UniProt Accession

 EF1A1_HUMAN; P68104; P04719; P04720 

Genbank Protein ID

 X03558; J04617; X16869; AY043301; BC008587; BC009733; BC009875; BC010735; BC012891; BC014224; BC018150; BC018641; BC021686; BC028674; BC038339; BC057391; BC066893; BC072385; BC082268; X03689; M29548 

Genbank Nucleotide ID

 CAA27245.1; AAA52343.1; CAA34756.1; AAK95378.1; AAH08587.1; AAH09733.1; AAH09875.1; AAH10735.1; AAH12891.1; AAH14224.1; AAH18150.1; AAH18641.1; AAH21686.1; AAH28674.1; AAH38339.1; AAH57391.1; AAH66893.1; AAH72385.1; AAH82268.1; CAA27325.1; AAA52367.1 

Protein Name

 Elongation factor 1-alpha 1 

Protein Synonyms/Alias

 EF-1-alpha-1; Elongation factor Tu; EF-Tu; Eukaryotic elongation factor 1 A-1; eEF1A-1; Leukocyte receptor cluster member 7 

Gene Name

 EEF1A1 

Gene Synonyms/Alias

 EEF1A; EF1A; LENG7 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
30	TTGHLIYKCGGIDKR	ubiquitination	[1, 2, 3]
36	YKCGGIDKRTIEKFE	methylation	[4]
41	IDKRTIEKFEKEAAE	acetylation	[5]
41	IDKRTIEKFEKEAAE	ubiquitination	[3, 6]
44	RTIEKFEKEAAEMGK	acetylation	[5]
44	RTIEKFEKEAAEMGK	ubiquitination	[1, 2, 3, 6, 7, 8]
55	EMGKGSFKYAWVLDK	acetylation	[5]
55	EMGKGSFKYAWVLDK	methylation	[4, 9]
55	EMGKGSFKYAWVLDK	ubiquitination	[7, 8]
62	KYAWVLDKLKAERER	ubiquitination	[1, 3]
64	AWVLDKLKAERERGI	ubiquitination	[3]
79	TIDISLWKFETSKYY	acetylation	[10]
79	TIDISLWKFETSKYY	methylation	[4]
84	LWKFETSKYYVTIID	ubiquitination	[3, 6, 7, 8]
129	EFEAGISKNGQTREH	ubiquitination	[11]
146	LAYTLGVKQLIVGVN	acetylation	[5, 12, 13, 14, 15]
146	LAYTLGVKQLIVGVN	ubiquitination	[1, 2, 3, 6, 7, 8, 11, 15, 16]
154	QLIVGVNKMDSTEPP	ubiquitination	[1, 2, 3, 6, 7, 8, 11, 15]
165	TEPPYSQKRYEEIVK	methylation	[4, 17, 18, 19]
165	TEPPYSQKRYEEIVK	ubiquitination	[1, 2, 3, 7, 8, 11, 15]
172	KRYEEIVKEVSTYIK	acetylation	[5, 10, 13, 14, 15]
172	KRYEEIVKEVSTYIK	ubiquitination	[1, 2, 3, 6, 7, 8, 11, 15, 16, 20, 21, 22]
179	KEVSTYIKKIGYNPD	acetylation	[5, 13, 15]
179	KEVSTYIKKIGYNPD	ubiquitination	[2, 3, 7, 8, 11, 15, 16, 21]
180	EVSTYIKKIGYNPDT	ubiquitination	[3, 7, 8, 11, 15]
212	SANMPWFKGWKVTRK	ubiquitination	[2, 8, 11, 15]
215	MPWFKGWKVTRKDGN	ubiquitination	[3, 11]
219	KGWKVTRKDGNASGT	ubiquitination	[6, 7, 11]
244	PPTRPTDKPLRLPLQ	ubiquitination	[3, 11, 15, 20, 22]
255	LPLQDVYKIGGIGTV	acetylation	[5, 13, 14, 15]
255	LPLQDVYKIGGIGTV	ubiquitination	[1, 3, 6, 7, 8, 11, 15, 16, 20, 21, 22, 23]
273	RVETGVLKPGMVVTF	acetylation	[14, 15, 24]
273	RVETGVLKPGMVVTF	ubiquitination	[1, 2, 3, 6, 7, 8, 11, 15, 16, 20]
318	NVKNVSVKDVRRGNV	acetylation	[5, 15, 25]
318	NVKNVSVKDVRRGNV	methylation	[4, 17, 19]
318	NVKNVSVKDVRRGNV	ubiquitination	[2, 3, 7, 8, 11, 15]
330	GNVAGDSKNDPPMEA	phosphoglycerylation	[26]
385	KIDRRSGKKLEDGPK	ubiquitination	[2, 7]
386	IDRRSGKKLEDGPKF	acetylation	[5, 15]
386	IDRRSGKKLEDGPKF	ubiquitination	[7, 8]
392	KKLEDGPKFLKSGDA	acetylation	[5, 13, 14, 15]
392	KKLEDGPKFLKSGDA	ubiquitination	[2, 3, 6, 7, 8, 11, 15, 16, 21, 22]
395	EDGPKFLKSGDAAIV	acetylation	[5, 13]
395	EDGPKFLKSGDAAIV	ubiquitination	[2, 3, 6, 8, 11, 15, 16]
408	IVDMVPGKPMCVESF	ubiquitination	[2, 3, 7, 8, 11, 15]
439	TVAVGVIKAVDKKAA	acetylation	[5, 12, 13, 14, 15]
439	TVAVGVIKAVDKKAA	ubiquitination	[3, 6, 7, 8, 15, 16, 21, 22]
443	GVIKAVDKKAAGAGK	acetylation	[12]
444	VIKAVDKKAAGAGKV	acetylation	[12]
444	VIKAVDKKAAGAGKV	ubiquitination	[7]
450	KKAAGAGKVTKSAQK	ubiquitination	[2, 7]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [4] Update on activities at the Universal Protein Resource (UniProt) in 2013.
 e="String">UniProt Consortium.
 Nucleic Acids Res. 2013 Jan;41(Database issue):D43-7. [PMID: 23161681]
 [5] 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]
 [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] 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]
 [8] 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]
 [9] Post-translational modifications in the rat lumbar spinal cord in experimental autoimmune encephalomyelitis.
 Grant JE, Hu J, Liu T, Jain MR, Elkabes S, Li H.
 J Proteome Res. 2007 Jul;6(7):2786-91. [PMID: 17567059]
 [10] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [11] 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]
 [12] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [13] 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]
 [14] 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]
 [15] 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]
 [16] 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]
 [17] A general molecular affinity strategy for global detection and proteomic analysis of lysine methylation.
 Moore KE, Carlson SM, Camp ND, Cheung P, James RG, Chua KF, Wolf-Yadlin A, Gozani O.
 Mol Cell. 2013 May 9;50(3):444-56. [PMID: 23583077]
 [18] 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]
 [19] 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]
 [20] 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]
 [21] 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]
 [22] 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]
 [23] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [24] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [25] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [26] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237] 

Functional Description

 This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. With PARP1 and TXK, forms a complex that acts as a T helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production. 

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 36 36 N6,N6,N6-trimethyllysine (By similarity).
 MOD_RES 55 55 N6,N6,N6-trimethyllysine; alternate (By
 MOD_RES 55 55 N6,N6-dimethyllysine; alternate.
 MOD_RES 79 79 N6,N6,N6-trimethyllysine (By similarity).
 MOD_RES 141 141 Phosphotyrosine (By similarity).
 MOD_RES 165 165 N6,N6,N6-trimethyllysine; alternate (By
 MOD_RES 165 165 N6,N6-dimethyllysine; alternate.
 MOD_RES 179 179 N6-acetyllysine (By similarity).
 MOD_RES 300 300 Phosphoserine; by TGFBR1.
 MOD_RES 301 301 5-glutamyl
 MOD_RES 318 318 N6,N6,N6-trimethyllysine (By similarity).
 MOD_RES 374 374 5-glutamyl
 MOD_RES 432 432 Phosphothreonine; by PASK.
 MOD_RES 439 439 N6-acetyllysine (By similarity).  

Keyword

 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein; Protein biosynthesis; Reference proteome; Transcription; Transcription regulation; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 462 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005853; C:eukaryotic translation elongation factor 1 complex; TAS:UniProtKB.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005525; F:GTP binding; TAS:UniProtKB.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0003746; F:translation elongation factor activity; TAS:UniProtKB.
 GO:0006184; P:GTP catabolic process; IEA:GOC.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 

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.