Detail Information for IndEnz0002014236
IED ID IndEnz0002014236
Enzyme Type ID protease014236
Protein Name B2 bradykinin receptor
B2R
BK-2 receptor
Gene Name BDKRB2 BKR2
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MFSPWKISMFLSVREDSVPTTASFSADMLNVTLQGPTLNGTFAQSKCPQVEWLGWLNTIQPPFLWVLFVLATLENIFVLSVFCLHKSSCTVAEIYLGNLAAADLILACGLPFWAITISNNFDWLFGETLCRVVNAIISMNLYSSICFLMLVSIDRYLALVKTMSMGRMRGVRWAKLYSLVIWGCTLLLSSPMLVFRTMKEYSDEGHNVTACVISYPSLIWEVFTNMLLNVVGFLLPLSVITFCTMQIMQVLRNNEMQKFKEIQTERRATVLVLVVLLLFIICWLPFQISTFLDTLHRLGILSSCQDERIIDVITQIASFMAYSNSCLNPLVYVIVGKRFRKKSWEVYQGVCQKGGCRSEPIQMENSMGTLRTSISVERQIHKLQDWAGSRQ
Enzyme Length 391
Uniprot Accession Number P30411
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Receptor for bradykinin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (1); Chain (1); Disulfide bond (1); Glycosylation (3); Lipidation (1); Modified residue (6); Natural variant (2); Topological domain (8); Transmembrane (7)
Keywords 3D-structure;Alternative splicing;Cell membrane;Direct protein sequencing;Disulfide bond;G-protein coupled receptor;Glycoprotein;Lipoprotein;Membrane;Palmitate;Phosphoprotein;Receptor;Reference proteome;Transducer;Transmembrane;Transmembrane helix
Interact With P01042
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Modified Residue MOD_RES 156; /note=Phosphotyrosine; /evidence=ECO:0000250|UniProtKB:P25023; MOD_RES 347; /note=Phosphotyrosine; /evidence=ECO:0000250|UniProtKB:P25023; MOD_RES 366; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P25023; MOD_RES 369; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P25023; MOD_RES 373; /note=Phosphoserine; by GRK6; /evidence=ECO:0000269|PubMed:11517230; MOD_RES 375; /note=Phosphoserine; by GRK6; /evidence=ECO:0000269|PubMed:11517230
Post Translational Modification
Signal Peptide
Structure 3D Electron microscopy (1)
Cross Reference PDB 7F2O;
Mapped Pubmed ID 10191087; 10553917; 11324803; 11409654; 11446495; 11517947; 11699055; 11710536; 11747451; 11908480; 11954665; 12025967; 12039525; 12063092; 12107246; 12130679; 12450400; 12481150; 12489797; 12522467; 12640257; 12705334; 12851878; 14499231; 14607851; 15033977; 15112434; 15114524; 15117835; 15161928; 15301669; 15634338; 15643125; 15643126; 15654972; 15664665; 15771553; 15805101; 15894833; 16144969; 16226010; 16263113; 16294326; 16461337; 16489763; 16600946; 16740128; 16754659; 16950802; 17030791; 17077303; 17110500; 17207964; 17299793; 17303584; 17328065; 17363739; 17420253; 17522594; 17569300; 17593394; 17852785; 18039523; 18096516; 18127230; 18180402; 18187413; 18258629; 18430865; 18467203; 18577758; 18577888; 18810490; 18927465; 18938142; 19017652; 19038786; 1905813; 19074839; 19086053; 19110485; 19120546; 19339996; 19404481; 19420105; 19456859; 19565561; 19578796; 19580784; 19628666; 19716087; 19725054; 19744011; 19854233; 19885862; 19913121; 20036225; 20044476; 20045189; 20050188; 20189583; 20201926; 20300066; 20511677; 20592051; 20602751; 20628086; 20856803; 20944660; 20952631; 21052031; 21108627; 21145390; 21210858; 21451024; 21586566; 21600887; 21602894; 21626144; 21719759; 21871009; 21986469; 22016392; 22047990; 22108573; 22304584; 22468762; 22653778; 22706620; 22900090; 22935637; 23093849; 23127247; 23132855; 23176367; 23224295; 23243416; 23275384; 23351078; 23362199; 23428345; 23454239; 23588115; 23597562; 23613132; 23730990; 23805043; 23826374; 24047499; 24211782; 24236827; 24304135; 24401952; 25109623; 25289859; 2534964; 25529519; 25641172; 25713410; 25842860; 25970620; 26235941; 26360782; 26362411; 26588817; 26764266; 26907838; 26955769; 26982743; 27007662; 2748346; 27696692; 28069442; 28077802; 28099911; 2834384; 29034546; 29334504; 29894755; 30206938; 30236981; 30478260; 30817230; 3086311; 31059006; 31360266; 31552837; 32114020; 32361393; 33412234; 33497625; 3366244; 33686021; 34384552; 34518695; 8015379; 8063797; 8664309;
Motif
Gene Encoded By
Mass 44,461
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda