CPLM-008145

Genbank Nucleotide ID

Elongation factor Tu, mitochondrial

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
32	QGLLRLLKAPALPLL	ubiquitination	[1]
79	TLTAAITKILAEGGG	acetylation	[2, 3, 4]
79	TLTAAITKILAEGGG	ubiquitination	[1, 5, 6, 7, 8, 9]
88	LAEGGGAKFKKYEEI	acetylation	[2, 3, 9]
88	LAEGGGAKFKKYEEI	ubiquitination	[1, 5, 6, 7, 8, 9, 10]
90	EGGGAKFKKYEEIDN	acetylation	[9]
90	EGGGAKFKKYEEIDN	ubiquitination	[1, 7, 11]
91	GGGAKFKKYEEIDNA	acetylation	[3]
91	GGGAKFKKYEEIDNA	ubiquitination	[1, 5, 6]
234	RDPELGLKSVQKLLD	ubiquitination	[6, 7]
238	LGLKSVQKLLDAVDT	acetylation	[4]
238	LGLKSVQKLLDAVDT	ubiquitination	[5, 6, 7, 8]
256	VPARDLEKPFLLPVE	acetylation	[2, 3, 4, 12]
256	VPARDLEKPFLLPVE	ubiquitination	[1, 5, 6, 7, 8, 10, 13]
286	LERGILKKGDECELL	ubiquitination	[1]
297	CELLGHSKNIRTVVT	ubiquitination	[1, 9]
311	TGIEMFHKSLERAEA	ubiquitination	[1, 5, 6, 7, 8, 9]
342	RRGLVMVKPGSIKPH	acetylation	[4]
361	AQVYILSKEEGGRHK	ubiquitination	[1, 6, 7, 9]
395	RIILPPEKELAMPGE	ubiquitination	[7]
405	AMPGEDLKFNLILRQ	ubiquitination	[6]
418	RQPMILEKGQRFTLR	acetylation	[2, 3, 9]
418	RQPMILEKGQRFTLR	ubiquitination	[1]
447	LAMTEEEKNIKWG**	acetylation	[4, 9]
447	LAMTEEEKNIKWG**	ubiquitination	[6]
450	TEEEKNIKWG*****	ubiquitination	[6]

[1] 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]
[2] 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]
[3] 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]
[4] 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]
[5] 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]
[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] 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]
[8] 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]
[9] 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]
[10] 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]
[11] 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]
[12] 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]
[13] 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]

Functional Description

This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.

NP_BIND 64 71 GTP (By similarity).
NP_BIND 126 130 GTP (By similarity).
NP_BIND 181 184 GTP (By similarity).
MOD_RES 79 79 N6-acetyllysine.
MOD_RES 88 88 N6-acetyllysine.
MOD_RES 256 256 N6-acetyllysine.
MOD_RES 418 418 N6-acetyllysine.

Acetylation; Complete proteome; Direct protein sequencing; Disease mutation; Elongation factor; GTP-binding; Mitochondrion; Nucleotide-binding; Protein biosynthesis; Reference proteome; Transit peptide.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO:0003924; F:GTPase activity; IEA:InterPro.
GO:0003746; F:translation elongation factor activity; IDA:UniProtKB.
GO:0006184; P:GTP catabolic process; IEA:GOC.

IPR000795; EF_GTP-bd_dom.
IPR027417; P-loop_NTPase.
IPR009001; Transl_elong_EF1A/Init_IF2_C.
IPR004161; Transl_elong_EFTu/EF1A_2.
IPR004541; Transl_elong_EFTu/EF1A_bac/org.
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.