UniProt Accession

 GBLP_HUMAN; P63244; B3KTJ0; D3DWS0; P25388; P99049; Q53HU2; Q5J8M6; Q5VLR4; Q6FH47 

Genbank Protein ID

 M24194; AY159316; AY336089; AK095666; CR456978; CR541909; AK222488; CH471165; CH471165; BC000214; BC000366; BC010119; BC014256; BC014788; BC017287; BC019093; BC019362; BC021993; BC032006 

Genbank Nucleotide ID

 AAA59626.1; AAO21313.1; AAR24619.1; BAG53102.1; CAG33259.1; CAG46707.1; BAD96208.1; EAW53692.1; EAW53702.1; AAH00214.1; AAH00366.1; AAH10119.1; AAH14256.1; AAH14788.1; AAH17287.1; AAH19093.1; AAH19362.1; AAH21993.1; AAH32006.1 

Protein Name

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

Protein Synonyms/Alias

 Cell proliferation-inducing gene 21 protein; Guanine nucleotide-binding protein subunit beta-like protein 12.3; Human lung cancer oncogene 7 protein; HLC-7; Receptor for activated C kinase; Receptor of activated protein kinase C 1; RACK1 

Gene Name

 GNB2L1 

Gene Synonyms/Alias

 HLC7; PIG21 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
12	MTLRGTLKGHNGWVT	ubiquitination	[1, 2, 3, 4, 5]
38	ILSASRDKTIIMWKL	ubiquitination	[1, 3, 4, 5]
44	DKTIIMWKLTRDETN	ubiquitination	[1, 3, 4, 5]
106	RRFVGHTKDVLSVAF	ubiquitination	[1, 3, 4, 5]
130	GSRDKTIKLWNTLGV	acetylation	[6]
130	GSRDKTIKLWNTLGV	ubiquitination	[1, 3, 4, 7]
139	WNTLGVCKYTVQDES	ubiquitination	[1, 3, 4]
172	IVSCGWDKLVKVWNL	ubiquitination	[1, 3, 4, 7]
175	CGWDKLVKVWNLANC	ubiquitination	[1, 2, 4, 7]
183	VWNLANCKLKTNHIG	ubiquitination	[1, 3, 4]
185	NLANCKLKTNHIGHT	ubiquitination	[3, 4, 7]
212	SLCASGGKDGQAMLW	ubiquitination	[4]
225	LWDLNEGKHLYTLDG	ubiquitination	[2]
257	AATGPSIKIWDLEGK	ubiquitination	[1, 3, 4, 7]
264	KIWDLEGKIIVDELK	ubiquitination	[4, 5]
271	KIIVDELKQEVISTS	sumoylation	[8]
271	KIIVDELKQEVISTS	ubiquitination	[1, 2, 3, 4, 5, 7]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [3] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [7] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [8] Targeted identification of SUMOylation sites in human proteins using affinity enrichment and paralog-specific reporter ions.
 Lamoliatte F, Bonneil E, Durette C, Caron-Lizotte O, Wildemann D, Zerweck J, Wenschuh H, Thibault P.
 Mol Cell Proteomics. 2013 Jun 7;. [PMID: 23750026] 

Functional Description

 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. 

Sequence Annotation

 REPEAT 13 44 WD 1.
 REPEAT 61 91 WD 2.
 REPEAT 103 133 WD 3.
 REPEAT 146 178 WD 4.
 REPEAT 190 220 WD 5.
 REPEAT 231 260 WD 6.
 REPEAT 281 311 WD 7.
 MOD_RES 2 2 N-acetylthreonine.
 MOD_RES 52 52 Phosphotyrosine; by ABL1 (Probable).
 MOD_RES 130 130 N6-acetyllysine.
 MOD_RES 228 228 Phosphotyrosine.  

Keyword

 3D-structure; Acetylation; Apoptosis; Biological rhythms; Cell cycle; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein; Direct protein sequencing; Gastrulation; Growth regulation; Host-virus interaction; Membrane; Nucleus; Phosphoprotein; Reference proteome; Repeat; Translation regulation; WD repeat. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 317 AA 

Protein Sequence

Gene Ontology

 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0030425; C:dendrite; ISS:UniProtKB.
 GO:0030496; C:midbody; IDA:UniProtKB.
 GO:0043025; C:neuronal cell body; ISS:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0001891; C:phagocytic cup; IDA:UniProtKB.
 GO:0015935; C:small ribosomal subunit; ISS:UniProtKB.
 GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IMP:UniProtKB.
 GO:0008200; F:ion channel inhibitor activity; ISS:UniProtKB.
 GO:0005080; F:protein kinase C binding; IDA:UniProtKB.
 GO:0030292; F:protein tyrosine kinase inhibitor activity; IDA:UniProtKB.
 GO:0030971; F:receptor tyrosine kinase binding; IDA:UniProtKB.
 GO:0042169; F:SH2 domain binding; IDA:UniProtKB.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0007369; P:gastrulation; IEA:UniProtKB-KW.
 GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
 GO:0050765; P:negative regulation of phagocytosis; IMP:UniProtKB.
 GO:0051898; P:negative regulation of protein kinase B signaling cascade; IMP:UniProtKB.
 GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
 GO:0030178; P:negative regulation of Wnt receptor signaling pathway; ISS:UniProtKB.
 GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
 GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
 GO:2000543; P:positive regulation of gastrulation; ISS:UniProtKB.
 GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
 GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
 GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
 GO:0032464; P:positive regulation of protein homooligomerization; IDA:UniProtKB.
 GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
 GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
 GO:0051302; P:regulation of cell division; ISS:UniProtKB.
 GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB.
 GO:0090003; P:regulation of establishment of protein localization to plasma membrane; IEA:Compara.
 GO:0032880; P:regulation of protein localization; ISS:UniProtKB.
 GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 

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. 

Pfam

 PF00400; WD40 

SMART

 SM00320; WD40 

PROSITE

 PS00678; WD_REPEATS_1
 PS50082; WD_REPEATS_2
 PS50294; WD_REPEATS_REGION 

PRINTS

 PR00320; GPROTEINBRPT.