CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011304
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation factor 1-alpha 2 
Protein Synonyms/Alias
 EF-1-alpha-2; Eukaryotic elongation factor 1 A-2; eEF1A-2; Statin-S1 
Gene Name
 EEF1A2 
Gene Synonyms/Alias
 EEF1AL; STN 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
41IDKRTIEKFEKEAAEubiquitination[1, 2, 3]
44RTIEKFEKEAAEMGKubiquitination[1, 3, 4]
55EMGKGSFKYAWVLDKubiquitination[4]
62KYAWVLDKLKAERERubiquitination[2]
79TIDISLWKFETTKYYmethylation[5, 6]
84LWKFETTKYYITIIDmethylation[5, 6]
146LAYTLGVKQLIVGVNubiquitination[2, 3, 4]
154QLIVGVNKMDSTEPAubiquitination[4]
165TEPAYSEKRYDEIVKmethylation[5, 6]
165TEPAYSEKRYDEIVKubiquitination[4]
172KRYDEIVKEVSAYIKubiquitination[2, 3, 7]
179KEVSAYIKKIGYNPAacetylation[8, 9]
255LPLQDVYKIGGIGTVubiquitination[1, 2, 3, 4]
318NVKNVSVKDIRRGNVacetylation[9]
318NVKNVSVKDIRRGNVmethylation[6]
439TVAVGVIKNVEKKSGacetylation[8, 9, 10]
Reference
 [1] 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]
 [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] 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]
 [5] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510]
 [6] Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome.
 Bremang M, Cuomo A, Agresta AM, Stugiewicz M, Spadotto V, Bonaldi T.
 Mol Biosyst. 2013 Jul 30;9(9):2231-47. [PMID: 23748837]
 [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]
 [8] 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]
 [9] 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]
 [10] 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] 
Functional Description
 This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. 
Sequence Annotation
 NP_BIND 14 21 GTP (By similarity).
 NP_BIND 91 95 GTP (By similarity).
 NP_BIND 153 156 GTP (By similarity).
 MOD_RES 29 29 Phosphotyrosine (By similarity).
 MOD_RES 55 55 N6,N6,N6-trimethyllysine (By similarity).
 MOD_RES 141 141 Phosphotyrosine (By similarity).
 MOD_RES 165 165 N6,N6,N6-trimethyllysine (By similarity).
 MOD_RES 179 179 N6-acetyllysine.
 MOD_RES 301 301 5-glutamyl glycerylphosphorylethanolamine
 MOD_RES 374 374 5-glutamyl glycerylphosphorylethanolamine
 MOD_RES 439 439 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Elongation factor; GTP-binding; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 463 AA 
Protein Sequence
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL 60
DKLKAERERG ITIDISLWKF ETTKYYITII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV 120
GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP AYSEKRYDEI VKEVSAYIKK 180
IGYNPATVPF VPISGWHGDN MLEPSPNMPW FKGWKVERKE GNASGVSLLE ALDTILPPTR 240
PTDKPLRLPL QDVYKIGGIG TVPVGRVETG ILRPGMVVTF APVNITTEVK SVEMHHEALS 300
EALPGDNVGF NVKNVSVKDI RRGNVCGDSK SDPPQEAAQF TSQVIILNHP GQISAGYSPV 360
IDCHTAHIAC KFAELKEKID RRSGKKLEDN PKSLKSGDAA IVEMVPGKPM CVESFSQYPP 420
LGRFAVRDMR QTVAVGVIKN VEKKSGGAGK VTKSAQKAQK AGK 463 
Gene Ontology
 GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:Compara.
 GO:0043025; C:neuronal cell body; IEA:Compara.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
 GO:0008135; F:translation factor activity, nucleic acid binding; NAS:ProtInc.
 GO:0006184; P:GTP catabolic process; IEA:GOC.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:0010035; P:response to inorganic substance; IEA:Compara. 
Interpro
 IPR000795; EF_GTP-bd_dom.
 IPR027417; P-loop_NTPase.
 IPR009001; Transl_elong_EF1A/Init_IF2_C.
 IPR004539; Transl_elong_EF1A_euk/arc.
 IPR004161; Transl_elong_EFTu/EF1A_2.
 IPR004160; Transl_elong_EFTu/EF1A_C.
 IPR009000; Transl_elong_init/rib_B-barrel. 
Pfam
 PF00009; GTP_EFTU
 PF03144; GTP_EFTU_D2
 PF03143; GTP_EFTU_D3 
SMART
  
PROSITE
 PS00301; EFACTOR_GTP 
PRINTS
 PR00315; ELONGATNFCT.