Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P43250

- GRK6_HUMAN

UniProt

P43250 - GRK6_HUMAN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 2 (23 Jan 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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
    3. protein binding Source: IntAct

    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

    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

    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

    ArrayExpressiP43250.
    BgeeiP43250.
    CleanExiHS_GRK6.
    GenevestigatoriP43250.

    Organism-specific databases

    HPAiHPA015327.
    HPA018903.

    Interactioni

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi109128. 15 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.
    HOGENOMiHOG000006742.
    HOVERGENiHBG004532.
    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_dom.
    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

    MELENIVANT VLLKAREGGG GNRKGKSKKW RQMLQFPHIS QCEELRLSLE    50
    RDYHSLCERQ PIGRLLFREF CATRPELSRC VAFLDGVAEY EVTPDDKRKA 100
    CGRQLTQNFL SHTGPDLIPE VPRQLVTNCT QRLEQGPCKD LFQELTRLTH 150
    EYLSVAPFAD YLDSIYFNRF LQWKWLERQP VTKNTFRQYR VLGKGGFGEV 200
    CACQVRATGK MYACKKLEKK RIKKRKGEAM ALNEKQILEK VNSRFVVSLA 250
    YAYETKDALC LVLTLMNGGD LKFHIYHMGQ AGFPEARAVF YAAEICCGLE 300
    DLHRERIVYR DLKPENILLD DHGHIRISDL GLAVHVPEGQ TIKGRVGTVG 350
    YMAPEVVKNE RYTFSPDWWA LGCLLYEMIA GQSPFQQRKK KIKREEVERL 400
    VKEVPEEYSE RFSPQARSLC SQLLCKDPAE RLGCRGGSAR EVKEHPLFKK 450
    LNFKRLGAGM LEPPFKPDPQ AIYCKDVLDI EQFSTVKGVE LEPTDQDFYQ 500
    KFATGSVPIP WQNEMVETEC FQELNVFGLD GSVPPDLDWK GQPPAPPKKG 550
    LLQRLFSRQD CCGNCSDSEE ELPTRL 576
    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. 15 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.
    HOGENOMi HOG000006742.
    HOVERGENi HBG004532.
    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

    ArrayExpressi P43250.
    Bgeei P43250.
    CleanExi HS_GRK6.
    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_dom.
    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

    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 1, 2014
    This is version 153 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