GRK6_HUMAN - dbPTM
GRK6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GRK6_HUMAN
UniProt AC P43250
Protein Name G protein-coupled receptor kinase 6
Gene Name GRK6
Organism Homo sapiens (Human).
Sequence Length 576
Subcellular Localization Membrane
Lipid-anchor.
Protein Description 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)..
Protein Sequence MELENIVANTVLLKAREGGGGNRKGKSKKWRQMLQFPHISQCEELRLSLERDYHSLCERQPIGRLLFREFCATRPELSRCVAFLDGVAEYEVTPDDKRKACGRQLTQNFLSHTGPDLIPEVPRQLVTNCTQRLEQGPCKDLFQELTRLTHEYLSVAPFADYLDSIYFNRFLQWKWLERQPVTKNTFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGGDLKFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYSERFSPQARSLCSQLLCKDPAERLGCRGGSAREVKEHPLFKKLNFKRLGAGMLEPPFKPDPQAIYCKDVLDIEQFSTVKGVELEPTDQDFYQKFATGSVPIPWQNEMVETECFQELNVFGLDGSVPPDLDWKGQPPAPPKKGLLQRLFSRQDCCGNCSDSEEELPTRL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
10 (in isoform 2)Phosphorylation-11.6424719451
10PhosphorylationLENIVANTVLLKARE
HHHHHHCEEEEHHHC		11.6424719451
14UbiquitinationVANTVLLKAREGGGG
HHCEEEEHHHCCCCC		41.03-
53PhosphorylationRLSLERDYHSLCERQ
HHHHHCCHHHHHHCC		10.2629496907
106PhosphorylationKACGRQLTQNFLSHT
HHHHHHHHHHHHHHH		17.0928122231
111PhosphorylationQLTQNFLSHTGPDLI
HHHHHHHHHHCCCCC		18.1828122231
113PhosphorylationTQNFLSHTGPDLIPE
HHHHHHHHCCCCCCC		47.2128122231
139 (in isoform 2)Ubiquitination-61.68-
139UbiquitinationRLEQGPCKDLFQELT
HHHHCCCHHHHHHHH		61.68-
152PhosphorylationLTRLTHEYLSVAPFA
HHHHHHHHHCHHHHH		9.1818083107
161PhosphorylationSVAPFADYLDSIYFN
CHHHHHHHHHHHHHH		14.6918083107
166PhosphorylationADYLDSIYFNRFLQW
HHHHHHHHHHHHHCC		9.9618083107
183UbiquitinationLERQPVTKNTFRQYR
HHCCCCCCCCCHHEE		54.98-
194UbiquitinationRQYRVLGKGGFGEVC
HHEEECCCCCCCCCC		52.26-
210UbiquitinationCQVRATGKMYACKKL
EEEEECCCEEECHHH		25.12-
226UbiquitinationKKRIKKRKGEAMALN
HHHHHHHHHHHHHCC		70.72-
235AcetylationEAMALNEKQILEKVN
HHHHCCHHHHHHHHH		41.3818602981
235UbiquitinationEAMALNEKQILEKVN
HHHHCCHHHHHHHHH		41.38-
240 (in isoform 2)Ubiquitination-43.1821890473
240 (in isoform 1)Ubiquitination-43.1821890473
240AcetylationNEKQILEKVNSRFVV
CHHHHHHHHHHHHHH		43.1818602993
240UbiquitinationNEKQILEKVNSRFVV
CHHHHHHHHHHHHHH		43.1821890473
255PhosphorylationSLAYAYETKDALCLV
HHHHHHHCHHHHHHH		22.88-
313 (in isoform 2)Ubiquitination-55.35-
313UbiquitinationRIVYRDLKPENILLD
HEEECCCCHHHEEEC		55.35-
343UbiquitinationVPEGQTIKGRVGTVG
CCCCCEECCCEECCC		44.0121906983
343 (in isoform 2)Ubiquitination-44.0121890473
343 (in isoform 1)Ubiquitination-44.0121890473
348PhosphorylationTIKGRVGTVGYMAPE
EECCCEECCCCCCCH		14.1128509920
351PhosphorylationGRVGTVGYMAPEVVK
CCEECCCCCCCHHHC		5.9328509920
358 (in isoform 2)Ubiquitination-59.26-
358UbiquitinationYMAPEVVKNERYTFS
CCCCHHHCCCCCCCC		59.26-
402 (in isoform 1)Ubiquitination-58.5521890473
402UbiquitinationEEVERLVKEVPEEYS
HHHHHHHHHCCHHHH		58.5521906983
402 (in isoform 2)Ubiquitination-58.5521890473
408PhosphorylationVKEVPEEYSERFSPQ
HHHCCHHHHHHCCHH		17.7326657352
426UbiquitinationLCSQLLCKDPAERLG
HHHHHHCCCHHHHHC		67.71-
426 (in isoform 2)Ubiquitination-67.71-
443UbiquitinationGGSAREVKEHPLFKK
CCCHHHHHHCCHHHH		45.62-
443 (in isoform 2)Ubiquitination-45.62-
466UbiquitinationGMLEPPFKPDPQAIY
CCCCCCCCCCCCCEE		55.04-
473 (in isoform 2)Phosphorylation-9.1027642862
484 (in isoform 3)Phosphorylation-31.80-
484PhosphorylationVLDIEQFSTVKGVEL
CCCHHHHCCCCCCEE		31.8029255136
484 (in isoform 2)Phosphorylation-31.8024719451
485PhosphorylationLDIEQFSTVKGVELE
CCHHHHCCCCCCEEC		27.7629255136
485 (in isoform 2)Phosphorylation-27.7621406692
485 (in isoform 3)Phosphorylation-27.76-
487 (in isoform 1)Ubiquitination-58.2821890473
487 (in isoform 2)Ubiquitination-58.2821890473
487UbiquitinationIEQFSTVKGVELEPT
HHHHCCCCCCEECCC		58.282190698
494PhosphorylationKGVELEPTDQDFYQK
CCCEECCCCHHHHHH		36.6028060719
557PhosphorylationGLLQRLFSRQDCCGN
CHHHHHHCCCCCCCC		33.36-
561S-palmitoylationRLFSRQDCCGNCSDS
HHHCCCCCCCCCCCC		2.127961702
562S-palmitoylationLFSRQDCCGNCSDSE
HHCCCCCCCCCCCCH		6.207961702
565S-palmitoylationRQDCCGNCSDSEEEL
CCCCCCCCCCCHHHC		2.657961702
566PhosphorylationQDCCGNCSDSEEELP
CCCCCCCCCCHHHCC		48.4428450419
568PhosphorylationCCGNCSDSEEELPTR
CCCCCCCCHHHCCCC		30.5228450419
572 (in isoform 2)Phosphorylation-6.2525159151
573 (in isoform 2)Phosphorylation-20.8225159151
574PhosphorylationDSEEELPTRL-----
CCHHHCCCCC-----		58.1730177828
577 (in isoform 2)Phosphorylation-25262027
578 (in isoform 2)Phosphorylation-25262027
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
484SPhosphorylationKinaseGRK6P43250
PSP
485TPhosphorylationKinaseGRK6P43250
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
561CPalmitoylation

7961702
562CPalmitoylation

7961702
565CPalmitoylation

7961702
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of GRK6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FSHR_HUMANFSHRphysical
10379886
SYUA_HUMANSNCAphysical
10852916
SYUB_HUMANSNCBphysical
10852916
SYUG_HUMANSNCGphysical
10852916
ADRB2_HUMANADRB2physical
9819198
HS90A_HUMANHSP90AA1physical
19996089
HS90B_HUMANHSP90AB1physical
19996089
CSEN_HUMANKCNIP3physical
17102134
DDB1_HUMANDDB1physical
22952844
ITA5_HUMANITGA5physical
21988832
TA2R_HUMANTBXA2Rphysical
11504827
GRK5_HUMANGRK5physical
28514442
NOLC1_HUMANNOLC1physical
28514442
NUCG_HUMANENDOGphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GRK6_HUMAN

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Related Literatures of Post-Translational Modification

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