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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P07987 | GUX2_HYPJE | MIVGILTTLATLATLAASVPLEERQACSSVWGQCGGQNWSGPTCCASGSTCVYSNDYYSQCLPGAASSSSSTRAASTTSRVSPTTSRSSSATPPPGSTTTRVPPVGSGTATYSGNPFVGVTPWANAYYASEVSSLAIPSLTGAMATAAAAVAKVPSFMWLDTLDKTPLMEQTLADIRTANKNGGNYAGQFVVYDLPDRDCAALASNGEYSIADGGVAKYKNYIDTIRQIVVEYSDIRTLLVIEPDSLANLVTNLGTPKCANAQSAYLECINYAVTQLNLPNVAMYLDAGHAGWLGWPANQDPAAQLFANVYKNASSPRAL... | 3.2.1.91 | null | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | cellulose 1,4-beta-cellobiosidase activity [GO:0016162]; cellulose binding [GO:0030248]; identical protein binding [GO:0042802] | PF00734;PF01341; | 3.20.20.40; | Glycosyl hydrolase 6 (cellulase B) family | PTM: Asn-334 contains mainly a high-mannose-type glycan (Hex(7-9)GlcNAc(2)) in a 3:1 ration with a single GlcNAc. Asn-313 was primarily unglycosylated with a small fraction (18%) bearing a single GlcNAc at this site. {ECO:0000250|UniProtKB:A0A024SH76}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.3}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.; EC=3.2.1.91; Evidence={ECO:0000269|Ref.3}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=17 uM for cellotriose {ECO:0000269|PubMed:12188666}; KM=2.6 uM for cellotetraose {ECO:0000269|PubMed:12188666}; KM=1.3 uM for cellopentaose {ECO:0000269|PubMed:12188666}; KM=14 uM for cellohexaose {ECO:0000269|PubMed:12188666}; Note=kcat is 0.06 sec(-1) with cellot... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-6. {ECO:0000269|PubMed:12188666}; | null | FUNCTION: Exocellobiohydrolases (CBH) that catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide cellobiose (Ref.3). The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with endoglucanases (EGs), which cut internal beta-... | Hypocrea jecorina (Trichoderma reesei) |
P07988 | PSPB_HUMAN | MAESHLLQWLLLLLPTLCGPGTAAWTTSSLACAQGPEFWCQSLEQALQCRALGHCLQEVWGHVGADDLCQECEDIVHILNKMAKEAIFQDTMRKFLEQECNVLPLKLLMPQCNQVLDDYFPLVIDYFQNQTDSNGICMHLGLCKSRQPEPEQEPGMSDPLPKPLRDPLPDPLLDKLVLPVLPGALQARPGPHTQDLSEQQFPIPLPYCWLCRALIKRIQAMIPKGALAVAVAQVCRVVPLVAGGICQCLAERYSVILLDTLLGRMLPQLVCRLVLRCSMDDSAGPRSPTGEWLPRDSECHLCMSVTTQAGNSSEQAIPQA... | null | null | animal organ morphogenesis [GO:0009887]; respiratory gaseous exchange by respiratory system [GO:0007585]; sphingolipid metabolic process [GO:0006665] | alveolar lamellar body [GO:0097208]; clathrin-coated endocytic vesicle [GO:0045334]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; lamellar body [GO:0042599]; lysosome [GO:0005764]; multivesicular body [GO:0005771]; multivesicular body lumen [GO:0097486] | null | PF02199;PF05184;PF03489; | 1.10.225.10; | null | null | SUBCELLULAR LOCATION: Secreted, extracellular space, surface film. | null | null | null | null | null | FUNCTION: Pulmonary surfactant-associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. SP-B increases the collapse pressure of palmitic acid to nearly 70 millinewtons per meter. | Homo sapiens (Human) |
P07991 | OAT_YEAST | MSEATLSSKQTIEWENKYSAHNYHPLPVVFHKAKGAHVWDPEGKLYLDFLSAYSAVNQGHCHPHIIKALTEQAQTLTLSSRAFHNDVYAQFAKFVTEFFGFETVLPMNTGAEAVETALKLARRWGYMKKNIPQDKAIILGAEGNFHGRTFGAISLSTDYEDSKLHFGPFVPNVASGHSVHKIRYGHAEDFVPILESPEGKNVAAIILEPIQGEAGIVVPPADYFPKVSALCRKHNVLLIVDEIQTGIGRTGELLCYDHYKAEAKPDIVLLGKALSGGVLPVSCVLSSHDIMSCFTPGSHGSTFGGNPLASRVAIAALEVI... | 2.6.1.13 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | arginine catabolic process to glutamate [GO:0019544]; arginine catabolic process to proline via ornithine [GO:0010121]; L-proline biosynthetic process [GO:0055129]; ornithine metabolic process [GO:0006591] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | identical protein binding [GO:0042802]; ornithine aminotransferase activity [GO:0004587]; pyridoxal phosphate binding [GO:0030170] | PF00202; | 3.90.1150.10;3.40.640.10; | Class-III pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=a 2-oxocarboxylate + L-ornithine = an L-alpha-amino acid + L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:13877, ChEBI:CHEBI:35179, ChEBI:CHEBI:46911, ChEBI:CHEBI:58066, ChEBI:CHEBI:59869; EC=2.6.1.13; Evidence={ECO:0000305|PubMed:3036506}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:1... | null | PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-ornithine: step 1/1. {ECO:0000305|PubMed:3036506}. | null | null | FUNCTION: Catalyzes the transamination of ornithine into L-glutamate gamma-semialdehyde, the second step of arginine degradation. {ECO:0000305|PubMed:3036506}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07992 | ERCC1_HUMAN | MDPGKDKEGVPQPSGPPARKKFVIPLDEDEVPPGVAKPLFRSTQSLPTVDTSAQAAPQTYAEYAISQPLEGAGATCPTGSEPLAGETPNQALKPGAKSNSIIVSPRQRGNPVLKFVRNVPWEFGDVIPDYVLGQSTCALFLSLRYHNLHPDYIHGRLQSLGKNFALRVLLVQVDVKDPQQALKELAKMCILADCTLILAWSPEEAGRYLETYKAYEQKPADLLMEKLEQDFVSRVTECLTTVKSVNKTDSQTLLTTFGSLEQLIAASREDLALCPGLGPQKARRLFDVLHEPFLKVP | null | null | cell population proliferation [GO:0008283]; determination of adult lifespan [GO:0008340]; DNA repair [GO:0006281]; double-strand break repair via nonhomologous end joining [GO:0006303]; embryonic organ development [GO:0048568]; insulin-like growth factor receptor signaling pathway [GO:0048009]; interstrand cross-link r... | chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; ERCC4-ERCC1 complex [GO:0070522]; nucleoplasm [GO:0005654]; nucleotide-excision repair complex [GO:0000109]; nucleotide-excision repair factor 1 complex [GO:0000110] | damaged DNA binding [GO:0003684]; promoter-specific chromatin binding [GO:1990841]; single-stranded DNA binding [GO:0003697]; TFIID-class transcription factor complex binding [GO:0001094] | PF14520;PF03834; | 3.40.50.10130;1.10.150.20; | ERCC1/RAD10/SWI10 family | PTM: Ubiquitinated with both 'Lys-48' and 'Lys-63' linkages (PubMed:25538220). Deubiquitinated by USP45 (PubMed:25538220). {ECO:0000269|PubMed:25538220}. | SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000269|PubMed:24036546}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:24036546}. Nucleus {ECO:0000269|PubMed:24036546}.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus {ECO:0000269|PubMed:24036546}.; SUBCELLULAR LOCATION: [Isoform 4]: Nucleus {ECO:000026... | null | null | null | null | null | FUNCTION: [Isoform 1]: Non-catalytic component of a structure-specific DNA repair endonuclease responsible for the 5'-incision during DNA repair. Responsible, in conjunction with SLX4, for the first step in the repair of interstrand cross-links (ICL). Participates in the processing of anaphase bridge-generating DNA str... | Homo sapiens (Human) |
P07995 | INHBA_BOVIN | MPLLWLRGFLLASCWIIVRSSPTPGSEGHSAAPDCPSCALATLPKDVPNSQPEMVEAVKKHILNMLHLKKRPDVTQPVPKAALLNAIRKLHVGKVGENGYVEIEDDIGRRAEMNELMEQTSEIITFAESGTARKTLHFEISKEGSDLSVVERAEIWLFLKVPKANRTRSKVTIRLFQQQKHLQGSLDAGEEAEEVGLKGEKSEMLISEKVVDARKSTWHIFPVSSCIQRLLDQGKSSLDIRIACEQCQETGASLVLLGKKKKKEEEGEGKKRDGEGGAGGDEEKEQSHRPFLMLQARQSEDHPHRRRRRGLECDGKVNIC... | null | null | activin receptor signaling pathway [GO:0032924]; eyelid development in camera-type eye [GO:0061029]; hair follicle development [GO:0001942]; hematopoietic progenitor cell differentiation [GO:0002244]; hemoglobin biosynthetic process [GO:0042541]; male gonad development [GO:0008584]; negative regulation of cell growth [... | activin A complex [GO:0043509]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; inhibin A complex [GO:0043512] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; hormone activity [GO:0005179]; identical protein binding [GO:0042802]; peptide hormone binding [GO:0017046] | PF00019;PF00688; | 2.60.120.970;2.10.90.10; | TGF-beta family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, eryth... | Bos taurus (Bovine) |
P07996 | TSP1_HUMAN | MGLAWGLGVLFLMHVCGTNRIPESGGDNSVFDIFELTGAARKGSGRRLVKGPDPSSPAFRIEDANLIPPVPDDKFQDLVDAVRAEKGFLLLASLRQMKKTRGTLLALERKDHSGQVFSVVSNGKAGTLDLSLTVQGKQHVVSVEEALLATGQWKSITLFVQEDRAQLYIDCEKMENAELDVPIQSVFTRDLASIARLRIAKGGVNDNFQGVLQNVRFVFGTTPEDILRNKGCSSSTSVLLTLDNNVVNGSSPAIRTNYIGHKTKDLQAICGISCDELSSMVLELRGLRTIVTTLQDSIRKVTEENKELANELRRPPLCYH... | null | null | apoptotic process [GO:0006915]; behavioral response to pain [GO:0048266]; cell adhesion [GO:0007155]; cell migration [GO:0016477]; cellular response to growth factor stimulus [GO:0071363]; cellular response to heat [GO:0034605]; cellular response to tumor necrosis factor [GO:0071356]; chronic inflammatory response [GO:... | cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extrace... | calcium ion binding [GO:0005509]; collagen V binding [GO:0070052]; endopeptidase inhibitor activity [GO:0004866]; extracellular matrix structural constituent [GO:0005201]; fibrinogen binding [GO:0070051]; fibroblast growth factor binding [GO:0017134]; fibronectin binding [GO:0001968]; heparin binding [GO:0008201]; inte... | PF12947;PF00090;PF02412;PF05735;PF00093; | 2.60.120.200;6.20.200.20;2.10.25.10;2.20.100.10;4.10.1080.10; | Thrombospondin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:101549, ECO:0000269|PubMed:14568985, ECO:0000269|PubMed:6777381}. Cell surface {ECO:0000269|PubMed:6777381}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18285447, ECO:0000269|PubMed:6341993}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P354... | null | null | null | null | null | FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions (PubMed:15014436, PubMed:18285447, PubMed:2430973, PubMed:6489349). Multifunctional, involved in inflammation, angiogenesis, wound healing, reactive oxygen species (ROS) signaling, nitrous oxide (NO) signaling, apoptosis, senesce... | Homo sapiens (Human) |
P07997 | HEM1_CHICK | MEAVVRRCPFLARVSQAFLQKAGPSLLFYAQHCPKMMEAAPPAAARGLATSASRGQQVEETPAAQPEAKKAKEVAQQNTDGSQPPAGHPPAAAVQSSATKCPFLAAQMNHKSSNVFCKASLELQEDVKEMQVDRKGKEFAKIPTNSVVRNTEAEGEEQSGLLKKFKDIMLKQRPESVSHLLQDNLPKSVSTFQYDQFFEKKIDEKKKDHTYRVFKTVNRKAQIFPMADDYSDSLITKKEVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLEKELADLHGKDAALLFSSCFVANDSTLFTLAK... | 2.3.1.37 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P13196}; | erythrocyte development [GO:0048821]; heme biosynthetic process [GO:0006783]; hemoglobin biosynthetic process [GO:0042541]; protoporphyrinogen IX biosynthetic process [GO:0006782]; response to bile acid [GO:1903412] | cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | 5-aminolevulinate synthase activity [GO:0003870]; pyridoxal phosphate binding [GO:0030170] | PF00155;PF09029; | 3.90.1150.10;3.40.640.10; | Class-II pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P22557}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22557}. Note=Localizes to the matrix side of the mitochondrion inner membrane. {ECO:0000250|UniProtKB:P22557}. | CATALYTIC ACTIVITY: Reaction=glycine + H(+) + succinyl-CoA = 5-aminolevulinate + CO2 + CoA; Xref=Rhea:RHEA:12921, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:57305, ChEBI:CHEBI:356416; EC=2.3.1.37; Evidence={ECO:0000250|UniProtKB:P13196}; PhysiologicalDirection=left-to-right;... | null | PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1. | null | null | FUNCTION: Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products. {ECO:0000250|UniProtKB:P13196}. | Gallus gallus (Chicken) |
P07998 | RNAS1_HUMAN | MALEKSLVRLLLLVLILLVLGWVQPSLGKESRAKKFQRQHMDSDSSPSSSSTYCNQMMRRRNMTQGRCKPVNTFVHEPLVDVQNVCFQEKVTCKNGQGNCYKSNSSMHITDCRLTNGSRYPNCAYRTSPKERHIIVACEGSPYVPVHFDASVEDST | 4.6.1.18 | null | defense response to Gram-positive bacterium [GO:0050830] | extracellular exosome [GO:0070062] | lyase activity [GO:0016829]; nucleic acid binding [GO:0003676]; ribonuclease A activity [GO:0004522]; RNA nuclease activity [GO:0004540] | PF00074; | 3.10.130.10; | Pancreatic ribonuclease family | PTM: N-linked glycans are of complex type. {ECO:0000269|PubMed:3202829}. | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18; CATALYTIC ACTIVITY: Reaction=an [RNA] containing uridine + H2O = an [RNA]-3'-uridine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18; | null | null | null | null | FUNCTION: Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA. {ECO:0000269|PubMed:17350650}. | Homo sapiens (Human) |
P08001 | ACRO_PIG | MLPTAVLLVLAVSVAARDNATCDGPCGLRFRQKLESGMRVVGGMSAEPGAWPWMVSLQIFMYHNNRRYHTCGGILLNSHWVLTAAHCFKNKKKVTDWRLIFGANEVVWGSNKPVKPPLQERFVEEIIIHEKYVSGLEINDIALIKITPPVPCGPFIGPGCLPQFKAGPPRAPQTCWVTGWGYLKEKGPRTSPTLQEARVALIDLELCNSTRWYNGRIRSTNVCAGYPRGKIDTCQGDSGGPLMCRDRAENTFVVVGITSWGVGCARAKRPGVYTSTWPYLNWIASKIGSNALQMVQLGTPPRPSTPAPPVRPPSVQTPVR... | 3.4.21.10 | null | acrosome reaction [GO:0007340]; activation of adenylate cyclase activity [GO:0007190]; proteolysis [GO:0006508]; single fertilization [GO:0007338] | acrosomal matrix [GO:0043159]; protein-containing complex [GO:0032991] | amidase activity [GO:0004040]; fucose binding [GO:0042806]; mannose binding [GO:0005537]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236] | PF00089; | 2.40.10.10; | Peptidase S1 family | null | null | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.10; | null | null | null | null | FUNCTION: Acrosin is the major protease of mammalian spermatozoa. It is a serine protease of trypsin-like cleavage specificity, it is synthesized in a zymogen form, proacrosin and stored in the acrosome. | Sus scrofa (Pig) |
P08003 | PDIA4_MOUSE | MKLRKAWLLVLLLALTQLLAAASAGDAHEDTSDTENATEEEEEEDDDDLEVKEENGVWVLNDGNFDNFVADKDTVLLEFYAPWCGHCKQFAPEYEKIASTLKDNDPPIAVAKIDATSASMLASKFDVSGYPTIKILKKGQAVDYDGSRTQEEIVAKVREVSQPDWTPPPEVTLSLTKDNFDDVVNNADIILVEFYAPWCGHCKKLAPEYEKAAKELSKRSPPIPLAKVDATEQTDLAKRFDVSGYPTLKIFRKGRPFDYNGPREKYGIVDYMIEQSGPPSKEILTLKQVQEFLKDGDDVVIIGLFQGDGDPAYLQYQDAA... | 5.3.4.1 | null | blood coagulation, fibrin clot formation [GO:0072378]; chaperone-mediated protein folding [GO:0061077]; platelet aggregation [GO:0070527]; positive regulation of protein folding [GO:1903334]; protein folding [GO:0006457]; response to endoplasmic reticulum stress [GO:0034976] | cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum chaperone complex [GO:0034663]; endoplasmic reticulum lumen [GO:0005788]; melanosome [GO:0042470]; smooth endoplasmic reticulum [GO:0005790] | integrin binding [GO:0005178]; protein disulfide isomerase activity [GO:0003756] | PF00085;PF13848; | 3.40.30.10; | Protein disulfide isomerase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P13667}. Melanosome {ECO:0000250|UniProtKB:P13667}. | CATALYTIC ACTIVITY: Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; EC=5.3.4.1; Evidence={ECO:0000305|PubMed:23956175}; | null | null | null | null | null | Mus musculus (Mouse) |
P08004 | CHS1_YEAST | MSDQNNRSRNEYHSNRKNEPSYELQNAHSGLFHSSNEELTNRNQRYTNQNASMGSFTPVQSLQFPEQSQQTNMLYNGDDGNNNTINDNERDIYGGFVNHHRQRPPPATAEYNDVFNTNSQQLPSEHQYNNVPSYPLPSINVIQTTPELIHNGSQTMATPIERPFFNENDYYYNNRNSRTSPSIASSSDGYADQEARPILEQPNNNMNSGNIPQYHDQPFGYNNGYHGLQAKDYYDDPEGGYIDQRGDDYQINSYLGRNGEMVDPYDYENSLRHMTPMERREYLHDDSRPVNDGKEELDSVKSGYSHRDLGEYDKDDFSRD... | 2.4.1.16 | null | cell wall chitin biosynthetic process [GO:0006038]; cell wall organization [GO:0071555]; septum digestion after cytokinesis [GO:0000920] | cell periphery [GO:0071944]; cell septum [GO:0030428]; chitosome [GO:0045009]; plasma membrane [GO:0005886] | chitin synthase activity [GO:0004100] | PF01644;PF08407; | null | Chitin synthase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:2523889}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9595, ChEBI:CHEBI:15378, ChEBI:CHEBI:17029, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223; EC=2.4.1.16; | null | null | null | null | FUNCTION: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer (PubMed:2941152). Required for mitotic division septum formation during adverse conditions (PubMed:2523889). {ECO:0000269|PubMed:2523889, E... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P08009 | GSTM7_RAT | MPMTLGYWDIRGLAHAIRLLLEYTDSSYEEKRYTMGDAPDFDRSQWLNEKFKLGLDFPNLPYLIDGSHKITQSNAILRYLGRKHNLCGETEEERIRVDILENQLMDNRMVLARLCYNPDFEKLKPGYLEQLPGMMRLYSEFLGKRPWFAGDKITFVDFIAYDVLERNQVFEATCLDAFPNLKDFIARFEGLKKISDYMKSSRFLPRPLFTKMAIWGSK | 2.5.1.18 | null | cellular detoxification of nitrogen compound [GO:0070458]; cellular response to caffeine [GO:0071313]; glutathione metabolic process [GO:0006749]; hepoxilin biosynthetic process [GO:0051122]; linoleic acid metabolic process [GO:0043651]; nitrobenzene metabolic process [GO:0018916]; regulation of release of sequestered ... | cytosol [GO:0005829]; intercellular bridge [GO:0045171]; sarcoplasmic reticulum [GO:0016529] | enzyme binding [GO:0019899]; fatty acid binding [GO:0005504]; glutathione binding [GO:0043295]; glutathione peroxidase activity [GO:0004602]; glutathione transferase activity [GO:0004364]; protein homodimerization activity [GO:0042803]; signaling receptor binding [GO:0005102] | PF00043;PF02798; | 1.20.1050.10;3.40.30.10; | GST superfamily, Mu family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28161}. | CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000250|UniProtKB:P28161}; | null | null | null | null | FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. {ECO:0000250|UniProtKB:P28161}. | Rattus norvegicus (Rat) |
P08010 | GSTM2_RAT | MPMTLGYWDIRGLAHAIRLFLEYTDTSYEDKKYSMGDAPDYDRSQWLSEKFKLGLDFPNLPYLIDGSHKITQSNAILRYLGRKHNLCGETEEERIRVDVLENQAMDTRLQLAMVCYSPDFERKKPEYLEGLPEKMKLYSEFLGKQPWFAGNKITYVDFLVYDVLDQHRIFEPKCLDAFPNLKDFVARFEGLKKISDYMKSGRFLSKPIFAKMAFWNPK | 2.5.1.18 | null | cellular detoxification of nitrogen compound [GO:0070458]; cellular response to caffeine [GO:0071313]; glutathione metabolic process [GO:0006749]; hepoxilin biosynthetic process [GO:0051122]; linoleic acid metabolic process [GO:0043651]; nitrobenzene metabolic process [GO:0018916]; regulation of release of sequestered ... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; protein-containing complex [GO:0032991]; sarcoplasmic reticulum [GO:0016529] | enzyme binding [GO:0019899]; fatty acid binding [GO:0005504]; glutathione binding [GO:0043295]; glutathione peroxidase activity [GO:0004602]; glutathione transferase activity [GO:0004364]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; signaling receptor binding [GO:0005102] | PF00043;PF02798; | 1.20.1050.10;3.40.30.10; | GST superfamily, Mu family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000250|UniProtKB:P28161}; PhysiologicalDirection=left-to-right; Xref=Rhea... | null | null | null | null | FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Participates in the formation of novel hepoxilin regioisomers. {ECO:0000250|UniProtKB:P28161}. | Rattus norvegicus (Rat) |
P08011 | MGST1_RAT | MADLKQLMDNEVLMAFTSYATIILAKMMFLSSATAFQRLTNKVFANPEDCAGFGKGENAKKFLRTDEKVERVRRAHLNDLENIVPFLGIGLLYSLSGPDLSTALIHFRIFVGARIYHTIAYLTPLPQPNRGLAFFVGYGVTLSMAYRLLRSRLYL | 2.5.1.18 | null | cellular response to lipid hydroperoxide [GO:0071449]; glutathione metabolic process [GO:0006749]; glutathione transport [GO:0034635]; Leydig cell differentiation [GO:0033327]; response to lipopolysaccharide [GO:0032496]; response to organonitrogen compound [GO:0010243]; response to xenobiotic stimulus [GO:0009410] | apical part of cell [GO:0045177]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; peroxisomal membrane [GO:0005778] | glutathione binding [GO:0043295]; glutathione peroxidase activity [GO:0004602]; glutathione transferase activity [GO:0004364]; identical protein binding [GO:0042802] | PF01124; | 1.20.120.550; | MAPEG family | PTM: In vitro, peroxynitrite induces nitration at Tyr-93 which activates the enzyme. {ECO:0000269|PubMed:16314419}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:6439207}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000269|PubMed:6439207}. | CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000269|PubMed:11106493, ECO:0000269|PubMed:16314419, ECO:0000269|PubMed:1... | null | null | null | null | FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. {ECO:0000269|PubMed:11106493, ECO:0000269|PubMed:16314419}. | Rattus norvegicus (Rat) |
P08018 | PBS2_YEAST | MEDKFANLSLHEKTGKSSIQLNEQTGSDNGSAVKRTSSTSSHYNNINADLHARVKAFQEQRALKRSASVGSNQSEQDKGSSQSPKHIQQIVNKPLPPLPVAGSSKVSQRMSSQVVQASSKSTLKNVLDNQETQNITDVNINIDTTKITATTIGVNTGLPATDITPSVSNTASATHKAQLLNPNRRAPRRPLSTQHPTRPNVAPHKAPAIINTPKQSLSARRGLKLPPGGMSLKMPTKTAQQPQQFAPSPSNKKHIETLSNSKVVEGKRSNPGSLINGVQSTSTSSSTEGPHDTVGTTPRTGNSNNSSNSGSSGGGGLFAN... | 2.7.12.2 | null | actin filament organization [GO:0007015]; cellular hyperosmotic response [GO:0071474]; hyperosmotic response [GO:0006972]; MAPK cascade [GO:0000165]; osmosensory signaling pathway [GO:0007231]; protein import into nucleus [GO:0006606]; protein phosphorylation [GO:0006468]; response to antibiotic [GO:0046677] | cellular bud neck [GO:0005935]; cellular bud tip [GO:0005934]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; NatB complex [GO:0031416] | ATP binding [GO:0005524]; MAP kinase kinase activity [GO:0004708]; MAP-kinase scaffold activity [GO:0005078]; peptide alpha-N-acetyltransferase activity [GO:0004596]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosin... | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase subfamily | PTM: Activated by phosphorylation by SSK2 or SSK22. Ser/Thr phosphorylation is also necessary for SHO1-mediated activation. {ECO:0000269|PubMed:7624781}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. | 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=2.7.12.2; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Seems to phosphorylate HOG1 on a tyrosine residue. {ECO:0000269|PubMed:10970855, ECO:0000269|PubMed:15256499, ECO:0000269|PubMed:7681220}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P08021 | FMRF_APLCA | MRPWCQLALLACLSLKWLTSHVTAESFLCDDSELCENGYLRFGRSMSVEEPHFRLERRSYPPVVYHKRFLRFGRSQEPDIEDYARAIALIESEEPLYRKRRSADADGQSEKVLHRARREAESEHKSLEEVSPDTKQDVEKRDADDVLDAEKRFMRFGKRFMRFGRGSSDDDESGDDDVQDLTDIGDGLGGEGEVNKRFMRFGKRFMRFGKREDGEPDKRFMRFGKSMADNDLDKRFMRFGKRFMRFGKSLPDSEVDKRFMRFGKSVDGDVDKRFMRFGKSVDGDVDKRFMRFGKSVDGDVDKRFMRFGKSVDGDVDKRFM... | null | null | neuropeptide signaling pathway [GO:0007218] | extracellular region [GO:0005576] | null | PF01581; | null | FARP (FMRFamide related peptide) family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: FMRFamide induces contractions in visceral and somatic musculature as well as in the heart. | Aplysia californica (California sea hare) |
P08023 | ACTA_CHICK | MCEEEDSTALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILSERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEIT... | 3.6.4.- | null | mesenchyme migration [GO:0090131]; positive regulation of gene expression [GO:0010628] | cell body [GO:0044297]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extracellular space [GO:0005615]; filopodium [GO:0030175]; lamellipodium [GO:0030027] | ATP binding [GO:0005524]; hydrolase activity [GO:0016787] | PF00022; | 3.30.420.40; | Actin family | PTM: [Actin, aortic smooth muscle, intermediate form]: N-terminal cleavage of acetylated cysteine of intermediate muscle actin by ACTMAP. {ECO:0000250|UniProtKB:P62737}.; PTM: Oxidation of Met-46 and Met-49 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P68137}; | null | null | null | null | FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. | Gallus gallus (Chicken) |
P08025 | IGF1_RAT | MGKISSLPTQLFKICLCDFLKIKIHIMSSSHLFYLALCLLTFTSSATAGPETLCGAELVDALQFVCGPRGFYFNKPTGYGSSIRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPTKSARSIRAQRHTDMPKTQKEVHLKNTSRGSAGNKTYRM | null | null | androgen receptor signaling pathway [GO:0030521]; blood vessel remodeling [GO:0001974]; bone development [GO:0060348]; bone mineralization involved in bone maturation [GO:0035630]; branching morphogenesis of an epithelial tube [GO:0048754]; cardiac atrium development [GO:0003230]; cell activation [GO:0001775]; cell dev... | alphav-beta3 integrin-IGF-1-IGF1R complex [GO:0035867]; exocytic vesicle [GO:0070382]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; insulin-like growth factor ternary complex [GO:0042567]; interstitial matrix [GO:0005614]; neuronal cell body [GO:0043025]; neuronal dense core vesicle lumen [GO:0... | growth factor activity [GO:0008083]; hormone activity [GO:0005179]; insulin receptor binding [GO:0005158]; insulin-like growth factor receptor binding [GO:0005159]; integrin binding [GO:0005178]; protein serine/threonine kinase activator activity [GO:0043539]; receptor ligand activity [GO:0048018]; steroid binding [GO:... | 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... | Rattus norvegicus (Rat) |
P08030 | APT_MOUSE | MSEPELKLVARRIRSFPDFPIPGVLFRDISPLLKDPDSFRASIRLLASHLKSTHSGKIDYIAGLDSRGFLFGPSLAQELGVGCVLIRKQGKLPGPTVSASYSLEYGKAELEIQKDALEPGQRVVIVDDLLATGGTMFAACDLLHQLRAEVVECVSLVELTSLKGRERLGPIPFFSLLQYD | 2.4.2.7 | null | adenine metabolic process [GO:0046083]; adenine salvage [GO:0006168]; AMP salvage [GO:0044209]; GMP salvage [GO:0032263]; grooming behavior [GO:0007625]; IMP salvage [GO:0032264]; lactation [GO:0007595]; purine ribonucleoside salvage [GO:0006166] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654] | adenine binding [GO:0002055]; adenine phosphoribosyltransferase activity [GO:0003999]; AMP binding [GO:0016208] | PF00156; | 3.40.50.2020; | Purine/pyrimidine phosphoribosyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine; Xref=Rhea:RHEA:16609, ChEBI:CHEBI:16708, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:456215; EC=2.4.2.7; Evidence={ECO:0000250|UniProtKB:P07741}; | null | PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1. {ECO:0000250|UniProtKB:P07741}. | null | null | FUNCTION: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. {ECO:0000250|UniProtKB:P07741}. | Mus musculus (Mouse) |
P08032 | SPTA1_MOUSE | METPKETAVESSGPKVLETAEEIQHRRAEVLNQYQRFKDRVAERGQKLEESYHYQVFRRDADDLEKWIMEKLEIAKDKTYEPTNIQGKYQKHESFVSEVQAKSRVLPELEEIREARFAEDHFAHEATKTHLKQLRLLWDLLLELTQEKSDVLLRALKFYQYSQECEDILEWVKEKEAIVTLVELGDDWERTEVLHKKFEEFQEELTARKGKVDRVNQYANECAQEKHPKLPEIKAKQDEVNAAWDRLWSLALKRRESLSNAADLQRFKRDVNEAIQWMEEKEPQLTSEDYGKDLVSSEALFHNHKRLERNLAVMDDKVKE... | null | null | actin cytoskeleton organization [GO:0030036]; actin filament bundle assembly [GO:0051017]; actin filament capping [GO:0051693]; hemopoiesis [GO:0030097]; lymphocyte homeostasis [GO:0002260]; plasma membrane organization [GO:0007009]; porphyrin-containing compound biosynthetic process [GO:0006779]; positive regulation o... | actin filament bundle [GO:0032432]; actomyosin contractile ring [GO:0005826]; axon [GO:0030424]; cell junction [GO:0030054]; cell projection [GO:0042995]; cortical actin cytoskeleton [GO:0030864]; cortical cytoskeleton [GO:0030863]; cuticular plate [GO:0032437]; cytoplasmic side of plasma membrane [GO:0009898]; membran... | actin filament binding [GO:0051015]; actin lateral binding [GO:0003786]; calcium ion binding [GO:0005509] | PF08726;PF00018;PF00435; | 1.20.5.170;1.20.58.60;1.10.238.10;2.30.30.40; | Spectrin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. | null | null | null | null | null | FUNCTION: Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. | Mus musculus (Mouse) |
P08033 | CXB1_RAT | MNWTGLYTLLSGVNRHSTAIGRVWLSVIFIFRIMVLVVAAESVWGDEKSSFICNTLQPGCNSVCYDHFFPISHVRLWSLQLILVSTPALLVAMHVAHQQHIEKKMLRLEGHGDPLHLEEVKRHKVHISGTLWWTYVISVVFRLLFEAVFMYVFYLLYPGYAMVRLVKCEAFPCPNTVDCFVSRPTEKTVFTVFMLAASGICIILNVAEVVYLIIRACARRAQRRSNPPSRKGSGFGHRLSPEYKQNEINKLLSEQDGSLKDILRRSPGTGAGLAEKSDRCSAC | null | null | cell-cell signaling [GO:0007267]; epididymis development [GO:1905867]; purine ribonucleotide transport [GO:0015868] | connexin complex [GO:0005922]; cytoplasm [GO:0005737]; gap junction [GO:0005921]; lateral plasma membrane [GO:0016328]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | gap junction channel activity [GO:0005243]; identical protein binding [GO:0042802] | PF00029; | 1.20.1440.80; | Connexin family, Beta-type (group I) subfamily | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction. | null | null | null | null | null | FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. | Rattus norvegicus (Rat) |
P08034 | CXB1_HUMAN | MNWTGLYTLLSGVNRHSTAIGRVWLSVIFIFRIMVLVVAAESVWGDEKSSFICNTLQPGCNSVCYDQFFPISHVRLWSLQLILVSTPALLVAMHVAHQQHIEKKMLRLEGHGDPLHLEEVKRHKVHISGTLWWTYVISVVFRLLFEAVFMYVFYLLYPGYAMVRLVKCDVYPCPNTVDCFVSRPTEKTVFTVFMLAASGICIILNVAEVVYLIIRACARRAQRRSNPPSRKGSGFGHRLSPEYKQNEINKLLSEQDGSLKDILRRSPGTGAGLAEKSDRCSAC | null | null | cell-cell signaling [GO:0007267]; epididymis development [GO:1905867]; gap junction assembly [GO:0016264]; nervous system development [GO:0007399]; purine ribonucleotide transport [GO:0015868] | connexin complex [GO:0005922]; endoplasmic reticulum membrane [GO:0005789]; lateral plasma membrane [GO:0016328] | gap junction channel activity [GO:0005243]; identical protein binding [GO:0042802] | PF00029; | 1.20.1440.80; | Connexin family, Beta-type (group I) subfamily | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction. | null | null | null | null | null | FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. | Homo sapiens (Human) |
P08037 | B4GT1_BOVIN | MKFREPLLGGSAAMPGASLQRACRLLVAVCALHLGVTLVYYLAGRDLRRLPQLVGVHPPLQGSSHGAAAIGQPSGELRLRGVAPPPPLQNSSKPRSRAPSNLDAYSHPGPGPGPGSNLTSAPVPSTTTRSLTACPEESPLLVGPMLIEFNIPVDLKLVEQQNPKVKLGGRYTPMDCISPHKVAIIIPFRNRQEHLKYWLYYLHPILQRQQLDYGIYVINQAGESMFNRAKLLNVGFKEALKDYDYNCFVFSDVDLIPMNDHNTYRCFSQPRHISVAMDKFGFSLPYVQYFGGVSALSKQQFLSINGFPNNYWGWGGEDDD... | 2.4.1.-; 2.4.1.22; 2.4.1.275; 2.4.1.38; 2.4.1.90 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P15291}; | lactose biosynthetic process [GO:0005989]; lipid metabolic process [GO:0006629]; oligosaccharide biosynthetic process [GO:0009312]; positive regulation of circulating fibrinogen levels [GO:0061755]; protein galactosylation [GO:0042125]; protein N-linked glycosylation [GO:0006487] | basolateral plasma membrane [GO:0016323]; brush border membrane [GO:0031526]; desmosome [GO:0030057]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; filopodium [GO:0030175]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; Golgi trans cisterna [GO:0000138] | alpha-tubulin binding [GO:0043014]; beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity [GO:0003831]; beta-tubulin binding [GO:0048487]; cytoskeletal protein binding [GO:0008092]; identical protein binding [GO:0042802]; lactose synthase activity [GO:0004461]; manganese ion binding [GO:0030145]... | PF02709;PF13733; | null | Glycosyltransferase 7 family | PTM: The soluble form derives from the membrane forms by proteolytic processing. | SUBCELLULAR LOCATION: [Isoform Long]: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:P15535}; Single-pass type II membrane protein. Cell membrane; Single-pass type II membrane protein. Cell surface. Cell projection, filopodium {ECO:0000250|UniProtKB:P15535}. Note=Found in trans cisternae of Golgi. B4GALT1... | CATALYTIC ACTIVITY: Reaction=D-glucose + UDP-alpha-D-galactose = H(+) + lactose + UDP; Xref=Rhea:RHEA:12404, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:17716, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.22; Evidence={ECO:0000269|PubMed:12927542, ECO:0000269|PubMed:9405390}; PhysiologicalDirection=left-to-right... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.034 mM for UDP-galactose {ECO:0000269|PubMed:9405390}; KM=0.53 mM for benzyl-beta-D-GlcNAc {ECO:0000269|PubMed:9405390}; KM=9.6 mM for D-GlcNAc {ECO:0000269|PubMed:9405390}; Vmax=73 pmol/min/mg enzyme towards UDP-galactose {ECO:0000269|PubMed:9405390}; Vmax=44.1 ... | PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:9405390}. | null | null | FUNCTION: [Beta-1,4-galactosyltransferase 1]: The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. {ECO:0000269|PubMed... | Bos taurus (Bovine) |
P08044 | SNAI_DROME | MAANYKSCPLKKRPIVFVEERLPQTEALALTKDSQFAQDQPQDLSLKRGRDEETQDYQQPEPKRDYVLNLSKTPERNSSSSSNSCLLSPPVEAQDYLPTEIHMRGLTAGTTGYTTATPTTINPFQSAFVMAAGCNPISALWSSYQPHLAAFPSPASSMASPQSVYSYQQMTPPSSPGSDLETGSEPEDLSVRNDIPLPALFHLFDEAKSSSSGASVSSSSGYSYTPAMSASSASVAANHAKNYRFKCDECQKMYSTSMGLSKHRQFHCPAAECNQEKKTHSCEECGKLYTTIGALKMHIRTHTLPCKCPICGKAFSRPWL... | null | null | asymmetric neuroblast division [GO:0055059]; central nervous system development [GO:0007417]; compound eye development [GO:0048749]; ectoderm and mesoderm interaction [GO:0007499]; gastrulation involving germ band extension [GO:0010004]; Malpighian tubule morphogenesis [GO:0007443]; mesoderm development [GO:0007498]; n... | 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]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulat... | PF00096; | 3.30.160.60; | Snail C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Essential for the correct specification of ventral-dorsal patterns. | Drosophila melanogaster (Fruit fly) |
P08046 | EGR1_MOUSE | MAAAKAEMQLMSPLQISDPFGSFPHSPTMDNYPKLEEMMLLSNGAPQFLGAAGTPEGSGGNSSSSTSSGGGGGGGSNSGSSAFNPQGEPSEQPYEHLTTESFSDIALNNEKAMVETSYPSQTTRLPPITYTGRFSLEPAPNSGNTLWPEPLFSLVSGLVSMTNPPTSSSSAPSPAASSSSSASQSPPLSCAVPSNDSSPIYSAAPTFPTPNTDIFPEPQSQAFPGSAGTALQYPPPAYPATKGGFQVPMIPDYLFPQQQGDLSLGTPDQKPFQGLENRTQQPSLTPLSTIKAFATQSGSQDLKALNTTYQSQLIKPSRMR... | null | null | BMP signaling pathway [GO:0030509]; cellular response to gamma radiation [GO:0071480]; cellular response to heparin [GO:0071504]; cellular response to interleukin-8 [GO:0098759]; cellular response to mycophenolic acid [GO:0071506]; cellular response to organic substance [GO:0071310]; circadian regulation of gene expres... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded DNA binding [GO:0003690]; double-stranded methylate... | PF11914;PF11928;PF00096; | 3.30.160.60; | EGR C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11100120, ECO:0000269|PubMed:15958557, ECO:0000269|PubMed:8336701}. Cytoplasm {ECO:0000250|UniProtKB:P18146}. | null | null | null | null | null | FUNCTION: Transcriptional regulator (PubMed:15958557, PubMed:8336701, PubMed:8703054). Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'(EGR-site) in the promoter region of target genes (PubMed:15958557, PubMed:2028256, PubMed:8703054, PubMed:8939742). Binds double-stranded target DNA, irrespective of the cy... | Mus musculus (Mouse) |
P08047 | SP1_HUMAN | MSDQDHSMDEMTAVVKIEKGVGGNNGGNGNGGGAFSQARSSSTGSSSSTGGGGQESQPSPLALLAATCSRIESPNENSNNSQGPSQSGGTGELDLTATQLSQGANGWQIISSSSGATPTSKEQSGSSTNGSNGSESSKNRTVSGGQYVVAAAPNLQNQQVLTGLPGVMPNIQYQVIPQFQTVDGQQLQFAATGAQVQQDGSGQIQIIPGANQQIITNRGSGGNIIAAMPNLLQQAVPLQGLANNVLSGQTQYVTNVPVALNGNITLLPVNSVSAATLTPSSQAVTISSSGSQESGSQPVTSGTTISSASLVSSQASSSSF... | null | null | cellular response to estrogen stimulus [GO:0071391]; cellular response to insulin stimulus [GO:0032869]; cellular response to wortmannin [GO:1904568]; cellular response to zinc ion starvation [GO:0034224]; positive regulation by host of viral transcription [GO:0043923]; positive regulation of amyloid-beta formation [GO... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; euchromatin [GO:0000791]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-DNA complex [GO:0032993]; transcription repressor complex [GO:0017053] | bHLH transcription factor binding [GO:0043425]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded DNA... | PF00096; | 3.30.160.60; | Sp1 C2H2-type zinc-finger protein family | PTM: Phosphorylated on multiple serine and threonine residues. Phosphorylation is coupled to ubiquitination, sumoylation and proteolytic processing. Phosphorylation on Ser-59 enhances proteolytic cleavage. Phosphorylation on Ser-7 enhances ubiquitination and protein degradation. Hyperphosphorylation on Ser-101 in respo... | SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear location is governed by glycosylated/phosphorylated states. Insulin promotes nuclear location, while glucagon favors cytoplasmic location. | null | null | null | null | null | FUNCTION: Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immun... | Homo sapiens (Human) |
P08048 | ZFY_HUMAN | MDEDEFELQPQEPNSFFDGIGADATHMDGDQIVVEIQEAVFVSNIVDSDITVHNFVPDDPDSVVIQDVVEDVVIEEDVQCSDILEEADVSENVIIPEQVLDSDVTEEVSLPHCTVPDDVLASDITSTSMSMPEHVLTSESMHVCDIGHVEHMVHDSVVEAEIITDPLTSDIVSEEVLVADCAPEAVIDASGISVDQQDNDKASCEDYLMISLDDAGKIEHDGSTGVTIDAESEMDPCKVDSTCPEVIKVYIFKADPGEDDLGGTVDIVESEPENDHGVELLDQNSSIRVPREKMVYMTVNDSQQEDEDLNVAEIADEVYM... | null | null | positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulato... | PF00096;PF13909;PF04704; | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family, ZFX/ZFY subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Probable transcriptional activator. Binds to the consensus sequence 5'-AGGCCY-3'. {ECO:0000269|PubMed:20028140}. | Homo sapiens (Human) |
P08049 | NEP_RABIT | MGRSESQMDITDINTPKPKKKQRWTPLEISLSVLVLLLTVIAVTMIALYATYDDGICKSSDCIKSAARLIQNMDATAEPCTDFFKYACGGWLKRNVIPETSSRYSNFDILRDELEVILKDVLQEPKTEDIVAVQKAKTLYRSCVNETAIDSRGGQPLLKLLPDVYGWPVATQNWEQTYGTSWSAEKSIAQLNSNYGKKVLINFFVGTDDKNSMNHIIHIDQPRLGLPSRDYYECTGIYKEACTAYVDFMIAVAKLIRQEEGLPIDENQISVEMNKVMELEKEIANATTKSEDRNDPMLLYNKMTLAQIQNNFSLEINGKP... | 3.4.24.11 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:3162886}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08473}; | amyloid-beta clearance [GO:0097242]; amyloid-beta metabolic process [GO:0050435]; bradykinin catabolic process [GO:0010815]; cellular response to cytokine stimulus [GO:0071345]; cellular response to UV-A [GO:0071492]; cellular response to UV-B [GO:0071493]; creatinine metabolic process [GO:0046449]; hormone catabolic p... | axon [GO:0030424]; brush border [GO:0005903]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; neuron projection terminus [GO:0044306]; plasma membrane [GO:0005886]; synapse [GO:0045202]; synaptic vesicle [GO:0008021] | metalloendopeptidase activity [GO:0004222]; peptide binding [GO:0042277]; zinc ion binding [GO:0008270] | PF01431;PF05649; | 3.40.390.10;1.10.1380.10; | Peptidase M13 family | PTM: Myristoylation is a determinant of membrane targeting. {ECO:0000250|UniProtKB:P08473}.; PTM: Glycosylation at Asn-628 is necessary both for surface expression and neutral endopeptidase activity. {ECO:0000250|UniProtKB:P08473}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08473}; Single-pass type II membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'.; EC=3.4.24.11; Evidence={ECO:0000269|PubMed:3162886}; CATALYTIC ACTIVITY: Reaction=H2O + substance P = L-Leu-L-Met-NH2 + substance P(1-9); Xref=Rhea:RHEA:71459, ChEBI:CHEBI:15377, ChEBI:... | null | null | null | null | FUNCTION: Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids (PubMed:3162886). Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Catalyzes cleavage of bradykinin, substance P and neurotensin pe... | Oryctolagus cuniculus (Rabbit) |
P08050 | CXA1_RAT | MGDWSALGKLLDKVQAYSTAGGKVWLSVLFIFRILLLGTAVESAWGDEQSAFRCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSVPTLLYLAHVFYVMRKEEKLNKKEEELKVAQTDGVNVEMHLKQIEIKKFKYGIEEHGKVKMRGGLLRTYIISILFKSVFEVAFLLIQWYIYGFSLSAVYTCKRDPCPHQVDCFLSRPTEKTIFIIFMLVVSLVSLALNIIELFYVFFKGVKDRVKGRSDPYHATTGPLSPSKDCGSPKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYSAEQNRM... | null | null | adult heart development [GO:0007512]; ATP transport [GO:0015867]; atrial ventricular junction remodeling [GO:0003294]; blood vessel morphogenesis [GO:0048514]; bone development [GO:0060348]; bone remodeling [GO:0046849]; cardiac conduction [GO:0061337]; cell communication by chemical coupling [GO:0010643]; cell communi... | apical plasma membrane [GO:0016324]; cell junction [GO:0030054]; cell-cell contact zone [GO:0044291]; cell-cell junction [GO:0005911]; connexin complex [GO:0005922]; contractile fiber [GO:0043292]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; endoplasmic reticulum membrane [GO:0005789]; en... | beta-catenin binding [GO:0008013]; beta-tubulin binding [GO:0048487]; connexin binding [GO:0071253]; disordered domain specific binding [GO:0097718]; efflux transmembrane transporter activity [GO:0015562]; gap junction channel activity [GO:0005243]; gap junction channel activity involved in cell communication by electr... | PF00029;PF03508; | 1.20.5.1130;1.20.1440.80; | Connexin family, Alpha-type (group II) subfamily | PTM: Contains at least one intramolecular disulfide bond.; PTM: Phosphorylation at Ser-325, Ser-328 and Ser-330 by CK1 modulates gap junction assembly. Phosphorylated at Ser-368 by PRKCG; phosphorylation induces disassembly of gap junction plaques and inhibition of gap junction activity (By similarity). Phosphorylation... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18636092}; Multi-pass membrane protein {ECO:0000255}. Cell junction, gap junction {ECO:0000269|PubMed:15213231, ECO:0000269|PubMed:18636092, ECO:0000269|PubMed:2472402}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P23242}. Note=Localizes at the intercalated disk ... | null | null | null | null | null | FUNCTION: Gap junction protein that acts as a regulator of bladder capacity. A gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. Negative regulator of bladder functional capacity: acts by en... | Rattus norvegicus (Rat) |
P08057 | TNNI3_BOVIN | MADRSGGSTAGDTVPAPPPVRRRSSANYRAYATEPHAKKKSKISASRKLQLKTLMLQIAKQELEREAEERRGEKGRALSTRCQPLELAGLGFAELQDLCRQLHARVDKVDEERYDVEAKVTKNITEIADLNQKIFDLRGKFKRPTLRRVRISADAMMQALLGARAKETLDLRAHLKQVKKEDTEKENREVGDWRKNIDALSGMEGRKKKFEG | null | null | cardiac muscle contraction [GO:0060048]; skeletal muscle contraction [GO:0003009] | cardiac myofibril [GO:0097512]; cardiac Troponin complex [GO:1990584]; troponin complex [GO:0005861] | actin binding [GO:0003779]; ATP binding [GO:0005524]; ATPase inhibitor activity [GO:0042030]; magnesium ion binding [GO:0000287]; troponin C binding [GO:0030172] | PF00992;PF11636; | 1.20.5.350;6.10.250.180; | Troponin I family | PTM: Phosphorylated at Ser-24 and Ser-25 by PRKD1; phosphorylation reduces myofilament calcium sensitivity. Phosphorylated preferentially at Thr-33. Phosphorylation by STK4/MST1 alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylated at Ser-44 and Ser-46 by PRKCE; phosphorylation in... | null | null | null | null | null | null | FUNCTION: Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. | Bos taurus (Bovine) |
P08059 | G6PI_PIG | MAALTQNPQFKKLQTWYHEHRSDLNLRRLFEGDKDRFNHFSLNLNTNHGRILLDYSKNLVTEAVMQMLVDLAKSRGVEAARERMFNGEKINFTEDRAVLHVALRNRSNTPILVDGKDVMPEVNRVLEKMKSFCKRVRSGEWKGYSGKSITDVINIGIGGSDLGPLMVTEALKPYSAEGPRVWFVSNIDGTHIAKTLATLNPESSLFIIASKTFTTQETITNAETAKEWFLQSAKDPSAVAKHFVALSTNTTKVKEFGIDPQNMFEFWDWVGGRYSLWSAIGLSIALHVGFDNFEQLLSGAHWMDQHFRTTPLEKNAPVLL... | 5.3.1.9 | null | gluconeogenesis [GO:0006094]; glucose 6-phosphate metabolic process [GO:0051156]; glycolytic process [GO:0006096] | cytosol [GO:0005829]; extracellular space [GO:0005615] | carbohydrate derivative binding [GO:0097367]; cytokine activity [GO:0005125]; glucose-6-phosphate isomerase activity [GO:0004347]; monosaccharide binding [GO:0048029] | PF00342; | 1.10.1390.10; | GPI family | PTM: Phosphorylation at Ser-185 by CK2 has been shown to decrease enzymatic activity and may contribute to secretion by a non-classical secretory pathway. {ECO:0000250|UniProtKB:P06744}.; PTM: ISGylated. {ECO:0000250|UniProtKB:P06744}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06744}. Secreted {ECO:0000250|UniProtKB:P06744}. | CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate; Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225; EC=5.3.1.9; Evidence={ECO:0000250|UniProtKB:P06744}; | null | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4. {ECO:0000250|UniProtKB:P06744}. | null | null | FUNCTION: In the cytoplasm, catalyzes the conversion of glucose-6-phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis (By similarity). Besides it's role as a glycolytic enzyme, also acts as a secreted cytokine: acts as an angiogenic factor (AMF) that stimula... | Sus scrofa (Pig) |
P08067 | UCRI_YEAST | MLGIRSSVKTCFKPMSLTSKRLISQSLLASKSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAGAKSTVETFISSMTATADVLAMAKVEVNLAAIPLGKNVVVKWQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDPQWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGRIRKGPAPLNLEIPAYEFDGDKVIVG | 7.1.1.8 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:... | aerobic respiration [GO:0009060]; cellular respiration [GO:0045333]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122] | mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | 2 iron, 2 sulfur cluster binding [GO:0051537]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; ubiquinol-cytochrome-c reductase activity [GO:0008121] | PF00355;PF02921; | 2.102.10.10;1.20.5.270; | Rieske iron-sulfur protein family | PTM: Processed by both the mitochondrial processing peptidase (MPP) and the mitochondrial intermediate protease (MIP). Initially, MPP removes 22 amino acids from the newly imported precursor in the mitochondrial matrix. This proteolytic processing is then followed by a second proteolytic cleavage by MIP, which removes ... | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Single-pass membrane protein {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}. | CATALYTIC ACTIVITY: Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000... | null | null | null | null | FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P08069 | IGF1R_HUMAN | MKSGSGGGSPTSLWGLLFLSAALSLWPTSGEICGPGIDIRNDYQQLKRLENCTVIEGYLHILLISKAEDYRSYRFPKLTVITEYLLLFRVAGLESLGDLFPNLTVIRGWKLFYNYALVIFEMTNLKDIGLYNLRNITRGAIRIEKNADLCYLSTVDWSLILDAVSNNYIVGNKPPKECGDLCPGTMEEKPMCEKTTINNEYNYRCWTTNRCQKMCPSTCGKRACTENNECCHPECLGSCSAPDNDTACVACRHYYYAGVCVPACPPNTYRFEGWRCVDRDFCANILSAESSDSEGFVIHDGECMQECPSGFIRNGSQSMY... | 2.7.10.1 | null | amyloid-beta clearance [GO:0097242]; axonogenesis [GO:0007409]; cardiac atrium development [GO:0003230]; cellular response to aldosterone [GO:1904045]; cellular response to amyloid-beta [GO:1904646]; cellular response to angiotensin [GO:1904385]; cellular response to dexamethasone stimulus [GO:0071549]; cellular respon... | alphav-beta3 integrin-IGF-1-IGF1R complex [GO:0035867]; axon [GO:0030424]; caveola [GO:0005901]; insulin receptor complex [GO:0005899]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; protein kinase complex [GO:1902911]; recept... | ATP binding [GO:0005524]; G-protein alpha-subunit binding [GO:0001965]; identical protein binding [GO:0042802]; insulin binding [GO:0043559]; insulin receptor activity [GO:0005009]; insulin receptor binding [GO:0005158]; insulin receptor substrate binding [GO:0043560]; insulin-like growth factor binding [GO:0005520]; i... | PF00041;PF00757;PF07714;PF01030; | 2.60.40.10;3.80.20.20;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily | PTM: Autophosphorylated on tyrosine residues in response to ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Autophosphorylation occurs in a sequential manner; Tyr-1165 is predominantly phosphorylated first, followed by ... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17524361}; Single-pass type I membrane protein {ECO:0000269|PubMed:17524361}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Receptor tyrosine kinase which mediates actions of insulin-like growth factor 1 (IGF1). Binds IGF1 with high affinity and IGF2 and insulin (INS) with a lower affinity. The activated IGF1R is involved in cell growth and survival control. IGF1R is crucial for tumor transformation and survival of malignant cell.... | Homo sapiens (Human) |
P08071 | TRFL_MOUSE | MRLLIPSLIFLEALGLCLAKATTVQWCAVSNSEEEKCLRWQNEMRKVGGPPLSCVKKSSTRQCIQAIVTNRADAMTLDGGTMFDAGKPPYKLRPVAAEVYGTKEQPRTHYYAVAVVKNSSNFHLNQLQGLRSCHTGIGRSAGWKIPIGTLRPYLNWNGPPASLEEAVSKFFSKSCVPGAQKDRFPNLCSSCAGTGANKCASSPEEPYSGYAGALRCLRDNAGDVAFTRGSTVFEELPNKAERDQYKLLCPDNTWKPVTEYKECHLAQVPSHAVVSRSTNDKEEAIWELLRQSQEKFGKKQASGFQLFASPSGQKDLLFKE... | 3.4.21.- | null | antibacterial humoral response [GO:0019731]; antifungal humoral response [GO:0019732]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; bone morphogenesis [GO:0060349]; defense response to Gram-negative bacterium [GO:0050829]; innate immune response in mucosa [GO:0002227]; iron ion ... | cell surface [GO:0009986]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; recycling endosome [GO:0055037]; secretory granule [GO:0030141]; specific granule [GO:0042581] | cysteine-type endopeptidase inhibitor activity [GO:0004869]; heparin binding [GO:0008201]; iron ion binding [GO:0005506]; lipopolysaccharide binding [GO:0001530]; membrane destabilizing activity [GO:0140912]; peptidase activity [GO:0008233]; protein serine/threonine kinase activator activity [GO:0043539]; serine-type e... | PF00405; | 3.40.190.10; | Transferrin family | PTM: Poly-N-acetyllactosaminic carbohydrate moiety seems to be needed for TLR4 activation. {ECO:0000250|UniProtKB:P02788}. | SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule {ECO:0000250}. Note=Secreted into most exocrine fluids by various endothelial cells. Stored in the secondary granules of neutrophils (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. {ECO:0000250|UniProtKB:P02788}.; FUNCTION: [Lactotransferrin]: Major iron-binding and multifunctional protein found in exocrine fluids such as breast milk and mucos... | Mus musculus (Mouse) |
P08074 | CBR2_MOUSE | MKLNFSGLRALVTGAGKGIGRDTVKALHASGAKVVAVTRTNSDLVSLAKECPGIEPVCVDLGDWDATEKALGGIGPVDLLVNNAALVIMQPFLEVTKEAFDRSFSVNLRSVFQVSQMVARDMINRGVPGSIVNVSSMVAHVTFPNLITYSSTKGAMTMLTKAMAMELGPHKIRVNSVNPTVVLTDMGKKVSADPEFARKLKERHPLRKFAEVEDVVNSILFLLSDRSASTSGGGILVDAGYLAS | 1.1.1.184 | null | glucose metabolic process [GO:0006006]; NADH oxidation [GO:0006116]; xylulose metabolic process [GO:0005997] | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | carbonyl reductase (NADPH) activity [GO:0004090]; identical protein binding [GO:0042802]; L-xylulose reductase (NADP+) activity [GO:0050038]; protein self-association [GO:0043621] | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:8040004}. | CATALYTIC ACTIVITY: Reaction=a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH; Xref=Rhea:RHEA:19257, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087, ChEBI:CHEBI:35681, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.184; Evidence={ECO:0000269|PubMed:7705352}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19259; Evid... | null | null | null | null | FUNCTION: May function in the pulmonary metabolism of endogenous carbonyl compounds, such as aliphatic aldehydes and ketones derived from lipid peroxidation, 3-ketosteroids and fatty aldehydes, as well as in xenobiotic metabolism. {ECO:0000269|PubMed:7705352}. | Mus musculus (Mouse) |
P08081 | CLCA_RAT | MAELDPFGAPAGAPGGPALGNGVAGAGEEDPAAAFLAQQESEIAGIENDEAFAILDGGAPGPQAHGEPPGGPDAVDGVMNGEYYQESNGPTDSYAAISEVDRLQSEPESIRKWREEQTERLEALDANSRKQEAEWKEKAVKELEEWYARQDEQLQKTKASNRVADEAFYKQPFADVIGYVTNINHPCYSLEQAAEEAFVNDIDESSPGTEWERVARLCDFNPKSSKQAKDVSRMRSVLISLKQAPLVH | null | null | cell cycle [GO:0007049]; cell division [GO:0051301]; clathrin coat assembly [GO:0048268]; clathrin-dependent endocytosis [GO:0072583]; endocytosis [GO:0006897]; intracellular protein transport [GO:0006886] | clathrin coat [GO:0030118]; clathrin coat of coated pit [GO:0030132]; clathrin coat of trans-Golgi network vesicle [GO:0030130]; clathrin complex [GO:0071439]; clathrin vesicle coat [GO:0030125]; clathrin-coated endocytic vesicle membrane [GO:0030669]; clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:00301... | clathrin heavy chain binding [GO:0032050]; GTPase binding [GO:0051020]; peptide binding [GO:0042277]; protein-containing complex binding [GO:0044877]; structural molecule activity [GO:0005198] | PF01086; | null | Clathrin light chain family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P09496}. Note=Cytoplasmic face of coated pits and vesicles. In complex with TACC3 and CKAP5 (for... | null | null | null | null | null | FUNCTION: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Acts as a component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge (By similarity). {ECO:0000250|UniProtKB:P09496}. | Rattus norvegicus (Rat) |
P08082 | CLCB_RAT | MAEDFGFFSSSESGAPEAAEEDPAAAFLAQQESEIAGIENDSGFGAPAASQVASAQPGLASGGGSEDMGTTVNGDVFQEANGPADGYAAIAQADRLTQEPESIRKWREEQKKRLQELDAASKVTEQEWREKAKKDLEEWNQRQSEQVEKNKINNRIADKAFYQQPDADTIGYVASEEAFVKESKEETPGTEWEKVAQLCDFNPKSSKQCKDVSRLRSVLMSLKQTPLSR | null | null | clathrin-dependent endocytosis [GO:0072583]; intracellular protein transport [GO:0006886]; neurotransmitter secretion [GO:0007269]; neurotransmitter transport [GO:0006836]; synaptic vesicle coating [GO:0016183] | ciliary membrane [GO:0060170]; clathrin coat [GO:0030118]; clathrin coat of coated pit [GO:0030132]; clathrin coat of trans-Golgi network vesicle [GO:0030130]; clathrin vesicle coat [GO:0030125]; cytosol [GO:0005829]; plasma membrane [GO:0005886]; postsynaptic endocytic zone cytoplasmic component [GO:0099631]; presynap... | clathrin heavy chain binding [GO:0032050]; neurotransmitter transmembrane transporter activity [GO:0005326]; peptide binding [GO:0042277]; structural molecule activity [GO:0005198] | PF01086; | null | Clathrin light chain family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic face of coated pits and vesicles. | null | null | null | null | null | FUNCTION: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. | Rattus norvegicus (Rat) |
P08092 | RAN1_SCHPO | MMRENPELLLGQVLGDSLRFVSIIGAGAYGVVYKAEDIYDGTLYAVKALCKDGLNEKQKKLQARELALHARVSSHPYIITLHRVLETEDAIYVVLQYCPNGDLFTYITEKKVYQGNSHLIKTVFLQLISAVEHCHSVGIYHRDLKPENIMVGNDVNTVYLADFGLATTEPYSSDFGCGSLFYMSPECQREVKKLSSLSDMLPVTPEPIESQSSSFATAPNDVWALGIILINLCCKRNPWKRACSQTDGTYRSYVHNPSTLLSILPISRELNSLLNRIFDRNPKTRITLPELSTLVSNCKNLTRRLRPAPLVSSRYLAYQQ... | 2.7.11.1 | null | cell cycle G1/S phase transition [GO:0044843]; intracellular signal transduction [GO:0035556]; meiotic cell cycle [GO:0051321]; negative regulation of cell cycle switching, mitotic to meiotic cell cycle [GO:0110045]; negative regulation of induction of conjugation with cellular fusion [GO:0010515]; negative regulation ... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; 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] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | 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 is a negative regulator of both sexual conjugation and meiosis. It phosphorylates mei2. It blocks the onset of meiosis until conjugation takes place. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P08096 | TOP2_SCHPO | MSIDADFSDYEDEASGDENVLPNTTTKRKASTTSSKSRAKKASTPDLRQTSLTSMTASEQIPLVTNNGNGNSNVSTQYQRLTPREHVLRRPDTYIGSIEPTTSEMWVFDSEKNKLDYKAVTYVPGLYKIFDEIIVNAADNKVRDPNMNTLKVTLDPEANVISIYNNGKGIPIEIHDKEKIYIPELIFGNLLTSSNYDDNQKKVTGGRNGYGAKLCNIFSTEFVVETADKERMKKYKQTWYDNMSRKSEPVITSLKKPDEYTKITFKPDLAKFGMDKIDDDMVSIIKRRIYDMAGTVRETKVYLNNERISISGFKKYVEMY... | 5.6.2.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995}; Note=Binds two Mg(2+) per subunit. The magnesium ion... | chromatin organization [GO:0006325]; DNA topological change [GO:0006265]; mitotic chromosome condensation [GO:0007076]; resolution of meiotic recombination intermediates [GO:0000712]; sister chromatid segregation [GO:0000819] | chromatin [GO:0000785]; chromosome, centromeric core domain [GO:0034506]; euchromatin [GO:0000791]; nuclear chromosome [GO:0000228]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity [GO:0003918]; metal ion binding [GO:0046872] | PF00204;PF00521;PF02518;PF01751;PF16898; | 3.30.1360.40;3.30.1490.30;3.30.230.10;3.40.50.670;3.30.565.10;3.90.199.10;1.10.268.10; | Type II topoisomerase family | PTM: Phosphorylated at multiple sites at both extremities of the protein. {ECO:0000269|PubMed:1332977, ECO:0000269|PubMed:18257517}. | SUBCELLULAR LOCATION: Nucleus. | CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995}; | null | null | null | null | FUNCTION: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P08099 | OPS2_DROME | MERSHLPETPFDLAHSGPRFQAQSSGNGSVLDNVLPDMAHLVNPYWSRFAPMDPMMSKILGLFTLAIMIISCCGNGVVVYIFGGTKSLRTPANLLVLNLAFSDFCMMASQSPVMIINFYYETWVLGPLWCDIYAGCGSLFGCVSIWSMCMIAFDRYNVIVKGINGTPMTIKTSIMKILFIWMMAVFWTVMPLIGWSAYVPEGNLTACSIDYMTRMWNPRSYLITYSLFVYYTPLFLICYSYWFIIAAVAAHEKAMREQAKKMNVKSLRSSEDCDKSAEGKLAKVALTTISLWFMAWTPYLVICYFGLFKIDGLTPLTTIW... | null | null | cellular response to light stimulus [GO:0071482]; G protein-coupled receptor signaling pathway [GO:0007186]; phototransduction [GO:0007602]; visual perception [GO:0007601] | membrane [GO:0016020] | G protein-coupled photoreceptor activity [GO:0008020]; G protein-coupled receptor activity [GO:0004930] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Opsin subfamily | PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region. | SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. | Drosophila melanogaster (Fruit fly) |
P08100 | OPSD_HUMAN | MNGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQFSMLAAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVLGGFTSTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLAGWSRYIPEGLQCSCGIDYYTLKPEVNNESFVIYMFVVHFTIPMIIIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWVPYASVAFYIFTHQGSNFGPIFMTIPAFFAKSAAIYNPVIYIMMNKQFRNCMLTT... | null | null | absorption of visible light [GO:0016038]; adaptation of rhodopsin mediated signaling [GO:0016062]; cellular response to light stimulus [GO:0071482]; detection of temperature stimulus involved in thermoception [GO:0050960]; G protein-coupled receptor signaling pathway [GO:0007186]; gene expression [GO:0010467]; microtub... | cell-cell junction [GO:0005911]; ciliary membrane [GO:0060170]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi-associated vesicle membrane [GO:0030660]; membrane [GO:0016020]; photoreceptor disc membrane [GO:0097381]; photoreceptor inner segment [GO:0001917]; photoreceptor inner segment membrane [GO:0... | 11-cis retinal binding [GO:0005502]; G protein-coupled photoreceptor activity [GO:0008020]; G protein-coupled receptor activity [GO:0004930]; metal ion binding [GO:0046872] | PF00001;PF10413; | 1.20.1070.10; | G-protein coupled receptor 1 family, Opsin subfamily | PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region (By similarity). After activation by light, phosphorylated by GRK1 (in vitro) (PubMed:28524165). {ECO:0000250|UniProtKB:P02699, ECO:0000269|PubMed:28524165}.; PTM: Contains one covalently linked retinal chromophore.... | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12566452, ECO:0000269|PubMed:19934218, ECO:0000269|PubMed:25664179, ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425}; Multi-pass membrane protein {ECO:0000269|PubMed:19934218, ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425}. Cell projection, cilium, ... | null | null | null | null | null | FUNCTION: Photoreceptor required for image-forming vision at low light intensity (PubMed:7846071, PubMed:8107847). Required for photoreceptor cell viability after birth (PubMed:12566452, PubMed:2215617). Light-induced isomerization of the chromophore 11-cis-retinal to all-trans-retinal triggers a conformational change ... | Homo sapiens (Human) |
P08101 | FCGR2_MOUSE | MESNWTVHVFSRTLCHMLLWTAVLNLAAGTHDLPKAVVKLEPPWIQVLKEDTVTLTCEGTHNPGNSSTQWFHNGRSIRSQVQASYTFKATVNDSGEYRCQMEQTRLSDPVDLGVISDWLLLQTPQLVFLEGETITLRCHSWRNKLLNRISFFHNEKSVRYHHYSSNFSIPKANHSHSGDYYCKGSLGRTLHQSKPVTITVQGPKSSRSLPVLTIVAAVTGIAVAAIVIILVSLVYLKKKQVPALPGNPDHREMGETLPEEVGEYRQPSGGSVPVSPGPPSGLEPTSSSPYNPPDLEEAAKTEAENTITYSLLKHPEALDE... | null | null | antibody-dependent cellular cytotoxicity [GO:0001788]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; B cell proliferation [GO:0042100]; cell surface receptor signaling pathway [GO:0007166]; cellular response to amyloid-beta [GO:1904646]; cellular response to molecule of... | cell body [GO:0044297]; cell surface [GO:0009986]; cytoskeleton [GO:0005856]; dendritic spine [GO:0043197]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; membrane [GO:0016020]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037] | IgG binding [GO:0019864]; IgG receptor activity [GO:0019770]; immunoglobulin binding [GO:0019865] | PF13895; | 2.60.40.10; | null | PTM: Glycosylated.; PTM: When coaggregated to BCR, isoform IIB1 and isoform IIB1' become tyrosine phosphorylated and bind to the SH2 domains of the protein tyrosine phosphatase PTPC1. Phosphorylated by SRC-type Tyr-kinases such as LYN, BLK, FYN and SYK (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform IIB1]: Cytoplasm, cytoskeleton. Note=Binds the cytoskeleton and is not localized in endocytotic pits.; SUBCELLULAR LOCATION: [Isoform IIB3]: Secreted. Note=Released as a soluble molecule. | null | null | null | null | null | FUNCTION: Receptor for the Fc region of complexed immunoglobulins gamma. Low affinity receptor. Involved in a variety of effector and regulatory functions such as phagocytosis of antigen-antibody complexes from the circulation and modulation of antibody production by B-cells. Isoform IIB1 and isoform IIB1' form caps bu... | Mus musculus (Mouse) |
P08103 | HCK_MOUSE | MGGRSSCEDPGCPRSEGRAPRMGCVKSRFLRDGSKASKTEPSANQKGPVYVPDPTSSSKLGPNNSNSMPPGFVEGSEDTIVVALYDYEAIHREDLSFQKGDQMVVLEEAGEWWKARSLATKKEGYIPSNYVARVNSLETEEWFFKGISRKDAERHLLAPGNMLGSFMIRDSETTKGSYSLSVRDFDPQHGDTVKHYKIRTLDSGGFYISPRSTFSSLQELVLHYKKGKDGLCQKLSVPCVSPKPQKPWEKDAWEIPRESLQMEKKLGAGQFGEVWMATYNKHTKVAVKTMKPGSMSVEAFLAEANLMKSLQHDKLVKLHA... | 2.7.10.2 | null | cell differentiation [GO:0030154]; defense response to Gram-positive bacterium [GO:0050830]; exocytosis [GO:0006887]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; peptidyl-tyrosine phosphorylation [GO:0018108]; phagocytosis [GO:0006909]; positive regulation of cell population proliferation [... | caveola [GO:0005901]; cell projection [GO:0042995]; cytoplasmic side of plasma membrane [GO:0009898]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; lysosome [GO:0005764]; nucleus [GO:00... | ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713]; signaling receptor binding [GO:0005102] | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | PTM: Phosphorylated on several tyrosine residues. Autophosphorylated. Becomes rapidly phosphorylated upon activation of the immunoglobulin receptors FCGR1A and FCGR2A. Phosphorylation at Tyr-409 increases kinase activity. Phosphorylation at Tyr-520 inhibits kinase activity. Kinase activity is not required for phosphory... | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 1]: Membrane; Lipid-anchor. Membrane, caveola {ECO:0000250}. Lysosome {ECO:0000250}. Cell projection, podosome membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cytoplasm, cyto... | 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: Non-receptor tyrosine-protein kinase found in hematopoietic cells that transmits signals from cell surface receptors and plays an important role in the regulation of innate immune responses, including neutrophil, monocyte, macrophage and mast cell functions, phagocytosis, cell survival and proliferation, cell... | Mus musculus (Mouse) |
P08104 | SCN3A_RAT | MAQALLVPPGPESFRLFTRESLAAIEKRAAEEKAKKPKKEQDIDDENKPKPNSDLEAGKNLPFIYGDIPPEMVSEPLEDLDPYYVSKKTFVVLNKGKAIFRFSATSALYILTPLNPVRKIAIKILVHSLFSMLIMCTILTNCVFMTLSNPPDWTKNVEYTFTGIYTFESLIKILARGFCLEDFTFLRDPWNWLDFSVIVMAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCSQWPPSDSAFETNTTSYFNGTMDSNGTFVNVTMSTFNWKDYIA... | null | null | behavioral response to pain [GO:0048266]; cellular response to antibiotic [GO:0071236]; membrane depolarization during action potential [GO:0086010]; nervous system development [GO:0007399]; neuronal action potential [GO:0019228]; response to pyrethroid [GO:0046684]; sodium ion transmembrane transport [GO:0035725] | axon [GO:0030424]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; sarcoplasm [GO:0016528]; voltage-gated sodium channel complex [GO:0001518] | calmodulin binding [GO:0005516]; sodium ion binding [GO:0031402]; voltage-gated sodium channel activity [GO:0005248] | PF00520;PF06512;PF11933; | 1.10.287.70;1.10.238.10;1.20.5.1190;1.20.120.350; | Sodium channel (TC 1.A.1.10) family, Nav1.3/SCN3A subfamily | PTM: May be ubiquitinated by NEDD4L; which would promote its endocytosis. {ECO:0000250|UniProtKB:Q9NY46}.; PTM: Phosphorylation at Ser-1452 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NY46}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. | null | null | null | null | null | FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient (By similarity)... | Rattus norvegicus (Rat) |
P08106 | HSP70_CHICK | MSGKGPAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKYDDPTVQSDMKHWPFRVVNEGGKPKVQVEYKGEMKTFFPEEISSMVLTKMKEIAEAYLGKKVETAVITVPAYFNDSQRQATKDAGTITGLNVMRIINEPTAAAIAYGLDKKGTRAGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNRFVEEFKGKHKRDNAGNKRAVRRLRTACERARRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELNADLFRGTLEPV... | null | null | chaperone cofactor-dependent protein refolding [GO:0051085]; protein refolding [GO:0042026]; response to cold [GO:0009409]; response to heat [GO:0009408]; response to organic cyclic compound [GO:0014070]; response to organonitrogen compound [GO:0010243]; response to progesterone [GO:0032570] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; heat shock protein binding [GO:0031072]; nuclear progesterone receptor binding [GO:0033142]; protein folding chaperone [GO:0044183] | PF00012; | 1.20.1270.10;3.30.30.30;3.30.420.40; | Heat shock protein 70 family | null | null | null | null | null | null | null | FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in th... | Gallus gallus (Chicken) |
P08110 | ENPL_CHICK | MKSAWALALACTLLLAASVTAEEVDVDATVEEDLGKSREGSRTDDEVVQREEEAIQLDGLNASQIKEIREKSEKFAFQAEVNRMMKLIINSLYKNKEIFLRELISNASDALDKIRLISLTDENALAGNEELTVKIKCDKEKNMLHVTDTGIGMTKEELIKNLGTIAKSGTSEFLNKMTEMQDDSQSTSELIGQFGVGFYSAFLVADRVIVTSKHNNDTQHIWESDSNEFSVIDDPRGNTLGRGTTITLVLKEEASDYLELDTVKNLVKKYSQFINFPIYVWSSKTETVEEPVEEEEAKEEKEETDDNEAAVEEEEEEKKP... | null | null | DNA damage response [GO:0006974]; ERAD pathway [GO:0036503]; intracellular sequestering of iron ion [GO:0006880]; protein folding [GO:0006457]; response to heat [GO:0009408] | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; melanosome [GO:0042470]; perinuclear region of cytoplasm [GO:0048471]; sarcoplasmic reticulum lumen [GO:0033018] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; unfolded protein binding [GO:0051082] | PF13589;PF00183; | 3.30.230.80;3.40.50.11260;1.20.120.790;3.30.565.10; | Heat shock protein 90 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q66HD0}. Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:P41148}. Melanosome {ECO:0000250|UniProtKB:P14625}. | null | null | null | null | null | FUNCTION: Molecular chaperone that functions in the processing and transport of secreted proteins (By similarity). Has ATPase activity (By similarity). {ECO:0000250|UniProtKB:P08113}. | Gallus gallus (Chicken) |
P08111 | L2GL_DROME | MLKFIRGKGQQPSADRHRLQKDLFAYRKTAQHGFPHKPSALAYDPVLKLMAIGTQTGALKVFGQPGVELYGQHTLLNNSASELNVQLLEWVYGTGRILSLTAANQLILWEPVGATLLPIKTLPFDGKLKKVSSLCCSLSKDLLWIGTEGGNIYQLDLHTFTIKEPVIYHDVVLEQVPPAYKLNPGAIESIRQLPNSPSKLLVAYNRGLCVLWDFESASVQRAYIAPGHGQSVGLTVNFEGSEFTWYHADGSYATWSIDNPEPPSNVNYVPYGPDPCKSINRLYKGKRRSNDVIVFSGGMPRSAYGDHNCVSVHASDGHKV... | null | null | actin cytoskeleton organization [GO:0030036]; apical protein localization [GO:0045176]; asymmetric neuroblast division [GO:0055059]; asymmetric protein localization involved in cell fate determination [GO:0045167]; autophagic cell death [GO:0048102]; basal protein localization [GO:0045175]; cell competition in a multic... | apicolateral plasma membrane [GO:0016327]; cell cortex [GO:0005938]; cortical actin cytoskeleton [GO:0030864]; cortical cytoskeleton [GO:0030863]; cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; Golgi membrane [GO:0000139]; leading edge membrane [GO:0031256]; plasma membrane [GO:0005886]; presynaptic membran... | GTPase activator activity [GO:0005096]; myosin binding [GO:0017022]; myosin II binding [GO:0045159]; protein kinase binding [GO:0019901]; protein kinase inhibitor activity [GO:0004860]; SNARE binding [GO:0000149]; syntaxin binding [GO:0019905] | PF08366; | 2.130.10.10; | WD repeat L(2)GL family | PTM: Phosphorylated by aPKC which lowers lipid affinity and promotes dissociation from the cell cortex (PubMed:26481050). In developing oocytes, aPKC-mediated phosphorylation restricts activity to the oocyte posterior and is required for oocyte polarity formation (PubMed:18094021, PubMed:18327897). {ECO:0000269|PubMed:... | SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:12545176, ECO:0000269|PubMed:18948416, ECO:0000269|PubMed:26481050}. Cytoplasm {ECO:0000269|PubMed:26481050}. Note=In larval and embryonic neuroblasts, detected in the cortex with apical enrichment from late interphase to metaphase, and uniform cortical l... | null | null | null | null | null | FUNCTION: Essential for the development of polarized epithelia, for cell polarity associated with asymmetric cell division of neuroblasts during development, and for oocyte polarity formation. Promotes the formation of actin-rich projections at the oocyte cortex and the posterior enrichment of par-1 which is required f... | Drosophila melanogaster (Fruit fly) |
P08113 | ENPL_MOUSE | MRVLWVLGLCCVLLTFGFVRADDEVDVDGTVEEDLGKSREGSRTDDEVVQREEEAIQLDGLNASQIRELREKSEKFAFQAEVNRMMKLIINSLYKNKEIFLRELISNASDALDKIRLISLTDENALAGNEELTVKIKCDKEKNLLHVTDTGVGMTREELVKNLGTIAKSGTSEFLNKMTEAQEDGQSTSELIGQFGVGFYSAFLVADKVIVTSKHNNDTQHIWESDSNEFSVIADPRGNTLGRGTTITLVLKEEASDYLELDTIKNLVRKYSQFINFPIYVWSSKTETVEEPLEEDEAAKEEKEESDDEAAVEEEEEEKK... | null | null | actin rod assembly [GO:0031247]; cellular response to ATP [GO:0071318]; DNA damage response [GO:0006974]; ERAD pathway [GO:0036503]; insulin processing [GO:0030070]; negative regulation of apoptotic process [GO:0043066]; protein folding [GO:0006457]; response to heat [GO:0009408]; response to hypoxia [GO:0001666]; retr... | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum chaperone complex [GO:0034663]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; melanosome [GO:0042470]; midbody [GO:0030496]; perinuclear region of cytoplasm [GO:004... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; low-density lipoprotein particle receptor binding [GO:0050750]; protein folding chaperone [GO:0044183]; protein phosphatase binding [GO:0019903]; RNA binding [GO:0003723]; unfolded protein binding [GO:0... | PF13589;PF00183; | 3.30.230.80;3.40.50.11260;1.20.120.790;3.30.565.10; | Heat shock protein 90 family | PTM: N-glycosylated. {ECO:0000269|PubMed:8179819}. | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:20865800}. Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:P41148}. Melanosome {ECO:0000250|UniProtKB:P14625}. | null | null | null | null | null | FUNCTION: Molecular chaperone that functions in the processing and transport of secreted proteins (PubMed:20865800). When associated with CNPY3, required for proper folding of Toll-like receptors (PubMed:20865800). Functions in endoplasmic reticulum associated degradation (ERAD) (By similarity). Has ATPase activity (Pu... | Mus musculus (Mouse) |
P08118 | MSMB_HUMAN | MNVLLGSVVIFATFVTLCNASCYFIPNEGVPGDSTRKCMDLKGNKHPINSEWQTDNCETCTCYETEISCCTLVSTPVGYDKDNCQRIFKKEDCKYIVVEKKDPKKTCSVSEWII | null | null | null | extracellular space [GO:0005615]; nucleus [GO:0005634] | null | PF05825; | 2.20.25.590;2.10.70.10; | Beta-microseminoprotein family | null | SUBCELLULAR LOCATION: Secreted. Note=Sperm surface. | null | null | null | null | null | null | Homo sapiens (Human) |
P08120 | CO4A1_DROME | MLPFWKRLLYAAVIAGALVGADAQFWKTAGTAGSIQDSVKHYNRNEPKFPIDDSYDIVDSAGVARGDLPPKNCTAGYAGCVPKCIAEKGNRGLPGPLGPTGLKGEMGFPGMEGPSGDKGQKGDPGPYGQRGDKGERGSPGLHGQAGVPGVQGPAGNPGAPGINGKDGCDGQDGIPGLEGLSGMPGPRGYAGQLGSKGEKGEPAKENGDYAKGEKGEPGWRGTAGLAGPQGFPGEKGERGDSGPYGAKGPRGEHGLKGEKGASCYGPMKPGAPGIKGEKGEPASSFPVKPTHTVMGPRGDMGQKGEPGLVGRKGEPGPEGD... | null | null | basement membrane organization [GO:0071711]; cardiac muscle cell development [GO:0055013]; dorsal closure [GO:0007391]; extracellular matrix organization [GO:0030198]; intestinal epithelial structure maintenance [GO:0060729]; oviduct morphogenesis [GO:0035848]; post-embryonic digestive tract morphogenesis [GO:0048621] | basement membrane [GO:0005604]; collagen type IV trimer [GO:0005587]; collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615] | extracellular matrix structural constituent [GO:0005201]; extracellular matrix structural constituent conferring tensile strength [GO:0030020] | PF01413;PF01391; | 2.170.240.10; | Type IV collagen family | PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.; PTM: Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known typ... | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. | null | null | null | null | null | FUNCTION: Collagen type IV is specific for basement membranes. | Drosophila melanogaster (Fruit fly) |
P08121 | CO3A1_MOUSE | MMSFVQSGTWFLLTLLHPTLILAQQSNVDELGCSHLGQSYESRDVWKPEPCQICVCDSGSVLCDDIICDEEPLDCPNPEIPFGECCAICPQPSTPAPVLPDGHGPQGPKGDPGPPGIPGRNGDPGLPGQPGLPGPPGSPGICESCPTGGQNYSPQFDSYDVKSGVGGMGGYPGPAGPPGPPGPPGSSGHPGSPGSPGYQGPPGEPGQAGPAGPPGPPGALGPAGPAGKDGESGRPGRPGERGLPGPPGIKGPAGMPGFPGMKGHRGFDGRNGEKGETGAPGLKGENGLPGDNGAPGPMGPRGAPGERGRPGLPGAAGARG... | null | null | aorta development [GO:0035904]; aorta smooth muscle tissue morphogenesis [GO:0060414]; basement membrane organization [GO:0071711]; blood vessel development [GO:0001568]; cartilage development [GO:0051216]; cell-matrix adhesion [GO:0007160]; cellular response to amino acid stimulus [GO:0071230]; cerebral cortex develop... | collagen trimer [GO:0005581]; collagen type III trimer [GO:0005586]; collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | extracellular matrix structural constituent conferring tensile strength [GO:0030020]; integrin binding [GO:0005178]; metal ion binding [GO:0046872]; platelet-derived growth factor binding [GO:0048407]; protease binding [GO:0002020]; SMAD binding [GO:0046332] | PF01410;PF01391;PF00093; | 2.60.120.1000;2.10.70.10; | Fibrillar collagen family | PTM: Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.; PTM: O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. | null | null | null | null | null | FUNCTION: Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of ADGRG1 in the developing brain and binding to ADGRG1 inhibits neuronal migration and activates the RhoA pathway by coupling ADGRG1 to GNA13 and possibly G... | Mus musculus (Mouse) |
P08122 | CO4A2_MOUSE | MDRVRFKASGPPLRGWLLLATVTVGLLAQSVLGGVKKLDVPCGGRDCSGGCQCYPEKGARGQPGAVGPQGYNGPPGLQGFPGLQGRKGDKGERGVPGPTGPKGDVGARGVSGFPGADGIPGHPGQGGPRGRPGYDGCNGTRGDAGPQGPSGSGGFPGLPGPQGPKGQKGEPYALSKEDRDKYRGEPGEPGLVGYQGPPGRPGPIGQMGPMGAPGRPGPPGPPGPKGQPGNRGLGFYGQKGEKGDIGQPGPNGIPSDITLVGPTTSTIHPDLYKGEKGDEGEQGIPGVISKGEEGIMGFPGIRGFPGLDGEKGVVGQKGSR... | null | null | angiogenesis [GO:0001525]; cellular response to transforming growth factor beta stimulus [GO:0071560]; collagen-activated tyrosine kinase receptor signaling pathway [GO:0038063]; DNA-templated transcription [GO:0006351]; endodermal cell differentiation [GO:0035987]; extracellular matrix organization [GO:0030198]; glome... | basement membrane [GO:0005604]; collagen type IV trimer [GO:0005587]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | extracellular matrix structural constituent conferring tensile strength [GO:0030020] | PF01413;PF01391; | 2.170.240.10; | Type IV collagen family | PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.; PTM: Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known typ... | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000255|PROSITE-ProRule:PRU00736}. | null | null | null | null | null | FUNCTION: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen. {ECO:0000269|PubMed:3597383}.; FUNCTION: Canstatin, a cleavage product corresponding to the collagen alpha 2(IV) NC1 domain, ... | Mus musculus (Mouse) |
P08123 | CO1A2_HUMAN | MLSFVDTRTLLLLAVTLCLATCQSLQEETVRKGPAGDRGPRGERGPPGPPGRDGEDGPTGPPGPPGPPGPPGLGGNFAAQYDGKGVGLGPGPMGLMGPRGPPGAAGAPGPQGFQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNGLDGLKGQPGAPGVKGEPGAPGENGTPGQTGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGEIGAVGNAGPAGPAGPRGEVGLPGLSGPVGPPGNPGANGLTGAKGAAGLPGVAGA... | null | null | blood vessel development [GO:0001568]; bone mineralization [GO:0030282]; cellular response to amino acid stimulus [GO:0071230]; collagen fibril organization [GO:0030199]; collagen metabolic process [GO:0032963]; extracellular matrix assembly [GO:0085029]; extracellular matrix organization [GO:0030198]; odontogenesis [G... | collagen type I trimer [GO:0005584]; collagen type IV trimer [GO:0005587]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | extracellular matrix structural constituent [GO:0005201]; extracellular matrix structural constituent conferring tensile strength [GO:0030020]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; platelet-derived growth factor binding [GO:0048407]; protease binding [GO:0002020]; protein-macromolecul... | PF01410;PF01391; | 2.60.120.1000; | Fibrillar collagen family | PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000269|PubMed:4412529}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. | null | null | null | null | null | FUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen). | Homo sapiens (Human) |
P08124 | COL1_CAEEL | METDGRLKAYKFVAYAAVGFSIAAVASVLLTLPMVYSYVSHVRQQMHHEINFCKGSAKDIFAEVNYMKANAGPVPPRNRTTRQAYGGPEVNPAPNLQCEGCCLPGPPGPAGAPGKPGKPGRPGAPGTPGTPGKPPVAPCEPTTPPPCKPCPQGPPGPPGPPGAPGDPGEAGTPGRPGTDAAPGSPGPRGPPGPAGEAGAPGPAGEPGTPAISEPLTPGAPGEPGDSGPPGPPGPPGAPGNDGPPGPPGPKGAPGPDGPPGVDGQSGPPGPPGPAGTPGEKGICPKYCALDGGVFFEDGTRR | null | null | collagen and cuticulin-based cuticle development [GO:0040002]; cuticle development involved in collagen and cuticulin-based cuticle molting cycle [GO:0042338] | collagen and cuticulin-based cuticle extracellular matrix [GO:0060102]; collagen trimer [GO:0005581]; extracellular region [GO:0005576] | structural constituent of cuticle [GO:0042302] | PF01484;PF01391; | null | Cuticular collagen family | null | null | null | null | null | null | null | FUNCTION: Nematode cuticles are composed largely of collagen-like proteins. The cuticle functions both as an exoskeleton and as a barrier to protect the worm from its environment. | Caenorhabditis elegans |
P08125 | COAA1_CHICK | MHLQISLLLLFCLNIVHGSDGYFSERYQKQSSIKGPPHFLPFNVKSQGVQMRGEQGPPGPPGPIGPRGQPGPAGKPGFGSPGPQGPPGPLGPPGFSTVGKLGMPGLPGKPGERGLNGEKGEAGPVGLPGARGPQGPPGIPGPAGLSVLGKPGPQGPPGAQGPRGPPGEKGEPGVPGINGQKGEMGFGVPGRPGNRGLPGPQGPQGLPGSAGIGKPGENGLPGQPGMKGDRGLPGARGEAGIPGPQGPPGEPGEVGIGKPGPMGPPGPAGIPGAKGLPGPAGLPGSPGLPGFGKPGLPGMKGHRGPEGPPGFPGPKGDQGP... | null | null | extracellular matrix organization [GO:0030198] | collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; receptor complex [GO:0043235] | extracellular matrix structural constituent conferring tensile strength [GO:0030020]; metal ion binding [GO:0046872] | PF00386;PF01391; | 2.60.120.40; | null | PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000269|PubMed:3082876}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. | null | null | null | null | null | FUNCTION: Type X collagen is a product of hypertrophic chondrocytes and has been localized to presumptive mineralization zones of hyaline cartilage. | Gallus gallus (Chicken) |
P08132 | ANXA4_PIG | MAAKGGTVKAASGFNAAEDAQTLRKAMKGLGTDEDAIISVLAYRSTAQRQEIRTAYKSTIGRDLLDDLKSELSGNFEQVILGMMTPTVLYDVQELRRAMKGAGTDEGCLIEILASRTPEEIRRINQTYQLQYGRSLEDDIRSDTSFMFQRVLVSLSAGGRDEGNYLDDALVRQDAQDLYEAGEKKWGTDEVKFLTVLCSRNRNHLLHVFDEYKRISQKDIEQSIKSETSGSFEDALLAIVKCMRNKSAYFAERLYKSMKGLGTDDNTLIRVMVSRAEIDMMDIRANFKRLYGKSLYSFIKGDTSGDYRKVLLILCGGDD | null | null | null | cytoplasm [GO:0005737]; plasma membrane [GO:0005886]; zymogen granule membrane [GO:0042589] | calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; phosphatidylserine binding [GO:0001786] | PF00191; | 1.10.220.10; | Annexin family | null | SUBCELLULAR LOCATION: Zymogen granule membrane {ECO:0000250|UniProtKB:P50994}; Peripheral membrane protein {ECO:0000250|UniProtKB:P50994}. | null | null | null | null | null | FUNCTION: Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. {ECO:0000250}. | Sus scrofa (Pig) |
P08133 | ANXA6_HUMAN | MAKPAQGAKYRGSIHDFPGFDPNQDAEALYTAMKGFGSDKEAILDIITSRSNRQRQEVCQSYKSLYGKDLIADLKYELTGKFERLIVGLMRPPAYCDAKEIKDAISGIGTDEKCLIEILASRTNEQMHQLVAAYKDAYERDLEADIIGDTSGHFQKMLVVLLQGTREEDDVVSEDLVQQDVQDLYEAGELKWGTDEAQFIYILGNRSKQHLRLVFDEYLKTTGKPIEASIRGELSGDFEKLMLAVVKCIRSTPEYFAERLFKAMKGLGTRDNTLIRIMVSRSELDMLDIREIFRTKYEKSLYSMIKNDTSGEYKKTLLKL... | null | null | apoptotic signaling pathway [GO:0097190]; growth plate cartilage chondrocyte differentiation [GO:0003418]; mitochondrial calcium ion homeostasis [GO:0051560]; monoatomic ion transmembrane transport [GO:0034220]; negative regulation of sequestering of calcium ion [GO:0051283]; neural crest cell migration [GO:0001755]; p... | collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; melanosome [GO:0042470]; membrane [GO:0016020]; mitochondrion [GO:0005739]; perinuclear region of cytoplas... | actin filament binding [GO:0051015]; calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; calcium-dependent protein binding [GO:0048306]; cholesterol binding [GO:0015485]; chondroitin sulfate binding [GO:0035374]; GTP binding [GO:0005525]; identic... | PF00191; | 1.10.220.10; | Annexin family | PTM: Phosphorylated in response to growth factor stimulation. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. | null | null | null | null | null | FUNCTION: May associate with CD21. May regulate the release of Ca(2+) from intracellular stores. | Homo sapiens (Human) |
P08134 | RHOC_HUMAN | MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYIADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRQDEHTRRELAKMKQEPVRSEEGRDMANRISAFGYLECSAKTKEGVREVFEMATRAGLQVRKNKRRRGCPIL | null | null | actin filament organization [GO:0007015]; apical junction assembly [GO:0043297]; mitotic cytokinesis [GO:0000281]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell migration [GO:0030335]; positive regulation of lipase activity [GO:0060193]; positive regulation of ... | cleavage furrow [GO:0032154]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; stereocilium [GO:0032420] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein kinase binding [GO:0019901] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rho family | PTM: (Microbial infection) Glycosylated at Tyr-34 by Photorhabdus asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230 inhibits downstream signaling by an impaired interaction with diverse regulator and effector proteins of Rho and leads to actin disassembly. {ECO:0000269|PubMed:24141704}.; PTM: (Microbial in... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cleavage furrow {ECO:0000269|PubMed:16236794}. Note=Translocates to the equatorial region before furrow formation in a ECT2-dependent manner. | null | null | null | null | null | FUNCTION: Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Serves as a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Regulates apical junction formation in bronch... | Homo sapiens (Human) |
P08138 | TNR16_HUMAN | MGAGATGRAMDGPRLLLLLLLGVSLGGAKEACPTGLYTHSGECCKACNLGEGVAQPCGANQTVCEPCLDSVTFSDVVSATEPCKPCTECVGLQSMSAPCVEADDAVCRCAYGYYQDETTGRCEACRVCEAGSGLVFSCQDKQNTVCEECPDGTYSDEANHVDPCLPCTVCEDTERQLRECTRWADAECEEIPGRWITRSTPPEGSDSTAPSTQEPEAPPEQDLIASTVAGVVTTVMGSSQPVVTRGTTDNLIPVYCSILAAVVVGLVAYIAFKRWNSCKQNKQGANSRPVNQTPPPEGEKLHSDSGISVDSQSLHDQQPH... | null | null | activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; axon guidance [GO:0007411]; cellular response to amyloid-beta [GO:1904646]; central nervous system development [GO:0007417]; circadian regulation of gene expression [GO:0032922]; detection of temperature stimulus [GO:0016048]... | cell surface [GO:0009986]; cell-cell junction [GO:0005911]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; endosome [GO:0005768]; extracellular region [GO:0005576]; growth cone [GO:0030426]; membrane [GO:0016020]; neuromuscular junction [GO:0031594]; nucleoplasm [GO:0005654]; perikaryon [GO:0043204]; plasma membra... | amyloid-beta binding [GO:0001540]; calmodulin binding [GO:0005516]; coreceptor activity [GO:0015026]; death receptor activity [GO:0005035]; nerve growth factor binding [GO:0048406]; neurotrophin binding [GO:0043121]; signaling receptor activity [GO:0038023]; small GTPase binding [GO:0031267]; transmembrane signaling re... | PF00531;PF18422;PF00020; | 6.10.250.1780;1.10.533.10;2.10.50.10; | null | PTM: N- and O-glycosylated.; PTM: O-linked glycans consist of Gal(1-3)GalNAc core elongated by 1 or 2 NeuNAc.; PTM: Phosphorylated on serine residues. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:3022937}; Single-pass type I membrane protein {ECO:0000305}. Perikaryon {ECO:0000250|UniProtKB:Q9Z0W1}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q9Z0W1}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q9Z0W1}. | null | null | null | null | null | FUNCTION: Low affinity receptor which can bind to NGF, BDNF, NTF3, and NTF4. Forms a heterodimeric receptor with SORCS2 that binds the precursor forms of NGF, BDNF and NTF3 with high affinity, and has much lower affinity for mature NGF and BDNF (PubMed:24908487). Plays an important role in differentiation and survival ... | Homo sapiens (Human) |
P08142 | ILVB_ECOLI | MASSGTTSTRKRFTGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVTAIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWIDIPKDVQTAVFEIETQPAMAEKAAAPAFSEESIRDAAAMINAAKRPVLYLGGGVINAPARVRELAEKAQLPTTMTLMALGMLPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPH... | 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] | 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 | null | 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; | null | PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 1/4. | null | null | null | Escherichia coli (strain K12) |
P08144 | AMYA_DROME | MFLAKSIVCLALLAVANAQFDTNYASGRSGMVHLFEWKWDDIAAECENFLGPNGYAGVQVSPVNENAVKDSRPWWERYQPISYKLETRSGNEEQFASMVKRCNAVGVRTYVDVVFNHMAADGGTYGTGGSTASPSSKSYPGVPYSSLDFNPTCAISNYNDANEVRNCELVGLRDLNQGNSYVQDKVVEFLDHLIDLGVAGFRVDAAKHMWPADLAVIYGRLKNLNTDHGFASGSKAYIVQEVIDMGGEAISKSEYTGLGAITEFRHSDSIGKVFRGKDQLQYLTNWGTAWGFAASDRSLVFVDNHDNQRGHGAGGADVLT... | 3.2.1.1 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P04746}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P04746}; COFACTOR: Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:P04746}; Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250|UniProtKB:P04746}; | carbohydrate metabolic process [GO:0005975] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | alpha-amylase activity [GO:0004556]; calcium ion binding [GO:0005509] | PF00128;PF02806; | 3.20.20.80;2.60.40.1180; | Glycosyl hydrolase 13 family | null | null | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; Evidence={ECO:0000250|UniProtKB:P04746}; | null | null | null | null | null | Drosophila melanogaster (Fruit fly) |
P08148 | GP63_LEIMA | MSVDSSSTHRRRCVAARLVRLAAAGAAVTVAVGTAAAWAHAGALQHRCVHDAMQARVRQSVADHHKAPGAVSAVGLPYVTLDAAHTAAAADPRPGSARSVVRDVNWGALRIAVSTEDLTDPAYHCARVGQHVKDHAGAIVTCTAEDILTNEKRDILVKHLIPQAVQLHTERLKVQQVQGKWKVTDMVGDICGDFKVPQAHITEGFSNTDFVMYVASVPSEEGVLAWATTCQTFSDGHPAVGVINIPAANIASRYDQLVTRVVTHEMAHALGFSGPFFEDARIVANVPNVRGKNFDVPVINSSTAVAKAREQYGCDTLEYL... | 3.4.24.36 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:9739094}; | cell adhesion [GO:0007155]; proteolysis [GO:0006508]; symbiont-mediated activation of host signal transduction pathway [GO:0052028]; symbiont-mediated perturbation of host inflammatory response [GO:0052032] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237] | PF01457; | 3.10.170.20;3.90.132.10;2.10.55.10;2.30.34.10; | Peptidase M8 family | PTM: The phosphatidylinositol moiety of the GPI-anchor contains a fully saturated, unbranched 1-O-alkyl chain (mainly C24:0) and a mixture of fully saturated unbranched 2-O-acyl chains (C12:0, C14:0, C16:0, and C18:0). | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. | CATALYTIC ACTIVITY: Reaction=Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-|-Leu-Lys-Lys-.; EC=3.4.24.36; | null | null | null | null | FUNCTION: Has an integral role during the infection of macrophages in the mammalian host. | Leishmania major |
P08149 | PBP2_NEIGO | MLIKSEYKPRMLPKEEQVKKPMTSNGRISFVLMAMAVLFACLIARGLYLQTVTYNFLKEQGDNRIVRTQALPATRGTVSDRNGAVLALSAPTESLFAVPKDMKEMPSAAQLERLSELVDVPVDVLRNKLEQKGKSFIWIKRQLDPKVAEEVKALGLENFVFEKELKRHYPMGNLFAHVIGFTDIDGKGQEGLELSLEDSLYGEDGAEVVLRDRQGNIVDSLDSPRNKAPQNGKDIILSLDQRIQTLAYEELNKAVEYHQAKAGTVVVLDARTGEILALANTPAYDPNRPGRADSEQRRNRAVTDMIEPGSAIKPFVIAKA... | 3.4.16.4 | null | cell wall organization [GO:0071555]; division septum assembly [GO:0000917]; FtsZ-dependent cytokinesis [GO:0043093]; peptidoglycan biosynthetic process [GO:0009252]; proteolysis [GO:0006508]; regulation of cell shape [GO:0008360]; response to antibiotic [GO:0046677] | plasma membrane [GO:0005886] | penicillin binding [GO:0008658]; peptidoglycan glycosyltransferase activity [GO:0008955]; serine-type D-Ala-D-Ala carboxypeptidase activity [GO:0009002] | PF03717;PF00905; | 1.10.150.770;3.30.450.330;3.40.710.10;3.90.1310.10; | Transpeptidase family, FtsI subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02080}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02080}. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.; EC=3.4.16.4; Evidence={ECO:0000255|HAMAP-Rule:MF_02080}; | null | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02080}. | null | null | FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum. {ECO:0000255|HAMAP-Rule:MF_02080}. | Neisseria gonorrhoeae |
P08151 | GLI1_HUMAN | MFNSMTPPPISSYGEPCCLRPLPSQGAPSVGTEGLSGPPFCHQANLMSGPHSYGPARETNSCTEGPLFSSPRSAVKLTKKRALSISPLSDASLDLQTVIRTSPSSLVAFINSRCTSPGGSYGHLSIGTMSPSLGFPAQMNHQKGPSPSFGVQPCGPHDSARGGMIPHPQSRGPFPTCQLKSELDMLVGKCREEPLEGDMSSPNSTGIQDPLLGMLDGREDLEREEKREPESVYETDCRWDGCSQEFDSQEQLVHHINSEHIHGERKEFVCHWGGCSRELRPFKAQYMLVVHMRRHTGEKPHKCTFEGCRKSYSRLENLKT... | null | null | cerebellar cortex morphogenesis [GO:0021696]; digestive tract morphogenesis [GO:0048546]; dorsal/ventral pattern formation [GO:0009953]; epidermal cell differentiation [GO:0009913]; liver regeneration [GO:0097421]; lung development [GO:0030324]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; notoc... | axoneme [GO:0005930]; ciliary base [GO:0097546]; ciliary tip [GO:0097542]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; GLI-SUFU complex [GO:1990788]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; microtubule binding [GO:0008017]; RNA polymerase II cis-reg... | PF00096; | 3.30.160.60; | GLI C2H2-type zinc-finger protein family | PTM: Phosphorylated in vitro by ULK3. {ECO:0000269|PubMed:19878745}.; PTM: Acetylation at Lys-518 down-regulates transcriptional activity. Deacetylated by HDAC1. {ECO:0000269|PubMed:20081843}.; PTM: Ubiquitinated by the CRL2(FEM1B) complex, suppressing GLI1 transcriptional activator activity. {ECO:0000269|PubMed:240761... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10806483, ECO:0000269|PubMed:19706761, ECO:0000269|PubMed:19878745, ECO:0000269|PubMed:24076122}. Nucleus {ECO:0000269|PubMed:10806483, ECO:0000269|PubMed:11238441, ECO:0000269|PubMed:19706761, ECO:0000269|PubMed:19878745, ECO:0000269|PubMed:2105456}. Note=Tethered in... | null | null | null | null | null | FUNCTION: Acts as a transcriptional activator (PubMed:10806483, PubMed:19706761, PubMed:19878745, PubMed:24076122, PubMed:24217340, PubMed:24311597). Binds to the DNA consensus sequence 5'-GACCACCCA-3' (PubMed:2105456, PubMed:24217340, PubMed:8378770). Regulates the transcription of specific genes during normal develop... | Homo sapiens (Human) |
P08152 | EGR2_MOUSE | MMTAKAVDKIPVTLSGFMHQLPDSLYPVEDLAASSVTIFPNGELGGPFDQMNGVAGDGMINIDMTGEKRPLDLPYPSSFAPISAPRNQTFTYMGKFSIDPQYPGASCYPEGIINIVSAGILQGVTPPASTTASSSVTSASPNPLATGPLGVCTMSQTQPELDHLYSPPPPPPPYSGCTGDLYQDPSAFLSPPSTTSTSSLAYQPPPSYPSPKPAMDPGLIPMIPDYPGFFPSPCQRDPHGAAGPDRKPFPCPLDSLRVPPPLTPLSTIRNFTLGGPGAGVTGPGASGGGEGPRLPGSGSAAVTATPYNPHHLPLRPILRP... | 2.3.2.- | null | aorta development [GO:0035904]; brain segmentation [GO:0035284]; cellular response to organic substance [GO:0071310]; facial nerve structural organization [GO:0021612]; fat cell differentiation [GO:0045444]; gene expression [GO:0010467]; learning or memory [GO:0007611]; motor neuron axon guidance [GO:0008045]; myelinat... | cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; HMG box domain binding [GO:0071837]... | PF11928;PF00096; | 3.30.160.60; | EGR C2H2-type zinc-finger protein family | PTM: Ubiquitinated by WWP2 leading to proteasomal degradation. {ECO:0000269|PubMed:19651900}.; PTM: Acetylated at Lys-247. May be deacetylated by HDAC6, HDAC10 or SIRT1. {ECO:0000269|PubMed:28576496}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17938205}. | null | null | PATHWAY: Protein modification; protein sumoylation. | null | null | FUNCTION: Sequence-specific DNA-binding transcription factor (PubMed:11823429, PubMed:1674431, PubMed:1969796, PubMed:31852952). Plays a role in hindbrain segmentation by regulating the expression of a subset of homeobox containing genes and in Schwann cell myelination by regulating the expression of genes involved in ... | Mus musculus (Mouse) |
P08153 | SWI5_YEAST | MDTSNSWFDASKVQSLNFDLQTNSYYSNARGSDPSSYAIEGEYKTLATDDLGNILNLNYGETNEVIMNEINDLNLPLGPLSDEKSVKVSTFSELIGNDWQSMNFDLENNSREVTLNATSLLNENRLNQDSGMTVYQKTMSDKPHDEKKISMADNLLSTINKSEINKGFDRNLGELLLQQQQELREQLRAQQEANKKLELELKQTQYKQQQLQATLENSDGPQFLSPKRKISPASENVEDVYANSLSPMISPPMSNTSFTGSPSRRNNRQKYCLQRKNSSGTVGPLCFQELNEGFNDSLISPKKIRSNPNENLSSKTKFIT... | null | null | negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of mating type switching [GO:0031496]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; mediator complex binding [GO:0036033]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [... | PF00096; | 3.30.160.60; | null | PTM: Cell cycle-dependent phosphorylation of three serine residues prevents SWI5 from entering the nucleus, and it accumulates in the cytoplasm. As a consequence of CDC28 kinase inactivation at the end of anaphase, the three serine residues are dephosphorylated and SWI5 enters the nucleus to activate transcription. It ... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1652372}. Cytoplasm {ECO:0000269|PubMed:1652372}. Note=Nuclear in G1, cytoplasmic in S, G2 and M cell cycle phases. | null | null | null | null | null | FUNCTION: Determines the mother-cell-specific transcription of the HO endonuclease gene that is responsible for the initiation of mating-type switching in yeast. Recognizes a specific sequence in the promoter of the HO gene. Activates EGT2 transcription in a concentration-dependent manner. Synthesized during G2 and ear... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P08154 | EGR1_RAT | MDNYPKLEEMMLLSNGAPQFLGAAGTPEGSGGNNSSSSSSSSSGGGGGGGSNSGSSAFNPQGEPSEQPYEHLTTESFSDIALNNEKALVETSYPSQTTRLPPITYTGRFSLEPAPNSGNTLWPEPLFSLVSGLVSMTNPPTSSSSAPSPAASSSSSASQSPPLSCAVPSNDSSPIYSAAPTFPTPNTDIFPEPQSQAFPGSAGTALQYPPPAYPATKGGFQVPMIPDYLFPQQQGDLSLGTPDQKPFQGLENRTQQPSLTPLSTIKAFATQSGSQDLKALNNTYQSQLIKPSRMRKYPNRPSKTPPHERPYACPVESCDR... | null | null | BMP signaling pathway [GO:0030509]; cellular response to antibiotic [GO:0071236]; cellular response to cAMP [GO:0071320]; cellular response to follicle-stimulating hormone stimulus [GO:0071372]; cellular response to gamma radiation [GO:0071480]; cellular response to gonadotropin stimulus [GO:0071371]; cellular response... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded DNA binding [GO:0003690]; double-stranded methylate... | PF11914;PF11928;PF00096; | 3.30.160.60; | EGR C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1859855}. Cytoplasm {ECO:0000250|UniProtKB:P18146}. | null | null | null | null | null | FUNCTION: Transcriptional regulator (PubMed:8413279). Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'(EGR-site) in the promoter region of target genes (PubMed:15220929). Binds double-stranded target DNA, irrespective of the cytosine methylation status (By similarity). Regulates the transcription of numerou... | Rattus norvegicus (Rat) |
P08155 | KRH1_DROME | MTESKNDTKSWAPKQIWIKDVLKKSGTELLDISKSPAKAVAVKKSPAKDSATTKMVYYSANQLLIKTEQSSQAQFCLQVPPPLTATTTSVGLGVPPSGGQQEHFELLQTPQQRQMQLQLQDQHQQEQQQFVSYQLAIQQHQKQQQQQQHESITNAAPTAAPSAQRIKTEPVGGFPASAAVVSQVRKPSASKPQFKCDQCGMTFGSKSAHTSHTKSHSKNQDLSLNGASGAGVAAPVSTAAIELNDAGLPVGIPKSPTIKPLANVAAGADPYQCNVCQKTFAVPARLIRHYRTHTGERPFECEFCHKLFSVKENLQVHRRI... | null | null | metamorphosis [GO:0007552]; negative regulation of compound eye photoreceptor development [GO:0045316]; negative regulation of neuron projection development [GO:0010977]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; response to ecdysone [GO:00350... | cytosol [GO:0005829]; nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00096; | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | null | null | null | null | null | null | FUNCTION: Plays a general role in the hierarchies of gene expression leading to metamorphosis. {ECO:0000269|PubMed:10772791}. | Drosophila melanogaster (Fruit fly) |
P08157 | ALDH_EMENI | MSDLFTTIETPVIKYEQPLGLFINNEFVKGVEGKTFQVINPSNEKVITSVHEATEKDVDVAVAAARAAFEGPWRQVTPSERGILINKLADLMERDIDTLAAIESLDNGKAFTMAKVDLANSIGCLRYYAGWADKIHGQTIDTNPETLTYTRHEPVGVCGQIIPWNFPLLMWSWKIGPAVAAGNTVVLKTAEQTPLSALYAAKLIKEAGFPAGVINVISGFGRTAGAAISSHMDIDKVAFTGSTLVGRTILQAAAKSNLKKVTLELGGKSPNIVFDDADIDNAISWANFGIFFNHGQCCCAGSRILVQEGIYDKFVARFKE... | 1.2.1.3 | null | acetaldehyde catabolic process [GO:0046187]; acetate biosynthetic process [GO:0019413]; carbon catabolite activation of transcription [GO:0045991]; cellular response to osmotic stress [GO:0071470]; ethanol catabolic process [GO:0006068]; ethanol metabolic process [GO:0006067]; threonine catabolic process [GO:0006567] | extracellular region [GO:0005576] | aldehyde dehydrogenase (NAD+) activity [GO:0004029]; aldehyde dehydrogenase [NAD(P)+] activity [GO:0004030]; glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity [GO:0043878]; phenylacetaldehyde dehydrogenase activity [GO:0008957] | PF00171; | null | Aldehyde dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.3; | null | PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. | null | null | null | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
P08159 | HDNO_PAENI | MSSKLATPLSIQGEVIYPDDSGFDAIANIWDGRHLQRPSLIARCLSAGDVAKSVRYACDNGLEISVRSGGHNPNGYATNDGGIVLDLRLMNSIHIDTAGSRARIGGGVISGDLVKEAAKFGLAAVTGMHPKVGFCGLALNGGVGFLTPKYGLASDNILGATLVTATGDVIYCSDDERPELFWAVRGAGPNFGVVTEVEVQLYELPRKMLAGFITWAPSVSELAGLLTSLLDALNEMADHIYPSVFVGVDENRAPSVTVCVGHLGGLDIAERDIARLRGLGRTVSDSIAVRSYDEVVALNAEVGSFEDGMSNLWIDREIAM... | 1.5.3.6 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:16095622, ECO:0000269|PubMed:2115879, ECO:0000269|PubMed:2680607, ECO:0000269|PubMed:4628374, ECO:0000269|PubMed:5083098}; Note=Binds 1 FAD per subunit (PubMed:16095622, PubMed:4628374). The FAD is covalently bound to the protein (PubMed:16095622,... | alkaloid metabolic process [GO:0009820]; nicotine catabolic process [GO:0019608] | cytoplasm [GO:0005737] | (R)-6-hydroxynicotine oxidase activity [GO:0018530]; FAD binding [GO:0071949] | PF08031;PF01565; | 3.30.465.10;3.40.462.20;3.30.43.10; | Oxygen-dependent FAD-linked oxidoreductase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:4019415}. | CATALYTIC ACTIVITY: Reaction=(R)-6-hydroxynicotine + H2O + O2 = 6-hydroxypseudooxynicotine + H2O2; Xref=Rhea:RHEA:10012, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58413, ChEBI:CHEBI:58682; EC=1.5.3.6; Evidence={ECO:0000269|PubMed:2680607, ECO:0000269|PubMed:31046245, ECO:0000269|PubMed:462837... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.1 mM for (R)-6-hydroxynicotine {ECO:0000269|PubMed:5849820}; KM=0.05 mM for (R)-6-hydroxynicotine {ECO:0000269|PubMed:4628374}; | PATHWAY: Alkaloid degradation; nicotine degradation; 6-hydroxypseudooxynicotine from nicotine (R-isomer route): step 2/2. {ECO:0000305|PubMed:5849820}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Fairly stable at neutral or alkaline pH. {ECO:0000269|PubMed:4628374}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Inactivated at temperatures above 45 degrees Celsius. {ECO:0000269|PubMed:4628374}; | FUNCTION: Involved in the degradation of D-nicotine (PubMed:4628374, PubMed:5849820). Catalyzes the oxidation of (R)-6-hydroxynicotine (6-hydroxy-D-nicotine) to 6-hydroxypseudooxynicotine (PubMed:2680607, PubMed:31046245, PubMed:4628374, PubMed:4965794, PubMed:5849820). Oxidation of the pyrrolidine ring of (R)-6-hydrox... | Paenarthrobacter nicotinovorans (Arthrobacter nicotinovorans) |
P08164 | NADE_BACSU | MSMQEKIMRELHVKPSIDPKQEIEDRVNFLKQYVKKTGAKGFVLGISGGQDSTLAGRLAQLAVESIREEGGDAQFIAVRLPHGTQQDEDDAQLALKFIKPDKSWKFDIKSTVSAFSDQYQQETGDQLTDFNKGNVKARTRMIAQYAIGGQEGLLVLGTDHAAEAVTGFFTKYGDGGADLLPLTGLTKRQGRTLLKELGAPERLYLKEPTADLLDEKPQQSDETELGISYDEIDDYLEGKEVSAKVSEALEKRYSMTEHKRQVPASMFDDWWK | 6.3.1.5 | null | NAD biosynthetic process [GO:0009435]; sporulation resulting in formation of a cellular spore [GO:0030435] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; glutaminase activity [GO:0004359]; metal ion binding [GO:0046872]; NAD+ synthase (glutamine-hydrolyzing) activity [GO:0003952]; NAD+ synthase activity [GO:0008795] | PF02540; | 3.40.50.620; | NAD synthetase family | PTM: Phosphorylated during sporulation. {ECO:0000269|PubMed:1556067}. | null | CATALYTIC ACTIVITY: Reaction=ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+); Xref=Rhea:RHEA:21188, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_00193, ECO:0000269|P... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.62 mM for NH(4)(+) {ECO:0000269|PubMed:7890752}; KM=0.28 mM for deamido-NAD {ECO:0000269|PubMed:7890752}; KM=0.21 mM for ATP {ECO:0000269|PubMed:7890752}; | PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00193, ECO:0000269|PubMed:7890752}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.2-8.7. {ECO:0000269|PubMed:7890752}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40-45 degrees Celsius. {ECO:0000269|PubMed:7890752}; | FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00193, ECO:0000269|PubMed:7890752}. | Bacillus subtilis (strain 168) |
P08165 | ADRO_BOVIN | MAPRCWRWWPWSSWTRTRLPPSRSIQNFGQHFSTQEQTPQICVVGSGPAGFYTAQHLLKHHSRAHVDIYEKQLVPFGLVRFGVAPDHPEVKNVINTFTQTARSDRCAFYGNVEVGRDVTVQELQDAYHAVVLSYGAEDHQALDIPGEELPGVFSARAFVGWYNGLPENRELAPDLSCDTAVILGQGNVALDVARILLTPPDHLEKTDITEAALGALRQSRVKTVWIVGRRGPLQVAFTIKELREMIQLPGTRPMLDPADFLGLQDRIKEAARPRKRLMELLLRTATEKPGVEEAARRASASRAWGLRFFRSPQQVLPSPD... | 1.18.1.6 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:10369776}; | cholesterol metabolic process [GO:0008203]; electron transport chain [GO:0022900]; steroid biosynthetic process [GO:0006694]; ubiquinone biosynthetic process [GO:0006744] | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | flavin adenine dinucleotide binding [GO:0050660]; NADP binding [GO:0050661]; NADPH-adrenodoxin reductase activity [GO:0015039] | PF07992; | 3.50.50.60;3.40.50.720; | Ferredoxin--NADP reductase type 1 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P48360}; Peripheral membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=H(+) + NADP(+) + 2 reduced [adrenodoxin] = NADPH + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:42312, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.18.1.6; Evidence={ECO:0000269|PubMed:7811729}; | null | PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000269|PubMed:7811729}. | null | null | FUNCTION: Serves as the first electron transfer protein in all the mitochondrial P450 systems including cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C-27 hydroxylation in the liver. {ECO:000... | Bos taurus (Bovine) |
P08166 | KAD2_BOVIN | MAPNVPAAEPVPESPKGVRAVLLGPPGAGKGTQAPKLAKNFCVCHLATGDMLRAMVASGSELGKKLKATMDAGKLVSDEMVLELIEKNLETPPCKNGFLLDGFPRTVRQAEMLDDLMEKRKEKLDSVIEFSIPDSLLIRRITGRLIHPQSGRSYHEEFNPPKEPMKDDITGEPLIRRSDDNKKALKIRLEAYHTQTTPLVEYYSKRGIHSAIDASQTPDVVFASILAAFSKATCKDLVMFI | 2.7.4.3 | null | ADP biosynthetic process [GO:0006172]; AMP metabolic process [GO:0046033]; ATP metabolic process [GO:0046034]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; sperm mitochondrial sheath [GO:0097226] | adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524] | PF00406;PF05191; | 3.40.50.300; | Adenylate kinase family, AK2 subfamily | null | SUBCELLULAR LOCATION: Mitochondrion intermembrane space. | CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_03168}; | null | null | null | null | FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. Plays... | Bos taurus (Bovine) |
P08168 | ARRS_BOVIN | MKANKPAPNHVIFKKISRDKSVTIYLGKRDYIDHVERVEPVDGVVLVDPELVKGKRVYVSLTCAFRYGQEDIDVMGLSFRRDLYFSQVQVFPPVGASGATTRLQESLIKKLGANTYPFLLTFPDYLPCSVMLQPAPQDVGKSCGVDFEIKAFATHSTDVEEDKIPKKSSVRLLIRKVQHAPRDMGPQPRAEASWQFFMSDKPLRLAVSLSKEIYYHGEPIPVTVAVTNSTEKTVKKIKVLVEQVTNVVLYSSDYYIKTVAAEEAQEKVPPNSSLTKTLTLVPLLANNRERRGIALDGKIKHEDTNLASSTIIKEGIDKTV... | null | null | G protein-coupled receptor internalization [GO:0002031]; response to light stimulus [GO:0009416]; signal transduction [GO:0007165] | cytosol [GO:0005829]; membrane [GO:0016020]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750] | G protein-coupled receptor binding [GO:0001664]; identical protein binding [GO:0042802] | PF02752;PF00339; | 2.60.40.640;2.60.40.840; | Arrestin family | null | SUBCELLULAR LOCATION: [Isoform A]: Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:7515057}. Membrane {ECO:0000250|UniProtKB:P20443}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20443}. Note=Highly expressed in photoreceptor outer segments in light-exposed retina (PubMed:7515057). Evenl... | null | null | null | null | null | FUNCTION: Binds to photoactivated, phosphorylated RHO and terminates RHO signaling via G-proteins by competing with G-proteins for the same binding site on RHO (PubMed:25205354, PubMed:8003967). May play a role in preventing light-dependent degeneration of retinal photoreceptor cells (By similarity). {ECO:0000250|UniPr... | Bos taurus (Bovine) |
P08169 | MPRI_BOVIN | MEAAAGRSSHLGPAPAGRPPRCPLLLQLQLLLLLLLLPPGWVPGAAGTQGAEFPELCSYTWEAVDTKNNMLYKINICGNMGVAQCGPSSAVCMHDLKTDSFHSVGDSLLKTASRSLLEFNTTVNCKQQNHKIQSSITFLCGKTLGTPEFVTATDCVHYFEWRTTAACKKNIFKANKEVPCYAFDRELKKHDLNPLIKTSGAYLVDDSDPDTSLFINVCRDIEVLRASSPQVRVCPTGAAACLVRGDRAFDVGRPQEGLKLVSNDRLVLSYVKEGAGQPDFCDGHSPAVTITFVCPSERREGTIPKLTAKSNCRFEIEWVT... | null | null | lysosomal transport [GO:0007041] | cell surface [GO:0009986]; endocytic vesicle [GO:0030139]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; late endosome [GO:0005770]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802] | insulin-like growth factor binding [GO:0005520]; kringle domain binding [GO:0036143]; mannose binding [GO:0005537]; phosphoprotein binding [GO:0051219]; signaling receptor activity [GO:0038023] | PF00878;PF00040; | 2.10.10.10;2.70.130.10; | MRL1/IGF2R family | PTM: Palmitoylated. Undergoes cysteine S-palmitoylation which promotes interaction with the retromer cargo-selective complex which mediates its retrograde trafficking to the Golgi apparatus. {ECO:0000250|UniProtKB:P11717}. | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:P11717}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P11717}. Endosome membrane {ECO:0000250|UniProtKB:P11717}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P11717}. Note=Mainly localized in the Golgi at steady state and ... | null | null | null | null | null | FUNCTION: Mediates the transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidi... | Bos taurus (Bovine) |
P08170 | LOX1_SOYBN | MFSAGHKIKGTVVLMPKNELEVNPDGSAVDNLNAFLGRSVSLQLISATKADAHGKGKVGKDTFLEGINTSLPTLGAGESAFNIHFEWDGSMGIPGAFYIKNYMQVEFFLKSLTLEAISNQGTIRFVCNSWVYNTKLYKSVRIFFANHTYVPSETPAPLVSYREEELKSLRGNGTGERKEYDRIYDYDVYNDLGNPDKSEKLARPVLGGSSTFPYPRRGRTGRGPTVTDPNTEKQGEVFYVPRDENLGHLKSKDALEIGTKSLSQIVQPAFESAFDLKSTPIEFHSFQDVHDLYEGGIKLPRDVISTIIPLPVIKELYRTD... | 1.13.11.12 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE-ProRule:PRU00726, ECO:0000269|PubMed:8518276}; Note=Binds 1 Fe cation per subunit. Iron is tightly bound. {ECO:0000255|PROSITE-ProRule:PRU00726, ECO:0000269|PubMed:8518276}; | fatty acid biosynthetic process [GO:0006633]; fatty acid oxidation [GO:0019395]; lipid oxidation [GO:0034440]; oxylipin biosynthetic process [GO:0031408] | cytoplasm [GO:0005737] | iron ion binding [GO:0005506]; linoleate 13S-lipoxygenase activity [GO:0016165]; linolenate 9R-lipoxygenase activity [GO:0102299]; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen [GO:0016702] | PF00305;PF01477; | 3.10.450.60;2.60.60.20; | Lipoxygenase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + O2 = (13S)-hydroperoxy-(9Z,11E)-octadecadienoate; Xref=Rhea:RHEA:22780, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245, ChEBI:CHEBI:57466; EC=1.13.11.12; Evidence={ECO:0000269|PubMed:16157595, ECO:0000269|PubMed:2492826}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecat... | null | PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-ProRule:PRU00726}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Inactive below pH 6.0. {ECO:0000269|PubMed:2492826}; | null | FUNCTION: Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. With linoleate as substrate, L-1 shows a preference for carbon 13 as the site for hydroperoxidation (in contrast to L-2 and L-3, whi... | Glycine max (Soybean) (Glycine hispida) |
P08171 | EST6_DROME | MNYVGLGLIIVLSCLWLGSNASDTDDPLLVQLPQGKLRGRDNGSYYSYESIPYAEPPTGDLRFEAPEPYKQKWSDIFDATKTPVACLQWDQFTPGANKLVGEEDCLTVSVYKPKNSKRNSFPVVAHIHGGAFMFGAAWQNGHENVMREGKFILVKISYRLGPLGFVSTGDRDLPGNYGLKDQRLALKWIKQNIASFGGEPQNVLLVGHSAGGASVHLQMLREDFGQLARAAFSFSGNALDPWVIQKGARGRAFELGRNVGCESAEDSTSLKKCLKSKPASELVTAVRKFLIFSYVPFAPFSPVLEPSDAPDAIITQDPRD... | 3.1.1.1 | null | courtship behavior [GO:0007619]; mating [GO:0007618]; organic substance catabolic process [GO:1901575]; ovulation [GO:0030728]; pheromone biosynthetic process [GO:0042811]; regulation of egg-laying behavior [GO:0046662]; regulation of female receptivity, post-mating [GO:0046008]; sexual reproduction [GO:0019953]; sperm... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | carboxylesterase activity [GO:0106435]; serine hydrolase activity [GO:0017171]; short-chain carboxylesterase activity [GO:0034338] | PF00135; | 3.40.50.1820; | Type-B carboxylesterase/lipase family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+); Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10039}; | null | null | null | null | FUNCTION: Transferred from the ejaculatory bulbs of males to the female genitals upon copulation, plays an important role in the reproductive biology. | Drosophila melanogaster (Fruit fly) |
P08172 | ACM2_HUMAN | MNNSTNSSNNSLALTSPYKTFEVVFIVLVAGSLSLVTIIGNILVMVSIKVNRHLQTVNNYFLFSLACADLIIGVFSMNLYTLYTVIGYWPLGPVVCDLWLALDYVVSNASVMNLLIISFDRYFCVTKPLTYPVKRTTKMAGMMIAAAWVLSFILWAPAILFWQFIVGVRTVEDGECYIQFFSNAAVTFGTAIAAFYLPVIIMTVLYWHISRASKSRIKKDKKEPVANQDPVSPSLVQGRIVKPNNNNMPSSDDGLEHNKIQNGKAPRDPVTENCVQGEEKESSNDSTSVSAVASNMRDDEITQDENTVSTSLGHSKDENS... | null | null | adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway [GO:0007197]; adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; chemical synaptic transmission [GO:0007268]; G protein-coupled acetylcholine receptor signaling pathway [GO:0007213]; G protein-co... | asymmetric synapse [GO:0032279]; axon terminus [GO:0043679]; cholinergic synapse [GO:0098981]; clathrin-coated endocytic vesicle membrane [GO:0030669]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; postsynaptic membrane [... | arrestin family protein binding [GO:1990763]; G protein-coupled acetylcholine receptor activity [GO:0016907]; G protein-coupled serotonin receptor activity [GO:0004993] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Muscarinic acetylcholine receptor subfamily, CHRM2 sub-subfamily | PTM: Phosphorylated in response to agonist treatment. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22278061, ECO:0000269|PubMed:24256733, ECO:0000269|PubMed:3443095}; Multi-pass membrane protein {ECO:0000269|PubMed:22278061, ECO:0000269|PubMed:24256733}. Postsynaptic cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Phosphorylation in... | null | null | null | null | null | FUNCTION: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is adenylate cyclase inhibition. Signaling promotes phospholipa... | Homo sapiens (Human) |
P08173 | ACM4_HUMAN | MANFTPVNGSSGNQSVRLVTSSSHNRYETVEMVFIATVTGSLSLVTVVGNILVMLSIKVNRQLQTVNNYFLFSLACADLIIGAFSMNLYTVYIIKGYWPLGAVVCDLWLALDYVVSNASVMNLLIISFDRYFCVTKPLTYPARRTTKMAGLMIAAAWVLSFVLWAPAILFWQFVVGKRTVPDNQCFIQFLSNPAVTFGTAIAAFYLPVVIMTVLYIHISLASRSRVHKHRPEGPKEKKAKTLAFLKSPLMKQSVKKPPPGEAAREELRNGKLEEAPPPALPPPPRPVADKDTSNESSSGSATQNTKERPATELSTTEATT... | null | null | adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway [GO:0007197]; cell surface receptor signaling pathway [GO:0007166]; chemical synaptic transmission [GO:0007268]; G protein-coupled acetylcholine receptor signaling pathway [GO:0007213]; G protein-coupled receptor signaling pathway, ... | dendrite [GO:0030425]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202] | G protein-coupled acetylcholine receptor activity [GO:0016907]; G protein-coupled serotonin receptor activity [GO:0004993] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Muscarinic acetylcholine receptor subfamily, CHRM4 sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Postsynaptic cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is inhibition of adenylate cyclase. | Homo sapiens (Human) |
P08174 | DAF_HUMAN | MTVARPSVPAALPLLGELPRLLLLVLLCLPAVWGDCGLPPDVPNAQPALEGRTSFPEDTVITYKCEESFVKIPGEKDSVICLKGSQWSDIEEFCNRSCEVPTRLNSASLKQPYITQNYFPVGTVVEYECRPGYRREPSLSPKLTCLQNLKWSTAVEFCKKKSCPNPGEIRNGQIDVPGGILFGATISFSCNTGYKLFGSTSSFCLISGSSVQWSDPLPECREIYCPAPPQIDNGIIQGERDHYGYRQSVTYACNKGFTMIGEHSIYCTVNNDEGEWSGPPPECRGKSLTSKVPPTVQKPTTVNVPTTEVSPTSQKTTTKT... | null | null | complement activation, classical pathway [GO:0006958]; innate immune response [GO:0045087]; negative regulation of complement activation [GO:0045916]; negative regulation of complement activation, classical pathway [GO:0045959]; positive regulation of CD4-positive, alpha-beta T cell activation [GO:2000516]; positive re... | cell surface [GO:0009986]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule membrane [GO:0101003]; Golgi membrane [GO:0000139]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; secretory gra... | lipid binding [GO:0008289]; virus receptor activity [GO:0001618] | PF00084; | 2.10.70.10; | Receptors of complement activation (RCA) family | PTM: The Ser/Thr-rich domain is heavily O-glycosylated. {ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:26207632}. | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Lipid-anchor, GPI-anchor.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000269|PubMed:16503113}.; SUBCELLULAR LOCATION: [Isoform 4]: Secreted {ECO:0000269|PubMed:16503113}.; SUB... | null | null | null | null | null | FUNCTION: This protein recognizes C4b and C3b fragments that condense with cell-surface hydroxyl or amino groups when nascent C4b and C3b are locally generated during C4 and c3 activation. Interaction of daf with cell-associated C4b and C3b polypeptides interferes with their ability to catalyze the conversion of C2 and... | Homo sapiens (Human) |
P08176 | PEPT1_DERPT | MKIVLAIASLLALSAVYARPSSIKTFEEYKKAFNKSYATFEDEEAARKNFLESVKYVQSNGGAINHLSDLSLDEFKNRFLMSAEAFEHLKTQFDLNAETNACSINGNAPAEIDLRQMRTVTPIRMQGGCGSCWAFSGVAATESAYLAYRNQSLDLAEQELVDCASQHGCHGDTIPRGIEYIQHNGVVQESYYRYVAREQSCRRPNAQRFGISNYCQIYPPNVNKIREALAQTHSAIAVIIGIKDLDAFRHYDGRTIIQRDNGYQPNYHAVNIVGYSNAQGVDYWIVRNSWDTNWGDNGYGYFAANIDLMMIEEYPYVVIL | 3.4.22.65 | null | proteolysis involved in protein catabolic process [GO:0051603] | extracellular space [GO:0005615]; lysosome [GO:0005764] | cysteine-type endopeptidase activity [GO:0004197] | PF00112; | 3.90.70.10; | Peptidase C1 family | PTM: N-glycosylated. N-glycanase treatment does not completely remove carbohydrates, suggesting that the protein contains additional glycosylation sites. {ECO:0000269|PubMed:16148130}. | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Broad endopeptidase specificity.; EC=3.4.22.65; | null | null | null | null | FUNCTION: Thiol protease, with a preference for substrates with a large hydrophobic side chain in the P2 position, or with basic residues. | Dermatophagoides pteronyssinus (European house dust mite) |
P08179 | PUR3_ECOLI | MNIVVLISGNGSNLQAIIDACKTNKIKGTVRAVFSNKADAFGLERARQAGIATHTLIASAFDSREAYDRELIHEIDMYAPDVVVLAGFMRILSPAFVSHYAGRLLNIHPSLLPKYPGLHTHRQALENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGDSEDDITARVQTQEHAIYPLVISWFADGRLKMHENAAWLDGQRLPPQGYAADE | 2.1.2.2 | null | 'de novo' IMP biosynthetic process [GO:0006189]; DNA damage response [GO:0006974] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | phosphoribosylglycinamide formyltransferase activity [GO:0004644] | PF00551; | 3.40.50.170; | GART family | null | null | CATALYTIC ACTIVITY: Reaction=(6R)-10-formyltetrahydrofolate + N(1)-(5-phospho-beta-D-ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide; Xref=Rhea:RHEA:15053, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, ChEBI:CHEBI:143788, ChEBI:CHEBI:147286, ChEBI:CHEBI:195366... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=77.5 uM for (6R)-N10-formyltetrahydrofolate (at pH 8.5) {ECO:0000269|PubMed:2185839}; KM=84.8 uM for (6R)-N10-formyltetrahydrofolate (at pH 7.5) {ECO:0000269|PubMed:2185839}; Note=kcat is 20.7 sec(-1) for (6R)-N10-formyltetrahydrofolate (at pH 8.5). kcat is 13.5 se... | PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:8688421}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:2185839}; | null | FUNCTION: Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate. {ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:2185839, ECO:0000269|PubMed:350869}. | Escherichia coli (strain K12) |
P08181 | CSK2A_DROME | MTLPSAARVYTDVNAHKPDEYWDYENYVVDWGNQDDYQLVRKLGRGKYSEVFEAINITTTEKCVVKILKPVKKKKIKREIKILENLRGGTNIITLLAVVKDPVSRTPALIFEHVNNTDFKQLYQTLTDYEIRYYLFELLKALDYCHSMGIMHRDVKPHNVMIDHENRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEELYAYLDKYNIDLDPRFHDILQRHSRKRWERFVHSDNQHLVSPEALDFLDKLLRYDHVDRLTAREAMAHP... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:24615015}; | aggressive behavior [GO:0002118]; chaeta development [GO:0022416]; circadian rhythm [GO:0007623]; compound eye development [GO:0048749]; DNA damage response [GO:0006974]; intracellular mRNA localization involved in pattern specification process [GO:0060810]; lateral inhibition [GO:0046331]; locomotor rhythm [GO:0045475... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleus [GO:0005634]; protein kinase CK2 complex [GO:0005956] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, CK2 subfamily | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:24615015}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:24615015}; CATALYTIC... | null | null | null | null | FUNCTION: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha chain contains the catalytic site. May participate in Wnt signaling. | Drosophila melanogaster (Fruit fly) |
P08182 | CSK2B_DROME | MSSSEEVSWVTWFCGLRGNEFFCEVDEDYIQDKFNLTGLNEQVPNYRQALDMILDLEPEDELEDNPLQSDMTEQAAEMLYGLIHARYILTNRGIAQMIEKYQTGDFGHCPRVYCESQPMLPLGLSDIPGEAMVKTYCPKCIDVYTPKSSRHHHTDGAYFGTGFPHMLFMVHPEYRPKRPTNQFVPRLYGFKIHSLAYQIQLQAAANFKMPLRAQRGQPPKDEEPENNADTVPKRL | null | null | circadian rhythm [GO:0007623]; eclosion rhythm [GO:0008062]; intracellular mRNA localization involved in pattern specification process [GO:0060810]; locomotor rhythm [GO:0045475]; mushroom body development [GO:0016319]; oocyte dorsal/ventral axis specification [GO:0007310]; protein phosphorylation [GO:0006468]; regulat... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; neuromuscular junction [GO:0031594]; nucleus [GO:0005634]; presynaptic cytosol [GO:0099523]; protein kinase CK2 complex [GO:0005956]; UTP-C complex [GO:0034456] | protein kinase regulator activity [GO:0019887] | PF01214; | 2.20.25.20;1.10.1820.10; | Casein kinase 2 subunit beta family | PTM: Phosphorylated by alpha subunit. {ECO:0000250}. | null | null | null | null | null | null | FUNCTION: Participates in Wnt signaling (By similarity). Plays a complex role in regulating the basal catalytic activity of the alpha subunit. {ECO:0000250, ECO:0000269|PubMed:3119988}. | Drosophila melanogaster (Fruit fly) |
P08183 | MDR1_HUMAN | MDLEGDRNGGAKKKNFFKLNNKSEKDKKEKKPTVSVFSMFRYSNWLDKLYMVVGTLAAIIHGAGLPLMMLVFGEMTDIFANAGNLEDLMSNITNRSDINDTGFFMNLEEDMTRYAYYYSGIGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTL... | 7.6.2.1; 7.6.2.2 | null | carboxylic acid transmembrane transport [GO:1905039]; ceramide translocation [GO:0099040]; export across plasma membrane [GO:0140115]; G2/M transition of mitotic cell cycle [GO:0000086]; phospholipid translocation [GO:0045332]; positive regulation of anion channel activity [GO:1901529]; regulation of chloride transport... | apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; external side of apical plasma membrane [GO:0098591]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; plasma membrane [GO:0005886] | ABC-type oligopeptide transporter activity [GO:0015421]; ABC-type xenobiotic transporter activity [GO:0008559]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; carboxylic acid transmembrane transporter activity [GO:0046943]; ceramide floppa... | PF00664;PF00005; | 1.20.1560.10;3.40.50.300; | ABC transporter superfamily, ABCB family, Multidrug resistance exporter (TC 3.A.1.201) subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:35970996}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. Apical cell membrane {ECO:0000269|PubMed:28408210, ECO:0000269|PubMed:8898203}. Cytoplasm {ECO:0000269|PubMed:35970996}. Note=ABCB1 localization is influenced by C1orf115 expression lev... | CATALYTIC ACTIVITY: Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2.; EC=7.6.2.2; Evidence={ECO:0000269|PubMed:9038218}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000269|PubMed:8898203}; CATALYTIC ACTIVITY: ... | null | null | null | null | FUNCTION: Translocates drugs and phospholipids across the membrane (PubMed:2897240, PubMed:35970996, PubMed:8898203, PubMed:9038218). Catalyzes the flop of phospholipids from the cytoplasmic to the exoplasmic leaflet of the apical membrane. Participates mainly to the flop of phosphatidylcholine, phosphatidylethanolamin... | Homo sapiens (Human) |
P08185 | CBG_HUMAN | MPLLLYTCLLWLPTSGLWTVQAMDPNAAYVNMSNHHRGLASANVDFAFSLYKHLVALSPKKNIFISPVSISMALAMLSLGTCGHTRAQLLQGLGFNLTERSETEIHQGFQHLHQLFAKSDTSLEMTMGNALFLDGSLELLESFSADIKHYYESEVLAMNFQDWATASRQINSYVKNKTQGKIVDLFSGLDSPAILVLVNYIFFKGTWTQPFDLASTREENFYVDETTVVKVPMMLQSSTISYLHDSELPCQLVQMNYVGNGTVFFILPDKGKMNTVIAALSRDTINRWSAGLTSSQVDLYIPKVTISGVYDLGDVLEEMG... | null | null | glucocorticoid metabolic process [GO:0008211] | extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | serine-type endopeptidase inhibitor activity [GO:0004867]; steroid binding [GO:0005496] | PF00079; | 2.30.39.10;3.30.497.10; | Serpin family | PTM: N-glycosylated; binds 5 oligosaccharide chains.; PTM: Glycosylation in position Asn-260 is needed for steroid binding. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Major transport protein for glucocorticoids and progestins in the blood of almost all vertebrate species. {ECO:0000269|PubMed:18513745}. | Homo sapiens (Human) |
P08191 | FIMH_ECOLI | MKRVITLFAVLLMGWSVNAWSFACKTANGTAIPIGGGSANVYVNLAPVVNVGQNLVVDLSTQIFCHNDYPETITDYVTLQRGSAYGGVLSNFSGTVKYSGSSYPFPTTSETPRVVYNSRTDKPWPVALYLTPVSSAGGVAIKAGSLIAVLILRQTNNYNSDDFQFVWNIYANNDVVVPTGGCDVSARDVTVTLPDYPGSVPIPLTVYCAKSQNLGYYLSGTTADAGNSIFTNTASFSPAQGVGVQLTRNGTIIPANNTVSLGAVGTSAVSLGLTANYARTGGQVTAGNVQSIIGVTFVYQ | null | null | cell adhesion [GO:0007155]; cell adhesion involved in single-species biofilm formation [GO:0043709]; cell-substrate adhesion [GO:0031589]; mechanosensory behavior [GO:0007638] | host cell membrane [GO:0033644]; pilus [GO:0009289]; pilus tip [GO:0009419] | mannose binding [GO:0005537] | PF00419;PF09160; | 2.60.40.1090; | Fimbrial protein family | null | SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:1971261}. | null | null | null | null | null | FUNCTION: Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF a... | Escherichia coli (strain K12) |
P08192 | FOLC_ECOLI | MIIKRTPQAASPLASWLSYLENLHSKTIDLGLERVSLVAARLGVLKPAPFVFTVAGTNGKGTTCRTLESILMAAGYKVGVYSSPHLVRYTERVRVQGQELPESAHTASFAEIESARGDISLTYFEYGTLSALWLFKQAQLDVVILEVGLGGRLDATNIVDADVAVVTSIALDHTDWLGPDRESIGREKAGIFRSEKPAIVGEPEMPSTIADVAQEKGALLQRRGVEWNYSVTDHDWAFSDAHGTLENLPLPLVPQPNAATALAALRASGLEVSENAIRDGIASAILPGRFQIVSESPRVIFDVAHNPHAAEYLTGRMKAL... | 6.3.2.12; 6.3.2.17 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:15705579}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000269|PubMed:15705579}; | folic acid biosynthetic process [GO:0046656]; folic acid-containing compound biosynthetic process [GO:0009396]; one-carbon metabolic process [GO:0006730]; tetrahydrofolate biosynthetic process [GO:0046654] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; dihydrofolate synthase activity [GO:0008841]; guanosine tetraphosphate binding [GO:0097216]; metal ion binding [GO:0046872]; tetrahydrofolylpolyglutamate synthase activity [GO:0004326] | PF02875;PF08245; | 3.90.190.20;3.40.1190.10; | Folylpolyglutamate synthase family | null | null | CATALYTIC ACTIVITY: Reaction=7,8-dihydropteroate + ATP + L-glutamate = 7,8-dihydrofolate + ADP + H(+) + phosphate; Xref=Rhea:RHEA:23584, ChEBI:CHEBI:15378, ChEBI:CHEBI:17839, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57451, ChEBI:CHEBI:456216; EC=6.3.2.12; Evidence={ECO:0000269|PubMed:1823271... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.6 uM for 7,8-dihydropteroate {ECO:0000269|PubMed:2985605}; KM=6.9 uM for ATP (in the assay for DHFS activity) {ECO:0000269|PubMed:2985605}; KM=3.9 mM for glutamate (in the assay for DHFS activity) {ECO:0000269|PubMed:2985605}; KM=0.6 uM for (6RS)-10-formyl-tetrah... | PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 2/2. {ECO:0000305|PubMed:2985605}.; PATHWAY: Cofactor biosynthesis; tetrahydrofolylpolyglutamate biosynthesis. {ECO:0000305|PubMed:2985605}. | null | null | FUNCTION: Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes successive additions of L-glutamate to tetrahydro... | Escherichia coli (strain K12) |
P08195 | 4F2_HUMAN | MELQPPEASIAVVSIPRQLPGSHSEAGVQGLSAGDDSELGSHCVAQTGLELLASGDPLPSASQNAEMIETGSDCVTQAGLQLLASSDPPALASKNAEVTGTMSQDTEVDMKEVELNELEPEKQPMNAASGAAMSLAGAEKNGLVKIKVAEDEAEAAAAAKFTGLSKEELLKVAGSPGWVRTRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPAQKWWHTGALYRIGDLQAFQGHGAGNLAGLKGRLDYLSSLKVKGLVLGPIHKNQKDDVAQTDLLQIDPNFGSKEDFDSLLQSAKKKSIRVILDLTPNYRGENSWFS... | null | null | amino acid transport [GO:0006865]; calcium ion transport [GO:0006816]; carbohydrate metabolic process [GO:0005975]; isoleucine transport [GO:0015818]; L-alanine import across plasma membrane [GO:1904273]; L-histidine transport [GO:1902024]; L-leucine import across plasma membrane [GO:1903801]; leucine import across pla... | amino acid transport complex [GO:1990184]; anchoring junction [GO:0070161]; apical plasma membrane [GO:0016324]; apical pole of neuron [GO:0044225]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; extracellular exosome [GO:0070062]; lysosomal membrane [GO:0005765... | aromatic amino acid transmembrane transporter activity [GO:0015173]; cadherin binding [GO:0045296]; calcium:sodium antiporter activity [GO:0005432]; double-stranded RNA binding [GO:0003725]; exogenous protein binding [GO:0140272]; L-alanine transmembrane transporter activity [GO:0015180]; L-leucine transmembrane transp... | PF00128;PF16028; | 3.20.20.80;2.60.40.1180; | SLC3A transporter family | PTM: N-glycosylated; N-glycosylation is crucial for trafficking and stability of SLC3A2 to the plasma membrane. {ECO:0000269|PubMed:36028562}.; PTM: Phosphorylation on Ser-406; Ser-408 or Ser-410 and on Ser-527 or Ser-531 by ecto-protein kinases favors heterotypic cell-cell interactions. {ECO:0000269|PubMed:19065266}. | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:11742812}. Cell membrane {ECO:0000269|PubMed:11311135, ECO:0000269|PubMed:11389679, ECO:0000269|PubMed:11557028, ECO:0000269|PubMed:11564694, ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:15769744, ECO:0000269|PubMed:16496379, ECO:0000269|PubMed:25998567,... | null | null | null | null | null | FUNCTION: Acts as a chaperone that facilitates biogenesis and trafficking of functional transporters heterodimers to the plasma membrane. Forms heterodimer with SLC7 family transporters (SLC7A5, SLC7A6, SLC7A7, SLC7A8, SLC7A10 and SLC7A11), a group of amino-acid antiporters (PubMed:10574970, PubMed:10903140, PubMed:115... | Homo sapiens (Human) |
P08199 | NUCL_MESAU | MVKLAKAGKTHGEAKKMAPPPKEVEEDSEDEEMSEEEDDSSGEEVVIPQKKGKKATATPAKKVVVSQTKKVAVPTPAKKAAVTPGKKAAATPAKKAVTPAKAVATPGKKGATQAKALVATPGKKGAVTPAKGAKNGKNAKKEDSDEDEDDDDDEDDSDEDEEDEEEDEFEPPVVKGKQGKVAAAAPASEDEDEEEDEEEEEEDEEEEDDSEEEEAMEITPAKGKKAPAKVVPVKAKNVAEEDDDDEEEDEDEEEDEEEEEDEEEEEEEEEEEPVKPAPGKRKKEMTKQKEVPEAKKQKVEGSESTTPFNLFIGNLNPNKS... | null | null | positive regulation of mRNA splicing, via spliceosome [GO:0048026] | cytoplasm [GO:0005737]; nucleolus [GO:0005730]; ribonucleoprotein complex [GO:1990904]; spliceosomal complex [GO:0005681] | RNA binding [GO:0003723]; telomeric DNA binding [GO:0042162] | PF00076; | 3.30.70.330; | null | PTM: Some glutamate residues are glycylated by TTLL8. This modification occurs exclusively on glutamate residues and results in a glycine chain on the gamma-carboxyl group (By similarity). {ECO:0000250}.; PTM: Symmetrically methylated by PRMT5 (By similarity). {ECO:0000250|UniProtKB:P19338}. | SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm {ECO:0000250}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in... | Mesocricetus auratus (Golden hamster) |
P08200 | IDH_ECOLI | MESKVVVPAQGKKITLQNGKLNVPENPIIPYIEGDGIGVDVTPAMLKVVDAAVEKAYKGERKISWMEIYTGEKSTQVYGQDVWLPAETLDLIREYRVAIKGPLTTPVGGGIRSLNVALRQELDLYICLRPVRYYQGTPSPVKHPELTDMVIFRENSEDIYAGIEWKADSADAEKVIKFLREEMGVKKIRFPEHCGIGIKPCSEEGTKRLVRAAIEYAIANDRDSVTLVHKGNIMKFTEGAFKDWGYQLAREEFGGELIDGGPWLKVKNPNTGKEIVIKDVIADAFLQQILLRPAEYDVIACMNLNGDYISDALAAQVGGI... | 1.1.1.42 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:7761851}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:7761851}; | electron transport chain [GO:0022900]; glyoxylate cycle [GO:0006097]; response to oxidative stress [GO:0006979]; tricarboxylic acid cycle [GO:0006099] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | guanosine tetraphosphate binding [GO:0097216]; isocitrate dehydrogenase (NADP+) activity [GO:0004450]; magnesium ion binding [GO:0000287]; NAD binding [GO:0051287] | PF00180; | 3.40.718.10; | Isocitrate and isopropylmalate dehydrogenases family | PTM: Phosphorylation state of this enzyme is controlled by isocitrate dehydrogenase kinase/phosphatase (AceK). {ECO:0000269|PubMed:2204109}.; PTM: Succinylation probably inhibits enzymatic activity. {ECO:0000269|PubMed:21151122}. | null | CATALYTIC ACTIVITY: Reaction=D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH; Xref=Rhea:RHEA:19629, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.42; Evidence={ECO:0000269|PubMed:21151122, ECO:0000269|PubMed:3112144, ECO:0000269|PubMed:7761851, ECO:0... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11.4 uM for isocitrate {ECO:0000269|PubMed:7819221}; KM=13 uM for isocitrate {ECO:0000269|PubMed:7761851}; | null | null | null | null | Escherichia coli (strain K12) |
P08201 | NIRB_ECOLI | MSKVRLAIIGNGMVGHRFIEDLLDKSDAANFDITVFCEEPRIAYDRVHLSSYFSHHTAEELSLVREGFYEKHGIKVLVGERAITINRQEKVIHSSAGRTVFYDKLIMATGSYPWIPPIKGSDTQDCFVYRTIEDLNAIESCARRSKRGAVVGGGLLGLEAAGALKNLGIETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEIVQEGVEARKTMRFADGSELEVDFIVFSTGIRPRDKLATQCGLDVAPRGGIVINDSCQTSDPDIYAIGECASWNNRVFGLVAPGYKMAQVAVDHILGSENAFEGADLS... | 1.7.1.15 | COFACTOR: Name=siroheme; Xref=ChEBI:CHEBI:60052; Note=Binds 1 siroheme per subunit.; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 1 [4Fe-4S] cluster per subunit.; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; | fermentation [GO:0006113]; NADH oxidation [GO:0006116]; nitrate assimilation [GO:0042128] | nitrite reductase complex [NAD(P)H] [GO:0009344] | 2 iron, 2 sulfur cluster binding [GO:0051537]; 4 iron, 4 sulfur cluster binding [GO:0051539]; flavin adenine dinucleotide binding [GO:0050660]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; NADP binding [GO:0050661]; nitrite reductase NADH activity [GO:0106316] | PF04324;PF01077;PF03460;PF07992;PF18267; | 3.30.390.30;3.90.480.20;1.10.10.1100;3.50.50.60;3.30.413.10; | Nitrite and sulfite reductase 4Fe-4S domain family | null | null | CATALYTIC ACTIVITY: Reaction=2 H2O + 3 NAD(+) + NH4(+) = 5 H(+) + 3 NADH + nitrite; Xref=Rhea:RHEA:24628, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:28938, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.7.1.15; | null | PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation). | null | null | null | Escherichia coli (strain K12) |
P08203 | ARAD_ECOLI | MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVFVIKPSGVDYSVMTADDMVVVSIETGEVVEGTKKPSSDTPTHRLLYQAFPSIGGIVHTHSRHATIWAQAGQSIPATGTTHADYFYGTIPCTRKMTDAEINGEYEWETGNVIVETFEKQGIDAAQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFCRQLAPQLPDMQQTLLDKHYLRKHGAKAYYGQ | 5.1.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00989, ECO:0000269|PubMed:10769139, ECO:0000269|PubMed:11732895, ECO:0000269|PubMed:11732896, ECO:0000269|PubMed:9548961}; Note=Binds 1 zinc ion per subunit (PubMed:10769139, PubMed:11732895, PubMed:11732896, PubMed:9548961). Also able t... | L-arabinose catabolic process to xylulose 5-phosphate [GO:0019569]; L-lyxose metabolic process [GO:0019324]; pentose catabolic process [GO:0019323] | cytosol [GO:0005829]; protein-containing complex [GO:0032991] | aldehyde-lyase activity [GO:0016832]; identical protein binding [GO:0042802]; L-ribulose-phosphate 4-epimerase activity [GO:0008742]; zinc ion binding [GO:0008270] | PF00596; | 3.40.225.10; | Aldolase class II family, AraD/FucA subfamily | null | null | CATALYTIC ACTIVITY: Reaction=L-ribulose 5-phosphate = D-xylulose 5-phosphate; Xref=Rhea:RHEA:22368, ChEBI:CHEBI:57737, ChEBI:CHEBI:58226; EC=5.1.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00989, ECO:0000269|PubMed:10769138, ECO:0000269|PubMed:10769139, ECO:0000269|PubMed:11732896, ECO:0000269|PubMed:4879898, ECO:0000269|... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.17 uM for Zn(2+) {ECO:0000269|PubMed:10769139}; KM=0.29 uM for Co(2+) {ECO:0000269|PubMed:10769139}; KM=0.54 uM for Mn(2+) {ECO:0000269|PubMed:10769139}; KM=47 uM for L-ribulose 5-phosphate (LRu5P) (with zinc ion) {ECO:0000269|PubMed:10769139, ECO:0000269|PubMed:... | PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route): step 3/3. {ECO:0000255|HAMAP-Rule:MF_00989, ECO:0000305|PubMed:13890280}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:4879898}; | null | FUNCTION: Involved in the degradation of L-arabinose (PubMed:13890280). Catalyzes the interconversion of L-ribulose 5-phosphate (LRu5P) and D-xylulose 5-phosphate (D-Xu5P) via a retroaldol/aldol mechanism (carbon-carbon bond cleavage analogous to a class II aldolase reaction). {ECO:0000255|HAMAP-Rule:MF_00989, ECO:0000... | Escherichia coli (strain K12) |
P08207 | S10AA_MOUSE | MPSQMEHAMETMMLTFHRFAGDKDHLTKEDLRVLMEREFPGFLENQKDPLAVDKIMKDLDQCRDGKVGFQSFLSLVAGLTIACNDYFVVNMKQKGKK | null | null | membrane raft assembly [GO:0001765]; mRNA transcription by RNA polymerase II [GO:0042789]; positive regulation of exocytosis [GO:0045921]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of plasma membrane repair [GO:1905686]; positive regulation of plasminogen activation [GO:0010756]; ... | AnxA2-p11 complex [GO:1990665]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; membrane raft [GO:0045121]; nuclear matrix [GO:0016363]; plasma membrane [GO:0005886]; plasma membrane protein complex [GO:0098797]; RNA polymerase ... | calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; protein homodimerization activity [GO:0042803]; transmembrane transporter binding [GO:0044325] | PF01023; | 1.10.238.10; | S-100 family | null | null | null | null | null | null | null | FUNCTION: Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase. | Mus musculus (Mouse) |
P08217 | CEL2A_HUMAN | MIRTLLLSTLVAGALSCGDPTYPPYVTRVVGGEEARPNSWPWQVSLQYSSNGKWYHTCGGSLIANSWVLTAAHCISSSRTYRVGLGRHNLYVAESGSLAVSVSKIVVHKDWNSNQISKGNDIALLKLANPVSLTDKIQLACLPPAGTILPNNYPCYVTGWGRLQTNGAVPDVLQQGRLLVVDYATCSSSAWWGSSVKTSMICAGGDGVISSCNGDSGGPLNCQASDGRWQVHGIVSFGSRLGCNYYHKPSVFTRVSNYIDWINSVIANN | 3.4.21.71 | null | insulin catabolic process [GO:1901143]; proteolysis [GO:0006508]; regulation of insulin secretion [GO:0050796]; regulation of platelet aggregation [GO:0090330]; response to insulin [GO:0032868] | cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; keratohyalin granule [GO:0036457] | endopeptidase activity [GO:0004175]; serine hydrolase activity [GO:0017171]; serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.40.10.10; | Peptidase S1 family, Elastase subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31358993}. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Leu-|-Xaa, Met-|-Xaa and Phe-|-Xaa. Hydrolyzes elastin.; EC=3.4.21.71; Evidence={ECO:0000269|PubMed:31358993}; | null | null | null | null | FUNCTION: Elastase that enhances insulin signaling and might have a physiologic role in cellular glucose metabolism. Circulates in plasma and reduces platelet hyperactivation, triggers both insulin secretion and degradation, and increases insulin sensitivity. {ECO:0000269|PubMed:31358993}. | Homo sapiens (Human) |
P08218 | CEL2B_HUMAN | MIRTLLLSTLVAGALSCGVSTYAPDMSRMLGGEEARPNSWPWQVSLQYSSNGQWYHTCGGSLIANSWVLTAAHCISSSGIYRVMLGQHNLYVAESGSLAVSVSKIVVHKDWNSDQVSKGNDIALLKLANPVSLTDKIQLACLPPAGTILPNNYPCYVTGWGRLQTNGALPDDLKQGQLLVVDYATCSSSGWWGSTVKTNMICAGGDGVICTCNGDSGGPLNCQASDGRWEVHGIGSLTSVLGCNYYYKPSIFTRVSNYNDWINSVIANN | 3.4.21.71 | null | proteolysis [GO:0006508] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.40.10.10; | Peptidase S1 family, Elastase subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Leu-|-Xaa, Met-|-Xaa and Phe-|-Xaa. Hydrolyzes elastin.; EC=3.4.21.71; | null | null | null | null | FUNCTION: Acts upon elastin. | Homo sapiens (Human) |
P08219 | GBRA1_BOVIN | MKKSPGLSDYLWAWTLFLSTLTGRSYGQPSLQDELKDNTTVFTRILDRLLDGYDNRLRPGLGERVTEVKTDIFVTSFGPVSDHDMEYTIDVFFRQSWKDERLKFKGPMTVLRLNNLMASKIWTPDTFFHNGKKSVAHNMTMPNKLLRITEDGTLLYTMRLTVRAECPMHLEDFPMDAHACPLKFGSYAYTRAEVVYEWTREPARSVVVAEDGSRLNQYDLLGQTVDSGIVQSSTGEYVVMTTHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVC... | null | null | chloride transmembrane transport [GO:1902476]; gamma-aminobutyric acid signaling pathway [GO:0007214]; inhibitory synapse assembly [GO:1904862]; nervous system process [GO:0050877]; regulation of postsynaptic membrane potential [GO:0060078]; signal transduction [GO:0007165]; synaptic transmission, GABAergic [GO:0051932... | chloride channel complex [GO:0034707]; cytoplasmic vesicle membrane [GO:0030659]; dendrite membrane [GO:0032590]; GABA-A receptor complex [GO:1902711]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]; transmembrane transpor... | benzodiazepine receptor activity [GO:0008503]; GABA-A receptor activity [GO:0004890]; GABA-gated chloride ion channel activity [GO:0022851]; inhibitory extracellular ligand-gated monoatomic ion channel activity [GO:0005237] | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily, GABRA1 sub-subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000305|PubMed:3037384}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P14867}. Cell membrane {ECO:0000269|PubMed:3037384}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P14867}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P62813}. | CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:3037384}; | null | null | null | null | FUNCTION: Alpha subunit of the heteropentameric ligand-gated chloride channel gated by gamma-aminobutyric acid (GABA), a major inhibitory neurotransmitter in the brain. GABA-gated chloride channels, also named GABA(A) receptors (GABAAR), consist of five subunits arranged around a central pore and contain GABA active bi... | Bos taurus (Bovine) |
P08220 | GBRB1_BOVIN | MWTVQNRESLGLLSFPVMIAMVCCAHSANEPSNMSYVKETVDRLLKGYDIRLRPDFGGPPVDVGMRIDVASIDMVSEVNMDYTLTMYFQQSWKDKRLSYSGIPLNLTLDNRVADQLWVPDTYFLNDKKSFVHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDEQNCTLEIESYGYTTDDIEFYWNGGEGAVTGVNKIELPQFSIVDYKMVSKKVEFTTGAYPRLSLSFRLKRNIGYFILQTYMPSTLITILSWVSFWINYDASAARVALGITTVLTMTTISTHLRETLPKIPYVKAIDIYLMGCFVFVFLA... | null | null | cellular response to histamine [GO:0071420]; chemical synaptic transmission [GO:0007268]; chloride transmembrane transport [GO:1902476]; gamma-aminobutyric acid signaling pathway [GO:0007214]; monoatomic ion transport [GO:0006811]; nervous system process [GO:0050877]; regulation of membrane potential [GO:0042391]; sign... | chloride channel complex [GO:0034707]; GABA-A receptor complex [GO:1902711]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]; transmembrane transporter complex [GO:1902495] | GABA-A receptor activity [GO:0004890]; GABA-gated chloride ion channel activity [GO:0022851]; ligand-gated monoatomic ion channel activity [GO:0015276]; neurotransmitter receptor activity [GO:0030594] | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily, GABRB1 sub-subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000269|PubMed:3037384}; Multi-pass membrane protein {ECO:0000269|PubMed:3037384}. Cell membrane {ECO:0000269|PubMed:3037384}; Multi-pass membrane protein {ECO:0000269|PubMed:3037384}. | CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:3037384}; | null | null | null | null | FUNCTION: Beta subunit of the heteropentameric ligand-gated chloride channel gated by gamma-aminobutyric acid (GABA), a major inhibitory neurotransmitter in the brain (PubMed:3037384). GABA-gated chloride channels, also named GABA(A) receptors (GABAAR), consist of five subunits arranged around a central pore and contai... | Bos taurus (Bovine) |
P08226 | APOE_MOUSE | MKALWAVLLVTLLTGCLAEGEPEVTDQLEWQSNQPWEQALNRFWDYLRWVQTLSDQVQEELQSSQVTQELTALMEDTMTEVKAYKKELEEQLGPVAEETRARLGKEVQAAQARLGADMEDLRNRLGQYRNEVHTMLGQSTEEIRARLSTHLRKMRKRLMRDAEDLQKRLAVYKAGAREGAERGVSAIRERLGPLVEQGRQRTANLGAGAAQPLRDRAQAFGDRIRGRLEEVGNQARDRLEEVREHMEEVRSKMEEQTQQIRLQAEIFQARLKGWFEPIVEDMHRQWANLMEKIQASVATNPIITPVAQENQ | null | null | acylglycerol homeostasis [GO:0055090]; amyloid precursor protein metabolic process [GO:0042982]; artery morphogenesis [GO:0048844]; cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; chylomicron remnant clearance... | cell surface [GO:0009986]; chylomicron [GO:0042627]; chylomicron remnant [GO:0034360]; cytosol [GO:0005829]; dendrite [GO:0030425]; discoidal high-density lipoprotein particle [GO:0034365]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; ... | amyloid-beta binding [GO:0001540]; antioxidant activity [GO:0016209]; cholesterol transfer activity [GO:0120020]; enzyme binding [GO:0019899]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; hydroxyapatite binding [GO:0046848]; identical protein binding [GO:0042802]; lipid transporter a... | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000269|PubMed:29516132}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular m... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Mus musculus (Mouse) |
P08228 | SODC_MOUSE | MAMKAVCVLKGDGPVQGTIHFEQKASGEPVVLSGQITGLTEGQHGFHVHQYGDNTQGCTSAGPHFNPHSKKHGGPADEERHVGDLGNVTAGKDGVANVSIEDRVISLSGEHSIIGRTMVVHEKQDDLGKGGNEESTKTGNAGSRLACGVIGIAQ | 1.15.1.1 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:P00441}; Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:P00441}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00441}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00441}; | action potential initiation [GO:0099610]; anterograde axonal transport [GO:0008089]; apoptotic process [GO:0006915]; auditory receptor cell stereocilium organization [GO:0060088]; determination of adult lifespan [GO:0008340]; ectopic germ cell programmed cell death [GO:0035234]; embryo implantation [GO:0007566]; gene e... | 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]; mitochondrial intermembrane space [GO:0005758]; mitoc... | 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|UniProtKB:P00441}.; PTM: Succinylation, adjacent to copper catalytic site, probably inhibits activity. Desuccinylation by SIRT5 enhances activity. {ECO:0000250|UniProtKB:P00441}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00441}. Nucleus {ECO:0000250|UniProtKB:P00441}. | 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:0000250|UniProtKB:P00441}; | null | null | null | null | FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. {ECO:0000250|UniProtKB:P00441}. | Mus musculus (Mouse) |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.