P34947 (GRK5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	590 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Apoptosis Wnt signaling pathway
Cellular component	Cell membrane Cytoplasm Membrane Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Lipid-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor 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_component	cytoplasm 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_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW G-protein coupled receptor kinase activity Inferred from electronic annotation. Source: 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 590	590	G protein-coupled receptor kinase 5		PRO_0000085971
Regions
	Domain	53 – 171	119	RGS
	Domain	186 – 448	263	Protein kinase
	Domain	449 – 514	66	AGC-kinase C-terminal
	Nucleotide binding	192 – 200	9	ATP By similarity
	Region	1 – 185	185	N-terminal
	Region	20 – 39	20	Interaction with calmodulin
	Region	546 – 565	20	Sufficient for membrane localization
	Motif	388 – 395	8	Nuclear localization signal Ref.9
Sites
	Active site	311	1	Proton acceptor By similarity
	Binding site	215	1	ATP By similarity
Amino acid modifications
	Modified residue	484	1	Phosphoserine; by autocatalysis Ref.10
	Modified residue	485	1	Phosphothreonine; by autocatalysis Ref.10
Natural variations
	Natural variant	41	1	Q → L Exerts a protective effect in heart failure and ischemia. Ref.16 Ref.17 Corresponds to variant rs17098707 [ dbSNP | Ensembl ].		VAR_040517
	Natural variant	119	1	A → V. Ref.16 Corresponds to variant rs55980792 [ dbSNP | Ensembl ].		VAR_040518
	Natural variant	122	1	G → S. Ref.16 Corresponds to variant rs55902633 [ dbSNP | Ensembl ].		VAR_040519
	Natural variant	129	1	T → M. Ref.16 Corresponds to variant rs34679178 [ dbSNP | Ensembl ].		VAR_040520
	Natural variant	141	1	L → I. Ref.16 Corresponds to variant rs56254855 [ dbSNP | Ensembl ].		VAR_040521
	Natural variant	163	1	D → E in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.16		VAR_040522
	Natural variant	172	1	Q → H. Corresponds to variant rs45630572 [ dbSNP | Ensembl ].		VAR_059766
	Natural variant	304	1	R → H. Ref.16 Corresponds to variant rs2230349 [ dbSNP | Ensembl ].		VAR_040523
Experimental info
	Mutagenesis	215	1	K → R: Failed to phosphorylate p53/TP53. Ref.13
	Mutagenesis	388	1	R → A: Nuclear exclusion; when associated with A-389; A-391; A-393 and A-394. Ref.9
	Mutagenesis	389	1	K → A: Nuclear exclusion; when associated with A-388; A-391; A-393 and A-394. Ref.9
	Mutagenesis	391	1	K → A: Nuclear exclusion; when associated with A-388; A-389; A-393 and A-394. Ref.9
	Mutagenesis	393	1	K → A: Nuclear exclusion; when associated with A-388; A-389; A-391 and A-394. Ref.9
	Mutagenesis	394	1	R → A: Nuclear exclusion; when associated with A-388; A-389; A-391 and A-393. Ref.9
	Mutagenesis	484	1	S → A: 15-20 fold defects in kinase activity; when associated with A-485. Ref.6
	Mutagenesis	485	1	T → A: 15-20 fold defects in kinase activity; when associated with A-484. Ref.6
	Mutagenesis	550	1	L → A: No detectable plasma membrane localization; when associated with A-551; A-554; and A-555. Ref.8
	Mutagenesis	551	1	L → A: No detectable plasma membrane localization; when associated with A-550; A-554; and A-555. Ref.8
	Mutagenesis	554	1	L → A: No detectable plasma membrane localization; when associated with A-550; A-551; and A-555. Ref.8
	Mutagenesis	555	1	F → A: No detectable plasma membrane localization; when associated with A-550; A-551; and A-554. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	P34947 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: D363567ECFF5CF21	FASTA	590	67,787
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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. , 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.
IPI	IPI00414058.
PIR	A48277. B48682.
RefSeq	NP_005299.1. NM_005308.2.
UniGene	Hs.524625. Hs.736460.
3D structure databases
ProteinModelPortal	P34947.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-3013589.
STRING	9606.ENSP00000376609.
PTM databases
PhosphoSite	P34947.
Polymorphism databases
DMDM	462203.
Proteomic databases
PaxDb	P34947.
PRIDE	P34947.
Protocols and materials databases
DNASU	2869.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000392870; ENSP00000376609; ENSG00000198873.
GeneID	2869.
KEGG	hsa:2869.
UCSC	uc001led.3. human.
Organism-specific databases
CTD	2869.
GeneCards	GC10P120957.
HGNC	HGNC:4544. GRK5.
HPA	CAB025579.
MIM	600870. gene.
neXtProt	NX_P34947.
PharmGKB	PA180.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000006742.
HOVERGEN	HBG004532.
InParanoid	P34947.
KO	K08291.
OMA	EMMETEC.
OrthoDB	EOG4HHP24.
Enzyme and pathway databases
BRENDA	2.7.11.16. 2681.
Pathway_Interaction_DB	alphasynuclein_pathway. Alpha-synuclein signaling.
Reactome	REACT_111102. Signal Transduction.
SignaLink	P34947.
Gene expression databases
ArrayExpress	P34947.
Bgee	P34947.
CleanEx	HS_GRK5.
Genevestigator	P34947.
GermOnline	ENSG00000198873. Homo sapiens.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR000239. GPCR_kinase. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR000342. Regulat_G_prot_signal. IPR016137. Regulat_G_prot_signal_superfam. IPR002290. Ser/Thr_dual-sp_kinase_dom. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. PF00615. RGS. 1 hit. [Graphical view]
PRINTS	PR00717. GPCRKINASE.
SMART	SM00315. RGS. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit. SSF48097. Regulat_G_prot_signal_superfam. 1 hit.
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. False negative. PS50132. RGS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P34947.
ChEMBL	CHEMBL5678.
ChiTaRS	GRK5. human.
GenomeRNAi	2869.
NextBio	11319.
SOURCE	Search...

Entry information

Entry name

GRK5_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 132 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.