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Protein Page:
GRK6 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
GRK6 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 dopamin receptors in striatum and chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis. Phosphorylates rhodopsin (RHO) (in vitro) and a non G-protein-coupled receptor: LRP6 during Wnt signaling (in vitro). Widely expressed. Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. GPRK subfamily. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 2.7.11.16; Protein kinase, Ser/Thr (non-receptor); Protein kinase, AGC; Kinase, protein; AGC group; GRK family; GRK subfamily
Cellular Component: membrane
Molecular Function: G-protein coupled receptor kinase activity; protein binding; ATP binding
Biological Process: Wnt receptor signaling pathway; protein amino acid phosphorylation; regulation of G-protein coupled receptor protein signaling pathway
Reference #:  P43250 (UniProtKB)
Alt. Names/Synonyms: FLJ32135; G protein-coupled receptor kinase 6; G protein-coupled receptor kinase GRK6; GPRK6; GRK6
Gene Symbols: GRK6
Molecular weight: 65,991 Da
Basal Isoelectric point: 8.32  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

GRK6

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 S78 CATRPELSRCVAFLD
0 1 V81 RPELSRCVAFLDGVA
0 3 T106-p KACGRQLtQNFLsHt
0 1 S111-p QLtQNFLsHtGPDLI
0 1 T113-p tQNFLsHtGPDLIPE
0 1 K139-ub RLEQGPCkDLFQELT
0 1 Y152-p LTRLTHEyLSVAPFA
0 1 Y161-p SVAPFADyLDSIyFN
0 1 Y166-p ADyLDSIyFNRFLQW
0 1 K235-ac EAMALNEkQILEkVN
0 1 K240-ac NEkQILEkVNSRFVV
0 6 K240-ub NEkQILEkVNSRFVV
0 1 K343-ub VPEGQTIkGRVGTVG
0 1 K358-ub YMAPEVVkNERYTFS
0 4 K402-ub EEVERLVkEVPEEYS
0 1 K426-ub LCSQLLCkDPAERLG
0 1 Y473 KPDPQAIYCKDVLDI
1 30 S484-p VLDIEQFstVkGVEL
1 21 T485-p LDIEQFstVkGVELE
0 2 K487-ub IEQFstVkGVELEPT
0 1 S557-p GLLQRLFsRQDCCGN
0 2 S566-p QDCCGNCsDsEEELP
0 2 S568-p CCGNCsDsEEELPTR
0 1 - gap
0 3 - gap
0 3 - gap
  GRK6 iso2  
S78 CATRPELSRCVAFLD
V81 RPELSRCVAFLDGVA
T106 KACGRQLTQNFLSHT
S111 QLTQNFLSHTGPDLI
T113 TQNFLSHTGPDLIPE
K139 RLEQGPCKDLFQELT
Y152 LTRLTHEYLSVAPFA
Y161 SVAPFADYLDSIYFN
Y166 ADYLDSIYFNRFLQW
K235 EAMALNEKQILEKVN
K240 NEKQILEKVNSRFVV
K240 NEKQILEKVNSRFVV
K343 VPEGQTIKGRVGTVG
K358 YMAPEVVKNERYTFS
K402 EEVERLVKEVPEEYS
K426 LCSQLLCKDPAERLG
Y473 KPDPQAIYCKDVLDI
S484 VLDIEQFSTVKGVEL
T485 LDIEQFSTVKGVELE
K487 IEQFSTVKGVELEPT
S557 GLLQRLFSRQRIAVE
- gap
- gap
S572 TAATARKSsPPASsP
S573-p AATARKSsPPASsPQ
S578-p KSsPPASsPQPEAPT
  mouse

► Hide Isoforms
 
T78 CATRPELTRCTAFLD
T81 RPELTRCTAFLDGVS
M106 KACGRRLMQNFLSHT
S111 RLMQNFLSHTGPDLI
T113 MQNFLSHTGPDLIPE
K139 RLEQGPCKDLFQELT
Y152 LTRLTHEYLSTAPFA
Y161 STAPFADYLDSIYFN
Y166 ADYLDSIYFNRFLQW
K235 EAMALNEKQILEKVN
K240 NEKQILEKVNSRFVV
K240 NEKQILEKVNSRFVV
K343 VPEGQTIKGRVGTVG
R358 YMAPEVVRNERYTFS
K402 EEVERLVKEVAEEYT
K426 LCSQLLSKDPAERLG
Y473-p KPDPQAIyCKDVLDI
S484-p VLDIEQFstVkGVDL
T485-p LDIEQFstVkGVDLE
K487-ub IEQFstVkGVDLEPT
S557 GLLQRLFSRQDCCGN
S566-p QDCCGNCsDsEEELP
S568-p CCGNCsDsEEELPTR
- gap
- gap
- gap
  GRK6 iso2  
T78 CATRPELTRCTAFLD
T81 RPELTRCTAFLDGVS
M106 KACGRRLMQNFLSHT
S111 RLMQNFLSHTGPDLI
T113 MQNFLSHTGPDLIPE
K139 RLEQGPCKDLFQELT
Y152 LTRLTHEYLSTAPFA
Y161 STAPFADYLDSIYFN
Y166 ADYLDSIYFNRFLQW
K235 EAMALNEKQILEKVN
K240 NEKQILEKVNSRFVV
K240 NEKQILEKVNSRFVV
K343 VPEGQTIKGRVGTVG
R358 YMAPEVVRNERYTFS
K402 EEVERLVKEVAEEYT
K426 LCSQLLSKDPAERLG
Y473 KPDPQAIYCKDVLDI
S484 VLDIEQFSTVKGVDL
T485 LDIEQFSTVKGVDLE
K487 IEQFSTVKGVDLEPT
S557 GLLQRLFSRQRIAVG
- gap
- gap
S572-p TAATVRKssPPASsP
S573-p AATVRKssPPASsPQ
S578-p KssPPASsPQAEAPT
  rat

 
T78-p CATRPELtRCtAFLD
T81-p RPELtRCtAFLDGVA
M106 KACGCRLMQNFLSHT
S111 RLMQNFLSHTGPDLI
T113 MQNFLSHTGPDLIPE
K139 RLEQGPCKDLFQELT
Y152 LTRLTHEYLSMAPFA
Y161 SMAPFADYLDSIYFN
Y166 ADYLDSIYFNRFLQW
K235 EAMALNEKQILEKVN
K240 NEKQILEKVNSRFVV
K240 NEKQILEKVNSRFVV
K343 VPEGQTIKGRVGTVG
K358 YMAPEVVKNERYTFS
K402 EEVERLVKEVAEEYT
K426 LCSQLPNKDPAERLG
Y473 KPDPQAIYCKDVLDI
S484-p VLDIEQFsTVKGVDL
T485 LDIEQFsTVKGVDLE
K487 IEQFsTVKGVDLEPT
S557 GLLQRLFSRQDCCGN
S566 QDCCGNCSDSEEELP
S568 CCGNCSDSEEELPTR
- gap
- gap
- gap
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