UniProt Accession

 EF1A_YEAST; P02994; D6VQB6; Q7Z7U8; Q7Z8Q8; Q7Z8Q9 

Genbank Protein ID

 X00779; X01638; M10992; M15666; M15667; X78993; Z35987; U51033; AY692927; X73532; AF402004; AY130810; AY130811; AY130812; AY130813; BK006936; BK006949 

Genbank Nucleotide ID

 CAA25356.1; CAA25798.1; AAA34585.1; AAA34584.1; AAA34586.1; CAA55620.1; CAA85075.1; AAB68129.1; AAT92946.1; CAA51936.1; AAP86465.1; AAM83111.1; AAM83112.1; AAM83113.1; AAM83114.1; DAA07236.1; DAA11498.1 

Protein Name

 Elongation factor 1-alpha 

Protein Synonyms/Alias

 EF-1-alpha; Eukaryotic elongation factor 1A; eEF1A; Translation elongation factor 1A 

Gene Name

 TEF1; TEF2 

Gene Synonyms/Alias

 YPR080W; P9513.7; YBR118W; YBR0913 

Created Date

 July 27, 2013 

Organism

 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 

NCBI Taxa ID

 559292 

Lysine Modification

Position	Peptide	Type	References
30	TTGHLIYKCGGIDKR	acetylation	[1]
30	TTGHLIYKCGGIDKR	methylation	[2]
41	IDKRTIEKFEKEAAE	acetylation	[1]
41	IDKRTIEKFEKEAAE	ubiquitination	[3]
44	RTIEKFEKEAAELGK	acetylation	[1]
44	RTIEKFEKEAAELGK	ubiquitination	[3]
51	KEAAELGKGSFKYAW	ubiquitination	[3, 4]
55	ELGKGSFKYAWVLDK	acetylation	[1]
55	ELGKGSFKYAWVLDK	ubiquitination	[3]
62	KYAWVLDKLKAERER	acetylation	[1]
62	KYAWVLDKLKAERER	ubiquitination	[3, 4]
79	TIDIALWKFETPKYQ	methylation	[2, 5, 6]
84	LWKFETPKYQVTVID	ubiquitination	[3]
129	EFEAGISKDGQTREH	ubiquitination	[3]
154	QLIVAVNKMDSVKWD	acetylation	[1]
154	QLIVAVNKMDSVKWD	ubiquitination	[3]
159	VNKMDSVKWDESRFQ	acetylation	[1]
159	VNKMDSVKWDESRFQ	ubiquitination	[3]
170	SRFQEIVKETSNFIK	acetylation	[1]
170	SRFQEIVKETSNFIK	ubiquitination	[3]
177	KETSNFIKKVGYNPK	acetylation	[1]
177	KETSNFIKKVGYNPK	ubiquitination	[3]
178	ETSNFIKKVGYNPKT	acetylation	[1]
178	ETSNFIKKVGYNPKT	ubiquitination	[3]
184	KKVGYNPKTVPFVPI	ubiquitination	[3]
210	TTNAPWYKGWEKETK	ubiquitination	[3]
217	KGWEKETKAGVVKGK	ubiquitination	[3]
224	KAGVVKGKTLLEAID	ubiquitination	[4]
242	QPSRPTDKPLRLPLQ	acetylation	[1]
242	QPSRPTDKPLRLPLQ	ubiquitination	[3, 4]
253	LPLQDVYKIGGIGTV	acetylation	[1]
253	LPLQDVYKIGGIGTV	ubiquitination	[3, 4]
271	RVETGVIKPGMVVTF	acetylation	[1, 7]
271	RVETGVIKPGMVVTF	ubiquitination	[3, 4]
288	AGVTTEVKSVEMHHE	ubiquitination	[4]
311	DNVGFNVKNVSVKEI	ubiquitination	[3]
316	NVKNVSVKEIRRGNV	methylation	[2]
316	NVKNVSVKEIRRGNV	ubiquitination	[3]
328	GNVCGDAKNDPPKGC	acetylation	[1]
328	GNVCGDAKNDPPKGC	ubiquitination	[3, 4]
333	DAKNDPPKGCASFNA	ubiquitination	[3]
376	RFDELLEKNDRRSGK	acetylation	[1]
376	RFDELLEKNDRRSGK	ubiquitination	[3]
390	KKLEDHPKFLKSGDA	acetylation	[1]
390	KKLEDHPKFLKSGDA	methylation	[2]
393	EDHPKFLKSGDAALV	acetylation	[1]
393	EDHPKFLKSGDAALV	ubiquitination	[3, 4]
401	SGDAALVKFVPSKPM	acetylation	[1]
401	SGDAALVKFVPSKPM	ubiquitination	[3]
406	LVKFVPSKPMCVEAF	acetylation	[1]
406	LVKFVPSKPMCVEAF	ubiquitination	[3]
437	TVAVGVIKSVDKTEK	acetylation	[1]
437	TVAVGVIKSVDKTEK	ubiquitination	[3, 4]
454	KVTKAAQKAAKK***	acetylation	[8]
457	KAAQKAAKK******	acetylation	[8]

Reference

 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] A novel post-translational modification of yeast elongation factor 1A. Methylesterification at the C terminus.
 Zobel-Thropp P, Yang MC, Machado L, Clarke S.
 J Biol Chem. 2000 Nov 24;275(47):37150-8. [PMID: 10973948]
 [3] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [4] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
 [5] Characterization of yeast EF-1 alpha: non-conservation of post-translational modifications.
 Cavallius J, Zoll W, Chakraburtty K, Merrick WC.
 Biochim Biophys Acta. 1993 Apr 21;1163(1):75-80. [PMID: 8476932]
 [6] 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]
 [7] Preparative peptide isoelectric focusing as a tool for improving the identification of lysine-acetylated peptides from complex mixtures.
 Xie H, Bandhakavi S, Roe MR, Griffin TJ.
 J Proteome Res. 2007 May;6(5):2019-26. [PMID: 17397211]
 [8] mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases.
 Mitchell L, Huard S, Cotrut M, Pourhanifeh-Lemeri R, Steunou AL, Hamza A, Lambert JP, Zhou H, Ning Z, Basu A, Côté J, Figeys DA, Baetz K.
 Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):E1641-50. [PMID: 23572591] 

Functional Description

 GTP-binding component of the eukaryotic elongation factor 1 complex (eEF1). In its active GTP-bound form, binds to and delivers aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. In the presence of a correct codon-anticodon match between the aminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, the ribosome acts as a GTPase activator and the GTP is hydrolyzed. The inactive GDP-bound form leaves the ribosome and must be recycled by its guanine nucleotide exchange factor (GEF) (eEF1B subcomplex) before binding another molecule of aminoacyl-tRNA. Required for nuclear export of aminoacyl-tRNAs. May also be involved in translational quality control by targeting cotranslationally damaged proteins to the proteasome. Also exhibits actin filament-binding and -bundling activities and is involved in cytoskeleton organization. 

Sequence Annotation

 NP_BIND 14 21 GTP.
 NP_BIND 91 95 GTP.
 NP_BIND 153 156 GTP.
 MOD_RES 1 1 Blocked amino end (Met).
 MOD_RES 18 18 Phosphoserine.
 MOD_RES 30 30 N6-methyllysine; by EFM1 (Probable).
 MOD_RES 72 72 Phosphothreonine.
 MOD_RES 79 79 N6,N6,N6-trimethyllysine.
 MOD_RES 82 82 Phosphothreonine.
 MOD_RES 163 163 Phosphoserine.
 MOD_RES 259 259 Phosphothreonine.
 MOD_RES 289 289 Phosphoserine.
 MOD_RES 316 316 N6,N6-dimethyllysine; by SEE1 (Probable).
 MOD_RES 390 390 N6-methyllysine; by EFM1 (Probable).
 MOD_RES 414 414 Phosphoserine.
 MOD_RES 430 430 Phosphothreonine.
 MOD_RES 458 458 Lysine methyl ester.  

Keyword

 3D-structure; Actin-binding; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Elongation factor; GTP-binding; Methylation; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 458 AA 

Protein Sequence

Gene Ontology

 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005853; C:eukaryotic translation elongation factor 1 complex; ISS:SGD.
 GO:0005739; C:mitochondrion; IPI:SGD.
 GO:0005840; C:ribosome; TAS:SGD.
 GO:0019003; F:GDP binding; IDA:SGD.
 GO:0005525; F:GTP binding; IDA:SGD.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0003746; F:translation elongation factor activity; IMP:SGD.
 GO:0006184; P:GTP catabolic process; IEA:GOC.
 GO:0006409; P:tRNA export from nucleus; IMP:SGD. 

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.