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Reviewed, UniProtKB/Swiss-Prot P21146 (ARBK1_BOVIN)

Last modified June 16, 2009. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Beta-adrenergic receptor kinase 1
      Short name=Beta-ARK-1
    EC=2.7.11.15
Alternative name(s):
    G-protein-coupled receptor kinase 2
Gene names
Name: ADRBK1
Synonyms: GRK2
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length689 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors, probably inducing a desensitization of them.

Catalytic activity

ATP + [beta-adrenergic receptor] = ADP + [beta-adrenergic receptor] phosphate.

Subunit structure

Interacts with GIT1. Interacts with, and phosphorylates chemokine-stimulated CCR5 By similarity.

Tissue specificity

Ubiquitous; brain, spleen > heart, lung > kidney.

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. GPRK subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 PH domain.

Contains 1 protein kinase domain.

Contains 1 RGS domain.

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Ontologies

Keywords
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processcardiac muscle contraction

Inferred from mutant phenotype. Source: UniProtKB

desensitization of G-protein coupled receptor protein signaling pathway

Inferred from mutant phenotype. Source: UniProtKB

heart development

Inferred from sequence or structural similarity. Source: AgBase

intracellular protein transport

Inferred from mutant phenotype. Source: UniProtKB

muscarinic acetylcholine receptor signaling pathway

Inferred from direct assay. Source: UniProtKB

negative regulation of striated muscle contraction

Inferred from mutant phenotype. Source: UniProtKB

negative regulation of the force of heart contraction by chemical signal

Inferred from mutant phenotype. Source: UniProtKB

peptidyl-serine phosphorylation

Inferred from direct assay. Source: UniProtKB

   Cellular componentcytosol

Inferred from direct assay. Source: UniProtKB

membrane

Inferred from direct assay. Source: UniProtKB

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

G-protein coupled receptor kinase activity

Inferred from direct assay. Source: UniProtKB

beta-adrenergic receptor kinase activity

Inferred from electronic annotation. Source: EC

protein binding

Inferred from sequence or structural similarity. Source: AgBase

signal transducer activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 689689Beta-adrenergic receptor kinase 1
PRO_0000085626

Regions

Domain54 – 175122RGS
Domain191 – 453263Protein kinase
Domain454 – 52168AGC-kinase C-terminal
Domain558 – 65295PH
Nucleotide binding197 – 2059ATP By similarity
Region1 – 190190N-terminal
Region454 – 689236C-terminal

Sites

Active site3171Proton acceptor By similarity
Binding site2201ATP By similarity

Amino acid modifications

Modified residue6701Phosphoserine By similarity

Secondary structure

1 ........................................................................................................ 689
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P21146-1 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 4AB95DB5E630B9DA

FASTA68979,647
        10         20         30         40         50         60 
MADLEAVLAD VSYLMAMEKS KATPAARASK KILLPEPSIR SVMQKYLEDR GEVTFEKIFS 

        70         80         90        100        110        120 
QKLGYLLFRD FCLKHLEEAK PLVEFYEEIK KYEKLETEEE RLVCSREIFD TYIMKELLAC 

       130        140        150        160        170        180 
SHPFSKSAIE HVQGHLVKKQ VPPDLFQPYI EEICQNLRGD VFQKFIESDK FTRFCQWKNV 

       190        200        210        220        230        240 
ELNIHLTMND FSVHRIIGRG GFGEVYGCRK ADTGKMYAMK CLDKKRIKMK QGETLALNER 

       250        260        270        280        290        300 
IMLSLVSTGD CPFIVCMSYA FHTPDKLSFI LDLMNGGDLH YHLSQHGVFS EADMRFYAAE 

       310        320        330        340        350        360 
IILGLEHMHN RFVVYRDLKP ANILLDEHGH VRISDLGLAC DFSKKKPHAS VGTHGYMAPE 

       370        380        390        400        410        420 
VLQKGVAYDS SADWFSLGCM LFKLLRGHSP FRQHKTKDKH EIDRMTLTMA VELPDSFSPE 

       430        440        450        460        470        480 
LRSLLEGLLQ RDVNRRLGCL GRGAQEVKES PFFRSLDWQM VFLQKYPPPL IPPRGEVNAA 

       490        500        510        520        530        540 
DAFDIGSFDE EDTKGIKLLD SDQELYRNFP LTISERWQQE VAETVFDTIN AETDRLEARK 

       550        560        570        580        590        600 
KTKNKQLGHE EDYALGKDCI MHGYMSKMGN PFLTQWQRRY FYLFPNRLEW RGEGEAPQSL 

       610        620        630        640        650        660 
LTMEEIQSVE ETQIKERKCL LLKIRGGKQF VLQCDSDPEL VQWKKELRDA YREAQQLVQR 

       670        680 
VPKMKNKPRS PVVELSKVPL IQRGSANGL

« Hide

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References

[1]"Beta-adrenergic receptor kinase: primary structure delineates a multigene family."
Benovic J.L., Deblasi A., Stone W.C., Caron M.G., Lefkowitz R.J.
Science 246:235-240(1989) [PubMed: 2552582] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Beta2-adrenergic receptor regulation by GIT1, a G protein-coupled receptor kinase-associated ADP ribosylation factor GTPase-activating protein."
Premont R.T., Claing A., Vitale N., Freeman J.L.R., Pitcher J.A., Patton W.A., Moss J., Vaughan M., Lefkowitz R.J.
Proc. Natl. Acad. Sci. U.S.A. 95:14082-14087(1998) [PubMed: 9826657] [Abstract]
Cited for: INTERACTION WITH GIT1.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M34019 mRNA. Translation: AAA30384.1.
IPIIPI00695737.
PIRA40088.
RefSeqNP_777135.1.
UniGeneBt.4693

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1OMWX-ray2.50A1-689[»]
1YM7X-ray4.50A/B/C/D1-689[»]
2BCJX-ray3.06A1-689[»]
ModBaseSearch...

Genome annotation databases

EnsemblENSBTAG00000005832. Bos taurus. [Contig view]
GeneID282682.
KEGGbta:282682.

Phylogenomic databases

HOVERGENP21146.

Enzyme and pathway databases

BRENDA2.7.11.15. 251.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR015743. B-adrenergic_rcpt_kinase.
IPR000239. GPCR_kinase.
IPR011993. PH_type.
IPR001849. Pleckstrin_homology.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR000342. Regulat_G_prot_signal.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]
Gene3DG3DSA:2.30.29.30. PH_type. 1 hit.
PANTHERPTHR22985:SF5. BARK. 1 hit.
PfamPF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view]
PRINTSPR00717. GPCRKINASE.
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00233. PH. 1 hit.
SM00315. RGS. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameARBK1_BOVIN
AccessionPrimary (citable) accession number: P21146
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: June 16, 2009
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents