P63244 (GBLP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	GNB2L1
ORF Names:	HLC7, PIG21

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	317 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.30 Ref.32 Ref.34 Ref.35 Ref.36 Ref.38 Ref.39 Ref.40
Subunit structure	Component of the small (40S) ribosomal subunit By similarity. 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 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.30 Ref.31 Ref.32 Ref.34 Ref.35 Ref.36 Ref.38 Ref.39 Ref.40 Ref.42
Subcellular location	Cell membrane; Peripheral membrane protein. Cytoplasm. Cytoplasm › perinuclear region. Cytoplasm › cytoskeleton. Nucleus. Perikaryon By similarity. Cell projection › dendrite By similarity. Cell projection › phagocytic 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.30 Ref.36 Ref.38 Ref.40
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.32
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 process	Apoptosis Biological rhythms Cell cycle Gastrulation Growth regulation Host-virus interaction Translation regulation
Cellular component	Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane Nucleus
Domain	Repeat WD repeat
Molecular function	Developmental protein
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW gastrulation Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of Wnt receptor 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.40. Source: UniProtKB negative regulation of protein kinase B signaling cascade Inferred from mutant phenotype PubMed 19767770. Source: UniProtKB negative regulation of translation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of GTPase activity Inferred from direct assay Ref.38. Source: UniProtKB positive regulation of apoptotic process Inferred from direct assay Ref.34. Source: UniProtKB positive regulation of cell migration Inferred from direct assay Ref.38. Source: UniProtKB 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 proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.30. Source: UniProtKB positive regulation of protein homooligomerization Inferred from direct assay Ref.34. 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: Compara regulation of protein localization Inferred from sequence or structural similarity. Source: UniProtKB rhythmic process Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell dendrite Inferred from sequence or structural similarity. Source: UniProtKB midbody Inferred from direct assay PubMed 15166316. 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.40. Source: UniProtKB small ribosomal subunit Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	SH2 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 ion channel inhibitor activity Inferred from sequence or structural similarity. Source: UniProtKB protein kinase C binding Inferred from direct assay Ref.13. Source: UniProtKB protein tyrosine kinase inhibitor activity Inferred from direct assay Ref.11. Source: UniProtKB receptor tyrosine kinase binding Inferred from direct assay Ref.11. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACHE	P22303	2	EBI-296739,EBI-1637793
BCL2L11	O43521	2	EBI-296739,EBI-526406
Bcl2l11	O54918-1	2	EBI-296739,EBI-526076	From a different organism.
DYNLL1	P63167	6	EBI-296739,EBI-349105
IFNAR2	P48551	4	EBI-296739,EBI-958408
LRP12	Q9Y561	2	EBI-296739,EBI-296693
PPID	Q08752	4	EBI-296739,EBI-716596
VHL	P40337	9	EBI-296739,EBI-301246

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.9

Chain

2 – 317

316

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

PRO_0000127731

Regions

Repeat

13 – 44

32

WD 1

Repeat

61 – 91

31

WD 2

Repeat

103 – 133

31

WD 3

Repeat

146 – 178

33

WD 4

Repeat

190 – 220

31

WD 5

Repeat

231 – 260

30

WD 6

Repeat

281 – 311

31

WD 7

Amino acid modifications

Modified residue

2

1

N-acetylthreonine Ref.9 Ref.41

Modified residue

52

1

Phosphotyrosine; by ABL1 Probable

Modified residue

130

1

N6-acetyllysine Ref.33

Modified residue

228

1

Phosphotyrosine Ref.13

Experimental info

Mutagenesis

52

1

Y → F: No effect on binding to SRC. Abolishes binding to PTK2/FAK1 and reduces cell adhesion and foci formation. Ref.13 Ref.17 Ref.32

Mutagenesis

57

1

R → A: Decreased binding to PTK2/FAK1; when associated with A-60. Ref.32

Mutagenesis

60

1

R → A: Decreased binding to PTK2/FAK1; when associated with A-57. Ref.32

Mutagenesis

127

1

K → A: Decreased binding to PTK2/FAK1; when associated with A-130. Ref.32

Mutagenesis

130

1

K → A: Decreased binding to PTK2/FAK1; when associated with A-127. Ref.32

Mutagenesis

140

1

Y → F: No effect on binding to SRC. Ref.13 Ref.17

Mutagenesis

194

1

Y → F: No effect on binding to SRC. Ref.13 Ref.17

Mutagenesis

228

1

Y → 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

Mutagenesis

246

1

Y → 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

Mutagenesis

302

1

Y → F: No effect on binding to SRC. Abolishes phosphorylation by SRC; when associated with F-228 and F-246. Ref.13 Ref.17

Sequence conflict

70 – 111

42

Missing in BAG53102. Ref.4

Sequence conflict

94

1

T → TRK in AAR24619. Ref.3

Sequence conflict

221

1

L → F in BAD96208. Ref.6

Secondary structure

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317

Helix Strand Turn

Details...

Beta strand

4 – 11

8

Beta strand

18 – 23

6

Beta strand

30 – 35

6

Beta strand

40 – 45

6

Beta strand

48 – 50

3

Beta strand

52 – 59

8

Beta strand

66 – 71

6

Beta strand

75 – 82

8

Beta strand

85 – 91

7

Turn

92 – 95

4

Beta strand

96 – 102

7

Beta strand

108 – 113

6

Beta strand

120 – 124

5

Beta strand

129 – 132

4

Beta strand

138 – 142

5

Beta strand

144 – 146

3

Beta strand

151 – 156

6

Beta strand

160 – 162

3

Beta strand

164 – 169

6

Beta strand

174 – 178

5

Turn

179 – 182

4

Beta strand

183 – 188

6

Beta strand

195 – 200

6

Beta strand

204 – 211

8

Beta strand

215 – 220

6

Turn

221 – 224

4

Beta strand

225 – 231

7

Beta strand

236 – 241

6

Beta strand

243 – 252

10

Beta strand

255 – 260

6

Turn

261 – 264

4

Beta strand

265 – 270

6

Beta strand

286 – 291

6

Beta strand

295 – 302

8

Beta strand

307 – 313

7

Sequences

	Sequence		Length	Mass (Da)
	P63244 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 257F91E369ED2044	FASTA	317	35,077
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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, 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]	"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.
[31]	"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.
[32]	"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.
[33]	"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, MASS SPECTROMETRY.
[34]	"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.
[35]	"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.
[36]	"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.
[37]	"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].
[38]	"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.
[39]	"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.
[40]	"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.
[41]	"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, MASS SPECTROMETRY.
[42]	"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.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00848226.

PIR

B33928.

RefSeq

NP_006089.1. NM_006098.4.

UniGene

Hs.5662.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4AOW	X-ray	2.45	A/B/C	1-317	[»]

ProteinModelPortal

P63244.

ModBase

Search...

Protein-protein interaction databases

IntAct

P63244. 53 interactions.

MINT

MINT-105673.

STRING

9606.ENSP00000366013.

PTM databases

PhosphoSite

P63244.

Polymorphism databases

DMDM

54037168.

2D gel databases

REPRODUCTION-2DPAGE

IPI00848226.
P63244.

Proteomic databases

PaxDb

P63244.

PRIDE

P63244.

Protocols and materials databases

DNASU

10399.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000512805; ENSP00000426909; ENSG00000204628.

GeneID

10399.

KEGG

hsa:10399.

UCSC

uc003mni.1. human.

Organism-specific databases

CTD

10399.

GeneCards

GC05M180663.

HGNC

HGNC:4399. GNB2L1.

HPA

CAB004288.
HPA021676.

MIM

176981. gene.

neXtProt

NX_P63244.

PharmGKB

PA28779.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2319.

HOVERGEN

HBG000277.

InParanoid

P63244.

KO

K14753.

OMA

IRVWQVM.

Enzyme and pathway databases

Pathway_Interaction_DB

hif1apathway. Hypoxic and oxygen homeostasis regulation of HIF-1-alpha.
igf1_pathway. IGF1 pathway.
ar_tf_pathway. Regulation of Androgen receptor activity.
syndecan_2_pathway. Syndecan-2-mediated signaling events.
tnfpathway. TNF receptor signaling pathway.

Gene expression databases

ArrayExpress

P63244.

Bgee

P63244.

CleanEx

HS_GNB2L1.

Genevestigator

P63244.

GermOnline

ENSG00000204628. Homo sapiens.

Family and domain databases

Gene3D

2.130.10.10. 2 hits.

InterPro

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]

Pfam

PF00400. WD40. 7 hits.
[Graphical view]

PRINTS

PR00320. GPROTEINBRPT.

SMART

SM00320. WD40. 7 hits.
[Graphical view]

SUPFAM

SSF50978. WD40_like. 1 hit.

PROSITE

PS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

GNB2L1. human.

GenomeRNAi

10399.

NextBio

39404.

SOURCE

Search...

Entry information

Entry name

GBLP_HUMAN

Accession

Primary (citable) accession number: P63244
Secondary accession number(s): B3KTJ0 , 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:	May 1, 2013
This is version 95 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.