Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 118 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 11.3k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.75k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.09k ⌀ | Pfam stringlengths 8 232 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 8.52k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 64 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.3k ⌀ | Organism stringlengths 8 196 |
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P13342 | HLOAD_BPT4 | MIKLRMPAGGERYIDGKSVYKLYLMIKQHMNGKYDVIKYNWCMRVSDAAYQKRRDKYFFQKLSEKYKLKELALIFISNLVANQDAWIGDISDADALVFYREYIGRLKQIKFKFEEDIRNIYYFSKKVEVSAFKEIFEYNPKVQSSYIFKLLQSNIISFETFILLDSFLNIIDKHDEQTDNLVWNNYSIKLKAYRKILNIDSQKAKNVFIETVKSCKY | null | null | bidirectional double-stranded viral DNA replication [GO:0039686]; DNA replication [GO:0006260] | null | DNA binding [GO:0003677] | PF08994;PF08993; | 1.10.8.60;1.10.220.50; | Tequatrovirus DNA helicase assembly protein family | null | null | null | null | null | null | null | FUNCTION: DNA helicase loader protein that participates in viral DNA replication, recombination, and repair (PubMed:10871615). At the fork, required for loading of the replicative helicase onto DNA protected by the ssDNA-binding protein (PubMed:10871615, PubMed:11459967, PubMed:22427673, PubMed:7806533). Coordinates si... | Enterobacteria phage T4 (Bacteriophage T4) |
P13346 | FOSB_MOUSE | MFQAFPGDYDSGSRCSSSPSAESQYLSSVDSFGSPPTAAASQECAGLGEMPGSFVPTVTAITTSQDLQWLVQPTLISSMAQSQGQPLASQPPAVDPYDMPGTSYSTPGLSAYSTGGASGSGGPSTSTTTSGPVSARPARARPRRPREETLTPEEEEKRRVRRERNKLAAAKCRNRRRELTDRLQAETDQLEEEKAELESEIAELQKEKERLEFVLVAHKPGCKIPYEEGPGPGPLAEVRDLPGSTSAKEDGFGWLLPPPPPPPLPFQSSRDAPPNLTASLFTHSEVQVLGDPFPVVSPSYTSSFVLTCPEVSAFAGAQRT... | null | null | behavioral response to cocaine [GO:0048148]; cellular response to calcium ion [GO:0071277]; cellular response to hormone stimulus [GO:0032870]; female pregnancy [GO:0007565]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; response t... | cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded DNA binding [GO:0003690]; RNA polymerase II cis-reg... | PF00170; | 1.20.5.170; | BZIP family, Fos subfamily | PTM: Phosphorylated. {ECO:0000269|PubMed:16687504}.; PTM: [Isoform 2]: Phosphorylated at Ser-27 by CSNK2A1; phosphorylation increases protein stability and transactivation potential. {ECO:0000269|PubMed:16687504, ECO:0000269|PubMed:17241283}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17241283, ECO:0000269|PubMed:23303048, ECO:0000269|PubMed:2498083, ECO:0000269|PubMed:30902680, ECO:0000269|PubMed:9294222}. | null | null | null | null | null | FUNCTION: Heterodimerizes with proteins of the JUN family to form an AP-1 transcription factor complex, thereby enhancing their DNA binding activity to gene promoters containing an AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing their transcriptional activity (PubMed:1900040, PubMed:2498083). As part of the AP-1... | Mus musculus (Mouse) |
P13349 | MYF5_HUMAN | MDVMDGCQFSPSEYFYDGSCIPSPEGEFGDEFVPRVAAFGAHKAELQGSDEDEHVRAPTGHHQAGHCLMWACKACKRKSTTMDRRKAATMRERRRLKKVNQAFETLKRCTTTNPNQRLPKVEILRNAIRYIESLQELLREQVENYYSLPGQSCSEPTSPTSNCSDGMPECNSPVWSRKSSTFDSIYCPDVSNVYATDKNSLSSLDCLSNIVDRITSSEQPGLPLQDLASLSPVASTDSQPATPGASSSRLIYHVL | null | null | camera-type eye development [GO:0043010]; cartilage condensation [GO:0001502]; embryonic skeletal system morphogenesis [GO:0048704]; extracellular matrix organization [GO:0030198]; muscle cell fate commitment [GO:0042693]; muscle organ development [GO:0007517]; muscle tissue morphogenesis [GO:0060415]; ossification [GO... | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; RNA polymerase II transcription regulator complex [GO:0090575] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF01586;PF00010;PF12232; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29887215}. | null | null | null | null | null | FUNCTION: Transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation (PubMed:29887215). Together with MYOG and MYOD1, co-occupies muscle-specific gene promoter core region during myogenesis. Induces fibroblasts to differentiate into myoblasts. Probab... | Homo sapiens (Human) |
P13360 | GLAS_DROME | MGLLYKGSKLLNTILDSLEDQEGGAMYISCDVSNGGPVEPETGYVPNNPLFGLALDSPQQECAASCVGCLSCQGSTALPISSLTSSDFDCGGCFDPTIGVGVGIGGGHIQISTTPPASSGNGSSNNGAGGGSSGNHGYWSTDEMASTFPGLPPLDIDPLPSLFPFSPCGASYNFAAGNPHQAASLSYTVHPHQMLISPNSHNHGQMHSQHQQHQHQQSQVQASHVGNSLLQSSGGNNIGSNGSAGGVANAASCYYETSAGTAAPPPPPAAAMYPSMSVNVSMNMTMHHGYGAGDAGGVPMQCSQMNWTPPSNSTSAAAAA... | null | null | circadian temperature homeostasis [GO:0060086]; compound eye morphogenesis [GO:0001745]; compound eye photoreceptor cell differentiation [GO:0001751]; compound eye photoreceptor fate commitment [GO:0001752]; entrainment of circadian clock [GO:0009649]; entrainment of circadian clock by photoperiod [GO:0043153]; photore... | 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] | PF00096; | 3.30.160.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Transcription factor required for gene expression specific to photoreceptor cells. {ECO:0000269|PubMed:7604032}. | Drosophila melanogaster (Fruit fly) |
P13365 | CG13_YEAST | MAILKDTIIRYANARYATASGTSTATAASVSAASCPNLPLLLQKRRAIASAKSKNPNLVKRELQAHHSAISEYNNDQLDHYFRLSHTERPLYNLTNFNSQPQVNPKMRFLIFDFIMYCHTRLNLSTSTLFLTFTILDKYSSRFIIKSYNYQLLSLTALWISSKFWDSKNRMATLKVLQNLCCNQYSIKQFTTMEMHLFKSLDWSICQSATFDSYIDIFLFQSTSPLSPGVVLSAPLEAFIQQKLALLNNAAGTAINKSSSSQGPSLNINEIKLGAIMLCELASFNLELSFKYDRSLIALGAINLIKLSLNYYNSNLWENI... | null | null | cell division [GO:0051301]; G1/S transition of mitotic cell cycle [GO:0000082]; regulation of cell cycle G1/S phase transition [GO:1902806]; regulation of protein phosphorylation [GO:0001932]; regulation of transcription by RNA polymerase II [GO:0006357]; traversing start control point of mitotic cell cycle [GO:0007089... | cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; spindle pole body [GO:0005816] | cyclin-dependent protein serine/threonine kinase regulator activity [GO:0016538] | PF00134; | 1.10.472.10; | Cyclin family | null | null | null | null | null | null | null | FUNCTION: Essential for the control of the cell cycle at the G1/S (start) transition. CLN3 may be an upstream activator of the G1 cyclins which directly catalyze start. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P13368 | 7LESS_DROME | MTMFWQQNVDHQSDEQDKQAKGAAPTKRLNISFNVKIAVNVNTKMTTTHINQQAPGTSSSSSNSQNASPSKIVVRQQSSSFDLRQQLARLGRQLASGQDGHGGISTILIINLLLLILLSICCDVCRSHNYTVHQSPEPVSKDQMRLLRPKLDSDVVEKVAIWHKHAAAAPPSIVEGIAISSRPQSTMAHHPDDRDRDRDPSEEQHGVDERMVLERVTRDCVQRCIVEEDLFLDEFGIQCEKADNGEKCYKTRCTKGCAQWYRALKELESCQEACLSLQFYPYDMPCIGACEMAQRDYWHLQRLAISHLVERTQPQLERAP... | 2.7.10.1 | null | germ-line stem-cell niche homeostasis [GO:0060250]; peptidyl-tyrosine autophosphorylation [GO:0038083]; R7 cell fate commitment [GO:0007465]; regulation of TOR signaling [GO:0032006]; sevenless signaling pathway [GO:0045500]; visual perception [GO:0007601] | plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; boss receptor activity [GO:0008288]; transmembrane receptor protein kinase activity [GO:0019199]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF00041;PF07714; | 2.60.40.10;2.120.10.30;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | 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 for an extracellular signal required to instruct a cell to differentiate into an R7 photoreceptor. The ligand for sev is the boss (bride of sevenless) protein on the surface of the neighboring R8 cell. {ECO:0000269|PubMed:2840202}. | Drosophila melanogaster (Fruit fly) |
P13369 | CSF1R_FELCA | MGPRALLVLLVATAWHAQGVPVIQPSGPELVVEPGTTVTLRCVGNGSVEWDGPISPHWNLDLDPPSSILTTNNATFQNTGTYHCTEPGNPQGGNATIHLYVKDPARPWKVLAQEVTVLEGQDALLPCLLTDPALEAGVSLVRVRGRPVLRQTNYSFSPWHGFTIHKAKFIENHVYQCSARVDGRTVTSMGIWLKVQKDISGPATLTLEPAELVRIQGEAAQIVCSASNIDVNFDVSLRHGDTKLTISQQSDFHDNRYQKVLTLNLDHVSFQDAGNYSCTATNAWGNHSASMVFRVVESAYLNLTSEQSLLQEVTVGEKVD... | 2.7.10.1 | null | cellular response to cytokine stimulus [GO:0071345]; cellular response to macrophage colony-stimulating factor stimulus [GO:0036006]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; osteoclast differentiation [GO:0030316]; peptidyl-tyrosine phosphorylation [GO:0018108]; positive regulation of c... | cell surface [GO:0009986]; CSF1-CSF1R complex [GO:1990682]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; cytokine binding [GO:0019955]; growth factor binding [GO:0019838]; macrophage colony-stimulating factor receptor activity [GO:0005011] | PF00047;PF07714; | 2.60.40.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamily | PTM: Autophosphorylated in response to CSF1 or IL34 binding. Phosphorylation at Tyr-558 is important for normal down-regulation of signaling by ubiquitination, internalization and degradation. Phosphorylation at Tyr-558 and Tyr-807 is important for interaction with SRC family members, including FYN, YES1 and SRC, and f... | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Note=The autophosphorylated receptor is ubiquitinated and internalized, leading to its degradation. {ECO:0000250}. | 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: Tyrosine-protein kinase that acts as a cell-surface receptor for CSF1 and IL34 and plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes. Promotes the release of pro-inflam... | Felis catus (Cat) (Felis silvestris catus) |
P13372 | VPREB_MOUSE | MAWTSVLLMLLAYLTGCGPQPMVHQPPLASSSLGATIRLSCTLSNDHNIGIYSIYWYQQRPGHPPRFLLRYFSHSDKHQGPDIPPRFSGSKDTTRNLGYLSISELQPEDEAVYYCAVGLRSQEKKRMEREWEGEKSYTDLGS | null | null | B cell homeostasis [GO:0001782]; B cell proliferation [GO:0042100]; cell morphogenesis [GO:0000902]; hemopoiesis [GO:0030097]; immune response [GO:0006955]; regulation of cell size [GO:0008361] | endoplasmic reticulum [GO:0005783]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | signaling receptor activity [GO:0038023] | PF07686; | 2.60.40.10; | Immunoglobulin superfamily | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000305|PubMed:29907570}. | null | null | null | null | null | FUNCTION: Associates with the Ig-mu chain to form a molecular complex that is expressed on the surface of pre-B-cells. This complex presumably regulates Ig gene rearrangements in the early steps of B-cell differentiation. | Mus musculus (Mouse) |
P13378 | HXD8_HUMAN | MSSYFVNPLYSKYKAAAAAAAAAGEAINPTYYDCHFAPEVGGRHAAAAAALQLYGNSAAGFPHAPPQAHAHPHPSPPPSGTGCGGREGRGQEYFHPGGGSPAAAYQAAPPPPPHPPPPPPPPPCGGIACHGEPAKFYGYDNLQRQPIFTTQQEAELVQYPDCKSSSGNIGEDPDHLNQSSSPSQMFPWMRPQAAPGRRRGRQTYSRFQTLELEKEFLFNPYLTRKRRIEVSHALALTERQVKIWFQNRRMKWKKENNKDKFPVSRQEVKDGETKKEAQELEEDRAEGLTN | null | null | anterior/posterior axis specification, embryo [GO:0008595]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; skeletal system morphogenesis [GO:0048705] | chromatin [GO:0000785]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific double-stranded DNA binding [GO:19908... | PF00046; | 1.10.10.60; | Antp homeobox family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. | Homo sapiens (Human) |
P13379 | CD5_MOUSE | MDSHEVLLAATYLLGTLAAFCLGQSGRGGLDIQVMLSGSNSKCQGQVEIQMENKWKTVCSSSWRLSQDHSKNAQQASAVCKQLRCGDPLALGPFPSLNRPQNQVFCQGSPWSISNCNNTSSQDQCLPLSLICLEPQRTTPPPTTTPPTTVPEPTAPPRLQLVPGHEGLRCTGVVEFYNGSWGGTILYKAKDRPLGLGNLICKSLQCGSFLTHLSGTEAAGTPAPAELRDPRPLPIRWEAPNGSCVSLQQCFQKTTAQEGGQALTVICSDFQPKVQSRLVGGSSVCEGIAEVRQRSQWEALCDSSAARGRGRWEELCREQQ... | null | null | apoptotic signaling pathway [GO:0097190]; T cell costimulation [GO:0031295] | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886] | null | PF00530; | 3.10.250.10; | null | PTM: Phosphorylated on tyrosine residues by LYN; this creates binding sites for PTPN6/SHP-1. {ECO:0000269|PubMed:11007759}. | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: May act as a receptor in regulating T-cell proliferation. | Mus musculus (Mouse) |
P13382 | DPOLA_YEAST | MSSKSEKLEKLRKLQAARNGTSIDDYEGDESDGDRIYDEIDEKEYRARKRQELLHDDFVVDDDGVGYVDRGVEEDWREVDNSSSDEDTGNLASKDSKRKKNIKREKDHQITDMLRTQHSKSTLLAHAKKSQKKSIPIDNFDDILGEFESGEVEKPNILLPSKLRENLNSSPTSEFKSSIKRVNGNDESSHDAGISKKVKIDPDSSTDKYLEIESSPLKLQSRKLRYANDVQDLLDDVENSPVVATKRQNVLQDTLLANPPSAQSLADEEDDEDSDEDIILKRRTMRSVTTTRRVNIDSRSNPSTSPFVTAPGTPIGIKGL... | 2.7.7.7 | null | DNA replication [GO:0006260]; DNA replication initiation [GO:0006270]; DNA synthesis involved in DNA repair [GO:0000731]; double-strand break repair [GO:0006302]; lagging strand elongation [GO:0006273]; leading strand elongation [GO:0006272]; mitotic DNA replication initiation [GO:1902975]; premeiotic DNA replication [... | alpha DNA polymerase:primase complex [GO:0005658]; mitochondrion [GO:0005739]; replication fork [GO:0005657] | 4 iron, 4 sulfur cluster binding [GO:0051539]; chromatin binding [GO:0003682]; DNA replication origin binding [GO:0003688]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; single-stranded DNA binding [GO:0003697] | PF12254;PF00136;PF03104;PF08996; | 2.40.50.730;3.30.70.2820;1.10.3200.20;1.10.132.60;3.90.1600.10;3.30.420.10; | DNA polymerase type-B family | null | SUBCELLULAR LOCATION: Nucleus. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000269|PubMed:22119860}; | null | null | null | null | FUNCTION: Catalytic component of DNA polymerase alpha, which in complex with DNA primase (DNA polymerase alpha:primase) constitutes a replicative polymerase (PubMed:10898792, PubMed:22119860, PubMed:31488849). POL1 has a role in promoting telomere replication during interaction with CDC13 (PubMed:10898792). {ECO:000026... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P13383 | NUCL_RAT | MVKLAKAGKTHGESKKMAPPPKEVEEDSEDEEMSEDEDDSSGEEEVVIPQKKGKKATTTPAKKVVVSQTKKAAVPTPAKKAAVTPGKKAAATPAKKAVTPAKVVPTPGKKGAAQAKALVPTPGKKGAVTPAKGAKNGKNAKKEDSDEDEDEEDEDDSDEDEDEEDEFEPPVVKGVKPAKAAPAAPASEDEDEEDDDDEDDDDDDEEEEEEDDSEEEVMEITPAKGKKTPAKVVPVKAKSVAEEEEDDEDDEDEEEDEDEEDEEDDEDEDEEEEEEPVKAAPGKRKKEMTKQKEAPEAKKQKIEGSEPTTPFNLFIGNLNP... | null | null | angiogenesis [GO:0001525]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to leukemia inhibitory factor [GO:1990830]; cellular response to lipopolysaccharide [GO:0071222]; endocytosis [GO:0006897]; liver regeneration [GO:0097421]; negative regulation of apoptotic process [GO:00430... | cell cortex [GO:0005938]; cell surface [GO:0009986]; cornified envelope [GO:0001533]; dense fibrillar component [GO:0001651]; fibrillar center [GO:0001650]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]; spliceosomal complex [GO:0005681] | calcium ion binding [GO:0005509]; DNA topoisomerase binding [GO:0044547]; ErbB-4 class receptor binding [GO:1990631]; histone binding [GO:0042393]; identical protein binding [GO:0042802]; insulin receptor substrate binding [GO:0043560]; laminin binding [GO:0043236]; mRNA 5'-UTR binding [GO:0048027]; PH domain binding [... | PF00076; | 3.30.70.330; | null | PTM: Some glutamate residues are glycylated by TTLL8. This modification occurs exclusively on glutamate residues and results in a glycine chain on the gamma-carboxyl group (By similarity). {ECO:0000250}.; PTM: Symmetrically methylated by PRMT5 (By similarity). {ECO:0000250|UniProtKB:P19338}. | SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm {ECO:0000250}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in... | Rattus norvegicus (Rat) |
P13385 | TDGF1_HUMAN | MDCRKMARFSYSVIWIMAISKVFELGLVAGLGHQEFARPSRGYLAFRDDSIWPQEEPAIRPRSSQRVPPMGIQHSKELNRTCCLNGGTCMLGSFCACPPSFYGRNCEHDVRKENCGSVPHDTWLPKKCSLCKCWHGQLRCFPQAFLPGCDGLVMDEHLVASRTPELPPSARTTTFMLVGICLSIQSYY | null | null | anterior/posterior axis specification, embryo [GO:0008595]; anterior/posterior pattern specification [GO:0009952]; blood vessel development [GO:0001568]; cell differentiation [GO:0030154]; cell migration involved in sprouting angiogenesis [GO:0002042]; cellular response to epidermal growth factor stimulus [GO:0071364];... | apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extrinsic component of plasma membrane [GO:0019897]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | activin receptor binding [GO:0070697]; growth factor activity [GO:0008083]; nodal binding [GO:0038100]; signaling receptor binding [GO:0005102] | PF09443; | 2.10.25.10; | EGF-CFC (Cripto-1/FRL1/Cryptic) family | PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, it is processed by GPI processing phospholipase A2 (TMEM8A), removing an acyl-chain at the sn-2 position of GPI and releasing CRIPTO as a lysophosphatidylinositol-bearing form, which ... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18930707, ECO:0000269|PubMed:27881714}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:18930707, ECO:0000269|PubMed:27881714}. Secreted {ECO:0000269|PubMed:27881714}. Note=Released from the cell membrane by GPI cleavage. {ECO:0000269|PubMed:27881714}. | null | null | null | null | null | FUNCTION: GPI-anchored cell membrane protein involved in Nodal signaling. Cell-associated CRIPTO acts as a Nodal coreceptor in cis. Shedding of CRIPTO by TMEM8A modulates Nodal signaling by allowing soluble CRIPTO to act as a Nodal coreceptor on other cells (PubMed:27881714). Could play a role in the determination of t... | Homo sapiens (Human) |
P13386 | FCERB_RAT | MDTENKSRADLALPNPQESPSAPDIELLEASPPAKALPEKPASPPPQQTWQSFLKKELEFLGVTQVLVGLICLCFGTVVCSTLQTSDFDDEVLLLYRAGYPFWGAVLFVLSGFLSIMSERKNTLYLVRGSLGANIVSSIAAGLGIAILILNLSNNSAYMNYCKDITEDDGCFVTSFITELVLMLLFLTILAFCSAVLLIIYRIGQEFERSKVPDDRLYEELHVYSPIYSALEDTREASAPVVS | null | null | cell surface receptor signaling pathway [GO:0007166]; Fc-epsilon receptor signaling pathway [GO:0038095]; immune response [GO:0006955]; positive regulation of mast cell degranulation [GO:0043306]; protein kinase C-activating G protein-coupled receptor signaling pathway [GO:0007205]; regulation of release of sequestered... | endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; Fc-epsilon receptor I complex [GO:0032998]; plasma membrane [GO:0005886] | IgE binding [GO:0019863]; phosphoprotein binding [GO:0051219]; protein kinase binding [GO:0019901]; SH2 domain binding [GO:0042169] | PF04103; | null | MS4A family | PTM: Phosphorylated on tyrosine residues by LYN. {ECO:0000250}. | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:21746961}; Multi-pass membrane protein {ECO:0000269|PubMed:21746961}. | null | null | null | null | null | FUNCTION: High affinity receptor that binds to the Fc region of immunoglobulins epsilon. Aggregation of FCER1 by multivalent antigens is required for the full mast cell response, including the release of preformed mediators (such as histamine) by degranulation and de novo production of lipid mediators and cytokines. Al... | Rattus norvegicus (Rat) |
P13387 | EGFR_CHICK | MGVRSPLSASGPRGAAVLVLLLLGVALCSAVEEKKVCQGTNNKLTQLGHVEDHFTSLQRMYNNCEVVLSNLEITYVEHNRDLTFLKTIQEVAGYVLIALNMVDVIPLENLQIIRGNVLYDNSFALAVLSNYHMNKTQGLRELPMKRLSEILNGGVKISNNPKLCNMDTVLWNDIIDTSRKPLTVLDFASNLSSCPKCHPNCTEDHCWGAGEQNCQTLTKVICAQQCSGRCRGKVPSDCCHNQCAAGCTGPRESDCLACRKFRDDATCKDTCPPLVLYNPTTYQMDVNPEGKYSFGATCVRECPHNYVVTDHGSCVRSCNT... | 2.7.10.1 | null | cellular response to epidermal growth factor stimulus [GO:0071364]; epidermal growth factor receptor signaling pathway [GO:0007173]; learning or memory [GO:0007611]; phosphorylation [GO:0016310] | endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; Golgi membrane [GO:0000139]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein tyrosine kinase activity [GO:0004713]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF00757;PF14843;PF01030;PF21314; | 6.10.250.2930;3.80.20.20; | Protein kinase superfamily, Tyr protein kinase family, EGF receptor subfamily | PTM: Phosphorylated. Autophosphorylates. {ECO:0000269|PubMed:3260329}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:3260329}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P00533}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}... | 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 binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses (PubMed:3260329). Known ligands include EGF and TGFA/TGF-alpha (PubMed:3260329). Ligand binding triggers receptor homo- and/or heterodimerizati... | Gallus gallus (Chicken) |
P13388 | XMRK_XIPMA | MEFLRGGAALLQLLLVLSISRCCSTDPDRKVCQGTSNQMTMLDNHYLKMKKMYSGCNVVLENLEITYTQENQDLSFLQSIQEVGGYVLIAMNEVSTIPLVNLRLIRGQNLYEGNFTLLVMSNYQKNPSSPDVYQVGLKQLQLSNLTEILSGGVKVSHNPLLCNVETINWWDIVDKTSNPTMNLIPHAFERQCQKCDHGCVNGSCWAPGPGHCQKFTKLLCAEQCNRRCRGPKPIDCCNEHCAGGCTGPRATDCLACRDFNDDGTCKDTCPPPKIYDIVSHQVVDNPNIKYTFGAACVKECPSNYVVTEGACVRSCSAGML... | 2.7.10.1 | null | negative regulation of apoptotic process [GO:0043066]; neurogenesis [GO:0022008]; phosphorylation [GO:0016310]; positive regulation of epithelial cell proliferation [GO:0050679]; regulation of cell communication [GO:0010646]; regulation of signaling [GO:0023051] | basal plasma membrane [GO:0009925]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; epidermal growth factor binding [GO:0048408]; epidermal growth factor receptor activity [GO:0005006] | PF00757;PF14843;PF07714;PF01030;PF21314; | 6.10.250.2930;3.80.20.20;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, EGF receptor subfamily | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | 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: Probable receptor with tyrosine-protein kinase activity. | Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus) |
P13390 | FIBL1_BPT5 | MAITKIILQQMVTMDQNSITASKYPKYTVVLSNSISSITAADVTSAIESSKASGPAAKQSEINAKQSELNAKDSENEAEISATSSQQSATQSASSATASANSAKAAKTSETNANNSKNAAKTSETNAASSASSASSFATAAENSARAAKTSETNAGNSAQAADASKTAAANSATAAKTSETNAKKSETAAKTSETNAKTSENKAKEYLDMASELVSPVTQYDWPVGTNNNSVYVKIAKLTDPGAVSCHLTLMITNGGNYGSSYGNIDFVEISARGLNDARGVTSENITKFLSVRRLGSPNLAWDNQLRYGLVEGDGYFEV... | 3.4.21.- | null | adhesion receptor-mediated virion attachment to host cell [GO:0098671]; lipopolysaccharide-mediated virion attachment to host cell [GO:0039638]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718] | virus tail, fiber [GO:0098024] | serine-type peptidase activity [GO:0008236] | PF13884; | 1.10.10.10; | null | PTM: The cleaved C-terminus functions as an intramolecular chaperone and is removed by an autoproteolytic process after correct trimerization and folding. {ECO:0000269|PubMed:24316831, ECO:0000269|PubMed:26670244}. | SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:24198424}. Note=Component of the tail. Forms the L-shaped side fibers and are anchored onto the p132 dodecameric ring. {ECO:0000269|PubMed:24198424}. | null | null | null | null | null | FUNCTION: [Mature tail spike protein]: Assembles together with p132 to form the three L-shaped long tail fibers and the collar structure at the junction between the tail tube and the conical tail tip (PubMed:24198424). The three L-shaped long tail fibers recognize the host lipopolysaccharides that serve as adhesion rec... | Escherichia phage T5 (Enterobacteria phage T5) |
P13393 | TBP_YEAST | MADEERLKEFKEANKIVFDPNTRQVWENQNRDGTKPATTFQSEEDIKRAAPESEKDTSATSGIVPTLQNIVATVTLGCRLDLKTVALHARNAEYNPKRFAAVIMRIREPKTTALIFASGKMVVTGAKSEDDSKLASRKYARIIQKIGFAAKFTDFKIQNIVGSCDVKFPIRLEGLAFSHGTFSSYEPELFPGLIYRMVKPKIVLLIFVSGKIVLTGAKQREEIYQAFEAIYPVLSEFRKM | null | null | DNA-templated transcription initiation [GO:0006352]; negative regulation of DNA-templated transcription [GO:0045892]; nucleolar large rRNA transcription by RNA polymerase I [GO:0042790]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase III [GO:0006359... | nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; transcription factor TFIIA complex [GO:0005672]; transcription factor TFIID complex [GO:0005669]; transcription factor TFIIIB complex [GO:0000126]; transcription regulator complex [GO:0005667] | chromatin binding [GO:0003682]; disordered domain specific binding [GO:0097718]; DNA binding, bending [GO:0008301]; DNA-binding transcription factor binding [GO:0140297]; RNA polymerase I general transcription initiation factor binding [GO:0001179]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000... | PF00352; | 3.30.310.10; | TBP family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: General transcription factor that functions at the core of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P13395 | SPTCA_DROME | MENFTPKEVKILETVEDIQERREQVLSRYNDFKIETRQKREKLEDSRRFQYFKRDADELESWIHEKLQAASEESYRDPTNLQAKIQKHQAFEAEVSAHSNAIVSLDNTGQEMINQQHFASESIQVRLDELHKLWELLLSRLAEKGLKLQQALVLVQFLRQCEEVMFWIKDKETFVTADEFGQDLEHVEVLQRKFDEFQKDMASQEYRVTEVNQLADKLVQDGHPERDTITKRKEELNEAWQRLKQLAIVRQEKLFGAHEIQRFNRDADETVAWIAEKDVVLSSDDYGRDLASVQALQRKHEGVERDLAALEDKVSTLGAE... | null | null | actin cytoskeleton organization [GO:0030036]; actin filament capping [GO:0051693]; axon midline choice point recognition [GO:0016199]; central nervous system development [GO:0007417]; fusome organization [GO:0045478]; germarium-derived female germ-line cyst formation [GO:0030727]; germarium-derived oocyte fate determin... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cell cortex [GO:0005938]; cell junction [GO:0030054]; cell projection [GO:0042995]; cortical actin cytoskeleton [GO:0030864]; fusome [GO:0045169]; Golgi apparatus [GO:0005794]; lateral plasma membrane [GO:0016328]; motile cilium [GO:0031514]... | actin binding [GO:0003779]; actin filament binding [GO:0051015]; calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; microtubule binding [GO:0008017] | PF13499;PF08726;PF00018;PF00435; | 1.20.58.60;1.10.238.10;2.30.30.40; | Spectrin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11076973}. Golgi apparatus {ECO:0000269|PubMed:11076973}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:20237161}. Note=Near the inner surface of the plasma membrane of nearly all cells. Lva-alpha-spectrin complexes are found at the Golgi. Local... | null | null | null | null | null | FUNCTION: Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. Essential for larval survival and development. Stabilizes cell to cell interactions that a... | Drosophila melanogaster (Fruit fly) |
P13405 | RB_MOUSE | MPPKAPRRAAAAEPPPPPPPPPREDDPAQDSGPEELPLARLEFEEIEEPEFIALCQKLKVPDHVRERAWLTWEKVSSVDGILEGYIQKKKELWGICIFIAAVDLDEMPFTFTELQKSIETSVYKFFDLLKEIDTSTKVDNAMSRLLKKYNVLCALYSKLERTCELIYLTQPSSALSTEINSMLVLKISWITFLLAKGEVLQMEDDLVISFQLMLCVVDYFIKFSPPALLREPYKTAAIPINGSPRTPRRGQNRSARIAKQLENDTRIIEVLCKEHECNIDEVKNVYFKNFIPFINSLGIVSSNGLPEVESLSKRYEEVYL... | null | null | aortic valve morphogenesis [GO:0003180]; apoptotic process [GO:0006915]; cell differentiation [GO:0030154]; cell division [GO:0051301]; cell morphogenesis involved in neuron differentiation [GO:0048667]; cell population proliferation [GO:0008283]; cellular response to insulin stimulus [GO:0032869]; cellular response to... | chromatin [GO:0000785]; chromatin lock complex [GO:0061793]; cyclin/CDK positive transcription elongation factor complex [GO:0008024]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]; Rb-E2F complex [GO:0035189]; spindle [GO:0005819]; transcription regulator complex [GO:0005667] | disordered domain specific binding [GO:0097718]; DNA-binding transcription factor binding [GO:0140297]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; importin-alpha family protein binding [GO:0061676]; kinase binding [GO:0019900]; phosphoprotein binding [GO:0051219]; RNA polymerase II transcripti... | PF11934;PF01858;PF01857;PF08934; | 1.10.472.140;6.10.140.1380;6.10.250.530;1.10.472.10; | Retinoblastoma protein (RB) family | PTM: Phosphorylated (PubMed:8336704). Phosphorylated by CDK6 and CDK4, and subsequently by CDK2 at Ser-561 in G1, thereby releasing E2F1 which is then able to activate cell growth. Dephosphorylated at the late M phase. Phosphorylation of threonine residues in domain C promotes interaction between the C-terminal domain ... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8336704}. Note=During keratinocyte differentiation, acetylation by KAT2B/PCAF is required for nuclear localization. {ECO:0000250|UniProtKB:P06400}. | null | null | null | null | null | FUNCTION: Tumor suppressor that is a key regulator of the G1/S transition of the cell cycle (PubMed:8336704). The hypophosphorylated form binds transcription regulators of the E2F family, preventing transcription of E2F-responsive genes. Both physically blocks E2Fs transactivating domain and recruits chromatin-modifyin... | Mus musculus (Mouse) |
P13406 | FYN_XENLA | MGCVQCKDKEATKLTDERDNSLTQSLGYRYGTDPTPQHYPSFTVTTIPNYNNFHATAGQGLTVFGGVNSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFQKGEKFQILNSSEGDWWEARSLTTGGTGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTYLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKK... | 2.7.10.2 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; | cell differentiation [GO:0030154]; innate immune response [GO:0045087]; phosphorylation [GO:0016310]; T cell receptor signaling pathway [GO:0050852]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | extrinsic component of cytoplasmic side of plasma membrane [GO:0031234] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; signaling receptor binding [GO:0005102] | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Tyrosine-protein kinase implicated in the control of cell growth. Plays a role in the regulation of intracellular calcium levels (By similarity). Required in brain development and mature brain function with important roles in the regulation of axon growth, axon guidance, and neurite extension. Blocks axon out... | Xenopus laevis (African clawed frog) |
P13418 | POLS_CRPVC | ATFQDKQENSHIENEDKRLMSEQKEIVHFVSEGITPSTTALPDIVNLSTNYLDMTTREDRIHSIKDFLSGPIIIATNLWSSSDPVEKQLYTANFPEVLISNAMYQDKLKGFVGLRATLVVKVQVNSQPFQQGRLMLQYIPYAQYMPNRVTLINETLQGRSGCPTTDLELSVGTEVEMRIPYVSPHLYYNLITGQGSFGSIYVVVYSQLHDQVSGTGSIEYTVWAHLEDVDVQYPTGANIFTGNSPNYLSIAERIATGDFTETEMRKLWIHKTYLKRPARIYAQAAKELKQLETNNSPSTALGQISEGLTTLSHIPVLGNI... | null | null | null | host cell cytoplasm [GO:0030430]; viral capsid [GO:0019028] | structural molecule activity [GO:0005198] | PF08762;PF11492;PF00073; | 2.60.120.20; | Picornaviruses polyprotein family | PTM: Specific enzymatic cleavages in vivo yield mature proteins. | SUBCELLULAR LOCATION: [Capsid protein 1]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein 4]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein 2]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein 3]: Virion. Host cytoplasm {ECO:0000305... | null | null | null | null | null | FUNCTION: [Structural polyprotein]: Precursor of all the viral capsid proteins.; FUNCTION: Capsid protein 1, together with capsid proteins 2 and 3, form an icosahedral capsid protecting the viral RNA genome. The icosahedral capsid has a pseudo-T=3 symmetry with a diameter of approximately 300 Angstroms, and is composed... | Cricket paralysis virus (isolate Teleogryllus commodus/Australia/CrPVVIC/1968) (CrPV) |
P13423 | PAG_BACAN | MKKRKVLIPLMALSTILVSSTGNLEVIQAEVKQENRLLNESESSSQGLLGYYFSDLNFQAPMVVTSSTTGDLSIPSSELENIPSENQYFQSAIWSGFIKVKKSDEYTFATSADNHVTMWVDDQEVINKASNSNKIRLEKGRLYQIKIQYQRENPTEKGLDFKLYWTDSQNKKEVISSDNLQLPELKQKSSNSRKKRSTSAGPTVPDRDNDGIPDSLEVEGYTVDVKNKRTFLSPWISNIHEKKGLTKYKSSPEKWSTASDPYSDFEKVTGRIDKNVSPEARHPLVAAYPIVHVDMENIILSKNEDQSTQNTDSQTRTISK... | null | null | negative regulation of MAPK cascade [GO:0043409]; positive regulation of apoptotic process in another organism [GO:0044533]; protein homooligomerization [GO:0051260] | extracellular region [GO:0005576]; host cell cytosol [GO:0044164]; host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; toxin activity [GO:0090729] | PF03495;PF17475;PF17476;PF07691;PF20835; | 2.60.40.810;3.10.20.110;2.60.120.240;3.90.182.10; | Bacterial binary toxin family | PTM: Proteolytic activation by FURIN cleaves the protein in two parts, PA-20 and PA-63; the latter is the mature protein (PubMed:11207581, PubMed:1438214, PubMed:1644824, PubMed:8051159). The cleavage occurs at the cell surface and probably in the serum of infected animals as well; both native and cleaved PA are able t... | SUBCELLULAR LOCATION: [Protective antigen]: Secreted {ECO:0000269|PubMed:11207581, ECO:0000269|PubMed:12606539}. Host cell membrane {ECO:0000269|PubMed:11700562, ECO:0000269|PubMed:14507921}. Note=Secreted through the Sec-dependent secretion pathway (PubMed:12606539). Therefore, PA is translocated across the membrane i... | null | null | null | null | null | FUNCTION: Protective antigen constitutes one of the three proteins composing the anthrax toxin; it mediates attachment to host cells and translocation of edema factor (EF) and lethal factor (LF) into the host cytoplasm (PubMed:11700562, PubMed:14507921, PubMed:15243628, PubMed:15326297). PA associated with LF forms the... | Bacillus anthracis |
P13432 | SMR1_RAT | MKSLYLIFGLWILLACFQSGEGVRGPRRQHNPRRQQDPSTLPHYLGLQPDPNGGQIGVTITIPLNLQPPRVLVNLPGFITGPPLVVQGTTEYQYQWQLTAPDPTPLSNPPTQLHSTEQANTKTDAKISNTTATTQNSTDIFEGGGK | null | null | cellular response to lipopolysaccharide [GO:0071222]; negative regulation of peptidase activity [GO:0010466]; regulation of sensory perception of pain [GO:0051930] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | endopeptidase inhibitor activity [GO:0004866]; hormone activity [GO:0005179]; peptidase inhibitor activity [GO:0030414] | PF15621; | null | null | PTM: Several O-linked glycosylation sites might be present in the C-terminal part. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8112327}. Note=Found in blood. Secreted from the salivary compartment into the blood circulation, rather than through absorption by the gastro-intestinal tract. | null | null | null | null | null | FUNCTION: Sialorphin may be involved in the modulation of mineral balance between at least four systems: kidney, bone, tooth and circulation.; FUNCTION: Submandibular gland peptide T is able to directly or indirectly down-regulate cardiovascular depression induced by septic shock (endotoxin stimuli), or anaphylactic ch... | Rattus norvegicus (Rat) |
P13433 | RPOM_YEAST | MLRPAYKSLVKTSLLQRRLISSKGSKLFKPSPDSTSTILISEDPLVTGSSPTSSTTSGIISSNDFPLFNKNRKDAKSSISYQWKNPSELEFDPFNKSHASAVTSMTRTRDVMQLWSLLEACLQSNLMKRAFSILESLYLVPEHKQRFIEDYNMYLNSFSKNDPNFPILKMNEKLTNDLETSFKDVNYNDKTLAIMIHHALNFHSTTSSMLLKPIISAYLKMSVNGIREIFSCLDILTISDLNILMNDLKVITPSQLPNSVRPILESLTLSPTPVNNIENEEGLNKVEAENDSKLHKASNASSDSIKKPSLDPLREVSFHG... | 2.7.7.6 | null | DNA replication, synthesis of RNA primer [GO:0006269]; mitochondrial genome maintenance [GO:0000002]; mitochondrial transcription [GO:0006390] | cytoplasm [GO:0005737]; mitochondrial DNA-directed RNA polymerase complex [GO:0034245]; mitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739] | DNA primase activity [GO:0003896]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; mitochondrial promoter sequence-specific DNA binding [GO:0001018] | PF00940;PF14700; | 1.10.287.260;1.10.287.280;1.10.150.20;1.10.1320.10; | Phage and mitochondrial RNA polymerase family | null | SUBCELLULAR LOCATION: Mitochondrion. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10031, ECO:0000255|PROSITE-ProRule:PRU10032}; | null | null | null | null | FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P13437 | THIM_RAT | MALLRGVFIVAAKRTPFGAYGGLLKDFTATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETGALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYSVRNVRFGTKFGLDLKLEDTLWAGLTDQHVKLPMGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQNLPPVFKKEGTVTAGNASGMSDGAGVVIIASEDAVKKHNFTPLARVVGYFVSGCDPAIMGIGPVPAITGALKKAGLSLKDMDLIDVN... | 2.3.1.16; 2.3.1.9; 3.1.2.-; 3.1.2.1; 3.1.2.2 | null | acetyl-CoA metabolic process [GO:0006084]; cellular response to hypoxia [GO:0071456]; fatty acid beta-oxidation [GO:0006635]; negative regulation of mitochondrial membrane permeability involved in apoptotic process [GO:1902109]; negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic ... | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | acetyl-CoA C-acetyltransferase activity [GO:0003985]; acetyl-CoA C-acyltransferase activity [GO:0003988]; acetyl-CoA hydrolase activity [GO:0003986]; fatty acyl-CoA hydrolase activity [GO:0047617] | PF02803;PF00108; | 3.40.47.10; | Thiolase-like superfamily, Thiolase family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16476568}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA; Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16; Evidence={ECO:0000269|PubMed:16476568}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21565; Evidence={ECO:0000305|PubMed:1... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.4 uM for acetoacetyl-CoA {ECO:0000269|PubMed:16476568}; KM=0.71 mM for acetyl-CoA {ECO:0000269|PubMed:16476568}; | PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000269|PubMed:16476568}. | null | null | FUNCTION: In the production of energy from fats, this is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA (Probable). Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain unbranched 3... | Rattus norvegicus (Rat) |
P13439 | UMPS_MOUSE | MEVASQALGPLVTELYDVQAFKFGSFVLKSGLSSPVYIDLRGIVSRPRLLSQVADILFQTAKNAGISFDSVCGVPYTALPLATVICSANHIPMLIRRKETKDYGTKRLVEGEINPGQTCLVIEDVVTSGASVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQAQGIRLHAVCTLSQMLEILQQQEKIDADMVGRVKRFIQENVFSAANHNGLPPPEKKACKELSFGARAELPGTHPLASKLLRLMQKKETNLCLSADVSEARELLQLADALGPSICMLKTHVDILNDFTLDVMEELTALAKRHEFLIFEDRKFADIGN... | 2.4.2.10; 4.1.1.23 | null | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; cellular response to xenobiotic stimulus [GO:0071466]; female pregnancy [GO:0007565]; lactation [GO:0007595]; pyrimidine nucleobase biosynthetic process [GO:0019856]; UDP biosynthetic process [GO:0006225]... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | orotate phosphoribosyltransferase activity [GO:0004588]; orotidine-5'-phosphate decarboxylase activity [GO:0004590] | PF00215;PF00156; | 3.40.50.2020;3.20.20.70; | Purine/pyrimidine phosphoribosyltransferase family; OMP decarboxylase family | null | null | CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000250|UniProtKB:P11172}; PhysiologicalDirection=right-to-left; Xref=Rhea:RH... | null | PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. {ECO:0000250|UniProtKB:P11172}.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. {ECO:0000250|UniProtKB:P11172}. | null | null | FUNCTION: Bifunctional enzyme catalyzing the last two steps of de novo pyrimidine biosynthesis, orotate phosphoribosyltransferase (OPRT), which converts orotate to orotidine-5'-monophosphate (OMP), and orotidine-5'-monophosphate decarboxylase (ODC), the terminal enzymatic reaction that decarboxylates OMP to uridine mon... | Mus musculus (Mouse) |
P13444 | METK1_RAT | MNGPVDGLCDHSLSEEGAFMFTSESVGEGHPDKICDQISDAVLDAHLKQDPNAKVACETVCKTGMVLLCGEITSMAMIDYQRVVRDTIKHIGYDDSAKGFDFKTCNVLVALEQQSPDIAQCVHLDRNEEDVGAGDQGLMFGYATDETEECMPLTIVLAHKLNTRMADLRRSGVLPWLRPDSKTQVTVQYVQDNGAVIPVRVHTIVISVQHNEDITLEAMREALKEQVIKAVVPAKYLDEDTIYHLQPSGRFVIGGPQGDAGVTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKAGLCRRVLVQVS... | 2.5.1.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:10873471}; Note=Binds 2 magnesium ions per subunit. The magnesium ions interact primarily with the substrate. {ECO:0000305|PubMed:10873471}; COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000305|PubMed:10873471}; Note=Binds 1 potas... | methionine catabolic process [GO:0009087]; one-carbon metabolic process [GO:0006730]; protein homotetramerization [GO:0051289]; protein-containing complex assembly [GO:0065003]; S-adenosylmethionine biosynthetic process [GO:0006556] | cytosol [GO:0005829]; methionine adenosyltransferase complex [GO:0048269]; nuclear matrix [GO:0016363] | ADP binding [GO:0043531]; amino acid binding [GO:0016597]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; methionine adenosyltransferase activity [GO:0004478] | PF02773;PF02772;PF00438; | 3.30.300.10; | AdoMet synthase family | PTM: S-nitrosylation of Cys-121 inactivates the enzyme. {ECO:0000269|PubMed:10358060, ECO:0000269|PubMed:9755242}.; PTM: An intrachain disulfide bond can be formed (PubMed:10601859). The protein structure shows that the relevant Cys residues are in a position that would permit formation of a disulfide bond (PubMed:1087... | null | CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000269|PubMed:10873471, ECO:0000269|PubMed:1517209... | null | PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. {ECO:0000269|PubMed:10873471, ECO:0000269|PubMed:1517209, ECO:0000269|PubMed:9755242}. | null | null | FUNCTION: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate. {ECO:0000269|PubMed:10873471, ECO:0000269|PubMed:151... | Rattus norvegicus (Rat) |
P13445 | RPOS_ECOLI | MSQNTLKVHDLNEDAEFDENGVEVFDEKALVEQEPSDNDLAEEELLSQGATQRVLDATQLYLGEIGYSPLLTAEEEVYFARRALRGDVASRRRMIESNLRLVVKIARRYGNRGLALLDLIEEGNLGLIRAVEKFDPERGFRFSTYATWWIRQTIERAIMNQTRTIRLPIHIVKELNVYLRTARELSHKLDHEPSAEEIAEQLDKPVDDVSRMLRLNERITSVDTPLGGDSEKALLDILADEKENGPEDTTQDDDMKQSIVKWLFELNAKQREVLARRFGLLGYEAATLEDVGREIGLTRERVRQIQVEGLRRLREILQTQ... | null | null | DNA-templated transcription initiation [GO:0006352]; negative regulation of DNA-templated transcription [GO:0045892]; regulation of DNA-templated transcription initiation [GO:2000142] | cytoplasm [GO:0005737]; cytosolic DNA-directed RNA polymerase complex [GO:0000345]; sigma factor antagonist complex [GO:1903865] | bacterial-type RNA polymerase core enzyme binding [GO:0001000]; DNA binding [GO:0003677]; sigma factor activity [GO:0016987] | PF00140;PF04542;PF04539;PF04545; | 1.10.601.10;1.10.10.10; | Sigma-70 factor family, RpoS subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00959}. | null | null | null | null | null | FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the master transcriptional regulator of the stationary phase and the general stress response. Controls, positively or negatively, the expression of severa... | Escherichia coli (strain K12) |
P13448 | NHAA_RHOER | MSVTIDHTTENAAPAQAPVSDRAWALFRALDGKGLVPDGYVEGWKKTFEEDFSPRRGAELVARAWTDPEFRQLLLTDGTAAVAQYGYLGPQGEYIVAVEDTPTLKNVIVCSLCSCTAWPILGLPPTWYKSFEYRARVVREPRKVLSEMGTEIASDIEIRVYDTTAETRYMVLPQRPAGTEGWSQEQLQEIVTKDCLIGVAIPQVPTV | 4.2.1.84 | COFACTOR: Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000269|PubMed:9586994}; Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000269|PubMed:9586994}; | null | null | indole-3-acetonitrile nitrile hydratase activity [GO:0080109]; transition metal ion binding [GO:0046914] | PF02979; | 3.90.330.10; | Nitrile hydratase subunit alpha family | PTM: Oxidation on Cys-113 is essential for the activity. {ECO:0000269|PubMed:9368004, ECO:0000269|PubMed:9586994}.; PTM: Oxidation on Cys-115 stabilizes the Fe-NO ligand coordinated in the inactive form. {ECO:0000269|PubMed:9586994}. | null | CATALYTIC ACTIVITY: Reaction=an aliphatic amide = a nitrile + H2O; Xref=Rhea:RHEA:12673, ChEBI:CHEBI:15377, ChEBI:CHEBI:18379, ChEBI:CHEBI:65285; EC=4.2.1.84; | null | null | null | null | FUNCTION: NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. Industrial production of acrylamide is now being developed using some of the enzymes of this class. | Rhodococcus erythropolis (Arthrobacter picolinophilus) |
P13458 | SBCC_ECOLI | MKILSLRLKNLNSLKGEWKIDFTREPFASNGLFAITGPTGAGKTTLLDAICLALYHETPRLSNVSQSQNDLMTRDTAECLAEVEFEVKGEAYRAFWSQNRARNQPDGNLQVPRVELARCADGKILADKVKDKLELTATLTGLDYGRFTRSMLLSQGQFAAFLNAKPKERAELLEELTGTEIYGQISAMVFEQHKSARTELEKLQAQASGVTLLTPEQVQSLTASLQVLTDEEKQLITAQQQEQQSLNWLTRQDELQQEASRRQQALQQALAEEEKAQPQLAALSLAQPARNLRPHWERIAEHSAALAHIRQQIEEVNTRL... | null | null | DNA recombination [GO:0006310]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; double-strand break repair [GO:0006302] | DNA repair complex [GO:1990391] | 3'-5'-DNA exonuclease activity [GO:0008296]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA exonuclease activity [GO:0004529]; double-stranded DNA endonuclease activity [GO:1990238]; single-stranded DNA endodeoxyribonuclease activity [GO:0000014] | PF13476;PF13558; | 3.40.50.300; | SMC family, SbcC subfamily | null | null | null | null | null | null | null | FUNCTION: SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity. | Escherichia coli (strain K12) |
P13466 | GELA_DICDI | MAAAPSGKTWIDVQKKTFTGWANNYLKERILKIEDLATSLEDGVLLINLLEIISSKKILKYNKAPKIRMQKIENNNMAVNFIKSEGLKLVGIGAEDIVDSQLKLILGLIWTLILRYQIQMSESDNSPKAALLEWVRKQVAPYKVVVNNFTDSWCDGRVLSALTDSLKPGVREMSTLTGDAVQDIDRSMDIALEEYEIPKIMDANDMNSLPDELSVITYVSYFRDYALNKEKRDADALAALEKKRRETSDASKVEVYGPGVEGGFVNKSADFHIKAVNYYGEPLANGGEGFTVSVVGADGVEVPCKLVDNKNGIYDASYTA... | null | null | actin crosslink formation [GO:0051764]; actin cytoskeleton organization [GO:0030036]; cell migration [GO:0016477]; cell motility [GO:0048870]; chemotaxis to cAMP [GO:0043327]; hyperosmotic response [GO:0006972]; lamellipodium assembly [GO:0030032]; phagocytosis [GO:0006909]; phototaxis [GO:0042331]; pseudopodium assemb... | anterior cell cortex [GO:0061802]; cell cortex [GO:0005938]; cell leading edge [GO:0031252]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; lateral cell cortex [GO:0097575]; macropinocytic cup [GO:0070685]; phagocytic cup [GO:0001891]; plasma membrane [GO:0005886]; ... | actin filament binding [GO:0051015]; mitogen-activated protein kinase binding [GO:0051019]; protein kinase B binding [GO:0043422]; small GTPase binding [GO:0031267] | PF00307;PF00630; | 1.10.418.10;2.60.40.10; | null | null | null | null | null | null | null | null | FUNCTION: F-actin cross-linking protein. | Dictyostelium discoideum (Social amoeba) |
P13469 | MODU_DROME | MAQKKAVTVKGKKATNGEEKPLAKRVTKSTKVQEEETVVPQSPSKKSRKQPVKEVPQFSEEDESDVEEQNDEQPGDDSDFETEEAAGLIDDEAEEDEEYNSDDEEDDDDDELEPGEVSKSEGADEVDESDDDEEAPVEKPVSKKSEKANSEKSEENRGIPKVKVGKIPLGTPKNQIVFVTNLPNEYLHKDLVALFAKFGRLSALQRFTNLNGNKSVLIAFDTSTGAEAVLQAKPKALTLGDNVLSVSQPRNKEENNERTVVVGLIGPNITKDDLKTFFEKVAPVEAVTISSNRLMPRAFVRLASVDDIPKALKLHSTELF... | null | null | mRNA splicing, via spliceosome [GO:0000398]; nuclear mRNA surveillance [GO:0071028]; poly(A)+ mRNA export from nucleus [GO:0016973] | cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; ribonucleoprotein complex [GO:1990904] | DNA binding [GO:0003677]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]; sequence-specific DNA binding [GO:0043565] | PF00076; | 3.30.70.330; | null | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Its capacity to bind DNA and protein(s), and its differential expression during development suggest a role in the regulation of gene expression during Drosophila development. It could, in interaction with other factors, be required for the translation of instructions provided by pattern forming genes and cont... | Drosophila melanogaster (Fruit fly) |
P13470 | GTFC_STRMU | MEKKVRFKLRKVKKRWVTVSVASAVVTLTSLSGSLVKADSTDDRQQAVTESQASLVTTSEAAKETLTATDTSTATSATSQPTATVTDNVSTTNQSTNTTANTANFDVKPTTTSEQSKTDNSDKIIATSKAVNRLTATGKFVPANNNTAHSRTVTDKIVPIKPKIGKLKQPSSLSQDDIAALGNVKNIRKVNGKYYYYKEDGTLQKNYALNINGKTFFFDETGALSNNTLPSKKGNITNNDNTNSFAQYNQVYSTDAANFEHVDHYLTAESWYRPKYILKDGKTWTQSTEKDFRPLLMTWWPDQETQRQYVNYMNAQLGIH... | 2.4.1.5 | null | glucan biosynthetic process [GO:0009250] | extracellular region [GO:0005576] | dextransucrase activity [GO:0047849]; glucosyltransferase activity [GO:0046527] | PF01473;PF19127;PF02324;PF19258; | 2.10.270.10;3.20.20.470;2.30.30.420; | Glycosyl hydrolase 70 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=[(1->6)-alpha-D-glucosyl](n) + sucrose = [(1->6)-alpha-D-glucosyl](n+1) + D-fructose; Xref=Rhea:RHEA:18825, Rhea:RHEA-COMP:11144, Rhea:RHEA-COMP:11145, ChEBI:CHEBI:17992, ChEBI:CHEBI:18269, ChEBI:CHEBI:37721; EC=2.4.1.5; | null | null | null | null | FUNCTION: Production of extracellular glucans, that are thought to play a key role in the development of the dental plaque because of their ability to adhere to smooth surfaces and mediate the aggregation of bacterial cells and food debris. | Streptococcus mutans serotype c (strain ATCC 700610 / UA159) |
P13473 | LAMP2_HUMAN | MVCFRLFPVPGSGLVLVCLVLGAVRSYALELNLTDSENATCLYAKWQMNFTVRYETTNKTYKTVTISDHGTVTYNGSICGDDQNGPKIAVQFGPGFSWIANFTKAASTYSIDSVSFSYNTGDNTTFPDAEDKGILTVDELLAIRIPLNDLFRCNSLSTLEKNDVVQHYWDVLVQAFVQNGTVSTNEFLCDKDKTSTVAPTIHTTVPSPTTTPTPKEKPEAGTYSVNNGNDTCLLATMGLQLNITQDKVASVININPNTTHSTGSCRSHTALLRLNSSTIKYLDFVFAVKNENRFYLKEVNISMYLVNGSVFSIANNNLSY... | null | null | autophagosome maturation [GO:0097352]; cellular response to starvation [GO:0009267]; chaperone-mediated autophagy [GO:0061684]; lysosomal lumen acidification [GO:0007042]; lysosomal protein catabolic process [GO:1905146]; muscle cell cellular homeostasis [GO:0046716]; negative regulation of NLRP3 inflammasome complex a... | autolysosome [GO:0044754]; autophagosome membrane [GO:0000421]; azurophil granule membrane [GO:0035577]; chaperone-mediated autophagy translocation complex [GO:0061742]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; ficolin-1-rich granule membrane [GO:0101003]; intracellular membrane-bounded org... | enzyme binding [GO:0019899]; ion channel inhibitor activity [GO:0008200]; protein domain specific binding [GO:0019904]; signaling adaptor activity [GO:0035591] | PF01299;PF21222; | 2.40.160.110; | LAMP family | PTM: O- and N-glycosylated; some of the 16 N-linked glycans are polylactosaminoglycans. {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:2243102, ECO:0000269|PubMed:2912382, ECO:0000269|PubMed:8323299}. | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000255|PROSITE-ProRule:PRU00740, ECO:0000269|PubMed:11082038, ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:18644871, ECO:0000269|PubMed:2912382}; Single-pass type I membrane protein {ECO:0000255|PROSITE-ProRule:PRU00740, ECO:0000269|PubMed:17897319}. Endosome membrane {E... | null | null | null | null | null | FUNCTION: Lysosomal membrane glycoprotein which plays an important role in lysosome biogenesis, lysosomal pH regulation and autophagy (PubMed:11082038, PubMed:18644871, PubMed:24880125, PubMed:27628032, PubMed:36586411, PubMed:37390818, PubMed:8662539). Acts as an important regulator of lysosomal lumen pH regulation by... | Homo sapiens (Human) |
P13481 | P53_CHLAE | MEEPQSDPSIEPPLSQETFSDLWKLLPENNVLSPLPSQAVDDLMLSPDDLAQWLTEDPGPDEAPRMSEAAPHMAPTPAAPTPAAPAPAPSWPLSSSVPSQKTYHGSYGFRLGFLHSGTAKSVTCTYSPDLNKMFCQLAKTCPVQLWVDSTPPPGSRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYSDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENFRKKGEPCHELPPGSTKRALPNNTSSSPQPKK... | 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]; cellular senescence [GO:0090398]; circadian behavior [GO:0048512]; DNA damage response [GO:0006974]; entrainment of circadian clock by photoperiod [GO:0043153]; negative regulation of cell growth [GO:0030308]; negative regulation of DNA-templated transcription [GO:0045892]; nucleotide-excision ... | centrosome [GO:0005813]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634]; PML body [GO:0016605] | ATP-dependent DNA/DNA annealing activity [GO:0036310]; copper ion binding [GO:0005507]; DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [G... | PF00870;PF08563;PF07710;PF18521; | 2.60.40.720;6.10.50.20;4.10.170.10; | P53 family | PTM: Phosphorylation on Ser residues mediates transcriptional activation. Phosphorylation at Ser-9 by HIPK4 increases repression activity on BIRC5 promoter (By similarity). Phosphorylated on Thr-18 by VRK1, which may prevent the interaction with MDM2. Phosphorylated on Ser-20 by CHEK2 in response to DNA damage, which p... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04637}. Nucleus {ECO:0000250|UniProtKB:P04637}. Nucleus, PML body {ECO:0000250|UniProtKB:P04637}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P04637}. Mitochondrion matrix {ECO:0000250|UniProtKB:P04637}. Cytoplasm, cytoskeleton, microtubule organizing center, cen... | null | null | null | null | null | FUNCTION: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of t... | Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops) |
P13482 | TREA_ECOLI | MKSPAPSRPQKMALIPACIFLCFAALSVQAEETPVTPQPPDILLGPLFNDVQNAKLFPDQKTFADAVPNSDPLMILADYRMQQNQSGFDLRHFVNVNFTLPKEGEKYVPPEGQSLREHIDGLWPVLTRSTENTEKWDSLLPLPEPYVVPGGRFREVYYWDSYFTMLGLAESGHWDKVADMVANFAHEIDTYGHIPNGNRSYYLSRSQPPFFALMVELLAQHEGDAALKQYLPQMQKEYAYWMDGVENLQAGQQEKRVVKLQDGTLLNRYWDDRDTPRPESWVEDIATAKSNPNRPATEIYRDLRSAAASGWDFSSRWMDN... | 3.2.1.28 | null | cellular hyperosmotic response [GO:0071474]; DNA damage response [GO:0006974]; trehalose catabolic process [GO:0005993] | outer membrane-bounded periplasmic space [GO:0030288] | alpha,alpha-trehalase activity [GO:0004555] | PF01204; | 1.50.10.10; | Glycosyl hydrolase 37 family | null | SUBCELLULAR LOCATION: Periplasm. | CATALYTIC ACTIVITY: Reaction=alpha,alpha-trehalose + H2O = alpha-D-glucose + beta-D-glucose; Xref=Rhea:RHEA:32675, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:16551, ChEBI:CHEBI:17925; EC=3.2.1.28; Evidence={ECO:0000255|HAMAP-Rule:MF_01060, ECO:0000269|PubMed:17455176, ECO:0000269|PubMed:19123216}; | null | null | null | null | FUNCTION: Provides the cells with the ability to utilize trehalose at high osmolarity by splitting it into glucose molecules that can subsequently be taken up by the phosphotransferase-mediated uptake system. | Escherichia coli (strain K12) |
P13485 | TAGF_BACSU | MSLVVDTNKRKQKGKSFYTEEQKKVMIENTVIKCILKSLKNNLGSLELLISIDSEHQFLEDYQLFLKLKERRSGTESEFPLQNTGSLEYKTEINAHVLPMPVEMGQTYDFYVEFRKKYEDAEQEPLLKRLSAEVNSIERAFHVDQTTELLILPYTTDKGNFSIKVKREAKIIRFDQIEISSEEISITGYAGYLSSENQYRIKNLNLILKKGGETPIEEKFPIKLERKTHGLENMRADGFVPELYDFEVKVPLKEIPFSNEKRYVYRLFMEYICNDDEGTDIQFNSTALVLGDRKNKLKGLVSIIKTNNAPVRYEVFKKKK... | 2.7.8.12 | null | cell wall organization [GO:0071555]; teichoic acid biosynthetic process [GO:0019350] | plasma membrane [GO:0005886] | CDP-glycerol glycerophosphotransferase activity [GO:0047355] | PF04464; | 3.40.50.11820;3.40.50.12580; | CDP-glycerol glycerophosphotransferase family | null | SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=4-O-[(2R)-glycerylphospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + n CDP-glycerol = 4-O-{[(2R)-1-glycerylphospho](n)-(2R)-1-glycerylphospho}-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl undecaprenyl ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=340 uM for CDP-glycerol {ECO:0000269|PubMed:12637499}; KM=230 uM for CDP-glycerol {ECO:0000269|PubMed:16141206}; KM=152 uM for CDP-glycerol {ECO:0000269|PubMed:19520862}; KM=2.6 uM for lipid III analog {ECO:0000269|PubMed:18465758}; Note=kcat for CDP-glycerol is 14... | PATHWAY: Cell wall biogenesis; poly(glycerol phosphate) teichoic acid biosynthesis. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:16141206}; | null | FUNCTION: Responsible for the polymerization of the main chain of the major teichoic acid by sequential transfer of glycerol phosphate units from CDP-glycerol to the disaccharide linkage unit. Synthesizes polymers of approximately 35 glycerol phosphate units in length. {ECO:0000269|PubMed:12637499, ECO:0000269|PubMed:1... | Bacillus subtilis (strain 168) |
P13487 | KAX11_LEIHE | MKILSVLLLALIICSIVGWSEAQFTNVSCTTSKECWSVCQRLHNTSRGKCMNKKCRCYS | null | null | defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; potassium channel regulator activity [GO:0015459]; toxin activity [GO:0090729] | PF00451; | 3.30.30.10; | Short scorpion toxin superfamily, Potassium channel inhibitor family, Alpha-KTx 01 subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2453055}. | null | null | null | null | null | FUNCTION: This toxin inhibits numerous potassium channels: shaker (Ki=227 nM), Kv1.2/KCNA2 (nanomolar range), Kv1.3/KCNA3 (nanomolar range), Kv1.5/KCNA5 (Kd>100 nM), Kv1.6/KCNA6 (Ki=22 nM), KCa1.1/KCNMA1 (IC(50)=5.9 nM). It blocks channel activity by a simple bimolecular inhibition process. It also shows a weak interac... | Leiurus hebraeus (Deathstalker scorpion) (Leiurus quinquestriatus hebraeus) |
P13489 | RINI_HUMAN | MSLDIQSLDIQCEELSDARWAELLPLLQQCQVVRLDDCGLTEARCKDISSALRVNPALAELNLRSNELGDVGVHCVLQGLQTPSCKIQKLSLQNCCLTGAGCGVLSSTLRTLPTLQELHLSDNLLGDAGLQLLCEGLLDPQCRLEKLQLEYCSLSAASCEPLASVLRAKPDFKELTVSNNDINEAGVRVLCQGLKDSPCQLEALKLESCGVTSDNCRDLCGIVASKASLRELALGSNKLGDVGMAELCPGLLHPSSRLRTLWIWECGITAKGCGDLCRVLRAKESLKELSLAGNELGDEGARLLCETLLEPGCQLESLWV... | null | null | cell migration [GO:0016477]; mRNA catabolic process [GO:0006402]; regulation of angiogenesis [GO:0045765]; regulation of Arp2/3 complex-mediated actin nucleation [GO:0034315]; regulation of inflammatory response [GO:0050727] | angiogenin-PRI complex [GO:0032311]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; lamellipodium [GO:0030027]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886] | ribonuclease inhibitor activity [GO:0008428] | PF13516;PF18779; | 3.80.10.10; | null | PTM: The N-terminus is blocked.; PTM: At least 30 of the 32 cysteine residues are in the reduced form. | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play a role in redox homeostasis. {ECO:0000269|PubMed:12578357, ECO:0000269|PubMed:14515218, ECO:0000269|PubMed:17292889}. | Homo sapiens (Human) |
P13496 | DCTN1_DROME | MSEKNLKVGARVELTGKDLLGTVAYVGMTSFAVGKWVGVVLDEPKGKNSGSIKGQQYFQCDENCGMFVRPTQLRLLEAAPGSRRSIEDVSGATPTAAQPTKARLSSSRTSLSSSRQSLLGSRTQLTTSLSERTASSSSIGPRKSLAPQNSKDKESPSTSLAEGAPAASGGNGAASHASSKRASFVETGFLEILKPQFTPSQPLRSPSFTMPSNSGAEDKVALLEAQKTSAELQAQLADLTEKLETLKQRRNEDKERLREFDKMKIQFEQLQEFRTKIMGAQASLQKELLRAKQEAKDAIEAKEQHAQEMADLADNVEMIT... | null | null | axon extension [GO:0048675]; axonal transport of mitochondrion [GO:0019896]; cell fate determination [GO:0001709]; cellularization [GO:0007349]; centrosome localization [GO:0051642]; centrosome separation [GO:0051299]; compound eye photoreceptor cell differentiation [GO:0001751]; compound eye photoreceptor development ... | aster [GO:0005818]; axon [GO:0030424]; axon cytoplasm [GO:1904115]; cell tip [GO:0051286]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; dynactin complex [GO:0005869]; dynein complex [GO:0030286]; kinetochore [GO:0000776]; microtubule associated complex [GO:0005875]; microtubule plus-end [GO:0035371]; midbody [GO:00... | dynein complex binding [GO:0070840]; dynein intermediate chain binding [GO:0045505]; microtubule binding [GO:0008017]; microtubule plus-end binding [GO:0051010] | PF01302;PF12455; | 2.30.30.190; | Dynactin 150 kDa subunit family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q14203}. | null | null | null | null | null | FUNCTION: Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity). Plays a key role in dynein-mediated retrograde transport of vesicles and organelles along microtubules by recruiting and tethering dynein to microtubules. Binds to both dyn... | Drosophila melanogaster (Fruit fly) |
P13497 | BMP1_HUMAN | MPGVARLPLLLGLLLLPRPGRPLDLADYTYDLAEEDDSEPLNYKDPCKAAAFLGDIALDEEDLRAFQVQQAVDLRRHTARKSSIKAAVPGNTSTPSCQSTNGQPQRGACGRWRGRSRSRRAATSRPERVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPCGCCSYVGRRGGGPQAISIGKNCDKFGIVVHELGHVVGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEPQEVESLGETYDFDSIMHYARNTFSRGIFLDTIVPKYEVNGVKPPIGQRTRLSKGDIAQARKLYKCP... | 3.4.24.19 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|PROSITE-ProRule:PRU01211, ECO:0000269|PubMed:18824173}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU01211, ECO:0000269|PubMed:18824173}; | cartilage condensation [GO:0001502]; cell differentiation [GO:0030154]; collagen fibril organization [GO:0030199]; dorsal/ventral pattern formation [GO:0009953]; ossification [GO:0001503]; positive regulation of cartilage development [GO:0061036]; protein processing [GO:0016485]; proteolysis [GO:0006508]; skeletal syst... | extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; vesicle [GO:0031982] | calcium ion binding [GO:0005509]; cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; identical protein binding [GO:0042802]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]; zinc ion bi... | PF01400;PF00431;PF07645;PF14670; | 3.40.390.10;2.10.25.10;2.60.120.290; | null | PTM: Proteolytically activated in the trans-Golgi network by furin-like/paired basic proprotein convertases, cleavage is not required for secretion. {ECO:0000269|PubMed:12637569}. | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:12637569}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:12637569}. Secreted {ECO:0000269|PubMed:33206546}. Note=Co-localizes with POSTN in the Golgi. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform BMP1-3]: Secreted... | CATALYTIC ACTIVITY: Reaction=Cleavage of the C-terminal propeptide at Ala-|-Asp in type I and II procollagens and at Arg-|-Asp in type III.; EC=3.4.24.19; | null | null | null | null | FUNCTION: Metalloprotease that plays key roles in regulating the formation of the extracellular matrix (ECM) via processing of various precursor proteins into mature functional enzymes or structural proteins (PubMed:33206546). Thereby participates in several developmental and physiological processes such as cartilage a... | Homo sapiens (Human) |
P13498 | CY24A_HUMAN | MGQIEWAMWANEQALASGLILITGGIVATAGRFTQWYFGAYSIVAGVFVCLLEYPRGKRKKGSTMERWGQKYMTAVVKLFGPFTRNYYVRAVLHLLLSVPAGFLLATILGTACLAIASGIYLLAAVRGEQWTPIEPKPRERPQIGGTIKQPPSNPPPRPPAEARKKPSEEEAAVAAGGPPGGPQVNPIPVTDEVV | null | null | cytochrome complex assembly [GO:0017004]; establishment of localization in cell [GO:0051649]; hydrogen peroxide biosynthetic process [GO:0050665]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; mucus secretion [GO:0070254]; positive regulation of defense response to bacterium [GO:1900426]; pos... | endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; membrane [GO:0016020]; NADPH oxidase complex [GO:0043020]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; secretory granule [GO:0030141]; specific granule membrane [GO:0035579]; tertiary granule membrane [GO:0070821] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; protein heterodimerization activity [GO:0046982]; SH3 domain binding [GO:0017124] | PF05038; | null | P22phox family | PTM: The heme prosthetic group could be coordinated with residues of the light chain, the heavy chain, or both, and it is possible that more than one heme is present per cytochrome b-245.; PTM: Phosphorylation at Thr-147 enhances NADPH oxidase activity by promoting p47phox binding. {ECO:0000250}.; PTM: Ubiquitinated at... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15585859, ECO:0000269|PubMed:17140397, ECO:0000269|PubMed:22808130}. Note=As unassembled monomer may localize to the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q61462}. | null | null | null | null | null | FUNCTION: Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. Associates with NOX3 to form a functional NADPH oxidase constitutively generating superoxide. {ECO:0000269|PubMed:15824103, ECO:0000269|PubMed:17140397}. | Homo sapiens (Human) |
P13500 | CCL2_HUMAN | MKVSAALLCLLLIAATFIPQGLAQPDAINAPVTCCYNFTNRKISVQRLASYRRITSSKCPKEAVIFKTIVAKEICADPKQKWVQDSMDHLDKQTQTPKT | null | null | angiogenesis [GO:0001525]; animal organ morphogenesis [GO:0009887]; astrocyte cell migration [GO:0043615]; cell adhesion [GO:0007155]; cell surface receptor signaling pathway [GO:0007166]; cellular homeostasis [GO:0019725]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to interl... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | CCR chemokine receptor binding [GO:0048020]; CCR2 chemokine receptor binding [GO:0031727]; chemokine activity [GO:0008009]; protein kinase activity [GO:0004672]; signaling receptor binding [GO:0005102] | PF00048; | 2.40.50.40; | Intercrine beta (chemokine CC) family | PTM: Processing at the N-terminus can regulate receptor and target cell selectivity (PubMed:8627182). Deletion of the N-terminal residue converts it from an activator of basophil to an eosinophil chemoattractant (PubMed:8627182). {ECO:0000269|PubMed:8627182}.; PTM: N-Glycosylated. {ECO:0000269|PubMed:2513477}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23955712, ECO:0000269|PubMed:2513477}. | null | null | null | null | null | FUNCTION: Acts as a ligand for C-C chemokine receptor CCR2 (PubMed:10529171, PubMed:10587439, PubMed:9837883). Signals through binding and activation of CCR2 and induces a strong chemotactic response and mobilization of intracellular calcium ions (PubMed:10587439, PubMed:9837883). Exhibits a chemotactic activity for mo... | Homo sapiens (Human) |
P13501 | CCL5_HUMAN | MKVSAAALAVILIATALCAPASASPYSSDTTPCCFAYIARPLPRAHIKEYFYTSGKCSNPAVVFVTRKNRQVCANPEKKWVREYINSLEMS | null | null | activation of phospholipase D activity [GO:0031584]; calcium ion transport [GO:0006816]; cell-cell signaling [GO:0007267]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to t... | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | CCR chemokine receptor binding [GO:0048020]; CCR1 chemokine receptor binding [GO:0031726]; CCR4 chemokine receptor binding [GO:0031729]; CCR5 chemokine receptor binding [GO:0031730]; chemoattractant activity [GO:0042056]; chemokine activity [GO:0008009]; chemokine receptor antagonist activity [GO:0046817]; chemokine re... | PF00048; | 2.40.50.40; | Intercrine beta (chemokine CC) family | PTM: N-terminal processed form RANTES(3-68) is produced by proteolytic cleavage, probably by DPP4, after secretion from peripheral blood leukocytes and cultured sarcoma cells. {ECO:0000269|PubMed:9516414}.; PTM: N-terminal processed form RANTES(4-68) is produced by proteolytic cleavage by cathepsin CTSG. {ECO:0000269|P... | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Chemoattractant for blood monocytes, memory T-helper cells and eosinophils. Causes the release of histamine from basophils and activates eosinophils. May activate several chemokine receptors including CCR1, CCR3, CCR4 and CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant RAN... | Homo sapiens (Human) |
P13504 | IL1R1_MOUSE | MENMKVLLGLICLMVPLLSLEIDVCTEYPNQIVLFLSVNEIDIRKCPLTPNKMHGDTIIWYKNDSKTPISADRDSRIHQQNEHLWFVPAKVEDSGYYYCIVRNSTYCLKTKVTVTVLENDPGLCYSTQATFPQRLHIAGDGSLVCPYVSYFKDENNELPEVQWYKNCKPLLLDNVSFFGVKDKLLVRNVAEEHRGDYICRMSYTFRGKQYPVTRVIQFITIDENKRDRPVILSPRNETIEADPGSMIQLICNVTGQFSDLVYWKWNGSEIEWNDPFLAEDYQFVEHPSTKRKYTLITTLNISEVKSQFYRYPFICVVKNT... | 3.2.2.6 | null | cytokine-mediated signaling pathway [GO:0019221]; heat acclimation [GO:0010286]; inflammatory response [GO:0006954]; interleukin-1-mediated signaling pathway [GO:0070498]; positive regulation of interleukin-1-mediated signaling pathway [GO:2000661]; positive regulation of neuron migration [GO:2001224]; positive regulat... | axon [GO:0030424]; cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; protein-containing complex [GO:0032991] | interleukin-1 binding [GO:0019966]; interleukin-1 receptor activity [GO:0004908]; interleukin-1, type I, activating receptor activity [GO:0004909]; ionotropic glutamate receptor binding [GO:0035255]; NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; platelet-derived ... | PF07679;PF13895;PF01582; | 2.60.40.10;3.40.50.10140; | Interleukin-1 receptor family | PTM: A soluble form (sIL1R1) is probably produced by proteolytic cleavage at the cell surface (shedding). {ECO:0000250}.; PTM: Rapidly phosphorylated on Tyr-499 in response to IL-1, which creates a SH2 binding site for the PI 3-kinase regulatory subunit PIK3R1. {ECO:0000250}. | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Cell membrane {ECO:0000305}. Secreted {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU00204}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Ev... | null | null | null | null | FUNCTION: Receptor for IL1A, IL1B and IL1RN. After binding to interleukin-1 associates with the coreceptor IL1RAP to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B, MAPK and other pathways. Signaling involves the recruitment of adapter molecules suc... | Mus musculus (Mouse) |
P13507 | AMT4_STUST | MSHILRAAVLAAMLLPLPSMADQAGKSPNAVRYHGGDEIILQGFHWNVVREAPNDWYNILRQQAATIAADGFSAIWMPVPWRDFSSWSDGSKSGGGEGYFWHDFNKNGRYGSDAQLRQAASALGGAGVKVLYDVVPNHMNRGYPDKEINLPAGQGFWRNDCADPGNYPNDCDDGDRFIGGDADLNTGHPQVYGMFRDEFTNLRSQYGAGGFRFDFVRGYAPERVNSWMTDSADNSFCVGELWKGPSEYPNWDWRNTASWQQIIKDWSDRAKCPVFDFALKERMQNGSIADWKHGLNGNPDPRWREVAVTFVDNHDTGYSP... | 3.2.1.60 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:9126844, ECO:0000269|PubMed:9281429}; Note=Binds 2 calcium ions per subunit. {ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:9126844, ECO:0000269|PubMed:9281429}; | starch catabolic process [GO:0005983] | extracellular space [GO:0005615] | alpha-amylase activity [GO:0004556]; glucan 1,4-alpha-maltotetraohydrolase activity [GO:0033910]; metal ion binding [GO:0046872]; starch binding [GO:2001070] | PF00128;PF09081;PF00686; | 3.20.20.80;2.60.40.1180;2.60.40.10; | Glycosyl hydrolase 13 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:2646279}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends.; EC=3.2.1.60; Evidence={ECO:0000269|PubMed:10556241, ECO:0000269|PubMed:2646279, ECO:0000269|PubMed:9281429}; | null | PATHWAY: Glycan degradation; starch degradation. {ECO:0000305|PubMed:10556241, ECO:0000305|PubMed:9281429}. | null | null | null | Stutzerimonas stutzeri (Pseudomonas stutzeri) |
P13508 | GLP1_CAEEL | MRVLLILLAFFAPIASQLMGGECGREGACSVNGKCYNGKLIETYWCRCKKGFGGAFCERECDLDCKRGEKCIYDVYGENPTCICQDCEDETPPTERTQKGCEEGYGGPDCKTPLFSGVNPCDSDPCNNGLCYPFYGGFQCICNNGYGGSYCEEGIDHCAQNECAEGSTCVNSVYNYYCDCPIGKSGRYCERTECALMGNICNHGRCIPNRDEDKNFRCVCDSGYEGEFCNKDKNECLIEETCVNNSTCFNLHGDFTCTCKPGYAGKYCEEAIDMCKDYVCQNDGYCAHDSNQMPICYCEQGFTGQRCEIECPSGFGGIHC... | null | null | cell fate specification [GO:0001708]; cellularization [GO:0007349]; chordate pharyngeal muscle development [GO:0043282]; cytoplasmic streaming [GO:0099636]; embryonic pattern specification [GO:0009880]; establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; heterophilic cell-cell adhesion v... | axon [GO:0030424]; cytoplasm [GO:0005737]; endomembrane system [GO:0012505]; lateral plasma membrane [GO:0016328]; plasma membrane [GO:0005886]; RNA polymerase II transcription regulator complex [GO:0090575] | calcium ion binding [GO:0005509]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription coactivator activity [GO:0003713]; transmembrane signaling receptor activity [GO:0004888] | PF00023;PF12796;PF00008;PF06816;PF07684;PF00066; | 3.30.300.320;3.30.70.3310;1.25.40.20;2.10.25.10; | null | PTM: Upon binding its ligands, it is cleaved (S2 cleavage) in its extracellular domain, close to the transmembrane domain (By similarity). S2 cleavage is probably mediated by the metalloproteases adm-4 and sup-17 (PubMed:16197940). It is then cleaved (S3 cleavage) downstream of its transmembrane domain, releasing it fr... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7607081}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000269|PubMed:18599512}. Note=Localized to axons during dauer larval stage. {ECO:0000269|PubMed:18599512}.; SUBCELLULAR LOCATION: [glp-1/Notch intracellular domain]: Nucleus {... | null | null | null | null | null | FUNCTION: Essential signaling protein which has a major role in germline and embryonic development; involved in cell fate decisions that require cell-cell interactions (PubMed:16319922, PubMed:19379690, PubMed:8156602). Probable membrane-bound receptor for putative ligands lag-2 and apx-1 (PubMed:7607081, PubMed:815660... | Caenorhabditis elegans |
P13512 | CZCD_CUPMC | MGAGHSHDHPGGNERSLKIALALTGTFLIAEVVGGVMTKSLALISDAAHMLTDTVALAIALAAIAIAKRPADKKRTFGYYRFEILAAAFNALLLFGVAIYILYEAYLRLKSPPQIESTGMFVVAVLGLIINLISMRMLSSGQSSSLNVKGAYLEVWSDLLGSVGVIAGAIIIRFTGWAWVDSAIAVLIGLWVLPRTWILLKSSLNVLLEGVPDDVDLAEVEKQILATPGVKSFHDLHIWALTSGKASLTVHVVNDTAVNPEMEVLPELKQMLADKFDITHVTIQFELAPCEQADAAQHFNASPALVGSKSLAAGGN | null | null | detoxification of zinc ion [GO:0010312]; response to cadmium ion [GO:0046686] | plasma membrane [GO:0005886]; vacuole [GO:0005773] | zinc ion transmembrane transporter activity [GO:0005385] | PF01545; | 1.20.1510.10; | Cation diffusion facilitator (CDF) transporter (TC 2.A.4) family, SLC30A subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:10559151}; Multi-pass membrane protein {ECO:0000269|PubMed:10559151}. | null | null | null | null | null | FUNCTION: Mediates a low-level metal ion resistance, probably by efflux of cations from the cytoplasm into the periplasm. Also mediates resistance to cobalt, cadmium and zinc via regulation of the Czc system. May repress expression of the Czc system by an export of the inducing cations. Binds and transports zinc. Can a... | Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans) |
P13513 | TRI5_FUSSP | MENFPTEYFLNTTVRLLEYIRYRDSNYTREERIENLHYAYNKAAHHFAQPRQQQLLKVDPKRLQASLQTIVGMVVYSWAKVSKECMADLSIHYTYTLVLDDSKDDPYPTMVNYFDDLQAGREQAHPWWALVNEHFPNVLRHFGPFCSLNLIRSTLDFFEGCWIEQYNFGGFPGSHDYPQFLRRMNGLGHCVGASLWPKEQFNERSLFLEITSAIAQMENWMVWVNDLMSFYKEFDDERDQISLVKNYVVSDEISLHEALEKLTQDTLHSSKQMVAVFSDKDPQVMDTIECFMHGYVTWHLCDRRYRLSEIYEKVKEEKTE... | 4.2.3.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15835903, ECO:0000269|PubMed:16171386, ECO:0000269|PubMed:17678871, ECO:0000269|PubMed:17996718, ECO:0000269|PubMed:3800398, ECO:0000269|PubMed:8823172}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:8823172}; Note=Some of t... | sesquiterpenoid biosynthetic process [GO:0016106] | null | metal ion binding [GO:0046872]; trichodiene synthase activity [GO:0045482] | PF06330; | 1.10.600.10; | Trichodiene synthase family | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + trichodiene; Xref=Rhea:RHEA:12052, ChEBI:CHEBI:15861, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.6; Evidence={ECO:0000269|PubMed:16171386, ECO:0000269|PubMed:17678871, ECO:0000269|PubMed:3800398, ECO:0000269|PubMed:7873527, ECO:0000269|PubMe... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=62 nM for farnesyl pyrophosphate {ECO:0000269|PubMed:3800398, ECO:0000269|PubMed:7873527}; KM=78 nM for Mg(2+) {ECO:0000269|PubMed:8823172}; KM=84.8 nM for Mn(2+) {ECO:0000269|PubMed:8823172}; | PATHWAY: Sesquiterpene biosynthesis; trichothecene biosynthesis. {ECO:0000269|PubMed:3800398}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.75-7.75. {ECO:0000269|PubMed:3800398}; | null | FUNCTION: Trichodiene synthase; part of the core gene cluster that mediates the biosynthesis of trichothecenes, a very large family of chemically related bicyclic sesquiterpene compounds acting as mycotoxins, including T2-toxin (PubMed:11352533, PubMed:2817906). The biosynthesis of trichothecenes begins with the cycliz... | Fusarium sporotrichioides |
P13516 | ACOD1_MOUSE | MPAHMLQEISSSYTTTTTITAPPSGNEREKVKTVPLHLEEDIRPEMKEDIHDPTYQDEEGPPPKLEYVWRNIILMVLLHLGGLYGIILVPSCKLYTCLFGIFYYMTSALGITAGAHRLWSHRTYKARLPLRIFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRGFFFSHVGWLLVRKHPAVKEKGGKLDMSDLKAEKLVMFQRRYYKPGLLLMCFILPTLVPWYCWGETFVNSLFVSTFLRYTLVLNATWLVNSAAHLYGYRPYDKNIQSRENILVSLGAVGEGFHNYHHTFPFDYSASEYRWHINFTTFFI... | 1.14.19.1 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000305|PubMed:26098370}; Note=Expected to bind 2 Fe(2+) ions per subunit, instead of the Zn(2+) ions seen in the 3D-structure. {ECO:0000305|PubMed:26098370}; | brown fat cell differentiation [GO:0050873]; cholesterol homeostasis [GO:0042632]; defense response to Gram-positive bacterium [GO:0050830]; fatty acid biosynthetic process [GO:0006633]; lipid biosynthetic process [GO:0008610]; lipid homeostasis [GO:0055088]; monounsaturated fatty acid biosynthetic process [GO:1903966]... | endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020] | iron ion binding [GO:0005506]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; palmitoyl-CoA 9-desaturase activity [GO:0032896]; stearoyl-CoA 9-desaturase activity [GO:0004768] | PF00487; | null | Fatty acid desaturase type 1 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16275639, ECO:0000305|PubMed:16443825}; Multi-pass membrane protein {ECO:0000269|PubMed:16275639}. Microsome membrane {ECO:0000269|PubMed:10899171, ECO:0000269|PubMed:11500518, ECO:0000269|PubMed:11533264, ECO:0000269|PubMed:16443825}. | CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA = (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:19721, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI... | null | null | null | null | FUNCTION: Stearoyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates. Catalyzes the insertion of a cis double bond at the Delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (PubMed:... | Mus musculus (Mouse) |
P13517 | CAPZB_YEAST | MSDAQFDAALDLLRRLNPTTLQENLNNLIELQPNLAQDLLSSVDVPLSTQKDSADSNREYLCCDYNRDIDSFRSPWSNTYYPELSPKDLQDSPFPSAPLRKLEILANDSFDVYRDLYYEGGISSVYLWDLNEEDFNGHDFAGVVLFKKNQSDHSNWDSIHVFEVTTSPSSPDSFNYRVTTTIILHLDKTKTDQNSHMMLSGNLTRQTEKDIAIDMSRPLDVIFTSHVANLGSLIEDIESQMRNLLETVYFEKTRDIFHQTKNAAIASSAEEANKDAQAEVIRGLQSL | null | null | actin cytoskeleton organization [GO:0030036]; barbed-end actin filament capping [GO:0051016]; cell morphogenesis [GO:0000902]; filamentous growth [GO:0030447]; negative regulation of filopodium assembly [GO:0051490]; regulation of lamellipodium assembly [GO:0010591] | actin cortical patch [GO:0030479]; actin cytoskeleton [GO:0015629]; cellular bud tip [GO:0005934]; F-actin capping protein complex [GO:0008290]; incipient cellular bud site [GO:0000131]; mating projection tip [GO:0043332]; plasma membrane [GO:0005886] | actin filament binding [GO:0051015] | PF01115; | 1.20.58.570;3.90.1150.210; | F-actin-capping protein beta subunit family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch {ECO:0000269|PubMed:1315784}. Bud {ECO:0000269|PubMed:1315784}. Bud tip {ECO:0000269|PubMed:1315784}. Note=Found at cortical actin spots at the site of bud emergence and at the tips of growing buds and shmoos. | null | null | null | null | null | FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. {ECO:0000269|PubMed:1315784}... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P13518 | CSRD_ECOLI | MRLTTKFSAFVTLLTGLTIFVTLLGCSLSFYNAIQYKFSHRVQAVATAIDTHLVSNDFSVLRPQITELMMSADIVRVDLLHGDKQVYTLARNGSYRPVGSSDLFRELSVPLIKHPGMSLRLVYQDPMGNYFHSLMTTAPLTGAIGFIIVMLFLAVRWLQRQLAGQELLETRATRILNGERGSNVLGTIYEWPPRTSSALDTLLREIQNAREQHSRLDTLIRSYAAQDVKTGLNNRLFFDNQLATLLEDQEKVGTHGIVMMIRLPDFNMLSDTWGHSQVEEQFFTLTNLLSTFMMRYPGALLARYHRSDFAALLPHRTLKE... | null | null | ncRNA catabolic process [GO:0034661]; regulation of RNA metabolic process [GO:0051252] | plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | identical protein binding [GO:0042802] | PF00563;PF17157;PF00990; | 3.30.70.270;3.20.20.450; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Serves as a specificity factor required for RNase E-mediated decay of the small global regulatory RNAs CsrB and CsrC, it is probably not a nuclease. Nor does its activity involve c-di-GMP, despite its domain composition. Positively modulates motility gene expression, is also required for curli expression. {EC... | Escherichia coli (strain K12) |
P13520 | VOLD_BPP2 | MTVRLASVSISNFRSCKSTSAILRPFTALVGYNNAGKSNIILAIKWLLDGSLISESDVYDPTHPVSVEGVIQGITDDTLSLLTEENQQKIAPFIIDGTLTFARRQEFNKETGKAKKSLDVYDGTTWKKNPGGIDGAISNIFPEPIHIPAMSDAVEDSTKCKNTTTIGKILSAIVSEIKQEHEEKFSKNISEIGKYLSHNGENRLESLNKIDSGVNKKVNQFFPDVSVKLHFPTPTLDEIFKSGTLKVFESREDEPVMRDISRFGHGTQRSIQMALIQYLAEIKKENSESKKSNTLIFIDEPELYLHPSAINSVRESLVTL... | 3.1.11.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:7836278}; Note=Mg(2+) gave the most activity in a maltose-binding protein fusion. {ECO:0000269|PubMed:7836278}; | null | null | ATP binding [GO:0005524]; exonuclease activity [GO:0004527]; metal ion binding [GO:0046872] | PF13175;PF20469; | 3.40.50.300; | Class 1 OLD nuclease family | null | null | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.3; Evidence={ECO:0000269|PubMed:7836278}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2-8.8. {ECO:0000269|PubMed:7836278}; | null | FUNCTION: An exonuclease that acts preferentially on linear dsDNA, processively degrading it from 5'-3', releasing 5'-phosphomononucleotides. Initiates on 5'-phosphate and 5'-hydroxyl ends. Also acts on linear ssDNA, nicked DNA and RNA. ATP enhances but is not necessary for exonuclease activity; has ATPase activity tha... | Escherichia phage P2 (Bacteriophage P2) |
P13521 | SCG2_HUMAN | MAEAKTHWLGAALSLIPLIFLISGAEAASFQRNQLLQKEPDLRLENVQKFPSPEMIRALEYIENLRQQAHKEESSPDYNPYQGVSVPLQQKENGDESHLPERDSLSEEDWMRIILEALRQAENEPQSAPKENKPYALNSEKNFPMDMSDDYETQQWPERKLKHMQFPPMYEENSRDNPFKRTNEIVEEQYTPQSLATLESVFQELGKLTGPNNQKRERMDEEQKLYTDDEDDIYKANNIAYEDVVGGEDWNPVEEKIESQTQEEVRDSKENIEKNEQINDEMKRSGQLGIQEEDLRKESKDQLSDDVSKVIAYLKRLVNA... | null | null | angiogenesis [GO:0001525]; endothelial cell migration [GO:0043542]; eosinophil chemotaxis [GO:0048245]; induction of positive chemotaxis [GO:0050930]; inflammatory response [GO:0006954]; intracellular signal transduction [GO:0035556]; MAPK cascade [GO:0000165]; negative regulation of endothelial cell apoptotic process ... | endoplasmic reticulum lumen [GO:0005788]; extracellular space [GO:0005615]; neuronal dense core vesicle [GO:0098992]; secretory granule [GO:0030141] | chemoattractant activity [GO:0042056]; cytokine activity [GO:0005125] | PF01271; | null | Chromogranin/secretogranin protein family | PTM: O-glycosylated. {ECO:0000269|PubMed:23234360}. | SUBCELLULAR LOCATION: Secreted. Note=Neuroendocrine and endocrine secretory granules. | null | null | null | null | null | FUNCTION: Neuroendocrine protein of the granin family that regulates the biogenesis of secretory granules. {ECO:0000269|PubMed:19357184}. | Homo sapiens (Human) |
P13528 | UNC86_CAEEL | MQNTAPVPTTTTASKMQPFNNSLFGSFDDPILNARAAQVALADIDVKNVPQLTNPLMRPHDMFSYSNYFSGIHDTSAATNIYQGLPSSSEPFDASVVVPTSSDDQMTPLQQVMAMQQSYGAPPPFQYNMTHPFSTTSIASSNNLARYPIAPPTSDMDTDPRQLETFAEHFKQRRIKLGVTQADVGKALAHLKMPGVGSLSQSTICRFESLTLSHNNMVALKPILHSWLEKAEEAMKQKDTIGDINGILPNTDKKRKRTSIAAPEKRELEQFFKQQPRPSGERIASIADRLDLKKNVVRVWFCNQRQKQKRDFRSQFRARS... | null | null | mechanosensory behavior [GO:0007638]; neuron development [GO:0048666]; neuron fate specification [GO:0048665]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; response to mechanical stimulus [GO:0009612]; sensory perception of smell ... | nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | 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 transcription regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II-specific DNA-binding transcription facto... | PF00046;PF00157; | 1.10.10.60;1.10.260.40; | POU transcription factor family, Class-4 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00530, ECO:0000269|PubMed:2257628}. | null | null | null | null | null | FUNCTION: Transcription factor required for correct cell fate determination and differentiation in diverse neuronal cell lineages where it plays a role in specifying the fate of daughter cells during cell divisions (PubMed:10899123, PubMed:2257628, PubMed:26096732, PubMed:7237544). Involved in sensory neuron production... | Caenorhabditis elegans |
P13529 | POLG_PPVD | MSTIVFGSFTCHLDAAIHQDNADRLAKAWTRPENRQVSNVHLLCRRAAKSLINTYESATASAWKGLEEKLQPMFAKREFSKTVTKRKGLRCFKESSEKFIEKKLRKQYQEERERFQFVNGPDAIVNQISVDKCEASVWVPFPHIIEKPSFATPSMKKKVVFTKVRMSEASLQLFMRRVAANAKANGQKVEIIGRKRVVGNYTTKSRLTYFRTHVRHLDGSKPRYDLVLDEATKKILQLFANTSRFHHVHKKGEVTPGMSGFVVNPINLSDPMQVYDTDLFIVRGKHNSILVDSRCKVSKKQSNEIIHYSDPGKQFSDGFT... | 2.7.7.48; 3.4.-.-; 3.4.22.44; 3.4.22.45; 3.6.4.- | null | DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; viral RNA genome replication [GO:0039694]; virus-mediated perturbation of host defense response [GO:0019049] | helical viral capsid [GO:0019029]; host cell cytoplasmic vesicle [GO:0044161]; host cell nucleus [GO:0042025] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; helicase activity [GO:0004386]; hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides [GO:0016818]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type peptidase activity [GO:0... | PF00270;PF00271;PF00863;PF00851;PF01577;PF00767;PF08440;PF13608;PF00680; | 3.30.70.270;3.90.70.150;3.40.50.300;2.40.10.10; | Potyviridae genome polyprotein family | PTM: [Viral genome-linked protein]: VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity). {ECO:0000250|UniProtKB:P09814}.; PTM: [Genome polyprotein]: Potyviral RNA is expressed as ... | SUBCELLULAR LOCATION: [6 kDa protein 1]: Host cytoplasmic vesicle. Note=Probably colocalizes with 6K2-induced vesicles associated with host chloroplasts. {ECO:0000269|PubMed:26962227}.; SUBCELLULAR LOCATION: [6 kDa protein 2]: Host cytoplasmic vesicle {ECO:0000250|UniProtKB:P09814}. Note=6K-induced vesicles associate w... | CATALYTIC ACTIVITY: Reaction=Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but oth... | null | null | null | null | FUNCTION: [Helper component proteinase]: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a m... | Plum pox potyvirus (strain D) (PPV) |
P13533 | MYH6_HUMAN | MTDAQMADFGAAAQYLRKSEKERLEAQTRPFDIRTECFVPDDKEEFVKAKILSREGGKVIAETENGKTVTVKEDQVLQQNPPKFDKIEDMAMLTFLHEPAVLFNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFASIAAIGDRGKKDNANANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVS... | null | null | adult heart development [GO:0007512]; ATP metabolic process [GO:0046034]; atrial cardiac muscle tissue morphogenesis [GO:0055009]; cardiac muscle cell development [GO:0055013]; cardiac muscle contraction [GO:0060048]; cardiac muscle hypertrophy in response to stress [GO:0014898]; in utero embryonic development [GO:0001... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; muscle myosin complex [GO:0005859]; myofibril [GO:0030016]; myosin complex [GO:0016459]; myosin filament [GO:0032982]; myosin II complex [GO:0016460]; sarcomere [GO:0030017]; stress fiber [GO:0001725]; Z disc [GO:0030018] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]; myosin phosphatase activity [GO:0017018]; protein kinase binding [GO:0019901] | PF00063;PF02736;PF01576; | 1.10.10.820;1.20.5.340;1.20.5.370;1.20.5.4820;1.20.58.530;6.10.250.2420;3.40.850.10;2.30.30.360;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils. | null | null | null | null | null | FUNCTION: Muscle contraction. | Homo sapiens (Human) |
P13535 | MYH8_HUMAN | MSASSDAEMAVFGEAAPYLRKSEKERIEAQNKPFDAKTSVFVAEPKESYVKSTIQSKEGGKVTVKTEGGATLTVREDQVFPMNPPKYDKIEDMAMMTHLHEPGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYKPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKDESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGE... | null | null | ATP metabolic process [GO:0046034]; muscle contraction [GO:0006936]; muscle filament sliding [GO:0030049]; skeletal muscle contraction [GO:0003009] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; muscle myosin complex [GO:0005859]; myosin filament [GO:0032982]; myosin II complex [GO:0016460]; sarcomere [GO:0030017] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]; myosin light chain binding [GO:0032027]; myosin phosphatase activity [GO:0017018]; structural constituent of muscle [GO:0008307] | PF00063;PF02736;PF01576; | 1.10.10.820;1.20.5.340;1.20.5.370;1.20.5.4820;1.20.58.530;6.10.250.2420;3.40.850.10;2.30.30.360;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils. | null | null | null | null | null | FUNCTION: Muscle contraction. | Homo sapiens (Human) |
P13536 | ACHG_BOVIN | MCGGQRPLFLLPLLAVCLGAKGRNQEERLLGDLMQGYNPHLRPAEHDSDVVNVSLKLTLTNLISLNEREEALTTNVWIEMQWCDYRLRWDPRDYGGLWVLRVPSTMVWRPDIVLENNVDGVFEVALYCNVLVSPDGCVYWLPPAIFRSSCPVSVTFFPFDWQNCSLIFQSQTYSTNEINLQLSQEDGQTIEWIFIDPEAFTENGEWAIRHRPAKMLLDEAAPAEEAGHQKVVFYLLIQRKPLFYVINIIAPCVLISSVAILIYFLPAKAGGQKCTVAINVLLAQTVFLFLVAKKVPETSQAVPLISKYLTFLLVVTILIV... | null | null | acetylcholine receptor signaling pathway [GO:0095500]; membrane depolarization [GO:0051899] | acetylcholine-gated channel complex [GO:0005892]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202] | acetylcholine receptor activity [GO:0015464]; acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315] | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Gamma/CHRNG sub-subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:2423878}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:2423878}; | null | null | null | null | FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. {ECO:0000269|PubMed:2423878}. | Bos taurus (Bovine) |
P13538 | MYSS_CHICK | MASPDAEMAAFGEAAPYLRKSEKERIEAQNKPFDAKSSVFVVHPKESFVKGTIQSKEGGKVTVKTEGGETLTVKEDQVFSMNPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVLAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAASGEKKKEEQSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLPAERSYHIFYQIMSNKKPELIDMLLITTNPYDYHYVSQGE... | null | null | muscle contraction [GO:0006936] | cytoplasm [GO:0005737]; myofibril [GO:0030016]; myosin filament [GO:0032982]; myosin II complex [GO:0016460] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146] | PF00063;PF02736;PF01576; | 1.10.10.820;1.20.5.340;1.20.5.370;1.20.5.4820;1.20.58.530;6.10.250.2420;3.40.850.10;2.30.30.360;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils. | null | null | null | null | null | FUNCTION: Muscle contraction. Myosin is a protein that binds to F-actin and has ATPase activity that is activated by F-actin. | Gallus gallus (Chicken) |
P13540 | MYH7_MESAU | MADREMAAFGAAAFLRKSEKERLEAQTRPFDLKKDVFVPDDKEEFVKAKIVSREGGKVTAETENGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKDGYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPAHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFIPQGETTVA... | null | null | adult heart development [GO:0007512]; cardiac muscle contraction [GO:0060048]; muscle filament sliding [GO:0030049]; sarcomere organization [GO:0045214] | myofibril [GO:0030016]; myosin filament [GO:0032982]; myosin II complex [GO:0016460]; sarcomere [GO:0030017] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146] | PF00063;PF02736;PF01576; | 1.10.10.820;1.20.5.340;1.20.5.370;1.20.5.4820;1.20.58.530;6.10.250.2420;3.40.850.10;2.30.30.360;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril {ECO:0000250|UniProtKB:P02564}. Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:P02564}. Note=Thick filaments of the myofibrils. {ECO:0000250|UniProtKB:P02564}. | null | null | null | null | null | FUNCTION: Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction. Forms regular bipolar thick filaments that, together with actin thin filaments, constitute the fundamental contractile unit of skeletal and cardiac muscle. {ECO:0000250|UniProtKB:P12883}. | Mesocricetus auratus (Golden hamster) |
P13541 | MYH3_MOUSE | MSSDTEMEVFGIAAPFLRKSEKERIEAQNQPFDAKTYCFVVDSKEEYVKGKIKSSQDGKVTVETEDSRTLVVKPEDVYAMNPPKFDKIEDMAMLTHLNEPAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEIL... | null | null | ATP metabolic process [GO:0046034]; muscle contraction [GO:0006936]; skeletal muscle contraction [GO:0003009] | contractile fiber [GO:0043292]; cytoplasm [GO:0005737]; myofibril [GO:0030016]; myosin complex [GO:0016459]; myosin filament [GO:0032982]; myosin II complex [GO:0016460] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146] | PF00063;PF02736;PF01576; | 1.10.10.820;1.20.5.340;1.20.5.370;1.20.5.4820;1.20.58.530;6.10.250.2420;3.40.850.10;2.30.30.360;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils. | null | null | null | null | null | FUNCTION: Muscle contraction. | Mus musculus (Mouse) |
P13542 | MYH8_MOUSE | MSAGSDAEMAIFGEAAPYLRKSEKERIEAQNKPFDAKTSVFVAEPKESYVKSVIQSKDGGKVTVKTESGATLTVKEDQVFPMNPPKYDKIEDMAMMTHLHEPGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGDKKKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYAFVSQGE... | null | null | ATP metabolic process [GO:0046034]; muscle contraction [GO:0006936]; muscle filament sliding [GO:0030049]; skeletal muscle contraction [GO:0003009] | cytoplasm [GO:0005737]; myofibril [GO:0030016]; myosin complex [GO:0016459]; myosin filament [GO:0032982]; myosin II complex [GO:0016460] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microfilament motor activity [GO:0000146] | PF00063;PF02736;PF01576; | 1.10.10.820;1.20.5.340;1.20.5.370;1.20.5.4820;1.20.58.530;6.10.250.2420;3.40.850.10;2.30.30.360;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils. | null | null | null | null | null | FUNCTION: Muscle contraction. | Mus musculus (Mouse) |
P13562 | GON1_MOUSE | MILKLMAGILLLTVCLEGCSSQHWSYGLRPGGKRNTEHLVESFQEMGKEVDQMAEPQHFECTVHWPRSPLRDLRGALESLIEEEARQKKM | null | null | male sex determination [GO:0030238]; negative regulation of apoptotic process [GO:0043066]; negative regulation of immature T cell proliferation [GO:0033087]; negative regulation of neuron migration [GO:2001223]; regulation of gene expression [GO:0010468]; regulation of ovarian follicle development [GO:2000354]; reprod... | axon terminus [GO:0043679]; cytoplasmic side of rough endoplasmic reticulum membrane [GO:0098556]; dendrite [GO:0030425]; extracellular space [GO:0005615]; Golgi-associated vesicle [GO:0005798]; neurosecretory vesicle [GO:1990008]; perikaryon [GO:0043204] | gonadotropin hormone-releasing hormone activity [GO:0005183]; gonadotropin-releasing hormone receptor binding [GO:0031530] | PF00446; | null | GnRH family | PTM: [Gonadoliberin-1]: The precursor is cleaved by ACE, which removes the Gly-Lys-Arg peptide at the C-terminus, leading to mature hormone. The mature form of Gonadoliberin-1 is also cleaved and degraded by ACE. {ECO:0000250|UniProtKB:P01148}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:37189369}. | null | null | null | null | null | FUNCTION: Stimulates the secretion of gonadotropins; it stimulates the secretion of both luteinizing and follicle-stimulating hormones. | Mus musculus (Mouse) |
P13569 | CFTR_HUMAN | MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELASKKNPKLINALRRCFFWRFMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGLGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFL... | 5.6.1.6 | null | amelogenesis [GO:0097186]; bicarbonate transport [GO:0015701]; cellular response to cAMP [GO:0071320]; cellular response to forskolin [GO:1904322]; chloride transmembrane transport [GO:1902476]; cholesterol biosynthetic process [GO:0006695]; cholesterol transport [GO:0030301]; establishment of localization in cell [GO:... | apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; chloride channel complex [GO:0034707]; clathrin-coated endocytic vesicle membrane [GO:0030669]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endoplasmic reticulum membrane [GO:0005789]; en... | ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled inorganic anion transmembrane transporter activity [GO:0043225]; ATPase-coupled transmembrane transporter activity [GO:0042626]; bicarbonate transmembrane transporter activity [GO:0015106]; chlorid... | PF00664;PF00005;PF14396; | 1.20.1560.10;3.40.50.300; | ABC transporter superfamily, ABCC family, CFTR transporter (TC 3.A.1.202) subfamily | PTM: N-glycosylated. {ECO:0000269|PubMed:12529365, ECO:0000269|PubMed:1699669, ECO:0000269|PubMed:20008117, ECO:0000269|PubMed:21884936, ECO:0000269|PubMed:28067262}.; PTM: Phosphorylated; cAMP treatment promotes phosphorylation and activates the channel (PubMed:12588899, PubMed:17036051, PubMed:8910473). Dephosphoryla... | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:12519745, ECO:0000269|PubMed:12529365, ECO:0000269|PubMed:1284548, ECO:0000269|PubMed:15247260, ECO:0000269|PubMed:15716351, ECO:0000269|PubMed:17462998, ECO:0000269|PubMed:19398555, ECO:0000269|PubMed:19621064, ECO:0000269|PubMed:20008117, ECO:0000269|PubM... | CATALYTIC ACTIVITY: Reaction=ATP + H2O + closed Cl(-) channel = ADP + phosphate + open Cl(-) channel.; EC=5.6.1.6; Evidence={ECO:0000269|PubMed:11524016, ECO:0000269|PubMed:15284228, ECO:0000269|PubMed:26627831, ECO:0000269|PubMed:8910473}; CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.47 mM for glutathione (in the presence of MgAMP-PNP) {ECO:0000269|PubMed:12727866}; Vmax=612 pmol/h/ug enzyme (in the presence of MgAMP-PNP) {ECO:0000269|PubMed:12727866}; | null | null | null | FUNCTION: Epithelial ion channel that plays an important role in the regulation of epithelial ion and water transport and fluid homeostasis (PubMed:26823428). Mediates the transport of chloride ions across the cell membrane (PubMed:10792060, PubMed:11524016, PubMed:11707463, PubMed:12519745, PubMed:12529365, PubMed:125... | Homo sapiens (Human) |
P13574 | STE12_YEAST | MKVQITNSRTEEILKVQANNENDEVSKATPGEVEESLRLIGDLKFFLATAPVNWQENQIIRRYYLNSGQGFVSCVFWNNLYYITGTDIVKCCLYRMQKFGREVVQKKKFEEGIFSDLRNLKCGIDATLEQPKSEFLSFLFRNMCLKTQKKQKVFFWFSVAHDKLFADALERDLKRESLNQPSTTKPVNEPALSFSYDSSSDKPLYDQLLQHLDSRRPSSTTKSDNSPPKLESENFKDNELVTVTNQPLLGVGLMDDDAPESPSQINDFIPQKLIIEPNTLELNGLTEETPHDLPKNTAKGRDEEDFPLDYFPVSVEYPTE... | null | null | conjugation with cellular fusion [GO:0000747]; invasive growth in response to glucose limitation [GO:0001403]; negative regulation of mating-type specific transcription, DNA-templated [GO:0045894]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polyme... | nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Ste12p-Dig1p-Dig2p complex [GO:1990526]; Tec1p-Ste12p-Dig1p complex [GO:1990527] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700] | PF02200; | null | STE12 transcription factor family | PTM: Phosphorylated by the STE7, STE11 and STE20 kinases. | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Binds to the DNA sequence mediating pheromone induction (called the pheromone response element = PRE) which is found in the upstream control region of several a-, alpha- and haploid-specific genes. Involved in mating of haploids and in pseudohyphae formation in diploids. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P13582 | EAST_DROME | MLKPSIICLFLGILAKSSAGQFYFPNEAAQVPNYGRCITPNRERALCIHLEDCKYLYGLLTTTPLRDTDRLYLSRSQCGYTNGKVLICCPDRYRESSSETTPPPKPNVTSNSLLPLPGQCGNILSNRIYGGMKTKIDEFPWMALIEYTKSQGKKGHHCGGSLISTRYVITASHCVNGKALPTDWRLSGVRLGEWDTNTNPDCEVDVRGMKDCAPPHLDVPVERTIPHPDYIPASKNQVNDIALLRLAQQVEYTDFVRPICLPLDVNLRSATFDGITMDVAGWGKTEQLSASNLKLKAAVEGSRMDECQNVYSSQDILLED... | 3.4.21.- | null | dorsal/ventral axis specification [GO:0009950]; dorsal/ventral pattern formation [GO:0009953]; maternal specification of dorsal/ventral axis, oocyte, germ-line encoded [GO:0007311]; proteolysis [GO:0006508]; Toll receptor ligand protein activation cascade [GO:0160032]; ventral furrow formation [GO:0007370] | extracellular region [GO:0005576]; extracellular space [GO:0005615]; perivitelline space [GO:0098595] | metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252] | PF12032;PF00089; | 3.30.1640.30;2.40.10.10; | Peptidase S1 family, CLIP subfamily | PTM: Activation peptide and active catalytic domain are associated by a disulfide bond. Processed easter is present in extremely low amounts in the early embryo as it is rapidly converted into a high molecular mass complex, which may contain a protease inhibitor. Zymogen activation is also controlled by a negative feed... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9477324}. | null | null | null | null | null | FUNCTION: Component of the extracellular signaling pathway that establishes the dorsal-ventral pathway of the embryo (PubMed:12493753, PubMed:2107028, PubMed:9477324). Three proteases; ndl, gd and snk process easter to create active easter (PubMed:9477324). Active easter defines cell identities along the dorsal-ventral... | Drosophila melanogaster (Fruit fly) |
P13584 | CP4B1_HUMAN | MVPSFLSLSFSSLGLWASGLILVLGFLKLIHLLLRRQTLAKAMDKFPGPPTHWLFGHALEIQETGSLDKVVSWAHQFPYAHPLWFGQFIGFLNIYEPDYAKAVYSRGDPKAPDVYDFFLQWIGRGLLVLEGPKWLQHRKLLTPGFHYDVLKPYVAVFTESTRIMLDKWEEKAREGKSFDIFCDVGHMALNTLMKCTFGRGDTGLGHRDSSYYLAVSDLTLLMQQRLVSFQYHNDFIYWLTPHGRRFLRACQVAHDHTDQVIRERKAALQDEKVRKKIQNRRHLDFLDILLGARDEDDIKLSDADLRAEVDTFMFEGHDTT... | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P51869}; | biphenyl metabolic process [GO:0018879]; fatty acid metabolic process [GO:0006631] | endoplasmic reticulum membrane [GO:0005789] | aromatase activity [GO:0070330]; heme binding [GO:0020037]; heterocyclic compound binding [GO:1901363]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxygen binding [GO:0019825] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | null | null | null | FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. | Homo sapiens (Human) |
P13585 | AT2A1_CHICK | MENAHAKTAEECLAFFGVNESVGLSGEQVRRALEKYGHNELPAEEGKTIWELVVEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILIANAVVGVWQERNAENAIEALKEYEPEMGKVYRADRKAVQRIKARDLVPGDIAEVAVGDKVPADIRIISIKSTTLRVDQSILTGESVSVIKHTEPVPDPRAVNQDKKNMLFSGTNIGAGKAVGIVVATGVNTEIGKIRDEMAATEQDKTPLQQKLDEFGEQLSKVISLICVAVWLINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLA... | 7.2.2.10 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P04191}; | calcium ion import into sarcoplasmic reticulum [GO:1990036]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; intracellular calcium ion homeostasis [GO:0006874]; negative regulation of striated muscle contraction [GO:0045988]; positive regulation of fast-twitch skeletal muscle fiber... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; H zone [GO:0031673]; I band [GO:0031674]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum m... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calcium ion binding [GO:0005509]; P-type calcium transporter activity [GO:0005388] | PF13246;PF00689;PF00690;PF00122;PF00702; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIA subfamily | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P04191}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P04191}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:P04191}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P04191}. | CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; Evidence={ECO:0000250|UniProtKB:P04191}; PhysiologicalDirection=left-to-right;... | null | null | null | null | FUNCTION: Key regulator of striated muscle performance by acting as the major Ca(2+) ATPase responsible for the reuptake of cytosolic Ca(2+) into the sarcoplasmic reticulum. Catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to cal... | Gallus gallus (Chicken) |
P13586 | ATC1_YEAST | MSDNPFNASLLDEDSNREREILDATAEALSKPSPSLEYCTLSVDEALEKLDTDKNGGLRSSNEANNRRSLYGPNEITVEDDESLFKKFLSNFIEDRMILLLIGSAVVSLFMGNIDDAVSITLAIFIVVTVGFVQEYRSEKSLEALNKLVPAECHLMRCGQESHVLASTLVPGDLVHFRIGDRIPADIRIIEAIDLSIDESNLTGENEPVHKTSQTIEKSSFNDQPNSIVPISERSCIAYMGTLVKEGHGKGIVVGTGTNTSFGAVFEMMNNIEKPKTPLQLTMDKLGKDLSLVSFIVIGMICLVGIIQGRSWLEMFQISV... | 7.2.2.10 | null | calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; intracellular calcium ion homeostasis [GO:0006874]; intracellular manganese ion homeostasis [GO:0030026]; macroautophagy [GO:0016236]; manganese ion transport [GO:0006828] | endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calcium ion binding [GO:0005509]; P-type calcium transporter activity [GO:0005388]; P-type manganese transporter activity [GO:0140613] | PF13246;PF00689;PF00690;PF00122;PF00702; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; | null | null | null | null | FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Has a role in the secretory pathway. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P13587 | ATN1_YEAST | MGEGTTKENNNAEFNAYHTLTAEEAAEFIGTSLTEGLTQDEFVHRLKTVGENTLGDDTKIDYKAMVLHQVCNAMIMVLLISMIISFAMHDWITGGVISFVIAVNVLIGLVQEYKATKTMNSLKNLSSPNAHVIRNGKSETINSKDVVPGDICLVKVGDTIPADLRLIETKNFDTDESLLTGESLPVSKDANLVFGKEEETSVGDRLNLAFSSSAVVKGRAKGIVIKTALNSEIGKIAKSLQGDSGLISRDPSKSWLQNTWISTKKVTGAFLGTNVGTPLHRKLSKLAVLLFWIAVLFAIIVMASQKFDVDKRVAIYAICV... | 7.2.2.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P04191}; | cellular response to glucose starvation [GO:0042149]; hyperosmotic response [GO:0006972]; intracellular calcium ion homeostasis [GO:0006874]; monoatomic ion transmembrane transport [GO:0034220]; potassium ion transport [GO:0006813]; response to pH [GO:0009268]; response to salt stress [GO:0009651]; sodium ion transport... | cell periphery [GO:0071944]; fungal-type vacuole [GO:0000324]; plasma membrane [GO:0005886] | ABC-type sodium transporter activity [GO:0140679]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; P-type potassium transmembrane transporter activity [GO:0008556]; P-type sodium transporter activity [GO:0008554]; salt transmembrane transporter activity [GO:1901702] | PF13246;PF00689;PF00690;PF00122;PF00702; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IID subfamily | PTM: The active site is phosphorylated in presence of sodium or potassium and in conditions of higher pH (PubMed:9315618). Not phosphorylated in presence of calcium ions (PubMed:9315618). {ECO:0000269|PubMed:9315618}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:7664728, ECO:0000269|PubMed:9315618}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:7664728, ECO:0000269|PubMed:9315618}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + Na(+)(in) = ADP + H(+) + Na(+)(out) + phosphate; Xref=Rhea:RHEA:14633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.3; Evidence={ECO:0000305|PubMed:9315618}; PhysiologicalDirection=left-to-right; Xref... | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of ATP coupled with the export of sodium and potassium from the cell (PubMed:14617094, PubMed:22329368, PubMed:7664728, PubMed:9315618). May export potassium less efficiently (PubMed:14617094). May transport other cations such as lithium (PubMed:7664728, PubMed:9315618). Sodium/potass... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P13589 | PACA_RAT | MTMCSGARLALLVYGIIMHNSVSCSPAAGLSFPGIRPEEEAYDQDGNPLQDFYDWDPPGAGSPASALRDAYALYYPADRRDVAHEILNEAYRKVLDQLSARKYLQSMVARGMGENLAAAAVDDRAPLTKRHSDGIFTDSYSRYRKQMAVKKYLAAVLGKRYKQRVKNKGRRIAYL | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; behavioral fear response [GO:0001662]; cAMP-mediated signaling [GO:0019933]; cellular response to glucocorticoid stimulus [GO:0071385]; histamine secretion [GO:0001821]; insulin secretion [GO:0030073]; negative regulation of acute i... | cytosol [GO:0005829]; extracellular space [GO:0005615]; neuron projection [GO:0043005]; perikaryon [GO:0043204]; terminal bouton [GO:0043195] | neuropeptide hormone activity [GO:0005184]; peptide hormone receptor binding [GO:0051428]; pituitary adenylate cyclase activating polypeptide activity [GO:0016521]; pituitary adenylate cyclase-activating polypeptide receptor binding [GO:0031858]; signaling receptor binding [GO:0005102] | PF00123; | 6.10.250.590; | Glucagon family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Binding to its receptor activates G proteins and stimulates adenylate cyclase in pituitary cells (By similarity). Promotes neuron projection development through the RAPGEF2/Rap1/B-Raf/ERK pathway. In chromaffin cells, induces long-lasting increase of intracellular calcium concentrations and neuroendocrine sec... | Rattus norvegicus (Rat) |
P13590 | NCAM1_CHICK | MLPAAALPWTLFFLGAAASLQVDIVPSQGEISVGESKFFLCQVAGEAKYKDISWFSPNGEKLTPNQQRISVVRNDDFSSTLTIYNANIDDAGIYKCVVSSVEEGDSEATVNVKIFQKLMFKNAPTPQEFKEGDDAVIVCDVVSSLPPTIIWKHKGRDVMLKKDVRFIVLSNNYLQIRGIKKTDEGTYRCEGRILARGEINFKDIQVIVNVPPSVRARQSTMNATANLSQSVTLACDADGFPEPTMTWTKDGEPIEQEDNEEKYSFNYDGSELIIKKVDKSDEAEYICIAENKAGEQDATIHLKVFAKPKITYVENKTAME... | null | null | homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; synaptic membrane adhesion [GO:0099560] | axon [GO:0030424]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886] | axon guidance receptor activity [GO:0008046] | PF00041;PF07679;PF13927; | 2.60.40.10; | null | PTM: Polysialylated by ST8SIA2 and ST8SIA4. Polysialylation modulates cell interactions by confering both attractive and repulsive properties that are highly regulated by ST8SIA2 and ST8SIA4. Polysialylation is formed on a-2,3-linked sialic acid of core glycans. {ECO:0000250|UniProtKB:P13591}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc. | Gallus gallus (Chicken) |
P13591 | NCAM1_HUMAN | MLQTKDLIWTLFFLGTAVSLQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLTPNQQRISVVWNDDSSSTLTIYNANIDDAGIYKCVVTGEDGSESEATVNVKIFQKLMFKNAPTPQEFREGEDAVIVCDVVSSLPPTIIWKHKGRDVILKKDVRFIVLSNNYLQIRGIKKTDEGTYRCEGRILARGEINFKDIQVIVNVPPTIQARQNIVNATANLGQSVTLVCDAEGFPEPTMSWTKDGEQIEQEEDDEKYIFSDDSSQLTIKKVDKNDEAEYICIAENKAGEQDATIHLKVFAKPKITYVENQTAME... | null | null | cell adhesion [GO:0007155]; commissural neuron axon guidance [GO:0071679]; epithelial to mesenchymal transition [GO:0001837]; regulation of semaphorin-plexin signaling pathway [GO:2001260] | cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; plasma membrane [GO:0005886] | virus receptor activity [GO:0001618] | PF00041;PF07679;PF13927; | 2.60.40.10; | null | PTM: Polysialylated at Asn-459 and Asn-488 by ST8SIA2 and ST8SIA4 (PubMed:28810663). Polysialylation modulates cell interactions by confering both attractive and repulsive properties that are highly regulated by ST8SIA2 and ST8SIA4 (PubMed:28810663). Polysialylation is formed on a-2,3-linked sialic acid of core glycans... | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane; Lipid-anchor, GPI-anchor.; SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000305}; Lip... | null | null | null | null | null | FUNCTION: This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc.; FUNCTION: (Microbial infection) Acts as a receptor for rabies virus. {ECO:0000269|PubMed:9696812}.; FUNCTION: (Microbial infection) Acts as a receptor for Zika virus. {ECO:0000269|P... | Homo sapiens (Human) |
P13595 | NCAM1_MOUSE | MLRTKDLIWTLFFLGTAVSLQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLSPNQQRISVVWNDDDSSTLTIYNANIDDAGIYKCVVTAEDGTQSEATVNVKIFQKLMFKNAPTPQEFKEGEDAVIVCDVVSSLPPTIIWKHKGRDVILKKDVRFIVLSNNYLQIRGIKKTDEGTYRCEGRILARGEINFKDIQVIVNVPPTVQARQSIVNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIENEEEDDEKHIFSDDSSELTIRNVDKNDEAEYVCIAENKAGEQDASIHLKVFAKPKITYVENQTAM... | null | null | axonal fasciculation [GO:0007413]; calcium-mediated signaling [GO:0019722]; cell surface receptor signaling pathway [GO:0007166]; commissural neuron axon guidance [GO:0071679]; epithelial to mesenchymal transition [GO:0001837]; homotypic cell-cell adhesion [GO:0034109]; learning or memory [GO:0007611]; modulation of ch... | axon [GO:0030424]; cell-cell junction [GO:0005911]; external side of plasma membrane [GO:0009897]; glutamatergic synapse [GO:0098978]; growth cone [GO:0030426]; myelin sheath [GO:0043209]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734... | heparin binding [GO:0008201]; LRR domain binding [GO:0030275]; phosphatase binding [GO:0019902] | PF00041;PF07679;PF13927; | 2.60.40.10; | null | PTM: Polysialylated by ST8SIA2 and ST8SIA4. Polysialylation modulates cell interactions by confering both attractive and repulsive properties that are highly regulated by ST8SIA2 and ST8SIA4. Polysialylation is formed on a-2,3-linked sialic acid of core glycans. {ECO:0000250|UniProtKB:P13591}. | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane; Lipid-anchor, GPI-anchor. | null | null | null | null | null | FUNCTION: This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc. | Mus musculus (Mouse) |
P13596 | NCAM1_RAT | MLRTKDLIWTLFFLGTAVSLQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLSPNQQRISVVWNDDDSSTLTIYNANIDDAGIYKCVVTAEDGTQSEATVNVKIFQKLMFKNAPTPQEFKEGEDAVIVCDVVSSLPPTIIWKHKGRDVILKKDVRFIVLSNNYLQIRGIKKTDEGTYRCEGRILARGEINFKDIQVIVNVPPTVQARQSIVNATANLGQSVTLVCDADGFPEPTMSWTKDGEPIENEEEDDEKHIFSDDSSELTIRNVDKNDEAEYVCIAENKAGEQDASIHLKVFAKPKITYVENQTAM... | null | null | animal organ regeneration [GO:0031100]; axonal fasciculation [GO:0007413]; calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules [GO:0016338]; calcium-mediated signaling [GO:0019722]; cell adhesion [GO:0007155]; cell surface receptor signaling pathway [GO:0007166]; cellular response to inor... | axon [GO:0030424]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; external side of plasma membrane [GO:0009897]; glutamatergic synapse [GO:0098978]; growth cone [GO:0030426]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]... | cytoskeletal protein binding [GO:0008092]; fibroblast growth factor receptor binding [GO:0005104]; heparin binding [GO:0008201]; LRR domain binding [GO:0030275]; phosphatase binding [GO:0019902] | PF00041;PF07679;PF13927; | 2.60.40.10; | null | PTM: Polysialylated by ST8SIA2 and ST8SIA4. Polysialylation modulates cell interactions by confering both attractive and repulsive properties that are highly regulated by ST8SIA2 and ST8SIA4. Polysialylation is formed on a-2,3-linked sialic acid of core glycans. {ECO:0000250|UniProtKB:P13591}. | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc. | Rattus norvegicus (Rat) |
P13597 | ICAM1_MOUSE | MASTRAKPTLPLLLALVTVVIPGPGDAQVSIHPREAFLPQGGSVQVNCSSSCKEDLSLGLETQWLKDELESGPNWKLFELSEIGEDSSPLCFENCGTVQSSASATITVYSFPESVELRPLPAWQQVGKDLTLRCHVDGGAPRTQLSAVLLRGEEILSRQPVGGHPKDPKEITFTVLASRGDHGANFSCRTELDLRPQGLALFSNVSEARSLRTFDLPATIPKLDTPDLLEVGTQQKLFCSLEGLFPASEARIYLELGGQMPTQESTNSSDSVSATALVEVTEEFDRTLPLRCVLELADQILETQRTLTVYNFSAPVLTLS... | null | null | acute inflammatory response to antigenic stimulus [GO:0002438]; cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell-cell adhesion [GO:0098609]; cellular response to amyloid-beta [GO:1904646]; cellular response to glucose stimulus [GO:0071333]; cellular response to leukemia inhibitory facto... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; immunological synapse [GO:0001772] | integrin binding [GO:0005178]; protein-containing complex binding [GO:0044877] | PF21146;PF03921;PF13895; | 2.60.40.10; | Immunoglobulin superfamily, ICAM family | PTM: Monoubiquitinated, which is promoted by MARCH9 and leads to endocytosis. {ECO:0000250}. | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). During leukocyte trans-endothelial migration, ICAM1 engagement promotes the assembly of endothelial apical cups through ARHGEF26/SGEF and RHOG activation (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
P13598 | ICAM2_HUMAN | MSSFGYRTLTVALFTLICCPGSDEKVFEVHVRPKKLAVEPKGSLEVNCSTTCNQPEVGGLETSLDKILLDEQAQWKHYLVSNISHDTVLQCHFTCSGKQESMNSNVSVYQPPRQVILTLQPTLVAVGKSFTIECRVPTVEPLDSLTLFLFRGNETLHYETFGKAAPAPQEATATFNSTADREDGHRNFSCLAVLDLMSRGGNIFHKHSAPKMLEIYEPVSDSQMVIIVTVVSVLLSLFVTSVLLCFIFGQHLRQQRMGTYGVRAAWRRLPQAFRP | null | null | cell adhesion [GO:0007155]; cell-cell adhesion [GO:0098609] | cleavage furrow [GO:0032154]; membrane [GO:0016020]; microvillus [GO:0005902]; plasma membrane [GO:0005886]; uropod [GO:0001931] | integrin binding [GO:0005178] | PF03921; | 2.60.40.10; | Immunoglobulin superfamily, ICAM family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, microvillus {ECO:0000250|UniProtKB:P35330}. Note=Co-localizes with RDX, EZR and MSN in microvilli. {ECO:0000250|UniProtKB:P35330}. | null | null | null | null | null | FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). ICAM2 may play a role in lymphocyte recirculation by blocking LFA-1-dependent cell adhesion. It mediates adhesive interactions important for antigen-specific immune response, NK-cell mediated clearance, lymphocyte re... | Homo sapiens (Human) |
P13599 | FCGRN_RAT | MGMSQPGVLLSLLLVLLPQTWGAEPRLPLMYHLAAVSDLSTGLPSFWATGWLGAQQYLTYNNLRQEADPCGAWIWENQVSWYWEKETTDLKSKEQLFLEAIRTLENQINGTFTLQGLLGCELAPDNSSLPTAVFALNGEEFMRFNPRTGNWSGEWPETDIVGNLWMKQPEAARKESEFLLTSCPERLLGHLERGRQNLEWKEPPSMRLKARPGNSGSSVLTCAAFSFYPPELKFRFLRNGLASGSGNCSTGPNGDGSFHAWSLLEVKRGDEHHYQCQVEHEGLAQPLTVDLDSPARSSVPVVGIILGLLLVVVAIAGGVL... | null | null | humoral immune response [GO:0006959]; immune response [GO:0006955] | endosome membrane [GO:0010008]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615] | beta-2-microglobulin binding [GO:0030881]; IgG binding [GO:0019864]; IgG receptor activity [GO:0019770] | PF07654;PF00129; | 2.60.40.10;3.30.500.10; | Immunoglobulin superfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2911353}; Single-pass type I membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:P55899}. | null | null | null | null | null | FUNCTION: Cell surface receptor that transfers passive humoral immunity from the mother to the newborn. Binds to the Fc region of monomeric immunoglobulin gamma and mediates its selective uptake from milk (PubMed:18818657, PubMed:7969498). IgG in the milk is bound at the apical surface of the intestinal epithelium. The... | Rattus norvegicus (Rat) |
P13601 | AL1A7_RAT | MSSPAQPAVPAPLANLKIQHTKIFINNEWHNSLNGKKFPVINPATEEVICHVEEGDKADVDKAVKAARQAFQIGSPWRTMDASERGCLLNKLADLMERDRVLLATMESMNAGKIFTHAYLLDTEVSIKALKYFAGWADKIHGQTIPSDGDVFTYTRREPIGVCGQIIPWNGPLILFIWKIGAALSCGNTVIVKPAEQTPLTALYMASLIKEAGFPPGVVNVVPGYGSTAGAAISSHMDIDKVSFTGSTEVGKLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDSAVEFAHQGVFFHQGQICVAASRLFVEESIYDEFV... | 1.2.1.3 | null | ethanol catabolic process [GO:0006068]; operant conditioning [GO:0035106] | cytoplasm [GO:0005737] | 3-chloroallyl aldehyde dehydrogenase activity [GO:0004028]; aldehyde dehydrogenase (NAD+) activity [GO:0004029]; benzaldehyde dehydrogenase (NAD+) activity [GO:0018479]; glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity [GO:0043878]; identical protein binding [GO:0042802]; NAD binding [GO:0... | PF00171; | null | Aldehyde dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.3; Evidence={ECO:0000269|PubMed:10998257}; PhysiologicalDirection=left-to-right; Xref=... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.4 mM for acetaldehyde {ECO:0000269|PubMed:10998257}; KM=1.6 mM for propionaldehyde {ECO:0000269|PubMed:10998257}; KM=4.7 uM for benzaldehyde {ECO:0000269|PubMed:10998257}; Note=The highest catalytic efficiency is observed with benzaldehyde as substrate. No activi... | PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. {ECO:0000305|PubMed:10998257}. | null | null | FUNCTION: Can oxidize benzaldehyde, propionaldehyde and acetaldehyde. No detectable activity with retinal. {ECO:0000269|PubMed:10998257}. | Rattus norvegicus (Rat) |
P13607 | ATNA_DROME | MALRSDYEHGRADSYRVATVIATDDDNRTADGQYKSRRKMPAKVNKKENLDDLKQELDIDFHKISPEELYQRFQTHPENGLSHAKAKENLERDGPNALTPPKQTPEWVKFCKNLFGGFAMLLWIGAILCFVAYSIQASTSEEPADDNLYLGIVLSAVVIVTGIFSYYQESKSSKIMESFKNMVPQFATVIREGEKLTLRAEDLVLGDVVEVKFGDRIPADIRIIEARNFKVDNSSLTGESEPQSRGAEFTHENPLETKNLAFFSTNAVEGTAKGVVISCGDHTVMGRIAGLASGLDTGETPIAKEIHHFIHLITGVAVFL... | 7.2.2.13 | null | adult locomotory behavior [GO:0008344]; chemical synaptic transmission [GO:0007268]; determination of adult lifespan [GO:0008340]; intracellular potassium ion homeostasis [GO:0030007]; intracellular sodium ion homeostasis [GO:0006883]; jump response [GO:0007630]; locomotory behavior [GO:0007626]; monoatomic cation tran... | basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; septate junction [GO:0005918]; sodium:potassium-exchanging ATPase complex [GO:0005890]; synapse [GO:0045202] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; P-type sodium:potassium-exchanging transporter activity [GO:0005391] | PF13246;PF00689;PF00690;PF00122;PF00702; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIC subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.13; Evidence={ECO:0000305|PubMed:9648860};... | null | null | null | null | FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nut... | Drosophila melanogaster (Fruit fly) |
P13608 | PGCA_BOVIN | MTTLLLVFVTLRVITAAISVEVSEPDNSLSVSIPEPSPLRVLLGSSLTIPCYFIDPMHPVTTAPSTAPLAPRIKWSRISKEKEVVLLVATEGRVRVNSAYQDKVTLPNYPAIPSDATLEIQNMRSNDSGILRCEVMHGIEDSQATLEVVVKGIVFHYRAISTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKDEFPGVRTYGIRDTNETYDVYCFAEEMEGEVFYATSPEKFTFQEAANECRRLGARLATTGQLYLAWQGGMDMCSAGWLADRSVRYPISKARPNCGG... | null | null | cell adhesion [GO:0007155]; central nervous system development [GO:0007417]; glial cell differentiation [GO:0010001]; positive regulation of neuroblast proliferation [GO:0002052]; skeletal system development [GO:0001501] | extracellular region [GO:0005576]; extracellular space [GO:0005615]; perineuronal net [GO:0072534]; synapse [GO:0045202] | calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; hyaluronic acid binding [GO:0005540] | PF00008;PF00059;PF00084;PF07686;PF00193; | 2.10.70.10;2.60.40.10;2.10.25.10;3.10.100.10; | Aggrecan/versican proteoglycan family | PTM: Contains mostly chondroitin sulfate, but also N-linked and O-linked (about 40) oligosaccharides.; PTM: The keratan sulfate contents differ considerably between adult and fetal bovine proteoglycans. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. | null | null | null | null | null | FUNCTION: This proteoglycan is a major component of extracellular matrix of cartilagenous tissues. A major function of this protein is to resist compression in cartilage. It binds avidly to hyaluronic acid via an N-terminal globular region. May play a regulatory role in the matrix assembly of the cartilage. | Bos taurus (Bovine) |
P13609 | SRGN_MOUSE | MQVPVGSRLVLALAFVLVWGSSVQGYPARRARYQWVRCKPNGFFANCIEEKGPQFDLIDESNNIGPPMNNPVLMEGPSKDFISNYDDYGSGSGSGSGSGSGSGSGSGSGFLGDMEWEYQPTDESNIVYFNYKPFDRILTEQNQDQPEDDFII | null | null | apoptotic process [GO:0006915]; biomineral tissue development [GO:0031214]; granzyme-mediated programmed cell death signaling pathway [GO:0140507]; maintenance of granzyme B location in T cell secretory granule [GO:0033382]; maintenance of protease location in mast cell secretory granule [GO:0033373]; mast cell secreto... | cytolytic granule [GO:0044194]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; mast cell granule [GO:0042629]; postsynaptic specialization, intracellular component [GO:0099091]; Schaffer collateral - CA1 synapse [GO:0098685]; secretory granule [GO:0030141]; zymogen g... | collagen binding [GO:0005518] | PF04360; | null | Serglycin family | PTM: O-glycosylated; contains chondroitin sulfate and heparan sulfate. {ECO:0000269|PubMed:17010166, ECO:0000269|PubMed:7535771}. | SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000269|PubMed:16046402}. Cytolytic granule {ECO:0000250|UniProtKB:P10124}. Secreted, extracellular space {ECO:0000269|PubMed:16046402}. Golgi apparatus {ECO:0000250|UniProtKB:P10124}. Note=Found in mast cell granules and in cytoplasmic granules of cytolytic T-lymphocytes ... | null | null | null | null | null | FUNCTION: Plays a role in formation of mast cell secretory granules and mediates storage of various compounds in secretory vesicles. Required for storage of some proteases in both connective tissue and mucosal mast cells and for storage of granzyme B in T-lymphocytes. Plays a role in localizing neutrophil elastase in a... | Mus musculus (Mouse) |
P13611 | CSPG2_HUMAN | MFINIKSILWMCSTLIVTHALHKVKVGKSPPVRGSLSGKVSLPCHFSTMPTLPPSYNTSEFLRIKWSKIEVDKNGKDLKETTVLVAQNGNIKIGQDYKGRVSVPTHPEAVGDASLTVVKLLASDAGLYRCDVMYGIEDTQDTVSLTVDGVVFHYRAATSRYTLNFEAAQKACLDVGAVIATPEQLFAAYEDGFEQCDAGWLADQTVRYPIRAPRVGCYGDKMGKAGVRTYGFRSPQETYDVYCYVDHLDGDVFHLTVPSKFTFEEAAKECENQDARLATVGELQAAWRNGFDQCDYGWLSDASVRHPVTVARAQCGGGLL... | null | null | cell adhesion [GO:0007155]; cell recognition [GO:0008037]; central nervous system development [GO:0007417]; glial cell differentiation [GO:0010001]; glial cell migration [GO:0008347]; osteoblast differentiation [GO:0001649]; positive regulation of neuroblast proliferation [GO:0002052]; skeletal system development [GO:0... | collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; interphotoreceptor matrix [GO:0033165]; lysosomal lumen [GO:0043202]; membrane [GO:0016020]; ... | calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; extracellular matrix structural constituent conferring compression resistance [GO:0030021]; glycosaminoglycan binding [GO:0005539]; hyaluronic acid binding [GO:0005540] | PF00008;PF00059;PF00084;PF07686;PF00193; | 2.10.70.10;2.60.40.10;2.10.25.10;3.10.100.10; | Aggrecan/versican proteoglycan family | PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000269|PubMed:26091039}.; PTM: Proteolytically cleaved by ADAMTS5 and ADAMTS15 in the pericellular matrix surrounding myoblasts, facilitating myoblast contact and fusion which is required for skeletal muscle development and regeneration. {ECO:0000250|UniP... | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305|PubMed:2583089}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:29777959}. Secreted, extracellular space, extracellular matrix, interphotoreceptor matrix {ECO:0000269|PubMed:29777959}. Secreted {ECO:0000269|... | null | null | null | null | null | FUNCTION: May play a role in intercellular signaling and in connecting cells with the extracellular matrix. May take part in the regulation of cell motility, growth and differentiation. Binds hyaluronic acid. | Homo sapiens (Human) |
P13612 | ITA4_HUMAN | MAWEARREPGPRRAAVRETVMLLLCLGVPTGRPYNVDTESALLYQGPHNTLFGYSVVLHSHGANRWLLVGAPTANWLANASVINPGAIYRCRIGKNPGQTCEQLQLGSPNGEPCGKTCLEERDNQWLGVTLSRQPGENGSIVTCGHRWKNIFYIKNENKLPTGGCYGVPPDLRTELSKRIAPCYQDYVKKFGENFASCQAGISSFYTKDLIVMGAPGSSYWTGSLFVYNITTNKYKAFLDKQNQVKFGSYLGYSVGAGHFRSQHTTEVVGGAPQHEQIGKAYIFSIDEKELNILHEMKGKKLGSYFGASVCAVDLNADGF... | null | null | axonogenesis involved in innervation [GO:0060385]; B cell differentiation [GO:0030183]; cell adhesion mediated by integrin [GO:0033627]; cell-cell adhesion [GO:0098609]; cell-cell adhesion in response to extracellular stimulus [GO:0140039]; cell-cell adhesion mediated by integrin [GO:0033631]; cell-matrix adhesion [GO:... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; growth cone [GO:0030426]; integrin alpha4-beta1 complex [GO:0034668]; integrin alpha4-beta7 complex [GO:0034669]; integrin complex [GO:0008305]; membrane [GO:0016020]; neuronal cell... | cell adhesion molecule binding [GO:0050839]; coreceptor activity [GO:0015026]; fibronectin binding [GO:0001968]; integrin binding [GO:0005178]; metal ion binding [GO:0046872]; protein antigen binding [GO:1990405] | PF01839;PF08441;PF20805;PF20806; | 1.20.5.930;2.130.10.130;2.60.40.1460;2.60.40.1510;2.60.40.1530; | Integrin alpha chain family | PTM: Phosphorylation on Ser-1027 inhibits PXN binding. {ECO:0000269|PubMed:11533025}. | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Integrins alpha-4/beta-1 (VLA-4) and alpha-4/beta-7 are receptors for fibronectin. They recognize one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. They are also receptors for VCAM1. Integrin alpha-4/beta-1 recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-4/bet... | Homo sapiens (Human) |
P13615 | L_VSNJH | MDFNLIEDSTHWEEEESDFLLRDILSKEDQMSYLNSADYNLNSPLISDDMVYLIKRMNHEEVPPIWRSKEWDSPLDMLKGCQAQPLSHQDMHNWFGTWIQNIQHDSAQGFTFLKEVDKEAEMTYDLVSTFLKGWVGKEYPFKPKGREIDSIALVGPLCQKFLDLHKVTLILNAVSLGETKELLTTFKGKYRMSCENIPIARLRLPSLGPVFMCKGWTYIHKERVLMDRNFLLMCKDVIIGRMQTFLSMIGRSDNKFSPDQIYTLANVYRIGDRILEQCGNRAYDLIKMIEPICNLKMMELARLHRPKIPKFPHFEEHLKG... | 2.1.1.375; 2.7.7.48; 2.7.7.88; 3.6.1.- | null | negative stranded viral RNA replication [GO:0039689] | host cell cytoplasm [GO:0030430]; virion component [GO:0044423] | ATP binding [GO:0005524]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; RNA-dependent RNA polymerase activity [GO:0003968] | PF21080;PF14314;PF21081;PF14318;PF00946; | null | Rhabdoviridae protein L family | null | SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03523}. Host cytoplasm {ECO:0000250|UniProtKB:P03523}. Note=L and P are packaged asymmetrically towards the blunt end of the virus. {ECO:0000250|UniProtKB:P03523}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=GTP + H2... | null | null | null | null | FUNCTION: Responsible for RNA synthesis (replicase and transcriptase), cap addition, and cap methylation (By similarity). Performs also the polyadenylation of subgenomic mRNAs by a stuttering mechanism at a slipery stop site present at the end of viral genes (By similarity). The template is composed of the viral RNA ti... | Vesicular stomatitis New Jersey virus (strain Hazelhurst subtype Hazelhurst) (VSNJV) |
P13622 | NFIB_MESAU | MMYSPICLTQDEFHPFIEALLPHVRAIAYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLSEKPEIKQKWASRLLAKLRKDIRQEYREDFVLTVTGKKHPCCVLSNPDQKGKIRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLMKSPHCTNPALCVQPHHITVSVKELDLFLAYYVQEQDSGQSGSPSHNDPAKNPPGYLEDSFVKSGVFNVSELVRVSRTPITQGTGVNFPIGEIPSQPYYHDMNSGVNLQRSLSSPPSSKRPKTISIDENMEPSPTGDFYPSPNSPAAGSRTWHERDQDMSSPTTMKKPE... | null | null | anterior commissure morphogenesis [GO:0021960]; chondrocyte differentiation [GO:0002062]; club cell differentiation [GO:0060486]; commissural neuron axon guidance [GO:0071679]; DNA replication [GO:0006260]; glial cell differentiation [GO:0010001]; lung ciliated cell differentiation [GO:0061141]; negative regulation of ... | cerebellar mossy fiber [GO:0044300]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00859;PF03165;PF10524; | null | CTF/NF-I family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Transcriptional activator of GFAP, essential for proper brain development. Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and ... | Mesocricetus auratus (Golden hamster) |
P13631 | RARG_HUMAN | MATNKERLFAAGALGPGSGYPGAGFPFAFPGALRGSPPFEMLSPSFRGLGQPDLPKEMASLSVETQSTSSEEMVPSSPSPPPPPRVYKPCFVCNDKSSGYHYGVSSCEGCKGFFRRSIQKNMVYTCHRDKNCIINKVTRNRCQYCRLQKCFEVGMSKEAVRNDRNKKKKEVKEEGSPDSYELSPQLEELITKVSKAHQETFPSLCQLGKYTTNSSADHRVQLDLGLWDKFSELATKCIIKIVEFAKRLPGFTGLSIADQITLLKAACLDILMLRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFAGQLLP... | null | null | anterior/posterior pattern specification [GO:0009952]; apoptotic process [GO:0006915]; canonical Wnt signaling pathway [GO:0060070]; cell differentiation [GO:0030154]; cellular response to corticotropin-releasing hormone stimulus [GO:0071376]; cellular response to leukemia inhibitory factor [GO:1990830]; cellular respo... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; nuclear glucocorticoid receptor binding [GO:0035259]; nuclear receptor activity [GO:0004879]; nuclear retinoid X receptor ... | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR1 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28167758}. Cytoplasm {ECO:0000269|PubMed:28167758}. | null | null | null | null | null | FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) c... | Homo sapiens (Human) |
P13635 | CERU_RAT | MKFLLLSALLFLHSSLAWTREKHYYIGITEAVWDYASGSEEKELISVDTEQSNFYLRNGPDRIGRKYKKALYSEYTDGTFTKTIDKPAWLGFLGPVIKAEVGDKVSVHVKNFASRPYTFHAHGVTYTKANEGAIYPDNTTDFQRADDKLFPGQQYLYVLRANEPSPGEGDSNCVTRIYHSHVDAPKDIASGLIGPLILCKKGSLHKEKEENIDQEFVLMFSVVDENLSWYLEDNIKTFCSEPEKVDKDNEDFQESNRMYSINGYTFGSLPGLSMCAEDRVKWYLFGMGNEVDVHSELFHGQALTSKNYHTDIINLFPATL... | 1.11.1.27; 1.11.1.9; 1.16.3.1; 1.16.3.4 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:P00450}; Note=Binds 6 Cu(2+) cations per monomer. {ECO:0000250|UniProtKB:P00450}; | female pregnancy [GO:0007565]; intracellular copper ion homeostasis [GO:0006878]; intracellular iron ion homeostasis [GO:0006879]; iron ion transport [GO:0006826]; lactation [GO:0007595]; liver development [GO:0001889]; lung development [GO:0030324]; mammary gland involution [GO:0060056]; plasma membrane copper ion tra... | cell surface [GO:0009986]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | copper ion binding [GO:0005507]; ferroxidase activity [GO:0004322]; glutathione peroxidase activity [GO:0004602]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on metal ions, oxygen as acceptor [GO:0016724]; phospholipid-hydroperoxide glutathione peroxidase activity [GO:0047066]; protein-folding... | PF00394;PF07731;PF07732; | 2.60.40.420; | Multicopper oxidase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14707133}. Note=Colocalizes with GCP1 in secretory intracellular compartments. {ECO:0000269|PubMed:14707133}. | CATALYTIC ACTIVITY: Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O; Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1; Evidence={ECO:0000250|UniProtKB:P00450}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11150; Evidence={ECO:000... | null | null | null | null | FUNCTION: Multifunctional blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Copper ions provide a large number of enzymatic activites. Oxidizes highly tox... | Rattus norvegicus (Rat) |
P13637 | AT1A3_HUMAN | MGDKKDDKDSPKKNKGKERRDLDDLKKEVAMTEHKMSVEEVCRKYNTDCVQGLTHSKAQEILARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAYGIQAGTEDDPSGDNLYLGIVLAAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIREGEKMQVNAEEVVVGDLVEIKGGDRVPADLRIISAHGCKVDNSSLTGESEPQTRSPDCTHDNPLETRNITFFSTNCVEGTARGVVVATGDRTVMGRIATLASGLEVGKTPIAIEIEHFIQLITGVAVFLGVSFFILSLILGYTWLEAVIFLIGIIVA... | 7.2.2.13 | null | cell communication by electrical coupling involved in cardiac conduction [GO:0086064]; cellular response to amyloid-beta [GO:1904646]; cellular response to steroid hormone stimulus [GO:0071383]; intracellular potassium ion homeostasis [GO:0030007]; intracellular sodium ion homeostasis [GO:0006883]; neuron projection ma... | axon [GO:0030424]; endoplasmic reticulum [GO:0005783]; extracellular vesicle [GO:1903561]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; neuron to neuron synapse [GO:0098984]; neuronal cell body [GO:0043025]; neuronal cell body membrane [GO:0032809]; organelle membrane [GO:0031090]; photoreceptor inner segment [... | amyloid-beta binding [GO:0001540]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; P-type sodium:potassium-exchanging transporter activity [GO:0005391]; protein-folding chaperone binding [GO:0051087]; steroid hormone binding [GO:1990239] | PF13246;PF00689;PF00690;PF00122; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIC subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7711835}; Multi-pass membrane protein {ECO:0000269|PubMed:7711835}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.13; | null | null | null | null | FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nut... | Homo sapiens (Human) |
P13638 | AT1B2_RAT | MVIQKEKKSCGQVVEEWKEFVWNPRTHQFMGRTGTSWAFILLFYLVFYGFLTAMFTLTMWVMLQTVSDHTPKYQDRLATPGLMIRPKTENLDVIVNISDTESWDQHVQKLNKFLEPYNDSIQAQKNDVCRPGRYYEQPDNGVLNYPKRACQFNRTQLGNCSGIGDPTHYGYSTGQPCVFIKMNRVINFYAGANQSMNVTCVGKKDEDAENLGHFIMFPANGNIDLMYFPYYGKKFHVNYTQPLVAVKFLNVTPNVEVNVECRINAANIATDDERDKFAARVAFKLRINKA | null | null | cell-substrate adhesion [GO:0031589]; intracellular potassium ion homeostasis [GO:0030007]; intracellular sodium ion homeostasis [GO:0006883]; lateral ventricle development [GO:0021670]; membrane repolarization [GO:0086009]; motor behavior [GO:0061744]; negative regulation of glial cell migration [GO:1903976]; neuronal... | apical plasma membrane [GO:0016324]; astrocyte end-foot [GO:0097450]; astrocyte projection [GO:0097449]; cell body membrane [GO:0044298]; cell periphery [GO:0071944]; cell projection membrane [GO:0031253]; cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; lateral plasma membrane [GO:0016328]; membr... | ATPase activator activity [GO:0001671]; ATPase binding [GO:0051117]; P-type sodium:potassium-exchanging transporter activity [GO:0005391]; protein heterodimerization activity [GO:0046982]; protein-macromolecule adaptor activity [GO:0030674] | PF00287; | 1.20.5.170;2.60.40.1660; | X(+)/potassium ATPases subunit beta family | null | SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. | null | null | null | null | null | FUNCTION: This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-2 subunit is not known.; FUNCTION: Mediates cell adhesion of neurons and astrocytes, and promotes neurite ... | Rattus norvegicus (Rat) |
P13639 | EF2_HUMAN | MVNFTVDQIRAIMDKKANIRNMSVIAHVDHGKSTLTDSLVCKAGIIASARAGETRFTDTRKDEQERCITIKSTAISLFYELSENDLNFIKQSKDGAGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLELQLEPEELYQTFQRIVENVNVIISTYGEGESGPMGNIMIDPVLGTVGFGSGLHGWAFTLKQFAEMYVAKFAAKGEGQLGPAERAKKVEDMMKKLWGDRYFDPANGKFSKSATSPEGKKLPRTFCQLILDPIFKVFDAIMNFKKEETAKLIEKLD... | 3.6.5.- | null | hematopoietic progenitor cell differentiation [GO:0002244]; positive regulation of translation [GO:0045727]; translational elongation [GO:0006414] | aggresome [GO:0016235]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; ribonucleoprotein complex [GO:1990904]; ribosome [GO:0005840]... | cadherin binding [GO:0045296]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein kinase binding [GO:0019901]; ribosome binding [GO:0043022]; RNA binding [GO:0003723]; translation elongation factor activity [GO:0003746] | PF00679;PF14492;PF03764;PF00009;PF03144; | 3.30.230.10;3.30.70.240;3.30.70.870;3.40.50.300;2.40.30.10; | TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, EF-G/EF-2 subfamily | PTM: Phosphorylation by EF-2 kinase completely inactivates EF-2; it requires prior phosphorylation by CDK2 at Ser-595 during mitotic prometaphase. Phosphorylation by CSK promotes SUMOylation, proteolytic cleavage, and nuclear translocation if the C-terminal fragment. {ECO:0000269|PubMed:23184662, ECO:0000269|PubMed:246... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25064856}. Nucleus {ECO:0000269|PubMed:24648518}. Note=Phosphorylation by CSK promotes cleavage and SUMOylation-dependent nuclear translocation of the C-terminal cleavage product. {ECO:0000269|PubMed:24648518}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000305|PubMed:26593721}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000305|PubMed:26593721}... | null | null | null | null | FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation (PubMed:26593721). During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to t... | Homo sapiens (Human) |
P13640 | MT1G_HUMAN | MDPNCSCAAAGVSCTCASSCKCKECKCTSCKKSCCSCCPVGCAKCAQGCICKGASEKCSCCA | null | null | cellular response to cadmium ion [GO:0071276]; cellular response to copper ion [GO:0071280]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; cellular response to zinc ion [GO:0071294]; detoxification of copper ion [GO:0010273]; intracellular zinc ion homeostasis [GO:0006882]; monocyte act... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | metal ion binding [GO:0046872]; zinc ion binding [GO:0008270] | PF00131; | 4.10.10.10; | Metallothionein superfamily, Type 1 family | null | null | null | null | null | null | null | FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids. | Homo sapiens (Human) |
P13642 | SYSC_RABIT | MVLDLDLFRVDKGGDPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEPVGDDESIPENVLNFDDVTADTLTNLKVSQIKKVRLLIDEAILKCDAERIKLEAERFESLREIGNLLHPSVPISNDEDADNKVERIWGDCTVRKKYSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLRNRGYTPIYTPFFMRKEVMQEVAQLSQFDEELYKVIGKGSEKSDDNSYDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRVHQ... | 6.1.1.11 | null | cytoplasmic translation [GO:0002181]; mitochondrial seryl-tRNA aminoacylation [GO:0070158]; negative regulation of angiogenesis [GO:0016525]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of vascular endothelial growth factor production [GO:1904046]; selenocysteine incorpor... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | ATP binding [GO:0005524]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; selenocysteine-tRNA ligase activity [GO:0098619]; serine-tRNA ligase activity [GO:0004828]; tRNA binding [GO:0000049] | PF02403;PF00587; | 1.10.287.40; | Class-II aminoacyl-tRNA synthetase family, Type-1 seryl-tRNA synthetase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P49591}. Nucleus {ECO:0000250|UniProtKB:P49591}. Note=Predominantly cytoplasmic, but a minor proportion is also found in the nucleus. {ECO:0000250|UniProtKB:P49591}. | CATALYTIC ACTIVITY: Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669, Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442, ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11; Evide... | null | PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. | null | null | FUNCTION: Catalyzes the attachment of serine to tRNA(Ser) in a two-step reaction: serine is first activated by ATP to form Ser-AMP and then transferred to the acceptor end of tRNA(Ser). Is probably also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further con... | Oryctolagus cuniculus (Rabbit) |
P13645 | K1C10_HUMAN | MSVRYSSSKHYSSSRSGGGGGGGGCGGGGGVSSLRISSSKGSLGGGFSSGGFSGGSFSRGSSGGGCFGGSSGGYGGLGGFGGGSFRGSYGSSSFGGSYGGIFGGGSFGGGSFGGGSFGGGGFGGGGFGGGFGGGFGGDGGLLSGNEKVTMQNLNDRLASYLDKVRALEESNYELEGKIKEWYEKHGNSHQGEPRDYSKYYKTIDDLKNQILNLTTDNANILLQIDNARLAADDFRLKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRNVSTGDVNVEMNAAPGVDLTQLLNN... | null | null | epidermis development [GO:0008544]; epithelial cell differentiation [GO:0030855]; intermediate filament organization [GO:0045109]; keratinocyte differentiation [GO:0030216]; peptide cross-linking [GO:0018149]; positive regulation of epidermis development [GO:0045684]; protein heterotetramerization [GO:0051290] | cell surface [GO:0009986]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; intermediate filament [GO:0005882]; keratin filament [GO:0045095]; membrane [GO:0016020]; nucleus [GO:0005634] | protein heterodimerization activity [GO:0046982]; structural constituent of skin epidermis [GO:0030280] | PF00038; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | null | SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:12427098}. Cell surface {ECO:0000269|PubMed:19627498}. Cytoplasm {ECO:0000269|PubMed:32179842}. | null | null | null | null | null | FUNCTION: Plays a role in the establishment of the epidermal barrier on plantar skin (By similarity). Involved in the maintenance of cell layer development and keratin filament bundles in suprabasal cells of the epithelium (By similarity). {ECO:0000250|UniProtKB:P02535}.; FUNCTION: (Microbial infection) Acts as a media... | Homo sapiens (Human) |
P13646 | K1C13_HUMAN | MSLRLQSSSASYGGGFGGGSCQLGGGRGVSTCSTRFVSGGSAGGYGGGVSCGFGGGAGSGFGGGYGGGLGGGYGGGLGGGFGGGFAGGFVDFGACDGGLLTGNEKITMQNLNDRLASYLEKVRALEEANADLEVKIRDWHLKQSPASPERDYSPYYKTIEELRDKILTATIENNRVILEIDNARLAADDFRLKYENELALRQSVEADINGLRRVLDELTLSKTDLEMQIESLNEELAYMKKNHEEEMKEFSNQVVGQVNVEMDATPGIDLTRVLAEMREQYEAMAERNRRDAEEWFHTKSAELNKEVSTNTAMIQTSKTE... | null | null | cytoskeleton organization [GO:0007010]; epithelial cell differentiation [GO:0030855]; intermediate filament organization [GO:0045109]; regulation of translation in response to stress [GO:0043555] | cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intermediate filament cytoskeleton [GO:0045111]; keratin filament [GO:0045095]; nucleus [GO:0005634] | structural molecule activity [GO:0005198] | PF00038; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | PTM: O-glycosylated; glycans consist of single N-acetylglucosamine residues. {ECO:0000269|PubMed:2474541}. | null | null | null | null | null | null | FUNCTION: Type 1 keratin (Probable). Maintains postnatal tongue mucosal cell homeostasis and tissue organization in response to mechanical stress, potentially via regulation of the G1/S phase cyclins CCNE1 and CCNE2 (By similarity). {ECO:0000250|UniProtKB:P08730, ECO:0000305}. | Homo sapiens (Human) |
P13647 | K2C5_HUMAN | MSRQSSVSFRSGGSRSFSTASAITPSVSRTSFTSVSRSGGGGGGGFGRVSLAGACGVGGYGSRSLYNLGGSKRISISTSGGSFRNRFGAGAGGGYGFGGGAGSGFGFGGGAGGGFGLGGGAGFGGGFGGPGFPVCPPGGIQEVTVNQSLLTPLNLQIDPSIQRVRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRQNLEPLFEQYINNLRRQLDSIVGERGRLDSELRNMQDLVEDFKNKYEDEINKRTTAENEFVMLKKDVDAAYMNKVELEAKVDALMDEINFMKMFFDAELSQMQTHVSD... | null | null | epidermis development [GO:0008544]; intermediate filament organization [GO:0045109]; intermediate filament polymerization [GO:0045107]; keratinization [GO:0031424]; regulation of cell migration [GO:0030334]; regulation of protein localization [GO:0032880]; response to mechanical stimulus [GO:0009612] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intermediate filament [GO:0005882]; keratin filament [GO:0045095]; membrane [GO:0016020]; nucleus [GO:0005634] | scaffold protein binding [GO:0097110]; structural constituent of cytoskeleton [GO:0005200]; structural constituent of skin epidermis [GO:0030280] | PF00038;PF16208; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | PTM: Phosphorylated by CDK1, AURKB and Rho-kinase, phosphorylation is regulated by the cell cycle (By similarity). Thr-24 phosphorylation, mediated by CDK1, peaks during prometaphase or metaphase cells with phosphorylated filamentous structures evident throughout the cytoplasm during early mitosis (By similarity). CDK1... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20128788}. | null | null | null | null | null | FUNCTION: Required for the formation of keratin intermediate filaments in the basal epidermis and maintenance of the skin barrier in response to mechanical stress (By similarity). Regulates the recruitment of Langerhans cells to the epidermis, potentially by modulation of the abundance of macrophage chemotactic cytokin... | Homo sapiens (Human) |
P13649 | PYRF_CANAL | MTVNTKTYSERAETHASPVAQRLFRLMESKKTNLCASIDVDTTKEFLELIDKLGPYVCLIKTHIDIINDFSYESTIEPLLGLSRKHQFMIFEDRKFADIGNTVKKQYIGGVYKISSWADITNAHGVTGNGVVEGLKQGAKETTTNQEPRGLLMLAELSSVGSLAYGEYSQKTVEIAKSDKEFVVGFIAQRDMGGQEEGFDWLIMTPGVGLDDKGDGLGQQYRTVDEVVSTGTDIIIVGRGLFGKGRDPDIEGKRYRDAGWNAYLKKTGQL | 4.1.1.23 | null | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; adhesion of symbiont to host [GO:0044406]; cell migration [GO:0016477]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms [GO:0044182]; pyrimidine nucleobase bio... | cytosol [GO:0005829]; fungal biofilm matrix [GO:0062040] | orotate phosphoribosyltransferase activity [GO:0004588]; orotidine-5'-phosphate decarboxylase activity [GO:0004590] | PF00215; | 3.20.20.70; | OMP decarboxylase family | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU10110}; | null | PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. | null | null | null | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
P13650 | DHGB_ACICA | MNKHLLAKIALLSAVQLVTLSAFADVPLTPSQFAKAKSENFDKKVILSNLNKPHALLWGPDNQIWLTERATGKILRVNPESGSVKTVFQVPEIVNDADGQNGLLGFAFHPDFKNNPYIYISGTFKNPKSTDKELPNQTIIRRYTYNKSTDTLEKPVDLLAGLPSSKDHQSGRLVIGPDQKIYYTIGDQGRNQLAYLFLPNQAQHTPTQQELNGKDYHTYMGKVLRLNLDGSIPKDNPSFNGVVSHIYTLGHRNPQGLAFTPNGKLLQSEQGPNSDDEINLIVKGGNYGWPNVAGYKDDSGYAYANYSAAANKSIKDLAQN... | 1.1.5.2 | COFACTOR: Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442; Note=Binds 1 PQQ group per subunit.; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 3 Ca(2+) ions per subunit.; | null | null | metal ion binding [GO:0046872]; quinoprotein glucose dehydrogenase activity [GO:0008876] | PF07995; | 2.120.10.30; | PQQ oxidoreductase GdhB family | null | null | CATALYTIC ACTIVITY: Reaction=a ubiquinone + D-glucose = a ubiquinol + D-glucono-1,5-lactone; Xref=Rhea:RHEA:22152, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:4167, ChEBI:CHEBI:16217, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976; EC=1.1.5.2; | null | null | null | null | FUNCTION: Oxidizes glucose to gluconolactone. | Acinetobacter calcoaceticus |
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