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P43250

- GRK6_HUMAN

UniProt

P43250 - GRK6_HUMAN

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Protein

G protein-coupled receptor kinase 6

Gene

GRK6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity2 Publications

Catalytic activityi

ATP + [G-protein-coupled receptor] = ADP + [G-protein-coupled receptor] phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei215 – 2151ATP
Active sitei311 – 3111Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi192 – 2009ATP
Nucleotide bindingi264 – 2707ATP
Nucleotide bindingi315 – 3184ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. G-protein coupled receptor kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. regulation of G-protein coupled receptor protein signaling pathway Source: ProtInc
  2. termination of G-protein coupled receptor signaling pathway Source: InterPro
  3. Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Wnt signaling pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.16. 2681.
SignaLinkiP43250.

Names & Taxonomyi

Protein namesi
Recommended name:
G protein-coupled receptor kinase 6 (EC:2.7.11.16)
Alternative name(s):
G protein-coupled receptor kinase GRK6
Gene namesi
Name:GRK6
Synonyms:GPRK6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:4545. GRK6.

Subcellular locationi

GO - Cellular componenti

  1. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi6 – 61I → A: 12-13 fold defects in kinase activity; 180-fold defects in kinase activity; when associated with A-7. 1 Publication
Mutagenesisi7 – 71V → A: 12-13 fold defects in kinase activity; 180-fold defects in kinase activity; when associated with A-6. 1 Publication
Mutagenesisi9 – 91N → A: 140-fold defects in kinase activity. 1 Publication
Mutagenesisi12 – 121L → A: 1100-fold defects in kinase activity. 1 Publication
Mutagenesisi561 – 5611C → S: Abolishes palmitoylation; when associated with S-562 and S-565. 1 Publication
Mutagenesisi562 – 5621C → S: Abolishes palmitoylation; when associated with S-561 and S-565. 1 Publication
Mutagenesisi565 – 5651C → S: Abolishes palmitoylation; when associated with S-561 and S-562. 1 Publication

Organism-specific databases

PharmGKBiPA28942.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 576576G protein-coupled receptor kinase 6PRO_0000085974Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei484 – 4841Phosphoserine2 Publications
Modified residuei485 – 4851Phosphothreonine2 Publications
Lipidationi561 – 5611S-palmitoyl cysteine1 Publication
Lipidationi562 – 5621S-palmitoyl cysteine1 Publication
Lipidationi565 – 5651S-palmitoyl cysteine1 Publication

Post-translational modificationi

It is uncertain whether palmitoylation is on Cys-561 and/or Cys-562 and/or Cys-565.1 Publication

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP43250.
PaxDbiP43250.
PRIDEiP43250.

PTM databases

PhosphoSiteiP43250.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiP43250.
CleanExiHS_GRK6.
ExpressionAtlasiP43250. baseline and differential.
GenevestigatoriP43250.

Organism-specific databases

HPAiHPA015327.
HPA018903.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ROM1P522059EBI-722747,EBI-8176947From a different organism.

Protein-protein interaction databases

BioGridi109128. 16 interactions.
IntActiP43250. 8 interactions.
MINTiMINT-1425525.
STRINGi9606.ENSP00000377204.

Structurei

Secondary structure

1
576
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1816
Beta strandi23 – 253
Helixi30 – 334
Helixi40 – 423
Helixi43 – 486
Helixi53 – 575
Helixi61 – 7111
Helixi75 – 9117
Turni95 – 973
Helixi98 – 10912
Beta strandi112 – 1143
Beta strandi117 – 1204
Helixi123 – 13513
Turni139 – 1424
Helixi143 – 15311
Helixi156 – 1627
Helixi165 – 17713
Helixi183 – 1853
Beta strandi186 – 19510
Beta strandi198 – 2058
Turni206 – 2083
Beta strandi211 – 2188
Helixi219 – 2246
Helixi228 – 24013
Beta strandi249 – 2546
Beta strandi256 – 2638
Helixi271 – 2766
Beta strandi277 – 2804
Helixi285 – 30420
Helixi314 – 3163
Beta strandi317 – 3193
Beta strandi325 – 3273
Helixi349 – 3513
Helixi354 – 3574
Beta strandi361 – 3644
Helixi365 – 38016
Beta strandi384 – 3863
Beta strandi388 – 3903
Helixi394 – 40310
Beta strandi410 – 4123
Helixi414 – 42310
Helixi428 – 4303
Beta strandi435 – 4373
Helixi438 – 4436
Helixi446 – 4483
Helixi453 – 4575
Helixi477 – 4793
Helixi493 – 50210
Helixi508 – 51710
Helixi520 – 5256
Beta strandi527 – 5304
Helixi549 – 5557

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ACXX-ray2.60A/B1-576[»]
3NYNX-ray2.72A/B2-576[»]
3NYOX-ray2.92A/B2-576[»]
ProteinModelPortaliP43250.
SMRiP43250. Positions 2-557.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43250.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 171119RGSPROSITE-ProRule annotationAdd
BLAST
Domaini186 – 448263Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini449 – 51466AGC-kinase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 185185N-terminalAdd
BLAST

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 RGS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118793.
HOGENOMiHOG000006742.
HOVERGENiHBG004532.
InParanoidiP43250.
KOiK08291.
OMAiMLEPPFK.
OrthoDBiEOG7V1FQK.
PhylomeDBiP43250.
TreeFamiTF313940.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR000239. GPCR_kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view]
PRINTSiPR00717. GPCRKINASE.
SMARTiSM00315. RGS. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF48097. SSF48097. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. 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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform GRK6A (identifier: P43250-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MELENIVANT VLLKAREGGG GNRKGKSKKW RQMLQFPHIS QCEELRLSLE
60 70 80 90 100
RDYHSLCERQ PIGRLLFREF CATRPELSRC VAFLDGVAEY EVTPDDKRKA
110 120 130 140 150
CGRQLTQNFL SHTGPDLIPE VPRQLVTNCT QRLEQGPCKD LFQELTRLTH
160 170 180 190 200
EYLSVAPFAD YLDSIYFNRF LQWKWLERQP VTKNTFRQYR VLGKGGFGEV
210 220 230 240 250
CACQVRATGK MYACKKLEKK RIKKRKGEAM ALNEKQILEK VNSRFVVSLA
260 270 280 290 300
YAYETKDALC LVLTLMNGGD LKFHIYHMGQ AGFPEARAVF YAAEICCGLE
310 320 330 340 350
DLHRERIVYR DLKPENILLD DHGHIRISDL GLAVHVPEGQ TIKGRVGTVG
360 370 380 390 400
YMAPEVVKNE RYTFSPDWWA LGCLLYEMIA GQSPFQQRKK KIKREEVERL
410 420 430 440 450
VKEVPEEYSE RFSPQARSLC SQLLCKDPAE RLGCRGGSAR EVKEHPLFKK
460 470 480 490 500
LNFKRLGAGM LEPPFKPDPQ AIYCKDVLDI EQFSTVKGVE LEPTDQDFYQ
510 520 530 540 550
KFATGSVPIP WQNEMVETEC FQELNVFGLD GSVPPDLDWK GQPPAPPKKG
560 570
LLQRLFSRQD CCGNCSDSEE ELPTRL
Length:576
Mass (Da):65,991
Last modified:January 23, 2002 - v2
Checksum:i3BF8C3B1CDE2BD74
GO
Isoform GRK6B (identifier: P43250-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:589
Mass (Da):67,257
Checksum:iBD7C24E9624DDFEC
GO
Isoform GRK6C (identifier: P43250-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:560
Mass (Da):64,294
Checksum:i2686CECDFC7B3516
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 612QP → HA in AAA60175. (PubMed:8366096)Curated
Sequence conflicti104 – 1052QL → HV in AAA60175. (PubMed:8366096)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti31 – 311R → Q in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
VAR_040524
Natural varianti73 – 731T → M.1 Publication
Corresponds to variant rs56382815 [ dbSNP | Ensembl ].
VAR_040525
Natural varianti275 – 2751I → M in a breast infiltrating ductal carcinoma sample; somatic mutation. 1 Publication
VAR_040526

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei560 – 57617DCCGN…LPTRL → RIAVETAATARKSSPPASSP QPEAPTSSWR in isoform GRK6B. 1 PublicationVSP_004938Add
BLAST
Alternative sequencei560 – 5601D → R in isoform GRK6C. 1 PublicationVSP_041813
Alternative sequencei561 – 57616Missing in isoform GRK6C. 1 PublicationVSP_041814Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS34303.1. [P43250-1]
CCDS43406.1. [P43250-3]
CCDS47348.1. [P43250-2]
PIRiA48765.
RefSeqiNP_001004105.1. NM_001004105.2. [P43250-3]
NP_001004106.1. NM_001004106.2. [P43250-1]
NP_002073.2. NM_002082.3. [P43250-2]
UniGeneiHs.235116.

Genome annotation databases

EnsembliENST00000355472; ENSP00000347655; ENSG00000198055. [P43250-1]
ENST00000355958; ENSP00000348230; ENSG00000198055. [P43250-3]
ENST00000528793; ENSP00000433511; ENSG00000198055. [P43250-2]
GeneIDi2870.
KEGGihsa:2870.
UCSCiuc003mgq.2. human. [P43250-3]
uc021yit.1. human. [P43250-1]
uc021yiu.1. human. [P43250-2]

Polymorphism databases

DMDMi20141386.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS34303.1. [P43250-1 ]
CCDS43406.1. [P43250-3 ]
CCDS47348.1. [P43250-2 ]
PIRi A48765.
RefSeqi NP_001004105.1. NM_001004105.2. [P43250-3 ]
NP_001004106.1. NM_001004106.2. [P43250-1 ]
NP_002073.2. NM_002082.3. [P43250-2 ]
UniGenei Hs.235116.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P43250.
SMRi P43250. Positions 2-557.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109128. 16 interactions.
IntActi P43250. 8 interactions.
MINTi MINT-1425525.
STRINGi 9606.ENSP00000377204.

Chemistry

BindingDBi P43250.
ChEMBLi CHEMBL6144.
GuidetoPHARMACOLOGYi 1470.

PTM databases

PhosphoSitei P43250.

Polymorphism databases

DMDMi 20141386.

Proteomic databases

MaxQBi P43250.
PaxDbi P43250.
PRIDEi P43250.

Protocols and materials databases

DNASUi 2870.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000355472 ; ENSP00000347655 ; ENSG00000198055 . [P43250-1 ]
ENST00000355958 ; ENSP00000348230 ; ENSG00000198055 . [P43250-3 ]
ENST00000528793 ; ENSP00000433511 ; ENSG00000198055 . [P43250-2 ]
GeneIDi 2870.
KEGGi hsa:2870.
UCSCi uc003mgq.2. human. [P43250-3 ]
uc021yit.1. human. [P43250-1 ]
uc021yiu.1. human. [P43250-2 ]

Organism-specific databases

CTDi 2870.
GeneCardsi GC05P176853.
HGNCi HGNC:4545. GRK6.
HPAi HPA015327.
HPA018903.
MIMi 600869. gene.
neXtProti NX_P43250.
PharmGKBi PA28942.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118793.
HOGENOMi HOG000006742.
HOVERGENi HBG004532.
InParanoidi P43250.
KOi K08291.
OMAi MLEPPFK.
OrthoDBi EOG7V1FQK.
PhylomeDBi P43250.
TreeFami TF313940.

Enzyme and pathway databases

BRENDAi 2.7.11.16. 2681.
SignaLinki P43250.

Miscellaneous databases

EvolutionaryTracei P43250.
GeneWikii GRK6.
GenomeRNAii 2870.
NextBioi 11323.
PROi P43250.
SOURCEi Search...

Gene expression databases

Bgeei P43250.
CleanExi HS_GRK6.
ExpressionAtlasi P43250. baseline and differential.
Genevestigatori P43250.

Family and domain databases

InterProi IPR000961. AGC-kinase_C.
IPR000239. GPCR_kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view ]
PRINTSi PR00717. GPCRKINASE.
SMARTi SM00315. RGS. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF48097. SSF48097. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484 AND THR-485, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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.

Entry informationi

Entry nameiGRK6_HUMAN
AccessioniPrimary (citable) accession number: P43250
Secondary accession number(s): O60541, Q13652
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2002
Last modified: October 29, 2014
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3