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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P07320 | CRGD_HUMAN | MGKITLYEDRGFQGRHYECSSDHPNLQPYLSRCNSARVDSGCWMLYEQPNYSGLQYFLRRGDYADHQQWMGLSDSVRSCRLIPHSGSHRIRLYEREDYRGQMIEFTEDCSCLQDRFRFNEIHSLNVLEGSWVLYELSNYRGRQYLLMPGDYRRYQDWGATNARVGSLRRVIDFS | null | null | cellular response to reactive oxygen species [GO:0034614]; lens development in camera-type eye [GO:0002088]; lens fiber cell differentiation [GO:0070306]; visual perception [GO:0007601] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | structural constituent of eye lens [GO:0005212] | PF00030; | 2.60.20.10; | Beta/gamma-crystallin family | null | null | null | null | null | null | null | FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. | Homo sapiens (Human) |
P07321 | EPO_MOUSE | MGVPERPTLLLLLSLLLIPLGLPVLCAPPRLICDSRVLERYILEAKEAENVTMGCAEGPRLSENITVPDTKVNFYAWKRMEVEEQAIEVWQGLSLLSEAILQAQALLANSSQPPETLQLHIDKAISGLRSLTSLLRVLGAQKELMSPPDTTPPAPLRTLTVDTFCKLFRVYANFLRGKLKLYTGEVCRRGDR | null | null | acute-phase response [GO:0006953]; angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; cardiac muscle tissue morphogenesis [GO:0055008]; cellular hyperosmotic response [GO:0071474]; embryo implantation [GO:0007566]; erythrocyte differentiation [GO:0030218]; erythrocyte maturation [GO:0043249]; erythropoietin-med... | cell body [GO:0044297]; cell surface [GO:0009986]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; erythropoietin receptor binding [GO:0005128]; hormone activity [GO:0005179]; protein kinase activator activity [GO:0030295] | PF00758; | 1.20.1250.10; | EPO/TPO family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Hormone involved in the regulation of erythrocyte proliferation and differentiation and the maintenance of a physiological level of circulating erythrocyte mass. Binds to EPOR leading to EPOR dimerization and JAK2 activation thereby activating specific downstream effectors, including STAT1 and STAT3. {ECO:000... | Mus musculus (Mouse) |
P07323 | ENOG_RAT | MSIQKIWAREILDSRGNPTVEVDLHTAKGLFRAAVPSGASTGIYEALELRDGDKQRYLGKGVLKAVDHINSTIAPALISSGLSVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKAGAAEKDLPLYRHIAQLAGNSDLILPVPAFNVINGGSHAGNKLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYGKDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKMVIGMDVAASEFYRDGKYDLDFKSPADPSRCITGDQLGALYQDFVRNYPVVSIEDPFDQDDWAAWSKFTANVGIQIVGDDL... | 4.2.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Mg(2+) is required for catalysis and for stabilizing the dimer.; | canonical glycolysis [GO:0061621]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; multicellular organismal reproductive process [GO:0048609]; response to estradiol [GO:0032355]; response to organic cyclic compound [GO:0014070]; response to xenobiotic stimulus [GO:0009410] | cell cortex [GO:0005938]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; growth cone [GO:0030426]; membrane [GO:0016020]; membrane raft [GO:0045121]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; phosphopyruvate hydratase complex [GO:0000015]; photoreceptor inner segment [GO:0001917]; synaptic membrane ... | enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634]; protein-containing complex binding [GO:0044877] | PF00113;PF03952; | 3.20.20.120;3.30.390.10; | Enolase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. | null | null | FUNCTION: Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival. | Rattus norvegicus (Rat) |
P07327 | ADH1A_HUMAN | MSTAGKVIKCKAAVLWELKKPFSIEEVEVAPPKAHEVRIKMVAVGICGTDDHVVSGTMVTPLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLAIPQCGKCRICKNPESNYCLKNDVSNPQGTLQDGTSRFTCRRKPIHHFLGISTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTGYGSAVNVAKVTPGSTCAVFGLGGVGLSAIMGCKAAGAARIIAVDINKDKFAKAKELGATECINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPDSQNLSMNPMLLLTGRTWKGAIL... | 1.1.1.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:11274460, ECO:0000269|PubMed:15449945}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:11274460, ECO:0000269|PubMed:15449945}; | alcohol metabolic process [GO:0006066]; ethanol oxidation [GO:0006069]; retinoic acid metabolic process [GO:0042573]; retinol metabolic process [GO:0042572] | cytosol [GO:0005829]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886] | alcohol dehydrogenase (NAD+) activity [GO:0004022]; alcohol dehydrogenase activity, zinc-dependent [GO:0004024]; butanol dehydrogenase activity [GO:1990362]; NAD-retinol dehydrogenase activity [GO:0004745]; zinc ion binding [GO:0008270] | PF08240;PF00107; | 3.90.180.10;3.40.50.720; | Zinc-containing alcohol dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH; Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000269|PubMed:2738060}; CATALYTIC ACTIVITY: Reaction=a secondary alcohol + NAD(+) = a keton... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=32 uM for butan-1-ol {ECO:0000269|PubMed:2738060}; KM=14 uM for 1-propanol {ECO:0000269|PubMed:2738060}; KM=6100 uM for ethanol {ECO:0000269|PubMed:2738060}; | null | null | null | FUNCTION: Alcohol dehydrogenase (PubMed:2738060). Oxidizes primary as well as secondary alcohols. Ethanol is a very poor substrate (PubMed:2738060). {ECO:0000269|PubMed:2738060}. | Homo sapiens (Human) |
P07328 | NIFD_AZOVI | MTGMSREEVESLIQEVLEVYPEKARKDRNKHLAVNDPAVTQSKKCIISNKKSQPGLMTIRGCAYAGSKGVVWGPIKDMIHISHGPVGCGQYSRAGRRNYYIGTTGVNAFVTMNFTSDFQEKDIVFGGDKKLAKLIDEVETLFPLNKGISVQSECPIGLIGDDIESVSKVKGAELSKTIVPVRCEGFRGVSQSLGHHIANDAVRDWVLGKRDEDTTFASTPYDVAIIGDYNIGGDAWSSRILLEEMGLRCVAQWSGDGSISEIELTPKVKLNLVHCYRSMNYISRHMEEKYGIPWMEYNFFGPTKTIESLRAIAAKFDESI... | 1.18.6.1 | COFACTOR: Name=[8Fe-7S] cluster; Xref=ChEBI:CHEBI:21143; Note=Binds 1 [8Fe-7S] cluster per heterodimer.; COFACTOR: Name=[7Fe-Mo-9S-C-homocitryl] cluster; Xref=ChEBI:CHEBI:30409; Note=Binds 1 [7Fe-Mo-9S-C-homocitryl] cluster per subunit.; | nitrogen fixation [GO:0009399] | molybdenum-iron nitrogenase complex [GO:0016612] | ATP binding [GO:0005524]; carbonyl sulfide nitrogenase activity [GO:0018697]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; nitrogenase activity [GO:0016163] | PF00148; | 3.40.50.1980; | NifD/NifK/NifE/NifN family | null | null | CATALYTIC ACTIVITY: Reaction=16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16 ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-[ferredoxin] + 16 phosphate; Xref=Rhea:RHEA:21448, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17997, ChEBI:CHEBI:18276, ChEBI:CHE... | null | null | null | null | FUNCTION: This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. | Azotobacter vinelandii |
P07329 | NIFK_AZOVI | MSQQVDKIKASYPLFLDQDYKDMLAKKRDGFEEKYPQDKIDEVFQWTTTKEYQELNFQREALTVNPAKACQPLGAVLCALGFEKTMPYVHGSQGCVAYFRSYFNRHFREPVSCVSDSMTEDAAVFGGQQNMKDGLQNCKATYKPDMIAVSTTCMAEVIGDDLNAFINNSKKEGFIPDEFPVPFAHTPSFVGSHVTGWDNMFEGIARYFTLKSMDDKVVGSNKKINIVPGFETYLGNFRVIKRMLSEMGVGYSLLSDPEEVLDTPADGQFRMYAGGTTQEEMKDAPNALNTVLLQPWHLEKTKKFVEGTWKHEVPKLNIPM... | 1.18.6.1 | COFACTOR: Name=[8Fe-7S] cluster; Xref=ChEBI:CHEBI:21143; Note=Binds 1 [8Fe-7S] cluster per heterodimer.; | nitrogen fixation [GO:0009399] | molybdenum-iron nitrogenase complex [GO:0016612] | ATP binding [GO:0005524]; carbonyl sulfide nitrogenase activity [GO:0018697]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; nitrogenase activity [GO:0016163] | PF11844;PF00148; | 3.40.50.1980;1.20.89.10; | NifD/NifK/NifE/NifN family | null | null | CATALYTIC ACTIVITY: Reaction=16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16 ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-[ferredoxin] + 16 phosphate; Xref=Rhea:RHEA:21448, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17997, ChEBI:CHEBI:18276, ChEBI:CHE... | null | null | null | null | FUNCTION: This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. | Azotobacter vinelandii |
P07330 | CHEB_ECOLI | MSKIRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVSSLTGKGSEVTLRALELGAIDFVTKPQLGIREGMLAYNEMIAEKVRTAAKASLAAHKPLSAPTTLKAGPLLSSEKLIAIGASTGGTEAIRHVLQPLPLSSPALLITQHMPPGFTRSFADRLNKLCQIGVKEAEDGERVLPGHAYIAPGDRHMELSRSGANYQIKIHDGPAVNRHRPSVDVLFHSVAKQAGRNAVGVILTGMGNDGAAGMLAMRQAGAWTLAQNEASCVVFGMPREAIN... | 3.1.1.61; 3.5.1.44 | null | chemotaxis [GO:0006935]; protein deamination [GO:0018277]; protein demethylation [GO:0006482]; signal transduction [GO:0007165] | cytosol [GO:0005829]; plasma membrane [GO:0005886] | deaminase binding [GO:1990827]; phosphorelay response regulator activity [GO:0000156]; protein-glutamate methylesterase activity [GO:0008984]; protein-glutamine glutaminase activity [GO:0050568] | PF01339;PF00072; | 3.40.50.2300;3.40.50.180; | CheB family | PTM: Phosphorylated by CheA (PubMed:2188960, PubMed:3280143). Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity (PubMed:2188960). {ECO:0000269|PubMed:2188960, ECO:0000269|PubMed:3280143}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00099, ECO:0000269|PubMed:358191}. | CATALYTIC ACTIVITY: Reaction=[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol; Xref=Rhea:RHEA:23236, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:10311, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:29973, ChEBI:CHEBI:82795; EC=3.1.1.61; Evidence={ECO:0000255|HAMAP-Ru... | null | null | null | null | FUNCTION: Involved in chemotaxis (PubMed:2188960, PubMed:324984, PubMed:358191, PubMed:392505). Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli (PubMed:2188960, PubMed:392505). Catalyzes the demethylation of specific methylglutamate residues introduced into the c... | Escherichia coli (strain K12) |
P07332 | FES_HUMAN | MGFSSELCSPQGHGVLQQMQEAELRLLEGMRKWMAQRVKSDREYAGLLHHMSLQDSGGQSRAISPDSPISQSWAEITSQTEGLSRLLRQHAEDLNSGPLSKLSLLIRERQQLRKTYSEQWQQLQQELTKTHSQDIEKLKSQYRALARDSAQAKRKYQEASKDKDRDKAKDKYVRSLWKLFAHHNRYVLGVRAAQLHHQHHHQLLLPGLLRSLQDLHEEMACILKEILQEYLEISSLVQDEVVAIHREMAAAAARIQPEAEYQGFLRQYGSAPDVPPCVTFDESLLEEGEPLEPGELQLNELTVESVQHTLTSVTDELAVA... | 2.7.10.2 | null | cardiac muscle cell proliferation [GO:0060038]; cell adhesion [GO:0007155]; cellular response to vitamin D [GO:0071305]; centrosome cycle [GO:0007098]; chemotaxis [GO:0006935]; microtubule bundle formation [GO:0001578]; myoblast proliferation [GO:0051450]; peptidyl-tyrosine phosphorylation [GO:0018108]; positive regula... | cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; microtubule cytoskeleton [GO:0015630] | ATP binding [GO:0005524]; immunoglobulin receptor binding [GO:0034987]; microtubule binding [GO:0008017]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphatidylinositol binding [GO:0035091]; protein tyrosine kinase activity [GO:0004713] | PF00611;PF07714;PF00017; | 1.20.1270.60;1.10.287.160;3.30.505.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Fes/fps subfamily | PTM: Autophosphorylated on Tyr-713. Phosphorylated by LYN in response to FCER1 activation. Phosphorylated by HCK. {ECO:0000269|PubMed:15485904, ECO:0000269|PubMed:18046454, ECO:0000269|PubMed:18775312, ECO:0000269|PubMed:19001085, ECO:0000269|PubMed:19382747, ECO:0000269|PubMed:20111072, ECO:0000269|PubMed:7687763}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle. Golgi apparatus. Cell junction, focal adhesion. Note=Distributed throughout the cytosol when the kinase is not activated. Association with microtubules requires activatio... | 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 that acts downstream of cell surface receptors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, cell attachment and cell spreading. Plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Acts down-strea... | Homo sapiens (Human) |
P07333 | CSF1R_HUMAN | MGPGVLLLLLVATAWHGQGIPVIEPSVPELVVKPGATVTLRCVGNGSVEWDGPPSPHWTLYSDGSSSILSTNNATFQNTGTYRCTEPGDPLGGSAAIHLYVKDPARPWNVLAQEVVVFEDQDALLPCLLTDPVLEAGVSLVRVRGRPLMRHTNYSFSPWHGFTIHRAKFIQSQDYQCSALMGGRKVMSISIRLKVQKVIPGPPALTLVPAELVRIRGEAAQIVCSASSVDVNFDVFLQHNNTKLAIPQQSDFHNNRYQKVLTLNLDQVDFQHAGNYSCVASNVQGKHSTSMFFRVVESAYLNLSSEQNLIQEVTVGEGLN... | 2.7.10.1 | null | axon guidance [GO:0007411]; cell population proliferation [GO:0008283]; cell-cell junction maintenance [GO:0045217]; cellular response to cytokine stimulus [GO:0071345]; cellular response to macrophage colony-stimulating factor stimulus [GO:0036006]; cytokine-mediated signaling pathway [GO:0019221]; forebrain neuron di... | cell surface [GO:0009986]; CSF1-CSF1R complex [GO:1990682]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; 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]; protein homodimerization activity [GO:0042803]; protein phosphatase binding [GO:0019903]; protein tyrosine kinase activity [GO:0004713] | PF00047;PF13927;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 (PubMed:20489731, PubMed:23408870, PubMed:24336230). Phosphorylation at Tyr-561 is important for normal down-regulation of signaling by ubiquitination, internalization and degradation. Phosphorylation at Tyr-561 and Tyr-809 is important for interaction with SR... | SUBCELLULAR LOCATION: Cell 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: 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... | Homo sapiens (Human) |
P07334 | CDR1_SCHPO | MVKRHKNTIGVWRLGKTLGTGSTSCVRLAKHAKTGDLAAIKIIPIRYASIGMEILMMRLLRHPNILRLYDVWTDHQHMYLALEYVPDGELFHYIRKHGPLSEREAAHYLSQILDAVAHCHRFRFRHRDLKLENILIKVNEQQIKIADFGMATVEPNDSCLENYCGSLHYLAPEIVSHKPYRGAPADVWSCGVILYSLLSNKLPFGGQNTDVIYNKIRHGAYDLPSSISSAAQDLLHRMLDVNPSTRITIPEVFSHPFLMGCTSLSSMDSTTPPTPSLSIDEIDPLVVDCMCVLWKKSSSKKVVRRLQQRDDNDEKYVYKV... | 2.7.11.1 | null | cell cycle [GO:0007049]; cell division [GO:0051301]; intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; signaling [GO:0023052] | Cdr2 medial cortical node complex [GO:0110115]; cell division site [GO:0032153]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; medial cortical node [GO:0071341]; nucleus [GO:0005634] | ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, NIM1 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: This protein, a dose-dependent mitotic inducer, appears to function as a negative regulator of mitosis inhibitor wee1 by phosphorylating and inactivating it. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P07335 | KCRB_RAT | MPFSNSHNTQKLRFPAEDEFPDLSSHNNHMAKVLTPELYAELRAKCTPSGFTLDDAIQTGVDNPGHPYIMTVGAVAGDEESYDVFKDLFDPIIEDRHGGYQPSDEHKTDLNPDNLQGGDDLDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLSGRYYALKSMTEAEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKTFLVWINEEDHLRVISMQKGGNMKEVFTRFCTGLTQIETLFKSKNYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLPHLGKHEKFSEVLKRLRLQKR... | 2.7.3.2 | null | cellular response to estrogen stimulus [GO:0071391]; cellular response to wortmannin [GO:1904568]; cerebellum development [GO:0021549]; futile creatine cycle [GO:0140651]; intracellular chloride ion homeostasis [GO:0030644]; phosphocreatine biosynthetic process [GO:0046314]; phosphorylation [GO:0016310] | cytosol [GO:0005829]; dendrite [GO:0030425]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; creatine kinase activity [GO:0004111]; ubiquitin protein ligase binding [GO:0031625] | PF00217;PF02807; | 1.10.135.10;3.30.590.10; | ATP:guanido phosphotransferase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q04447}. Mitochondrion {ECO:0000250|UniProtKB:Q04447}. Cell membrane {ECO:0000250|UniProtKB:P12277}. Note=Localizes to the mitochondria of thermogenic fat cells via the internal MTS-like signal (iMTS-L) region. {ECO:0000250|UniProtKB:Q04447}. | CATALYTIC ACTIVITY: Reaction=ATP + creatine = ADP + H(+) + N-phosphocreatine; Xref=Rhea:RHEA:17157, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57947, ChEBI:CHEBI:58092, ChEBI:CHEBI:456216; EC=2.7.3.2; Evidence={ECO:0000250|UniProtKB:Q04447, ECO:0000255|PROSITE-ProRule:PRU10029}; PhysiologicalDirection=left-to-ri... | null | null | null | null | FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa. Acts as a key regulator ... | Rattus norvegicus (Rat) |
P07338 | CTRB1_RAT | MAFLWLVSCFALVGATFGCGVPTIQPVLTGLSRIVNGEDAIPGSWPWQVSLQDKTGFHFCGGSLISEDWVVTAAHCGVKTSDVVVAGEFDQGSDEENIQVLKIAQVFKNPKFNMFTVRNDITLLKLATPAQFSETVSAVCLPNVDDDFPPGTVCATTGWGKTKYNALKTPEKLQQAALPIVSEADCKKSWGSKITDVMTCAGASGVSSCMGDSGGPLVCQKDGVWTLAGIVSWGSGVCSTSTPAVYSRVTALMPWVQQILEAN | 3.4.21.1 | null | digestion [GO:0007586]; positive regulation of apoptotic process [GO:0043065]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508]; response to cytokine [GO:0034097]; response to food [GO:0032094]; response to nutrient [GO:0007584]; response to peptide hormone [GO:0043434]; response to toxic substance [GO:... | extracellular region [GO:0005576] | peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236] | PF00089; | 2.40.10.10; | Peptidase S1 family | null | SUBCELLULAR LOCATION: Secreted, extracellular space. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.; EC=3.4.21.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10078, ECO:0000255|PROSITE-ProRule:PRU10079}; | null | null | null | null | null | Rattus norvegicus (Rat) |
P07339 | CATD_HUMAN | MQPSSLLPLALCLLAAPASALVRIPLHKFTSIRRTMSEVGGSVEDLIAKGPVSKYSQAVPAVTEGPIPEVLKNYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSVPCQSASSASALGGVKVERQVFGEATKQPGITFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNIFSFYLSRDPDAQPGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDQVEVASGLTLCKEGCEAIVDTGTSLMVGPVDEVRELQKAIGAVPL... | 3.4.23.5 | null | antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; autophagosome assembly [GO:0000045]; insulin catabolic process [GO:1901143]; insulin receptor recycling [GO:0038020]; lipoprotein catabolic process [GO:0042159]; positive regulation of apoptotic process [GO:0043065]; positiv... | collagen-containing extracellular matrix [GO:0062023]; endosome lumen [GO:0031904]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; ficolin-1-rich granule lumen [GO:1904813]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:000... | aspartic-type endopeptidase activity [GO:0004190]; aspartic-type peptidase activity [GO:0070001]; cysteine-type endopeptidase activity [GO:0004197]; peptidase activity [GO:0008233] | PF07966;PF00026; | 2.40.70.10; | Peptidase A1 family | PTM: N- and O-glycosylated. {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:23234360}.; PTM: Undergoes proteolytic cleavage and activation by ADAM30. {ECO:0000269|PubMed:27333034}.; PTM: As well as the major heavy chain which starts... | SUBCELLULAR LOCATION: Lysosome. Melanosome. Secreted, extracellular space. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. In aortic samples, detected as an extracellular protein loosely bound to the matrix (PubMed:20551380). {ECO:0000269|PubMed:20551380}. | CATALYTIC ACTIVITY: Reaction=Specificity similar to, but narrower than, that of pepsin A. Does not cleave the 4-Gln-|-His-5 bond in B chain of insulin.; EC=3.4.23.5; | null | null | null | null | FUNCTION: Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation (PubMed:27333034). Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease. {ECO:0000269|PubMed:27333... | Homo sapiens (Human) |
P07340 | AT1B1_RAT | MARGKAKEEGSWKKFIWNSEKKEFLGRTGGSWFKILLFYVIFYGCLAGIFIGTIQVMLLTISELKPTYQDRVAPPGLTQIPQIQKTEISFRPNDPKSYEAYVLNIIRFLEKYKDSAQKDDMIFEDCGSMPSEPKERGEFNHERGERKVCRFKLDWLGNCSGLNDESYGYKEGKPCIIIKLNRVLGFKPKPPKNESLETYPLTMKYNPNVLPVQCTGKRDEDKDKVGNIEYFGMGGFYGFPLQYYPYYGKLLQPKYLQPLLAVQFTNLTLDTEIRIECKAYGENIGYSEKDRFQGRFDVKIEVKS | null | null | ATP metabolic process [GO:0046034]; blastocyst development [GO:0001824]; cardiac muscle contraction [GO:0060048]; cell adhesion [GO:0007155]; innate immune response [GO:0045087]; intracellular calcium ion homeostasis [GO:0006874]; intracellular potassium ion homeostasis [GO:0030007]; intracellular sodium ion homeostasi... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; caveola [GO:0005901]; intercalated disc [GO:0014704]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; organelle membrane [GO:0031090]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; sodium:potassium-exchanging ATPase com... | ATPase activator activity [GO:0001671]; ATPase binding [GO:0051117]; P-type sodium:potassium-exchanging transporter activity [GO:0005391]; protein heterodimerization activity [GO:0046982]; protein kinase binding [GO:0019901]; protein-macromolecule adaptor activity [GO:0030674] | PF00287; | 1.20.5.170;2.60.40.1660; | X(+)/potassium ATPases subunit beta family | PTM: Glutathionylated. N-glycosylated (PubMed:14749213). {ECO:0000250|UniProtKB:P14094, ECO:0000269|PubMed:14749213}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:14749213}; Single-pass type II membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P14094}. Note=Colocalizes with OBSCN at the intercalated disk an... | 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 beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane (P... | Rattus norvegicus (Rat) |
P07341 | ALDOB_CHICK | MTHQFPALSPEQKKALSDIAQRIVASGKGILAADESVGTMGNRLQRINVENTEENRRAFREILFSSDASISKSIGGVILFHETLYQKDSSGKPFPAIIKEKGMVVGIKLDAGTAPLAGTNGETTIQGLDKLAERCAQYKKDGADFGKWRAVLKISSTTPSQLAIQENANTLARYASICQQNGLVPIVEPEVLPDGDHDLQRCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHSCPKKYTPQDVAVATVTTLLRTVPAAVPGICFLSGGQSEEEASLNLNAMNQSPLPKPWKLTFSYGRALQASALAAWLGKSEN... | 4.1.2.13 | null | fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate [GO:0061624]; fructose metabolic process [GO:0006000]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; liver development [GO:0001889]; NADH oxidation [GO:0006116... | centriolar satellite [GO:0034451]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; microtubule organizing center [GO:0005815] | ATPase binding [GO:0051117]; cytoskeletal protein binding [GO:0008092]; fructose binding [GO:0070061]; fructose-1-phosphate aldolase activity [GO:0061609]; fructose-bisphosphate aldolase activity [GO:0004332]; identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090] | PF00274; | 3.20.20.70; | Class I fructose-bisphosphate aldolase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; | null | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. | null | null | null | Gallus gallus (Chicken) |
P07342 | ILVB_YEAST | MIRQSTLKNFAIKRCFQHIAYRNTPAMRSVALAQRFYSSSSRYYSASPLPASKRPEPAPSFNVDPLEQPAEPSKLAKKLRAEPDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSNALNQLTSRAQDEFVMQSINKAADLINLAKKPVLYVGAGILNHADGPRLL... | 2.2.1.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250}; Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250}; | amino acid biosynthetic process [GO:0008652]; branched-chain amino acid biosynthetic process [GO:0009082]; isoleucine biosynthetic process [GO:0009097]; valine biosynthetic process [GO:0009099] | acetolactate synthase complex [GO:0005948]; mitochondrion [GO:0005739] | acetolactate synthase activity [GO:0003984]; flavin adenine dinucleotide binding [GO:0050660]; magnesium ion binding [GO:0000287]; thiamine pyrophosphate binding [GO:0030976] | PF02775;PF00205;PF02776; | 3.40.50.970;3.40.50.1220; | TPP enzyme family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:10213630}. | CATALYTIC ACTIVITY: Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2; Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6; Evidence={ECO:0000269|PubMed:10213630}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25250; Evidence={ECO:0000269|PubMed:10213... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8.6 mM for pyruvate (catalytic subunit only) {ECO:0000269|PubMed:10213630}; KM=18.1 mM for pyruvate (reconstituted into the acetolactate synthase complex with the regulatory subunit) {ECO:0000269|PubMed:10213630}; | PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4. {ECO:0000305|PubMed:10213630}.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 1/4. {ECO:0000305|PubMed:10213630}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-7.5. {ECO:0000269|PubMed:10213630}; | null | FUNCTION: Catalytic subunit of mitochondrial acetolactate synthase, which catalyzes the first of a series of common steps in the biosynthesis of the branched-chain amino acids. Catalyzes the irreversible decarboxylation of pyruvate to a bound hydroxyethyl group that then condenses with either a second pyruvate molecule... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07347 | ARD1_YEAST | MPINIRRATINDIICMQNANLHNLPENYMMKYYMYHILSWPEASFVATTTTLDCEDSDEQDENDKLELTLDGTNDGRTIKLDPTYLAPGEKLVGYVLVKMNDDPDQQNEPPNGHITSLSVMRTYRRMGIAENLMRQALFALREVHQAEYVSLHVRQSNRAALHLYRDTLAFEVLSIEKSYYQDGEDAYAMKKVLKLEELQISNFTHRRLKENEEKLEDDLESDLLEDIIKQGVNDIIV | 2.3.1.255 | null | N-terminal protein amino acid acetylation [GO:0006474]; N-terminal protein amino acid propionylation [GO:0061606] | NatA complex [GO:0031415] | identical protein binding [GO:0042802]; peptide-glutamate-alpha-N-acetyltransferase activity [GO:1990190]; peptide-serine-alpha-N-acetyltransferase activity [GO:1990189] | PF00583; | 3.40.630.30; | Acetyltransferase family, ARD1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal glycyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetylglycyl-[protein]; Xref=Rhea:RHEA:50496, Rhea:RHEA-COMP:12666, Rhea:RHEA-COMP:12700, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64723, ChEBI:CHEBI:133369; EC=2.3.1.255; Evidence={ECO:0... | null | null | null | null | FUNCTION: Catalytic component of the NatA N-terminal acetyltransferase, which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover. {ECO:0000269|PubMed:16009... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07355 | ANXA2_HUMAN | MSTVHEILCKLSLEGDHSTPPSAYGSVKAYTNFDAERDALNIETAIKTKGVDEVTIVNILTNRSNAQRQDIAFAYQRRTKKELASALKSALSGHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDARDLYDAGVKRKGTDVPKWISIMTERSVPHLQKVFDRYKSYSPYDMLESIRKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYYIQ... | null | null | angiogenesis [GO:0001525]; cell-matrix adhesion [GO:0007160]; collagen fibril organization [GO:0030199]; epithelial cell apoptotic process [GO:1904019]; fibrinolysis [GO:0042730]; lung development [GO:0030324]; membrane raft assembly [GO:0001765]; mRNA transcription by RNA polymerase II [GO:0042789]; negative regulatio... | adherens junction [GO:0005912]; AnxA2-p11 complex [GO:1990665]; azurophil granule lumen [GO:0035578]; basement membrane [GO:0005604]; basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; cytos... | cadherin binding involved in cell-cell adhesion [GO:0098641]; calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; calcium-dependent protein binding [GO:0048306]; cytoskeletal protein binding [GO:0008092]; identical protein binding [GO:0042802]; p... | PF00191; | 1.10.220.10; | Annexin family | PTM: Phosphorylation of Tyr-24 enhances heat stress-induced translocation to the cell surface. {ECO:0000269|PubMed:15302870, ECO:0000269|PubMed:2946940}.; PTM: ISGylated. {ECO:0000269|PubMed:16139798}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000269|PubMed:17081065}. Note=In the lamina beneath the plasma membrane. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Translocated from the cy... | null | null | null | null | null | FUNCTION: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechani... | Homo sapiens (Human) |
P07356 | ANXA2_MOUSE | MSTVHEILCKLSLEGDHSTPPSAYGSVKPYTNFDAERDALNIETAVKTKGVDEVTIVNILTNRSNVQRQDIAFAYQRRTKKELPSALKSALSGHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDARELYDAGVKRKGTDVPKWISIMTERSVCHLQKVFERYKSYSPYDMLESIKKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYYIQ... | null | null | angiogenesis [GO:0001525]; body fluid secretion [GO:0007589]; cell adhesion [GO:0007155]; cell-matrix adhesion [GO:0007160]; collagen fibril organization [GO:0030199]; epithelial cell apoptotic process [GO:1904019]; fibrinolysis [GO:0042730]; lung development [GO:0030324]; membrane raft assembly [GO:0001765]; mRNA tran... | AnxA2-p11 complex [GO:1990665]; basement membrane [GO:0005604]; basolateral plasma membrane [GO:0016323]; cell cortex [GO:0005938]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]... | bone sialoprotein binding [GO:0044730]; cadherin binding involved in cell-cell adhesion [GO:0098641]; calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; calcium-dependent protein binding [GO:0048306]; cytoskeletal protein binding [GO:0008092]; i... | PF00191; | 1.10.220.10; | Annexin family | PTM: ISGylated. {ECO:0000269|PubMed:16139798}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Melanosome {ECO:0000250}. Note=In the lamina beneath the plasma membrane. | null | null | null | null | null | FUNCTION: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response (By similarity). Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a trans... | Mus musculus (Mouse) |
P07357 | CO8A_HUMAN | MFAVVFFILSLMTCQPGVTAQEKVNQRVRRAATPAAVTCQLSNWSEWTDCFPCQDKKYRHRSLLQPNKFGGTICSGDIWDQASCSSSTTCVRQAQCGQDFQCKETGRCLKRHLVCNGDQDCLDGSDEDDCEDVRAIDEDCSQYEPIPGSQKAALGYNILTQEDAQSVYDASYYGGQCETVYNGEWRELRYDSTCERLYYGDDEKYFRKPYNFLKYHFEALADTGISSEFYDNANDLLSKVKKDKSDSFGVTIGIGPAGSPLLVGVGVSHSQDTSFLNELNKYNEKKFIFTRIFTKVQTAHFKMRKDDIMLDEGMLQSLME... | null | null | complement activation [GO:0006956]; complement activation, alternative pathway [GO:0006957]; complement activation, classical pathway [GO:0006958]; immune response [GO:0006955]; killing of cells of another organism [GO:0031640]; positive regulation of immune response [GO:0050778] | blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; membrane attack complex [GO:0005579]; plasma membrane [GO:0005886] | complement binding [GO:0001848]; protein-containing complex binding [GO:0044877] | PF21195;PF00057;PF01823;PF00090; | 4.10.400.10;2.20.100.10; | Complement C6/C7/C8/C9 family | null | SUBCELLULAR LOCATION: Secreted. Cell membrane; Multi-pass membrane protein. Note=Secreted as soluble protein. Inserts into the cell membrane of target cells. | null | null | null | null | null | FUNCTION: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C8A inserts into the target membrane, but does not form pores by itself. {ECO:0000269|PubMed:17872444, ECO:0000269|PubMed:7440581}. | Homo sapiens (Human) |
P07358 | CO8B_HUMAN | MKNSRTWAWRAPVELFLLCAALGCLSLPGSRGERPHSFGSNAVNKSFAKSRQMRSVDVTLMPIDCELSSWSSWTTCDPCQKKRYRYAYLLQPSQFHGEPCNFSDKEVEDCVTNRPCGSQVRCEGFVCAQTGRCVNRRLLCNGDNDCGDQSDEANCRRIYKKCQHEMDQYWGIGSLASGINLFTNSFEGPVLDHRYYAGGCSPHYILNTRFRKPYNVESYTPQTQGKYEFILKEYESYSDFERNVTEKMASKSGFSFGFKIPGIFELGISSQSDRGKHYIRRTKRFSHTKSVFLHARSDLEVAHYKLKPRSLMLHYEFLQR... | null | null | complement activation [GO:0006956]; complement activation, alternative pathway [GO:0006957]; complement activation, classical pathway [GO:0006958]; immune response [GO:0006955]; killing of cells of another organism [GO:0031640]; positive regulation of immune response [GO:0050778] | extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; membrane [GO:0016020]; membrane attack complex [GO:0005579]; plasma membrane [GO:0005886] | protein-containing complex binding [GO:0044877] | PF21195;PF00057;PF01823;PF00090; | 4.10.400.10;2.20.100.10; | Complement C6/C7/C8/C9 family | PTM: N-glycosylated; contains one or two bound glycans. Not O-glycosylated. {ECO:0000269|PubMed:10551839, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:2820472}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. | Homo sapiens (Human) |
P07359 | GP1BA_HUMAN | MPLLLLLLLLPSPLHPHPICEVSKVASHLEVNCDKRNLTALPPDLPKDTTILHLSENLLYTFSLATLMPYTRLTQLNLDRCELTKLQVDGTLPVLGTLDLSHNQLQSLPLLGQTLPALTVLDVSFNRLTSLPLGALRGLGELQELYLKGNELKTLPPGLLTPTPKLEKLSLANNNLTELPAGLLNGLENLDTLLLQENSLYTIPKGFFGSHLLPFAFLHGNPWLCNCEILYFRRWLQDNAENVYVWKQGVDVKAMTSNVASVQCDNSDKFPVYKYPGKGCPTLGDEGDTDLYDYYPEEDTEGDKVRATRTVVKFPTKAHT... | null | null | blood coagulation [GO:0007596]; blood coagulation, intrinsic pathway [GO:0007597]; cell adhesion [GO:0007155]; cell morphogenesis [GO:0000902]; cell surface receptor signaling pathway [GO:0007166]; fibrinolysis [GO:0042730]; megakaryocyte development [GO:0035855]; platelet activation [GO:0030168]; positive regulation o... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; glycoprotein Ib-IX-V complex [GO:1990779]; membrane [GO:0016020]; plasma membrane [GO:0005886] | thrombin-activated receptor activity [GO:0015057] | PF13855;PF01462; | 3.80.10.10; | null | PTM: Glycocalicin is the product of a proteolytic cleavage/shedding, catalyzed by ADAM17, which releases most of the extracellular domain. Binding sites for vWF and thrombin are in this part of the protein. {ECO:0000269|PubMed:17445093}. | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: GP-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to the A1 domain of vWF, which is already bound to the subendothelium. | Homo sapiens (Human) |
P07360 | CO8G_HUMAN | MLPPGTATLLTLLLAAGSLGQKPQRPRRPASPISTIQPKANFDAQQFAGTWLLVAVGSACRFLQEQGHRAEATTLHVAPQGTAMAVSTFRKLDGICWQVRQLYGDTGVLGRFLLQARDARGAVHVVVAETDYQSFAVLYLERAGQLSVKLYARSLPVSDSVLSGFEQRVQEAHLTEDQIFYFPKYGFCEAADQFHVLDEVRR | null | null | complement activation, alternative pathway [GO:0006957]; complement activation, classical pathway [GO:0006958]; killing of cells of another organism [GO:0031640]; positive regulation of immune response [GO:0050778] | blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; membrane attack complex [GO:0005579]; plasma membrane [GO:0005886] | complement binding [GO:0001848]; protein-containing complex binding [GO:0044877]; retinol binding [GO:0019841] | PF00061; | 2.40.128.20; | Calycin superfamily, Lipocalin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: C8 is a constituent of the membrane attack complex. C8 binds to the C5B-7 complex, forming the C5B-8 complex. C5-B8 binds C9 and acts as a catalyst in the polymerization of C9. The gamma subunit seems to be able to bind retinol. | Homo sapiens (Human) |
P07363 | CHEA_ECOLI | MSMDISDFYQTFFDEADELLADMEQHLLVLQPEAPDAEQLNAIFRAAHSIKGGAGTFGFSVLQETTHLMENLLDEARRGEMQLNTDIINLFLETKDIMQEQLDAYKQSQEPDAASFDYICQALRQLALEAKGETPSAVTRLSVVAKSEPQDEQSRSQSPRRIILSRLKAGEVDLLEEELGHLTTLTDVVKGADSLSAILPGDIAEDDITAVLCFVIEADQITFETVEVSPKISTPPVLKLAAEQAPTGRVEREKTTRSNESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSELDPVNHGDLITSMGQLQRNARDLQES... | 2.7.13.3 | null | aerotaxis [GO:0009454]; bacterial-type flagellum-dependent swimming motility [GO:0071977]; chemotaxis [GO:0006935]; establishment of localization in cell [GO:0051649]; negative regulation of protein modification process [GO:0031400]; phosphorelay signal transduction system [GO:0000160]; phosphorylation [GO:0016310]; po... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; methyl accepting chemotaxis protein complex [GO:0098561]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; phosphorelay sensor kinase activity [GO:0000155]; protein histidine kinase activity [GO:0004673] | PF01584;PF09078;PF02895;PF02518;PF01627; | 3.30.70.400;1.10.287.560;3.30.565.10;1.20.120.160;2.30.30.40; | null | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3; | null | null | null | null | FUNCTION: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY. | Escherichia coli (strain K12) |
P07371 | CB22_PEA | MAASSSSSMALSSPTLAGKQLKLNPSSQELGAARFTMRKSATTKKVASSGSPWYGPDRVKYLGPFSGESPSYLTGEFPGDYGWDTAGLSADPETFSKNRELEVIHSRWAMLGALGCVFPELLSRNGVKFGEAVWFKAGSQIFSEGGLDYLGNPSLVHAQSILAIWATQVILMGAVEGYRIAGGPLGEVVDPLYPGGSFDPLGLADDPEAFAELKVKELKNGRLAMFSMFGFFVQAIVTGKGPLENLADHLADPVNNNAWSYATNFVPGK | null | COFACTOR: Note=Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin. {ECO:0000305|PubMed:15719016}; | photosynthesis, light harvesting in photosystem I [GO:0009768]; response to light stimulus [GO:0009416] | chloroplast envelope [GO:0009941]; chloroplast thylakoid membrane [GO:0009535]; photosystem I [GO:0009522]; photosystem II [GO:0009523]; plastoglobule [GO:0010287] | chlorophyll binding [GO:0016168]; metal ion binding [GO:0046872] | PF00504; | 1.10.3460.10; | Light-harvesting chlorophyll a/b-binding (LHC) protein family | PTM: Photoregulated by reversible phosphorylation of its threonine residues. | SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. {ECO:0000269|PubMed:2174365}.; FUNCTION: May channel protons produced in the catalytic Mn center of water oxidation into the thylakoid lumen. {ECO:0... | Pisum sativum (Garden pea) (Lathyrus oleraceus) |
P07374 | UREA_CANEN | MKLSPREVEKLGLHNAGYLAQKRLARGVRLNYTEAVALIASQIMEYARDGEKTVAQLMCLGQHLLGRRQVLPAVPHLLNAVQVEATFPDGTKLVTVHDPISRENGELQEALFGSLLPVPSLDKFAETKEDNRIPGEILCEDECLTLNIGRKAVILKVTSKGDRPIQVGSHYHFIEVNPYLTFDRRKAYGMRLNIAAGTAVRFEPGDCKSVTLVSIEGNKVIRGGNAIADGPVNETNLEAAMHAVRSKGFGHEEEKDASEGFTKEDPNCPFNTFIHRKEYANKYGPTTGDKIRLGDTNLLAEIEKDYALYGDECVFGGGKV... | 3.5.1.5 | COFACTOR: Name=Ni cation; Xref=ChEBI:CHEBI:25516; Evidence={ECO:0000269|PubMed:11696010, ECO:0000269|PubMed:20471401}; Note=Binds 2 nickel ions per subunit. {ECO:0000269|PubMed:20471401}; | nitrogen compound metabolic process [GO:0006807]; urea catabolic process [GO:0043419] | urease complex [GO:0035550] | nickel cation binding [GO:0016151]; toxin activity [GO:0090729]; urease activity [GO:0009039] | PF01979;PF00449;PF00699;PF00547;PF18473; | 3.20.20.140;2.10.150.10;3.30.280.10;2.30.40.10; | Metallo-dependent hydrolases superfamily, Urease alpha subunit family | PTM: Carboxylation allows a single lysine to coordinate two nickel ions. {ECO:0000269|PubMed:20471401}. | null | CATALYTIC ACTIVITY: Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5; Evidence={ECO:0000269|PubMed:11696010}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20558; Evidence={ECO:0000269|Pu... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.5 mM for urea (at 37 degrees Celsius and pH 6.5) {ECO:0000269|PubMed:11696010}; KM=2.9 mM for urea (at 37 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:11696010}; KM=7.1 mM for urea (at 37 degrees Celsius and pH 8.5) {ECO:0000269|PubMed:11696010}; Vmax=6000 umo... | PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. {ECO:0000305}. | null | null | FUNCTION: Urea hydrolase involved in nitrogen recycling from ureide, purine, and arginine catabolism (PubMed:26690979). Is known to be highly toxic and lethal when given by intravenous route, producing convulsions and other signs of central nervous system intoxication associated with the high levels of ammonia formed i... | Canavalia ensiformis (Jack bean) (Dolichos ensiformis) |
P07379 | PCKGC_RAT | MPPQLHNGLDFSAKVIQGSLDSLPQEVRKFVEGNAQLCQPEYIHICDGSEEEYGRLLAHMQEEGVIRKLKKYDNCWLALTDPRDVARIESKTVIITQEQRDTVPIPKSGQSQLGRWMSEEDFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLAKIGIELTDSPYVVASMRIMTRMGTSVLEALGDGEFIKCLHSVGCPLPLKKPLVNNWACNPELTLIAHLPDRREIISFGSGYGGNSLLGKKCFALRIASRLAKEEGWLAEHMLILGITNPEGKKKYLAAAFPSACGKTNLAMMNPTLPGWKVECVGDDIAWMKFDAQ... | 2.7.11.-; 4.1.1.32 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:17685635, ECO:0000269|PubMed:18197707, ECO:0000269|PubMed:18772387, ECO:0000269|PubMed:20476774, ECO:0000269|PubMed:23127136, ECO:0000269|PubMed:24863970, ECO:0000269|PubMed:26322521, ECO:0000269|PubMed:26709450, ECO:0000269|PubMed:28345895}; N... | cellular hyperosmotic response [GO:0071474]; cellular hyperosmotic salinity response [GO:0071475]; cellular hypotonic response [GO:0071476]; cellular hypotonic salinity response [GO:0071477]; cellular response to cAMP [GO:0071320]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to fructose ... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783] | carboxylic acid binding [GO:0031406]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; nucleoside diphosphate kinase activity [GO:0004550]; phosphoenolpyruvate carboxykinase (GTP) activity [GO:0004613]; phosphoenolpyruvate carboxykinase activity... | PF00821;PF17297; | 3.90.228.20;3.40.449.10;2.170.8.10; | Phosphoenolpyruvate carboxykinase [GTP] family | PTM: Acetylated (PubMed:30193097). Lysine acetylation by p300/EP300 is increased on high glucose conditions and promotes ubiquitination by UBR5; acetylation is enhanced in the presence of BAG6. Deacetylated by SIRT2. Deacetylation of Lys-91 is carried out by SIRT1 and depends on PCK1 phosphorylation levels (By similari... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:4186849}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P35558}. Note=Phosphorylation at Ser-90 promotes translocation to the endoplasmic reticulum. {ECO:0000250|UniProtKB:P35558}. | CATALYTIC ACTIVITY: Reaction=GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate; Xref=Rhea:RHEA:10388, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:58702; EC=4.1.1.32; Evidence={ECO:0000269|PubMed:26322521, ECO:0000269|PubMed:26709450, ECO:0000269|PubMed:28345895, ECO:000026... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=39 uM for oxaloacetate {ECO:0000269|PubMed:30193097}; KM=161 uM for GTP {ECO:0000269|PubMed:30193097}; KM=301 uM for phosphoenolpyruvate {ECO:0000269|PubMed:30193097}; KM=79 uM for GDP {ECO:0000269|PubMed:30193097}; KM=475 uM for phosphoenolpyruvate (for phosphoeno... | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000269|PubMed:30193097}. | null | null | FUNCTION: Cytosolic phosphoenolpyruvate carboxykinase that catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate (OAA) and acts as the rate-limiting enzyme in gluconeogenesis (PubMed:26322521, PubMed:26709450, PubMed:28345895, PubMed:30193097, PubMed:31461616, PubMed:4186849). Regulates cataplero... | Rattus norvegicus (Rat) |
P07384 | CAN1_HUMAN | MSEEIITPVYCTGVSAQVQKQRARELGLGRHENAIKYLGQDYEQLRVRCLQSGTLFRDEAFPPVPQSLGYKDLGPNSSKTYGIKWKRPTELLSNPQFIVDGATRTDICQGALGDCWLLAAIASLTLNDTLLHRVVPHGQSFQNGYAGIFHFQLWQFGEWVDVVVDDLLPIKDGKLVFVHSAEGNEFWSALLEKAYAKVNGSYEALSGGSTSEGFEDFTGGVTEWYELRKAPSDLYQIILKALERGSLLGCSIDISSVLDMEAITFKKLVKGHAYSVTGAKQVNYRGQVVSLIRMRNPWGEVEWTGAWSDSSSEWNNVDPY... | 3.4.22.52 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:8954105, ECO:0000269|PubMed:9271093}; Note=Binds 4 Ca(2+) ions. {ECO:0000269|PubMed:9271093}; | mammary gland involution [GO:0060056]; positive regulation of cell population proliferation [GO:0008284]; proteolysis [GO:0006508]; receptor catabolic process [GO:0032801]; regulation of catalytic activity [GO:0050790]; regulation of macroautophagy [GO:0016241]; regulation of NMDA receptor activity [GO:2000310]; self p... | calpain complex [GO:0110158]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; focal adhesion [GO:0005925]; lysosome [GO:0005764]; membrane [GO:0016020]; mitochondrion [GO:0005... | calcium ion binding [GO:0005509]; calcium-dependent cysteine-type endopeptidase activity [GO:0004198]; peptidase activity [GO:0008233] | PF01067;PF13833;PF00648; | 2.60.120.380;3.90.70.10;1.10.238.10; | Peptidase C2 family | PTM: Undergoes calcium-induced successive autoproteolytic cleavages that generate a membrane-bound 78 kDa active form and an intracellular 75 kDa active form. Calpastatin reduces with high efficiency the transition from 78 kDa to 75 kDa calpain forms. {ECO:0000269|PubMed:8769305, ECO:0000269|PubMed:8954105}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21531719, ECO:0000269|PubMed:8769305}. Cell membrane {ECO:0000269|PubMed:8769305}. Note=Translocates to the plasma membrane upon Ca(2+) binding. In granular keratinocytes and in lower corneocytes, colocalizes with FLG and FLG2 (PubMed:21531719). {ECO:0000269|PubMed:21... | CATALYTIC ACTIVITY: Reaction=Broad endopeptidase specificity.; EC=3.4.22.52; Evidence={ECO:0000269|PubMed:16411745, ECO:0000269|PubMed:19617626, ECO:0000269|PubMed:21531719}; | null | null | null | null | FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction (PubMed:19617626, PubMed:21531719, PubMed:2400579). Proteolytically cleaves CTBP1 at 'Asn-375', 'Gly-387' and 'His-409' (PubMed:23707407). Cleaves and ac... | Homo sapiens (Human) |
P07395 | SYFB_ECOLI | MKFSELWLREWVNPAIDSDALANQITMAGLEVDGVEPVAGSFHGVVVGEVVECAQHPNADKLRVTKVNVGGDRLLDIVCGAPNCRQGLRVAVATIGAVLPGDFKIKAAKLRGEPSEGMLCSFSELGISDDHSGIIELPADAPIGTDIREYLKLDDNTIEISVTPNRADCLGIIGVARDVAVLNQLPLVQPEIVPVGATIDDTLPITVEAPEACPRYLGRVVKGINVKAPTPLWMKEKLRRCGIRSIDAVVDVTNYVLLELGQPMHAFDKDRIEGGIVVRMAKEGETLVLLDGTEAKLNADTLVIADHNKALAMGGIFGGE... | 6.1.1.20 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions per tetramer. {ECO:0000250}; | phenylalanyl-tRNA aminoacylation [GO:0006432] | cytosol [GO:0005829]; membrane [GO:0016020]; phenylalanine-tRNA ligase complex [GO:0009328] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; phenylalanine-tRNA ligase activity [GO:0004826]; tRNA binding [GO:0000049] | PF03483;PF03484;PF03147;PF01588;PF17759; | 3.30.56.10;3.30.70.380;2.40.50.140;3.50.40.10; | Phenylalanyl-tRNA synthetase beta subunit family, Type 1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668, Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442, ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6... | null | null | null | null | null | Escherichia coli (strain K12) |
P07396 | PG062_VACCW | MNSHFASAHTPFYINTKEGRYLVLKAVKVCDVRTVECEGSKASCVLKVDKPSSPACERRPSSPSRCERMNNPRKQVPFMRTDMLQNMFAANRDNVASRLLN | null | null | suppression by virus of host type I interferon production [GO:0039501]; symbiont-mediated suppression of host innate immune response [GO:0052170]; viral protein processing [GO:0019082] | host cell cytoplasm [GO:0030430]; virion component [GO:0044423] | DNA binding [GO:0003677]; molecular sequestering activity [GO:0140313] | PF04767; | null | Orthopoxvirus OPG062 family | PTM: Phosphorylated on two serines. While these phosphorylations do not play a role in virion assembly; they are essential for the interaction with host RICTOR and RPTOR. {ECO:0000269|PubMed:20392848, ECO:0000269|PubMed:30078703}. | SUBCELLULAR LOCATION: Virion {ECO:0000305|PubMed:16877059}. Note=Major component of the virion comprising about 10% of the virion mass. {ECO:0000305}. | null | null | null | null | null | FUNCTION: Plays an essential role in virion assembly and morphogenesis (PubMed:20392848). Also plays a role in the inhibition of host immune response by dysregulating mTOR. Sequesters host RICTOR and RPTOR, thereby disrupting mTORC1 and mTORC2 crosstalk. In turn, blocks the host antiviral response in part through mTOR-... | Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) |
P07399 | GLYC_LYCVW | MGQIVTMFEALPHIIDEVINIVIIVLIIITSIKAVYNFATCGILALVSFLFLAGRSCGMYGLNGPDIYKGVYQFKSVEFDMSHLNLTMPNACSVNNSHHYISMGSSGLEPTFTNDSILNHNFCNLTSALNKKSFDHTLMSIVSSLHLSIRGNSNYKAVSCDFNNGITIQYNLSSSDPQSAMSQCRTFRGRVLDMFRTAFGGKYMRSGWGWTGSDGKTTWCSQTSYQYLIIQNRTWENHCRYAGPFGMSRILFAQEKTKFLTRRLSGTFTWTLSDSSGVENPGGYCLTKWMILAAELKCFGNTAVAKCNVNHDEEFCDMLR... | null | null | fusion of virus membrane with host endosome membrane [GO:0039654]; receptor-mediated endocytosis of virus by host cell [GO:0019065]; virion attachment to host cell [GO:0019062] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | metal ion binding [GO:0046872] | PF00798; | 6.10.140.1590;2.20.28.180; | Arenaviridae GPC protein family | PTM: [Pre-glycoprotein polyprotein GP complex]: Specific enzymatic cleavages in vivo yield mature proteins. GP-C polyprotein is cleaved in the endoplasmic reticulum by the host protease MBTPS1. Only cleaved glycoprotein is incorporated into virions. The SSP remains stably associated with the GP complex following cleava... | SUBCELLULAR LOCATION: [Stable signal peptide]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Go... | null | null | null | null | null | FUNCTION: [Stable signal peptide]: Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C). Helps to stabilize the spike complex in its native conformation. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of G1 and G2, glyc... | Lymphocytic choriomeningitis virus (strain WE) (LCMV) |
P07410 | HBB_UROTO | VHLTDGEKNAISTAWGKVNAAEIGAEALGRLLVVYPWTQRFFDSFGDLSSASAVMGNAKVKAHGKKVIDSFSNGLKHLDNLKGTFASLSELHCDKLHVDPENFKLLGNMIVIVMAHHLGKDFTPEAQAAFQKVVAGVANALSHKYH | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. | Urocitellus townsendii (Townsend's ground squirrel) (Spermophilus townsendii) |
P07412 | HBB_FELCA | GFLTAEEKGLVNGLWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSSADAIMSNAKVKAHGKKVLNSFSDGLKNIDDLKGAFAKLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGHDFNPQVQAAFQKVVAGVANALAHKYH | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. | Felis catus (Cat) (Felis silvestris catus) |
P07428 | HBA_XENTR | MHLTADDKKHIKAIWPSVAAHGDKYGGEALHRMFMCAPKTKTYFPDFDFSEHSKHILAHGKKVSDALNEACNHLDNIAGCLSKLSDLHAYDLRVDPGNFPLLAHQILVVVAIHFPKQFDPATHKALDKFLVSVSNVLTSKYR | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
P07429 | HBB1_XENTR | MVNLTAKERQLITGTWSKICAKTLGKQALGSMLYTYPWTQRYFSSFGNLSSIEAIFHNAAVATHGEKVLTSIGEAIKHMDDIKGYYAQLSKYHSETLHVDPYNFKRFCSCTIISMAQTLQEDFTPELQAAFEKLFAAIADALGKGYH | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
P07432 | HBB1_XENBO | MGLTAHDRQLINSTWGKVCAKTIGKEALGRLLWTYPWTQRYFSSFGNLNSADAVFHNEAVAAHGEKVVTSIGEAIKHMDDIKGYYAQLSKYHSETLHVDPCNFKRFGGCLSISLARQFHEEYTPELHAAYEHLFDAIADALGKGYH | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. | Xenopus borealis (Kenyan clawed frog) |
P07433 | HBB2_XENBO | MGLTAHEKQLITGSWGKINAKAIGKEALGRLLNTFPWTQRYFSSFGNLGSAEAIFHNEAVAAHGEKVVTSVGEAIKHMDDIKGYYAELSKYHSETLHVDPNNFKRFGGCLSITLGHHFGEEYTPELHAAYEHLFDAIADALGKGYH | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. | Xenopus borealis (Kenyan clawed frog) |
P07437 | TBB5_HUMAN | MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQVFDAKNMMAACDPRHGRYLTVAAVFRGR... | null | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | cell division [GO:0051301]; cytoskeleton-dependent intracellular transport [GO:0030705]; microtubule cytoskeleton organization [GO:0000226]; microtubule-based process [GO:0007017]; mitotic cell cycle [GO:0000278]; natural killer cell mediated cytotoxicity [GO:0042267]; odontoblast differentiation [GO:0071895]; regulati... | azurophil granule lumen [GO:0035578]; cell body [GO:0044297]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; intercellular bridge [GO:0045171]; membrane raft [GO:0045121];... | GTP binding [GO:0005525]; GTPase activating protein binding [GO:0032794]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; MHC class I protein binding [GO:0042288]; protein domain specific binding [GO:0019904]; protein-containing complex binding [GO:0044877]; structural constituent of cytoskeleton [GO:0005... | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:26875866, PubMed:28576883). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with sh... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26637975}. | null | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Homo sapiens (Human) |
P07438 | MT1B_HUMAN | MDPNCSCTTGGSCACAGSCKCKECKCTSCKKCCCSCCPVGCAKCAQGCVCKGSSEKCRCCA | null | null | cellular response to cadmium ion [GO:0071276]; cellular response to copper ion [GO:0071280]; cellular response to zinc ion [GO:0071294]; detoxification of copper ion [GO:0010273]; intracellular zinc ion homeostasis [GO:0006882]; negative regulation of growth [GO:0045926] | 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) |
P07445 | SDIS_PSEPU | MNLPTAQEVQGLMARYIELVDVGDIEAIVQMYADDATVEDPFGQPPIHGREQIAAFYRQGLGGGKVRACLTGPVRASHNGCGAMPFRVEMVWNGQPCALDVIDVMRFDEHGRIQTMQAYWSEVNLSVREPQ | 5.3.3.1 | null | steroid metabolic process [GO:0008202] | null | steroid delta-isomerase activity [GO:0004769] | PF12680; | 3.10.450.50; | null | null | null | CATALYTIC ACTIVITY: Reaction=a 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid; Xref=Rhea:RHEA:14709, ChEBI:CHEBI:47907, ChEBI:CHEBI:47909; EC=5.3.3.1; | null | null | null | null | null | Pseudomonas putida (Arthrobacter siderocapsulatus) |
P07451 | CAH3_HUMAN | MAKEWGYASHNGPDHWHELFPNAKGENQSPVELHTKDIRHDPSLQPWSVSYDGGSAKTILNNGKTCRVVFDDTYDRSMLRGGPLPGPYRLRQFHLHWGSSDDHGSEHTVDGVKYAAELHLVHWNPKYNTFKEALKQRDGIAVIGIFLKIGHENGEFQIFLDALDKIKTKGKEAPFTKFDPSCLFPACRDYWTYQGSFTTPPCEECIVWLLLKEPMTVSSDQMAKLRSLLSSAENEPPVPLVSNWRPPQPINNRVVRASFK | 4.2.1.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16042381, ECO:0000269|PubMed:17427958}; | one-carbon metabolic process [GO:0006730]; response to bacterium [GO:0009617] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | carbonate dehydratase activity [GO:0004089]; nickel cation binding [GO:0016151]; zinc ion binding [GO:0008270] | PF00194; | 3.10.200.10; | Alpha-carbonic anhydrase family | PTM: S-thiolated both by thiol-disulfide exchange with glutathione disulfide and by oxyradical-initiated S-thiolation with reduced glutathione. {ECO:0000250|UniProtKB:P14141}.; PTM: S-glutathionylated in hepatocytes under oxidative stress. {ECO:0000250|UniProtKB:P14141}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18618712}. | CATALYTIC ACTIVITY: Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17544; EC=4.2.1.1; Evidence={ECO:0000269|PubMed:17427958, ECO:0000269|PubMed:18618712}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=52 mM for CO(2) {ECO:0000269|PubMed:18618712}; | null | null | null | FUNCTION: Reversible hydration of carbon dioxide. {ECO:0000269|PubMed:17427958, ECO:0000269|PubMed:18618712}. | Homo sapiens (Human) |
P07455 | IGF1_BOVIN | MGKISSLPTQLFKCCFCDFLKQVKMPITSSSHLFYLALCLLAFTSSATAGPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSARSVRAQRHTDMPKAQKEVHLKNTSRGSAGNKNYRM | null | null | cell population proliferation [GO:0008283]; hyperosmotic salinity response [GO:0042538]; insulin-like growth factor receptor signaling pathway [GO:0048009]; negative regulation of apoptotic process [GO:0043066]; negative regulation of P-type sodium:potassium-exchanging transporter activity [GO:1903407]; negative regula... | alphav-beta3 integrin-IGF-1-IGF1R complex [GO:0035867]; exocytic vesicle [GO:0070382]; extracellular space [GO:0005615] | growth factor activity [GO:0008083]; hormone activity [GO:0005179]; insulin-like growth factor receptor binding [GO:0005159] | PF00049; | 1.10.100.10; | Insulin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P05017}. | null | null | null | null | null | FUNCTION: The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in bon... | Bos taurus (Bovine) |
P07456 | IGF2_BOVIN | MGITAGKSVLVLLAFLAFASCCYAAYRPSETLCGGELVDTLQFVCGDRGFYFSRPSSRINRRSRGIVEECCFRSCDLALLETYCATPAKSERDVSASTTVLPDDVTAYPVGKFFQYDIWKQSTQRLRRGLPAFLRARRGRTLAKELEALREAKSHRPLIALPTQDPATHGGASSKASSD | null | null | embryonic placenta development [GO:0001892]; embryonic placenta morphogenesis [GO:0060669]; glucose metabolic process [GO:0006006]; in utero embryonic development [GO:0001701]; negative regulation of muscle cell differentiation [GO:0051148]; negative regulation of transcription by RNA polymerase II [GO:0000122]; ossifi... | extracellular space [GO:0005615] | growth factor activity [GO:0008083]; hormone activity [GO:0005179]; insulin-like growth factor receptor binding [GO:0005159]; integrin binding [GO:0005178]; protein serine/threonine kinase activator activity [GO:0043539] | PF08365;PF00049; | 1.10.100.10; | Insulin family | PTM: Proteolytically processed by PCSK4, proIGF2 is cleaved at Arg-128 and Arg-92 to generate big-IGF2 and mature IGF2. {ECO:0000250|UniProtKB:P01344}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01344, ECO:0000250|UniProtKB:P09535}. | null | null | null | null | null | FUNCTION: The insulin-like growth factors possess growth-promoting activity (By similarity). Major fetal growth hormone in mammals. Plays a key role in regulating fetoplacental development. IGF2 is influenced by placental lactogen. Also involved in tissue differentiation. In adults, involved in glucose metabolism in ad... | Bos taurus (Bovine) |
P07463 | CALM_PARTE | MAEQLTEEQIAEFKEAFALFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLSLMARKMKEQDSEEELIEAFKVFDRDGNGLISAAELRHVMTNLGEKLTDDEVDEMIREADIDGDGHINYEEFVRMMVSK | null | null | null | null | calcium ion binding [GO:0005509]; enzyme regulator activity [GO:0030234] | PF13499; | 1.10.238.10; | Calmodulin family | PTM: The pantophobiac mutant CAM2 is undermethylated on Lys-116. | null | null | null | null | null | null | FUNCTION: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. | Paramecium tetraurelia |
P07464 | THGA_ECOLI | MNMPMTERIRAGKLFTDMCEGLPEKRLRGKTLMYEFNHSHPSEVEKRESLIKEMFATVGENAWVEPPVYFSYGSNIHIGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDIPPNVVAAGVPCRVIREINDRDKHYYFKDYKVESSV | 2.3.1.18 | null | lactose biosynthetic process [GO:0005989] | cytoplasm [GO:0005737] | galactoside O-acetyltransferase activity [GO:0008870]; identical protein binding [GO:0042802] | PF00132;PF12464; | 2.160.10.10; | Transferase hexapeptide repeat family | PTM: The N-terminus of this protein is heterogeneous because the initiator methionine is only partially cleaved. {ECO:0000269|PubMed:3922433}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:3922433}. | CATALYTIC ACTIVITY: Reaction=a beta-D-galactoside + acetyl-CoA = a 6-acetyl-beta-D-galactoside + CoA; Xref=Rhea:RHEA:15713, ChEBI:CHEBI:28034, ChEBI:CHEBI:28250, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.18; Evidence={ECO:0000269|PubMed:14009486, ECO:0000269|PubMed:4630409}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.18 mM for acetyl-CoA {ECO:0000269|PubMed:4630409}; KM=0.104 mM for acetyl-CoA {ECO:0000269|PubMed:7592843}; KM=0.77 M for isopropyl beta-D-1-thiogalactopyranoside {ECO:0000269|PubMed:4630409}; KM=63.4 mM for p-nitrophenyl-b-D-galactopyranoside {ECO:0000269|PubMed... | null | null | null | FUNCTION: Catalyzes the CoA-dependent transfer of an acetyl group to the 6-O-methyl position of a range of galactosides, glucosides, and lactosides (PubMed:14009486, PubMed:4630409, PubMed:7592843). May assist cellular detoxification by acetylating non-metabolizable pyranosides, thereby preventing their reentry into th... | Escherichia coli (strain K12) |
P07470 | CX7A1_BOVIN | MRALRVSQALVRSFSSTARNRFENRVAEKQKLFQEDNGLPVHLKGGATDNILYRVTMTLCLGGTLYSLYCLGWASFPHKK | null | null | mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mitochondrial respirasome assembly [GO:0097250]; regulation of oxidative phosphorylation [GO:0002082] | mitochondrial respirasome [GO:0005746]; mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739]; respiratory chain complex IV [GO:0045277] | oxidoreductase activity [GO:0016491] | PF02238; | 4.10.91.10; | Cytochrome c oxidase VIIa family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}; Single-pass membrane protein {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}. | null | null | PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000250|UniProtKB:P10174}. | null | null | FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... | Bos taurus (Bovine) |
P07471 | CX6A2_BOVIN | MALPLKSLSRGLASAAKGDHGGTGARTWRFLTFGLALPSVALCTLNSWLHSGHRERPAFIPYHHLRIRTKPFSWGDGNHTFFHNPRVNPLPTGYEKP | null | null | mitochondrial electron transport, cytochrome c to oxygen [GO:0006123] | mitochondrial respiratory chain complex IV [GO:0005751]; respiratory chain complex IV [GO:0045277] | enzyme regulator activity [GO:0030234]; oxidoreductase activity [GO:0016491] | PF02046; | 4.10.95.10; | Cytochrome c oxidase subunit 6A family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}; Single-pass membrane protein {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}. | null | null | PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000250|UniProtKB:P32799}. | null | null | FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... | Bos taurus (Bovine) |
P07476 | INVO_HUMAN | MSQQHTLPVTLSPALSQELLKTVPPPVNTHQEQMKQPTPLPPPCQKVPVELPVEVPSKQEEKHMTAVKGLPEQECEQQQKEPQEQELQQQHWEQHEEYQKAENPEQQLKQEKTQRDQQLNKQLEEEKKLLDQQLDQELVKRDEQLGMKKEQLLELPEQQEGHLKHLEQQEGQLKHPEQQEGQLELPEQQEGQLELPEQQEGQLELPEQQEGQLELPEQQEGQLELPEQQEGQLELPQQQEGQLELSEQQEGQLELSEQQEGQLKHLEHQEGQLEVPEEQMGQLKYLEQQEGQLKHLDQQEKQPELPEQQMGQLKHLEQQE... | null | null | isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine [GO:0018153]; keratinization [GO:0031424]; keratinocyte differentiation [GO:0030216]; peptide cross-linking [GO:0018149]; response to UV-B [GO:0010224] | centrosome [GO:0005813]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nuclear body [GO:0016604] | null | PF00904;PF10583; | null | Involucrin family | PTM: Substrate of transglutaminase. Some glutamines and lysines are cross-linked to other involucrin molecules, to other proteins such as keratin, desmoplakin, periplakin and envoplakin, and to lipids like omega-hydroxyceramide. | SUBCELLULAR LOCATION: Cytoplasm. Note=Constituent of the scaffolding of the cornified envelope. | null | null | null | null | null | FUNCTION: Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia. | Homo sapiens (Human) |
P07477 | TRY1_HUMAN | MNPLLILTFVAAALAAPFDDDDKIVGGYNCEENSVPYQVSLNSGYHFCGGSLINEQWVVSAGHCYKSRIQVRLGEHNIEVLEGNEQFINAAKIIRHPQYDRKTLNNDIMLIKLSSRAVINARVSTISLPTAPPATGTKCLISGWGNTASSGADYPDELQCLDAPVLSQAKCEASYPGKITSNMFCVGFLEGGKDSCQGDSGGPVVCNGQLQGVVSWGDGCAQKNKPGVYTKVYNYVKWIKNTIAANS | 3.4.21.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 1 Ca(2+) ion per subunit.; | digestion [GO:0007586]; extracellular matrix disassembly [GO:0022617]; proteolysis [GO:0006508] | blood microparticle [GO:0072562]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.40.10.10; | Peptidase S1 family | PTM: Occurs in a single-chain form and a two-chain form, produced by proteolytic cleavage after Arg-122.; PTM: Sulfation at Tyr-154 increases selectivity towards basic versus apolar residues at the P2' position of inhibitors that bind in a substrate-like fashion. Although the increase in selectivity is relatively small... | SUBCELLULAR LOCATION: Secreted, extracellular space. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4; | null | null | null | null | FUNCTION: Has activity against the synthetic substrates Boc-Phe-Ser-Arg-Mec, Boc-Leu-Thr-Arg-Mec, Boc-Gln-Ala-Arg-Mec and Boc-Val-Pro-Arg-Mec. The single-chain form is more active than the two-chain form against all of these substrates. {ECO:0000269|PubMed:7945238}. | Homo sapiens (Human) |
P07478 | TRY2_HUMAN | MNLLLILTFVAAAVAAPFDDDDKIVGGYICEENSVPYQVSLNSGYHFCGGSLISEQWVVSAGHCYKSRIQVRLGEHNIEVLEGNEQFINAAKIIRHPKYNSRTLDNDILLIKLSSPAVINSRVSAISLPTAPPAAGTESLISGWGNTLSSGADYPDELQCLDAPVLSQAECEASYPGKITNNMFCVGFLEGGKDSCQGDSGGPVVSNGELQGIVSWGYGCAQKNRPGVYTKVYNYVDWIKDTIAANS | 3.4.21.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250}; | antimicrobial humoral response [GO:0019730]; collagen catabolic process [GO:0030574]; digestion [GO:0007586]; extracellular matrix disassembly [GO:0022617]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell growth [GO:0030307]; proteolysis [GO:0006508] | azurophil granule lumen [GO:0035578]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; metalloendopeptidase activity [GO:0004222]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236] | PF00089; | 2.40.10.10; | Peptidase S1 family | PTM: Sulfated on tyrosine. {ECO:0000269|PubMed:17087724}.; PTM: Sulfation at Tyr-154 increases selectivity towards basic versus apolar residues at the P2' position of inhibitors that bind in a substrate-like fashion. Although the increase in selectivity is relatively small, it may facilitate digestion of a broader rang... | SUBCELLULAR LOCATION: Secreted, extracellular space. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4; | null | null | null | null | FUNCTION: In the ileum, may be involved in defensin processing, including DEFA5. {ECO:0000269|PubMed:12021776}. | Homo sapiens (Human) |
P07483 | FABPH_RAT | MADAFVGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDTITIKTHSTFKNTEISFQLGVEFDEVTADDRKVKSVVTLDGGKLVHVQKWDGQETTLTRELSDGKLILTLTHGNVVSTRTYEKEA | null | null | brown fat cell differentiation [GO:0050873]; cholesterol homeostasis [GO:0042632]; fatty acid beta-oxidation [GO:0006635]; fatty acid metabolic process [GO:0006631]; intracellular lipid transport [GO:0032365]; long-chain fatty acid transport [GO:0015909]; phospholipid homeostasis [GO:0055091]; positive regulation of lo... | cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleus [GO:0005634]; sarcoplasm [GO:0016528] | cytoskeletal protein binding [GO:0008092]; fatty acid binding [GO:0005504]; icosatetraenoic acid binding [GO:0050543]; long-chain fatty acid binding [GO:0036041]; long-chain fatty acid transporter activity [GO:0005324]; oleic acid binding [GO:0070538] | PF00061; | 2.40.128.20; | Calycin superfamily, Fatty-acid binding protein (FABP) family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: FABPs are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. | Rattus norvegicus (Rat) |
P07486 | G3P1_DROME | MSKIGINGFGRIGRLVLRAAIDKGASVVAVNDPFIDVNYMVYLFKFDSTHGRFKGTVAAEGGFLVVNGQKITVFSERDPANINWASAGAEYVVESTGVFTTIDKASTHLKGGAKKVIISAPSADAPMFVCGVNLDAYSPDMKVVSNASCTTNCLAPLAKVINDNFEIVEGLMTTVHATTATQKTVDGPSGKLWRDGRGAAQNIIPAATGAAKAVGKVIPALNGKLTGMAFRVPTPNVSVVDLTVRLGKGATYDEIKAKVEEASKGPLKGILGYTDEEVVSTDFFSDTHSSVFDAKAGISLNDKFVKLISWYDNEFGYSNR... | 1.2.1.12 | null | canonical glycolysis [GO:0061621]; gluconeogenesis [GO:0006094]; glyceraldehyde-3-phosphate metabolic process [GO:0019682]; glycolytic process [GO:0006096] | cytosol [GO:0005829]; M band [GO:0031430]; Z disc [GO:0030018] | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; peptidyl-cysteine S-nitrosylase activity [GO:0035605] | PF02800;PF00044; | 3.40.50.720; | Glyceraldehyde-3-phosphate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000255|PROSITE-ProRule:PR... | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. | null | null | null | Drosophila melanogaster (Fruit fly) |
P07487 | G3P2_DROME | MSKIGINGFGRIGRLVLRAAIDKGANVVAVNDPFIDVNYMVYLFKFDSTHGRFKGTVAAEGGFLVVNGQKITVFSERDPANINWASAGAEYIVESTGVFTTIDKASTHLKGGAKKVIISAPSADAPMFVCGVNLDAYKPDMKVVSNASCTTNCLAPLAKVINDNFEIVEGLMTTVHATTATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNVSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFDAKAGISLNDKFVKLISWYDNEFGYSNR... | 1.2.1.12 | null | canonical glycolysis [GO:0061621]; gluconeogenesis [GO:0006094]; glucose homeostasis [GO:0042593]; glyceraldehyde-3-phosphate metabolic process [GO:0019682]; glycolytic process [GO:0006096] | cytosol [GO:0005829] | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity [GO:0004365]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; peptidyl-cysteine S-nitrosylase activity [GO:0035605] | PF02800;PF00044; | 3.40.50.720; | Glyceraldehyde-3-phosphate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000255|PROSITE-ProRule:PR... | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5. | null | null | null | Drosophila melanogaster (Fruit fly) |
P07490 | GON1_RAT | METIPKLMAAVVLLTVCLEGCSSQHWSYGLRPGGKRNTEHLVDSFQEMGKEEDQMAEPQNFECTVHWPRSPLRDLRGALERLIEEEAGQKKM | null | null | estrous cycle [GO:0044849]; female pregnancy [GO:0007565]; 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]; ovulation cycle [GO:0042698]; regulation of gene... | 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. | null | null | null | null | null | FUNCTION: Stimulates the secretion of gonadotropins; it stimulates the secretion of both luteinizing and follicle-stimulating hormones. | Rattus norvegicus (Rat) |
P07492 | GRP_HUMAN | MRGRELPLVLLALVLCLAPRGRAVPLPAGGGTVLTKMYPRGNHWAVGHLMGKKSTGESSSVSERGSLKQQLREYIRWEEAARNLLGLIEAKENRNHQPPQPKALGNQQPSWDSEDSSNFKDVGSKGKVGRLSAPGSQREGRNPQLNQQ | null | null | cellular response to sodium phosphate [GO:1904384]; mast cell degranulation [GO:0043303]; negative regulation of voltage-gated potassium channel activity [GO:1903817]; negative regulation of voltage-gated sodium channel activity [GO:1905151]; neuropeptide signaling pathway [GO:0007218]; ossification [GO:0001503]; posit... | extracellular region [GO:0005576]; extracellular space [GO:0005615]; neuron projection [GO:0043005]; neuronal dense core vesicle [GO:0098992]; secretory granule lumen [GO:0034774] | neuropeptide hormone activity [GO:0005184]; signaling receptor binding [GO:0005102] | PF02044; | null | Bombesin/neuromedin-B/ranatensin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3211139}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000250|UniProtKB:Q863C3}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q8R1I2}. Note=In neurons of the retrotrapezoid nucleus/parafacial respiratory group, expressed on neuron projections which p... | null | null | null | null | null | FUNCTION: Stimulates the release of gastrin and other gastrointestinal hormones (By similarity). Contributes to the perception of prurient stimuli and to the transmission of itch signals in the spinal cord that promote scratching behavior (By similarity). Contributes primarily to nonhistaminergic itch sensation (By sim... | Homo sapiens (Human) |
P07498 | CASK_HUMAN | MKSFLLVVNALALTLPFLAVEVQNQKQPACHENDERPFYQKTAPYVPMYYVPNSYPYYGTNLYQRRPAIAINNPYVPRTYYANPAVVRPHAQIPQRQYLPNSHPPTVVRRPNLHPSFIAIPPKKIQDKIIIPTINTIATVEPTPAPATEPTVDSVVTPEAFSESIITSTPETTTVAVTPPTA | null | null | lactation [GO:0007595]; protein stabilization [GO:0050821] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | null | PF00997; | null | Kappa-casein family | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk. | Homo sapiens (Human) |
P07499 | ANF_CANLF | MGSPIAASFLLFLAVQLLGQTGANPVYGSVSNADLLDFKNLLDRLEDKMPLEDEAESPQALSEQNAEAGAALSPLPEVPPWTGEVSPAQRDGGALGRSPWDSSDRSALLKSKLRALLAAPRSLRRSSCFGGRMDRIGAQSGLGCNSFRY | null | null | cGMP biosynthetic process [GO:0006182]; cGMP-mediated signaling [GO:0019934]; female pregnancy [GO:0007565]; negative regulation of systemic arterial blood pressure [GO:0003085]; neuropeptide signaling pathway [GO:0007218]; receptor guanylyl cyclase signaling pathway [GO:0007168]; regulation of blood pressure [GO:00082... | cell projection [GO:0042995]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; perikaryon [GO:0043204] | hormone activity [GO:0005179]; hormone receptor binding [GO:0051427] | PF00212; | null | Natriuretic peptide family | PTM: The precursor molecule is proteolytically cleaved by CORIN at Arg-121 to produce the atrial natriuretic peptide (By similarity). Undergoes further proteolytic cleavage by unknown proteases to give rise to long-acting natriuretic peptide, vessel dilator and kaliuretic peptide (By similarity). Additional processing ... | SUBCELLULAR LOCATION: [Long-acting natriuretic peptide]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Vessel dilator]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Kali... | null | null | null | null | null | FUNCTION: [Atrial natriuretic peptide]: Hormone that plays a key role in mediating cardio-renal homeostasis, and is involved in vascular remodeling and regulating energy metabolism (By similarity). Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn activates effector proteins, such as PRKG... | Canis lupus familiaris (Dog) (Canis familiaris) |
P07500 | ANF_RABIT | MGPFSTITVSFLFCLAFWHPDQIGANPVYNAMSNADLMDFKNLLDHLEDRMPFEDEAVPPQALSEQSDEAGAALSPLPEVPPWTGEVSPAQRDGEALGRSTWEASERSALLKSKLRALLTAPRSLRRSSCFGGRIDRIGAQSGLGCNSFRYRR | null | null | cGMP biosynthetic process [GO:0006182]; cGMP-mediated signaling [GO:0019934]; female pregnancy [GO:0007565]; negative regulation of systemic arterial blood pressure [GO:0003085]; neuropeptide signaling pathway [GO:0007218]; receptor guanylyl cyclase signaling pathway [GO:0007168]; regulation of blood pressure [GO:00082... | cell projection [GO:0042995]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; perikaryon [GO:0043204] | hormone activity [GO:0005179]; hormone receptor binding [GO:0051427] | PF00212; | null | Natriuretic peptide family | PTM: The precursor molecule is proteolytically cleaved by CORIN at Arg-123 to produce the atrial natriuretic peptide (By similarity). Undergoes further proteolytic cleavage by unknown proteases to give rise to long-acting natriuretic peptide, vessel dilator and kaliuretic peptide (By similarity). Additional processing ... | SUBCELLULAR LOCATION: [Long-acting natriuretic peptide]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Vessel dilator]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Kali... | null | null | null | null | null | FUNCTION: [Atrial natriuretic peptide]: Hormone that plays a key role in mediating cardio-renal homeostasis, and is involved in vascular remodeling and regulating energy metabolism (By similarity). Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn activates effector proteins, such as PRKG... | Oryctolagus cuniculus (Rabbit) |
P07501 | ANF_BOVIN | MGSSAITVSFLLFLAFQLPGQTGANPVYGSVSNADLMDFKNLLDRLEDKMPLEDEAVPSQVLSEQNEEAGAPLSPLSEMPPWMGEVNPAQREGGVLGRGPWESSDRSALLKSKLRALLTAPRSLRRSSCFGGRMDRIGAQSGLGCNSFRYRR | null | null | cGMP biosynthetic process [GO:0006182]; cGMP-mediated signaling [GO:0019934]; female pregnancy [GO:0007565]; negative regulation of systemic arterial blood pressure [GO:0003085]; neuropeptide signaling pathway [GO:0007218]; receptor guanylyl cyclase signaling pathway [GO:0007168]; regulation of blood pressure [GO:00082... | cell projection [GO:0042995]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; perikaryon [GO:0043204] | hormone activity [GO:0005179]; hormone receptor binding [GO:0051427] | PF00212; | null | Natriuretic peptide family | PTM: The precursor molecule is proteolytically cleaved by CORIN at Arg-122 to produce the atrial natriuretic peptide (By similarity). Undergoes further proteolytic cleavage by unknown proteases to give rise to long-acting natriuretic peptide, vessel dilator and kaliuretic peptide (By similarity). Additional processing ... | SUBCELLULAR LOCATION: [Long-acting natriuretic peptide]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Vessel dilator]: Secreted {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. {ECO:0000250|UniProtKB:P01160}.; SUBCELLULAR LOCATION: [Kali... | null | null | null | null | null | FUNCTION: [Atrial natriuretic peptide]: Hormone that plays a key role in mediating cardio-renal homeostasis, and is involved in vascular remodeling and regulating energy metabolism (By similarity). Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn activates effector proteins, such as PRKG... | Bos taurus (Bovine) |
P07505 | SODCP_SPIOL | MAAHTILASAPSHTTFSLISPFSSTPTNALSSSLQSSSFNGLSFKLSPTTQSLSLSTSAASKPLTIVAATKKAVAVLKGTSNVEGVVTLTQEDDGPTTVNVRISGLAPGKHGFHLHEFGDTTNGCMSTGPHFNPDKKTHGAPEDEVRHAGDLGNIVANTDGVAEATIVDNQIPLTGPNSVVGRALVVHELEDDLGKGGHELSPTTGNAGGRLACGVVGLTPV | 1.15.1.1 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000269|PubMed:1880134}; Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:1880134}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:1880134}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:1880134}; | null | chloroplast [GO:0009507]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; peroxisome [GO:0005777] | copper ion binding [GO:0005507]; superoxide dismutase activity [GO:0004784] | PF00080; | 2.60.40.200; | Cu-Zn superoxide dismutase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast. | CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; | null | null | null | null | FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. | Spinacia oleracea (Spinach) |
P07507 | MGP_BOVIN | MKSLLLLSILAALAVAALCYESHESLESYEINPFINRRNANSFISPQQRWRAKAQERIRELNKPQYELNREACDDFKLCERYAMVYGYNAAYDRYFRQRRGAK | null | null | cartilage development [GO:0051216]; cell differentiation [GO:0030154]; ossification [GO:0001503]; regulation of bone mineralization [GO:0030500] | collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576] | calcium ion binding [GO:0005509] | null | null | Osteocalcin/matrix Gla protein family | PTM: Requires vitamin K-dependent gamma-carboxylation for its function. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Associates with the organic matrix of bone and cartilage. Thought to act as an inhibitor of bone formation. | Bos taurus (Bovine) |
P07510 | ACHG_HUMAN | MHGGQGPLLLLLLLAVCLGAQGRNQEERLLADLMQNYDPNLRPAERDSDVVNVSLKLTLTNLISLNEREEALTTNVWIEMQWCDYRLRWDPRDYEGLWVLRVPSTMVWRPDIVLENNVDGVFEVALYCNVLVSPDGCIYWLPPAIFRSACSISVTYFPFDWQNCSLIFQSQTYSTNEIDLQLSQEDGQTIEWIFIDPEAFTENGEWAIQHRPAKMLLDPAAPAQEAGHQKVVFYLLIQRKPLFYVINIIAPCVLISSVAILIHFLPAKAGGQKCTVAINVLLAQTVFLFLVAKKVPETSQAVPLISKYLTFLLVVTILIV... | null | null | acetylcholine receptor signaling pathway [GO:0095500]; membrane depolarization [GO:0051899]; muscle contraction [GO:0006936]; signal transduction [GO:0007165] | acetylcholine-gated channel complex [GO:0005892]; 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]; channel activity [GO:0015267]; 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:0000250|UniProtKB:P13536}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P13536}; | 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. | Homo sapiens (Human) |
P07511 | GLYC_RABIT | MATAVNGAPRDAALWSSHEQMLAQPLKDSDAEVYDIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEHIDELETLCQKRALQAYGLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFFESMAYKVNPDTGYIDYDRLEENARLFHPKLIIAGTSCYSRNLDYGRLRKIADENGAYLMADMAHISGLVVAGVVPSPFEHCHVVTTTTHKTLRGCRAGMIFYRRGVRSVDPKTGKEILYNLESLINSAVFPGLQGGPHNHAIAGVAVALKQAM... | 2.1.2.1 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:10387080}; | cellular response to leukemia inhibitory factor [GO:1990830]; cellular response to tetrahydrofolate [GO:1904482]; folic acid metabolic process [GO:0046655]; glycine biosynthetic process from serine [GO:0019264]; glycine metabolic process [GO:0006544]; L-serine catabolic process [GO:0006565]; L-serine metabolic process ... | cytosol [GO:0005829]; nucleoplasm [GO:0005654] | cobalt ion binding [GO:0050897]; glycine hydroxymethyltransferase activity [GO:0004372]; mRNA 5'-UTR binding [GO:0048027]; mRNA regulatory element binding translation repressor activity [GO:0000900]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170]; serine binding [GO:0070905]; z... | PF00464; | 3.90.1150.10;3.40.640.10; | SHMT family | PTM: Deamidation of asparagine produces alternatively aspartate or isoaspartate, which in turn can be converted to aspartate through carboxylmethylation/demethylation. {ECO:0000269|PubMed:2318867}. | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384, ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1; Evidence={ECO:0000269|PubMed:1381582}; | null | PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. {ECO:0000305}. | null | null | FUNCTION: Interconversion of serine and glycine. {ECO:0000269|PubMed:1381582}. | Oryctolagus cuniculus (Rabbit) |
P07514 | NB5R3_BOVIN | MGAQLSTLGHVVLSPVWFLYSLIMKLFQRSTPAITLENPDIKYPLRLIDKEVISHDTRRFRFALPSPEHILGLPVGQHIYLSARIDGNLVIRPYTPVSSDDDKGFVDLVIKVYFKDTHPKFPAGGKMSQYLESMKIGDTIEFRGPNGLLVYQGKGKFAIRPDKKSDPVIKTVKSVGMIAGGTGITPMLQVIRAIMKDPDDHTVCHLLFANQTEKDILLRPELEELRNEHSARFKLWYTVDKAPEAWDYSQGFVNEEMIRDHLPPPEEEPLVLMCGPPPMIQYACLPNLDRVGHPKERCFAF | 1.6.2.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P00387}; | cholesterol biosynthetic process [GO:0006695] | endoplasmic reticulum membrane [GO:0005789]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739] | cytochrome-b5 reductase activity, acting on NAD(P)H [GO:0004128]; FAD binding [GO:0071949] | PF00970;PF00175; | 3.40.50.80;2.40.30.10; | Flavoprotein pyridine nucleotide cytochrome reductase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P20070}; Lipid-anchor {ECO:0000250|UniProtKB:P20070}; Cytoplasmic side {ECO:0000250|UniProtKB:P20070}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P20070}; Lipid-anchor {ECO:0000250|UniProtKB:P20070}; Cytoplasmic side {ECO:0000250|UniPr... | CATALYTIC ACTIVITY: Reaction=2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] + H(+) + NAD(+); Xref=Rhea:RHEA:46680, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.2.2; Evidence={ECO:0000269|PubMed:1370824}; Ph... | null | null | null | null | FUNCTION: Catalyzes the reduction of two molecules of cytochrome b5 using NADH as the electron donor. {ECO:0000269|PubMed:1370824}. | Bos taurus (Bovine) |
P07516 | PPR1B_BOVIN | MDPKDRKKIQFSVPAPPSQLDPRQVEMIRRRRPTPAMLFRLSEHSSPEEEASPHQRASGEGHHLKSKRSNPCAYTPPSLKAVQRIAESHLQSISNLGENQASEEEDELGELRELGYPREEEEEEEEEDEEEEEDSQAEVLKGSRGSAGQKTTYGQGLEGPWERPPPLDGPQRDGSSEDQVEDPALNEPGEEPQRPAHPEPGT | null | null | behavioral response to cocaine [GO:0048148]; cellular response to cocaine [GO:0071314]; DNA-templated transcription [GO:0006351]; intracellular signal transduction [GO:0035556]; locomotory behavior [GO:0007626]; negative regulation of female receptivity [GO:0007621]; response to amphetamine [GO:0001975]; response to mo... | axon cytoplasm [GO:1904115]; cytoplasm [GO:0005737]; dendrite cytoplasm [GO:0032839]; neuronal cell body [GO:0043025]; nucleus [GO:0005634] | molecular function inhibitor activity [GO:0140678]; protein phosphatase inhibitor activity [GO:0004864] | PF05395; | null | Protein phosphatase inhibitor 1 family | PTM: Dopamine- and cyclic AMP-regulated neuronal phosphoprotein.; PTM: Phosphorylation of Thr-34 is required for activity. {ECO:0000269|PubMed:3511054}. | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Inhibitor of protein-phosphatase 1. | Bos taurus (Bovine) |
P07519 | CBP1_HORVU | MARCRRRSGCTAGAALLLLLALALSGGGGAAPQGAEVTGLPGFDGALPSKHYAGYVTVDEGHGRNLFYYVVESERDPGKDPVVLWLNGGPGCSSFDGFVYEHGPFNFESGGSVKSLPKLHLNPYAWSKVSTMIYLDSPAGVGLSYSKNVSDYETGDLKTATDSHTFLLKWFQLYPEFLSNPFYIAGESYAGVYVPTLSHEVVKGIQGGAKPTINFKGYMVGNGVCDTIFDGNALVPFAHGMGLISDEIYQQASTSCHGNYWNATDGKCDTAISKIESLISGLNIYDILEPCYHSRSIKEVNLQNSKLPQSFKDLGTTNKP... | 3.4.16.5 | null | proteolysis [GO:0006508]; secondary metabolic process [GO:0019748] | extracellular region [GO:0005576] | acyltransferase activity, transferring groups other than amino-acyl groups [GO:0016747]; serine-type carboxypeptidase activity [GO:0004185] | PF00450; | 3.40.50.12670;3.40.50.1820; | Peptidase S10 family | PTM: The linker peptide is endoproteolytically excised during enzyme maturation. | SUBCELLULAR LOCATION: Secreted. Note=Secreted into the endosperm. | CATALYTIC ACTIVITY: Reaction=Release of a C-terminal amino acid with broad specificity.; EC=3.4.16.5; Evidence={ECO:0000255|PROSITE-ProRule:PRU10074, ECO:0000255|PROSITE-ProRule:PRU10075}; | null | null | null | null | FUNCTION: May be involved in the degradation of small peptides (2-5 residues) or in the degradation of storage proteins in the embryo. | Hordeum vulgare (Barley) |
P07522 | EGF_RAT | MLFSLTFLSVFLKITVLSVTAQQTRNCQSGPLERSGTTTYAAAGPPRFLIFLQGNSIFRINTDGTNHQQLVVDAGVSVVMDFHYKEERLYWVDLERQLLQRVFFNGSGQETVCKVDKNVSGLAINWIDGEILRTDRWKGVITVTDMNGNNSRVLLSSLKRPANILVDPTERLIFWSSVVTGNLHRADLGGMDVKTLLEAPERISVLILDILDKRLFWAQDGREGSHGYIHSCDYNGGSIHHIRHQARHDLLTMAIFGDKILYSALKEKAIWIADKHTGKNVVRVNLDPASVPPRELRVVHLHAQPGTENRAQASDSERCK... | null | null | angiogenesis [GO:0001525]; branching morphogenesis of an epithelial tube [GO:0048754]; canonical Wnt signaling pathway [GO:0060070]; cell population proliferation [GO:0008283]; cerebellar granule cell precursor proliferation [GO:0021930]; epidermal growth factor receptor signaling pathway [GO:0007173]; epithelial cell ... | extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; epidermal growth factor receptor binding [GO:0005154]; growth factor activity [GO:0008083]; guanyl-nucleotide exchange factor activity [GO:0005085]; receptor ligand activity [GO:0048018]; transmembrane receptor protein tyrosine kinase activator activity [GO:0030297]; Wnt receptor activ... | PF00008;PF07645;PF14670;PF00058; | 2.10.25.10;2.120.10.30; | null | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6 (By simil... | Rattus norvegicus (Rat) |
P07527 | WEE1_SCHPO | MSSSSNTSSHRSYGLRRSQRSMNLNRATLLAPPTPSSLYDANNSTSSTSSQKPNTSFTSLFGPRKQTTSSPSFSHAAPLHPLSPPSFTHSQPQIQAQPVPRRPSLFDRPNLVSRSSSRLGDSPSLSPVAQVANPIHHTAPSPSDVRAFPIHKNASTGVKRSFFSSSMSNGAMSPPSHSPSPFLQSSQHIPPSTPAQKLRKKNNFDSFRISNSHISPFASGSFSPFATSSPNFLSTSTPAPPNSNNANPSTLFSSIPSSRHTTSNHFPSNSAQSSLFSPTARPLTARKLGFASSQTKSAVSNNHSRNSSKDASFMMKSFIP... | 2.7.10.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250}; | cell division [GO:0051301]; mitotic cytokinesis checkpoint signaling [GO:0044878]; mitotic DNA damage checkpoint signaling [GO:0044773]; mitotic G2 cell size control checkpoint signaling [GO:0031569]; negative regulation of G2/M transition of mitotic cell cycle [GO:0010972]; negative regulation of G2/MI transition of m... | Cdr2 medial cortical node complex [GO:0110115]; cytoplasm [GO:0005737]; medial cortical node [GO:0071341]; mitotic spindle pole body [GO:0044732]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; microtubule binding [GO:0008017]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, WEE1 subfamily | PTM: Phosphorylated in the C-terminal by NIM1/CDR1. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889}. | 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: Protein kinase that acts both on serines and on tyrosines. It acts as a dosage-dependent negative regulator of entry into mitosis (G2 to M transition). Phosphorylates and inhibits cdc2. {ECO:0000269|PubMed:1825699}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P07547 | ARO1_EMENI | MSNPTKISILGRESIIADFGLWRNYVAKDLISDCSSTTYVLVTDTNIGSIYTPSFEEAFRKAAAEITPSPRLLIYNAPPGEVSKSRQTKADIEDWMLSQNPPCGRDTVVIALGGGVIGDLTGFVASTYMRGVRYVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPTKIYIDLEFLETLPVREFINGMAEVIKTAAISSEEEFTALEENAETILKAVRREVRPGEHRFEGIEEILKARILASARHKAYVVSADEREGGLRNLLNWGHSIGHAIEAILTPQILHGECVAIGMVKEAELARHLGILKGVAVSRIVKCL... | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:000476... | PF01761;PF01487;PF00275;PF18317;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xr... | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
P07548 | DFD_DROME | MSSFLMGYPHAPHHVQSPMSMGNGLDPKFPPLADDYHHYNGHYSMTASTGHMSGAVGGGAGVGSVGGGGAGGMTGHPHSMHPADMVSDYMAHHHNPHSHSHSHTHSLPHHHSNSAISGHHQASAGGYSSNYANATPPSHPHSHPHAHPHQSLGYYVHHAPEFISAGAVHSDPTNGYGPAANVPNTSNGGGGGGSGAVLGGGAVGGSANGYYGGYGGGYGTANGSVGSTHSQGHSPHSQMMDLPLQCSSTEPPTNTALGLQELGLKLEKRIEEAVPAGQQLQELGMRLRCDDMGSENDDMSEEDRLMLDRSPDELGSNDND... | null | null | anterior/posterior pattern specification [GO:0009952]; embryonic brain development [GO:1990403]; head development [GO:0060322]; head morphogenesis [GO:0060323]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of apoptotic process involved in morphogenesis [GO:1902339]; positi... | neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; molecular adaptor activity [GO:0060090]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcriptio... | PF00046; | 1.10.10.60; | Antp homeobox family, Deformed subfamily | 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. Homeotic protein controlling Drosophila head development. Transcriptional activator of the apoptotic activator protein rpr in cells ... | Drosophila melanogaster (Fruit fly) |
P07550 | ADRB2_HUMAN | MGQPGNGSAFLLAPNGSHAPDHDVTQERDEVWVVGMGIVMSLIVLAIVFGNVLVITAIAKFERLQTVTNYFITSLACADLVMGLAVVPFGAAHILMKMWTFGNFWCEFWTSIDVLCVTASIETLCVIAVDRYFAITSPFKYQSLLTKNKARVIILMVWIVSGLTSFLPIQMHWYRATHQEAINCYANETCCDFFTNQAYAIASSIVSFYVPLVIMVFVYSRVFQEAKRQLQKIDKSEGRFHVQNLSQVEQDGRTGHGLRRSSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNIVHVIQDNLIRKEVYILLNWIGYVNSG... | null | null | activation of adenylate cyclase activity [GO:0007190]; activation of transmembrane receptor protein tyrosine kinase activity [GO:0007171]; adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; adrenergic r... | apical plasma membrane [GO:0016324]; clathrin-coated endocytic vesicle membrane [GO:0030669]; early endosome [GO:0005769]; endosome [GO:0005768]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; lysosome [GO:0005764]; membrane [GO:0016020]; neuronal dense core vesicle [GO:0098992]; nucleus [GO:0005634]; pl... | adenylate cyclase binding [GO:0008179]; amyloid-beta binding [GO:0001540]; beta2-adrenergic receptor activity [GO:0004941]; identical protein binding [GO:0042802]; norepinephrine binding [GO:0051380]; potassium channel regulator activity [GO:0015459]; protein homodimerization activity [GO:0042803]; protein-containing c... | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Adrenergic receptor subfamily, ADRB2 sub-subfamily | PTM: Palmitoylated (PubMed:11146000, PubMed:17962520, PubMed:18547522, PubMed:2540197, PubMed:27481942). Mainly palmitoylated at Cys-341 (PubMed:17962520, PubMed:18547522, PubMed:2540197). Palmitoylation may reduce accessibility of phosphorylation sites by anchoring the receptor to the plasma membrane. Agonist stimulat... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19584355, ECO:0000269|PubMed:20559325, ECO:0000269|PubMed:23166351, ECO:0000269|PubMed:25220262, ECO:0000269|PubMed:2831218, ECO:0000269|PubMed:7915137}; Multi-pass membrane protein {ECO:0000269|PubMed:19584355}. Early endosome {ECO:0000269|PubMed:20559325}. Golgi... | null | null | null | null | null | FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine. {ECO:0000269|PubMed:2831218, ECO:0000269|PubMed:7915137}. | Homo sapiens (Human) |
P07560 | SEC4_YEAST | MSGLRTVSASSGNGKSYDSIMKILLIGDSGVGKSCLLVRFVEDKFNPSFITTIGIDFKIKTVDINGKKVKLQLWDTAGQERFRTITTAYYRGAMGIILVYDVTDERTFTNIKQWFKTVNEHANDEAQLLLVGNKSDMETRVVTADQGEALAKELGIPFIESSAKNDDNVNEIFFTLAKLIQEKIDSNKLVGVGNGKEGNISINSGSGNSSKSNCC | null | null | ascospore-type prospore assembly [GO:0031321]; autophagy [GO:0006914]; endocytic recycling [GO:0032456]; exocytosis [GO:0006887]; Golgi to plasma membrane transport [GO:0006893]; Golgi vesicle fusion to target membrane [GO:0048210]; membrane addition at site of cytokinesis [GO:0007107]; protein localization to plasma m... | cellular bud neck [GO:0005935]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; incipient cellular bud site [GO:0000131]; mating projection tip [GO:0043332]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]; trans-Golgi network transport vesicle [GO:0030140]... | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane; Lipid-anchor; Cytoplasmic side. Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm. Note=A small fraction is soluble. | null | null | null | null | null | FUNCTION: Involved in exocytosis. Maybe by regulating the binding and fusion of secretory vesicles with the cell surface. The GTP-bound form of SEC4 may interact with an effector, thereby stimulating its activity and leading to exocytotic fusion. SEC4 may be an upstream activator of the 19.5S SEC8/SEC15 particle. SEC4 ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07564 | POLG_DEN2J | MNNQRKKARSTPFNMLKRERNRVSTVQQLTKRFSLGMLQGRGPLKLFMALVAFLRFLTIPPTAGILKRWGTIKKSKAINVLRGFRKEIGRMLNILNRRRRTAGVIIMLIPTAMAFHLTTRNGEPHMIVGRQEKGKSLLFKTEDGVNMCTLMAIDLGELCEDTITYKCPLLRQNEPEDIDCWCNSTSTWVTYGTCATTGEHRREKRSVALVPHVGMGLETRTETWMSSEGAWKHVQRIETWILRHPGFTIMAAILAYTIGTTHFQRALIFILLTAVAPSMTMRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPT... | 2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont-mediated suppression of host cytoplasmic pattern recog... | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell mitochondrion [GO:0033650]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:00550... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; prot... | PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949; | 1.10.10.930;1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;2.40.10.10;3.40.50.150;3.30.67.10;3.30.387.10; | Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-m... | SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763... | CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:... | null | null | null | null | FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migr... | Dengue virus type 2 (strain Jamaica/1409/1983) (DENV-2) |
P07566 | POLS_RUBVT | MASTTPITMEDLQKALEAQSRALRAELAAGASQSRRPRPPRQRDSSTSGDDSGRDSGGPRRRRGNRGRGQRRDWSRAPPPPEERQETRSQTPAPKPSRAPPQQPQPPRMQTGRGGSAPRPELGPPTNPFQAAVARGLRPPLHDPDTEAPTEACVTSWLWSEGEGAVFYRVDLHFTNLGTPPLDEDGRWDPALMYNPCGPEPPAHVVRAYNQPAGDVRGVWGKGERTYAEQDFRVGGTRWHRLLRMPVRGLDGDSAPLPPHTTERIETRSARHPWRIRFGAPQAFLAGLLLATVAVGTARAGLQPRADMAAPPTLPQPPCA... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062] | host cell Golgi membrane [GO:0044178]; host cell mitochondrion [GO:0033650]; membrane [GO:0016020]; T=4 icosahedral viral capsid [GO:0039619]; viral envelope [GO:0019031]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | metal ion binding [GO:0046872]; RNA binding [GO:0003723] | PF05750;PF05748;PF05749; | 2.60.98.30;3.30.67.20;2.60.40.2650;3.10.50.50; | null | PTM: Structural polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. Two signal peptidase-mediated cleavages within the polyprotein produce the structural proteins capsid, E2, and E1. The E2 signal peptide remains attached to the C-terminus of the capsid protein after cleavage by the signal peptidas... | SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000250|UniProtKB:P08563}. Host cytoplasm. Host mitochondrion {ECO:0000250|UniProtKB:P08563}. Note=The capsid protein is concentrated around Golgi region (By similarity). In the virion, it is probably associated to the viral membrane (By similarity). {ECO:0000250|UniP... | null | null | null | null | null | FUNCTION: [Capsid protein]: Capsid protein interacts with genomic RNA and assembles into icosahedric core particles 65-70 nm in diameter. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions from host Golgi membranes.... | Rubella virus (strain Therien) (RUBV) |
P07567 | GAG_MPMV | MGQELSQHERYVEQLKQALKTRGVKVKYADLLKFFDFVKDTCPWFPQEGTIDIKRWRRVGDCFQDYYNTFGPEKVPVTAFSYWNLIKELIDKKEVNPQVMAAVAQTEEILKSNSQTDLTKTSQNPDLDLISLDSDDEGAKSSSLQDKGLSSTKKPKRFPVLLTAQTSKDPEDPNPSEVDWDGLEDEAAKYHNPDWPPFLTRPPPYNKATPSAPTVMAVVNPKEELKEKIAQLEEQIKLEELHQALISKLQKLKTGNETVTHPDTAGGLSRTPHWPGQHIPKGKCCASREKEEQIPKDIFPVTETVDGQGQAWRHHNGFDF... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell cytoplasm [GO:0030430]; viral nucleocapsid [GO:0019013] | metal ion binding [GO:0046872]; nucleic acid binding [GO:0003676]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270] | PF02337;PF00607;PF19317;PF14787; | 1.10.1200.30;1.10.375.10;1.10.150.490;4.10.60.10; | null | PTM: [Gag polyprotein]: Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and is required for the assembly of viral particles. {ECO:0000250|UniProtKB:P10258}.; PTM: [Gag polyprotein]: Specific enzymatic cleavages in vivo yield matu... | SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p14]: Virion {ECO:0000305}. | null | null | null | null | null | FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.; FUNCTION: [Nucleocapsid protein p14]: Nucleocapsid protein. {ECO:0000305}.; FUNCTION: [Capsid protein p27]: Capsid protein. {ECO:0000305}. | Mason-Pfizer monkey virus (MPMV) (Simian Mason-Pfizer virus) |
P07570 | PRO_MPMV | MGQELSQHERYVEQLKQALKTRGVKVKYADLLKFFDFVKDTCPWFPQEGTIDIKRWRRVGDCFQDYYNTFGPEKVPVTAFSYWNLIKELIDKKEVNPQVMAAVAQTEEILKSNSQTDLTKTSQNPDLDLISLDSDDEGAKSSSLQDKGLSSTKKPKRFPVLLTAQTSKDPEDPNPSEVDWDGLEDEAAKYHNPDWPPFLTRPPPYNKATPSAPTVMAVVNPKEELKEKIAQLEEQIKLEELHQALISKLQKLKTGNETVTHPDTAGGLSRTPHWPGQHIPKGKCCASREKEEQIPKDIFPVTETVDGQGQAWRHHNGFDF... | 3.4.23.-; 3.6.1.23 | null | nucleotide metabolic process [GO:0009117]; proteolysis [GO:0006508]; viral process [GO:0016032] | viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; dUTP diphosphatase activity [GO:0004170]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270] | PF00692;PF01585;PF02337;PF00607;PF19317;PF00077;PF14787; | 1.10.1200.30;2.70.40.10;2.40.70.10;1.10.375.10;1.10.150.490;4.10.60.10; | null | PTM: [Protease 17 kDa]: Released by autocatalytic processing. The protease can undergo further autoprocessing to yield 2 shorter but enzymatically active forms of 12 kDa and 13 kDa without the GDP domain. the 12 kDa form is monomeric. {ECO:0000269|PubMed:14568536, ECO:0000269|PubMed:16257973, ECO:0000269|PubMed:9636364... | SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein-dUTPase]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Protease 13 kDa]: Virion {ECO:0000269|PubMed:9636364}.; SUBCELLULAR LOCATION: [Proteas... | CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; Evidence={ECO:0000269|PubMed:17169987}; | null | null | null | null | FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.; FUNCTION: Nucleocapsid protein p14: Nucleocapsid protein. {ECO:0000305}.; FUNCTION: [Capsid protein p27]: Capsid protein. {ECO:0000305}.; FUNCTION: [Protease 17 kDa]: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins duri... | Mason-Pfizer monkey virus (MPMV) (Simian Mason-Pfizer virus) |
P07572 | POL_MPMV | MGQELSQHERYVEQLKQALKTRGVKVKYADLLKFFDFVKDTCPWFPQEGTIDIKRWRRVGDCFQDYYNTFGPEKVPVTAFSYWNLIKELIDKKEVNPQVMAAVAQTEEILKSNSQTDLTKTSQNPDLDLISLDSDDEGAKSSSLQDKGLSSTKKPKRFPVLLTAQTSKDPEDPNPSEVDWDGLEDEAAKYHNPDWPPFLTRPPPYNKATPSAPTVMAVVNPKEELKEKIAQLEEQIKLEELHQALISKLQKLKTGNETVTHPDTAGGLSRTPHWPGQHIPKGKCCASREKEEQIPKDIFPVTETVDGQGQAWRHHNGFDF... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.-; 3.6.1.23 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; Note=The RT polymerase active site binds 2 magnesium ions. {ECO:0000255|PROSITE-ProRule:PRU00405}; | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; viral genome integration into host DNA [GO:0044826] | viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; dUTP diphosphatase activity [GO:0004170]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural c... | PF00692;PF01585;PF02337;PF00607;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06817;PF14787; | 1.10.10.200;1.10.1200.30;2.70.40.10;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;2.30.30.10;1.10.150.490;3.30.420.10;4.10.60.10; | Retroviral Pol polyprotein family | PTM: [Protease 17 kDa]: Released by autocatalytic processing. The protease can undergo further autoprocessing to yield 2 shorter but enzymatically active forms of 12 kDa and 13 kDa. {ECO:0000269|PubMed:16257973, ECO:0000269|PubMed:9636364}.; PTM: [Gag-Pro-Pol polyprotein]: Myristoylated. Myristoylation of the matrix (M... | SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein-dUTPase]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Protease 13 kDa]: Virion {ECO:0000269|PubMed:9636364}.; SUBCELLULAR LOCATION: [Proteas... | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405, ECO:0000269|PubMed:22171253}; ... | null | null | null | null | FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.; FUNCTION: Nucleocapsid protein p14: Nucleocapsid protein. {ECO:0000305}.; FUNCTION: [Capsid protein p27]: Capsid protein. {ECO:0000305}.; FUNCTION: [Protease 17 kDa]: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins duri... | Mason-Pfizer monkey virus (MPMV) (Simian Mason-Pfizer virus) |
P07575 | ENV_MPMV | MNFNYHFIWSLVILSQISQVQAGFGDPREALAEIQQKHGKPCDCAGGYVSSPPINSLTTVSCSTHTAYSVTNSLKWQCVSTPTTPSNTHIGSCPGECNTISYDSVHASCYNHYQQCNIGNKTYLTATITGDRTPAIGDGNVPTVLGTSHNLITAGCPNGKKGQVVCWNSRPSVHISDGGGPQDKARDIIVNKKFEELHRSLFPELSYHPLALPEARGKEKIDAHTLDLLATVHSLLNASQPSLAEDCWLCLQSGDPVPLALPYNDTLCSNFACLSNHSCPLTPPFLVQPFNFTDSNCLYAHYQNNSFDIDVGLASFTNCS... | null | null | fusion of virus membrane with host plasma membrane [GO:0019064]; symbiont entry into host cell [GO:0046718]; syncytium formation by plasma membrane fusion [GO:0000768]; virion attachment to host cell [GO:0019062] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF00429; | 1.10.287.210; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires th... | SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral membrane protein. Host cell membrane... | null | null | null | null | null | FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).... | Mason-Pfizer monkey virus (MPMV) (Simian Mason-Pfizer virus) |
P07583 | LEG4_CHICK | MSCQGPVCTNLGLKPGQRLTVKGIIAPNAKSFVMNLGKDSTHLGLHFNPRFDAHGDVNLIVCNSKKMEEWGTEQRETVFPFQKGAPIEITFSINPSDLTVHLPGHQFSFPNRLGLSVFDYFDTHGDFTLRSVSWE | null | null | null | collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615] | galactoside binding [GO:0016936]; lactose binding [GO:0030395]; laminin binding [GO:0043236] | PF00337; | 2.60.120.200; | null | null | null | null | null | null | null | null | FUNCTION: This protein binds beta-galactoside. May participate in host antiviral defense through specific interaction with glycans on the viral envelope glycoproteins. {ECO:0000269|PubMed:28978647}. | Gallus gallus (Chicken) |
P07584 | ASTA_ASTAS | MQCAVLLVLLGVVAASPIIPEAARALYYNDGMFEGDIKLRAGRQPARVGAAILGDEYLWSGGVIPYTFAGVSGADQSAILSGMQELEEKTCIRFVPRTTESDYVEIFTSGSGCWSYVGRISGAQQVSLQANGCVYHGTIIHELMHAIGFYHEHTRMDRDNYVTINYQNVDPSMTSNFDIDTYSRYVGEDYQYYSIMHYGKYSFSIQWGVLETIVPLQNGIDLTDPYDKAHMLQTDANQINNLYTNECSLRH | 3.4.24.21 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|PROSITE-ProRule:PRU01211, ECO:0000269|PubMed:1319561, ECO:0000269|PubMed:8756323, ECO:0000269|Ref.3}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU01211, ECO:0000269|PubMed:1319561, ECO:0000269|PubMed:8756323, ECO:0000269|Ref.3}; | cell adhesion [GO:0007155]; fertilization [GO:0009566]; negative regulation of binding of sperm to zona pellucida [GO:2000360]; positive regulation of protein processing [GO:0010954]; prevention of polyspermy [GO:0060468]; proteolysis [GO:0006508] | cortical granule [GO:0060473]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | aspartic-type peptidase activity [GO:0070001]; glutamic-type peptidase activity [GO:0070002]; metalloendopeptidase activity [GO:0004222]; peptidase activity [GO:0008233]; zinc ion binding [GO:0008270] | PF01400; | 3.40.390.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of peptide bonds in substrates containing five or more amino acids, preferentially with Ala in P1', and Pro in P2'.; EC=3.4.24.21; Evidence={ECO:0000269|PubMed:2261483, ECO:0000269|Ref.3}; | null | null | null | null | FUNCTION: Metalloprotease. This protease prefers to cleave in front of small aliphatic residues (P1'). The presence of Lys or Arg in the P1 and P2 position yields high-turnover substrates. In the P3 position the enzyme prefers Pro > Val > Leu > Ala > Gly. {ECO:0000269|PubMed:2261483}. | Astacus astacus (Noble crayfish) (Astacus fluviatilis) |
P07585 | PGS2_HUMAN | MKATIILLLLAQVSWAGPFQQRGLFDFMLEDEASGIGPEVPDDRDFEPSLGPVCPFRCQCHLRVVQCSDLGLDKVPKDLPPDTTLLDLQNNKITEIKDGDFKNLKNLHALILVNNKISKVSPGAFTPLVKLERLYLSKNQLKELPEKMPKTLQELRAHENEITKVRKVTFNGLNQMIVIELGTNPLKSSGIENGAFQGMKKLSYIRIADTNITSIPQGLPPSLTELHLDGNKISRVDAASLKGLNNLAKLGLSFNSISAVDNGSLANTPHLRELHLDNNKLTRVPGGLAEHKYIQVVYLHNNNISVVGSSDFCPPGHNTK... | null | null | animal organ morphogenesis [GO:0009887]; negative regulation of angiogenesis [GO:0016525]; negative regulation of endothelial cell migration [GO:0010596]; negative regulation of vascular endothelial growth factor signaling pathway [GO:1900747]; positive regulation of autophagy [GO:0010508]; positive regulation of macro... | collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; lysosomal lumen [GO:0043202] | extracellular matrix binding [GO:0050840]; extracellular matrix structural constituent conferring compression resistance [GO:0030021]; glycosaminoglycan binding [GO:0005539]; RNA binding [GO:0003723] | PF13855;PF01462; | 3.80.10.10; | Small leucine-rich proteoglycan (SLRP) family, SLRP class I subfamily | PTM: The attached glycosaminoglycan chain can be either chondroitin sulfate or dermatan sulfate depending upon the tissue of origin. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. Secreted {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}. | null | null | null | null | null | FUNCTION: May affect the rate of fibrils formation. | Homo sapiens (Human) |
P07589 | FINC_BOVIN | MLGGPGPGLLLLLAVLSLGTAVPSAGASKSRRQAQQIVQPQSPLTVSQSKPGCYDNGKHYQINQQWERTYLGSALVCTCYGGSRGFNCESKPEPEETCFDKYTGNTYRVGDTYERPKDSMIWDCTCIGAGRGRISCTIANRCHEGGQSYKIGDTWRRPHETGGYMLECVCLGNGKGEWTCKPIAEKCFDQAAGTSYVVGETWEKPYQGWMMVDCTCLGEGSGRITCTSRNRCNDQDTRTSYRIGDTWSKKDNRGNLLQCICTGNGRGEWKCERHTSLQTTSAGSGSFTDVRTAIYQPQPHPQPPPYGHCVTDSGVVYSVG... | null | null | acute-phase response [GO:0006953]; angiogenesis [GO:0001525]; cell-matrix adhesion [GO:0007160]; cell-substrate junction assembly [GO:0007044]; heart development [GO:0007507]; nervous system development [GO:0007399]; regulation of cell shape [GO:0008360] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | disordered domain specific binding [GO:0097718]; extracellular matrix structural constituent [GO:0005201]; heparin binding [GO:0008201]; integrin binding [GO:0005178]; proteoglycan binding [GO:0043394] | PF00039;PF00040;PF00041; | 2.10.70.10;2.10.10.10;2.60.40.10; | null | PTM: Sulfated. {ECO:0000250|UniProtKB:P02751}.; PTM: Forms covalent cross-links mediated by a transglutaminase, such as F13A or TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers (e.g. fibrinogen-fibronectin, collagen-fibronectin heteropolymers). {ECO:0000... | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P11276}. Secreted {ECO:0000250|UniProtKB:P11276}. | null | null | null | null | null | FUNCTION: Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape (By similarity). Involved in osteoblast compaction through the fibronectin fibrilloge... | Bos taurus (Bovine) |
P07591 | TRXM_SPIOL | MAIENCLQLSTSASVGTVAVKSHVHHLQPSSKVNVPTFRGLKRSFPALSSSVSSSSPRQFRYSSVVCKASEAVKEVQDVNDSSWKEFVLESEVPVMVDFWAPWCGPCKLIAPVIDELAKEYSGKIAVYKLNTDEAPGIATQYNIRSIPTVLFFKNGERKESIIGAVPKSTLTDSIEKYLSP | null | null | null | chloroplast [GO:0009507] | enzyme activator activity [GO:0008047]; protein-disulfide reductase activity [GO:0015035] | PF00085; | 3.40.30.10; | Thioredoxin family, Plant M-type subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast. | null | null | null | null | null | FUNCTION: Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The M form is known to activate NADP-malate dehydrogenase. | Spinacia oleracea (Spinach) |
P07602 | SAP_HUMAN | MYALFLLASLLGAALAGPVLGLKECTRGSAVWCQNVKTASDCGAVKHCLQTVWNKPTVKSLPCDICKDVVTAAGDMLKDNATEEEILVYLEKTCDWLPKPNMSASCKEIVDSYLPVILDIIKGEMSRPGEVCSALNLCESLQKHLAELNHQKQLESNKIPELDMTEVVAPFMANIPLLLYPQDGPRSKPQPKDNGDVCQDCIQMVTDIQTAVRTNSTFVQALVEHVKEECDRLGPGMADICKNYISQYSEIAIQMMMHMQPKEICALVGFCDEVKEMPMQTLVPAKVASKNVIPALELVEPIKKHEVPAKSDVYCEVCEF... | null | null | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; epithelial cell differentiation involved in prostate gland development [GO:0060742]; ganglioside GM1 transport to membrane [GO:1905572]; lysosomal transport [GO:0007041]; positive regulation of beta-galactosidase activity [GO:190377... | azurophil granule membrane [GO:0035577]; collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; late endosome [GO:0005770]; lysosomal lumen [GO:0043202]; lysoso... | enzyme activator activity [GO:0008047]; ganglioside GM1 binding [GO:1905573]; ganglioside GM2 binding [GO:1905574]; ganglioside GM3 binding [GO:1905575]; ganglioside GP1c binding [GO:1905577]; ganglioside GT1b binding [GO:1905576]; identical protein binding [GO:0042802]; phospholipid binding [GO:0005543]; protease bind... | PF02199;PF05184;PF03489; | 1.10.225.10; | null | PTM: The lysosomal precursor is proteolytically processed to 4 small peptides, which are similar to each other and are sphingolipid hydrolase activator proteins.; PTM: N-linked glycans show a high degree of microheterogeneity. {ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19167329}.; PTM: The one residue extended Sa... | SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:14657016, ECO:0000269|PubMed:21835174, ECO:0000269|PubMed:22431521}.; SUBCELLULAR LOCATION: [Prosaposin]: Secreted {ECO:0000250|UniProtKB:Q61207}. Note=Secreted as a fully glycosylated 70 kDa protein composed of complex glycans. {ECO:0000250|UniProtKB:Q61207}. | null | null | null | null | null | FUNCTION: Saposin-A and saposin-C stimulate the hydrolysis of glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46). Saposin-C apparently acts by combining with the enzyme and acidic lipid to form an activated complex, rather than by solubilizing the... | Homo sapiens (Human) |
P07604 | TYRR_ECOLI | MRLEVFCEDRLGLTRELLDLLVLRGIDLRGIEIDPIGRIYLNFAELEFESFSSLMAEIRRIAGVTDVRTVPWMPSEREHLALSALLEALPEPVLSVDMKSKVDMANPASCQLFGQKLDRLRNHTAAQLINGFNFLRWLESEPQDSHNEHVVINGQNFLMEITPVYLQDENDQHVLTGAVVMLRSTIRMGRQLQNVAAQDVSAFSQIVAVSPKMKHVVEQAQKLAMLSAPLLITGDTGTGKDLFAYACHQASPRAGKPYLALNCASIPEDAVESELFGHAPEGKKGFFEQANGGSVLLDEIGEMSPRMQAKLLRFLNDGTF... | null | null | aromatic compound catabolic process [GO:0019439]; negative regulation of DNA-templated transcription [GO:0045892]; regulation of DNA-templated transcription [GO:0006355] | cytosol [GO:0005829] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677] | PF18024;PF13188;PF00158; | 1.10.8.60;3.30.70.260;1.10.10.60;3.40.50.300;3.30.450.20; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: Dual transcriptional regulator of the TyrR regulon, which includes a number of genes coding for proteins involved in the biosynthesis or transport of the three aromatic amino acids, phenylalanine, tyrosine and tryptophan (PubMed:14614536, PubMed:15049824, PubMed:1860819, PubMed:334742, PubMed:4399341, PubMed:... | Escherichia coli (strain K12) |
P07607 | TYSY_MOUSE | MLVVGSELQSDAQQLSAEAPRHGELQYLRQVEHILRCGFKKEDRTGTGTLSVFGMQARYSLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVRIWDANGSRDFLDSLGFSARQEGDLGPVYGFQWRHFGAEYKDMDSDYSGQGVDQLQKVIDTIKTNPDDRRIIMCAWNPKDLPLMALPPCHALCQFYVVNGELSCQLYQRSGDMGLGVPFNIASYALLTYMIAHITGLQPGDFVHTLGDAHIYLNHIEPLKIQLQREPRPFPKLKILRKVETIDDFKVEDFQIEGYNPHPTIKMEMAV | 2.1.1.45 | null | cartilage development [GO:0051216]; circadian rhythm [GO:0007623]; developmental growth [GO:0048589]; dTMP biosynthetic process [GO:0006231]; dTTP biosynthetic process [GO:0006235]; intestinal epithelial cell maturation [GO:0060574]; liver regeneration [GO:0097421]; methylation [GO:0032259]; regulation of translation [... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | dihydrofolate reductase activity [GO:0004146]; folic acid binding [GO:0005542]; heterocyclic compound binding [GO:1901363]; mRNA binding [GO:0003729]; mRNA regulatory element binding translation repressor activity [GO:0000900]; protein homodimerization activity [GO:0042803]; sequence-specific mRNA binding [GO:1990825];... | PF00303; | 3.30.572.10; | Thymidylate synthase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P04818}. Cytoplasm {ECO:0000250|UniProtKB:P04818}. Mitochondrion {ECO:0000250|UniProtKB:P04818}. Mitochondrion matrix {ECO:0000250|UniProtKB:P04818}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P04818}. | CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP; Xref=Rhea:RHEA:12104, ChEBI:CHEBI:15636, ChEBI:CHEBI:57451, ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.45; Evidence={ECO:0000250|UniProtKB:P45352}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12105... | null | PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. {ECO:0000250|UniProtKB:P45352}. | null | null | FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine 5'-monophosphate (dUMP) to thymidine 5'-monophosphate (dTMP), using the cosubstrate, 5,10- methylenetetrahydrofolate (CH2H4folate) as a 1-carbon donor and reductant and contributes to the de novo mitochondrial thymidylate biosynthesis pathway. {ECO:000025... | Mus musculus (Mouse) |
P07611 | PG094_VACCW | MGGGVSVELPKRDPPPGVPTDEMLLNVDKMHDVIAPAKLLEYVHIGPLAKDKEDKVKKRYPEFRLVNTGPGGLSALLRQSYNGTAPNCCRTFNRTHYWKKDGKISDKYEEGAVLESCWPDVHDTGKCDVDLFDWCQGDTFDRNICHQWIGSAFNRSNRTVEGQQSLINLYNKMQTLCSKDASVPICESFLHHLRAHNTEDSKEMIDYILRQQSADFKQKYMRCSYPTRDKLEESLKYAEPRECWDPECSNANVNFLLTRNYNNLGLCNIVRCNTSVNNLQMDKTSSLRLSCGLSNSDRFSTVPVNRAKVVQHNIKHSFDL... | null | null | fusion of virus membrane with host plasma membrane [GO:0019064]; symbiont entry into host cell [GO:0046718] | membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF03003; | null | Orthopoxvirus OPG086 family | PTM: Unglycosylated because produced in viral factories instead of the classic ER -Golgi route. {ECO:0000305|PubMed:34076488}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000305|PubMed:34076488}; Single-pass type II membrane protein {ECO:0000305}. Note=Component of the mature virion (MV) membrane. The mature virion is located in the cytoplasm of infected cells and is probably released by cell lysis. {ECO:0000269|PubMed:16973586, ECO:0000305|Pu... | null | null | null | null | null | FUNCTION: Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation. {ECO:0000269|PubMed:16... | Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) |
P07612 | PG095_VACCW | MGAAASIQTTVNTLSERISSKLEQEANASAQTKCDIEIGNFYIRQNHGCNLTVKNMCSADADAQLDAVLSAATETYSGLTPEQKAYVPAMFTAALNIQTSVNTVVRDFENYVKQTCNSSAVVDNKLKIQNVIIDECYGAPGSPTNLEFINTGSSKGNCAIKALMQLTTKATTQIAPKQVAGTGVQFYMIVIGVIILAALFMYYAKRMLFTSTNDKIKLILANKENVHWTTYMDTFFRTSPMVIATTDMQN | null | null | symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF02442; | null | Orthopoxvirus OPG095 family | PTM: Myristoylated. {ECO:0000269|PubMed:2243383, ECO:0000269|PubMed:9188589}.; PTM: Disulfid bonds are oxidized in the cytoplasm by OPG088 protein. {ECO:0000269|PubMed:11983854}.; PTM: Unglycosylated because produced in viral factories instead of the classic ER -Golgi route. {ECO:0000305|PubMed:34076488}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305|PubMed:34076488}. Note=Localizes to the membrane surrounding the core of mature virus particles (MV). {ECO:0000269|PubMed:9188589, ECO:0000305|PubMed:34076488}. | null | null | null | null | null | FUNCTION: Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation. {ECO:0000269|PubMed:34... | Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) |
P07617 | MCE_VACCW | MDVVSLDKPFMYFEEIDNELDYEPESANEVAKKLPYQGQLKLLLGELFFLSKLQRHGILDGATVVYIGSAPGTHIRYLRDHFYNLGVIIKWMLIDGRHHDPILNGLRDVTLVTRFVDEEYLRSIKKQLHPSKIILISDVRSKRGGNEPSTADLLSNYALQNVMISILNPVASSLKWRCPFPDQWIKDFYIPHGNKMLQPFAPSYSAEMRLLSIYTGENMRLTRVTKSDAVNYEKKMYYLNKIVRNKVVVNFDYPNQEYDYFHMYFMLRTVYCNKTFPTTKAKVLFLQQSIFRFLNIPTTSTEKVSHEPIQRKISSKNSMS... | 2.1.1.57 | null | 7-methylguanosine mRNA capping [GO:0006370]; regulation of mRNA 3'-end processing [GO:0031440] | virion component [GO:0044423] | mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; RNA binding [GO:0003723]; translation elongation factor activity [GO:0003746] | PF01358; | 3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, Poxvirus/kinetoplastid 2'-O-MTase family | null | SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=Localizes to the virion core. {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167, Rhea:RHEA-COMP:17168, ChEBI:CHE... | null | null | null | null | FUNCTION: Displays methyltransferase, positive regulation of the poly(A) polymerase and transcription elongation activities. Involved in the modification of both mRNA ends and in intermediate and late gene positive transcription elongation. At the mRNAs 5' end, methylates the ribose 2' OH group of the first transcribed... | Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) |
P07623 | METAS_ECOLI | MPIRVPDELPAVNFLREENVFVMTTSRASGQEIRPLKVLILNLMPKKIETENQFLRLLSNSPLQVDIQLLRIDSRESRNTPAEHLNNFYCNFEDIQDQNFDGLIVTGAPLGLVEFNDVAYWPQIKQVLEWSKDHVTSTLFVCWAVQAALNILYGIPKQTRTEKLSGVYEHHILHPHALLTRGFDDSFLAPHSRYADFPAALIRDYTDLEILAETEEGDAYLFASKDKRIAFVTGHPEYDAQTLAQEFFRDVEAGLDPDVPYNYFPHNDPQNTPRASWRSHGNLLFTNWLNYYVYQITPYDLRHMNPTLD | 2.3.1.46 | null | L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine [GO:0019281] | cytoplasm [GO:0005737] | homoserine O-acetyltransferase activity [GO:0004414]; homoserine O-succinyltransferase activity [GO:0008899]; protein homodimerization activity [GO:0042803] | PF04204; | 3.40.50.880; | MetA family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=L-homoserine + succinyl-CoA = CoA + O-succinyl-L-homoserine; Xref=Rhea:RHEA:22008, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:57476, ChEBI:CHEBI:57661; EC=2.3.1.46; Evidence={ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000269|PubMed:10572016, ECO:0000269|PubMed:17302437, ECO:0000269|PubMed... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.17 mM for succinyl-CoA {ECO:0000269|PubMed:10572016}; KM=0.13 mM for succinyl-CoA {ECO:0000269|PubMed:17302437}; KM=0.28 mM for succinyl-CoA {ECO:0000269|PubMed:17442255}; KM=1.6 mM for L-homoserine {ECO:0000269|PubMed:10572016}; KM=0.72 mM for L-homoserine {ECO:... | PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-succinyl-L-homoserine from L-homoserine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000305|PubMed:10572016}. | null | null | FUNCTION: Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine (PubMed:10572016, PubMed:17302437, PubMed:17442255, PubMed:28581482). Utilizes a ping-pong kinetic mechanism in which the succinyl group of succinyl-CoA is initially transferred to the enzyme to form a succinyl-enzyme ... | Escherichia coli (strain K12) |
P07630 | CAH2_CHICK | MSHHWGYDSHNGPAHWHEHFPIANGERQSPIAISTKAARYDPALKPLSFSYDAGTAKAIVNNGHSFNVEFDDSSDKSVLQGGALDGVYRLVQFHIHWGSCEGQGSEHTVDGVKYDAELHIVHWNVKYGKFAEALKHPDGLAVVGIFMKVGNAKPEIQKVVDALNSIQTKGKQASFTNFDPTGLLPPCRDYWTYPGSLTTPPLHECVIWHVLKEPITVSSEQMCKLRGLCFSAENEPVCRMVDNWRPCQPLKSREVRASFQ | 4.2.1.1; 4.2.1.69 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00921}; | carbon dioxide transport [GO:0015670]; cellular response to carbon dioxide [GO:0071244]; one-carbon metabolic process [GO:0006730]; regulation of intracellular pH [GO:0051453] | apical part of cell [GO:0045177]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | carbonate dehydratase activity [GO:0004089]; cyanamide hydratase activity [GO:0018820]; zinc ion binding [GO:0008270] | PF00194; | 3.10.200.10; | Alpha-carbonic anhydrase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00918}. Cell membrane {ECO:0000250|UniProtKB:P00918}. | CATALYTIC ACTIVITY: Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17544; EC=4.2.1.1; Evidence={ECO:0000250|UniProtKB:P00918}; CATALYTIC ACTIVITY: Reaction=urea = cyanamide + H2O; Xref=Rhea:RHEA:23056, ChEBI:CHEBI:15377, ChEBI:CH... | null | null | null | null | FUNCTION: Catalyzes the reversible hydration of carbon dioxide. Can also hydrate cyanamide to urea. {ECO:0000250|UniProtKB:P00918}. | Gallus gallus (Chicken) |
P07632 | SODC_RAT | MAMKAVCVLKGDGPVQGVIHFEQKASGEPVVVSGQITGLTEGEHGFHVHQYGDNTQGCTTAGPHFNPHSKKHGGPADEERHVGDLGNVAAGKDGVANVSIEDRVISLSGEHSIIGRTMVVHEKQDDLGKGGNEESTKTGNAGSRLACGVIGIAQ | 1.15.1.1 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250}; Note=Binds 1 copper ion per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | action potential initiation [GO:0099610]; anterograde axonal transport [GO:0008089]; apoptotic process [GO:0006915]; auditory receptor cell stereocilium organization [GO:0060088]; cellular response to ATP [GO:0071318]; cellular response to cadmium ion [GO:0071276]; cellular response to oxidative stress [GO:0034599]; ce... | axon cytoplasm [GO:1904115]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; dendrite cytoplasm [GO:0032839]; dense core granule [GO:0031045]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; lysosome [GO:0005764]; mitochondrion [GO:0005739]; neuronal cell body [GO:00... | copper ion binding [GO:0005507]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; protein phosphatase 2B binding [GO:0030346]; protein-folding chaperone binding [GO:0051087]; small GTPase binding [GO:0031267]; superoxide dismutase activity [GO:0004784]; zinc ion binding [GO:0008270] | PF00080; | 2.60.40.200; | Cu-Zn superoxide dismutase family | PTM: Palmitoylation helps nuclear targeting and decreases catalytic activity. {ECO:0000250}.; PTM: Succinylation, adjacent to copper catalytic site, probably inhibits activity. Desuccinylation by SIRT5 enhances activity. {ECO:0000250|UniProtKB:P00441}. | SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; Evidence={ECO:0000305|PubMed:2703531}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20697; Evidence={ECO:0000305|PubMed:2703531}; | null | null | null | null | FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. | Rattus norvegicus (Rat) |
P07634 | ANFB_PIG | MGPRMALPRVLLLLFLHLLLLGCRSHPLGGAGLASELPGIQELLDRLRDRVSELQAERTDLEPLRQDRGLTEAWEAREAAPTGVLGPRSSIFQVLRGIRSPKTMRDSGCFGRRLDRIGSLSGLGCNVLRRY | null | null | blood vessel diameter maintenance [GO:0097746]; cGMP biosynthetic process [GO:0006182]; cGMP-mediated signaling [GO:0019934]; negative regulation of systemic arterial blood pressure [GO:0003085]; neuropeptide signaling pathway [GO:0007218]; receptor guanylyl cyclase signaling pathway [GO:0007168] | cytoplasm [GO:0005737]; extracellular space [GO:0005615] | hormone activity [GO:0005179]; hormone receptor binding [GO:0051427] | PF00212; | null | Natriuretic peptide family | PTM: The precursor molecule is proteolytically cleaved by the endoproteases FURIN or CORIN at Arg-99 to produce the active brain natriuretic peptide 32 and the inactive NT-proBNP. CORIN also cleaves the precursor molecule at additional residues including Arg-96 and possibly Lys-102 (By similarity). Undergoes further pr... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P16860}. Note=Detected in blood. {ECO:0000250|UniProtKB:P16860}.; SUBCELLULAR LOCATION: [Brain natriuretic peptide 32]: Secreted {ECO:0000250|UniProtKB:P16860}. Note=Detected in blood. {ECO:0000250|UniProtKB:P16860}. | null | null | null | null | null | FUNCTION: [Brain natriuretic peptide 32]: Cardiac hormone that plays a key role in mediating cardio-renal homeostasis (By similarity). May also function as a paracrine antifibrotic factor in the heart (By similarity). Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn activates effector pr... | Sus scrofa (Pig) |
P07636 | TNPA_BPMU | MELWVSPKECANLPGLPKTSAGVIYVAKKQGWQNRTRAGVKGGKAIEYNANSLPVEAKAALLLRQGEIETSLGYFEIARPTLEAHDYDREALWSKWDNASDSQRRLAEKWLPAVQAADEMLNQGISTKTAFATVAGHYQVSASTLRDKYYQVQKFAKPDWAAALVDGRGASRRNVHKSEFDEDAWQFLIADYLRPEKPAFRKCYERLELAAREHGWSIPSRATAFRRIQQLDEAMVVACREGEHALMHLIPAQQRTVEHLDAMQWINGDGYLHNVFVRWFNGDVIRPKTWFWQDVKTRKILGWRCDVSENIDSIRLSFMD... | 3.1.22.-; 6.5.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:14661976, ECO:0000269|PubMed:7912831}; | DNA integration [GO:0015074]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA transposition [GO:0006313]; latency-replication decision [GO:0098689]; viral DNA genome replication [GO:0039693] | host cell cytoplasm [GO:0030430] | DNA binding [GO:0003677]; double-stranded DNA endonuclease activity [GO:1990238]; ligase activity [GO:0016874]; metal ion binding [GO:0046872]; transposase activity [GO:0004803] | PF02914;PF02316;PF09039;PF09299; | 6.10.250.2550;1.10.10.60;3.30.420.10;2.30.30.130;1.10.10.10; | Mulikevirus repressor c protein family | null | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: Responsible for viral genome integration into the host chromosome. During integration of the incoming virus, DDE-recombinase A cleaves both viral DNA ends and the resulting 3'-OH perform a nucleophilic attack of the host DNA. The 5' flanking DNA attached to the ends of the viral genome (flaps) are resected by... | Escherichia phage Mu (Bacteriophage Mu) |
P07639 | AROB_ECOLI | MERIVVTLGERSYPITIASGLFNEPASFLPLKSGEQVMLVTNETLAPLYLDKVRGVLEQAGVNVDSVILPDGEQYKSLAVLDTVFTALLQKPHGRDTTLVALGGGVVGDLTGFAAASYQRGVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVVDLDCLKTLPPRELASGLAEVIKYGIILDGAFFNWLEENLDALLRLDGPAMAYCIRRCCELKAEVVAADERETGLRALLNLGHTFGHAIEAEMGYGNWLHGEAVAAGMVMAARTSERLGQFSSAETQRIITLLKRAGLPVNGPREMSAQAYLPHML... | 4.2.3.4 | COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000255|HAMAP-Rule:MF_00110, ECO:0000269|PubMed:2514789}; COFACTOR: Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000255|HAMAP-Rule:MF_00110, ECO:0000269|PubMed:2514789}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00110, EC... | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423] | cytoplasm [GO:0005737] | 3-dehydroquinate synthase activity [GO:0003856]; NAD+ binding [GO:0070403]; zinc ion binding [GO:0008270] | PF01761; | 3.40.50.1970;1.20.1090.10; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00110}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00110, ECO:0000269|PubMed:2514789}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.6 uM for 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate (at pH 6.5) {ECO:0000269|PubMed:2514789}; KM=5.5 uM for 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate (at pH 8.5) {ECO:0000269|PubMed:2514789}; | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_00110}. | null | null | FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). {ECO:0000255|HAMAP-Rule:MF_00110, ECO:0000269|PubMed:2514789}. | Escherichia coli (strain K12) |
P07647 | KLK9_RAT | MWFLILFLALSLGQIDAAPPGQSRVVGGYNCETNSQPWQVAVIGTTFCGGVLIDPSWVITAAHCYSKNYRVLLGRNNLVKDEPFAQRRLVSQSFQHPDYIPVFMRNHTRQRAYDHNNDLMLLHLSKPADITGGVKVIDLPTEEPKVGSICLASGWGMTNPSEMKLSHDLQCVNIHLLSNEKCIETYKNIETDVTLCAGEMDGGKDTCTGDSGGPLICDGVLQGLTSGGATPCAKPKTPAIYAKLIKFTSWIKKVMKENP | 3.4.21.35 | null | positive regulation of vasoconstriction [GO:0045907]; regulation of systemic arterial blood pressure [GO:0003073]; zymogen activation [GO:0031638] | secretory granule [GO:0030141] | serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.40.10.10; | Peptidase S1 family, Kallikrein subfamily | null | null | CATALYTIC ACTIVITY: Reaction=Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.; EC=3.4.21.35; | null | null | null | null | FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. This enzyme has a vasoconstrictor activity. KLK-9 has both a chymotrypsin-like and a trypsin-like properties. | Rattus norvegicus (Rat) |
P07648 | RECC_ECOLI | MLRVYHSNRLDVLEALMEFIVERERLDDPFEPEMILVQSTGMAQWLQMTLSQKFGIAANIDFPLPASFIWDMFVRVLPEIPKESAFNKQSMSWKLMTLLPQLLEREDFTLLRHYLTDDSDKRKLFQLSSKAADLFDQYLVYRPDWLAQWETGHLVEGLGEAQAWQAPLWKALVEYTHQLGQPRWHRANLYQRFIETLESATTCPPGLPSRVFICGISALPPVYLQALQALGKHIEIHLLFTNPCRYYWGDIKDPAYLAKLLTRQRRHSFEDRELPLFRDSENAGQLFNSDGEQDVGNPLLASWGKLGRDYIYLLSDLESS... | null | null | clearance of foreign intracellular DNA [GO:0044355]; DNA recombination [GO:0006310]; double-strand break repair via homologous recombination [GO:0000724]; recombinational repair [GO:0000725]; response to radiation [GO:0009314] | exodeoxyribonuclease V complex [GO:0009338] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; exodeoxyribonuclease V activity [GO:0008854] | PF04257;PF17946; | 1.10.10.160;1.10.10.990;3.40.50.10930;3.40.50.300; | RecC family | null | null | null | null | null | null | null | FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a rapid (>1 kb/second) and highly processive (>30 kb) ATP-dependent bidirectional helicase. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator, 5'-GCTGGTGG-3') sequence fro... | Escherichia coli (strain K12) |
P07649 | TRUA_ECOLI | MSDQQQPPVYKIALGIEYDGSKYYGWQRQNEVRSVQEKLEKALSQVANEPITVFCAGRTDAGVHGTGQVVHFETTALRKDAAWTLGVNANLPGDIAVRWVKTVPDDFHARFSATARRYRYIIYNHRLRPAVLSKGVTHFYEPLDAERMHRAAQCLLGENDFTSFRAVQCQSRTPWRNVMHINVTRHGPYVVVDIKANAFVHHMVRNIVGSLMEVGAHNQPESWIAELLAAKDRTLAAATAKAEGLYLVAVDYPDRYDLPKPPMGPLFLAD | 5.4.99.12 | null | tRNA pseudouridine synthesis [GO:0031119] | null | protein homodimerization activity [GO:0042803]; pseudouridine synthase activity [GO:0009982]; tRNA binding [GO:0000049]; tRNA pseudouridine synthase activity [GO:0106029] | PF01416; | 3.30.70.660;3.30.70.580; | TRNA pseudouridine synthase TruA family | null | null | CATALYTIC ACTIVITY: Reaction=uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA; Xref=Rhea:RHEA:22376, Rhea:RHEA-COMP:10085, Rhea:RHEA-COMP:10087, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.12; Evidence={ECO:0000269|PubMed:17466622}; | null | null | null | null | FUNCTION: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. {ECO:0000269|PubMed:17466622}. | Escherichia coli (strain K12) |
P07658 | FDHF_ECOLI | MKKVVTVCPYCASGCKINLVVDNGKIVRAEAAQGKTNQGTLCLKGYYGWDFINDTQILTPRLKTPMIRRQRGGKLEPVSWDEALNYVAERLSAIKEKYGPDAIQTTGSSRGTGNETNYVMQKFARAVIGTNNVDCCARVUHGPSVAGLHQSVGNGAMSNAINEIDNTDLVFVFGYNPADSHPIVANHVINAKRNGAKIIVCDPRKIETARIADMHIALKNGSNIALLNAMGHVIIEENLYDKAFVASRTEGFEEYRKIVEGYTPESVEDITGVSASEIRQAARMYAQAKSAAILWGMGVTQFYQGVETVRSLTSLAMLTG... | 1.17.98.4 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 1 [4Fe-4S] cluster per subunit.; COFACTOR: Name=Mo-bis(molybdopterin guanine dinucleotide); Xref=ChEBI:CHEBI:60539; Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.; | anaerobic electron transport chain [GO:0019645]; anaerobic respiration [GO:0009061]; cellular respiration [GO:0045333]; formate oxidation [GO:0015944]; glucose catabolic process [GO:0006007]; urate catabolic process [GO:0019628] | cytosol [GO:0005829]; formate dehydrogenase complex [GO:0009326]; membrane [GO:0016020]; plasma membrane respiratory chain complex I [GO:0045272] | 4 iron, 4 sulfur cluster binding [GO:0051539]; formate dehydrogenase (NAD+) activity [GO:0008863]; metal ion binding [GO:0046872]; molybdopterin cofactor binding [GO:0043546]; oxidoreductase activity, acting on the aldehyde or oxo group of donors [GO:0016903] | PF04879;PF00384;PF01568; | 2.40.40.20;3.40.50.740;2.20.25.90;3.40.228.10;1.20.5.460; | Prokaryotic molybdopterin-containing oxidoreductase family | null | null | CATALYTIC ACTIVITY: Reaction=A + formate + H(+) = AH2 + CO2; Xref=Rhea:RHEA:27290, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:17499; EC=1.17.98.4; Evidence={ECO:0000269|PubMed:16830149, ECO:0000269|PubMed:9036855, ECO:0000269|PubMed:9521673}; | null | null | null | null | FUNCTION: Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors. | Escherichia coli (strain K12) |
P07662 | G7AC_PSEU7 | MLRVLHRAASALVMATVIGLAPAVAFALAEPTSTPQAPIAAYKPRSNEILWDGYGVPHIYGVDAPSAFYGYGWAQARSHGDNILRLYGEARGKGAEYWGPDYEQTTVWLLTNGVPERAQQWYAQQSPDFRANLDAFAAGINAYAQQNPDDISPEVRQVLPVSGADVVAHAHRLMNFLYVASPGRTLGEGDPPDLADQGSNSWAVAPGKTANGNALLLQNPHLSWTTDYFTYYEAHLVTPDFEIYGATQIGLPVIRFAFNQRMGITNTVNGMVGATNYRLTLQDGGYLYDGQVRPFERPQASYRLRQADGTTVDKPLEIRS... | 3.5.1.93 | null | antibiotic biosynthetic process [GO:0017000]; response to antibiotic [GO:0046677] | periplasmic space [GO:0042597] | glutaryl-7-aminocephalosporanic-acid acylase activity [GO:0033968] | PF01804; | 1.10.1400.10;2.30.120.10;3.60.20.10;1.10.439.10; | Peptidase S45 family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:2993240}. | CATALYTIC ACTIVITY: Reaction=(7R)-7-(4-carboxybutanamido)cephalosporanate + H2O = (7R)-7-aminocephalosporanate + glutarate; Xref=Rhea:RHEA:23508, ChEBI:CHEBI:15377, ChEBI:CHEBI:30921, ChEBI:CHEBI:58501, ChEBI:CHEBI:58693; EC=3.5.1.93; | null | null | null | null | FUNCTION: Catalyzes the deacylation of 7 beta-(4-carboxybutanamido)cephalosporanic acid (glutaryl-7-aminocephalosporanic acid or GL-7-ACA) to 7-aminocephalosporanic acid (7-ACA). {ECO:0000269|PubMed:2993240}. | Pseudomonas sp. (strain SY-77) |
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