P43250 (GRK6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
G protein-coupled receptor kinase 6
EC=2.7.11.16

Alternative name(s):
G protein-coupled receptor kinase GRK6

Gene names

Name:	GRK6
Synonyms:	GPRK6

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	576 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Specifically phosphorylates the activated forms of G protein-coupled receptors. Such receptor phosphorylation initiates beta-arrestin-mediated receptor desensitization, internalization, and signaling events leading to their desensitization. Seems to be involved in the desensitization of D2-like dopamine receptors in striatum and chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis By similarity. Phosphorylates rhodopsin (RHO) (in vitro) and a non G-protein-coupled receptor: LRP6 during Wnt signaling (in vitro). Ref.8 Ref.10
Catalytic activity	ATP + [G-protein-coupled receptor] = ADP + [G-protein-coupled receptor] phosphate.
Subcellular location	Membrane; Lipid-anchor.
Tissue specificity	Widely expressed. Ref.5
Post-translational modification	It is uncertain whether palmitoylation is on Cys-561 and/or Cys-562 and/or Cys-565. Ref.6
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	Wnt signaling pathway
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW regulation of G-protein coupled receptor protein signaling pathway Traceable author statement PubMed 8077221. Source: ProtInc termination of G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: InterPro
Cellular_component	membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW G-protein coupled receptor kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform GRK6A (identifier: P43250-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform GRK6B (identifier: P43250-2)

The sequence of this isoform differs from the canonical sequence as follows:
     560-576: DCCGNCSDSEEELPTRL → RIAVETAATARKSSPPASSPQPEAPTSSWR

Isoform GRK6C (identifier: P43250-3)

The sequence of this isoform differs from the canonical sequence as follows:
     560-560: D → R
     561-576: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 576

576

G protein-coupled receptor kinase 6

PRO_0000085974

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

Nucleotide binding

264 – 270

7

ATP

Nucleotide binding

315 – 318

4

ATP

Region

1 – 185

185

N-terminal

Sites

Active site

311

1

Proton acceptor By similarity

Binding site

215

1

ATP

Amino acid modifications

Modified residue

484

1

Phosphoserine Ref.7 Ref.9

Modified residue

485

1

Phosphothreonine Ref.7 Ref.9

Lipidation

561

1

S-palmitoyl cysteine Probable

Lipidation

562

1

S-palmitoyl cysteine Probable

Lipidation

565

1

S-palmitoyl cysteine Probable

Natural variations

Alternative sequence

560 – 576

17

DCCGN…LPTRL → RIAVETAATARKSSPPASSP QPEAPTSSWR in isoform GRK6B.

VSP_004938

Alternative sequence

560

1

D → R in isoform GRK6C.

VSP_041813

Alternative sequence

561 – 576

16

Missing in isoform GRK6C.

VSP_041814

Natural variant

31

1

R → Q in a gastric adenocarcinoma sample; somatic mutation. Ref.13

VAR_040524

Natural variant

73

1

T → M. Ref.13
Corresponds to variant rs56382815 [ dbSNP | Ensembl ].

VAR_040525

Natural variant

275

1

I → M in a breast infiltrating ductal carcinoma sample; somatic mutation. Ref.13

VAR_040526

Experimental info

Mutagenesis

6

1

I → A: 12-13 fold defects in kinase activity; 180-fold defects in kinase activity; when associated with A-7. Ref.12

Mutagenesis

7

1

V → A: 12-13 fold defects in kinase activity; 180-fold defects in kinase activity; when associated with A-6. Ref.12

Mutagenesis

9

1

N → A: 140-fold defects in kinase activity. Ref.12

Mutagenesis

12

1

L → A: 1100-fold defects in kinase activity. Ref.12

Mutagenesis

561

1

C → S: Abolishes palmitoylation; when associated with S-562 and S-565. Ref.6

Mutagenesis

562

1

C → S: Abolishes palmitoylation; when associated with S-561 and S-565. Ref.6

Mutagenesis

565

1

C → S: Abolishes palmitoylation; when associated with S-561 and S-562. Ref.6

Sequence conflict

60 – 61

2

QP → HA in AAA60175. Ref.1

Sequence conflict

104 – 105

2

QL → HV in AAA60175. Ref.1

Secondary structure

1

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576

Helix Strand Turn

Details...

Helix

3 – 18

16

Beta strand

23 – 25

3

Helix

30 – 33

4

Helix

40 – 42

3

Helix

43 – 48

6

Helix

53 – 57

5

Helix

61 – 71

11

Helix

75 – 91

17

Turn

95 – 97

3

Helix

98 – 109

12

Beta strand

112 – 114

3

Beta strand

117 – 120

4

Helix

123 – 135

13

Turn

139 – 142

4

Helix

143 – 153

11

Helix

156 – 162

7

Helix

165 – 177

13

Helix

183 – 185

3

Beta strand

186 – 195

10

Beta strand

198 – 205

8

Turn

206 – 208

3

Beta strand

211 – 218

8

Helix

219 – 224

6

Helix

228 – 240

13

Beta strand

249 – 254

6

Beta strand

256 – 263

8

Helix

271 – 276

6

Beta strand

277 – 280

4

Helix

285 – 304

20

Helix

314 – 316

3

Beta strand

317 – 319

3

Beta strand

325 – 327

3

Helix

349 – 351

3

Helix

354 – 357

4

Beta strand

361 – 364

4

Helix

365 – 380

16

Beta strand

384 – 386

3

Beta strand

388 – 390

3

Helix

394 – 403

10

Beta strand

410 – 412

3

Helix

414 – 423

10

Helix

428 – 430

3

Beta strand

435 – 437

3

Helix

438 – 443

6

Helix

446 – 448

3

Helix

453 – 457

5

Helix

477 – 479

3

Helix

493 – 502

10

Helix

508 – 517

10

Helix

520 – 525

6

Beta strand

527 – 530

4

Helix

549 – 555

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform GRK6A [UniParc]. Last modified January 23, 2002. Version 2. Checksum: 3BF8C3B1CDE2BD74	FASTA	576	65,991
	10 20 30 40 50 60 MELENIVANT VLLKAREGGG GNRKGKSKKW RQMLQFPHIS QCEELRLSLE RDYHSLCERQ 70 80 90 100 110 120 PIGRLLFREF CATRPELSRC VAFLDGVAEY EVTPDDKRKA CGRQLTQNFL SHTGPDLIPE 130 140 150 160 170 180 VPRQLVTNCT QRLEQGPCKD LFQELTRLTH EYLSVAPFAD YLDSIYFNRF LQWKWLERQP 190 200 210 220 230 240 VTKNTFRQYR VLGKGGFGEV CACQVRATGK MYACKKLEKK RIKKRKGEAM ALNEKQILEK 250 260 270 280 290 300 VNSRFVVSLA YAYETKDALC LVLTLMNGGD LKFHIYHMGQ AGFPEARAVF YAAEICCGLE 310 320 330 340 350 360 DLHRERIVYR DLKPENILLD DHGHIRISDL GLAVHVPEGQ TIKGRVGTVG YMAPEVVKNE 370 380 390 400 410 420 RYTFSPDWWA LGCLLYEMIA GQSPFQQRKK KIKREEVERL VKEVPEEYSE RFSPQARSLC 430 440 450 460 470 480 SQLLCKDPAE RLGCRGGSAR EVKEHPLFKK LNFKRLGAGM LEPPFKPDPQ AIYCKDVLDI 490 500 510 520 530 540 EQFSTVKGVE LEPTDQDFYQ KFATGSVPIP WQNEMVETEC FQELNVFGLD GSVPPDLDWK 550 560 570 GQPPAPPKKG LLQRLFSRQD CCGNCSDSEE ELPTRL
	Isoform GRK6B [UniParc]. Checksum: BD7C24E9624DDFEC	FASTA	589	67,257
	10 20 30 40 50 60 MELENIVANT VLLKAREGGG GNRKGKSKKW RQMLQFPHIS QCEELRLSLE RDYHSLCERQ 70 80 90 100 110 120 PIGRLLFREF CATRPELSRC VAFLDGVAEY EVTPDDKRKA CGRQLTQNFL SHTGPDLIPE 130 140 150 160 170 180 VPRQLVTNCT QRLEQGPCKD LFQELTRLTH EYLSVAPFAD YLDSIYFNRF LQWKWLERQP 190 200 210 220 230 240 VTKNTFRQYR VLGKGGFGEV CACQVRATGK MYACKKLEKK RIKKRKGEAM ALNEKQILEK 250 260 270 280 290 300 VNSRFVVSLA YAYETKDALC LVLTLMNGGD LKFHIYHMGQ AGFPEARAVF YAAEICCGLE 310 320 330 340 350 360 DLHRERIVYR DLKPENILLD DHGHIRISDL GLAVHVPEGQ TIKGRVGTVG YMAPEVVKNE 370 380 390 400 410 420 RYTFSPDWWA LGCLLYEMIA GQSPFQQRKK KIKREEVERL VKEVPEEYSE RFSPQARSLC 430 440 450 460 470 480 SQLLCKDPAE RLGCRGGSAR EVKEHPLFKK LNFKRLGAGM LEPPFKPDPQ AIYCKDVLDI 490 500 510 520 530 540 EQFSTVKGVE LEPTDQDFYQ KFATGSVPIP WQNEMVETEC FQELNVFGLD GSVPPDLDWK 550 560 570 580 GQPPAPPKKG LLQRLFSRQR IAVETAATAR KSSPPASSPQ PEAPTSSWR
	Isoform GRK6C [UniParc]. Checksum: 2686CECDFC7B3516	FASTA	560	64,294
	10 20 30 40 50 60 MELENIVANT VLLKAREGGG GNRKGKSKKW RQMLQFPHIS QCEELRLSLE RDYHSLCERQ 70 80 90 100 110 120 PIGRLLFREF CATRPELSRC VAFLDGVAEY EVTPDDKRKA CGRQLTQNFL SHTGPDLIPE 130 140 150 160 170 180 VPRQLVTNCT QRLEQGPCKD LFQELTRLTH EYLSVAPFAD YLDSIYFNRF LQWKWLERQP 190 200 210 220 230 240 VTKNTFRQYR VLGKGGFGEV CACQVRATGK MYACKKLEKK RIKKRKGEAM ALNEKQILEK 250 260 270 280 290 300 VNSRFVVSLA YAYETKDALC LVLTLMNGGD LKFHIYHMGQ AGFPEARAVF YAAEICCGLE 310 320 330 340 350 360 DLHRERIVYR DLKPENILLD DHGHIRISDL GLAVHVPEGQ TIKGRVGTVG YMAPEVVKNE 370 380 390 400 410 420 RYTFSPDWWA LGCLLYEMIA GQSPFQQRKK KIKREEVERL VKEVPEEYSE RFSPQARSLC 430 440 450 460 470 480 SQLLCKDPAE RLGCRGGSAR EVKEHPLFKK LNFKRLGAGM LEPPFKPDPQ AIYCKDVLDI 490 500 510 520 530 540 EQFSTVKGVE LEPTDQDFYQ KFATGSVPIP WQNEMVETEC FQELNVFGLD GSVPPDLDWK 550 560 GQPPAPPKKG LLQRLFSRQR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and expression of GRK6. A new member of the G protein-coupled receptor kinase family." Benovic J.L., Gomez J. J. Biol. Chem. 268:19521-19527(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GRK6A).
[2]	"The GRK4 subfamily of G protein-coupled receptor kinases. Alternative splicing, gene organization, and sequence conservation." Premont R.T., Macrae A.D., Aparicio S.A., Kendall H.E., Welch J.E., Lefkowitz R.J. J. Biol. Chem. 274:29381-29389(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS GRK6B AND GRK6C).
[3]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] 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] (ISOFORM GRK6A). Tissue: Uterus.
[5]	"Identification of additional members of human G-protein-coupled receptor kinase multigene family." Haribabu B., Snyderman R. Proc. Natl. Acad. Sci. U.S.A. 90:9398-9402(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-576, TISSUE SPECIFICITY.
[6]	"Palmitoylation of G protein-coupled receptor kinase, GRK6. Lipid modification diversity in the GRK family." Stoffel R.H., Randall R.R., Premont R.T., Lefkowitz R.J., Inglese J. J. Biol. Chem. 269:27791-27794(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PALMITOYLATION AT CYS-561; CYS-562 AND CYS-565, MUTAGENESIS OF CYS-561; CYS-562 AND CYS-565.
[7]	"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.
[8]	"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.
[9]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484 AND THR-485, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"Site-specific phosphorylation of CXCR4 is dynamically regulated by multiple kinases and results in differential modulation of CXCR4 signaling." Busillo J.M., Armando S., Sengupta R., Meucci O., Bouvier M., Benovic J.L. J. Biol. Chem. 285:7805-7817(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF CXCR4.
[11]	"The structure of G protein-coupled receptor kinase (GRK)-6 defines a second lineage of GRKs." Lodowski D.T., Tesmer V.M., Benovic J.L., Tesmer J.J. J. Biol. Chem. 281:16785-16793(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[12]	"Molecular basis for activation of G protein-coupled receptor kinases." Boguth C.A., Singh P., Huang C.C., Tesmer J.J. EMBO J. 29:3249-3259(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.72 ANGSTROMS) IN COMPLEX WITH AMP AND SANGIVAMYCIN, MUTAGENESIS OF ILE-6; VAL-7; ASN-9 AND LEU-12.
[13]	"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] GLN-31; MET-73 AND MET-275.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L16862 mRNA. Translation: AAA60175.1.
AF040751 mRNA. Translation: AAC09273.1.
AF040752 mRNA. Translation: AAC09274.1.
AC145098 Genomic DNA. No translation available.
BC009277 mRNA. Translation: AAH09277.1.
U00686 mRNA. Translation: AAA03565.1.

IPI

IPI00017330.
IPI00220242.
IPI00465441.

PIR

A48765.

RefSeq

NP_001004105.1. NM_001004105.2.
NP_001004106.1. NM_001004106.2.
NP_002073.2. NM_002082.3.

UniGene

Hs.235116.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ACX	X-ray	2.60	A/B	1-576	[»]
3NYN	X-ray	2.72	A/B	2-576	[»]
3NYO	X-ray	2.92	A/B	2-576	[»]

ProteinModelPortal

P43250.

ModBase

Search...

Protein-protein interaction databases

IntAct

P43250. 3 interactions.

MINT

MINT-1425525.

STRING

9606.ENSP00000377204.

PTM databases

PhosphoSite

P43250.

Polymorphism databases

DMDM

20141386.

Proteomic databases

PaxDb

P43250.

PRIDE

P43250.

Protocols and materials databases

DNASU

2870.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000355472; ENSP00000347655; ENSG00000198055.
ENST00000355958; ENSP00000348230; ENSG00000198055.
ENST00000528793; ENSP00000433511; ENSG00000198055.

GeneID

2870.

KEGG

hsa:2870.

UCSC

uc003mgq.2. human.
uc021yit.1. human.
uc021yiu.1. human.

Organism-specific databases

CTD

2870.

GeneCards

GC05P176853.

HGNC

HGNC:4545. GRK6.

HPA

HPA015327.
HPA018903.

MIM

600869. gene.

neXtProt

NX_P43250.

PharmGKB

PA28942.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000006742.

HOVERGEN

HBG004532.

KO

K08291.

OMA

PFKPDPQ.

OrthoDB

EOG4HHP24.

Enzyme and pathway databases

BRENDA

2.7.11.16. 2681.

Gene expression databases

ArrayExpress

P43250.

Bgee

P43250.

CleanEx

HS_GRK6.

Genevestigator

P43250.

GermOnline

ENSG00000198055. 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.
IPR008271. Ser/Thr_kinase_AS.
[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. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P43250.

ChEMBL

CHEMBL6144.

EvolutionaryTrace

P43250.

GenomeRNAi

2870.

NextBio

11323.

SOURCE

Search...

Entry information

Entry name

GRK6_HUMAN

Accession

Primary (citable) accession number: P43250
Secondary accession number(s): O60541, Q13652

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 23, 2002
Last modified:	May 1, 2013
This is version 139 of the entry and version 2 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.