CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005310
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation factor 1-beta 
Protein Synonyms/Alias
 EF-1-beta 
Gene Name
 EEF1B2 
Gene Synonyms/Alias
 EEF1B; EF1B 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
7*MGFGDLKSPAGLQVacetylation[1]
7*MGFGDLKSPAGLQVubiquitination[2, 3, 4]
60LRWYNHIKSYEKEKAacetylation[1]
60LRWYNHIKSYEKEKAubiquitination[2, 4, 5]
78GVKKALGKYGPADVEubiquitination[2, 3, 4, 6, 7]
129RLAQYESKKAKKPALacetylation[8]
133YESKKAKKPALVAKSubiquitination[5]
147SSILLDVKPWDDETDacetylation[9]
147SSILLDVKPWDDETDubiquitination[4, 5, 6, 10, 11]
176GLVWGSSKLVPVGYGacetylation[9]
176GLVWGSSKLVPVGYGubiquitination[2, 3, 4, 5, 6, 7, 8, 11]
185VPVGYGIKKLQIQCVacetylation[1, 8, 12]
185VPVGYGIKKLQIQCVubiquitination[2, 4]
186PVGYGIKKLQIQCVVubiquitination[3, 5]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [9] 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]
 [10] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [11] 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]
 [12] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773
Functional Description
 EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP. 
Sequence Annotation
 DOMAIN 2 84 GST C-terminal.
 MOD_RES 7 7 N6-acetyllysine.
 MOD_RES 8 8 Phosphoserine.
 MOD_RES 93 93 Phosphothreonine.
 MOD_RES 95 95 Phosphoserine.
 MOD_RES 106 106 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Elongation factor; Phosphoprotein; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 225 AA 
Protein Sequence
MGFGDLKSPA GLQVLNDYLA DKSYIEGYVP SQADVAVFEA VSSPPPADLC HALRWYNHIK 60
SYEKEKASLP GVKKALGKYG PADVEDTTGS GATDSKDDDD IDLFGSDDEE ESEEAKRLRE 120
ERLAQYESKK AKKPALVAKS SILLDVKPWD DETDMAKLEE CVRSIQADGL VWGSSKLVPV 180
GYGIKKLQIQ CVVEDDKVGT DMLEEQITAF EDYVQSMDVA AFNKI 225 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005853; C:eukaryotic translation elongation factor 1 complex; NAS:UniProtKB.
 GO:0003746; F:translation elongation factor activity; NAS:UniProtKB. 
Interpro
 IPR018940; EF-1_beta_acid_region_euk.
 IPR010987; Glutathione-S-Trfase_C-like.
 IPR014717; Transl_elong_EF1B/ribosomal_S6.
 IPR001326; Transl_elong_EF1B_B/D_CS.
 IPR014038; Transl_elong_fac_EF1B_bsu/dsu. 
Pfam
 PF10587; EF-1_beta_acid
 PF00736; EF1_GNE 
SMART
 SM00888; EF1_GNE 
PROSITE
 PS00824; EF1BD_1
 PS00825; EF1BD_2
 PS50405; GST_CTER 
PRINTS