CPLM-003771

Genbank Nucleotide ID

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

Mus musculus (Mouse)

Position	Peptide	Type	References
30	TTGHLIYKCGGIDKR	ubiquitination	[1]
41	IDKRTIEKFEKEAAE	acetylation	[2]
41	IDKRTIEKFEKEAAE	ubiquitination	[1]
44	RTIEKFEKEAAEMGK	ubiquitination	[1]
79	TIDISLWKFETSKYY	acetylation	[3]
146	LAYTLGVKQLIVGVN	ubiquitination	[1]
154	QLIVGVNKMDSTEPP	ubiquitination	[1]
165	TEPPYSQKRYEEIVK	ubiquitination	[1]
172	KRYEEIVKEVSTYIK	acetylation	[2]
172	KRYEEIVKEVSTYIK	ubiquitination	[1]
179	KEVSTYIKKIGYNPD	acetylation	[2]
180	EVSTYIKKIGYNPDT	ubiquitination	[1]
219	KGWKVTRKDGSASGT	ubiquitination	[1]
244	PPTRPTDKPLRLPLQ	acetylation	[2]
255	LPLQDVYKIGGIGTV	acetylation	[4, 5, 6, 7]
255	LPLQDVYKIGGIGTV	succinylation	[7]
255	LPLQDVYKIGGIGTV	ubiquitination	[1]
273	RVETGVLKPGMVVTF	acetylation	[4, 5, 6, 7]
273	RVETGVLKPGMVVTF	ubiquitination	[1]
386	IDRRSGKKLEDGPKF	acetylation	[5]
392	KKLEDGPKFLKSGDA	acetylation	[2, 4, 5, 6, 7, 8, 9]
392	KKLEDGPKFLKSGDA	succinylation	[7]
392	KKLEDGPKFLKSGDA	succinylation	[7]
392	KKLEDGPKFLKSGDA	ubiquitination	[1]
395	EDGPKFLKSGDAAIV	acetylation	[5]
395	EDGPKFLKSGDAAIV	ubiquitination	[1]
408	IVDMVPGKPMCVESF	acetylation	[5, 6]
408	IVDMVPGKPMCVESF	ubiquitination	[1]
439	TVAVGVIKAVDKKAA	acetylation	[2, 4, 5, 7, 9]
439	TVAVGVIKAVDKKAA	ubiquitination	[1]
443	GVIKAVDKKAAGAGK	acetylation	[5]

[1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
[2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
[3] Large-scale identification of proteins expressed in mouse embryonic stem cells.
Nagano K, Taoka M, Yamauchi Y, Itagaki C, Shinkawa T, Nunomura K, Okamura N, Takahashi N, Izumi T, Isobe T.
Proteomics. 2005 Apr;5(5):1346-61. [PMID: 15742316]
[4] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
Simon GM, Cheng J, Gordon JI.
Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
[5] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
[6] 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]
[7] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
[8] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
[9] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
J Biol Chem. 2013 Jul 17;. [PMID: 23864654]

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 (By similarity).

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 (By
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 (By
MOD_RES 179 179 N6-acetyllysine (By similarity).
MOD_RES 300 300 Phosphoserine; by TGFBR1 (By similarity).
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 (By
MOD_RES 439 439 N6-acetyllysine (By similarity).

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

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO:0005886; C:plasma membrane; IDA:MGI.
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:0006184; P:GTP catabolic process; IEA:GOC.

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.

PF00009; GTP_EFTU
PF03144; GTP_EFTU_D2
PF03143; GTP_EFTU_D3

PS00301; EFACTOR_GTP

PR00315; ELONGATNFCT.