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P63244

- GBLP_HUMAN

UniProt

P63244 - GBLP_HUMAN

Protein

Guanine nucleotide-binding protein subunit beta-2-like 1

Gene

GNB2L1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression. Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC-dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome-mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates internalization of the muscarinic receptor CHRM2. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration. Binds to Y.pseudotuberculosis yopK which leads to inhibition of phagocytosis and survival of bacteria following infection of host cells. Enhances phosphorylation of HIV-1 Nef by PKCs. Promotes migration of breast carcinoma cells by binding to and activating RHOA.19 Publications

    GO - Molecular functioni

    1. cysteine-type endopeptidase activator activity involved in apoptotic process Source: UniProtKB
    2. enzyme binding Source: BHF-UCL
    3. ion channel inhibitor activity Source: UniProtKB
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein complex scaffold Source: BHF-UCL
    7. protein homodimerization activity Source: ParkinsonsUK-UCL
    8. protein kinase C binding Source: UniProtKB
    9. protein phosphatase binding Source: UniProtKB
    10. protein tyrosine kinase inhibitor activity Source: UniProtKB
    11. receptor binding Source: UniProtKB
    12. receptor tyrosine kinase binding Source: UniProtKB
    13. SH2 domain binding Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    2. cell cycle Source: UniProtKB-KW
    3. gastrulation Source: UniProtKB-KW
    4. negative regulation of cell growth Source: UniProtKB
    5. negative regulation of gene expression Source: UniProt
    6. negative regulation of hydrogen peroxide-mediated programmed cell death Source: ParkinsonsUK-UCL
    7. negative regulation of neuron apoptotic process Source: ParkinsonsUK-UCL
    8. negative regulation of phagocytosis Source: UniProtKB
    9. negative regulation of protein kinase B signaling Source: UniProtKB
    10. negative regulation of protein tyrosine kinase activity Source: GOC
    11. negative regulation of translation Source: UniProtKB
    12. negative regulation of Wnt signaling pathway Source: UniProtKB
    13. positive regulation of apoptotic process Source: UniProtKB
    14. positive regulation of cAMP catabolic process Source: BHF-UCL
    15. positive regulation of cell migration Source: UniProtKB
    16. positive regulation of cyclic-nucleotide phosphodiesterase activity Source: BHF-UCL
    17. positive regulation of gastrulation Source: UniProtKB
    18. positive regulation of GTPase activity Source: UniProtKB
    19. positive regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
    20. positive regulation of mitochondrial depolarization Source: UniProtKB
    21. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
    22. positive regulation of protein homooligomerization Source: UniProtKB
    23. positive regulation of protein phosphorylation Source: UniProtKB
    24. regulation of cell cycle Source: UniProtKB
    25. regulation of cell division Source: UniProtKB
    26. regulation of establishment of cell polarity Source: UniProtKB
    27. regulation of establishment of protein localization to plasma membrane Source: Ensembl
    28. regulation of protein localization Source: UniProtKB
    29. rhythmic process Source: UniProtKB-KW
    30. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Apoptosis, Biological rhythms, Cell cycle, Gastrulation, Growth regulation, Host-virus interaction, Translation regulation

    Enzyme and pathway databases

    SignaLinkiP63244.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Guanine nucleotide-binding protein subunit beta-2-like 1
    Alternative name(s):
    Cell proliferation-inducing gene 21 protein
    Guanine nucleotide-binding protein subunit beta-like protein 12.3
    Human lung cancer oncogene 7 protein
    Short name:
    HLC-7
    Receptor for activated C kinase
    Receptor of activated protein kinase C 1
    Short name:
    RACK1
    Cleaved into the following chain:
    Gene namesi
    Name:GNB2L1
    ORF Names:HLC7, PIG21
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:4399. GNB2L1.

    Subcellular locationi

    Cell membrane; Peripheral membrane protein. Cytoplasm. Cytoplasmperinuclear region. Cytoplasmcytoskeleton. Nucleus. Perikaryon By similarity. Cell projectiondendrite By similarity. Cell projectionphagocytic cup
    Note: Recruited to the plasma membrane through interaction with KRT1 which binds to membrane-bound ITGB1. Also associated with the membrane in oncogene-transformed cells. PKC activation induces translocation from the perinuclear region to the cell periphery. In the brain, detected mainly in cell bodies and dendrites with little expression in axonal fibers or nuclei. Localized to phagocytic cups following infection by Y.pestis.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoskeleton Source: UniProtKB-SubCell
    3. cytosol Source: UniProtKB
    4. dendrite Source: UniProtKB
    5. extracellular vesicular exosome Source: UniProt
    6. midbody Source: UniProtKB
    7. mitochondrion Source: UniProtKB
    8. neuronal cell body Source: UniProtKB
    9. nucleus Source: UniProtKB
    10. perikaryon Source: UniProtKB-SubCell
    11. perinuclear region of cytoplasm Source: UniProtKB
    12. phagocytic cup Source: UniProtKB
    13. small ribosomal subunit Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi52 – 521Y → F: No effect on binding to SRC. Abolishes binding to PTK2/FAK1 and reduces cell adhesion and foci formation. 3 Publications
    Mutagenesisi57 – 571R → A: Decreased binding to PTK2/FAK1; when associated with A-60. 1 Publication
    Mutagenesisi60 – 601R → A: Decreased binding to PTK2/FAK1; when associated with A-57. 1 Publication
    Mutagenesisi127 – 1271K → A: Decreased binding to PTK2/FAK1; when associated with A-130. 1 Publication
    Mutagenesisi130 – 1301K → A: Decreased binding to PTK2/FAK1; when associated with A-127. 1 Publication
    Mutagenesisi140 – 1401Y → F: No effect on binding to SRC. 2 Publications
    Mutagenesisi194 – 1941Y → F: No effect on binding to SRC. 2 Publications
    Mutagenesisi228 – 2281Y → F: No effect on binding to SRC. Does not abolish phosphorylation by SRC. Abolishes phosphorylation by SRC; when associated with F-246 and F-302. 2 Publications
    Mutagenesisi246 – 2461Y → F: Abolishes binding to SRC. Does not abolish phosphorylation by SRC. Abolishes phosphorylation by SRC; when associated with F-228 and F-302. 2 Publications
    Mutagenesisi302 – 3021Y → F: No effect on binding to SRC. Abolishes phosphorylation by SRC; when associated with F-228 and F-246. 2 Publications

    Organism-specific databases

    PharmGKBiPA28779.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 317317Guanine nucleotide-binding protein subunit beta-2-like 1PRO_0000424480Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate4 Publications
    Chaini2 – 317316Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processedPRO_0000127731Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei2 – 21N-acetylthreonine; in Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed5 Publications
    Modified residuei52 – 521Phosphotyrosine; by ABL12 Publications
    Modified residuei130 – 1301N6-acetyllysine1 Publication
    Modified residuei183 – 1831N6-acetyllysineBy similarity
    Modified residuei228 – 2281Phosphotyrosine2 Publications

    Post-translational modificationi

    Phosphorylated on Tyr-228 and/or Tyr-246 by SRC. This is required for binding to SRC.3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP63244.
    PaxDbiP63244.
    PRIDEiP63244.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00848226.
    P63244.

    PTM databases

    PhosphoSiteiP63244.

    Expressioni

    Tissue specificityi

    In the liver, expressed at higher levels in activated hepatic stellate cells than in hepatocytes or Kupffer cells. Up-regulated in hepatocellular carcinomas and in the adjacent non-tumor liver tissue.1 Publication

    Gene expression databases

    ArrayExpressiP63244.
    BgeeiP63244.
    CleanExiHS_GNB2L1.
    GenevestigatoriP63244.

    Organism-specific databases

    HPAiCAB004288.
    HPA021676.

    Interactioni

    Subunit structurei

    Component of the small (40S) ribosomal subunit By similarity. Interacts with the 80S ribosome. Exists as a monomer and also forms oligomers. Binds SLC9A3R1. Forms a ternary complex with TRIM63 and PRKCE. Interacts with HABP4, KRT1 and OTUB1. Interacts with SRC (via SH2 domain); the interaction is enhanced by tyrosine phosphorylation of GNB2L1/RACK1. Recruited in a circadian manner into a nuclear complex which also includes BMAL1 and PRKCA. Interacts with AR. Interacts with IGF1R but not with INSR. Interacts with ADAM12. Interacts with CLEC1B (via N-terminal region) and with HIF1A; the interaction promotes their degradation. Interacts with RHOA; this enhances RHOA activation and promotes cell migration. Interacts with CHRM2; the interaction regulates CHRM2 internalization. Interacts with TRPM6 (via kinase domain). Interacts with PTK2/FAK1; required for PTK2/FAK1 phosphorylation and dephosphorylation. Interacts with FLT1. Interacts with TBXA2R isoform 2. Interacts with HRAS. Interacts with LARP4B. Interacts with PKD2L1. Interacts with Y.pseudotuberculosis yopK. Interacts with a number of viral proteins including Epstein-Barr virus BZLF1 and HIV-1 Nef; interaction with Nef increases Nef phosphorylation by PKC.By similarity28 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACHEP223032EBI-296739,EBI-1637793
    AGO2Q9UKV82EBI-296739,EBI-528269
    BCL2L11O435212EBI-296739,EBI-526406
    Bcl2l11O54918-12EBI-296739,EBI-526076From a different organism.
    DYNLL1P631676EBI-296739,EBI-349105
    IFNAR2P485514EBI-296739,EBI-958408
    LRP12Q9Y5612EBI-296739,EBI-296693
    LYNP079482EBI-296739,EBI-79452
    PAG1Q9NWQ82EBI-296739,EBI-2828115
    PIAS2O759282EBI-296739,EBI-348555
    PPIDQ087524EBI-296739,EBI-716596
    VHLP403379EBI-296739,EBI-301246

    Protein-protein interaction databases

    BioGridi115671. 156 interactions.
    DIPiDIP-46736N.
    IntActiP63244. 72 interactions.
    MINTiMINT-105673.
    STRINGi9606.ENSP00000366013.

    Structurei

    Secondary structure

    1
    317
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 118
    Beta strandi18 – 236
    Beta strandi30 – 356
    Beta strandi40 – 456
    Beta strandi48 – 503
    Beta strandi52 – 598
    Beta strandi66 – 716
    Beta strandi75 – 828
    Beta strandi85 – 917
    Turni92 – 954
    Beta strandi96 – 1027
    Beta strandi108 – 1136
    Beta strandi120 – 1245
    Beta strandi129 – 1324
    Beta strandi138 – 1425
    Beta strandi144 – 1463
    Beta strandi151 – 1566
    Beta strandi160 – 1623
    Beta strandi164 – 1696
    Beta strandi174 – 1785
    Turni179 – 1824
    Beta strandi183 – 1886
    Beta strandi195 – 2006
    Beta strandi204 – 2118
    Beta strandi215 – 2206
    Turni221 – 2244
    Beta strandi225 – 2317
    Beta strandi236 – 2416
    Beta strandi243 – 25210
    Beta strandi255 – 2606
    Turni261 – 2644
    Beta strandi265 – 2706
    Beta strandi286 – 2916
    Beta strandi295 – 3028
    Beta strandi307 – 3137

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Aelectron microscopy5.00g1-317[»]
    4AOWX-ray2.45A/B/C1-317[»]
    ProteinModelPortaliP63244.
    SMRiP63244. Positions 2-314.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati13 – 4432WD 1Add
    BLAST
    Repeati61 – 9131WD 2Add
    BLAST
    Repeati103 – 13331WD 3Add
    BLAST
    Repeati146 – 17833WD 4Add
    BLAST
    Repeati190 – 22031WD 5Add
    BLAST
    Repeati231 – 26030WD 6Add
    BLAST
    Repeati281 – 31131WD 7Add
    BLAST

    Sequence similaritiesi

    Belongs to the WD repeat G protein beta family.Curated
    Contains 7 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    HOVERGENiHBG000277.
    InParanoidiP63244.
    KOiK14753.
    OMAiKSIIMWK.
    PhylomeDBiP63244.
    TreeFamiTF300600.

    Family and domain databases

    Gene3Di2.130.10.10. 2 hits.
    InterProiIPR020472. G-protein_beta_WD-40_rep.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PfamiPF00400. WD40. 7 hits.
    [Graphical view]
    PRINTSiPR00320. GPROTEINBRPT.
    SMARTiSM00320. WD40. 7 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 1 hit.
    PROSITEiPS00678. WD_REPEATS_1. 4 hits.
    PS50082. WD_REPEATS_2. 6 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P63244-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTEQMTLRGT LKGHNGWVTQ IATTPQFPDM ILSASRDKTI IMWKLTRDET    50
    NYGIPQRALR GHSHFVSDVV ISSDGQFALS GSWDGTLRLW DLTTGTTTRR 100
    FVGHTKDVLS VAFSSDNRQI VSGSRDKTIK LWNTLGVCKY TVQDESHSEW 150
    VSCVRFSPNS SNPIIVSCGW DKLVKVWNLA NCKLKTNHIG HTGYLNTVTV 200
    SPDGSLCASG GKDGQAMLWD LNEGKHLYTL DGGDIINALC FSPNRYWLCA 250
    ATGPSIKIWD LEGKIIVDEL KQEVISTSSK AEPPQCTSLA WSADGQTLFA 300
    GYTDNLVRVW QVTIGTR 317
    Length:317
    Mass (Da):35,077
    Last modified:January 23, 2007 - v3
    Checksum:i257F91E369ED2044
    GO

    Sequence cautioni

    The sequence AAR24619.1 differs from that shown. Reason: Frameshift at position 94.
    The sequence AAO21313.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti70 – 11142Missing in BAG53102. (PubMed:14702039)CuratedAdd
    BLAST
    Sequence conflicti94 – 941T → TRK in AAR24619. 1 PublicationCurated
    Sequence conflicti221 – 2211L → F in BAD96208. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24194 mRNA. Translation: AAA59626.1.
    AY159316 mRNA. Translation: AAO21313.1. Different initiation.
    AY336089 mRNA. Translation: AAR24619.1. Frameshift.
    AK095666 mRNA. Translation: BAG53102.1.
    CR456978 mRNA. Translation: CAG33259.1.
    CR541909 mRNA. Translation: CAG46707.1.
    AK222488 mRNA. Translation: BAD96208.1.
    CH471165 Genomic DNA. Translation: EAW53692.1.
    CH471165 Genomic DNA. Translation: EAW53702.1.
    BC000214 mRNA. Translation: AAH00214.1.
    BC000366 mRNA. Translation: AAH00366.1.
    BC010119 mRNA. Translation: AAH10119.1.
    BC014256 mRNA. Translation: AAH14256.1.
    BC014788 mRNA. Translation: AAH14788.1.
    BC017287 mRNA. Translation: AAH17287.1.
    BC019093 mRNA. Translation: AAH19093.1.
    BC019362 mRNA. Translation: AAH19362.1.
    BC021993 mRNA. Translation: AAH21993.1.
    BC032006 mRNA. Translation: AAH32006.1.
    CCDSiCCDS34324.1.
    PIRiB33928.
    RefSeqiNP_006089.1. NM_006098.4.
    UniGeneiHs.5662.

    Genome annotation databases

    EnsembliENST00000512805; ENSP00000426909; ENSG00000204628.
    GeneIDi10399.
    KEGGihsa:10399.
    UCSCiuc003mni.1. human.

    Polymorphism databases

    DMDMi54037168.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24194 mRNA. Translation: AAA59626.1 .
    AY159316 mRNA. Translation: AAO21313.1 . Different initiation.
    AY336089 mRNA. Translation: AAR24619.1 . Frameshift.
    AK095666 mRNA. Translation: BAG53102.1 .
    CR456978 mRNA. Translation: CAG33259.1 .
    CR541909 mRNA. Translation: CAG46707.1 .
    AK222488 mRNA. Translation: BAD96208.1 .
    CH471165 Genomic DNA. Translation: EAW53692.1 .
    CH471165 Genomic DNA. Translation: EAW53702.1 .
    BC000214 mRNA. Translation: AAH00214.1 .
    BC000366 mRNA. Translation: AAH00366.1 .
    BC010119 mRNA. Translation: AAH10119.1 .
    BC014256 mRNA. Translation: AAH14256.1 .
    BC014788 mRNA. Translation: AAH14788.1 .
    BC017287 mRNA. Translation: AAH17287.1 .
    BC019093 mRNA. Translation: AAH19093.1 .
    BC019362 mRNA. Translation: AAH19362.1 .
    BC021993 mRNA. Translation: AAH21993.1 .
    BC032006 mRNA. Translation: AAH32006.1 .
    CCDSi CCDS34324.1.
    PIRi B33928.
    RefSeqi NP_006089.1. NM_006098.4.
    UniGenei Hs.5662.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3J3A electron microscopy 5.00 g 1-317 [» ]
    4AOW X-ray 2.45 A/B/C 1-317 [» ]
    ProteinModelPortali P63244.
    SMRi P63244. Positions 2-314.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115671. 156 interactions.
    DIPi DIP-46736N.
    IntActi P63244. 72 interactions.
    MINTi MINT-105673.
    STRINGi 9606.ENSP00000366013.

    PTM databases

    PhosphoSitei P63244.

    Polymorphism databases

    DMDMi 54037168.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00848226.
    P63244.

    Proteomic databases

    MaxQBi P63244.
    PaxDbi P63244.
    PRIDEi P63244.

    Protocols and materials databases

    DNASUi 10399.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000512805 ; ENSP00000426909 ; ENSG00000204628 .
    GeneIDi 10399.
    KEGGi hsa:10399.
    UCSCi uc003mni.1. human.

    Organism-specific databases

    CTDi 10399.
    GeneCardsi GC05M180663.
    HGNCi HGNC:4399. GNB2L1.
    HPAi CAB004288.
    HPA021676.
    MIMi 176981. gene.
    neXtProti NX_P63244.
    PharmGKBi PA28779.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOVERGENi HBG000277.
    InParanoidi P63244.
    KOi K14753.
    OMAi KSIIMWK.
    PhylomeDBi P63244.
    TreeFami TF300600.

    Enzyme and pathway databases

    SignaLinki P63244.

    Miscellaneous databases

    ChiTaRSi GNB2L1. human.
    GeneWikii GNB2L1.
    GenomeRNAii 10399.
    NextBioi 39404.
    PROi P63244.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P63244.
    Bgeei P63244.
    CleanExi HS_GNB2L1.
    Genevestigatori P63244.

    Family and domain databases

    Gene3Di 2.130.10.10. 2 hits.
    InterProi IPR020472. G-protein_beta_WD-40_rep.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF00400. WD40. 7 hits.
    [Graphical view ]
    PRINTSi PR00320. GPROTEINBRPT.
    SMARTi SM00320. WD40. 7 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS00678. WD_REPEATS_1. 4 hits.
    PS50082. WD_REPEATS_2. 6 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Physical linkage of a guanine nucleotide-binding protein-related gene to the chicken major histocompatibility complex."
      Guillemot F., Billault A., Auffray C.
      Proc. Natl. Acad. Sci. U.S.A. 86:4594-4598(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Identification of new tumor-related gene in human lung cancer."
      Kim J.W.
      Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "Identification of a proliferation-inducing gene."
      Kim J.W.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Adipose tissue.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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].
      Tissue: B-cell, Brain, Cervix, Lung, Lymph, Ovary and Skin.
    9. Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
      Submitted (MAY-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-11; 48-57; 107-118; 258-280 AND 309-317, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma and T-cell.
    10. Lubec G., Afjehi-Sadat L.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 48-57; 107-118; 140-155 AND 226-245, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    11. "RACK1, a receptor for activated C kinase and a homolog of the beta subunit of G proteins, inhibits activity of src tyrosine kinases and growth of NIH 3T3 cells."
      Chang B.Y., Conroy K.B., Machleder E.M., Cartwright C.A.
      Mol. Cell. Biol. 18:3245-3256(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SRC.
    12. "The PKC targeting protein RACK1 interacts with the Epstein-Barr virus activator protein BZLF1."
      Baumann M., Gires O., Kolch W., Mischak H., Zeidler R., Pich D., Hammerschmidt W.
      Eur. J. Biochem. 267:3891-3901(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EPSTEIN-BARR VIRUS BZLF1, SUBCELLULAR LOCATION.
    13. "The interaction of Src and RACK1 is enhanced by activation of protein kinase C and tyrosine phosphorylation of RACK1."
      Chang B.Y., Chiang M., Cartwright C.A.
      J. Biol. Chem. 276:20346-20356(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SRC, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-228, MUTAGENESIS OF TYR-52; TYR-140; TYR-194; TYR-228; TYR-246 AND TYR-302.
    14. "Rack1 binds HIV-1 Nef and can act as a Nef-protein kinase C adaptor."
      Gallina A., Rossi F., Milanesi G.
      Virology 283:7-18(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HIV-1 NEF, SUBCELLULAR LOCATION.
    15. "Protein kinase C epsilon-dependent regulation of cystic fibrosis transmembrane regulator involves binding to a receptor for activated C kinase (RACK1) and RACK1 binding to Na+/H+ exchange regulatory factor."
      Liedtke C.M., Yun C.H.C., Kyle N., Wang D.
      J. Biol. Chem. 277:22925-22933(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLC9A3R1.
    16. "RACK1, an insulin-like growth factor I (IGF-I) receptor-interacting protein, modulates IGF-I-dependent integrin signaling and promotes cell spreading and contact with extracellular matrix."
      Hermanto U., Zong C.S., Li W., Wang L.H.
      Mol. Cell. Biol. 22:2345-2365(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH IGF1R.
    17. "RACK1: a novel substrate for the Src protein-tyrosine kinase."
      Chang B.Y., Harte R.A., Cartwright C.A.
      Oncogene 21:7619-7629(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, MUTAGENESIS OF TYR-52; TYR-140; TYR-194; TYR-228; TYR-246 AND TYR-302.
    18. "Alternative splicing of the human proto-oncogene c-H-ras renders a new Ras family protein that trafficks to cytoplasm and nucleus."
      Guil S., de La Iglesia N., Fernandez-Larrea J., Cifuentes D., Ferrer J.C., Guinovart J.J., Bach-Elias M.
      Cancer Res. 63:5178-5187(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HRAS.
    19. "The scaffolding protein RACK1 interacts with androgen receptor and promotes cross-talk through a protein kinase C signaling pathway."
      Rigas A.C., Ozanne D.M., Neal D.E., Robson C.N.
      J. Biol. Chem. 278:46087-46093(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AR, SUBCELLULAR LOCATION.
    20. "RACK1 regulates integrin-mediated adhesion, protrusion, and chemotactic cell migration via its Src-binding site."
      Cox E.A., Bennin D., Doan A.T., O'Toole T., Huttenlocher A.
      Mol. Biol. Cell 14:658-669(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "Muscle ring finger protein-1 inhibits PKC-epsilon activation and prevents cardiomyocyte hypertrophy."
      Arya R., Kedar V., Hwang J.R., McDonough H., Li H.-H., Taylor J., Patterson C.
      J. Cell Biol. 167:1147-1159(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIM63 AND PRKCE.
    22. "Ki-1/57 interacts with RACK1 and is a substrate for the phosphorylation by phorbol 12-myristate 13-acetate-activated protein kinase C."
      Nery F.C., Passos D.O., Garcia V.S., Kobarg J.
      J. Biol. Chem. 279:11444-11455(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HABP4.
    23. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Receptor for activated C kinase 1 (RACK1) and Src regulate the tyrosine phosphorylation and function of the androgen receptor."
      Kraus S., Gioeli D., Vomastek T., Gordon V., Weber M.J.
      Cancer Res. 66:11047-11054(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AR.
    25. "Interaction of integrin beta1 with cytokeratin 1 in neuroblastoma NMB7 cells."
      Chuang N.N., Huang C.C.
      Biochem. Soc. Trans. 35:1292-1294(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH KRT1, SUBCELLULAR LOCATION.
    26. "RACK1 competes with HSP90 for binding to HIF-1alpha and is required for O(2)-independent and HSP90 inhibitor-induced degradation of HIF-1alpha."
      Liu Y.V., Baek J.H., Zhang H., Diez R., Cole R.N., Semenza G.L.
      Mol. Cell 25:207-217(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HIF1A, IDENTIFICATION BY MASS SPECTROMETRY.
    27. "RACK1 inhibits TRPM6 activity via phosphorylation of the fused alpha-kinase domain."
      Cao G., Thebault S., van der Wijst J., van der Kemp A., Lasonder E., Bindels R.J., Hoenderop J.G.
      Curr. Biol. 18:168-176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TRPM6.
    28. "RACK1, a new ADAM12 interacting protein. Contribution to liver fibrogenesis."
      Bourd-Boittin K., Le Pabic H., Bonnier D., L'Helgoualc'h A., Theret N.
      J. Biol. Chem. 283:26000-26009(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ADAM12, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    29. "RACK1 regulates the cell surface expression of the G protein-coupled receptor for thromboxane A(2)."
      Parent A., Laroche G., Hamelin E., Parent J.L.
      Traffic 9:394-407(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TBXA2R, SUBCELLULAR LOCATION.
    30. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "RACK1 associates with CLEC-2 and promotes its ubiquitin-proteasome degradation."
      Ruan Y., Guo L., Qiao Y., Hong Y., Zhou L., Sun L., Wang L., Zhu H., Wang L., Yun X., Xie J., Gu J.
      Biochem. Biophys. Res. Commun. 390:217-222(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CLEC1B, SUBCELLULAR LOCATION.
    32. "Structural basis and specificity of human otubain 1-mediated deubiquitination."
      Edelmann M.J., Iphoefer A., Akutsu M., Altun M., di Gleria K., Kramer H.B., Fiebiger E., Dhe-Paganon S., Kessler B.M.
      Biochem. J. 418:379-390(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH OTUB1.
    33. "Phosphorylation of RACK1 on tyrosine 52 by c-Abl is required for insulin-like growth factor I-mediated regulation of focal adhesion kinase."
      Kiely P.A., Baillie G.S., Barrett R., Buckley D.A., Adams D.R., Houslay M.D., O'Connor R.
      J. Biol. Chem. 284:20263-20274(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PTK2/FAK1, PHOSPHORYLATION AT TYR-52, MUTAGENESIS OF TYR-52; ARG-57; ARG-60; LYS-127 AND LYS-130.
    34. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    35. "RACK1 promotes Bax oligomerization and dissociates the interaction of Bax and Bcl-XL."
      Wu Y., Wang Y., Sun Y., Zhang L., Wang D., Ren F., Chang D., Chang Z., Jia B.
      Cell. Signal. 22:1495-1501(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BAX.
    36. "RACK1 associates with muscarinic receptors and regulates M(2) receptor trafficking."
      Reiner C.L., McCullar J.S., Kow R.L., Le J.H., Goodlett D.R., Nathanson N.M.
      PLoS ONE 5:E13517-E13517(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CHRM2, IDENTIFICATION BY MASS SPECTROMETRY.
    37. "A stimulatory role for the La-related protein 4B in translation."
      Schaffler K., Schulz K., Hirmer A., Wiesner J., Grimm M., Sickmann A., Fischer U.
      RNA 16:1488-1499(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PABPC1 AND GNB2L1.
    38. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    39. "RACK1 promotes breast carcinoma migration/metastasis via activation of the RhoA/Rho kinase pathway."
      Cao X.X., Xu J.D., Xu J.W., Liu X.L., Cheng Y.Y., Li Q.Q., Xu Z.D., Liu X.P.
      Breast Cancer Res. Treat. 126:555-563(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RHOA, SUBCELLULAR LOCATION.
    40. "RACK1 regulates VEGF/Flt1-mediated cell migration via activation of a PI3-K/Akt pathway."
      Wang F., Yamauchi M., Muramatsu M., Osawa T., Tsuchida R., Shibuya M.
      J. Biol. Chem. 286:9097-9106(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FLT1.
    41. "The RACK1 signaling scaffold protein selectively interacts with Yersinia pseudotuberculosis virulence function."
      Thorslund S.E., Edgren T., Pettersson J., Nordfelth R., Sellin M.E., Ivanova E., Francis M.S., Isaksson E.L., Wolf-Watz H., Fallman M.
      PLoS ONE 6:E16784-E16784(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH YERSINIA PSEUDOTUBERCULOSIS YOPK, SUBCELLULAR LOCATION.
    42. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    43. "Receptor for activated C kinase 1 (RACK1) inhibits function of transient receptor potential (TRP)-type channel Pkd2L1 through physical interaction."
      Yang J., Wang Q., Zheng W., Tuli J., Li Q., Wu Y., Hussein S., Dai X.Q., Shafiei S., Li X.G., Shen P.Y., Tu J.C., Chen X.Z.
      J. Biol. Chem. 287:6551-6561(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PKD2L1.
    44. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    45. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    46. Cited for: X-RAY SCATTERING SOLUTION STRUCTURE, INTERACTION WITH HABP4.
    47. Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
    48. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) IN COMPLEX WITH THE 80S RIBOSOME, SUBUNIT.

    Entry informationi

    Entry nameiGBLP_HUMAN
    AccessioniPrimary (citable) accession number: P63244
    Secondary accession number(s): B3KTJ0
    , D3DWS0, P25388, P99049, Q53HU2, Q5J8M6, Q5VLR4, Q6FH47
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 111 of the entry and version 3 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3