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P63244 (GBLP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Gene names
Name:GNB2L1
ORF Names:HLC7, PIG21
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11 Ref.14 Ref.16 Ref.19 Ref.20 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.31 Ref.33 Ref.35 Ref.36 Ref.37 Ref.39 Ref.40 Ref.41

Subunit structure

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. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.21 Ref.22 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.31 Ref.32 Ref.33 Ref.35 Ref.36 Ref.37 Ref.39 Ref.40 Ref.41 Ref.43 Ref.46 Ref.48

Subcellular location

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. Ref.12 Ref.13 Ref.14 Ref.16 Ref.19 Ref.25 Ref.28 Ref.29 Ref.31 Ref.37 Ref.39 Ref.41

Tissue specificity

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. Ref.28

Post-translational modification

Phosphorylated on Tyr-228 and/or Tyr-246 by SRC. This is required for binding to SRC. Ref.13 Ref.17 Ref.33

Sequence similarities

Belongs to the WD repeat G protein beta family.

Contains 7 WD repeats.

Sequence caution

The sequence AAO21313.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAR24619.1 differs from that shown. Reason: Frameshift at position 94.

Ontologies

Keywords
   Biological processApoptosis
Biological rhythms
Cell cycle
Gastrulation
Growth regulation
Host-virus interaction
Translation regulation
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
Nucleus
   DomainRepeat
WD repeat
   Molecular functionDevelopmental protein
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype PubMed 19767770. Source: UniProtKB

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

gastrulation

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of Wnt signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell growth

Inferred from direct assay Ref.11. Source: UniProtKB

negative regulation of phagocytosis

Inferred from mutant phenotype Ref.41. Source: UniProtKB

negative regulation of protein kinase B signaling

Inferred from mutant phenotype PubMed 19767770. Source: UniProtKB

negative regulation of protein tyrosine kinase activity

Inferred from direct assay Ref.11. Source: GOC

negative regulation of translation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of GTPase activity

Inferred from direct assay Ref.39. Source: UniProtKB

positive regulation of apoptotic process

Inferred from direct assay Ref.35. Source: UniProtKB

positive regulation of cAMP catabolic process

Inferred from mutant phenotype PubMed 20819076. Source: BHF-UCL

positive regulation of cell migration

Inferred from direct assay Ref.39. Source: UniProtKB

positive regulation of cyclic-nucleotide phosphodiesterase activity

Inferred from mutant phenotype PubMed 20819076. Source: BHF-UCL

positive regulation of gastrulation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of intrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 19767770. Source: UniProtKB

positive regulation of mitochondrial depolarization

Inferred from mutant phenotype PubMed 19767770. Source: UniProtKB

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.31. Source: UniProtKB

positive regulation of protein homooligomerization

Inferred from direct assay Ref.35. Source: UniProtKB

positive regulation of protein phosphorylation

Inferred from direct assay Ref.14Ref.24. Source: UniProtKB

regulation of cell cycle

Inferred from direct assay Ref.11. Source: UniProtKB

regulation of cell division

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of establishment of cell polarity

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of establishment of protein localization to plasma membrane

Inferred from electronic annotation. Source: Ensembl

regulation of protein localization

Inferred from sequence or structural similarity. Source: UniProtKB

rhythmic process

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay Ref.12Ref.31. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from mutant phenotype PubMed 19767770. Source: UniProtKB

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

midbody

Inferred from direct assay PubMed 15166316. Source: UniProtKB

mitochondrion

Inferred from mutant phenotype PubMed 19767770. Source: UniProtKB

neuronal cell body

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay Ref.12Ref.24. Source: UniProtKB

perikaryon

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from direct assay Ref.13. Source: UniProtKB

phagocytic cup

Inferred from direct assay Ref.41. Source: UniProtKB

small ribosomal subunit

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionSH2 domain binding

Inferred from direct assay Ref.13Ref.11. Source: UniProtKB

cysteine-type endopeptidase activator activity involved in apoptotic process

Inferred from mutant phenotype PubMed 19767770. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 20819076. Source: BHF-UCL

ion channel inhibitor activity

Inferred from sequence or structural similarity. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein complex scaffold

Traceable author statement PubMed 20819076. Source: BHF-UCL

protein kinase C binding

Inferred from direct assay Ref.13. Source: UniProtKB

protein phosphatase binding

Inferred from physical interaction PubMed 11278757. Source: UniProtKB

protein tyrosine kinase inhibitor activity

Inferred from direct assay Ref.11. Source: UniProtKB

receptor binding

Non-traceable author statement PubMed 12809483. Source: UniProtKB

receptor tyrosine kinase binding

Inferred from direct assay Ref.11. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 317317Guanine nucleotide-binding protein subunit beta-2-like 1
PRO_0000424480
Initiator methionine11Removed; alternate Ref.9
Chain2 – 317316Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed
PRO_0000127731

Regions

Repeat13 – 4432WD 1
Repeat61 – 9131WD 2
Repeat103 – 13331WD 3
Repeat146 – 17833WD 4
Repeat190 – 22031WD 5
Repeat231 – 26030WD 6
Repeat281 – 31131WD 7

Amino acid modifications

Modified residue11N-acetylmethionine Ref.45
Modified residue21N-acetylthreonine; in Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed Ref.9 Ref.30 Ref.42 Ref.44 Ref.45
Modified residue521Phosphotyrosine; by ABL1 Probable
Modified residue1301N6-acetyllysine Ref.34
Modified residue1831N6-acetyllysine By similarity
Modified residue2281Phosphotyrosine Ref.13

Experimental info

Mutagenesis521Y → F: No effect on binding to SRC. Abolishes binding to PTK2/FAK1 and reduces cell adhesion and foci formation. Ref.13 Ref.17 Ref.33
Mutagenesis571R → A: Decreased binding to PTK2/FAK1; when associated with A-60. Ref.33
Mutagenesis601R → A: Decreased binding to PTK2/FAK1; when associated with A-57. Ref.33
Mutagenesis1271K → A: Decreased binding to PTK2/FAK1; when associated with A-130. Ref.33
Mutagenesis1301K → A: Decreased binding to PTK2/FAK1; when associated with A-127. Ref.33
Mutagenesis1401Y → F: No effect on binding to SRC. Ref.13 Ref.17
Mutagenesis1941Y → F: No effect on binding to SRC. Ref.13 Ref.17
Mutagenesis2281Y → 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. Ref.13 Ref.17
Mutagenesis2461Y → F: Abolishes binding to SRC. Does not abolish phosphorylation by SRC. Abolishes phosphorylation by SRC; when associated with F-228 and F-302. Ref.13 Ref.17
Mutagenesis3021Y → F: No effect on binding to SRC. Abolishes phosphorylation by SRC; when associated with F-228 and F-246. Ref.13 Ref.17
Sequence conflict70 – 11142Missing in BAG53102. Ref.4
Sequence conflict941T → TRK in AAR24619. Ref.3
Sequence conflict2211L → F in BAD96208. Ref.6

Secondary structure

............................................................... 317
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P63244 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 257F91E369ED2044

FASTA31735,077
        10         20         30         40         50         60 
MTEQMTLRGT LKGHNGWVTQ IATTPQFPDM ILSASRDKTI IMWKLTRDET NYGIPQRALR 

        70         80         90        100        110        120 
GHSHFVSDVV ISSDGQFALS GSWDGTLRLW DLTTGTTTRR FVGHTKDVLS VAFSSDNRQI 

       130        140        150        160        170        180 
VSGSRDKTIK LWNTLGVCKY TVQDESHSEW VSCVRFSPNS SNPIIVSCGW DKLVKVWNLA 

       190        200        210        220        230        240 
NCKLKTNHIG HTGYLNTVTV SPDGSLCASG GKDGQAMLWD LNEGKHLYTL DGGDIINALC 

       250        260        270        280        290        300 
FSPNRYWLCA ATGPSIKIWD LEGKIIVDEL KQEVISTSSK AEPPQCTSLA WSADGQTLFA 

       310 
GYTDNLVRVW QVTIGTR 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[46]"Solution structure of the human signaling protein RACK1."
Goncalves K.A., Borges J.C., Silva J.C., Papa P.F., Bressan G.C., Torriani I.L., Kobarg J.
BMC Struct. Biol. 10:15-15(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY SCATTERING SOLUTION STRUCTURE, INTERACTION WITH HABP4.
[47]"Structure of human Rack1 protein at a resolution of 2.45 A."
Ruiz Carrillo D., Chandrasekaran R., Nilsson M., Cornvik T., Liew C.W., Tan S.M., Lescar J.
Acta Crystallogr. F 68:867-872(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
[48]"Structures of the human and Drosophila 80S ribosome."
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M., Wilson D.N., Beckmann R.
Nature 497:80-85(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) IN COMPLEX WITH THE 80S RIBOSOME, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRB33928.
RefSeqNP_006089.1. NM_006098.4.
UniGeneHs.5662.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Aelectron microscopy5.00g1-317[»]
4AOWX-ray2.45A/B/C1-317[»]
ProteinModelPortalP63244.
SMRP63244. Positions 2-314.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115671. 152 interactions.
DIPDIP-46736N.
IntActP63244. 71 interactions.
MINTMINT-105673.
STRING9606.ENSP00000366013.

PTM databases

PhosphoSiteP63244.

Polymorphism databases

DMDM54037168.

2D gel databases

REPRODUCTION-2DPAGEIPI00848226.
P63244.

Proteomic databases

PaxDbP63244.
PRIDEP63244.

Protocols and materials databases

DNASU10399.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000512805; ENSP00000426909; ENSG00000204628.
GeneID10399.
KEGGhsa:10399.
UCSCuc003mni.1. human.

Organism-specific databases

CTD10399.
GeneCardsGC05M180663.
HGNCHGNC:4399. GNB2L1.
HPACAB004288.
HPA021676.
MIM176981. gene.
neXtProtNX_P63244.
PharmGKBPA28779.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOVERGENHBG000277.
InParanoidP63244.
KOK14753.
OMAIRVWQVM.
PhylomeDBP63244.
TreeFamTF300600.

Enzyme and pathway databases

SignaLinkP63244.

Gene expression databases

ArrayExpressP63244.
BgeeP63244.
CleanExHS_GNB2L1.
GenevestigatorP63244.

Family and domain databases

Gene3D2.130.10.10. 2 hits.
InterProIPR020472. 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]
PfamPF00400. WD40. 7 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGNB2L1. human.
GeneWikiGNB2L1.
GenomeRNAi10399.
NextBio39404.
PROP63244.
SOURCESearch...

Entry information

Entry nameGBLP_HUMAN
AccessionPrimary (citable) accession number: P63244
Secondary accession number(s): B3KTJ0 expand/collapse secondary AC list , D3DWS0, P25388, P99049, Q53HU2, Q5J8M6, Q5VLR4, Q6FH47
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 106 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM