Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P34947 (GRK5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
G protein-coupled receptor kinase 5

EC=2.7.11.16
Alternative name(s):
G protein-coupled receptor kinase GRK5
Gene names
Name:GRK5
Synonyms:GPRK5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length590 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine kinase that phosphorylates preferentially the activated forms of a variety of G-protein-coupled receptors (GPCRs). Such receptor phosphorylation initiates beta-arrestin-mediated receptor desensitization, internalization, and signaling events leading to their down-regulation. Phosphorylates a variety of GPCRs, including adrenergic receptors, muscarinic acetylcholine receptors (more specifically Gi-coupled M2/M4 subtypes), dopamine receptors and opioid receptors. In addition to GPCRs, also phosphorylates various substrates: Hsc70-interacting protein/ST13, TP53/p53, HDAC5, and arrestin-1/ARRB1. Phosphorylation of ARRB1 by GRK5 inhibits G-protein independent MAPK1/MAPK3 signaling downstream of 5HT4-receptors. Phosphorylation of HDAC5, a repressor of myocyte enhancer factor 2 (MEF2) leading to nuclear export of HDAC5 and allowing MEF2-mediated transcription. Phosphorylation of TP53/p53, a crucial tumor suppressor, inhibits TP53/p53-mediated apoptosis. Phosphorylation of ST13 regulates internalization of the chemokine receptor. Phosphorylates rhodopsin (RHO) (in vitro) and a non G-protein-coupled receptor, LRP6 during Wnt signaling (in vitro). Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17

Catalytic activity

ATP + [G-protein-coupled receptor] = ADP + [G-protein-coupled receptor] phosphate.

Enzyme regulation

Inhibited by calmodulin with an IC50 of 50 nM. Calmodulin inhibits GRK5 association with receptor and phospholipid. Ref.7

Subunit structure

Interacts with ST13 (via the C-terminus 303-319 AA). Interacts with TP53/p53. Interacts with HTR4 (via C-terminus 330-346 AA); this interaction is promoted by 5-HT (serotonin). Interacts with HDAC5 By similarity. Ref.11 Ref.13 Ref.15

Subcellular location

Cytoplasm. Nucleus. Cell membrane; Peripheral membrane protein. Note: Predominantly localized at the plasma membrane; targeted to the cell surface through the interaction with phospholipids. Nucleus localization is regulated in a GPCR and Ca2+/calmodulin-dependent fashion. Ref.8 Ref.9

Tissue specificity

Highest levels in heart, placenta, lung > skeletal muscle > brain, liver, pancreas > kidney. Ref.1

Induction

Overexpressed during heart failure. Ref.5 Ref.7

Post-translational modification

Autophosphorylated. Autophosphorylation may play a critical role in the regulation of GRK5 kinase activity. Ref.6 Ref.14

Polymorphism

Variant Leu-41 variant is rare in European-Americans individuals but common in African-Americans individuals (40% of the African-American individuals studied carry at least one allele). Variant leu-41 is associated with decreased mortality in African-Americans with heart failure or cardiac ischemia.

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 protein kinase domain.

Contains 1 RGS domain.

Ontologies

Keywords
   Biological processApoptosis
Wnt signaling pathway
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityPolymorphism
   LigandATP-binding
Lipid-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

adenylate cyclase-modulating G-protein coupled receptor signaling pathway

Traceable author statement PubMed 8626574. Source: ProtInc

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of apoptotic process

Inferred from direct assay Ref.13. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.8. Source: UniProtKB

regulation of G-protein coupled receptor protein signaling pathway

Traceable author statement PubMed 8288567. Source: ProtInc

tachykinin receptor signaling pathway

Inferred from direct assay PubMed 17986524. Source: BHF-UCL

termination of G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Traceable author statement Ref.1. Source: ProtInc

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay Ref.8. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

G-protein coupled receptor kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

phospholipid binding

Traceable author statement PubMed 9813065. Source: ProtInc

protein kinase C binding

Traceable author statement PubMed 9813065. Source: ProtInc

protein serine/threonine kinase activity

Inferred from direct assay Ref.13. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Htr4P972888EBI-7149314,EBI-7149283From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 590590G protein-coupled receptor kinase 5
PRO_0000085971

Regions

Domain53 – 171119RGS
Domain186 – 448263Protein kinase
Domain449 – 51466AGC-kinase C-terminal
Nucleotide binding192 – 2009ATP By similarity
Region1 – 185185N-terminal
Region20 – 3920Interaction with calmodulin
Region546 – 56520Sufficient for membrane localization
Motif388 – 3958Nuclear localization signal Ref.9

Sites

Active site3111Proton acceptor By similarity
Binding site2151ATP By similarity

Amino acid modifications

Modified residue4841Phosphoserine; by autocatalysis Ref.10
Modified residue4851Phosphothreonine; by autocatalysis Ref.10

Natural variations

Natural variant411Q → L Exerts a protective effect in heart failure and ischemia. Ref.16 Ref.17
Corresponds to variant rs17098707 [ dbSNP | Ensembl ].
VAR_040517
Natural variant1191A → V. Ref.16
Corresponds to variant rs55980792 [ dbSNP | Ensembl ].
VAR_040518
Natural variant1221G → S. Ref.16
Corresponds to variant rs55902633 [ dbSNP | Ensembl ].
VAR_040519
Natural variant1291T → M. Ref.16
Corresponds to variant rs34679178 [ dbSNP | Ensembl ].
VAR_040520
Natural variant1411L → I. Ref.16
Corresponds to variant rs56254855 [ dbSNP | Ensembl ].
VAR_040521
Natural variant1631D → E in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.16
VAR_040522
Natural variant1721Q → H.
Corresponds to variant rs45630572 [ dbSNP | Ensembl ].
VAR_059766
Natural variant3041R → H. Ref.16
Corresponds to variant rs2230349 [ dbSNP | Ensembl ].
VAR_040523

Experimental info

Mutagenesis2151K → R: Failed to phosphorylate p53/TP53. Ref.13
Mutagenesis3881R → A: Nuclear exclusion; when associated with A-389; A-391; A-393 and A-394. Ref.9
Mutagenesis3891K → A: Nuclear exclusion; when associated with A-388; A-391; A-393 and A-394. Ref.9
Mutagenesis3911K → A: Nuclear exclusion; when associated with A-388; A-389; A-393 and A-394. Ref.9
Mutagenesis3931K → A: Nuclear exclusion; when associated with A-388; A-389; A-391 and A-394. Ref.9
Mutagenesis3941R → A: Nuclear exclusion; when associated with A-388; A-389; A-391 and A-393. Ref.9
Mutagenesis4841S → A: 15-20 fold defects in kinase activity; when associated with A-485. Ref.6
Mutagenesis4851T → A: 15-20 fold defects in kinase activity; when associated with A-484. Ref.6
Mutagenesis5501L → A: No detectable plasma membrane localization; when associated with A-551; A-554; and A-555. Ref.8
Mutagenesis5511L → A: No detectable plasma membrane localization; when associated with A-550; A-554; and A-555. Ref.8
Mutagenesis5541L → A: No detectable plasma membrane localization; when associated with A-550; A-551; and A-555. Ref.8
Mutagenesis5551F → A: No detectable plasma membrane localization; when associated with A-550; A-551; and A-554. Ref.8

Sequences

Sequence LengthMass (Da)Tools
P34947 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: D363567ECFF5CF21

FASTA59067,787
        10         20         30         40         50         60 
MELENIVANT VLLKAREGGG GKRKGKSKKW KEILKFPHIS QCEDLRRTID RDYCSLCDKQ 

        70         80         90        100        110        120 
PIGRLLFRQF CETRPGLECY IQFLDSVAEY EVTPDEKLGE KGKEIMTKYL TPKSPVFIAQ 

       130        140        150        160        170        180 
VGQDLVSQTE EKLLQKPCKE LFSACAQSVH EYLRGEPFHE YLDSMFFDRF LQWKWLERQP 

       190        200        210        220        230        240 
VTKNTFRQYR VLGKGGFGEV CACQVRATGK MYACKRLEKK RIKKRKGESM ALNEKQILEK 

       250        260        270        280        290        300 
VNSQFVVNLA YAYETKDALC LVLTIMNGGD LKFHIYNMGN PGFEEERALF YAAEILCGLE 

       310        320        330        340        350        360 
DLHRENTVYR DLKPENILLD DYGHIRISDL GLAVKIPEGD LIRGRVGTVG YMAPEVLNNQ 

       370        380        390        400        410        420 
RYGLSPDYWG LGCLIYEMIE GQSPFRGRKE KVKREEVDRR VLETEEVYSH KFSEEAKSIC 

       430        440        450        460        470        480 
KMLLTKDAKQ RLGCQEEGAA EVKRHPFFRN MNFKRLEAGM LDPPFVPDPR AVYCKDVLDI 

       490        500        510        520        530        540 
EQFSTVKGVN LDHTDDDFYS KFSTGSVSIP WQNEMIETEC FKELNVFGPN GTLPPDLNRN 

       550        560        570        580        590 
HPPEPPKKGL LQRLFKRQHQ NNSKSSPSSK TSFNHHINSN HVSSNSTGSS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of GRK5: a member of the G protein-coupled receptor kinase family."
Kunapuli P., Benovic J.L.
Proc. Natl. Acad. Sci. U.S.A. 90:5588-5592(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
[5]"Altered expression of beta-adrenergic receptor kinase and beta 1-adrenergic receptors in the failing human heart."
Ungerer M., Bohm M., Elce J.S., Erdmann E., Lohse M.J.
Circulation 87:454-463(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[6]"Phospholipid-stimulated autophosphorylation activates the G protein-coupled receptor kinase GRK5."
Kunapuli P., Gurevich V.V., Benovic J.L.
J. Biol. Chem. 269:10209-10212(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: AUTOPHOSPHORYLATION, MUTAGENESIS OF SER-484 AND THR-485.
[7]"Regulation of G protein-coupled receptor kinases by calmodulin and localization of the calmodulin binding domain."
Pronin A.N., Satpaev D.K., Slepak V.Z., Benovic J.L.
J. Biol. Chem. 272:18273-18280(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[8]"A predicted amphipathic helix mediates plasma membrane localization of GRK5."
Thiyagarajan M.M., Stracquatanio R.P., Pronin A.N., Evanko D.S., Benovic J.L., Wedegaertner P.B.
J. Biol. Chem. 279:17989-17995(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-550; LEU-551; LEU-554 AND PHE-555.
[9]"G protein-coupled receptor kinase 5 contains a DNA-binding nuclear localization sequence."
Johnson L.R., Scott M.G., Pitcher J.A.
Mol. Cell. Biol. 24:10169-10179(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF ARG-388; LYS-389; LYS-391; LYS-393 AND ARG-394.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484 AND THR-485, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Beta-arrestin1 phosphorylation by GRK5 regulates G protein-independent 5-HT4 receptor signalling."
Barthet G., Carrat G., Cassier E., Barker B., Gaven F., Pillot M., Framery B., Pellissier L.P., Augier J., Kang D.S., Claeysen S., Reiter E., Baneres J.L., Benovic J.L., Marin P., Bockaert J., Dumuis A.
EMBO J. 28:2706-2718(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF ARRB1, INTERACTION WITH HTR4.
[12]"G Protein-coupled receptor kinases phosphorylate LRP6 in the Wnt pathway."
Chen M., Philipp M., Wang J., Premont R.T., Garrison T.R., Caron M.G., Lefkowitz R.J., Chen W.
J. Biol. Chem. 284:35040-35048(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF LRP6.
[13]"G-protein-coupled receptor kinase 5 phosphorylates p53 and inhibits DNA damage-induced apoptosis."
Chen X., Zhu H., Yuan M., Fu J., Zhou Y., Ma L.
J. Biol. Chem. 285:12823-12830(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF TP53, INTERACTION WITH TP53, MUTAGENESIS OF LYS-215.
[14]"Role for the regulator of G-protein signaling homology domain of G protein-coupled receptor kinases 5 and 6 in beta 2-adrenergic receptor and rhodopsin phosphorylation."
Baameur F., Morgan D.H., Yao H., Tran T.M., Hammitt R.A., Sabui S., McMurray J.S., Lichtarge O., Clark R.B.
Mol. Pharmacol. 77:405-415(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF ADRB2, AUTOPHOSPHORYLATION.
[15]"G protein-coupled receptor kinase 5 phosphorylation of Hip regulates internalization of the chemokine receptor CXCR4."
Barker B.L., Benovic J.L.
Biochemistry 50:6933-6941(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF ST13, INTERACTION WITH ST13.
[16]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , 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 D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-41; VAL-119; SER-122; MET-129; ILE-141; GLU-163 AND HIS-304.
[17]"A GRK5 polymorphism that inhibits beta-adrenergic receptor signaling is protective in heart failure."
Liggett S.B., Cresci S., Kelly R.J., Syed F.M., Matkovich S.J., Hahn H.S., Diwan A., Martini J.S., Sparks L., Parekh R.R., Spertus J.A., Koch W.J., Kardia S.L., Dorn G.W. II
Nat. Med. 14:510-517(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LEU-41, CHARACTERIZATION OF VARIANT LEU-41, POLYMORPHISM, POSSIBLE PROTECTIVE ROLE IN THE PROGRESSION OF HEART FAILURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L15388 mRNA. Translation: AAA58620.1.
AL355273, AL355861, AL583824 Genomic DNA. Translation: CAI16487.1.
AL355861, AL355273, AL583824 Genomic DNA. Translation: CAI15804.1.
AL583824, AL355273, AL355861 Genomic DNA. Translation: CAI16759.1.
CH471066 Genomic DNA. Translation: EAW49394.1.
CH471066 Genomic DNA. Translation: EAW49395.1.
BC064506 mRNA. Translation: AAH64506.1.
PIRA48277.
B48682.
RefSeqNP_005299.1. NM_005308.2.
UniGeneHs.524625.
Hs.736460.

3D structure databases

ProteinModelPortalP34947.
SMRP34947. Positions 2-555.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109127. 171 interactions.
IntActP34947. 2 interactions.
MINTMINT-3013589.
STRING9606.ENSP00000376609.

Chemistry

BindingDBP34947.
ChEMBLCHEMBL5678.
GuidetoPHARMACOLOGY1469.

PTM databases

PhosphoSiteP34947.

Polymorphism databases

DMDM462203.

Proteomic databases

PaxDbP34947.
PRIDEP34947.

Protocols and materials databases

DNASU2869.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000392870; ENSP00000376609; ENSG00000198873.
GeneID2869.
KEGGhsa:2869.
UCSCuc001led.3. human.

Organism-specific databases

CTD2869.
GeneCardsGC10P120957.
HGNCHGNC:4544. GRK5.
HPACAB025579.
MIM600870. gene.
neXtProtNX_P34947.
PharmGKBPA180.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000006742.
HOVERGENHBG004532.
InParanoidP34947.
KOK08291.
OMAEMMETEC.
OrthoDBEOG7V1FQK.
PhylomeDBP34947.
TreeFamTF313940.

Enzyme and pathway databases

BRENDA2.7.11.16. 2681.
ReactomeREACT_111102. Signal Transduction.
SignaLinkP34947.

Gene expression databases

ArrayExpressP34947.
BgeeP34947.
CleanExHS_GRK5.
GenevestigatorP34947.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR000239. GPCR_kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view]
PRINTSPR00717. GPCRKINASE.
SMARTSM00315. RGS. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF48097. SSF48097. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGRK5. human.
GeneWikiGRK5.
GenomeRNAi2869.
NextBio11319.
PROP34947.
SOURCESearch...

Entry information

Entry nameGRK5_HUMAN
AccessionPrimary (citable) accession number: P34947
Secondary accession number(s): D3DRD0, Q5T059
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 16, 2014
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM