMPQSGTGVSVEAVDPVFQAKMLDMLKQTGRPEMVVGWYHSHPGFGCWLSGVDINTQQSFEALSERAVAVVVDPIQSVKGKVVIDAFRLINANMMVLGHEPRQTTSNLGHLNKPSIQALIHGLNRHYYSITINYRKNELEQKMLLNLHKKSWMEGLTLQDYSEHCKHNESVVKEMLELAKNYNKAVEEEDKMTPEQLAIKNVGKQDPKRHLEEHVDVLMTSNIVQCLAAMLDTVVFK | 3.4.19.- | null | double-strand break repair via homologous recombination [GO:0000724]; double-strand break repair via nonhomologous end joining [GO:0006303]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein K63-linked deubiquitination [GO:0070536]; regulation of proteasomal protein catabolic process [GO:0061136]; response to ethanol [GO:0045471]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytosol [GO:0005829]; cytosolic proteasome complex [GO:0031597]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome accessory complex [GO:0022624]; proteasome complex [GO:0000502]; proteasome regulatory particle, lid subcomplex [GO:0008541]; secretory granule lumen [GO:0034774] | endopeptidase activator activity [GO:0061133]; K63-linked deubiquitinase activity [GO:0061578]; metal ion binding [GO:0046872]; metal-dependent deubiquitinase activity [GO:0140492]; metallopeptidase activity [GO:0008237]; proteasome binding [GO:0070628] | PF01398; | 3.40.140.10; | Peptidase M67A family, PSMD14 subfamily | null | null | null | null | null | null | null | FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. The PSMD14 subunit is a metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains within the complex. Plays a role in response to double-strand breaks (DSBs): acts as a regulator of non-homologous end joining (NHEJ) by cleaving 'Lys-63'-linked polyubiquitin, thereby promoting retention of JMJD2A/KDM4A on chromatin and restricting TP53BP1 accumulation. Also involved in homologous recombination repair by promoting RAD51 loading. {ECO:0000269|PubMed:1317798, ECO:0000269|PubMed:22909820, ECO:0000269|PubMed:9374539}. | Homo sapiens (Human) |
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