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Showing Protein Beta-adrenergic receptor kinase 1 (HMDBP01262)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 3 metabolites
Identification
HMDB Protein ID HMDBP01262
Secondary Accession Numbers
  • 6558
Name Beta-adrenergic receptor kinase 1
Synonyms
  1. Beta-ARK-1
  2. G-protein coupled receptor kinase 2
Gene Name ADRBK1
Protein Type Enzyme
Biological Properties
General Function Involved in protein serine/threonine kinase activity
Specific Function Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors, probably inducing a desensitization of them. Key regulator of LPAR1 signaling. Competes with RALA for binding to LPAR1 thus affecting the signaling properties of the receptor. Desensitizes LPAR1 and LPAR2 in a phosphorylation-independent manner
Pathways Not Available
Reactions Not Available
GO Classification
Function
binding
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
kinase activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
g-protein coupled receptor kinase activity
molecular transducer activity
signal transducer activity
protein kinase activity
protein serine/threonine kinase activity
Process
phosphorus metabolic process
phosphate metabolic process
metabolic process
biological regulation
regulation of biological process
cellular metabolic process
regulation of cellular process
signal transduction
protein amino acid phosphorylation
phosphorylation
Cellular Location Not Available
Gene Properties
Chromosome Location Chromosome:1
Locus 11q13.1
SNPs ADRBK1
Gene Sequence 
>2070 bp
ATGGCGGACCTGGAGGCGGTGCTGGCCGACGTGAGCTACCTGATGGCCATGGAGAAGAGC
AAGGCCACGCCGGCCGCGCGCGCCAGCAAGAAGATACTGCTGCCCGAGCCCAGCATCCGC
AGTGTCATGCAGAAGTACCTGGAGGACCGGGGCGAGGTGACCTTTGAGAAGATCTTTTCC
CAGAAGCTGGGGTACCTGCTCTTCCGAGACTTCTGCCTGAACCACCTGGAGGAGGCCAGG
CCCTTGGTGGAATTCTATGAGGAGATCAAGAAGTACGAGAAGCTGGAGACGGAGGAGGAG
CGTGTGGCCCGCAGCCGGGAGATCTTCGACTCATACATCATGAAGGAGCTGCTGGCCTGC
TCGCATCCCTTCTCGAAGAGTGCCACTGAGCATGTCCAAGGCCACCTGGGGAAGAAGCAG
GTGCCTCCGGATCTCTTCCAGCCATACATCGAAGAGATTTGTCAAAACCTCCGAGGGGAC
GTGTTCCAGAAATTCATTGAGAGCGATAAGTTCACACGGTTTTGCCAGTGGAAGAATGTG
GAGCTCAACATCCACCTGACCATGAATGACTTCAGCGTGCATCGCATCATTGGGCGCGGG
GGCTTTGGCGAGGTCTATGGGTGCCGGAAGCGTGACACAGGCAAGATGTACGCCATGAAG
TGCCTGGACAAAAAGCGCATCAAGATGAAGCAGGGGGAGACCCTGGCCCTGAACGAGCGC
ATCATGCTCTCGCTCGTCAGCACTGGGGACTGCCCATTCATTGTCTGCATGTCATACGCG
TTCCACACGCCAGACAAGCTCAGCTTCATCCTGGACCTCATGAACGGTGGGGACCTGCAC
TACCACCTCTCCCAGCACGGGGTCTTCTCAGAGGCTGACATGCGCTTCTATGCGGCCGAG
ATCATCCTGGGCCTGGAGCACATGCACAACCGCTTCGTGGTCTACCGGGACCTGAAGCCA
GCCAACATCCTTCTGGACGAGCATGGCCACGTGCGGATCTCGGACCTGGGCCTGGCCTGT
GACTTCTCCAAGAAGAAGCCCCATGCCAGCGTGGGCACCCACGGGTACATGGCTCCGGAG
GTCCTGCAGAAGGGCGTGGCCTACGACAGCAGTGCCGACTGGTTCTCTCTGGGGTGCATG
CTCTTCAAGTTGCTGCGGGGGCACAGCCCCTTCCGGCAGCACAAGACCAAAGACAAGCAT
GAGATCGACCGCATGACGCTGACGATGGCCGTGGAGCTGCCCGACTCCTTCTCCCCTGAA
CTACACTCCCTGCTGGAGGGGTTGCTGCAGAGGGATGTCAACCGGAGATTGGGCTGCCTG
GGCCGAGGGGCTCAGGAGGTGAAAGAGAGCCCCTTTTTCCGCTCCCTGGACTGGCAGATG
GTCTTCTTGCAGAGGTACCCTCCCCCGCTGATCCCCCCACGAGGGGAGGTGAACGCGGCC
GACGCCTTCGACATTGGCTCCTTCGATGAGGAGGACACAAAAGGAATCAAGTTACTGGAC
AGTGATCAGGAGCTCTACCGCAACTTCCCCCTCACCATCTCGGAGCGGTGGCAGCAGGAG
GTGGCAGAGACTGTCTTCGACACCATCAACGCTGAGACAGACCGGCTGGAGGCTCGCAAG
AAAGCCAAGAACAAGCAGCTGGGCCATGAGGAAGACTACGCCCTGGGCAAGGACTGCATC
ATGCATGGCTACATGTCCAAGATGGGCAACCCCTTTCTGACCCAGTGGCAGCGGCGGTAC
TTCTACCTGTTCCCCAACCGCCTCGAGTGGCGGGGCGAGGGCGAGGCCCCGCAGAGCCTG
CTGACCATGGAGGAGATCCAGTCGGTGGAGGAGACGCAGATCAAGGAGCGCAAGTGCCTG
CTCCTCAAGATCCGCGGTGGGAAACAGTTCATTTTGCAGTGCGATAGCGACCCTGAGCTG
GTGCAGTGGAAGAAGGAGCTGCGCGACGCCTACCGCGAGGCCCAGCAGCTGGTGCAGCGG
GTGCCCAAGATGAAGAACAAGCCGCGCTCGCCCGTGGTGGAGCTGAGCAAGGTGCCGCTG
GTCCAGCGCGGCAGTGCCAACGGCCTCTGA
Protein Properties
Number of Residues 689
Molecular Weight 79573.0
Theoretical pI 7.3
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence 
>Beta-adrenergic receptor kinase 1
MADLEAVLADVSYLMAMEKSKATPAARASKKILLPEPSIRSVMQKYLEDRGEVTFEKIFS
QKLGYLLFRDFCLNHLEEARPLVEFYEEIKKYEKLETEEERVARSREIFDSYIMKELLAC
SHPFSKSATEHVQGHLGKKQVPPDLFQPYIEEICQNLRGDVFQKFIESDKFTRFCQWKNV
ELNIHLTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNER
IMLSLVSTGDCPFIVCMSYAFHTPDKLSFILDLMNGGDLHYHLSQHGVFSEADMRFYAAE
IILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHASVGTHGYMAPE
VLQKGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAVELPDSFSPE
LRSLLEGLLQRDVNRRLGCLGRGAQEVKESPFFRSLDWQMVFLQKYPPPLIPPRGEVNAA
DAFDIGSFDEEDTKGIKLLDSDQELYRNFPLTISERWQQEVAETVFDTINAETDRLEARK
KAKNKQLGHEEDYALGKDCIMHGYMSKMGNPFLTQWQRRYFYLFPNRLEWRGEGEAPQSL
LTMEEIQSVEETQIKERKCLLLKIRGGKQFILQCDSDPELVQWKKELRDAYREAQQLVQR
VPKMKNKPRSPVVELSKVPLVQRGSANGL
GenBank ID Protein 288308
UniProtKB/Swiss-Prot ID P25098
UniProtKB/Swiss-Prot Entry Name ARBK1_HUMAN
PDB IDs
GenBank Gene ID X61157
GeneCard ID ADRBK1
GenAtlas ID ADRBK1
HGNC ID HGNC:289
References
General References
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  2. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. doi: 10.1074/mcp.M800588-MCP200. Epub 2009 Apr 15. [PubMed:19369195 ]
  3. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed:18088087 ]
  4. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  5. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed:17344846 ]
  6. Benovic JL, Stone WC, Huebner K, Croce C, Caron MG, Lefkowitz RJ: cDNA cloning and chromosomal localization of the human beta-adrenergic receptor kinase. FEBS Lett. 1991 May 20;283(1):122-6. [PubMed:2037065 ]
  7. Chuang TT, Sallese M, Ambrosini G, Parruti G, De Blasi A: High expression of beta-adrenergic receptor kinase in human peripheral blood leukocytes. Isoproterenol and platelet activating factor can induce kinase translocation. J Biol Chem. 1992 Apr 5;267(10):6886-92. [PubMed:1339451 ]
  8. Penn RB, Benovic JL: Structure of the human gene encoding the beta-adrenergic receptor kinase. J Biol Chem. 1994 May 27;269(21):14924-30. [PubMed:8195124 ]
  9. Aragay AM, Mellado M, Frade JM, Martin AM, Jimenez-Sainz MC, Martinez-A C, Mayor F Jr: Monocyte chemoattractant protein-1-induced CCR2B receptor desensitization mediated by the G protein-coupled receptor kinase 2. Proc Natl Acad Sci U S A. 1998 Mar 17;95(6):2985-90. [PubMed:9501202 ]
  10. Oppermann M, Mack M, Proudfoot AE, Olbrich H: Differential effects of CC chemokines on CC chemokine receptor 5 (CCR5) phosphorylation and identification of phosphorylation sites on the CCR5 carboxyl terminus. J Biol Chem. 1999 Mar 26;274(13):8875-85. [PubMed:10085131 ]
  11. Aziziyeh AI, Li TT, Pape C, Pampillo M, Chidiac P, Possmayer F, Babwah AV, Bhattacharya M: Dual regulation of lysophosphatidic acid (LPA1) receptor signalling by Ral and GRK. Cell Signal. 2009 Jul;21(7):1207-17. doi: 10.1016/j.cellsig.2009.03.011. Epub 2009 Mar 21. [PubMed:19306925 ]
  12. Fushman D, Najmabadi-Haske T, Cahill S, Zheng J, LeVine H 3rd, Cowburn D: The solution structure and dynamics of the pleckstrin homology domain of G protein-coupled receptor kinase 2 (beta-adrenergic receptor kinase 1). A binding partner of Gbetagamma subunits. J Biol Chem. 1998 Jan 30;273(5):2835-43. [PubMed:9446593 ]