CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009840
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Guanine nucleotide-binding protein subunit beta-2-like 1 
Protein Synonyms/Alias
 12-3; Receptor for activated C kinase; Receptor of activated protein kinase C 1; RACK1; p205 
Gene Name
 Gnb2l1 
Gene Synonyms/Alias
 Gnb2-rs1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
12MTLRGTLKGHNGWVTubiquitination[1]
106RRFVGHTKDVLSVAFubiquitination[1]
130GSRDKTIKLWNTLGVacetylation[2, 3, 4, 5, 6, 7]
130GSRDKTIKLWNTLGVubiquitination[1]
172IVSCGWDKLVKVWNLubiquitination[1]
175CGWDKLVKVWNLANCacetylation[3, 6]
175CGWDKLVKVWNLANCsuccinylation[6]
175CGWDKLVKVWNLANCubiquitination[1]
183VWNLANCKLKTNHIGacetylation[3, 4, 5, 6, 7]
183VWNLANCKLKTNHIGsuccinylation[6]
183VWNLANCKLKTNHIGubiquitination[1]
257AATGPSIKIWDLEGKubiquitination[1]
271KIIVDELKQEVISTSacetylation[3, 4, 6]
271KIIVDELKQEVISTSubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [4] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [6] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [7] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654
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. 
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 (By similarity).
 MOD_RES 130 130 N6-acetyllysine (By similarity).
 MOD_RES 228 228 Phosphotyrosine (By similarity).  
Keyword
 Acetylation; Apoptosis; Biological rhythms; Cell cycle; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein; Direct protein sequencing; Gastrulation; Growth regulation; Membrane; Nucleus; Phosphoprotein; Reference proteome; Repeat; Translation regulation; WD repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 317 AA 
Protein Sequence
MTEQMTLRGT LKGHNGWVTQ IATTPQFPDM ILSASRDKTI IMWKLTRDET NYGIPQRALR 60
GHSHFVSDVV ISSDGQFALS GSWDGTLRLW DLTTGTTTRR FVGHTKDVLS VAFSSDNRQI 120
VSGSRDKTIK LWNTLGVCKY TVQDESHSEW VSCVRFSPNS SNPIIVSCGW DKLVKVWNLA 180
NCKLKTNHIG HTGYLNTVTV SPDGSLCASG GKDGQAMLWD LNEGKHLYTL DGGDIINALC 240
FSPNRYWLCA ATGPSIKIWD LEGKIIVDEL KQEVISTSSK AEPPQCTSLA WSADGQTLFA 300
GYTDNLVRVW QVTIGTR 317 
Gene Ontology
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0030425; C:dendrite; IDA:UniProtKB.
 GO:0030496; C:midbody; ISS:UniProtKB.
 GO:0043025; C:neuronal cell body; IDA:MGI.
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
 GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
 GO:0001891; C:phagocytic cup; ISS:UniProtKB.
 GO:0015935; C:small ribosomal subunit; IEA:Compara.
 GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IEA:Compara.
 GO:0008200; F:ion channel inhibitor activity; IDA:UniProtKB.
 GO:0005080; F:protein kinase C binding; ISS:UniProtKB.
 GO:0030292; F:protein tyrosine kinase inhibitor activity; ISS:UniProtKB.
 GO:0004872; F:receptor activity; ISA:MGI.
 GO:0030971; F:receptor tyrosine kinase binding; ISS:UniProtKB.
 GO:0042169; F:SH2 domain binding; ISS:UniProtKB.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0007369; P:gastrulation; IEA:UniProtKB-KW.
 GO:0035556; P:intracellular signal transduction; ISA:MGI.
 GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
 GO:0050765; P:negative regulation of phagocytosis; ISS:UniProtKB.
 GO:0051898; P:negative regulation of protein kinase B signaling cascade; IEA:Compara.
 GO:0017148; P:negative regulation of translation; IEA:Compara.
 GO:0030178; P:negative regulation of Wnt receptor signaling pathway; ISS:UniProtKB.
 GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
 GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
 GO:2000543; P:positive regulation of gastrulation; ISS:UniProtKB.
 GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
 GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IEA:Compara.
 GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
 GO:0032464; P:positive regulation of protein homooligomerization; ISS:UniProtKB.
 GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
 GO:0008104; P:protein localization; ISA:MGI.
 GO:0051726; P:regulation of cell cycle; ISS: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. 
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.