GRK5

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
4TNB, 4TND

Identifiers

Aliases

GRK5, GPRK5, G protein-coupled receptor kinase 5

External IDs

MGI: 109161 HomoloGene: 3879 GeneCards: GRK5

Genetically Related Diseases

type 2 diabetes mellitus^[1]

Gene ontology
Molecular function	• transferase activity • nucleotide binding • protein kinase activity • G-protein coupled receptor kinase activity • kinase activity • protein serine/threonine kinase activity • protein binding • phospholipid binding • ATP binding • protein kinase C binding • lipid binding • beta-adrenergic receptor kinase activity
Cellular component	• cytoplasm • nuclear membrane • membrane • focal adhesion • nucleus • plasma membrane
Biological process	• regulation of G-protein coupled receptor protein signaling pathway • phosphorylation • adenylate cyclase-modulating G-protein coupled receptor signaling pathway • negative regulation of apoptotic process • Wnt signaling pathway • tachykinin receptor signaling pathway • regulation of cell cycle • protein phosphorylation • positive regulation of cell proliferation • protein autophosphorylation • desensitization of G-protein coupled receptor protein signaling pathway • fat cell differentiation • response to drug • signal transduction • apoptotic process
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


2869


14773

Ensembl


ENSG00000198873


ENSMUSG00000003228

UniProt


P34947


Q8VEB1

RefSeq (mRNA)


NM_005308


NM_018869

RefSeq (protein)


NP_005299.1


NP_061357.3

Location (UCSC)

Chr 10: 119.21 – 119.46 Mb

Chr 19: 60.89 – 61.09 Mb

PubMed search

^[2]

^[3]

Wikidata

View/Edit Human

View/Edit Mouse

G protein-coupled receptor kinase 5 is an enzyme that in humans is encoded by the GRK5 gene.^[4]^[5]

Function

This gene encodes a member of the guanine nucleotide-binding protein (G protein)-coupled receptor kinase subfamily of the Ser/Thr protein kinase family. The protein phosphorylates the activated forms of G protein-coupled receptors thus initiating their deactivation. It has also been shown to play a role in regulating the motility of polymorphonuclear leukocytes (PMNs).^[5]

References

↑ "Diseases that are genetically associated with GRK5 view/edit references on wikidata".
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Kunapuli P, Benovic JL (Jun 1993). "Cloning and expression of GRK5: a member of the G protein-coupled receptor kinase family". Proceedings of the National Academy of Sciences of the United States of America. 90 (12): 5588–92. doi:10.1073/pnas.90.12.5588. PMC 46766. PMID 7685906.
1 2 "Entrez Gene: GRK5 G protein-coupled receptor kinase 5".

Komolov KE, Bhardwaj A, Benovic JL (Aug 2015). "Atomic Structure of GRK5 Reveals Distinct Structural Features Novel for G Protein-coupled Receptor Kinases". The Journal of Biological Chemistry. 290 (34): 20629–47. doi:10.1074/jbc.M115.647297. PMID 26032409.
Bullrich F, Druck T, Kunapuli P, Gomez J, Gripp KW, Schlegelberger B, Lasota J, Aronson M, Cannizzaro LA, Huebner K (1995). "Chromosomal mapping of the genes GPRK5 and GPRK6 encoding G protein-coupled receptor kinases GRK5 and GRK6". Cytogenetics and Cell Genetics. 70 (3-4): 250–4. doi:10.1159/000134045. PMID 7789183.
Kunapuli P, Gurevich VV, Benovic JL (Apr 1994). "Phospholipid-stimulated autophosphorylation activates the G protein-coupled receptor kinase GRK5". The Journal of Biological Chemistry. 269 (14): 10209–12. PMID 8144599.
Kunapuli P, Onorato JJ, Hosey MM, Benovic JL (Jan 1994). "Expression, purification, and characterization of the G protein-coupled receptor kinase GRK5". The Journal of Biological Chemistry. 269 (2): 1099–105. PMID 8288567.
Nagayama Y, Tanaka K, Hara T, Namba H, Yamashita S, Taniyama K, Niwa M (Apr 1996). "Involvement of G protein-coupled receptor kinase 5 in homologous desensitization of the thyrotropin receptor". The Journal of Biological Chemistry. 271 (17): 10143–8. doi:10.1074/jbc.271.17.10143. PMID 8626574.
Oppermann M, Freedman NJ, Alexander RW, Lefkowitz RJ (May 1996). "Phosphorylation of the type 1A angiotensin II receptor by G protein-coupled receptor kinases and protein kinase C". The Journal of Biological Chemistry. 271 (22): 13266–72. doi:10.1074/jbc.271.22.13266. PMID 8662816.
Fredericks ZL, Pitcher JA, Lefkowitz RJ (Jun 1996). "Identification of the G protein-coupled receptor kinase phosphorylation sites in the human beta2-adrenergic receptor". The Journal of Biological Chemistry. 271 (23): 13796–803. doi:10.1074/jbc.271.23.13796. PMID 8662852.
Bonaldo MF, Lennon G, Soares MB (Sep 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Pronin AN, Carman CV, Benovic JL (Nov 1998). "Structure-function analysis of G protein-coupled receptor kinase-5. Role of the carboxyl terminus in kinase regulation". The Journal of Biological Chemistry. 273 (47): 31510–8. doi:10.1074/jbc.273.47.31510. PMID 9813065.
Premont RT, Claing A, Vitale N, Freeman JL, Pitcher JA, Patton WA, Moss J, Vaughan M, Lefkowitz RJ (Nov 1998). "beta2-Adrenergic receptor regulation by GIT1, a G protein-coupled receptor kinase-associated ADP ribosylation factor GTPase-activating protein". Proceedings of the National Academy of Sciences of the United States of America. 95 (24): 14082–7. doi:10.1073/pnas.95.24.14082. PMC 24330. PMID 9826657.
Carman CV, Lisanti MP, Benovic JL (Mar 1999). "Regulation of G protein-coupled receptor kinases by caveolin". The Journal of Biological Chemistry. 274 (13): 8858–64. doi:10.1074/jbc.274.13.8858. PMID 10085129.
Brenninkmeijer CB, Price SA, López Bernal A, Phaneuf S (Sep 1999). "Expression of G-protein-coupled receptor kinases in pregnant term and non-pregnant human myometrium". The Journal of Endocrinology. 162 (3): 401–8. doi:10.1677/joe.0.1620401. PMID 10467231.
Okochi M, Walter J, Koyama A, Nakajo S, Baba M, Iwatsubo T, Meijer L, Kahle PJ, Haass C (Jan 2000). "Constitutive phosphorylation of the Parkinson's disease associated alpha-synuclein". The Journal of Biological Chemistry. 275 (1): 390–7. doi:10.1074/jbc.275.1.390. PMID 10617630.
Pronin AN, Morris AJ, Surguchov A, Benovic JL (Aug 2000). "Synucleins are a novel class of substrates for G protein-coupled receptor kinases". The Journal of Biological Chemistry. 275 (34): 26515–22. doi:10.1074/jbc.M003542200. PMID 10852916.
Berrada K, Plesnicher CL, Luo X, Thibonnier M (Sep 2000). "Dynamic interaction of human vasopressin/oxytocin receptor subtypes with G protein-coupled receptor kinases and protein kinase C after agonist stimulation". The Journal of Biological Chemistry. 275 (35): 27229–37. doi:10.1074/jbc.M002288200. PMID 10858434.
Zhou H, Yan F, Tai HH (Sep 2001). "Phosphorylation and desensitization of the human thromboxane receptor-alpha by G protein-coupled receptor kinases". The Journal of Pharmacology and Experimental Therapeutics. 298 (3): 1243–51. PMID 11504827.
Blaukat A, Pizard A, Breit A, Wernstedt C, Alhenc-Gelas F, Muller-Esterl W, Dikic I (Nov 2001). "Determination of bradykinin B2 receptor in vivo phosphorylation sites and their role in receptor function". The Journal of Biological Chemistry. 276 (44): 40431–40. doi:10.1074/jbc.M107024200. PMID 11517230.
Hu LA, Chen W, Premont RT, Cong M, Lefkowitz RJ (Jan 2002). "G protein-coupled receptor kinase 5 regulates beta 1-adrenergic receptor association with PSD-95". The Journal of Biological Chemistry. 277 (2): 1607–13. doi:10.1074/jbc.M107297200. PMID 11700307.
Warabi K, Richardson MD, Barry WT, Yamaguchi K, Roush ED, Nishimura K, Kwatra MM (Jun 2002). "Human substance P receptor undergoes agonist-dependent phosphorylation by G protein-coupled receptor kinase 5 in vitro". FEBS Letters. 521 (1-3): 140–4. doi:10.1016/S0014-5793(02)02858-2. PMID 12067742.

Kinases: Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1 LATS2 MAST1 MAST2 STK38 STK38L CIT ROCK1 SGK SGK2 SGK3 Protein kinase B AKT1 AKT2 AKT3 Ataxia telangiectasia mutated Mammalian target of rapamycin EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1

Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3

Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α PRKAA1 PRKAA2 β PRKAB1 PRKAB2 γ PRKAG1 PRKAG2 PRKAG3

3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)	BCKDK BCKDHA BCKDHB

(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2 IDH3A IDH3B IDH3G

(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4

Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase Aurora A kinase Aurora B kinase

Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK STK10

Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-

IκB kinase (EC 2.7.11.10)	CHUK IKK2 TBK1 IKBKE IKBKG IKBKAP

cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A PRKACG PRKACB PRKACA PRKY

cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G PRKG1

Protein kinase C (EC 2.7.11.13)	Protein kinase C Protein kinase Cζ PKC alpha PRKCB1 PRKCD PRKCE PRKCH PRKCG PRKCI PRKCQ Protein kinase N1 PKN2 PKN3

Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase

Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase Beta adrenergic receptor kinase-2

G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4 GRK5 GRK6

Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2 CAMK1 CAMK2A CAMK2B CAMK2D CAMK2G CAMK4 MLCK CASK CHEK1 CHEK2 DAPK1 DAPK2 DAPK3 STK11 MAPKAPK2 MAPKAPK3 MAPKAPK5 MARK1 MARK2 MARK3 MARK4 MELK MKNK1 MKNK2 NUAK1 NUAK2 OBSCN PASK PHKG1 PHKG2 PIM1 PIM2 PKD1 PRKD2 PRKD3 PSKH1 SNF1LK2 KIAA0999 STK40 SNF1LK SNRK SPEG TSSK2 Kalirin TRIB1 TRIB2 TRIB3 TRIO Titin DCLK1

Myosin light-chain kinase (EC 2.7.11.18)	MYLK MYLK2 MYLK3 MYLK4

Phosphorylase kinase (EC 2.7.11.19)	PHKA1 PHKA2 PHKB PHKG1 PHKG2

Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K STK19

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Cyclin-dependent kinase (EC 2.7.11.22)	CDK1 CDK2 CDKL2 CDK3 CDK4 CDK5 CDKL5 CDK6 CDK7 CDK8 CDK9 CDK10 CDK12 CDC2L5 PCTK1 PCTK2 PCTK3 PFTK1 CDC2L1

(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5 RPS6KA4 P70S6 kinase P70-S6 Kinase 1 RPS6KB2 RPS6KA2 RPS6KA3 RPS6KA1 RPS6KC1

Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated MAPK1 MAPK3 MAPK4 MAPK6 MAPK7 MAPK12 MAPK15 C-Jun N-terminal MAPK8 MAPK9 MAPK10 P38 mitogen-activated protein MAPK11 MAPK13 MAPK14

MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases MAP3K1 MAP3K2 MAP3K3 MAP3K4 MAP3K5 MAP3K6 MAP3K7 MAP3K8 RAFs ARAF BRAF KSR1 KSR2 MLKs MAP3K12 MAP3K13 MAP3K9 MAP3K10 MAP3K11 MAP3K7 ZAK CDC7 MAP3K14

Tau-protein kinase (EC 2.7.11.26)	TPK1 TTK GSK-3

(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)	-

Tropomyosin kinase (EC 2.7.11.28)	-

Low-density-lipoprotein receptor kinase (EC 2.7.11.29)	-

Receptor protein serine/threonine kinase (EC 2.7.11.30)	Bone morphogenetic protein receptors BMPR1 BMPR1A BMPR1B BMPR2 ACVR1 ACVR1B ACVR1C ACVR2A ACVR2B ACVRL1 Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1 MAP2K2 MAP2K3 MAP2K4 MAP2K5 MAP2K6 MAP2K7

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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GRK5

Function

References

Further reading