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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O15033 | AREL1_HUMAN | MFYVIGGITVSVVAFFFTIKFLFELAARVVSFLQNEDRERRGDRTIYDYVRGNYLDPRSCKVSWDWKDPYEVGHSMAFRVHLFYKNGQPFPAHRPVGLRVHISHVELAVEIPVTQEVLQEPNSNVVKVAFTVRKAGRYEITVKLGGLNVAYSPYYKIFQPGMVVPSKTKIVCHFSTLVLTCGQPHTLQIVPRDEYDNPTNNSMSLRDEHNYTLSIHELGPQEEESTGVSFEKSVTSNRQTFQVFLRLTLHSRGCFHACISYQNQPINNGEFDIIVLSEDEKNIVERNVSTSGVSIYFEAYLYNATNCSSTPWHLPPMHMT... | 2.3.2.26 | null | apoptotic process [GO:0006915]; negative regulation of apoptotic process [GO:0043066]; protein K11-linked ubiquitination [GO:0070979]; protein K33-linked ubiquitination [GO:1990390]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; regulation of inflammatory response [GO:0050727]; ubiquitin... | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842] | PF00630;PF00632; | 3.30.2160.10;3.30.2410.10;3.90.1750.10;2.60.40.10; | null | PTM: Autoubiquitinated in vitro in the presence of E2 enzyme UBE2D1/UBCH5A. {ECO:0000269|PubMed:23479728}. | null | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26; Evidence={ECO:0000269|PubMed:23479728, ECO:0000269|PubMed:25752577}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:23479728, ECO:0000269|PubMed:25752577}. | null | null | FUNCTION: E3 ubiquitin-protein ligase that catalyzes 'Lys-11'- or 'Lys-33'-linked polyubiquitin chains, with some preference for 'Lys-33' linkages (PubMed:25752577). E3 ubiquitin-protein ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin... | Homo sapiens (Human) |
O15040 | TCPR2_HUMAN | MASISEPVTFREFCPLYYLLNAIPTKIQKGFRSIVVYLTALDTNGDYIAVGSSIGMLYLYCRHLNQMRKYNFEGKTESITVVKLLSCFDDLVAAGTASGRVAVFQLVSSLPGRNKQLRRFDVTGIHKNSITALAWSPNGMKLFSGDDKGKIVYSSLDLDQGLCNSQLVLEEPSSIVQLDYSQKVLLVSTLQRSLLFYTEEKSVRQIGTQPRKSTGKFGACFIPGLCKQSDLTLYASRPGLRLWKADVHGTVQATFILKDAFAGGVKPFELHPRLESPNSGSCSLPERHLGLVSCFFQEGWVLSWNEYSIYLLDTVNQATV... | null | null | autophagy [GO:0006914]; protein exit from endoplasmic reticulum [GO:0032527] | cytoplasm [GO:0005737] | null | PF06462;PF19193; | 2.130.10.10; | WD repeat KIAA0329 family | null | null | null | null | null | null | null | FUNCTION: Probably plays a role as positive regulator of autophagy. {ECO:0000269|PubMed:23176824}. | Homo sapiens (Human) |
O15041 | SEM3E_HUMAN | MASAGHIITLLLWGYLLELWTGGHTADTTHPRLRLSHKELLNLNRTSIFHSPFGFLDLHTMLLDEYQERLFVGGRDLVYSLSLERISDGYKEIHWPSTALKMEECIMKGKDAGECANYVRVLHHYNRTHLLTCGTGAFDPVCAFIRVGYHLEDPLFHLESPRSERGRGRCPFDPSSSFISTLIGSELFAGLYSDYWSRDAAIFRSMGRLAHIRTEHDDERLLKEPKFVGSYMIPDNEDRDDNKVYFFFTEKALEAENNAHAIYTRVGRLCVNDVGGQRILVNKWSTFLKARLVCSVPGMNGIDTYFDELEDVFLLPTRDH... | null | null | axon guidance [GO:0007411]; branching involved in blood vessel morphogenesis [GO:0001569]; gonadotrophin-releasing hormone neuronal migration to the hypothalamus [GO:0021828]; negative chemotaxis [GO:0050919]; negative regulation of angiogenesis [GO:0016525]; negative regulation of axon extension involved in axon guida... | extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | chemorepellent activity [GO:0045499]; receptor ligand activity [GO:0048018]; semaphorin receptor binding [GO:0030215] | PF00047;PF01403; | 2.60.40.10;3.30.1680.10;2.130.10.10; | Semaphorin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Plays an important role in signaling via the cell surface receptor PLXND1. Mediates reorganization of the actin cytoskeleton, leading to the retraction of cell projections. Promotes focal adhesion disassembly and inhibits adhesion of endothelial cells to the extracellular matrix. Regulates angiogenesis, both ... | Homo sapiens (Human) |
O15042 | SR140_HUMAN | MADKTPGGSQKASSKTRSSDVHSSGSSDAHMDASGPSDSDMPSRTRPKSPRKHNYRNESARESLCDSPHQNLSRPLLENKLKAFSIGKMSTAKRTLSKKEQEELKKKEDEKAAAEIYEEFLAAFEGSDGNKVKTFVRGGVVNAAKEEHETDEKRGKIYKPSSRFADQKNPPNQSSNERPPSLLVIETKKPPLKKGEKEKKKSNLELFKEELKQIQEERDERHKTKGRLSRFEPPQSDSDGQRRSMDAPSRRNRSSGVLDDYAPGSHDVGDPSTTNLYLGNINPQMNEEMLCQEFGRFGPLASVKIMWPRTDEERARERNC... | null | null | RNA processing [GO:0006396] | nucleoplasm [GO:0005654]; nucleus [GO:0005634] | RNA binding [GO:0003723] | PF04818;PF08312;PF00076;PF01805; | 1.25.40.90;3.30.70.330;6.10.140.420;1.10.10.790; | Splicing factor SR family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20858735}. | null | null | null | null | null | null | Homo sapiens (Human) |
O15047 | SET1A_HUMAN | MDQEGGGDGQKAPSFQWRNYKLIVDPALDPALRRPSQKVYRYDGVHFSVNDSKYIPVEDLQDPRCHVRSKNRDFSLPVPKFKLDEFYIGQIPLKEVTFARLNDNVRETFLKDMCRKYGEVEEVEILLHPRTRKHLGLARVLFTSTRGAKETVKNLHLTSVMGNIIHAQLDIKGQQRMKYYELIVNGSYTPQTVPTGGKALSEKFQGSGAATETAESRRRSSSDTAAYPAGTTAVGTPGNGTPCSQDTSFSSSRQDTPSSFGQFTPQSSQGTPYTSRGSTPYSQDSAYSSSTTSTSFKPRRSENSYQDAFSRRHFSASSAS... | 2.1.1.364 | null | brain development [GO:0007420]; DNA damage response [GO:0006974]; methylation [GO:0032259]; regulation of chromatin organization [GO:1902275]; regulation of hematopoietic stem cell differentiation [GO:1902036] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; histone methyltransferase complex [GO:0035097]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Set1C/COMPASS complex [GO:0048188] | beta-catenin binding [GO:0008013]; histone H3K4 methyltransferase activity [GO:0042800]; histone H3K4 monomethyltransferase activity [GO:0140945]; histone H3K4 trimethyltransferase activity [GO:0140999]; RNA binding [GO:0003723]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629] | PF11764;PF00076;PF00856; | 3.30.70.330;2.170.270.10; | Class V-like SAM-binding methyltransferase superfamily | null | SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:17355966, ECO:0000269|PubMed:38003223}. Chromosome {ECO:0000269|PubMed:17355966}. Cytoplasm {ECO:0000269|PubMed:38003223}. Note=Localizes to a largely non-overlapping set of euchromatic nuclear speckles with SETD1B, suggesting that SETD1A and SETD1B each bind to... | CATALYTIC ACTIVITY: Reaction=L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60264, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1... | null | null | null | null | FUNCTION: Histone methyltransferase that catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism (PubMed:12670868, PubMed:25561738). Part of chromatin remodeling machinery, forms H3K4me1, H3K4me2 and H3K4me3 methylation marks... | Homo sapiens (Human) |
O15049 | N4BP3_HUMAN | MATAPGPAGIAMGSVGSLLERQDFSPEELRAALAGSRGSRQPDGLLRKGLGQREFLSYLHLPKKDSKSTKNTKRAPRNEPADYATLYYREHSRAGDFSKTSLPERGRFDKCRIRPSVFKPTAGNGKGFLSMQSLASHKGQKLWRSNGSLHTLACHPPLSPGPRASQARAQLLHALSLDEGGPEPEPSLSDSSSGGSFGRSPGTGPSPFSSSLGHLNHLGGSLDRASQGPKEAGPPAVLSCLPEPPPPYEFSCSSAEEMGAVLPETCEELKRGLGDEDGSNPFTQVLEERQRLWLAELKRLYVERLHEVTQKAERSERNLQ... | null | null | innate immune response [GO:0045087]; nervous system development [GO:0007399] | axon [GO:0030424]; cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425] | null | PF06818; | null | N4BP3 family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000269|PubMed:11717310}. Cell projection, axon {ECO:0000250|UniProtKB:Q3LUD3}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q3LUD3}. Note=In developing neurons, accumulates in early growth cones and at branching points of axons and dendrites. {ECO:0000250|UniProtKB:Q3... | null | null | null | null | null | FUNCTION: Plays a positive role in the antiviral innate immune signaling pathway. Mechanistically, interacts with MAVS and functions as a positive regulator to promote 'Lys-63'-linked polyubiquitination of MAVS and thus strengthens the interaction between MAVS and TRAF2 (PubMed:34880843). Also plays a role in axon and ... | Homo sapiens (Human) |
O15054 | KDM6B_HUMAN | MHRAVDPPGARAAREAFALGGLSCAGAWSSCPPHPPPRSAWLPGGRCSASIGQPPLPAPLPPSHGSSSGHPSKPYYAPGAPTPRPLHGKLESLHGCVQALLREPAQPGLWEQLGQLYESEHDSEEATRCYHSALRYGGSFAELGPRIGRLQQAQLWNFHTGSCQHRAKVLPPLEQVWNLLHLEHKRNYGAKRGGPPVKRAAEPPVVQPVPPAALSGPSGEEGLSPGGKRRRGCNSEQTGLPPGLPLPPPPLPPPPPPPPPPPPPLPGLATSPPFQLTKPGLWSTLHGDAWGPERKGSAPPERQEQRHSLPHPYPYPAPAY... | 1.14.11.68 | COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:17825402}; | cardiac muscle cell differentiation [GO:0055007]; cell fate commitment [GO:0045165]; cellular response to hydrogen peroxide [GO:0070301]; chromatin remodeling [GO:0006338]; endothelial cell differentiation [GO:0045446]; hippocampus development [GO:0021766]; inflammatory response to antigenic stimulus [GO:0002437]; meso... | MLL3/4 complex [GO:0044666]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | beta-catenin binding [GO:0008013]; chromatin DNA binding [GO:0031490]; histone demethylase activity [GO:0032452]; histone H3K27me2/H3K27me3 demethylase activity [GO:0071558]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF02373;PF21322;PF21326; | 1.20.58.1370;2.10.110.20;2.60.120.650; | UTX family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:17825402}. | CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-lysyl(27)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60224, Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15544, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:1... | null | null | null | null | FUNCTION: Histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code (PubMed:17713478, PubMed:17825402, PubMed:17851529, PubMed:18003914). Demethylates trimethylated and dimethylated H3 'Lys-27' (PubMed:17713478, PubMed:17825402, PubMed:17851529, PubMed:180... | Homo sapiens (Human) |
O15055 | PER2_HUMAN | MNGYAEFPPSPSNPTKEPVEPQPSQVPLQEDVDMSSGSSGHETNENCSTGRDSQGSDCDDSGKELGMLVEPPDARQSPDTFSLMMAKSEHNPSTSGCSSDQSSKVDTHKELIKTLKELKVHLPADKKAKGKASTLATLKYALRSVKQVKANEEYYQLLMSSEGHPCGADVPSYTVEEMESVTSEHIVKNADMFAVAVSLVSGKILYISDQVASIFHCKRDAFSDAKFVEFLAPHDVGVFHSFTSPYKLPLWSMCSGADSFTQECMEEKSFFCRVSVRKSHENEIRYHPFRMTPYLVKVRDQQGAESQLCCLLLAERVHSG... | null | null | chromatin remodeling [GO:0006338]; circadian regulation of gene expression [GO:0032922]; circadian regulation of translation [GO:0097167]; circadian rhythm [GO:0007623]; entrainment of circadian clock by photoperiod [GO:0043153]; fatty acid metabolic process [GO:0006631]; gluconeogenesis [GO:0006094]; glycogen biosynth... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | transcription cis-regulatory region binding [GO:0000976]; transcription coactivator activity [GO:0003713]; transcription corepressor binding [GO:0001222] | PF08447;PF21353;PF12114; | 3.30.450.20; | null | PTM: Acetylated. Deacetylated by SIRT1, resulting in decreased protein stability. Deacetylated by SIRT6, preventing its degradation by the proteasome, resulting in increased protein stability. {ECO:0000250|UniProtKB:O54943}.; PTM: Phosphorylated by CSNK1E and CSNK1D. Phosphorylation results in PER2 protein degradation.... | SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000269|PubMed:22274616}. Cytoplasm {ECO:0000250|UniProtKB:O54943}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54943}. Note=Nucleocytoplasmic shuttling is effected by interaction with other circadian core oscillator proteins and/or by phosphorylation. Transloca... | null | null | null | null | null | FUNCTION: Transcriptional repressor 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 a... | Homo sapiens (Human) |
O15056 | SYNJ2_HUMAN | MALSKGLRLLGRLGAEGDCSVLLEARGRDDCLLFEAGTVATLAPEEKEVIKGQYGKLTDAYGCLGELRLKSGGTSLSFLVLVTGCTSVGRIPDAEIYKITATDFYPLQEEAKEEERLIALKKILSSGVFYFSWPNDGSRFDLTVRTQKQGDDSSEWGNSFFWNQLLHVPLRQHQVSCCDWLLKIICGVVTIRTVYASHKQAKACLVSRVSCERTGTRFHTRGVNDDGHVSNFVETEQMIYMDDGVSSFVQIRGSVPLFWEQPGLQVGSHHLRLHRGLEANAPAFDRHMVLLKEQYGQQVVVNLLGSRGGEEVLNRAFKKL... | 3.1.3.36 | null | membrane organization [GO:0061024]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol dephosphorylation [GO:0046856]; synaptic vesicle endocytosis [GO:0048488] | cell projection [GO:0042995]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; membrane raft [GO:0045121]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; presynapse [GO:0098793] | phosphatidylinositol phosphate 4-phosphatase activity [GO:0034596]; phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity [GO:0052629]; phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity [GO:0043813]; phosphatidylinositol-3-phosphate phosphatase activity [GO:0004438]; phosphatidylinositol-4,5-bisphosph... | PF08952;PF02383; | 3.30.70.330;3.60.10.10; | Synaptojanin family; Inositol 1,4,5-trisphosphate 5-phosphatase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11084340}. Cell membrane {ECO:0000269|PubMed:11084340}. Membrane raft {ECO:0000269|PubMed:11084340}. Presynapse {ECO:0000250|UniProtKB:O55207}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O55207}. Note=Localizes at presynapse terminals in brain and at bundles of mi... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456; EC=3.1.3.36; Evidence={ECO:0000250|UniP... | null | null | null | null | FUNCTION: Inositol 5-phosphatase which may be involved in distinct membrane trafficking and signal transduction pathways. May mediate the inhibitory effect of Rac1 on endocytosis. | Homo sapiens (Human) |
O15060 | ZBT39_HUMAN | MGMRIKLQSTNHPNNLLKELNKCRLSETMCDVTIVVGSRSFPAHKAVLACAAGYFQNLFLNTGLDAARTYVVDFITPANFEKVLSFVYTSELFTDLINVGVIYEVAERLGMEDLLQACHSTFPDLESTARAKPLTSTSESHSGTLSCPSAEPAHPLGELRGGGDYLGADRNYVLPSDAGGSYKEEEKNVASDANHSLHLPQPPPPPPKTEDHDTPAPFTSIPSMMTQPLLGTVSTGIQTSTSSCQPYKVQSNGDFSKNSFLTPDNAVDITTGTNSCLSNSEHSKDPGFGQMDELQLEDLGDDDLQFEDPAEDIGTTEEVI... | null | null | negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of cytokine production [GO:0001817]; regulation of immune system process [GO:0002682] | nucleoplasm [GO:0005654] | DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00651;PF00096; | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: May be involved in transcriptional regulation. | Homo sapiens (Human) |
O15061 | SYNEM_HUMAN | MLSWRLQTGPEKAELQELNARLYDYVCRVRELERENLLLEEELRGRRGREGLWAEGQARCAEEARSLRQQLDELSWATALAEGERDALRRELRELQRLDAEERAARGRLDAELGAQQRELQEALGARAALEALLGRLQAERRGLDAAHERDVRELRARAASLTMHFRARATGPAAPPPRLREVHDSYALLVAESWRETVQLYEDEVRELEEALRRGQESRLQAEEETRLCAQEAEALRREALGLEQLRARLEDALLRMREEYGIQAEERQRVIDCLEDEKATLTLAMADWLRDYQDLLQVKTGLSLEVATYRALLEGESN... | null | null | fast-twitch skeletal muscle fiber contraction [GO:0031443]; intermediate filament cytoskeleton organization [GO:0045104] | adherens junction [GO:0005912]; costamere [GO:0043034]; intermediate filament [GO:0005882]; intermediate filament cytoskeleton [GO:0045111]; neurofilament cytoskeleton [GO:0060053]; sarcolemma [GO:0042383] | intermediate filament binding [GO:0019215]; structural constituent of cytoskeleton [GO:0005200]; structural constituent of muscle [GO:0008307]; vinculin binding [GO:0017166] | PF00038; | 1.20.5.170;1.20.5.1160; | Intermediate filament family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction, adherens junction. Note=There are at least two distinct SYNM subpopulations, one in which SYMN interacts with DES within the Z-lines, and another in which it interacts with both DTNA and DES at the costamere. | null | null | null | null | null | FUNCTION: Type-VI intermediate filament (IF) which plays an important cytoskeletal role within the muscle cell cytoskeleton. It forms heteromeric IFs with desmin and/or vimentin, and via its interaction with cytoskeletal proteins alpha-dystrobrevin, dystrophin, talin-1, utrophin and vinculin, is able to link these hete... | Homo sapiens (Human) |
O15062 | ZBTB5_HUMAN | MDFPGHFEQIFQQLNYQRLHGQLCDCVIVVGNRHFKAHRSVLAACSTHFRALFSVAEGDQTMNMIQLDSEVVTAEAFAALIDMMYTSTLMLGESNVMDVLLAASHLHLNSVVKACKHYLTTRTLPMSPPSERVQEQSARMQRSFMLQQLGLSIVSSALNSSQNGEEQPAPMSSSMRSNLDQRTPFPMRRLHKRKQSAEERARQRLRPSIDESAISDVTPENGPSGVHSREEFFSPDSLKIVDNPKADGMTDNQEDSAIMFDQSFGTQEDAQVPSQSDNSAGNMAQLSMASRATQVETSFDQEAAPEKSSFQCENPEVGLG... | null | null | negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977] | PF00651; | 3.30.160.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: May be involved in transcriptional regulation. | Homo sapiens (Human) |
O15066 | KIF3B_HUMAN | MSKLKSSESVRVVVRCRPMNGKEKAASYDKVVDVDVKLGQVSVKNPKGTAHEMPKTFTFDAVYDWNAKQFELYDETFRPLVDSVLQGFNGTIFAYGQTGTGKTYTMEGIRGDPEKRGVIPNSFDHIFTHISRSQNQQYLVRASYLEIYQEEIRDLLSKDQTKRLELKERPDTGVYVKDLSSFVTKSVKEIEHVMNVGNQNRSVGATNMNEHSSRSHAIFVITIECSEVGLDGENHIRVGKLNLVDLAGSERQAKTGAQGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNAKTVMVANVGPA... | null | null | anterograde axonal transport [GO:0008089]; anterograde dendritic transport of neurotransmitter receptor complex [GO:0098971]; cilium assembly [GO:0060271]; determination of left/right symmetry [GO:0007368]; intraciliary transport [GO:0042073]; microtubule-based movement [GO:0007018]; mitotic centrosome separation [GO:0... | axon cytoplasm [GO:1904115]; centrosome [GO:0005813]; ciliary tip [GO:0097542]; cilium [GO:0005929]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendrite cytoplasm [GO:0032839]; dendritic spine [GO:0043197]; extracellular exosome [GO:0070062]; kinesin complex [GO:0005871]; kinesin II complex [GO:0016939]; membrane [GO... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; intraciliary transport particle B binding [GO:0120170]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]; plus-end-directed microtubule motor activity [GO:0008574]; small GTPase binding [GO:0031267] | PF00225; | 3.40.850.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, Kinesin II subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, cilium {ECO:0000250|UniProtKB:Q61771}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q61771}. | null | null | null | null | null | FUNCTION: Microtubule-based molecular motor that transport intracellular cargos, such as vesicles, organelles and protein complexes. Uses ATP hydrolysis to generate force to bind and move along the microtubule (By similarity). Plays a role in cilia formation (PubMed:32386558). Involved in photoreceptor integrity and op... | Homo sapiens (Human) |
O15067 | PUR4_HUMAN | MSPVLHFYVRPSGHEGAAPGHTRRKLQGKLPELQGVETELCYNVNWTAEALPSAEETKKLMWLFGCPLLLDDVARESWLLPGSNDLLLEVGPRLNFSTPTSTNIVSVCRATGLGPVDRVETTRRYRLSFAHPPSAEVEAIALATLHDRMTEQHFPHPIQSFSPESMPEPLNGPINILGEGRLALEKANQELGLALDSWDLDFYTKRFQELQRNPSTVEAFDLAQSNSEHSRHWFFKGQLHVDGQKLVHSLFESIMSTQESSNPNNVLKFCDNSSAIQGKEVRFLRPEDPTRPSRFQQQQGLRHVVFTAETHNFPTGVCPF... | 6.3.5.3 | null | 'de novo' AMP biosynthetic process [GO:0044208]; 'de novo' IMP biosynthetic process [GO:0006189]; 'de novo' XMP biosynthetic process [GO:0097294]; anterior head development [GO:0097065]; glutamine metabolic process [GO:0006541]; GMP biosynthetic process [GO:0006177]; purine nucleotide biosynthetic process [GO:0006164];... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; phosphoribosylformylglycinamidine synthase activity [GO:0004642] | PF02769;PF18072;PF18076;PF13507; | 3.40.50.880;1.10.8.750;3.90.650.10;3.30.1330.10; | FGAMS family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:4... | null | PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000305|PubMed:10548741}. | null | null | FUNCTION: Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. {ECO:0000305|PubMed:10548741}. | Homo sapiens (Human) |
O15068 | MCF2L_HUMAN | MFDCWRFILCKRPGSNSYSSPQRPNEAKKEETDHQIDVSDVIRLVQDTPEATAMATDEIMHQDIVPLCAADIQDQLKKRFAYLSGGRGQDGSPVITFPDYPAFSEIPDKEFQNVMTYLTSIPSLQDAGIGFILVIDRRRDKWTSVKASVLRIAASFPANLQLVLVLRPTGFFQRTLSDIAFKFNRDDFKMKVPVIMLSSVPDLHGYIDKSQLTEDLGGTLDYCHSRWLCQRTAIESFALMVKQTAQMLQSFGTELAETELPNDVQSTSSVLCAHTEKKDKAKEDLRLALKEGHSVLESLRELQAEGSEPSVNQDQLDNQA... | null | null | intracellular signal transduction [GO:0035556]; positive regulation of Rho protein signal transduction [GO:0035025]; regulation of small GTPase mediated signal transduction [GO:0051056] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endomembrane system [GO:0012505]; extracellular space [GO:0005615]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; extrinsic component of membrane [GO:0019898]; plasma membrane [GO:0005886] | guanyl-nucleotide exchange factor activity [GO:0005085]; phosphatidylinositol binding [GO:0035091] | PF13716;PF00169;PF00621;PF07653;PF00435; | 1.20.58.60;1.20.900.10;2.30.29.30;2.30.30.40; | MCF2 family | null | SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm {ECO:0000269|PubMed:15157669}. Cell membrane {ECO:0000269|PubMed:15157669}; Peripheral membrane protein {ECO:0000269|PubMed:15157669}; Cytoplasmic side {ECO:0000269|PubMed:15157669}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:15157669}. Endomembrane sy... | null | null | null | null | null | FUNCTION: Guanine nucleotide exchange factor that catalyzes guanine nucleotide exchange on RHOA and CDC42, and thereby contributes to the regulation of RHOA and CDC42 signaling pathways (By similarity). Seems to lack activity with RAC1. Becomes activated and highly tumorigenic by truncation of the N-terminus (By simila... | Homo sapiens (Human) |
O15072 | ATS3_HUMAN | MVLLSLWLIAAALVEVRTSADGQAGNEEMVQIDLPIKRYREYELVTPVSTNLEGRYLSHTLSASHKKRSARDVSSNPEQLFFNITAFGKDFHLRLKPNTQLVAPGAVVEWHETSLVPGNITDPINNHQPGSATYRIRRTEPLQTNCAYVGDIVDIPGTSVAISNCDGLAGMIKSDNEEYFIEPLERGKQMEEEKGRIHVVYKRSAVEQAPIDMSKDFHYRESDLEGLDDLGTVYGNIHQQLNETMRRRRHAGENDYNIEVLLGVDDSVVRFHGKEHVQNYLLTLMNIVNEIYHDESLGVHINVVLVRMIMLGYAKSISLI... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | collagen biosynthetic process [GO:0032964]; collagen catabolic process [GO:0030574]; collagen fibril organization [GO:0030199]; extracellular matrix organization [GO:0030198]; in utero embryonic development [GO:0001701]; positive regulation of vascular endothelial growth factor signaling pathway [GO:1900748]; protein p... | extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | endopeptidase activity [GO:0004175]; heparin binding [GO:0008201]; metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270] | PF17771;PF19236;PF05986;PF01562;PF01421;PF19030;PF00090; | 2.60.120.830;3.40.1620.60;3.40.390.10;2.20.100.10; | null | PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.; PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, re... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28985353}. Secreted, extracellular space, extracellular matrix {ECO:0000250}. | null | null | null | null | null | FUNCTION: Cleaves the propeptides of type II collagen prior to fibril assembly. Does not act on types I and III collagens. | Homo sapiens (Human) |
O15075 | DCLK1_HUMAN | MSFGRDMELEHFDERDKAQRYSRGSRVNGLPSPTHSAHCSFYRTRTLQTLSSEKKAKKVRFYRNGDRYFKGIVYAISPDRFRSFEALLADLTRTLSDNVNLPQGVRTIYTIDGLKKISSLDQLVEGESYVCGSIEPFKKLEYTKNVNPNWSVNVKTTSASRAVSSLATAKGSPSEVRENKDFIRPKLVTIIRSGVKPRKAVRILLNKKTAHSFEQVLTDITDAIKLDSGVVKRLYTLDGKQVMCLQDFFGDDDIFIACGPEKFRYQDDFLLDESECRVVKSTSYTKIASSSRRSTTKSPGPSRRSKSPASTSSVNGTPGS... | 2.7.11.1 | null | axon extension [GO:0048675]; central nervous system development [GO:0007417]; central nervous system projection neuron axonogenesis [GO:0021952]; dendrite morphogenesis [GO:0048813]; endosomal transport [GO:0016197]; forebrain development [GO:0030900]; intracellular signal transduction [GO:0035556]; negative regulation... | plasma membrane [GO:0005886]; postsynaptic density [GO:0014069] | ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF03607;PF00069; | 3.10.20.230;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, CaMK subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Probable kinase that may be involved in a calcium-signaling pathway controlling neuronal migration in the developing brain. May also participate in functions of the mature nervous system. | Homo sapiens (Human) |
O15078 | CE290_HUMAN | MPPNINWKEIMKVDPDDLPRQEELADNLLISLSKVEVNELKSEKQENVIHLFRITQSLMKMKAQEVELALEEVEKAGEEQAKFENQLKTKVMKLENELEMAQQSAGGRDTRFLRNEICQLEKQLEQKDRELEDMEKELEKEKKVNEQLALRNEEAENENSKLRRENKRLKKKNEQLCQDIIDYQKQIDSQKETLLSRRGEDSDYRSQLSKKNYELIQYLDEIQTLTEANEKIEVQNQEMRKNLEESVQEMEKMTDEYNRMKAIVHQTDNVIDQLKKENDHYQLQVQELTDLLKSKNEEDDPIMVAVNAKVEEWKLILSSK... | null | null | camera-type eye development [GO:0043010]; ciliary basal body-plasma membrane docking [GO:0097711]; ciliary transition zone assembly [GO:1905349]; cilium assembly [GO:0060271]; eye photoreceptor cell development [GO:0042462]; hindbrain development [GO:0030902]; kidney development [GO:0001822]; non-motile cilium assembly... | centriolar satellite [GO:0034451]; centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; ciliary transition zone [GO:0035869]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; membrane [GO:0016020]; MKS complex [GO:0036038]; nucleus [GO:0005634]; photoreceptor... | identical protein binding [GO:0042802] | PF16574; | null | null | PTM: Ubiquitinated. May undergo monoubiquitination; monoubiquitination is inhibited in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock, but does not cause its displacement from centriolar satellites. {ECO:0000269|PubMed:24121310}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:16682973, ECO:0000269|PubMed:21493627, ECO:0000269|PubMed:21565611, ECO:0000269|PubMed:22797915}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satel... | null | null | null | null | null | FUNCTION: Involved in early and late steps in cilia formation. Its association with CCP110 is required for inhibition of primary cilia formation by CCP110 (PubMed:18694559). May play a role in early ciliogenesis in the disappearance of centriolar satellites and in the transition of primary ciliar vesicles (PCVs) to cap... | Homo sapiens (Human) |
O15079 | SNPH_HUMAN | MAMSLPGSRRTSAGSRRRTSPPVSVRDAYGTSSLSSSSNSGSYKGSDSSPTPRRSMKYTLCSDNHGIKPPTPEQYLTPLQQKEVCIRHLKARLKDTQDRLQDRDTEIDDLKTQLSRMQEDWIEEECHRVEAQLALKEARKEIKQLKQVIDTVKNNLIDKDKGLQKYFVDINIQNKKLETLLHSMEVAQNGMAKEDGTGESAGGSPARSLTRSSTYTKLSDPAVCGDRQPGDPSSGSAEDGADSGFAAADDTLSRTDALEASSLLSSGVDCGTEETSLHSSFGLGPRFPASNTYEKLLCGMEAGVQASCMQERAIQTDFVQ... | null | null | neuron differentiation [GO:0030182]; neurotransmitter secretion [GO:0007269]; synaptic vesicle docking [GO:0016081] | cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; membrane [GO:0016020]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]; presynapse [GO:0098793] | syntaxin-1 binding [GO:0017075] | PF15290; | null | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Synapse, synaptosome. | null | null | null | null | null | FUNCTION: Inhibits SNARE complex formation by absorbing free STX1A. {ECO:0000269|PubMed:10707983}. | Homo sapiens (Human) |
O15083 | ERC2_HUMAN | MYGSARTITNLEGSPSRSPRLPRSPRLGHRRTSSGGGGGTGKTLSMENIQSLNAAYATSGPMYLSDHEGVASTTYPKGTMTLGRATNRAVYGGRVTAMGSSPNIASAGLSHTDVLSYTDQHGGLTGSSHHHHHQVPSMLRQVRDSTMLDLQAQLKELQRENDLLRKELDIKDSKLGSSMNSIKTFWSPELKKERVLRKEEAARMSVLKEQMRVSHEENQHLQLTIQALQDELRTQRDLNHLLQQESGNRGAEHFTIELTEENFRRLQAEHDRQAKELFLLRKTLEEMELRIETQKQTLNARDESIKKLLEMLQSKGLPSK... | null | null | maintenance of presynaptic active zone structure [GO:0048790]; neuromuscular synaptic transmission [GO:0007274]; regulation of calcium-dependent activation of synaptic vesicle fusion [GO:0150037]; regulation of presynaptic cytosolic calcium ion concentration [GO:0099509]; regulation of synaptic plasticity [GO:0048167];... | cytoskeleton of presynaptic active zone [GO:0048788]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; growth cone [GO:0030426]; presynaptic active zone [GO:0048786]; presynaptic membrane [GO:0042734] | structural constituent of presynaptic active zone [GO:0098882] | PF10174; | 1.10.287.1490; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12923177}. Synapse {ECO:0000269|PubMed:12923177}. Presynaptic active zone {ECO:0000269|PubMed:12923177}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12923177}. Note=In neurons, localized to synapses, and colocalizes with PCLO. Localized to the active zone of presynapt... | null | null | null | null | null | FUNCTION: Thought to be involved in the organization of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release. Seems to act together with BSN. May recruit liprin-alpha proteins to the CAZ. | Homo sapiens (Human) |
O15084 | ANR28_HUMAN | MAFLKLRDQPSLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFS... | null | null | negative regulation of non-canonical NF-kappaB signal transduction [GO:1901223] | cytosol [GO:0005829]; nucleoplasm [GO:0005654] | null | PF00023;PF12796;PF13637; | 1.25.40.20; | null | null | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:16564677}. Note=Seems to be excluded from nucleoli. | null | null | null | null | null | FUNCTION: Putative regulatory subunit of protein phosphatase 6 (PP6) that may be involved in the recognition of phosphoprotein substrates. Involved in the PP6-mediated dephosphorylation of NFKBIE opposing its degradation in response to TNF-alpha. Selectively inhibits the phosphatase activity of PPP1C. Targets PPP1C to ... | Homo sapiens (Human) |
O15085 | ARHGB_HUMAN | MSVRLPQSIDRLSSLSSLGDSAPERKSPSHHRQPSDASETTGLVQRCVIIQKDQHGFGFTVSGDRIVLVQSVRPGGAAMKAGVKEGDRIIKVNGTMVTNSSHLEVVKLIKSGAYVALTLLGSSPSSMGISGLQQDPSPAGAPRITSVIPSPPPPPPLPPPQRITGPKPLQDPEVQKHATQILRNMLRQEEKELQDILPLYGDTSQRPSEGRLSLDSQEGDSGLDSGTERFPSLSESLMNRNSVLSDPGLDSPRTSPVIMARVAQHHRRQGSDAAVPSTGDQGVDQSPKPLIIGPEEDYDPGYFNNESDIIFQDLEKLKSR... | null | null | actin cytoskeleton organization [GO:0030036]; establishment of cell polarity [GO:0030010]; G protein-coupled receptor signaling pathway [GO:0007186]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of cell growth [GO:0001558]; regulation of small GTPase mediated signal transduction [GO:00510... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886] | G protein-coupled receptor binding [GO:0001664]; GTPase activator activity [GO:0005096]; guanyl-nucleotide exchange factor activity [GO:0005085] | PF00595;PF17838;PF09128;PF00621; | 2.30.42.10;1.20.900.10;2.30.29.30;1.10.167.10; | null | PTM: Phosphorylated by MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14).; PTM: Ubiquitinated by the BCR(KLHL20) E3 ubiquitin ligase complex when previously phosphorylated by MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14), leading to its degradation, thereby restricting RhoA activity and facilitating growth ... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10900204}. Membrane {ECO:0000269|PubMed:10900204}. Note=Translocated to the membrane upon stimulation. | null | null | null | null | null | FUNCTION: May play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as GTPase-activating protein (GAP) for GNA12 and GNA13. Involved in neurotrophin-induced neurite outgrowth. {ECO:00... | Homo sapiens (Human) |
O15091 | MRPP3_HUMAN | MTFYLFGIRSFPKLWKSPYLGLGPGHSYVSLFLADRCGIRNQQRLFSLKTMSPQNTKATNLIAKARYLRKDEGSNKQVYSVPHFFLAGAAKERSQMNSQTEDHALAPVRNTIQLPTQPLNSEEWDKLKEDLKENTGKTSFESWIISQMAGCHSSIDVAKSLLAWVAAKNNGIVSYDLLVKYLYLCVFHMQTSEVIDVFEIMKARYKTLEPRGYSLLIRGLIHSDRWREALLLLEDIKKVITPSKKNYNDCIQGALLHQDVNTAWNLYQELLGHDIVPMLETLKAFFDFGKDIKDDNYSNKLLDILSYLRNNQLYPGESFA... | 3.1.26.5 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:25953853}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305|PubMed:25953853}; Note=Binds 2 Mg(2+) or Mg(2+) ions per subunit. {ECO:0000305|PubMed:25953853}; | mitochondrial tRNA 5'-end processing [GO:0097745]; tRNA 5'-leader removal [GO:0001682] | mitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO:0042645]; mitochondrial ribonuclease P complex [GO:0030678]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654] | metal ion binding [GO:0046872]; ribonuclease P activity [GO:0004526] | PF16953; | 3.40.50.11980;1.25.40.10; | PPR family, P subfamily | PTM: Degraded by LONP1 following mitochondrial unfolded protein response, probably leading to inhibit translation in mitochondrion. {ECO:0000269|PubMed:27350246}. | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18984158}. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.; EC=3.1.26.5; Evidence={ECO:0000269|PubMed:25953853}; | null | null | null | null | FUNCTION: Catalytic ribonuclease component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3, which cleaves tRNA molecules in their 5'-ends (PubMed:18984158, PubMed:25953853, PubMed:34715011). The presence of TRMT10C/MRPP1, HSD17B10/MRPP2 is required to catalyze tRNA m... | Homo sapiens (Human) |
O15105 | SMAD7_HUMAN | MFRTKRSALVRRLWRSRAPGGEDEEEGAGGGGGGGELRGEGATDSRAHGAGGGGPGRAGCCLGKAVRGAKGHHHPHPPAAGAGAAGGAEADLKALTHSVLKKLKERQLELLLQAVESRGGTRTACLLLPGRLDCRLGPGAPAGAQPAQPPSSYSLPLLLCKVFRWPDLRHSSEVKRLCCCESYGKINPELVCCNPHHLSRLCELESPPPPYSRYPMDFLKPTADCPDAVPSSAETGGTNYLAPGGLSDSQLLLEPGDRSHWCVVAYWEEKTRVGRLYCVQEPSLDIFYDLPQGNGFCLGQLNSDNKSQLVQKVRSKIGCG... | null | null | adherens junction assembly [GO:0034333]; anatomical structure morphogenesis [GO:0009653]; artery morphogenesis [GO:0048844]; cell differentiation [GO:0030154]; cellular response to leukemia inhibitory factor [GO:1990830]; cellular response to transforming growth factor beta stimulus [GO:0071560]; negative regulation of... | centrosome [GO:0005813]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; fibrillar center [GO:0001650]; heteromeric SMAD protein complex [GO:0071144]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | activin receptor binding [GO:0070697]; beta-catenin binding [GO:0008013]; collagen binding [GO:0005518]; I-SMAD binding [GO:0070411]; metal ion binding [GO:0046872]; transcription corepressor activity [GO:0003714]; transcription regulator inhibitor activity [GO:0140416]; type I transforming growth factor beta receptor ... | PF03165;PF03166; | 2.60.200.10;3.90.520.10; | Dwarfin/SMAD family | PTM: Phosphorylation on Ser-249 does not affect its stability, nuclear localization or inhibitory function in TGFB signaling; however it affects its ability to regulate transcription (By similarity). Phosphorylated by PDPK1. {ECO:0000250|UniProtKB:O35253, ECO:0000269|PubMed:17327236}.; PTM: Ubiquitinated by WWP1 (By si... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:16601693, ECO:0000269|PubMed:17327236}. Cytoplasm {ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:16601693, ECO:0000269|PubMed:17327236}. Note=Interaction with NEDD4L or RNF111 induces translocation from the nucleus to the cytoplasm (PubMed... | null | null | null | null | null | FUNCTION: Antagonist of signaling by TGF-beta (transforming growth factor) type 1 receptor superfamily members; has been shown to inhibit TGF-beta (Transforming growth factor) and activin signaling by associating with their receptors thus preventing SMAD2 access (PubMed:21791611). Functions as an adapter to recruit SMU... | Homo sapiens (Human) |
O15111 | IKKA_HUMAN | MERPPGLRPGAGGPWEMRERLGTGGFGNVCLYQHRELDLKIAIKSCRLELSTKNRERWCHEIQIMKKLNHANVVKACDVPEELNILIHDVPLLAMEYCSGGDLRKLLNKPENCCGLKESQILSLLSDIGSGIRYLHENKIIHRDLKPENIVLQDVGGKIIHKIIDLGYAKDVDQGSLCTSFVGTLQYLAPELFENKPYTATVDYWSFGTMVFECIAGYRPFLHHLQPFTWHEKIKKKDPKCIFACEEMSGEVRFSSHLPQPNSLCSLVVEPMENWLQLMLNWDPQQRGGPVDLTLKQPRCFVLMDHILNLKIVHILNMTS... | 2.7.11.10 | null | anatomical structure morphogenesis [GO:0009653]; canonical NF-kappaB signal transduction [GO:0007249]; cellular response to cadmium ion [GO:0071276]; cellular response to reactive oxygen species [GO:0034614]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to virus [GO:0098586]; I-kappaB phos... | CD40 receptor complex [GO:0035631]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; IkappaB kinase complex [GO:0008385]; nucleoplasm [GO:0005654] | ATP binding [GO:0005524]; IkappaB kinase activity [GO:0008384]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; protein serine/threonine kinase activity [GO:0004674]; protein-containing complex binding [GO:0044877]; scaffold protein... | PF18397;PF12179;PF00069; | 1.20.1270.250;6.10.250.2110;1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, I-kappa-B kinase subfamily | PTM: Phosphorylated by MAP3K14/NIK, AKT and to a lesser extent by MEKK1, and dephosphorylated by PP2A. Autophosphorylated.; PTM: Ubiquitinated by TRIM56 via 'Lys-63'-linked ubiquitination, promoting activation of CHUK/IKKA. {ECO:0000269|PubMed:35952808}.; PTM: (Microbial infection) Acetylation of Thr-179 by Yersinia Yo... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12789342, ECO:0000269|PubMed:30341167}. Nucleus {ECO:0000269|PubMed:12789342}. Note=Shuttles between the cytoplasm and the nucleus. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[I-kappa-B protein] = ADP + H(+) + O-phospho-L-seryl-[I-kappa-B protein]; Xref=Rhea:RHEA:19073, Rhea:RHEA-COMP:13698, Rhea:RHEA-COMP:13699, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.10; Evidence={ECO:0000269|PubMe... | null | null | null | null | FUNCTION: Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses (PubMed:18626576, PubMed:9244310, PubMed:9252186, PubMed:9346484). Acts as a part of the can... | Homo sapiens (Human) |
O15116 | LSM1_HUMAN | MNYMPGTASLIEDIDKKHLVLLRDGRTLIGFLRSIDQFANLVLHQTVERIHVGKKYGDIPRGIFVVRGENVVLLGEIDLEKESDTPLQQVSIEEILEEQRVEQQTKLEAEKLKVQALKDRGLSIPRADTLDEY | null | null | deadenylation-dependent decapping of nuclear-transcribed mRNA [GO:0000290]; histone mRNA catabolic process [GO:0071044]; mRNA processing [GO:0006397]; negative regulation of neuron differentiation [GO:0045665]; neuron differentiation [GO:0030182]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactio... | axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; Lsm1-7-Pat1 complex [GO:1990726]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; P-body [GO:0000932]; ribonucleoprotein complex [GO:1990904] | mRNA binding [GO:0003729]; pre-mRNA binding [GO:0036002]; RNA binding [GO:0003723]; RNA cap binding [GO:0000339] | PF01423; | 2.30.30.100; | SnRNP Sm proteins family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:18172165}. Cytoplasm, P-body {ECO:0000305|PubMed:18172165}. | null | null | null | null | null | FUNCTION: Plays a role in the degradation of histone mRNAs, the only eukaryotic mRNAs that are not polyadenylated (PubMed:18172165). Probably also part of an LSm subunits-containing complex involved in the general process of mRNA degradation (By similarity). {ECO:0000250|UniProtKB:P47017, ECO:0000269|PubMed:18172165}. | Homo sapiens (Human) |
O15117 | FYB1_HUMAN | MAKYNTGGNPTEDVSVNSRPFRVTGPNSSSGIQARKNLFNNQGNASPPAGPSNVPKFGSPKPPVAVKPSSEEKPDKEPKPPFLKPTGAGQRFGTPASLTTRDPEAKVGFLKPVGPKPINLPKEDSKPTFPWPPGNKPSLHSVNQDHDLKPLGPKSGPTPPTSENEQKQAFPKLTGVKGKFMSASQDLEPKPLFPKPAFGQKPPLSTENSHEDESPMKNVSSSKGSPAPLGVRSKSGPLKPAREDSENKDHAGEISSLPFPGVVLKPAASRGGPGLSKNGEEKKEDRKIDAAKNTFQSKINQEELASGTPPARFPKAPSKL... | null | null | immune response [GO:0006955]; integrin-mediated signaling pathway [GO:0007229]; protein localization to plasma membrane [GO:0072659]; T cell receptor signaling pathway [GO:0050852] | actin cytoskeleton [GO:0015629]; anchoring junction [GO:0070161]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | lipid binding [GO:0008289]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102] | PF14603;PF07653; | 2.30.30.40; | null | PTM: T-cell receptor ligation leads to increased tyrosine phosphorylation. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9671755}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Cell junction {ECO:0000250|UniProtKB:O35601}. Note=Colocalizes with TMEM47 at cell-cell contacts in podocytes. {ECO:0000250|UniProtKB:O35601}. | null | null | null | null | null | FUNCTION: Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells (By similarity). May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton (PubMed:10747096, PubMed:16980616). Modulates the expression of IL2 (By similarity). Involved in platelet activation (By similarity)... | Homo sapiens (Human) |
O15118 | NPC1_HUMAN | MTARGLALGLLLLLLCPAQVFSQSCVWYGECGIAYGDKRYNCEYSGPPKPLPKDGYDLVQELCPGFFFGNVSLCCDVRQLQTLKDNLQLPLQFLSRCPSCFYNLLNLFCELTCSPRQSQFLNVTATEDYVDPVTNQTKTNVKELQYYVGQSFANAMYNACRDVEAPSSNDKALGLLCGKDADACNATNWIEYMFNKDNGQAPFTITPVFSDFPVHGMEPMNNATKGCDESVDEVTAPCSCQDCSIVCGPKPQPPPPPAPWTILGLDAMYVIMWITYMAFLLVFFGAFFAVWCYRKRYFVSEYTPIDSNIAFSVNASDKGE... | null | null | adult walking behavior [GO:0007628]; autophagy [GO:0006914]; bile acid metabolic process [GO:0008206]; cellular response to low-density lipoprotein particle stimulus [GO:0071404]; cellular response to steroid hormone stimulus [GO:0071383]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholester... | endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; membrane [GO:0016020]; membrane raft [GO:0045121]; nuclear envelope [GO:0005635]; perinucl... | cholesterol binding [GO:0015485]; signaling receptor activity [GO:0038023]; sterol transporter activity [GO:0015248]; transmembrane signaling receptor activity [GO:0004888]; virus receptor activity [GO:0001618] | PF16414;PF02460;PF12349; | 1.20.1640.10; | Patched family | PTM: N-glycosylated. {ECO:0000269|PubMed:10821832, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19563754}. | SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:12554680, ECO:0000269|PubMed:27378690}; Multi-pass membrane protein {ECO:0000269|PubMed:10821832, ECO:0000269|PubMed:27238017, ECO:0000269|PubMed:28784760}. Lysosome membrane {ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:27378690, ECO:0000269|PubMed:99... | CATALYTIC ACTIVITY: Reaction=cholesterol(in) = cholesterol(out); Xref=Rhea:RHEA:39747, ChEBI:CHEBI:16113; Evidence={ECO:0000269|PubMed:18772377}; | null | null | null | null | FUNCTION: Intracellular cholesterol transporter which acts in concert with NPC2 and plays an important role in the egress of cholesterol from the endosomal/lysosomal compartment (PubMed:10821832, PubMed:12554680, PubMed:18772377, PubMed:27238017, PubMed:9211849, PubMed:9927649). Unesterified cholesterol that has been r... | Homo sapiens (Human) |
O15119 | TBX3_HUMAN | MSLSMRDPVIPGTSMAYHPFLPHRAPDFAMSAVLGHQPPFFPALTLPPNGAAALSLPGALAKPIMDQLVGAAETGIPFSSLGPQAHLRPLKTMEPEEEVEDDPKVHLEAKELWDQFHKRGTEMVITKSGRRMFPPFKVRCSGLDKKAKYILLMDIIAADDCRYKFHNSRWMVAGKADPEMPKRMYIHPDSPATGEQWMSKVVTFHKLKLTNNISDKHGFTLAFPSDHATWQGNYSFGTQTILNSMHKYQPRFHIVRANDILKLPYSTFRTYLFPETEFIAVTAYQNDKITQLKIDNNPFAKGFRDTGNGRREKRKQLTLQ... | null | null | animal organ morphogenesis [GO:0009887]; anterior/posterior axis specification, embryo [GO:0008595]; atrioventricular bundle cell differentiation [GO:0003167]; atrioventricular canal development [GO:0036302]; atrioventricular canal morphogenesis [GO:1905222]; blood vessel development [GO:0001568]; branching involved in... | chromatin [GO:0000785]; cilium [GO:0005929]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regulatory region sequence-specific DNA ... | PF00907;PF12598;PF20627; | 2.60.40.820; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}. | null | null | null | null | null | FUNCTION: Transcriptional repressor involved in developmental processes (PubMed:10468588). Binds to the palindromic T site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence, or a half-site, which are present in the regulatory region of several genes (PubMed:12000749). Probably plays a role in limb pattern formation (PubMed:1046858... | Homo sapiens (Human) |
O15120 | PLCB_HUMAN | MELWPCLAAALLLLLLLVQLSRAAEFYAKVALYCALCFTVSAVASLVCLLRHGGRTVENMSIIGWFVRSFKYFYGLRFEVRDPRRLQEARPCVIVSNHQSILDMMGLMEVLPERCVQIAKRELLFLGPVGLIMYLGGVFFINRQRSSTAMTVMADLGERMVRENLKVWIYPEGTRNDNGDLLPFKKGAFYLAVQAQVPIVPVVYSSFSSFYNTKKKFFTSGTVTVQVLEAIPTSGLTAADVPALVDTCHRAMRTTFLHISKTPQENGATAGSGVQPAQ | 2.3.1.51 | null | CDP-diacylglycerol biosynthetic process [GO:0016024]; epidermis development [GO:0008544]; phosphatidic acid biosynthetic process [GO:0006654]; phospholipid metabolic process [GO:0006644]; positive regulation of cytokine production [GO:0001819]; positive regulation of cytokine-mediated signaling pathway [GO:0001961]; re... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]; specific granule membrane [GO:0035579] | 1-acylglycerol-3-phosphate O-acyltransferase activity [GO:0003841] | PF01553; | null | 1-acyl-sn-glycerol-3-phosphate acyltransferase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21873652}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709, ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342, ChEBI:CHEBI:58608; EC=2.3.1.51; Evidence={ECO:0000269|PubMed:15629135, ECO:0000269|PubMed:19075029, ECO:0000269|PubMed:21... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.05 uM for C15:0-CoA {ECO:0000269|PubMed:21873652}; KM=523.97 uM for C18:0-CoA {ECO:0000269|PubMed:21873652}; KM=30.21 uM for C18:1-CoA {ECO:0000269|PubMed:21873652}; KM=8.29 uM for LPA sn-1 C18:1 {ECO:0000269|PubMed:21873652}; Vmax=51.61 nmol/min/mg enzyme for C... | PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3. | null | null | FUNCTION: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. {ECO:0000269|PubMed:15629135, ECO:0000269|PubMed:19075029, ECO:0000269|PubMed:21873652, ECO:00... | Homo sapiens (Human) |
O15121 | DEGS1_HUMAN | MGSRVSREDFEWVYTDQPHADRRREILAKYPEIKSLMKPDPNLIWIIIMMVLTQLGAFYIVKDLDWKWVIFGAYAFGSCINHSMTLAIHEIAHNAAFGNCKAMWNRWFGMFANLPIGIPYSISFKRYHMDHHRYLGADGVDVDIPTDFEGWFFCTAFRKFIWVILQPLFYAFRPLFINPKPITYLEVINTVAQVTFDILIYYFLGIKSLVYMLAASLLGLGLHPISGHFIAEHYMFLKGHETYSYYGPLNLLTFNVGYHNEHHDFPNIPGKSLPLVRKIAAEYYDNLPHYNSWIKVLYDFVMDDTISPYSRMKRHQKGEM... | 1.14.19.17; 5.2.1.- | null | ceramide biosynthetic process [GO:0046513]; myelin maintenance [GO:0043217]; sphingolipid biosynthetic process [GO:0030148]; unsaturated fatty acid biosynthetic process [GO:0006636] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]; specific granule membrane [GO:0035579] | electron transfer activity [GO:0009055]; retinol isomerase activity [GO:0050251]; sphingolipid delta-4 desaturase activity [GO:0042284] | PF00487;PF08557; | null | Fatty acid desaturase type 1 family, DEGS subfamily | PTM: Myristoylation can target the enzyme to the mitochondria leading to an increase in ceramide levels. {ECO:0000269|PubMed:19647031}. | SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|PubMed:19647031, ECO:0000269|PubMed:30620338}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:19647031, ECO:0000269|PubMed:30620338, ECO:0000269|PubMed:9188692}; Multi-pass membrane protein {ECO:0000269|PubMed:19647031, ECO:0000269|PubMed:9188692}. | CATALYTIC ACTIVITY: Reaction=an N-acylsphinganine + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = an N-acylsphing-4-enine + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46544, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI... | null | null | null | null | FUNCTION: Has sphingolipid-delta-4-desaturase activity. Converts D-erythro-sphinganine to D-erythro-sphingosine (E-sphing-4-enine) (PubMed:11937514, PubMed:30620337, PubMed:30620338). Catalyzes the equilibrium isomerization of retinols (By similarity). {ECO:0000250|UniProtKB:Q5F3C1, ECO:0000269|PubMed:11937514, ECO:000... | Homo sapiens (Human) |
O15123 | ANGP2_HUMAN | MWQIVFFTLSCDLVLAAAYNNFRKSMDSIGKKQYQVQHGSCSYTFLLPEMDNCRSSSSPYVSNAVQRDAPLEYDDSVQRLQVLENIMENNTQWLMKLENYIQDNMKKEMVEIQQNAVQNQTAVMIEIGTNLLNQTAEQTRKLTDVEAQVLNQTTRLELQLLEHSLSTNKLEKQILDQTSEINKLQDKNSFLEKKVLAMEDKHIIQLQSIKEEKDQLQVLVSKQNSIIEELEKKIVTATVNNSVLQKQQHDLMETVNNLLTMMSTSNSAKDPTVAKEEQISFRDCAEVFKSGHTTNGIYTLTFPNSTEEIKAYCDMEAGGG... | null | null | angiogenesis [GO:0001525]; animal organ regeneration [GO:0031100]; cellular response to growth factor stimulus [GO:0071363]; gene expression [GO:0010467]; germ cell development [GO:0007281]; glomerulus vasculature development [GO:0072012]; maternal process involved in female pregnancy [GO:0060135]; negative regulation ... | cell projection [GO:0042995]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | metal ion binding [GO:0046872]; receptor tyrosine kinase binding [GO:0030971]; signaling receptor binding [GO:0005102] | PF00147; | 3.90.215.10;4.10.530.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:32908006}. | null | null | null | null | null | FUNCTION: Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating ANGPT1 signaling (PubMed:15284220, PubMed:19116766, PubMed:19223473, PubMed:9204896). Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1 (PubMed:15284220, PubMed:19116766, PubMed:19223473, PubMed:9204896). In the ab... | Homo sapiens (Human) |
O15126 | SCAM1_HUMAN | MSDFDSNPFADPDLNNPFKDPSVTQVTRNVPPGLDEYNPFSDSRTPPPGGVKMPNVPNTQPAIMKPTEEHPAYTQIAKEHALAQAELLKRQEELERKAAELDRREREMQNLSQHGRKNNWPPLPSNFPVGPCFYQDFSVDIPVEFQKTVKLMYYLWMFHAVTLFLNIFGCLAWFCVDSARAVDFGLSILWFLLFTPCSFVCWYRPLYGAFRSDSSFRFFVFFFVYICQFAVHVLQAAGFHNWGNCGWISSLTGLNQNIPVGIMMIIIAALFTASAVISLVMFKKVHGLYRTTGASFEKAQQEFATGVMSNKTVQTAAANA... | null | null | endocytosis [GO:0006897]; establishment of localization in cell [GO:0051649]; exocytosis [GO:0006887]; post-Golgi vesicle-mediated transport [GO:0006892]; protein transport [GO:0015031] | clathrin-coated vesicle [GO:0030136]; membrane [GO:0016020]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]; specific granule membrane [GO:0035579]; synaptic vesicle membrane [GO:0030672]; trans-Golgi network [GO:0005802]; trans-Golgi network membrane [GO:0032588]; zymogen granule membrane [GO:0... | protein domain specific binding [GO:0019904] | PF04144; | null | SCAMP family | null | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:15840657}; Multi-pass membrane protein {ECO:0000269|PubMed:15840657}. Recycling endosome membrane {ECO:0000269|PubMed:15840657}; Multi-pass membrane protein {ECO:0000269|PubMed:15840657}. | null | null | null | null | null | FUNCTION: Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface. | Homo sapiens (Human) |
O15127 | SCAM2_HUMAN | MSAFDTNPFADPVDVNPFQDPSVTQLTNAPQGGLAEFNPFSETNAATTVPVTQLPGSSQPAVLQPSVEPTQPTPQAVVSAAQAGLLRQQEELDRKAAELERKERELQNTVANLHVRQNNWPPLPSWCPVKPCFYQDFSTEIPADYQRICKMLYYLWMLHSVTLFLNLLACLAWFSGNSSKGVDFGLSILWFLIFTPCAFLCWYRPIYKAFRSDNSFSFFVFFFVFFCQIGIYIIQLVGIPGLGDSGWIAALSTLDNHSLAISVIMMVVAGFFTLCAVLSVFLLQRVHSLYRRTGASFQQAQEEFSQGIFSSRTFHRAASS... | null | null | post-Golgi vesicle-mediated transport [GO:0006892]; protein transport [GO:0015031] | extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; recycling endosome membrane [GO:0055038]; trans-Golgi network membrane [GO:0032588] | null | PF04144; | null | SCAMP family | null | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:15840657}; Multi-pass membrane protein {ECO:0000269|PubMed:15840657}. Recycling endosome membrane {ECO:0000269|PubMed:15840657}; Multi-pass membrane protein {ECO:0000269|PubMed:15840657}. | null | null | null | null | null | FUNCTION: Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface. | Homo sapiens (Human) |
O15130 | NPFF_HUMAN | MDSRQAAALLVLLLLIDGGCAEGPGGQQEDQLSAEEDSEPLPPQDAQTSGSLLHYLLQAMERPGRSQAFLFQPQRFGRNTQGSWRNEWLSPRAGEGLNSQFWSLAAPQRFGKK | null | null | chemical synaptic transmission [GO:0007268]; excitatory postsynaptic potential [GO:0060079]; neuropeptide signaling pathway [GO:0007218] | axon terminus [GO:0043679]; dendrite [GO:0030425]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; perikaryon [GO:0043204]; postsynapse [GO:0098794] | G protein-coupled receptor binding [GO:0001664]; neuropeptide hormone activity [GO:0005184]; signaling receptor binding [GO:0005102] | PF15085; | null | FARP (FMRFamide related peptide) family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Morphine modulating peptides. Have wide-ranging physiologic effects, including the modulation of morphine-induced analgesia, elevation of arterial blood pressure, and increased somatostatin secretion from the pancreas. Neuropeptide FF potentiates and sensitizes ASIC1 and ASIC3 channels. {ECO:0000269|PubMed:11... | Homo sapiens (Human) |
O15131 | IMA6_HUMAN | MDAMASPGKDNYRMKSYKNKALNPQEMRRRREEEGIQLRKQKREEQLFKRRNVYLPRNDESMLESPIQDPDISSTVPIPEEEVVTTDMVQMIFSNNADQQLTATQKFRKLLSKEPNPPIDQVIQKPGVVQRFVKFLERNENCTLQFEAAWALTNIASGTFLHTKVVIETGAVPIFIKLLNSEHEDVQEQAVWALGNIAGDNAECRDFVLNCEILPPLLELLTNSNRLTTTRNAVWALSNLCRGKNPPPNFSKVSPCLNVLSRLLFSSDPDVLADVCWALSYLSDGPNDKIQAVIDSGVCRRLVELLMHNDYKVVSPALRA... | null | null | NLS-bearing protein import into nucleus [GO:0006607]; protein import into nucleus [GO:0006606] | cytosol [GO:0005829]; NLS-dependent protein nuclear import complex [GO:0042564]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139] | PF00514;PF16186;PF01749; | 1.20.5.690;1.25.10.10; | Importin alpha family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin... | Homo sapiens (Human) |
O15143 | ARC1B_HUMAN | MAYHSFLVEPISCHAWNKDRTQIAICPNNHEVHIYEKSGAKWTKVHELKEHNGQVTGIDWAPESNRIVTCGTDRNAYVWTLKGRTWKPTLVILRINRAARCVRWAPNENKFAVGSGSRVISICYFEQENDWWVCKHIKKPIRSTVLSLDWHPNNVLLAAGSCDFKCRIFSAYIKEVEERPAPTPWGSKMPFGELMFESSSSCGWVHGVCFSASGSRVAWVSHDSTVCLADADKKMAVATLASETLPLLALTFITDNSLVAAGHDCFPVLFTYDAAAGMLSFGGRLDVPKQSSQRGLTARERFQNLDKKASSEGGTAAGAG... | null | null | Arp2/3 complex-mediated actin nucleation [GO:0034314]; response to estradiol [GO:0032355]; response to estrogen [GO:0043627] | actin cytoskeleton [GO:0015629]; Arp2/3 protein complex [GO:0005885]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; nucleus [GO:0005634]; tubulobulbar complex [GO:0036284] | actin filament binding [GO:0051015]; structural constituent of cytoskeleton [GO:0005200] | PF00400; | 2.130.10.10; | WD repeat ARPC1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11741539, ECO:0000269|PubMed:9230079}. Nucleus {ECO:0000269|PubMed:29925947}. | null | null | null | null | null | FUNCTION: Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:11741539, PubMed:9230079). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubM... | Homo sapiens (Human) |
O15144 | ARPC2_HUMAN | MILLEVNNRIIEETLALKFENAAAGNKPEAVEVTFADFDGVLYHISNPNGDKTKVMVSISLKFYKELQAHGADELLKRVYGSFLVNPESGYNVSLLYDLENLPASKDSIVHQAGMLKRNCFASVFEKYFQFQEEGKEGENRAVIHYRDDETMYVESKKDRVTVVFSTVFKDDDDVVIGKVFMQEFKEGRRASHTAPQVLFSHREPPLELKDTDAAVGDNIGYITFVLFPRHTNASARDNTINLIHTFRDYLHYHIKCSKAYIHTRMRAKTSDFLKVLNRARPDAEKKEMKTITGKTFSSR | null | null | actin filament polymerization [GO:0030041]; actin polymerization-dependent cell motility [GO:0070358]; Arp2/3 complex-mediated actin nucleation [GO:0034314]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of lamellipodium assembly [GO:0010592]; positive regulation of substrate ad... | actin cytoskeleton [GO:0015629]; Arp2/3 protein complex [GO:0005885]; cytosol [GO:0005829]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; glutamatergic synapse [GO:0098978]; lamellipodium [GO:0030027]; muscle cell projection membrane [GO:0036195]; neuron projection [GO:0043005]... | actin filament binding [GO:0051015]; structural constituent of cytoskeleton [GO:0005200] | PF04045; | 3.30.1460.20; | ARPC2 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9230079}. Cell projection {ECO:0000269|PubMed:9230079}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q9CVB6}. Nucleus {ECO:0000269|PubMed:29925947}. | null | null | null | null | null | FUNCTION: Actin-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:9230079). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubMed:... | Homo sapiens (Human) |
O15145 | ARPC3_HUMAN | MPAYHSSLMDPDTKLIGNMALLPIRSQFKGPAPRETKDTDIVDEAIYYFKANVFFKNYEIKNEADRTLIYITLYISECLKKLQKCNSKSQGEKEMYTLGITNFPIPGEPGFPLNAIYAKPANKQEDEVMRAYLQQLRQETGLRLCEKVFDPQNDKPSKWWTCFVKRQFMNKSLSGPGQ | null | null | actin polymerization-dependent cell motility [GO:0070358]; Arp2/3 complex-mediated actin nucleation [GO:0034314]; cellular response to nerve growth factor stimulus [GO:1990090]; regulation of actin filament polymerization [GO:0030833] | actin cytoskeleton [GO:0015629]; Arp2/3 protein complex [GO:0005885]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; filamentous actin [GO:0031941]; focal adhesion [GO:0005925]; growth cone leading edge [GO:0061850]; lamellipodium [GO:0030027]; membrane [GO:0016020]; nucleus [GO:0005634]; site of double-stra... | actin filament binding [GO:0051015]; structural constituent of cytoskeleton [GO:0005200] | PF04062; | 1.10.1760.10; | ARPC3 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9230079, ECO:0000269|PubMed:9359840}. Cell projection {ECO:0000269|PubMed:9230079, ECO:0000269|PubMed:9359840}. Nucleus {ECO:0000269|PubMed:29925947}. | null | null | null | null | null | FUNCTION: Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:9230079). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubMed:9230079). In a... | Homo sapiens (Human) |
O15146 | MUSK_HUMAN | MRELVNIPLVHILTLVAFSGTEKLPKAPVITTPLETVDALVEEVATFMCAVESYPQPEISWTRNKILIKLFDTRYSIRENGQLLTILSVEDSDDGIYCCTANNGVGGAVESCGALQVKMKPKITRPPINVKIIEGLKAVLPCTTMGNPKPSVSWIKGDSPLRENSRIAVLESGSLRIHNVQKEDAGQYRCVAKNSLGTAYSKVVKLEVEVFARILRAPESHNVTFGSFVTLHCTATGIPVPTITWIENGNAVSSGSIQESVKDRVIDSRLQLFITKPGLYTCIATNKHGEKFSTAKAAATISIAEWSKPQKDNKGYCAQY... | 2.7.10.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:25029443}; | cell differentiation [GO:0030154]; memory [GO:0007613]; neuromuscular junction development [GO:0007528]; positive regulation of gene expression [GO:0010628]; positive regulation of neuron projection development [GO:0010976]; positive regulation of protein geranylgeranylation [GO:2000541]; positive regulation of protein... | neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein tyrosine kinase activity [GO:0004713]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; Wnt-protein binding [GO:0017147] | PF01392;PF07679;PF13927;PF07714; | 1.10.2000.10;2.60.40.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family | PTM: Ubiquitinated by PDZRN3. Ubiquitination promotes endocytosis and lysosomal degradation (By similarity). {ECO:0000250}.; PTM: Phosphorylated (By similarity). Phosphorylation is induced by AGRIN in a LRP4-dependent manner (By similarity). Autophosphorylated (PubMed:25029443). Autophosphorylation at Tyr-554 is requir... | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000269|PubMed:23326516}; Single-pass type I membrane protein {ECO:0000305}. Note=Colocalizes with acetylcholine receptors (AChR) to the postsynaptic cell membrane of the neuromuscular junction. {ECO:0000269|PubMed:23326516}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Receptor tyrosine kinase which plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ), the synapse between the motor neuron and the skeletal muscle (PubMed:25537362). Recruitment of AGRIN by LRP4 to the MUSK signaling complex induces phosphorylation and activation of MUS... | Homo sapiens (Human) |
O15151 | MDM4_HUMAN | MTSFSTSAQCSTSDSACRISPGQINQVRPKLPLLKILHAAGAQGEMFTVKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLLGELLGRQSFSVKDPSPLYDMLRKNLVTLATATTDAAQTLALAQDHSMDIPSQDQLKQSAEESSTSRKRTTEDDIPTLPTSEHKCIHSREDEDLIENLAQDETSRLDLGFEEWDVAGLPWWFLGNLRSNYTPRSNGSTDLQTNQDVGTAIVSDTTDDLWFLNESVSEQLGVGIKVEAADTEQTSEEVGKVSDKKVIEVGKNDDLEDSKSLSDDTDVEVTSEDEWQCTECKKFNSPSKRYC... | null | null | atrial septum development [GO:0003283]; atrioventricular valve morphogenesis [GO:0003181]; cellular response to hypoxia [GO:0071456]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; endocardial cushion morphogenesis [GO:0003203]; heart valve development [GO:0003170]; negative regulation of ... | nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription repressor complex [GO:0017053] | enzyme binding [GO:0019899]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF13920;PF00641; | 1.10.245.10;3.30.40.10;2.30.30.380; | MDM2/MDM4 family | PTM: Phosphorylated. Phosphorylation at Ser-367 promotes interaction with YWHAG and subsequent ubiquitination and degradation. Phosphorylation at Ser-342 also induces ubiquitination and degradation but to a lower extent. {ECO:0000269|PubMed:16163388, ECO:0000269|PubMed:16511572, ECO:0000269|PubMed:19838211}.; PTM: Ubiq... | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Along with MDM2, contributes to TP53 regulation (PubMed:32300648). Inhibits p53/TP53- and TP73/p73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Inhibits degradation of MDM2. Can reverse MDM2-targeted degradation of TP53 while maintaining suppression of TP53 transa... | Homo sapiens (Human) |
O15155 | BET1_HUMAN | MRRAGLGEGVPPGNYGNYGYANSGYSACEEENERLTESLRSKVTAIKSLSIEIGHEVKTQNKLLAEMDSQFDSTTGFLGKTMGKLKILSRGSQTKLLCYMMLFSLFVFFIIYWIIKLR | null | null | endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; protein transport [GO:0015031]; vesicle fusion with Golgi apparatus [GO:0048280] | endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; SNARE complex [GO:0031201]; transport vesicle [GO:0030133] | SNAP receptor activity [GO:0005484] | null | 1.20.5.110; | BET1 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}. Note=Concentrated most in the intermediate compartment/cis-Golgi network and the cis-Golgi cisternae ... | null | null | null | null | null | FUNCTION: Required for vesicular transport from the ER to the Golgi complex. Functions as a SNARE involved in the docking process of ER-derived vesicles with the cis-Golgi membrane (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
O15156 | ZBT7B_HUMAN | MGSPEDDLIGIPFPDHSSELLSCLNEQRQLGHLCDLTIRTQGLEYRTHRAVLAACSHYFKKLFTEGGGGAVMGAGGSGTATGGAGAGVCELDFVGPEALGALLEFAYTATLTTSSANMPAVLQAARLLEIPCVIAACMEILQGSGLEAPSPDEDDCERARQYLEAFATATASGVPNGEDSPPQVPLPPPPPPPPRPVARRSRKPRKAFLQTKGARANHLVPEVPTVPAHPLTYEEEEVAGRVGSSGGSGPGDSYSPPTGTASPPEGPQSYEPYEGEEEEEELVYPPAYGLAQGGGPPLSPEELGSDEDAIDPDLMAYLSS... | null | null | adaptive thermogenesis [GO:1990845]; ectoderm development [GO:0007398]; lactation [GO:0007595]; negative regulation of CD8-positive, alpha-beta T cell differentiation [GO:0043377]; negative regulation of gene expression [GO:0010629]; negative regulation of NK T cell proliferation [GO:0051141]; negative regulation of T-... | nucleoplasm [GO:0005654] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity [GO:0001217]; histone deacetylase binding [GO:0042826]; metal ion binding [GO:0046872]; protein homodime... | PF00651;PF00096; | 3.30.160.60; | null | PTM: Acetylated directly and specifically by EP300 (PubMed:20810990). EP300-mediated acetylation of Lys-206, Lys-212 and Lys-335 stabilizes the protein by antagonizing ubiquitin conjugation (By similarity). {ECO:0000250|UniProtKB:Q64321, ECO:0000269|PubMed:20810990}.; PTM: Ubiquitinated, leading to proteasomal degradat... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q64321}. | null | null | null | null | null | FUNCTION: Transcription regulator that acts as a key regulator of lineage commitment of immature T-cell precursors. Exerts distinct biological functions in the mammary epithelial cells and T cells in a tissue-specific manner. Necessary and sufficient for commitment of CD4 lineage, while its absence causes CD8 commitmen... | Homo sapiens (Human) |
O15160 | RPAC1_HUMAN | MAASQAVEEMRSRVVLGEFGVRNVHTTDFPGNYSGYDDAWDQDRFEKNFRVDVVHMDENSLEFDMVGIDAAIANAFRRILLAEVPTMAVEKVLVYNNTSIVQDEILAHRLGLIPIHADPRLFEYRNQGDEEGTEIDTLQFRLQVRCTRNPHAAKDSSDPNELYVNHKVYTRHMTWIPLGNQADLFPEGTIRPVHDDILIAQLRPGQEIDLLMHCVKGIGKDHAKFSPVATASYRLLPDITLLEPVEGEAAEELSRCFSPGVIEVQEVQGKKVARVANPRLDTFSREIFRNEKLKKVVRLARVRDHYIFSVESTGVLPPDV... | null | null | transcription by RNA polymerase I [GO:0006360] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; fibrillar center [GO:0001650]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase I complex [GO:0005736]; RNA polymerase III complex [GO:0005666] | DNA binding [GO:0003677]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; protein dimerization activity [GO:0046983]; RNA polymerase I activity [GO:0001054]; RNA polymerase III activity [GO:0001056] | PF01000;PF01193; | 2.170.120.12;3.30.1360.10; | Archaeal Rpo3/eukaryotic RPB3 RNA polymerase subunit family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26151409, ECO:0000269|PubMed:33335104}. Nucleus, nucleolus {ECO:0000269|PubMed:34887565}. Cytoplasm, cytosol {ECO:0000269|PubMed:33335104}. | null | null | null | null | null | FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I and III which synthesize ribosomal RNA precursors and short non-coding RNAs including 5S rRNA, snRNAs, tRNAs and miRNAs, respectively. POLR1... | Homo sapiens (Human) |
O15162 | PLS1_HUMAN | MDKQNSQMNASHPETNLPVGYPPQYPPTAFQGPPGYSGYPGPQVSYPPPPAGHSGPGPAGFPVPNQPVYNQPVYNQPVGAAGVPWMPAPQPPLNCPPGLEYLSQIDQILIHQQIELLEVLTGFETNNKYEIKNSFGQRVYFAAEDTDCCTRNCCGPSRPFTLRIIDNMGQEVITLERPLRCSSCCCPCCLQEIEIQAPPGVPIGYVIQTWHPCLPKFTIQNEKREDVLKISGPCVVCSCCGDVDFEIKSLDEQCVVGKISKHWTGILREAFTDADNFGIQFPLDLDVKMKAVMIGACFLIDFMFFESTGSQEQKSGVW | 3.1.-.- | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:23590222, ECO:0000269|PubMed:23659204, ECO:0000269|PubMed:24343571, ECO:0000269|PubMed:24648509, ECO:0000269|PubMed:8663431}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:27206388}; Name=Zn(2+); Xref=ChEBI:CHEBI:2... | acute-phase response [GO:0006953]; apoptotic process [GO:0006915]; defense response to virus [GO:0051607]; negative regulation of phagocytosis [GO:0050765]; negative regulation of viral genome replication [GO:0045071]; phosphatidylserine biosynthetic process [GO:0006659]; phosphatidylserine exposure on apoptotic cell s... | collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; membrane raft [GO:0045121]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplas... | calcium ion binding [GO:0005509]; CD4 receptor binding [GO:0042609]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; enzyme binding [GO:0019899]; epidermal growth factor receptor binding [GO:0005154]; lead ion binding [GO:0032791]; magnesium ion binding [... | PF03803; | null | Phospholipid scramblase family | PTM: Phosphorylation at Thr-161 by PKC/PKCD increases its phospholipid scramblase activity during both cell stimulation and apoptosis (PubMed:10770950). Phosphorylated by OXSR1 in the presence of RELT. {ECO:0000269|PubMed:10770950, ECO:0000269|PubMed:22052202}.; PTM: Palmitoylation is required for its phospholipid scra... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12564925, ECO:0000269|PubMed:22052202, ECO:0000269|PubMed:23590222, ECO:0000269|PubMed:24648509, ECO:0000269|PubMed:26745724, ECO:0000269|PubMed:37438530}; Single-pass type II membrane protein {ECO:0000269|PubMed:26745724}. Cell membrane {ECO:0000269|PubMed:125649... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571, ChEBI:CHEBI:57643; Evidence={ECO:0000269|PubMed:10770950, ECO:0000269|PubMed:18629440, ECO:0000269|PubMed:23590222, ECO:0000269|PubMed:23659204, ECO:0000269|PubMed:24343571, E... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-9.0 for nuclease activity. {ECO:0000269|PubMed:27206388}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius for nuclease activity (PubMed:27206388). Activity reduced significantly beyond 45 degrees Celsius (PubMed:27206388). {ECO:0000269|PubMed:27206388}; | FUNCTION: Catalyzes calcium-induced ATP-independent rapid bidirectional and non-specific movement of phospholipids (lipid scrambling or lipid flip-flop) between the inner and outer leaflet of the plasma membrane resulting in collapse of the phospholipid asymmetry which leads to phosphatidylserine externalization on the... | Homo sapiens (Human) |
O15164 | TIF1A_HUMAN | MEVAVEKAVAAAAAASAAASGGPSAAPSGENEAESRQGPDSERGGEAARLNLLDTCAVCHQNIQSRAPKLLPCLHSFCQRCLPAPQRYLMLPAPMLGSAETPPPVPAPGSPVSGSSPFATQVGVIRCPVCSQECAERHIIDNFFVKDTTEVPSSTVEKSNQVCTSCEDNAEANGFCVECVEWLCKTCIRAHQRVKFTKDHTVRQKEEVSPEAVGVTSQRPVFCPFHKKEQLKLYCETCDKLTCRDCQLLEHKEHRYQFIEEAFQNQKVIIDTLITKLMEKTKYIKFTGNQIQNRIIEVNQNQKQVEQDIKVAIFTLMVEI... | 2.3.2.27 | null | calcium ion homeostasis [GO:0055074]; cellular response to estrogen stimulus [GO:0071391]; epithelial cell proliferation [GO:0050673]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of epithelial cell proliferation [GO:0050680]; positive regulation of gene expression [GO:0010628]; ... | cytosol [GO:0005829]; euchromatin [GO:0000791]; male germ cell nucleus [GO:0001673]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perichromatin fibrils [GO:0005726] | chromatin binding [GO:0003682]; estrogen response element binding [GO:0034056]; lysine-acetylated histone binding [GO:0070577]; nuclear receptor binding [GO:0016922]; p53 binding [GO:0002039]; protein kinase activity [GO:0004672]; signaling receptor binding [GO:0005102]; transcription coactivator activity [GO:0003713];... | PF00439;PF00628;PF00643; | 1.20.920.10;3.30.160.60;3.30.40.10; | null | PTM: Phosphorylated at Ser-768 by ATM kinase induces ubiquitination and degradation during DNA damage. {ECO:0000269|PubMed:24820418}.; PTM: Sumoylated. {ECO:0000250|UniProtKB:Q64127}.; PTM: Undergoes ubiquitination-mediated degradation in response to DNA damage. {ECO:0000269|PubMed:24820418}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21164480, ECO:0000269|PubMed:25593309, ECO:0000269|PubMed:32324863}. Cytoplasm {ECO:0000269|PubMed:21164480}. Mitochondrion {ECO:0000269|PubMed:32324863}. Note=Colocalizes with sites of active transcription. Predominantly nuclear. Translocated from nucleus to mitochondr... | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000269|PubMed:24820418, ECO:0000269|PubMed:32324863}; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Transcriptional coactivator that interacts with numerous nuclear receptors and coactivators and modulates the transcription of target genes. Interacts with chromatin depending on histone H3 modifications, having the highest affinity for histone H3 that is both unmodified at 'Lys-4' (H3K4me0) and acetylated at... | Homo sapiens (Human) |
O15165 | LRAD4_HUMAN | MPEAGFQATNAFTECKFTCTSGKCLYLGSLVCNQQNDCGDNSDEENCLLVTEHPPPGIFNSELEFAQIIIIVVVVTVMVVVIVCLLNHYKVSTRSFINRPNQSRRREDGLPQEGCLWPSDSAAPRLGASEIMHAPRSRDRFTAPSFIQRDRFSRFQPTYPYVQHEIDLPPTISLSDGEEPPPYQGPCTLQLRDPEQQMELNRESVRAPPNRTIFDSDLIDIAMYSGGPCPPSSNSGISASTCSSNGRMEGPPPTYSEVMGHHPGASFLHHQRSNAHRGSRLQFQQNNAESTIVPIKGKDRKPGNLV | null | null | negative regulation of cell migration [GO:0030336]; negative regulation of epithelial to mesenchymal transition [GO:0010719]; negative regulation of SMAD protein signal transduction [GO:0060392]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512] | early endosome membrane [GO:0031901]; Golgi membrane [GO:0000139]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020] | R-SMAD binding [GO:0070412] | PF00057; | 4.10.400.10; | PMEPA1 family | null | SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:24627487}; Single-pass membrane protein {ECO:0000269|PubMed:24627487}. | null | null | null | null | null | FUNCTION: Functions as a negative regulator of TGF-beta signaling and thereby probably plays a role in cell proliferation, differentiation, apoptosis, motility, extracellular matrix production and immunosuppression. In the canonical TGF-beta pathway, ZFYVE9/SARA recruits the intracellular signal transducer and transcri... | Homo sapiens (Human) |
O15169 | AXIN1_HUMAN | MNIQEQGFPLDLGASFTEDAPRPPVPGEEGELVSTDPRPASYSFCSGKGVGIKGETSTATPRRSDLDLGYEPEGSASPTPPYLKWAESLHSLLDDQDGISLFRTFLKQEGCADLLDFWFACTGFRKLEPCDSNEEKRLKLARAIYRKYILDNNGIVSRQTKPATKSFIKGCIMKQLIDPAMFDQAQTEIQATMEENTYPSFLKSDIYLEYTRTGSESPKVCSDQSSGSGTGKGISGYLPTLNEDEEWKCDQDMDEDDGRDAAPPGRLPQKLLLETAAPRVSSSRRYSEGREFRYGSWREPVNPYYVNAGYALAPATSAND... | null | null | activation of protein kinase activity [GO:0032147]; apoptotic process [GO:0006915]; axial mesoderm formation [GO:0048320]; canonical Wnt signaling pathway [GO:0060070]; cell development [GO:0048468]; cytoplasmic microtubule organization [GO:0031122]; dorsal/ventral axis specification [GO:0009950]; epigenetic programmin... | beta-catenin destruction complex [GO:0030877]; cell cortex [GO:0005938]; cell periphery [GO:0071944]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; lateral plasma membrane [GO:0016328]; microtubule cytoskeleton [GO:0015630]; nucleolus [GO:0005730]; nucleus [GO:0005634]; perinuclear reg... | armadillo repeat domain binding [GO:0070016]; beta-catenin binding [GO:0008013]; enzyme binding [GO:0019899]; I-SMAD binding [GO:0070411]; identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090]; p53 binding [GO:0002039]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO... | PF16646;PF08833;PF00778;PF00615; | 1.10.196.10;2.40.240.130;1.10.167.10; | null | PTM: Phosphorylation and dephosphorylation of AXIN1 regulates assembly and function of the beta-catenin complex. Phosphorylated by CK1 and GSK3B. Dephosphorylated by PPP1CA and PPP2CA. Phosphorylation by CK1 enhances binding of GSK3B to AXIN1. {ECO:0000269|PubMed:17318175, ECO:0000269|PubMed:9920888}.; PTM: ADP-ribosyl... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16601693}. Nucleus {ECO:0000269|PubMed:17210684}. Membrane {ECO:0000250|UniProtKB:O35625}. Cell membrane {ECO:0000250|UniProtKB:O35625}. Note=MACF1 is required for its translocation to cell membrane (By similarity). On UV irradiation, translocates to the nucleus and c... | null | null | null | null | null | FUNCTION: Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling (PubMed:12192039, PubMed:27098453, PubMed:28829046). Controls dorsoventral patterning via two opposing effects; down-regulates CTNNB1 to inhibit the ... | Homo sapiens (Human) |
O15173 | PGRC2_HUMAN | MAAGDGDVKLGTLGSGSESSNDGGSESPGDAGAAAEGGGWAAAALALLTGGGEMLLNVALVALVLLGAYRLWVRWGRRGLGAGAGAGEESPATSLPRMKKRDFSLEQLRQYDGSRNPRILLAVNGKVFDVTKGSKFYGPAGPYGIFAGRDASRGLATFCLDKDALRDEYDDLSDLNAVQMESVREWEMQFKEKYDYVGRLLKPGEEPSEYTDEEDTKDHNKQD | null | null | adipose tissue development [GO:0060612] | endomembrane system [GO:0012505]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nucleoplasm [GO:0005654] | heme binding [GO:0020037]; heme transmembrane transporter activity [GO:0015232]; nuclear steroid receptor activity [GO:0003707]; steroid binding [GO:0005496] | PF00173; | 3.10.120.10; | Cytochrome b5 family, MAPR subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:23793472}; Single-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000269|PubMed:27754849, ECO:0000269|PubMed:28111073}. Endoplasmic reticulum {ECO:0000269|PubMed:27754849}. Secreted {ECO:0000269|PubMed:37453717}. | null | null | null | null | null | FUNCTION: Required for the maintenance of uterine histoarchitecture and normal female reproductive lifespan (By similarity). May serve as a universal non-classical progesterone receptor in the uterus (Probable). Intracellular heme chaperone required for delivery of labile, or signaling heme, to the nucleus (By similari... | Homo sapiens (Human) |
O15178 | TBXT_HUMAN | MSSPGTESAGKSLQYRVDHLLSAVENELQAGSEKGDPTERELRVGLEESELWLRFKELTNEMIVTKNGRRMFPVLKVNVSGLDPNAMYSFLLDFVAADNHRWKYVNGEWVPGGKPEPQAPSCVYIHPDSPNFGAHWMKAPVSFSKVKLTNKLNGGGQIMLNSLHKYEPRIHIVRVGGPQRMITSHCFPETQFIAVTAYQNEEITALKIKYNPFAKAFLDAKERSDHKEMMEEPGDSQQPGYSQWGWLLPGTSTLCPPANPHPQFGGALSLPSTHSCDRYPTLRSHRSSPYPSPYAHRNNSPTYSDNSPACLSMLQSHDNW... | null | null | anterior/posterior axis specification, embryo [GO:0008595]; cardiac muscle cell myoblast differentiation [GO:0060379]; cell fate specification [GO:0001708]; heart morphogenesis [GO:0003007]; mesoderm development [GO:0007498]; mesoderm formation [GO:0001707]; negative regulation of DNA-binding transcription factor activ... | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; 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]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-speci... | PF00907; | 2.60.40.820; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22611028, ECO:0000269|PubMed:24253444}. | null | null | null | null | null | FUNCTION: Involved in the transcriptional regulation of genes required for mesoderm formation and differentiation. Binds to a palindromic T site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence and activates gene transcription when bound to such a site. {ECO:0000250|UniProtKB:P20293}. | Homo sapiens (Human) |
O15182 | CETN3_HUMAN | MSLALRSELVVDKTKRKKRRELSEEQKQEIKDAFELFDTDKDEAIDYHELKVAMRALGFDVKKADVLKILKDYDREATGKITFEDFNEVVTDWILERDPHEEILKAFKLFDDDDSGKISLRNLRRVARELGENMSDEELRAMIEEFDKDGDGEINQEEFIAIMTGDI | null | null | cell division [GO:0051301]; centrosome cycle [GO:0007098]; mRNA transport [GO:0051028]; protein transport [GO:0015031] | centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; microtubule organizing center [GO:0005815]; nuclear pore nuclear basket [GO:0044615]; nucleolus [GO:0005730]; photoreceptor connecting cilium [GO:0032391]; transcription export complex 2 [GO:0070390] | calcium ion binding [GO:0005509]; G-protein beta/gamma-subunit complex binding [GO:0031683]; microtubule binding [GO:0008017] | PF13499; | 1.10.238.10; | Centrin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:9256449}. Nucleus, nucleolus {ECO:0000303|PubMed:22307388}. Nucleus envelope {ECO:0000269|PubMed:23591820}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:23591820}. Cytoplasm, cy... | null | null | null | null | null | FUNCTION: Plays a fundamental role in microtubule-organizing center structure and function.; FUNCTION: As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores. {ECO:0000269|PubMed:22307388, ECO:0000305|PubMed:23591820}. | Homo sapiens (Human) |
O15194 | CTDSL_HUMAN | MDGPAIITQVTNPKEDEGRLPGAGEKASQCNVSLKKQRSRSILSSFFCCFRDYNVEAPPPSSPSVLPPLVEENGGLQKGDQRQVIPIPSPPAKYLLPEVTVLDYGKKCVVIDLDETLVHSSFKPISNADFIVPVEIDGTIHQVYVLKRPHVDEFLQRMGQLFECVLFTASLAKYADPVADLLDRWGVFRARLFRESCVFHRGNYVKDLSRLGRELSKVIIVDNSPASYIFHPENAVPVQSWFDDMTDTELLDLIPFFEGLSREDDVYSMLHRLCNR | 3.1.3.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000250}; | negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of protein phosphorylation [GO:0001933] | extracellular exosome [GO:0070062]; nucleus [GO:0005634] | metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]; RNA polymerase II CTD heptapeptide repeat phosphatase activity [GO:0008420] | PF03031; | 3.40.50.1000; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-... | null | null | null | null | FUNCTION: Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells (By similarity). Preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residue repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A... | Homo sapiens (Human) |
O15195 | VILL_HUMAN | MDISKGLPGMQGGLHIWISENRKMVPVPEGAYGNFFEEHCYVILHVPQSPKATQGASSDLHYWVGKQAGAEAQGAAEAFQQRLQDELGGQTVLHREAQGHESDCFCSYFRPGIIYRKGGLASDLKHVETNLFNIQRLLHIKGRKHVSATEVELSWNSFNKGDIFLLDLGKMMIQWNGPKTSISEKARGLALTYSLRDRERGGGRAQIGVVDDEAKAPDLMQIMEAVLGRRVGSLRAATPSKDINQLQKANVRLYHVYEKGKDLVVLELATPPLTQDLLQEEDFYILDQGGFKIYVWQGRMSSLQERKAAFSRAVGFIQAK... | null | null | actin filament severing [GO:0051014]; actin polymerization or depolymerization [GO:0008154]; barbed-end actin filament capping [GO:0051016] | actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737] | actin filament binding [GO:0051015]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; structural constituent of cytoskeleton [GO:0005200] | PF00626;PF02209; | 3.40.20.10;1.10.950.10; | Villin/gelsolin family | null | null | null | null | null | null | null | FUNCTION: Possible tumor suppressor. | Homo sapiens (Human) |
O15197 | EPHB6_HUMAN | MATEGAAQLGNRVAGMVCSLWVLLLVSSVLALEEVLLDTTGETSEIGWLTYPPGGWDEVSVLDDQRRLTRTFEACHVAGAPPGTGQDNWLQTHFVERRGAQRAHIRLHFSVRACSSLGVSGGTCRETFTLYYRQAEEPDSPDSVSSWHLKRWTKVDTIAADESFPSSSSSSSSSSSAAWAVGPHGAGQRAGLQLNVKERSFGPLTQRGFYVAFQDTGACLALVAVRLFSYTCPAVLRSFASFPETQASGAGGASLVAAVGTCVAHAEPEEDGVGGQAGGSPPRLHCNGEGKWMVAVGGCRCQPGYQPARGDKACQACPRG... | null | null | axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013] | cytosol [GO:0005829]; dendrite [GO:0030425]; extracellular region [GO:0005576]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ephrin receptor activity [GO:0005003]; signaling receptor activity [GO:0038023]; transmembrane-ephrin receptor activity [GO:0005005] | PF14575;PF01404;PF07699;PF00041;PF07714;PF07647; | 2.60.40.1770;2.60.120.260;2.60.40.10;1.10.150.50;1.10.510.10;2.10.50.10; | Protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily | PTM: Ligand-binding increases phosphorylation on tyrosine residues. Phosphorylation on tyrosine residues is mediated by transphosphorylation by the catalytically active EPHB1 in a ligand-independent manner. Tyrosine phosphorylation of the receptor may act as a switch on the functional transition from cell adhesion/attr... | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Kinase-defective receptor for members of the ephrin-B family. Binds to ephrin-B1 and ephrin-B2. Modulates cell adhesion and migration by exerting both positive and negative effects upon stimulation with ephrin-B2. Inhibits JNK activation, T-cell receptor-induced IL-2 secretion and CD25 expression upon stimula... | Homo sapiens (Human) |
O15198 | SMAD9_HUMAN | MHSTTPISSLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDSLVKKLKKKKGAMDELERALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYRRVETPVLPPVLVPRHSEYNPQLSLLAKFRSASLHSEPLMPHNATYPDSFQQPPCSALPPSPSHAFSQSPCTASYPHSPGSPSEPESPYQHSVDTPPLPYHATEASETQSGQPVDATADRHVVLSIPNGDFRPVCYEEPQHWCSVAYYELNNRVGETFQASSRSVLIDGFTDPSNNRNRFCLGLLSNVN... | null | null | anatomical structure morphogenesis [GO:0009653]; BMP signaling pathway [GO:0030509]; cell differentiation [GO:0030154]; cellular response to BMP stimulus [GO:0071773]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; SMAD protein sign... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; heteromeric SMAD protein complex [GO:0071144]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SMAD protein complex [GO:0071141] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; I-SMAD binding [GO:0070411]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF03165;PF03166; | 2.60.200.10;3.90.520.10; | Dwarfin/SMAD family | PTM: Phosphorylated on serine by BMP (bone morphogenetic proteins) type 1 receptor kinase. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=In the cytoplasm in the absence of ligand. Migration to the nucleus when complexed with SMAD4 (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD9 is a receptor-regulated SMAD (R-SMAD). | Homo sapiens (Human) |
O15204 | ADEC1_HUMAN | MLRGISQLPAVATMSWVLLPVLWLIVQTQAIAIKQTPELTLHEIVCPKKLHILHKREIKNNQTEKHGKEERYEPEVQYQMILNGEEIILSLQKTKHLLGPDYTETLYSPRGEEITTKPENMEHCYYKGNILNEKNSVASISTCDGLRGYFTHHHQRYQIKPLKSTDEKEHAVFTSNQEEQDPANHTCGVKSTDGKQGPIRISRSLKSPEKEDFLRAQKYIDLYLVLDNAFYKNYNENLTLIRSFVFDVMNLLNVIYNTIDVQVALVGMEIWSDGDKIKVVPSASTTFDNFLRWHSSNLGKKIHDHAQLLSGISFNNRRVG... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | immune response [GO:0006955]; negative regulation of cell adhesion [GO:0007162]; proteolysis [GO:0006508] | collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576] | metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270] | PF01562;PF01421; | 3.40.390.10;4.10.70.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: May play an important role in the control of the immune response and during pregnancy. {ECO:0000250}. | Homo sapiens (Human) |
O15205 | UBD_HUMAN | MAPNASCLCVHVRSEEWDLMTFDANPYDSVKKIKEHVRSKTKVPVQDQVLLLGSKILKPRRSLSSYGIDKEKTIHLTLKVVKPSDEELPLFLVESGDEAKRHLLQVRRSSSVAQVKAMIETKTGIIPETQIVTCNGKRLEDGKMMADYGIRKGNLLFLACYCIGG | null | null | aggresome assembly [GO:0070842]; myeloid dendritic cell differentiation [GO:0043011]; positive regulation of apoptotic process [GO:0043065]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; protein modification by small protein conjugation [GO:0032446]; protein ubiquitination [GO:0016567]; p... | aggresome [GO:0016235]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; fibrillar center [GO:0001650]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | proteasome binding [GO:0070628] | PF00240; | null | null | PTM: Can be acetylated. {ECO:0000269|PubMed:19033385}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12730673, ECO:0000269|PubMed:19033385}. Cytoplasm {ECO:0000250}. Note=Accumulates in aggresomes under proteasome inhibition conditions. | null | null | null | null | null | FUNCTION: Ubiquitin-like protein modifier which can be covalently attached to target protein and subsequently leads to their degradation by the 26S proteasome, in a NUB1-dependent manner. Probably functions as a survival factor. Conjugation ability activated by UBA6. Promotes the expression of the proteasome subunit be... | Homo sapiens (Human) |
O15209 | ZBT22_HUMAN | MEPSPLSPSGAALPLPLSLAPPPLPLPAAAVVHVSFPEVTSALLESLNQQRLQGQLCDVSIRVQGREFRAHRAVLAASSPYFHDQVLLKGMTSISLPSVMDPGAFETVLASAYTGRLSMAAADIVNFLTVGSVLQMWHIVDKCTELLREGRASATTTITTAAATSVTVPGAGVPSGSGGTVAPATMGSARSHASSRASENQSPSSSNYFSPRESTDFSSSSQEAFAASAVGSGERRGGGPVFPAPVVGSGGATSGKLLLEADELCDDGGDGRGAVVPGAGLRRPTYTPPSIMPQKHWVYVKRGGNCPAPTPLVPQDPDLE... | null | null | regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837] | PF00651; | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: May be involved in transcriptional regulation. | Homo sapiens (Human) |
O15211 | RGL2_HUMAN | MLPRPLRLLLDTSPPGGVVLSSFRSRDPEEGGGPGGLVVGGGQEEEEEEEEEAPVSVWDEEEDGAVFTVTSRQYRPLDPLVPMPPPRSSRRLRAGTLEALVRHLLDTRTSGTDVSFMSAFLATHRAFTSTPALLGLMADRLEALESHPTDELERTTEVAISVLSTWLASHPEDFGSEAKGQLDRLESFLLQTGYAAGKGVGGGSADLIRNLRSRVDPQAPDLPKPLALPGDPPADPTDVLVFLADHLAEQLTLLDAELFLNLIPSQCLGGLWGHRDRPGHSHLCPSVRATVTQFNKVAGAVVSSVLGATSTGEGPGEVTI... | null | null | negative regulation of cardiac muscle cell apoptotic process [GO:0010667]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; Ras protein signal transduction [GO:0007265]; regulation of Ral protein signal transduction [GO:0032485] | cytosol [GO:0005829]; plasma membrane [GO:0005886] | guanyl-nucleotide exchange factor activity [GO:0005085] | PF00788;PF00617;PF00618; | 1.10.840.10;1.20.870.10; | null | null | null | null | null | null | null | null | FUNCTION: Probable guanine nucleotide exchange factor. Putative effector of Ras and/or Rap. Associates with the GTP-bound form of Rap 1A and H-Ras in vitro (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
O15212 | PFD6_HUMAN | MAELIQKKLQGEVEKYQQLQKDLSKSMSGRQKLEAQLTENNIVKEELALLDGSNVVFKLLGPVLVKQELGEARATVGKRLDYITAEIKRYESQLRDLERQSEQQRETLAQLQQEFQRAQAAKAGAPGKA | null | null | chaperone-mediated protein complex assembly [GO:0051131]; chaperone-mediated protein folding [GO:0061077]; negative regulation of amyloid fibril formation [GO:1905907]; protein folding [GO:0006457]; protein stabilization [GO:0050821] | cytoplasm [GO:0005737]; prefoldin complex [GO:0016272]; protein folding chaperone complex [GO:0101031]; RPAP3/R2TP/prefoldin-like complex [GO:1990062] | amyloid-beta binding [GO:0001540]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082] | PF01920; | 1.10.287.370; | Prefoldin subunit beta family | null | null | null | null | null | null | null | FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. {ECO:0000269|PubMed:9630229}. | Homo sapiens (Human) |
O15213 | WDR46_HUMAN | METAPKPGKDVPPKKDKLQTKRKKPRRYWEEETVPTTAGASPGPPRNKKNRELRPQRPKNAYILKKSRISKKPQVPKKPREWKNPESQRGLSGTQDPFPGPAPVPVEVVQKFCRIDKSRKLPHSKAKTRSRLEVAEAEEEETSIKAARSELLLAEEPGFLEGEDGEDTAKICQADIVEAVDIASAAKHFDLNLRQFGPYRLNYSRTGRHLAFGGRRGHVAALDWVTKKLMCEINVMEAVRDIRFLHSEALLAVAQNRWLHIYDNQGIELHCIRRCDRVTRLEFLPFHFLLATASETGFLTYLDVSVGKIVAALNARAGRL... | null | null | maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; ribosomal small subunit biogenesis [GO:0042274] | 90S preribosome [GO:0030686]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; small-subunit processome [GO:0032040] | RNA binding [GO:0003723] | PF08149;PF00400; | 2.130.10.10; | null | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:23848194, ECO:0000269|PubMed:34516797}. | null | null | null | null | null | FUNCTION: Scaffold component of the nucleolar structure. Required for localization of DDX21 and NCL to the granular compartment of the nucleolus (PubMed:23848194). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucl... | Homo sapiens (Human) |
O15217 | GSTA4_HUMAN | MAARPKLHYPNGRGRMESVRWVLAAAGVEFDEEFLETKEQLYKLQDGNHLLFQQVPMVEIDGMKLVQTRSILHYIADKHNLFGKNLKERTLIDMYVEGTLDLLELLIMHPFLKPDDQQKEVVNMAQKAIIRYFPVFEKILRGHGQSFLVGNQLSLADVILLQTILALEEKIPNILSAFPFLQEYTVKLSNIPTIKRFLEPGSKKKPPPDEIYVRTVYNIFRP | 2.5.1.18 | null | glutathione metabolic process [GO:0006749]; xenobiotic metabolic process [GO:0006805] | cytosol [GO:0005829] | glutathione transferase activity [GO:0004364]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803] | PF14497;PF02798; | 1.20.1050.10;3.40.30.10; | GST superfamily, Alpha family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000269|PubMed:10329152, ECO:0000269|PubMed:20085333}; | null | null | null | null | FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. This isozyme has a high catalytic efficiency with 4-hydroxyalkenals such as 4-hydroxynonenal (4-HNE). {ECO:0000269|PubMed:10329152, ECO:0000269|PubMed:20085333}. | Homo sapiens (Human) |
O15226 | NKRF_HUMAN | MEKILQMAEGIDIGEMPSYDLVLSKPSKGQKRHLSTCDGQNPPKKQAGSKFHARPRFEPVHFVASSSKDERQEDPYGPQTKEVNEQTHFASMPRDIYQDYTQDSFSIQDGNSQYCDSSGFILTKDQPVTANMYFDSGNPAPSTTSQQANSQSTPEPSPSQTFPESVVAEKQYFIEKLTATIWKNLSNPEMTSGSDKINYTYMLTRCIQACKTNPEYIYAPLKEIPPADIPKNKKLLTDGYACEVRCQNIYLTTGYAGSKNGSRDRATELAVKLLQKRIEVRVVRRKFKHTFGEDLVVCQIGMSSYEFPPALKPPEDLVVL... | null | null | negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of transcription by RNA polymerase II [GO:0045944] | nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | ATPase activator activity [GO:0001671]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; RNA binding [GO:0003723]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF01585;PF01424; | 3.30.160.20;3.30.1370.50; | null | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}. | null | null | null | null | null | FUNCTION: Enhances the ATPase activity of DHX15 by acting like a brace that tethers mobile sections of DHX15 together, stabilizing a functional conformation with high RNA affinity of DHX15 (PubMed:12381793). Involved in the constitutive silencing of the interferon beta promoter, independently of the virus-induced signa... | Homo sapiens (Human) |
O15228 | GNPAT_HUMAN | MESSSSSNSYFSVGPTSPSAVVLLYSKELKKWDEFEDILEERRHVSDLKFAMKCYTPLVYKGITPCKPIDIKCSVLNSEEIHYVIKQLSKESLQSVDVLREEVSEILDEMSHKLRLGAIRFCAFTLSKVFKQIFSKVCVNEEGIQKLQRAIQEHPVVLLPSHRSYIDFLMLSFLLYNYDLPVPVIAAGMDFLGMKMVGELLRMSGAFFMRRTFGGNKLYWAVFSEYVKTMLRNGYAPVEFFLEGTRSRSAKTLTPKFGLLNIVMEPFFKREVFDTYLVPISISYDKILEETLYVYELLGVPKPKESTTGLLKARKILSEN... | 2.3.1.42 | null | cerebellum morphogenesis [GO:0021587]; ether lipid biosynthetic process [GO:0008611]; fatty acid metabolic process [GO:0006631]; glycerol-3-phosphate metabolic process [GO:0006072]; membrane organization [GO:0061024]; paranodal junction assembly [GO:0030913]; phosphatidic acid biosynthetic process [GO:0006654]; phospho... | cytosol [GO:0005829]; membrane [GO:0016020]; mitochondrial membrane [GO:0031966]; peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; plasma membrane [GO:0005886] | glycerol-3-phosphate O-acyltransferase activity [GO:0004366]; glycerone-phosphate O-acyltransferase activity [GO:0016287] | PF01553;PF19277; | null | GPAT/DAPAT family | null | SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:15687349}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9ES71}; Matrix side {ECO:0000250|UniProtKB:Q9ES71}. Note=Exclusively localized to the lumenal side of the peroxisomal membrane. {ECO:0000250|UniProtKB:Q9ES71}. | CATALYTIC ACTIVITY: Reaction=an acyl-CoA + dihydroxyacetone phosphate = a 1-acylglycerone 3-phosphate + CoA; Xref=Rhea:RHEA:17657, ChEBI:CHEBI:57287, ChEBI:CHEBI:57534, ChEBI:CHEBI:57642, ChEBI:CHEBI:58342; EC=2.3.1.42; Evidence={ECO:0000269|PubMed:10395968, ECO:0000269|PubMed:11152660, ECO:0000269|PubMed:15687349}; Ph... | null | PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism. {ECO:0000269|PubMed:11152660, ECO:0000269|PubMed:15687349}. | null | null | FUNCTION: Dihydroxyacetonephosphate acyltransferase catalyzing the first step in the biosynthesis of plasmalogens, a subset of phospholipids that differ from other glycerolipids by having an alkyl chain attached through a vinyl ether linkage at the sn-1 position of the glycerol backbone, and which unique physical prope... | Homo sapiens (Human) |
O15229 | KMO_HUMAN | MDSSVIQRKKVAVIGGGLVGSLQACFLAKRNFQIDVYEAREDTRVATFTRGRSINLALSHRGRQALKAVGLEDQIVSQGIPMRARMIHSLSGKKSAIPYGTKSQYILSVSRENLNKDLLTAAEKYPNVKMHFNHRLLKCNPEEGMITVLGSDKVPKDVTCDLIVGCDGAYSTVRSHLMKKPRFDYSQQYIPHGYMELTIPPKNGDYAMEPNYLHIWPRNTFMMIALPNMNKSFTCTLFMPFEEFEKLLTSNDVVDFFQKYFPDAIPLIGEKLLVQDFFLLPAQPMISVKCSSFHFKSHCVLLGDAAHAIVPFFGQGMNAG... | 1.14.13.9 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-Rule:MF_03018, ECO:0000269|PubMed:10672018, ECO:0000269|PubMed:29429898}; | 'de novo' NAD biosynthetic process from tryptophan [GO:0034354]; anthranilate metabolic process [GO:0043420]; cellular response to interleukin-1 [GO:0071347]; cellular response to lipopolysaccharide [GO:0071222]; kynurenic acid biosynthetic process [GO:0034276]; kynurenine metabolic process [GO:0070189]; L-kynurenine m... | cytosol [GO:0005829]; extracellular space [GO:0005615]; mitochondrial outer membrane [GO:0005741] | FAD binding [GO:0071949]; flavin adenine dinucleotide binding [GO:0050660]; kynurenine 3-monooxygenase activity [GO:0004502]; NAD(P)H oxidase H2O2-forming activity [GO:0016174] | PF01494; | 3.50.50.60; | Aromatic-ring hydroxylase family, KMO subfamily | null | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03018, ECO:0000269|PubMed:9237672}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03018, ECO:0000269|PubMed:9237672}. | CATALYTIC ACTIVITY: Reaction=H(+) + L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine + H2O + NADP(+); Xref=Rhea:RHEA:20545, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:57959, ChEBI:CHEBI:58125, ChEBI:CHEBI:58349; EC=1.14.13.9; Evidence={ECO:0000255|HAMAP-Rule:MF_03018, ECO:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=24.1 uM for L-kynurenine {ECO:0000269|PubMed:10672018, ECO:0000269|PubMed:23575632, ECO:0000269|PubMed:9237672}; KM=2 uM for L-kynurenine {ECO:0000269|PubMed:26752518}; KM=78 uM for L-kynurenine {ECO:0000269|PubMed:26752518}; Vmax=8.5 umol/min/mg enzyme {ECO:000026... | PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 1/3. {ECO:0000255|HAMAP-Rule:MF_03018}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:10672018, ECO:0000269|PubMed:9237672}; | null | FUNCTION: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn) (PubMed:23575632, PubMed:26752518, PubMed:28604669, PubMed:29208702, PubMed:29429898). Required for synthesis of quinolinic acid, a neurotoxic NMDA receptor antagonist and potential endogenous inhibitor of NMDA recep... | Homo sapiens (Human) |
O15230 | LAMA5_HUMAN | MAKRLCAGSALCVRGPRGPAPLLLVGLALLGAARAREEAGGGFSLHPPYFNLAEGARIAASATCGEEAPARGSPRPTEDLYCKLVGGPVAGGDPNQTIRGQYCDICTAANSNKAHPASNAIDGTERWWQSPPLSRGLEYNEVNVTLDLGQVFHVAYVLIKFANSPRPDLWVLERSMDFGRTYQPWQFFASSKRDCLERFGPQTLERITRDDAAICTTEYSRIVPLENGEIVVSLVNGRPGAMNFSYSPLLREFTKATNVRLRFLRTNTLLGHLMGKALRDPTVTRRYYYSIKDISIGGRCVCHGHADACDAKDPTDPFRL... | null | null | branching involved in salivary gland morphogenesis [GO:0060445]; branching involved in ureteric bud morphogenesis [GO:0001658]; cell migration [GO:0016477]; cilium assembly [GO:0060271]; hair follicle development [GO:0001942]; integrin-mediated signaling pathway [GO:0007229]; lung development [GO:0030324]; morphogenesi... | basement membrane [GO:0005604]; collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular matrix of synaptic cleft [GO:0098965]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; laminin-10 complex [GO:0043259]; lamini... | integrin binding [GO:0005178] | PF00052;PF00053;PF00054;PF02210;PF06008;PF06009;PF00055; | 2.60.120.200;2.60.120.260;2.10.25.10;2.170.300.10; | null | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component. | null | null | null | null | null | FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Plays a role in the regulation of skeletogenesis, through a mechanism that invol... | Homo sapiens (Human) |
O15231 | ZN185_HUMAN | MSISALGGRTKGKPLPPGEEERNNVLKQMKVRTTLKGDKSWITKQDESEGRTIELPSGRSRATSFSSAGEVPKPRPPSTRAPTGYIIRGVFTKPIDSSSQPQQQFPKANGTPKSAASLVRTANAGPPRPSSSGYKMTTEDYKKLAPYNIRRSSTSGDTEEEEEEEVVPFSSDEQKRRSEAASGVLRRTAPREHSYVLSAAKKSTGPTQETQAPFIAKRVEVVEEDGPSEKSQDPPALARSTPGSNSADGGRTKASRAIWIECLPSMPSPAGSQELSSRGEEIVRLQILTPRAGLRLVAPDVEGMRSSPGNKDKEAPCSRE... | null | null | null | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; focal adhesion [GO:0005925] | zinc ion binding [GO:0008270] | null | 2.10.110.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16799630}. Cell junction, focal adhesion {ECO:0000269|PubMed:16799630}. | null | null | null | null | null | FUNCTION: May be involved in the regulation of cellular proliferation and/or differentiation. | Homo sapiens (Human) |
O15232 | MATN3_HUMAN | MPRPAPARRLPGLLLLLWPLLLLPSAAPDPVARPGFRRLETRGPGGSPGRRPSPAAPDGAPASGTSEPGRARGAGVCKSRPLDLVFIIDSSRSVRPLEFTKVKTFVSRIIDTLDIGPADTRVAVVNYASTVKIEFQLQAYTDKQSLKQAVGRITPLSTGTMSGLAIQTAMDEAFTVEAGAREPSSNIPKVAIIVTDGRPQDQVNEVAARAQASGIELYAVGVDRADMASLKMMASEPLEEHVFYVETYGVIEKLSSRFQETFCALDPCVLGTHQCQHVCISDGEGKHHCECSQGYTLNADKKTCSALDRCALNTHGCEHI... | null | null | cartilage development [GO:0051216]; extracellular matrix organization [GO:0030198]; skeletal system development [GO:0001501] | collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; 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 {ECO:0000250|UniProtKB:O35701}. | null | null | null | null | null | FUNCTION: Major component of the extracellular matrix of cartilage and may play a role in the formation of extracellular filamentous networks. | Homo sapiens (Human) |
O15234 | CASC3_HUMAN | MADRRRQRASQDTEDEESGASGSDSGGSPLRGGGSCSGSAGGGGSGSLPSQRGGRTGALHLRRVESGGAKSAEESECESEDGIEGDAVLSDYESAEDSEGEEGEYSEEENSKVELKSEANDAVNSSTKEEKGEEKPDTKSTVTGERQSGDGQESTEPVENKVGKKGPKHLDDDEDRKNPAYIPRKGLFFEHDLRGQTQEEEVRPKGRQRKLWKDEGRWEHDKFREDEQAPKSRQELIALYGYDIRSAHNPDDIKPRRIRKPRYGSPPQRDPNWNGERLNKSHRHQGLGGTLPPRTFINRNAAGTGRMSAPRNYSRSGGFK... | null | null | intracellular mRNA localization [GO:0008298]; mRNA export from nucleus [GO:0006406]; mRNA splicing, via spliceosome [GO:0000398]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:2000622]; regulation o... | cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; dendrite [GO:0030425]; exon-exon junction complex [GO:0035145]; nuclear membrane [GO:0031965]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; U2-type catalytic step 1 spliceosome [GO... | enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]; ubiquitin protein ligase binding [GO:0031625] | PF09405; | null | CASC3 family | PTM: ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination. {ECO:0000269|PubMed:21478859}.; PTM: Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its degradation. {ECO:0000269|PubMed:21478859}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12080473}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8K3W3}. Nucleus {ECO:0000269|PubMed:12080473, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961}. Nucleus speckle {ECO:0000269|PubMed:16170325}. Cytoplasm, Stress granule {ECO:0000269|PubMed:17652... | null | null | null | null | null | FUNCTION: Required for pre-mRNA splicing as component of the spliceosome (PubMed:28502770, PubMed:29301961). Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear... | Homo sapiens (Human) |
O15239 | NDUA1_HUMAN | MWFEILPGLSVMGVCLLIPGLATAYIHRFTNGGKEKRVAHFGYHWSLMERDRRISGVDRYYVSKGLENID | null | null | aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776] | mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739] | NADH dehydrogenase (ubiquinone) activity [GO:0008137] | PF15879; | null | Complex I NDUFA1 subunit family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000305}. | null | null | null | null | null | FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. ... | Homo sapiens (Human) |
O15240 | VGF_HUMAN | MKALRLSASALFCLLLINGLGAAPPGRPEAQPPPLSSEHKEPVAGDAVPGPKDGSAPEVRGARNSEPQDEGELFQGVDPRALAAVLLQALDRPASPPAPSGSQQGPEEEAAEALLTETVRSQTHSLPAPESPEPAAPPRPQTPENGPEASDPSEELEALASLLQELRDFSPSSAKRQQETAAAETETRTHTLTRVNLESPGPERVWRASWGEFQARVPERAPLPPPAPSQFQARMPDSGPLPETHKFGEGVSSPKTHLGEALAPLSKAYQGVAAPFPKARRPESALLGGSEAGERLLQQGLAQVEAGRRQAEATRQAAAQ... | null | null | carbohydrate homeostasis [GO:0033500]; defense response to bacterium [GO:0042742]; generation of precursor metabolites and energy [GO:0006091]; glucose homeostasis [GO:0042593]; insulin secretion [GO:0030073]; ovarian follicle development [GO:0001541]; regulation of neuronal synaptic plasticity [GO:0048168]; regulation... | cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum lumen [GO:0005788]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; neuronal cell body [GO:0043025]; transport vesicle [GO:0030133] | growth factor activity [GO:0008083]; hormone activity [GO:0005179]; neuropeptide hormone activity [GO:0005184] | null | null | null | PTM: Multiple peptides are derived from VGF, with activities in synaptic plasticity, antidepression, penile erection, autonomic activation, and increases in energy expenditure. {ECO:0000250}. | SUBCELLULAR LOCATION: [Neurosecretory protein VGF]: Secreted {ECO:0000269|PubMed:19194657}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:19194657}. Note=Stored in secretory vesicles and then secreted, NERP peptides colocalize with vasopressin in the storage granules of hypothalamus. | null | null | null | null | null | FUNCTION: [Neurosecretory protein VGF]: Secreted polyprotein that is packaged and proteolytically processed by prohormone convertases PCSK1 and PCSK2 in a cell-type-specific manner (By similarity). VGF and peptides derived from its processing play many roles in neurogenesis and neuroplasticity associated with learning,... | Homo sapiens (Human) |
O15243 | OBRG_HUMAN | MAGVKALVALSFSGAIGLTFLMLGCALEDYGVYWPLFVLIFHAISPIPHFIAKRVTYDSDATSSACRELAYFFTTGIVVSAFGFPVILARVAVIKWGACGLVLAGNAVIFLTIQGFFLIFGRGDDFSWEQW | null | null | late endosome to vacuole transport via multivesicular body sorting pathway [GO:0032511]; negative regulation of growth hormone receptor signaling pathway [GO:0060400]; negative regulation of protein localization to cell surface [GO:2000009]; negative regulation of receptor signaling pathway via JAK-STAT [GO:0046426]; p... | endosome [GO:0005768]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139] | signaling receptor binding [GO:0005102] | PF04133; | null | OB-RGRP/VPS55 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endosome membrane {ECO:0000250}. | null | null | null | null | null | FUNCTION: Negatively regulates leptin receptor (LEPR) cell surface expression, and thus decreases response to leptin. Negatively regulates growth hormone (GH) receptor cell surface expression in liver. May play a role in liver resistance to GH during periods of reduced nutrient availability. {ECO:0000269|PubMed:1804272... | Homo sapiens (Human) |
O15244 | S22A2_HUMAN | MPTTVDDVLEHGGEFHFFQKQMFFLLALLSATFAPIYVGIVFLGFTPDHRCRSPGVAELSLRCGWSPAEELNYTVPGPGPAGEASPRQCRRYEVDWNQSTFDCVDPLASLDTNRSRLPLGPCRDGWVYETPGSSIVTEFNLVCANSWMLDLFQSSVNVGFFIGSMSIGYIADRFGRKLCLLTTVLINAAAGVLMAISPTYTWMLIFRLIQGLVSKAGWLIGYILITEFVGRRYRRTVGIFYQVAYTVGLLVLAGVAYALPHWRWLQFTVSLPNFFFLLYYWCIPESPRWLISQNKNAEAMRIIKHIAKKNGKSLPASLQR... | null | null | acetylcholine transport [GO:0015870]; activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; amine transport [GO:0015837]; amino acid import across plasma membrane [GO:0089718]; body fluid secretion [GO:0007589]; cellular detoxification [GO:1990748]; choline transport [GO:0015871... | apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; plasma membrane [GO:0005886]; presynapse [GO:0098793] | acetylcholine transmembrane transporter activity [GO:0005277]; amine transmembrane transporter activity [GO:0005275]; choline transmembrane transporter activity [GO:0015220]; efflux transmembrane transporter activity [GO:0015562]; L-amino acid transmembrane transporter activity [GO:0015179]; L-arginine transmembrane tr... | PF00083; | 1.20.1250.20; | Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family | PTM: Tyrosine phosphorylated by tyrosine-protein kinase YES1. {ECO:0000269|PubMed:26979622}. | SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000250|UniProtKB:Q9R0W2}; Multi-pass membrane protein {ECO:0000305}. Basal cell membrane {ECO:0000269|PubMed:35307651}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:15817714, ECO:0000269|PubMed:9260930}; Multi-pass membrane pro... | CATALYTIC ACTIVITY: Reaction=(R)-noradrenaline(out) = (R)-noradrenaline(in); Xref=Rhea:RHEA:73871, ChEBI:CHEBI:72587; Evidence={ECO:0000269|PubMed:16581093, ECO:0000269|PubMed:9687576}; CATALYTIC ACTIVITY: Reaction=(R)-adrenaline(out) = (R)-adrenaline(in); Xref=Rhea:RHEA:73875, ChEBI:CHEBI:71406; Evidence={ECO:0000269|... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=74 uM for cyclo(his-pro) {ECO:0000269|PubMed:17460754}; KM=80 uM for serotonin {ECO:0000269|PubMed:9687576}; KM=290 uM for serotonin {ECO:0000269|PubMed:16581093}; KM=130 uM for salsolinol {ECO:0000269|PubMed:17460754}; KM=150 uM for acetylcholine {ECO:0000269|PubM... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9 for agmatine and putrescine uptake. {ECO:0000269|PubMed:21128598}; | null | FUNCTION: Electrogenic voltage-dependent transporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics (PubMed:9260930, PubMed:9687576). Functions as a Na(+)-independent, bidirectional uniporter (PubMed:21128598, PubMed:9687576). Cation cellu... | Homo sapiens (Human) |
O15245 | S22A1_HUMAN | MPTVDDILEQVGESGWFQKQAFLILCLLSAAFAPICVGIVFLGFTPDHHCQSPGVAELSQRCGWSPAEELNYTVPGLGPAGEAFLGQCRRYEVDWNQSALSCVDPLASLATNRSHLPLGPCQDGWVYDTPGSSIVTEFNLVCADSWKLDLFQSCLNAGFLFGSLGVGYFADRFGRKLCLLGTVLVNAVSGVLMAFSPNYMSMLLFRLLQGLVSKGNWMAGYTLITEFVGSGSRRTVAIMYQMAFTVGLVALTGLAYALPHWRWLQLAVSLPTFLFLLYYWCVPESPRWLLSQKRNTEAIKIMDHIAQKNGKLPPADLKML... | null | null | acetylcholine transport [GO:0015870]; acyl carnitine transmembrane transport [GO:1902616]; cellular detoxification [GO:1990748]; dopamine transport [GO:0015872]; dopamine uptake [GO:0090494]; epinephrine transport [GO:0048241]; establishment or maintenance of transmembrane electrochemical gradient [GO:0010248]; metanep... | apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; plasma membrane [GO:0005886]; presynapse [GO:0098793] | (R)-carnitine transmembrane transporter activity [GO:1901235]; acetylcholine transmembrane transporter activity [GO:0005277]; dopamine:sodium symporter activity [GO:0005330]; identical protein binding [GO:0042802]; monoamine transmembrane transporter activity [GO:0008504]; neurotransmitter transmembrane transporter act... | PF00083; | 1.20.1250.20; | Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family | PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q63089}. | SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:12719534}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:15817714, ECO:0000269|PubMed:19536068, ECO:0000269|PubMed:23680637}; Multi-pass membrane protein {ECO:0000305}. Lateral cell membrane {ECO:0000269|PubMed:162... | CATALYTIC ACTIVITY: Reaction=1-methylnicotinamide(out) = 1-methylnicotinamide(in); Xref=Rhea:RHEA:73859, ChEBI:CHEBI:16797; Evidence={ECO:0000269|PubMed:9260930}; CATALYTIC ACTIVITY: Reaction=dopamine(out) = dopamine(in); Xref=Rhea:RHEA:73863, ChEBI:CHEBI:59905; Evidence={ECO:0000269|PubMed:35469921}; CATALYTIC ACTIVIT... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=440 uM for salsolinol {ECO:0000269|PubMed:17460754}; KM=558 uM for adrenaline {ECO:0000269|PubMed:35469921}; KM=655 uM for cyclo(his-pro) {ECO:0000269|PubMed:17460754}; KM=663 uM for serotonin {ECO:0000269|PubMed:35469921}; KM=674 uM for dopamine {ECO:0000269|PubMe... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 for the transport of MPP (PubMed:11388889). While optimum pH is 6.0 for the transport of the drug quinidine, no transport activity is observed at pH 7.5, possibly due to the protonation of quininide at pH6.0 (PubMed:11408531). {ECO:0000269|PubMed:11388889... | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 22 degrees Celsius for the transport of TEA. Doesn't show any transport activity of TEA at 4 degrees Celsius. {ECO:0000269|PubMed:9655880}; | FUNCTION: Electrogenic voltage-dependent transporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics (PubMed:11388889, PubMed:11408531, PubMed:12439218, PubMed:12719534, PubMed:15389554, PubMed:16263091, PubMed:16272756, PubMed:16581093, Pu... | Homo sapiens (Human) |
O15247 | CLIC2_HUMAN | MSGLRPGTQVDPEIELFVKAGSDGESIGNCPFCQRLFMILWLKGVKFNVTTVDMTRKPEELKDLAPGTNPPFLVYNKELKTDFIKIEEFLEQTLAPPRYPHLSPKYKESFDVGCNLFAKFSAYIKNTQKEANKNFEKSLLKEFKRLDDYLNTPLLDEIDPDSAEEPPVSRRLFLDGDQLTLADCSLLPKLNIIKVAAKKYRDFDIPAEFSGVWRYLHNAYAREEFTHTCPEDKEIENTYANVAKQKS | null | null | chloride transport [GO:0006821]; negative regulation of ryanodine-sensitive calcium-release channel activity [GO:0060315]; positive regulation of binding [GO:0051099]; regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion [GO:0010881]; regulation of release of sequestered calc... | chloride channel complex [GO:0034707]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | chloride channel activity [GO:0005254]; glutathione peroxidase activity [GO:0004602] | PF13410;PF13409; | 1.20.1050.10;3.40.30.10; | Chloride channel CLIC family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15916532}. Membrane {ECO:0000305|PubMed:15916532}; Single-pass membrane protein {ECO:0000305|PubMed:15916532}. Note=Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain. | null | 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. Modulates the activity of RYR2 and inhibits calcium influx. {ECO:0000269|PubMed:15147738, ECO:0000269|PubMed:15916532, ECO... | Homo sapiens (Human) |
O15254 | ACOX3_HUMAN | MASTVEGGDTALLPEFPRGPLDAYRARASFSWKELALFTEGEGMLRFKKTIFSALENDPLFARSPGADLSLEKYRELNFLRCKRIFEYDFLSVEDMFKSPLKVPALIQCLGMYDSSLAAKYLLHSLVFGSAVYSSGSERHLTYIQKIFRMEIFGCFALTELSHGSNTKAIRTTAHYDPATEEFIIHSPDFEAAKFWVGNMGKTATHAVVFAKLCVPGDQCHGLHPFIVQIRDPKTLLPMPGVMVGDIGKKLGQNGLDNGFAMFHKVRVPRQSLLNRMGDVTPEGTYVSPFKDVRQRFGASLGSLSSGRVSIVSLAILNLK... | 1.3.3.6 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P07872}; | fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; lipid homeostasis [GO:0055088] | cytosol [GO:0005829]; membrane [GO:0016020]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777] | FAD binding [GO:0071949]; fatty acid binding [GO:0005504]; flavin adenine dinucleotide binding [GO:0050660]; pristanoyl-CoA oxidase activity [GO:0016402] | PF01756;PF02770; | 2.40.110.10;1.20.140.10; | Acyl-CoA oxidase family | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2; Xref=Rhea:RHEA:38959, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.3.6; Evidence={ECO:0000250|UniProtKB:Q63448}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38960; Evidence={ECO:0000250|U... | null | PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation. | null | null | FUNCTION: Oxidizes the CoA-esters of 2-methyl-branched fatty acids. {ECO:0000250|UniProtKB:Q63448}. | Homo sapiens (Human) |
O15258 | RER1_HUMAN | MSEGDSVGESVHGKPSVVYRFFTRLGQIYQSWLDKSTPYTAVRWVVTLGLSFVYMIRVYLLQGWYIVTYALGIYHLNLFIAFLSPKVDPSLMEDSDDGPSLPTKQNEEFRPFIRRLPEFKFWHAATKGILVAMVCTFFDAFNVPVFWPILVMYFIMLFCITMKRQIKHMIKYRYIPFTHGKRRYRGKEDAGKAFAS | null | null | positive regulation of protein localization to plasma membrane [GO:1903078]; protein retention in ER lumen [GO:0006621]; retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum [GO:0006890]; skeletal muscle acetylcholine-gated channel clustering [GO:0071340] | cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886] | acetylcholine receptor binding [GO:0033130] | PF03248; | null | RER1 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment. {ECO:0000250}. | Homo sapiens (Human) |
O15259 | NPHP1_HUMAN | MLARRQRDPLQALRRRNQELKQQVDSLLSESQLKEALEPNKRQHIYQRCIQLKQAIDENKNALQKLSKADESAPVANYNQRKEEEHTLLDKLTQQLQGLAVTISRENITEVGAPTEEEEESESEDSEDSGGEEEDAEEEEEEKEENESHKWSTGEEYIAVGDFTAQQVGDLTFKKGEILLVIEKKPDGWWIAKDAKGNEGLVPRTYLEPYSEEEEGQESSEEGSEEDVEAVDETADGAEVKQRTDPHWSAVQKAISEAGIFCLVNHVSFCYLIVLMRNRMETVEDTNGSETGFRAWNVQSRGRIFLVSKPVLQINTVDVL... | null | null | actin cytoskeleton organization [GO:0030036]; cell projection organization [GO:0030030]; cell-cell adhesion [GO:0098609]; positive regulation of bicellular tight junction assembly [GO:1903348]; protein localization involved in establishment of planar polarity [GO:0090251]; retina development in camera-type eye [GO:0060... | adherens junction [GO:0005912]; bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; cilium [GO:0005929]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; membrane [GO:0016020]; motile cilium [GO:0031514]; photoreceptor connecting cilium [GO:0032391] | structural molecule activity [GO:0005198] | PF00018; | 2.30.30.40; | Nephrocystin-1 family | PTM: Phosphorylation by CK2 is required for the interaction with PACS1 and the targeting to the base region of cilia. {ECO:0000269|PubMed:16308564, ECO:0000269|PubMed:21357692}. | SUBCELLULAR LOCATION: Cell junction {ECO:0000250|UniProtKB:Q9QY53}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q9QY53}. Cell projection, cilium {ECO:0000269|PubMed:16885411}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:16308564, ECO:0000269|PubMed:16885411}. Cell junction, tight junction. N... | null | null | null | null | null | FUNCTION: Together with BCAR1 it may play a role in the control of epithelial cell polarity (By similarity). Involved in the organization of apical junctions in kidney cells together with NPHP4 and RPGRIP1L/NPHP8 (By similarity). Does not seem to be strictly required for ciliogenesis (By similarity). Seems to help to r... | Homo sapiens (Human) |
O15260 | SURF4_HUMAN | MGQNDLMGTAEDFADQFLRVTKQYLPHVARLCLISTFLEDGIRMWFQWSEQRDYIDTTWNCGYLLASSFVFLNLLGQLTGCVLVLSRNFVQYACFGLFGIIALQTIAYSILWDLKFLMRNLALGGGLLLLLAESRSEGKSMFAGVPTMRESSPKQYMQLGGRVLLVLMFMTLLHFDASFFSIVQNIVGTALMILVAIGFKTKLAALTLVVWLFAINVYFNAFWTIPVYKPMHDFLKYDFFQTMSVIGGLLLVVALGPGGVSMDEKKKEW | null | null | COPII-coated vesicle cargo loading [GO:0090110]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; Golgi organization [GO:0007030]; lipid export from cell [GO:0140353]; lipid homeostasis [GO:0055088]; lipoprotein transport [GO:0042953]; positive regulation of organelle organization [GO:0010638]; r... | azurophil granule membrane [GO:0035577]; COPII-coated ER to Golgi transport vesicle [GO:0030134]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endopl... | cargo receptor activity [GO:0038024]; COPII receptor activity [GO:0097020] | PF02077; | null | SURF4 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15308636, ECO:0000269|PubMed:18287528, ECO:0000269|PubMed:30251625, ECO:0000269|PubMed:33186557}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:18287528}; Multi-pass me... | null | null | null | null | null | FUNCTION: Endoplasmic reticulum cargo receptor that mediates the export of lipoproteins by recruiting cargos into COPII vesicles to facilitate their secretion (PubMed:29643117, PubMed:30251625, PubMed:33186557). Acts as a cargo receptor for lipoproteins bearing both APOB and APOA1, thereby regulating lipoprotein delive... | Homo sapiens (Human) |
O15263 | DFB4A_HUMAN | MRVLYLLFSFLFIFLMPLPGVFGGIGDPVTCLKSGAICHPVFCPRRYKQIGTCGLPGTKCCKKP | null | null | antifungal innate immune response [GO:0061760]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cell chemotaxis [GO:0060326]; chemotaxis [GO:0006935]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [G... | extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796] | CCR6 chemokine receptor binding [GO:0031731]; chemoattractant activity [GO:0042056]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546] | PF00711; | null | Beta-defensin family, LAP/TAP subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10837369}. | null | null | null | null | null | FUNCTION: Exhibits antimicrobial activity against Gram-negative bacteria and Gram-positive bacteria, with highest activity against Gram-negative bacteria (PubMed:10837369, PubMed:9202117). Antimicrobial activity against P.aruginosa seems to be salt-sensitive and is reduced with high salt concentrations greater than 25 ... | Homo sapiens (Human) |
O15264 | MK13_HUMAN | MSLIRKKGFYKQDVNKTAWELPKTYVSPTHVGSGAYGSVCSAIDKRSGEKVAIKKLSRPFQSEIFAKRAYRELLLLKHMQHENVIGLLDVFTPASSLRNFYDFYLVMPFMQTDLQKIMGMEFSEEKIQYLVYQMLKGLKYIHSAGVVHRDLKPGNLAVNEDCELKILDFGLARHADAEMTGYVVTRWYRAPEVILSWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVTGVPGTEFVQKLNDKAAKSYIQSLPQTPRKDFTQLFPRASPQAADLLEKMLELDVDKRLTAAQALTHPFFEPFRDPEEETEA... | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | cell cycle [GO:0007049]; cellular response to anisomycin [GO:0072740]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to interleukin-1 [GO:0071347]; cellular response to sodium arsenite [GO:1903936]; cellular response to sorbitol [GO:0072709]; cellular response to UV [GO:0034644]; intracellular ... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily | PTM: Dually phosphorylated on Thr-180 and Tyr-182 by MAP2K3/MKK3, MAP2K4/MKK4, MAP2K6/MKK6 and MAP2K7/MKK7, which activates the enzyme. Dephosphorylated by dual specificity phosphatase DUSP1. {ECO:0000269|PubMed:9374491}. | null | 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=2.7.11.24; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK13 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as pro-inflammatory cytokines or physical stress leading to di... | Homo sapiens (Human) |
O15265 | ATX7_HUMAN | MSERAADDVRGEPRRAAAAAGGAAAAAARQQQQQQQQQQPPPPQPQRQQHPPPPPRRTRPEDGGPGAASTSAAAMATVGERRPLPSPEVMLGQSWNLWVEASKLPGKDGTELDESFKEFGKNREVMGLCREDMPIFGFCPAHDDFYLVVCNDCNQVVKPQAFQSHYERRHSSSSKPPLAVPPTSVFSFFPSLSKSKGGSASGSNRSSSGGVLSASSSSSKLLKSPKEKLQLRGNTRPMHPIQQSRVPHGRIMTPSVKVEKIHPKMDGTLLKSAVGPTCPATVSSLVKPGLNCPSIPKPTLPSPGQILNGKGLPAPPTLEK... | null | null | microtubule cytoskeleton organization [GO:0000226]; negative regulation of microtubule depolymerization [GO:0007026]; nucleus organization [GO:0006997]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA repair [GO:0006282]; regulation of RNA splicing [GO:0043484]; regulation of transcri... | cytosol [GO:0005829]; microtubule cytoskeleton [GO:0015630]; nuclear matrix [GO:0016363]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SAGA complex [GO:0000124]; transcription factor TFTC complex [GO:0033276] | null | PF08313; | 6.10.140.670; | Ataxin-7 family | PTM: Proteolytically cleaved by caspase-7 (CASP7) (PubMed:17646170). The cleavage may be involved in SCA7 degeneration: the isoform fragments may exert distinct toxic influences that could contribute to selective neurodegeneration (PubMed:17646170). {ECO:0000269|PubMed:17646170}.; PTM: Sumoylation decreases the aggrega... | SUBCELLULAR LOCATION: [Isoform a]: Nucleus {ECO:0000269|PubMed:12533095, ECO:0000269|PubMed:16314424, ECO:0000269|PubMed:22100762}. Nucleus, nucleolus {ECO:0000269|PubMed:10441328}. Nucleus matrix {ECO:0000269|PubMed:10441328}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22100762}. Note=In addition to a diffuse distrib... | null | null | null | null | null | FUNCTION: Acts as a component of the STAGA transcription coactivator-HAT complex (PubMed:15932940, PubMed:18206972). Mediates the interaction of STAGA complex with the CRX and is involved in CRX-dependent gene activation (PubMed:15932940, PubMed:18206972). Necessary for microtubule cytoskeleton stabilization (PubMed:22... | Homo sapiens (Human) |
O15266 | SHOX_HUMAN | MEELTAFVSKSFDQKSKDGNGGGGGGGGKKDSITYREVLESGLARSRELGTSDSSLQDITEGGGHCPVHLFKDHVDNDKEKLKEFGTARVAEGIYECKEKREDVKSEDEDGQTKLKQRRSRTNFTLEQLNELERLFDETHYPDAFMREELSQRLGLSEARVQVWFQNRRAKCRKQENQMHKGVILGTANHLDACRVAPYVNMGALRMPFQQVQAQLQLEGVAHAHPHLHPHLAAHAPYLMFPPPPFGLPIASLAESASAAAVVAAAAKSNSKNSSIADLRLKARKHAEALGL | null | null | positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; skeletal system development [GO:0001501] | chromatin [GO:0000785]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837] | PF00046;PF03826; | 1.10.10.60; | Paired homeobox family, Bicoid subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138}. | null | null | null | null | null | FUNCTION: Controls fundamental aspects of growth and development. | Homo sapiens (Human) |
O15269 | SPTC1_HUMAN | MATATEQWVLVEMVQALYEAPAYHLILEGILILWIIRLLFSKTYKLQERSDLTVKEKEELIEEWQPEPLVPPVPKDHPALNYNIVSGPPSHKTVVNGKECINFASFNFLGLLDNPRVKAAALASLKKYGVGTCGPRGFYGTFDVHLDLEDRLAKFMKTEEAIIYSYGFATIASAIPAYSKRGDIVFVDRAACFAIQKGLQASRSDIKLFKHNDMADLERLLKEQEIEDQKNPRKARVTRRFIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGINIDDIDLISANMENALASIGGFCCG... | 2.3.1.50 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; | ceramide biosynthetic process [GO:0046513]; positive regulation of lipophagy [GO:1904504]; regulation of fat cell apoptotic process [GO:1904649]; sphinganine biosynthetic process [GO:0046511]; sphingolipid biosynthetic process [GO:0030148]; sphingolipid metabolic process [GO:0006665]; sphingomyelin biosynthetic process... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; serine C-palmitoyltransferase complex [GO:0017059]; SPOTS complex [GO:0035339] | pyridoxal phosphate binding [GO:0030170]; serine C-palmitoyltransferase activity [GO:0004758] | PF00155; | 3.90.1150.10;3.40.640.10; | Class-II pyridoxal-phosphate-dependent aminotransferase family | PTM: Phosphorylation at Tyr-164 inhibits activity and promotes cell survival. {ECO:0000269|PubMed:23629659}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21618344}; Single-pass membrane protein {ECO:0000250|UniProtKB:O35704}. | CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoyl-CoA + L-serine = 3-oxosphinganine + CO2 + CoA; Xref=Rhea:RHEA:14761, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:58299; EC=2.3.1.50; Evidence={ECO:0000269|PubMed:19416851}; PhysiologicalDirection=left-to-righ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.75 mM for L-serine {ECO:0000269|PubMed:20504773}; KM=0.3 mM for L-serine {ECO:0000269|PubMed:33558761}; Vmax=1350 pmol/min/mg enzyme {ECO:0000269|PubMed:20504773}; | PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:19416851}. | null | null | FUNCTION: Component of the serine palmitoyltransferase multisubunit enzyme (SPT) that catalyzes the initial and rate-limiting step in sphingolipid biosynthesis by condensing L-serine and activated acyl-CoA (most commonly palmitoyl-CoA) to form long-chain bases. The SPT complex is also composed of SPTLC2 or SPTLC3 and S... | Homo sapiens (Human) |
O15270 | SPTC2_HUMAN | MRPEPGGCCCRRTVRANGCVANGEVRNGYVRSSAAAAAAAAAGQIHHVTQNGGLYKRPFNEAFEETPMLVAVLTYVGYGVLTLFGYLRDFLRYWRIEKCHHATEREEQKDFVSLYQDFENFYTRNLYMRIRDNWNRPICSVPGARVDIMERQSHDYNWSFKYTGNIIKGVINMGSYNYLGFARNTGSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFATNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAIVYGQPRTRRPWKKILILVEGIYSM... | 2.3.1.50 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; | adipose tissue development [GO:0060612]; ceramide biosynthetic process [GO:0046513]; positive regulation of lipophagy [GO:1904504]; sphinganine biosynthetic process [GO:0046511]; sphingolipid biosynthetic process [GO:0030148]; sphingomyelin biosynthetic process [GO:0006686]; sphingosine biosynthetic process [GO:0046512... | endoplasmic reticulum membrane [GO:0005789]; serine C-palmitoyltransferase complex [GO:0017059] | pyridoxal phosphate binding [GO:0030170]; serine C-palmitoyltransferase activity [GO:0004758] | PF00155; | 3.90.1150.10;3.40.640.10; | Class-II pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P97363}; Single-pass membrane protein {ECO:0000250|UniProtKB:P97363}. | CATALYTIC ACTIVITY: Reaction=H(+) + hexadecanoyl-CoA + L-serine = 3-oxosphinganine + CO2 + CoA; Xref=Rhea:RHEA:14761, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:58299; EC=2.3.1.50; Evidence={ECO:0000269|PubMed:19416851}; CATALYTIC ACTIVITY: Reaction=H(+) +... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.75 mM for L-serine {ECO:0000269|PubMed:20504773}; KM=0.3 mM for L-serine {ECO:0000269|PubMed:33558761}; Vmax=1350 pmol/min/mg enzyme {ECO:0000269|PubMed:20504773}; | PATHWAY: Lipid metabolism; sphingolipid metabolism. | null | null | FUNCTION: Component of the serine palmitoyltransferase multisubunit enzyme (SPT) that catalyzes the initial and rate-limiting step in sphingolipid biosynthesis by condensing L-serine and activated acyl-CoA (most commonly palmitoyl-CoA) to form long-chain bases (PubMed:19416851, PubMed:19648650, PubMed:20504773, PubMed:... | Homo sapiens (Human) |
O15273 | TELT_HUMAN | MATSELSCEVSEENCERREAFWAEWKDLTLSTRPEEGCSLHEEDTQRHETYHQQGQCQVLVQRSPWLMMRMGILGRGLQEYQLPYQRVLPLPIFTPAKMGATKEEREDTPIQLQELLALETALGGQCVDRQEVAEITKQLPPVVPVSKPGALRRSLSRSMSQEAQRG | null | null | adult heart development [GO:0007512]; cardiac muscle cell development [GO:0055013]; cardiac muscle contraction [GO:0060048]; cardiac muscle hypertrophy [GO:0003300]; cardiac muscle hypertrophy in response to stress [GO:0014898]; cardiac muscle tissue morphogenesis [GO:0055008]; cardiac myofibril assembly [GO:0055003]; ... | cytosol [GO:0005829]; I band [GO:0031674]; Z disc [GO:0030018] | BMP binding [GO:0036122]; FATZ binding [GO:0051373]; molecular adaptor activity [GO:0060090]; protein-macromolecule adaptor activity [GO:0030674]; structural constituent of muscle [GO:0008307]; titin binding [GO:0031432]; titin Z domain binding [GO:0070080]; transmembrane transporter binding [GO:0044325] | PF09470; | 2.20.160.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:16713295}. | null | null | null | null | null | FUNCTION: Muscle assembly regulating factor. Mediates the antiparallel assembly of titin (TTN) molecules at the sarcomeric Z-disk. | Homo sapiens (Human) |
O15287 | FANCG_HUMAN | MSRQTTSVGSSCLDLWREKNDRLVRQAKVAQNSGLTLRRQQLAQDALEGLRGLLHSLQGLPAAVPVLPLELTVTCNFIILRASLAQGFTEDQAQDIQRSLERVLETQEQQGPRLEQGLRELWDSVLRASCLLPELLSALHRLVGLQAALWLSADRLGDLALLLETLNGSQSGASKDLLLLLKTWSPPAEELDAPLTLQDAQGLKDVLLTAFAYRQGLQELITGNPDKALSSLHEAASGLCPRPVLVQVYTALGSCHRKMGNPQRALLYLVAALKEGSAWGPPLLEASRLYQQLGDTTAELESLELLVEALNVPCSSKAPQ... | null | null | DNA damage response [GO:0006974]; DNA repair [GO:0006281]; interstrand cross-link repair [GO:0036297]; mitochondrion organization [GO:0007005]; ovarian follicle development [GO:0001541]; response to radiation [GO:0009314]; spermatid development [GO:0007286] | chromatin [GO:0000785]; cytosol [GO:0005829]; Fanconi anaemia nuclear complex [GO:0043240]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886] | damaged DNA binding [GO:0003684] | null | 1.25.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18550849}. Cytoplasm {ECO:0000269|PubMed:18550849}. Note=The major form is nuclear. The minor form is cytoplasmic. | null | null | null | null | null | FUNCTION: DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be implicated in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability. Candidate tumor suppressor gene. | Homo sapiens (Human) |
O15294 | OGT1_HUMAN | MASSVGNVADSTEPTKRMLSFQGLAELAHREYQAGDFEAAERHCMQLWRQEPDNTGVLLLLSSIHFQCRRLDRSAHFSTLAIKQNPLLAEAYSNLGNVYKERGQLQEAIEHYRHALRLKPDFIDGYINLAAALVAAGDMEGAVQAYVSALQYNPDLYCVRSDLGNLLKALGRLEEAKACYLKAIETQPNFAVAWSNLGCVFNAQGEIWLAIHHFEKAVTLDPNFLDAYINLGNVLKEARIFDRAVAAYLRALSLSPNHAVVHGNLACVYYEQGLIDLAIDTYRRAIELQPHFPDAYCNLANALKEKGSVAEAEDCYNTAL... | 2.4.1.255 | null | apoptotic process [GO:0006915]; cellular response to glucose stimulus [GO:0071333]; chromatin organization [GO:0006325]; circadian regulation of gene expression [GO:0032922]; hemopoiesis [GO:0030097]; mitophagy [GO:0000423]; negative regulation of cell migration [GO:0030336]; negative regulation of proteasomal ubiquiti... | cell projection [GO:0042995]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; histone acetyltransferase complex [GO:0000123]; mitochondrial membrane [GO:0031966]; NSL complex [GO:0044545]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein N-acetylglucosaminyltransferase com... | acetylglucosaminyltransferase activity [GO:0008375]; chromatin DNA binding [GO:0031490]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; protein O-acetylglucosaminyltransferase activity [GO:0097363] | PF13844;PF00515;PF13414;PF13424;PF13181; | 3.30.720.150;3.40.50.11380;3.40.50.2000;1.25.40.10; | Glycosyltransferase 41 family, O-GlcNAc transferase subfamily | PTM: Ubiquitinated, leading to its proteasomal degradation. {ECO:0000269|PubMed:21285374}.; PTM: Phosphorylation on Ser-3 or Ser-4 by GSK3-beta positively regulates its activity (By similarity). Phosphorylation at Thr-454 by AMPK promotes nuclear localization (PubMed:24563466). {ECO:0000250|UniProtKB:Q8CGY8, ECO:000026... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26678539, ECO:0000269|PubMed:27713473}. Cytoplasm {ECO:0000269|PubMed:26678539, ECO:0000269|PubMed:27713473}. Note=Predominantly localizes to the nucleus (PubMed:26678539). Translocates into the nucleus via association with importin KPNA1 (PubMed:27713473). {ECO:0000269... | CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:48904, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12251, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:90838; EC=2.4.1.... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.8 uM for UDP-N-acetyl-D-glucosamine {ECO:0000269|PubMed:21240259}; | PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:15361863, ECO:0000269|PubMed:21240259, ECO:0000269|PubMed:21285374, ECO:0000269|PubMed:23103939, ECO:0000269|PubMed:26678539, ECO:0000269|PubMed:27713473, ECO:0000269|PubMed:31527085, ECO:0000269|PubMed:37541260}. | null | null | FUNCTION: Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in cytoplasmic and nuclear proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc) (PubMed:12150998, PubMed:15361863, PubMed:19451179, PubMed:20018868, PubMed:21240259, Pu... | Homo sapiens (Human) |
O15296 | LX15B_HUMAN | MAEFRVRVSTGEAFGAGTWDKVSVSIVGTRGESPPLPLDNLGKEFTAGAEEDFQVTLPEDVGRVLLLRVHKAPPVLPLLGPLAPDAWFCRWFQLTPPRGGHLLFPCYQWLEGAGTLVLQEGTAKVSWADHHPVLQQQRQEELQARQEMYQWKAYNPGWPHCLDEKTVEDLELNIKYSTAKNANFYLQAGSAFAEMKIKGLLDRKGLWRSLNEMKRIFNFRRTPAAEHAFEHWQEDAFFASQFLNGLNPVLIRRCHYLPKNFPVTDAMVASVLGPGTSLQAELEKGSLFLVDHGILSGIQTNVINGKPQFSAAPMTLLYQS... | 1.13.11.-; 1.13.11.33 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE-ProRule:PRU00726, ECO:0000269|PubMed:24497644}; Note=Binds 1 Fe cation per subunit. {ECO:0000255|PROSITE-ProRule:PRU00726, ECO:0000269|PubMed:24497644}; | apoptotic process [GO:0006915]; arachidonic acid metabolic process [GO:0019369]; cannabinoid biosynthetic process [GO:1901696]; endocannabinoid signaling pathway [GO:0071926]; hepoxilin biosynthetic process [GO:0051122]; linoleic acid metabolic process [GO:0043651]; lipid metabolic process [GO:0006629]; lipid oxidation... | adherens junction [GO:0005912]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | arachidonate 15-lipoxygenase activity [GO:0050473]; arachidonate 8(S)-lipoxygenase activity [GO:0036403]; calcium ion binding [GO:0005509]; iron ion binding [GO:0005506]; linoleate 13S-lipoxygenase activity [GO:0016165]; linoleate 9S-lipoxygenase activity [GO:1990136]; lipid binding [GO:0008289] | PF00305;PF01477; | 3.10.450.60;2.60.60.20; | Lipoxygenase family | null | SUBCELLULAR LOCATION: [Isoform A]: Nucleus {ECO:0000269|PubMed:12704195}. Note=Other isoforms are excluded from the nucleus. {ECO:0000269|PubMed:12704195}.; SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12704195}. Cell membrane {ECO:0000269|PubMed:12704195, ECO:0000269|PubMed:27435673}. Cytoplasm, cytosk... | CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate; Xref=Rhea:RHEA:16869, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57446; EC=1.13.11.33; Evidence={ECO:0000269|PubMed:10625675, ECO:0000269|PubMed:11956198, ECO:0000269|PubMed:12704195, ECO:00... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1100 uM for arachidonate (isoform D at pH 7.4 and 20 degrees Celsius) {ECO:0000269|PubMed:10542053}; KM=10 uM for linoleate (isoform A at pH 7.4 and 20 degrees Celsius) {ECO:0000269|PubMed:10542053}; KM=25 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoate (isoform A at pH 7... | PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. {ECO:0000269|PubMed:10542053}. | null | null | FUNCTION: [Isoform A]: Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids (PUFAs) generating a spectrum of bioactive lipid mediators (Probable) (PubMed:10542053, PubMed:10625675, PubMed:12704195, PubMed:17493578, PubMed:18311922, PubMe... | Homo sapiens (Human) |
O15297 | PPM1D_HUMAN | MAGLYSLGVSVFSDQGGRKYMEDVTQIVVEPEPTAEEKPSPRRSLSQPLPPRPSPAALPGGEVSGKGPAVAAREARDPLPDAGASPAPSRCCRRRSSVAFFAVCDGHGGREAAQFAREHLWGFIKKQKGFTSSEPAKVCAAIRKGFLACHLAMWKKLAEWPKTMTGLPSTSGTTASVVIIRGMKMYVAHVGDSGVVLGIQDDPKDDFVRAVEVTQDHKPELPKERERIEGLGGSVMNKSGVNRVVWKRPRLTHNGPVRRSTVIDQIPFLAVARALGDLWSYDFFSGEFVVSPEPDTSVHTLDPQKHKYIILGSDGLWNMI... | 3.1.3.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250}; | cellular response to starvation [GO:0009267]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; DNA methylation-dependent heterochromatin formation [GO:0006346]; G2/M transition of mitotic cell cycle [GO:0000086]; negative regulation of cell population proliferation [GO:0008285]; negative reg... | cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | metal ion binding [GO:0046872]; mitogen-activated protein kinase binding [GO:0051019]; myosin phosphatase activity [GO:0017018]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine phosphatase activity [GO:0004722] | PF00481; | 3.60.40.10; | PP2C family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28343630, ECO:0000269|PubMed:9177166}. Cytoplasm, cytosol {ECO:0000269|PubMed:28343630}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-... | null | null | null | null | FUNCTION: Involved in the negative regulation of p53 expression (PubMed:23242139). Required for the relief of p53-dependent checkpoint mediated cell cycle arrest. Binds to and dephosphorylates 'Ser-15' of TP53 and 'Ser-345' of CHEK1 which contributes to the functional inactivation of these proteins (PubMed:15870257, Pu... | Homo sapiens (Human) |
O15303 | GRM6_HUMAN | MARPRRAREPLLVALLPLAWLAQAGLARAAGSVRLAGGLTLGGLFPVHARGAAGRACGQLKKEQGVHRLEAMLYALDRVNADPELLPGVRLGARLLDTCSRDTYALEQALSFVQALIRGRGDGDEVGVRCPGGVPPLRPAPPERVVAVVGASASSVSIMVANVLRLFAIPQISYASTAPELSDSTRYDFFSRVVPPDSYQAQAMVDIVRALGWNYVSTLASEGNYGESGVEAFVQISREAGGVCIAQSIKIPREPKPGEFSKVIRRLMETPNARGIIIFANEDDIRRVLEAARQANLTGHFLWVGSDSWGAKTSPILSLE... | null | null | chemical synaptic transmission [GO:0007268]; detection of light stimulus involved in visual perception [GO:0050908]; detection of visible light [GO:0009584]; G protein-coupled glutamate receptor signaling pathway [GO:0007216]; locomotory behavior [GO:0007626]; positive regulation of calcium ion import across plasma mem... | dendrite [GO:0030425]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; new growing cell tip [GO:0035841]; plasma membrane [GO:0005886]; synapse [GO:0045202] | adenylate cyclase inhibiting G protein-coupled glutamate receptor activity [GO:0001640]; G protein-coupled receptor activity [GO:0004930]; glutamate receptor activity [GO:0008066]; protein homodimerization activity [GO:0042803] | PF00003;PF01094;PF07562; | 3.40.50.2300;2.10.50.30; | G-protein coupled receptor 3 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17405131}; Multi-pass membrane protein {ECO:0000269|PubMed:17405131}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:17405131}; Multi-pass membrane protein {ECO:0000269|PubMed:17405131}. Golgi apparatus membrane {ECO:0000269|PubMed:17405131}; Multi-pass membra... | 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 (By similarity). Sign... | Homo sapiens (Human) |
O15304 | SIVA_HUMAN | MPKRSCPFADVAPLQLKVRVSQRELSRGVCAERYSQEVFEKTKRLLFLGAQAYLDHVWDEGCAVVHLPESPKPGPTGAPRAARGQMLIGPDGRLIRSLGQASEADPSGVASIACSSCVRAVDGKAVCGQCERALCGQCVRTCWGCGSVACTLCGLVDCSDMYEKVLCTSCAMFET | null | COFACTOR: [Isoform 1]: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16683188}; Note=Isoform 1 binds 3 Zn(2+) ions. {ECO:0000269|PubMed:16683188}; COFACTOR: [Isoform 2]: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16683188}; Note=Isoform 2 binds 2 Zn(2+) ions. {ECO:0000269|PubM... | activation-induced cell death of T cells [GO:0006924]; extrinsic apoptotic signaling pathway [GO:0097191]; intrinsic apoptotic signaling pathway [GO:0097193]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; positive regulation of mitochondrial outer membrane permeabilization involved in apo... | cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654] | CD27 receptor binding [GO:0005175]; metal ion binding [GO:0046872]; tumor necrosis factor receptor binding [GO:0005164]; virus receptor activity [GO:0001618]; zinc ion binding [GO:0008270] | PF05458; | null | null | PTM: Phosphorylated by ABL2/ARG in response to oxidative stress. {ECO:0000269|PubMed:11278261}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15034012}. Nucleus {ECO:0000269|PubMed:15034012}. Note=In the nucleus, accumulates in dot-like structures. | null | null | null | null | null | FUNCTION: Induces CD27-mediated apoptosis. Inhibits BCL2L1 isoform Bcl-x(L) anti-apoptotic activity. Inhibits activation of NF-kappa-B and promotes T-cell receptor-mediated apoptosis. {ECO:0000269|PubMed:12011449, ECO:0000269|PubMed:14739602, ECO:0000269|PubMed:15034012, ECO:0000269|PubMed:15958577, ECO:0000269|PubMed:... | Homo sapiens (Human) |
O15305 | PMM2_HUMAN | MAAPGPALCLFDVDGTLTAPRQKITKEMDDFLQKLRQKIKIGVVGGSDFEKVQEQLGNDVVEKYDYVFPENGLVAYKDGKLLCRQNIQSHLGEALIQDLINYCLSYIAKIKLPKKRGTFIEFRNGMLNVSPIGRSCSQEERIEFYELDKKENIRQKFVADLRKEFAGKGLTFSIGGQISFDVFPDGWDKRYCLRHVENDGYKTIYFFGDKTMPGGNDHEIFTDPRTMGYSVTAPEDTRRICELLFS | 5.4.2.8 | null | GDP-mannose biosynthetic process [GO:0009298]; mannose metabolic process [GO:0006013]; protein glycosylation [GO:0006486]; protein N-linked glycosylation [GO:0006487] | cytosol [GO:0005829]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654] | metal ion binding [GO:0046872]; phosphomannomutase activity [GO:0004615] | PF03332; | 3.30.1240.20;3.40.50.1000; | Eukaryotic PMM family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:16540464}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16 uM for alpha-D-mannose 1-phosphate {ECO:0000269|PubMed:16540464}; KM=13.5 uM for alpha-D-glucose 1-phosphate {ECO:0000269|PubMed:16540464}; | PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. | null | null | FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. {ECO:0000250|UniProtKB:Q92871}. | Homo sapiens (Human) |
O15315 | RA51B_HUMAN | MGSKKLKRVGLSQELCDRLSRHQILTCQDFLCLSPLELMKVTGLSYRGVHELLCMVSRACAPKMQTAYGIKAQRSADFSPAFLSTTLSALDEALHGGVACGSLTEITGPPGCGKTQFCIMMSILATLPTNMGGLEGAVVYIDTESAFSAERLVEIAESRFPRYFNTEEKLLLTSSKVHLYRELTCDEVLQRIESLEEEIISKGIKLVILDSVASVVRKEFDAQLQGNLKERNKFLAREASSLKYLAEEFSIPVILTNQITTHLSGALASQADLVSPADDLSLSEGTSGSSCVIAALGNTWSHSVNTRLILQYLDSERRQI... | null | null | blastocyst growth [GO:0001832]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; double-strand break repair via homologous recombination [GO:0000724]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; reciprocal meiotic ... | nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Rad51B-Rad51C-Rad51D-XRCC2 complex [GO:0033063]; replication fork [GO:0005657] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent DNA damage sensor activity [GO:0140664]; DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; four-way junction DNA binding [GO:0000400]; single-stranded DNA binding [GO:00036... | PF08423; | 3.40.50.300; | RecA family, RAD51 subfamily | PTM: Phosphorylated on tyrosine residues by BCR-ABL. {ECO:0000269|PubMed:19657362}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. May promote the assembly of presynaptic RAD51 nucleoprotein filaments. Binds single-stranded DNA and double-stranded DNA and has DNA-dependent ATPase ac... | Homo sapiens (Human) |
O15318 | RPC7_HUMAN | MAGNKGRGRAAYTFNIEAVGFSKGEKLPDVVLKPPPLFPDTDYKPVPLKTGEGEEYMLALKQELRETMKRMPYFIETPEERQDIERYSKRYMKVYKEEWIPDWRRLPREMMPRNKCKKAGPKPKKAKDAGKGTPLTNTEDVLKKMEELEKRGDGEKSDEENEEKEGSKEKSKEGDDDDDDDAAEQEEYDEEEQEEENDYINSYFEDGDDFGADSDDNMDEATY | null | null | cell population proliferation [GO:0008283]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of innate immune response [GO:0045089]; positive regulation of interferon-beta production [GO:0032728]; regulation of transcription by RNA polymerase III [GO:0006359]; transcripti... | cytosol [GO:0005829]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase III complex [GO:0005666] | chromatin binding [GO:0003682]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899] | PF11705; | null | Eukaryotic RPC7 RNA polymerase subunit family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20154270, ECO:0000269|PubMed:21898682, ECO:0000269|PubMed:33335104}. Cytoplasm {ECO:0000250|UniProtKB:Q6NXY9}. Note=Excluded from nucleoli (PubMed:21898682). In zygotes and the 2-cell stage embryos, mainly in the cytoplasm. Starts to localize to the nucleus in the 8-16 ... | null | null | null | null | null | FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (PubMed:20413673, PubMed:33558764, PubMed:34675218, PubMed:35637192). Specific peripheric component of RNA polymerase III (Pol III) which synthesizes small non-coding RNAs includi... | Homo sapiens (Human) |
O15327 | INP4B_HUMAN | MEIKEEGASEEGQHFLPTAQANDPGDCQFTSIQKTPNEPQLEFILACKDLVAPVRDRKLNTLVQISVIHPVEQSLTRYSSTEIVEGTRDPLFLTGVTFPSEYPIYEETKIKLTVYDVKDKSHDTVRTSVLPEHKDPPPEVGRSFLGYASFKVGELLKSKEQLLVLSLRTSDGGKVVGTIEVSVVKMGEIEDGEADHITTDVQGQKCALVCECTAPESVSGKDNLPFLNSVLKNPVCKLYRFPTSDNKWMRIREQMSESILSFHIPKELISLHIKEDLCRNQEIKELGELSPHWDNLRKNVLTHCDQMVNMYQDILTELSK... | 3.1.3.66 | null | inositol phosphate metabolic process [GO:0043647]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol dephosphorylation [GO:0046856]; signal transduction [GO:0007165] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | inositol-1,3,4-trisphosphate 4-phosphatase activity [GO:0017161]; inositol-3,4-bisphosphate 4-phosphatase activity [GO:0052828]; phosphatidylinositol-3,4-bisphosphate 4-phosphatase activity [GO:0016316] | null | 6.10.250.230;2.60.40.150; | Inositol 3,4-bisphosphate 4-phosphatase family | null | null | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + phosphate; Xref=Rhea:RHEA:17193, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57658, ChEBI:CHEBI:58088; EC=3.1.3.66; Evidence={ECO:0000269|PubM... | null | PATHWAY: Signal transduction; phosphatidylinositol signaling pathway. {ECO:0000250|UniProtKB:Q9QWG5}. | null | null | FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4-trisphosphate and inositol 3,4-trisphosphate (PubMed:24070612, PubMed:24591580). Plays a role in the late stages of macropinocytosis by dephosphorylating phosphatidylinositol 3,4-bisphosphate in membr... | Homo sapiens (Human) |
O15342 | VA0E1_HUMAN | MAYHGLTVPLIVMSVFWGFVGFLVPWFIPKGPNRGVIITMLVTCSVCCYLFWLIAILAQLNPLFGPQLKNETIWYLKYHWP | null | null | proton transmembrane transport [GO:1902600]; regulation of macroautophagy [GO:0016241]; transmembrane transport [GO:0055085]; vacuolar acidification [GO:0007035] | endosome membrane [GO:0010008]; lysosomal membrane [GO:0005765]; phagocytic vesicle membrane [GO:0030670]; proton-transporting V-type ATPase, V0 domain [GO:0033179] | ATPase-coupled ion transmembrane transporter activity [GO:0042625]; proton-transporting ATPase activity, rotational mechanism [GO:0046961] | PF05493; | null | V-ATPase e1/e2 subunit family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:33065002). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartm... | Homo sapiens (Human) |
O15344 | TRI18_HUMAN | METLESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATNESVESITAFQCPTCRHVITLSQRGLDGLKRNVTLQNIIDRFQKASVSGPNSPSETRRERAFDANTMTSAEKVLCQFCDQDPAQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEPIPDSHIRGLMCLEHEDEKVNMYCVTDDQLICALCKLVGRHRDHQVAALSERYDKLKQNLESNLTNLIKRNTELETLLAKLIQTCQHVEVNASRQEAKLTEECDLLIEIIQQRRQIIGTKIKEGKVMRLRKLAQQIANCKQCIERSASLISQAEHSL... | 2.3.2.27 | null | microtubule cytoskeleton organization [GO:0000226]; negative regulation of microtubule depolymerization [GO:0007026]; pattern specification process [GO:0007389]; positive regulation of stress-activated MAPK cascade [GO:0032874]; protein localization to microtubule [GO:0035372]; regulation of microtubule cytoskeleton or... | centriolar satellite [GO:0034451]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875]; spindle [GO:0005819] | enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; microtubule binding [GO:0008017]; phosphoprotein binding [GO:0051219]; protein homodimerization activity [GO:0042803]; transferase activity [GO:0016740]; ubiquitin protein ligase binding [GO:0031625]; zinc ion binding [GO:0008270] | PF18568;PF00041;PF00622;PF00643;PF13445; | 2.60.120.920;4.10.830.40;3.30.160.60;2.60.40.10;3.30.40.10; | TRIM/RBCC family | PTM: Phosphorylated on serine and threonine residues. {ECO:0000269|PubMed:11806752}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10077590}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10077590}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:10077590}. Note=Microtubule-associated. It is associated with microtubules throughout the cell cycle, co-localizing with cytoplasmic fibers in interp... | 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 | null | null | null | FUNCTION: Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination. {ECO:0000269|PubMed:10400985, ECO:0000269|PubMed:11685209, ECO:0000269|PubMed:22613722}. | Homo sapiens (Human) |
O15347 | HMGB3_HUMAN | MAKGDPKKPKGKMSAYAFFVQTCREEHKKKNPEVPVNFAEFSKKCSERWKTMSGKEKSKFDEMAKADKVRYDREMKDYGPAKGGKKKKDPNAPKRPPSGFFLFCSEFRPKIKSTNPGISIGDVAKKLGEMWNNLNDSEKQPYITKAAKLKEKYEKDVADYKSKGKFDGAKGPAKVARKKVEEEDEEEEEEEEEEEEEEDE | null | null | DNA geometric change [GO:0032392]; DNA recombination [GO:0006310]; innate immune response [GO:0045087]; regulation of transcription by RNA polymerase II [GO:0006357] | chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA binding, bending [GO:0008301]; double-stranded DNA binding [GO:0003690]; four-way junction DNA binding [GO:0000400]; RNA binding [GO:0003723] | PF00505;PF09011; | 1.10.30.10; | HMGB family | PTM: Reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-104 and a possible intramolecular disulfide bond involving Cys-23 and Cys-45 give rise to different redox forms with specific functional activities in various cellular compartments: 1- fully reduced HMGB3 (HMGB3C23hC45hC104h), 2- disulfide HMGB3 (HMGB... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P40618, ECO:0000255|PROSITE-ProRule:PRU00267}. Chromosome {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:O54879}. | null | null | null | null | null | FUNCTION: Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner. Associates with chromatin and binds DNA with a preference for non-canonical DNA structures such as single-stranded DNA. Can bend DNA and enhance DNA flexibility by looping thus providing a mecha... | Homo sapiens (Human) |
O15350 | P73_HUMAN | MAQSTATSPDGGTTFEHLWSSLEPDSTYFDLPQSSRGNNEVVGGTDSSMDVFHLEGMTTSVMAQFNLLSSTMDQMSSRAASASPYTPEHAASVPTHSPYAQPSSTFDTMSPAPVIPSNTDYPGPHHFEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPPPGTAIRAMPVYKKAEHVTDVVKRCPNHELGRDFNEGQSAPASHLIRVEGNNLSQYVDDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILIIITLEMRDGQVLGRRSFEGRICACPGRDRKADEDHYREQQALNESSA... | null | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | cell cycle [GO:0007049]; DNA damage response [GO:0006974]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; kidney development [GO:0001822]; mismatch repair [GO:0006298]; negative regulation ... | cell junction [GO:0030054]; chromatin [GO:0000785]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | 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]; DNA-binding transcription factor binding [GO:0140297]; identical protein binding [GO:0042802]... | PF00870;PF07710;PF07647; | 2.60.40.720;4.10.170.10;1.10.150.50; | P53 family | PTM: Isoform alpha (but not isoform beta) is sumoylated on Lys-627, which potentiates proteasomal degradation but does not affect transcriptional activity. Phosphorylation by PLK1 and PLK3 inhibits the transcription regulator activity and pro-apoptotic function. {ECO:0000269|PubMed:10961991}.; PTM: Higher levels of pho... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24314664}. Cytoplasm. Note=Accumulates in the nucleus in response to DNA damage. | null | null | null | null | null | FUNCTION: Participates in the apoptotic response to DNA damage. Isoforms containing the transactivation domain are pro-apoptotic, isoforms lacking the domain are anti-apoptotic and block the function of p53 and transactivating p73 isoforms. May be a tumor suppressor protein. Is an activator of FOXJ1 expression (By simi... | Homo sapiens (Human) |
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