CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022051
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Translation initiation factor eIF-2B subunit gamma 
Protein Synonyms/Alias
 eIF-2B GDP-GTP exchange factor subunit gamma 
Gene Name
 EIF2B3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
61VTTRDVQKALCAEFKubiquitination[1]
72AEFKMKMKPDIVCIPubiquitination[1]
96SLRYIYPKLKTDVLVubiquitination[1]
134SLAMLMRKGQDSIEPubiquitination[1, 2]
148PVPGQKGKKKAVEQRubiquitination[1]
165IGVDSTGKRLLFMANubiquitination[1, 2, 3, 4]
249SQQGQEEKEEDLKKKubiquitination[2]
259DLKKKELKSLDIYSFubiquitination[1, 5, 6, 7]
349SSAQIVSKHLVGVDSubiquitination[1]
367PETQIGEKSSIKRSVubiquitination[1]
382IGSSCLIKDRVTITNubiquitination[1]
Reference
 [1] 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]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] 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]
 [5] 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]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP. 
Sequence Annotation
 MOD_RES 1 1 N-acetylmethionine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Disease mutation; Initiation factor; Leukodystrophy; Polymorphism; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 452 AA 
Protein Sequence
MEFQAVVMAV GGGSRMTDLT SSIPKPLLPV GNKPLIWYPL NLLERVGFEE VIVVTTRDVQ 60
KALCAEFKMK MKPDIVCIPD DADMGTADSL RYIYPKLKTD VLVLSCDLIT DVALHEVVDL 120
FRAYDASLAM LMRKGQDSIE PVPGQKGKKK AVEQRDFIGV DSTGKRLLFM ANEADLDEEL 180
VIKGSILQKH PRIRFHTGLV DAHLYCLKKY IVDFLMENGS ITSIRSELIP YLVRKQFSSA 240
SSQQGQEEKE EDLKKKELKS LDIYSFIKEA NTLNLAPYDA CWNACRGDRW EDLSRSQVRC 300
YVHIMKEGLC SRVSTLGLYM EANRQVPKLL SALCPEEPPV HSSAQIVSKH LVGVDSLIGP 360
ETQIGEKSSI KRSVIGSSCL IKDRVTITNC LLMNSVTVEE GSNIQGSVIC NNAVIEKGAD 420
IKDCLIGSGQ RIEAKAKRVN EVIVGNDQLM EI 452 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005851; C:eukaryotic translation initiation factor 2B complex; IDA:UniProtKB.
 GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
 GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
 GO:0032057; P:negative regulation of translational initiation in response to stress; ISS:UniProtKB.
 GO:0014003; P:oligodendrocyte development; IMP:UniProtKB.
 GO:0009749; P:response to glucose stimulus; ISS:UniProtKB.
 GO:0009408; P:response to heat; ISS:UniProtKB.
 GO:0043434; P:response to peptide hormone stimulus; ISS:UniProtKB.
 GO:0006413; P:translational initiation; IDA:UniProtKB. 
Interpro
 IPR005835; NTP_transferase. 
Pfam
 PF00483; NTP_transferase 
SMART
  
PROSITE
  
PRINTS