CPLM-009122

Genbank Nucleotide ID

Protein Synonyms/Alias

Mus musculus (Mouse)

Position	Peptide	Type	References
42	LTDSLVCKAGIIASA	acetylation	[1, 2]
42	LTDSLVCKAGIIASA	succinylation	[2]
42	LTDSLVCKAGIIASA	ubiquitination	[3]
152	QAIAERIKPVLMMNK	acetylation	[2]
152	QAIAERIKPVLMMNK	succinylation	[2]
152	QAIAERIKPVLMMNK	ubiquitination	[3]
159	KPVLMMNKMDRALLE	ubiquitination	[3]
235	FAEMYVAKFAAKGEG	acetylation	[1]
235	FAEMYVAKFAAKGEG	ubiquitination	[3]
239	YVAKFAAKGEGQLSA	acetylation	[1, 2]
239	YVAKFAAKGEGQLSA	ubiquitination	[3]
252	SAAERAKKVEDMMKK	acetylation	[1]
259	KVEDMMKKLWGDRYF	acetylation	[1]
259	KVEDMMKKLWGDRYF	ubiquitination	[3]
272	YFDPANGKFSKSANS	acetylation	[1, 2, 4, 5]
272	YFDPANGKFSKSANS	succinylation	[2]
272	YFDPANGKFSKSANS	ubiquitination	[3]
275	PANGKFSKSANSPDG	acetylation	[1, 2, 6]
275	PANGKFSKSANSPDG	succinylation	[2]
275	PANGKFSKSANSPDG	ubiquitination	[3]
283	SANSPDGKKLPRTFC	ubiquitination	[3]
314	FRKEETAKLIEKLDI	acetylation	[4, 5]
314	FRKEETAKLIEKLDI	ubiquitination	[3]
318	ETAKLIEKLDIKLDS	acetylation	[1, 2, 5]
318	ETAKLIEKLDIKLDS	succinylation	[2]
318	ETAKLIEKLDIKLDS	ubiquitination	[3]
337	KEGKPLLKAVMRRWL	acetylation	[5]
391	GIKSCDPKGPLMMYI	acetylation	[1]
400	PLMMYISKMVPTSDK	acetylation	[1]
400	PLMMYISKMVPTSDK	ubiquitination	[3]
426	GVVSTGLKVRIMGPN	acetylation	[1, 5]
438	GPNYTPGKKEDLYLK	ubiquitination	[3]
439	PNYTPGKKEDLYLKP	acetylation	[1, 2]
439	PNYTPGKKEDLYLKP	ubiquitination	[3]
445	KKEDLYLKPIQRTIL	acetylation	[1, 2, 4, 5, 6]
498	AHNMRVMKFSVSPVV	acetylation	[1, 2]
498	AHNMRVMKFSVSPVV	ubiquitination	[3]
512	VRVAVEAKNPADLPK	acetylation	[2, 5]
512	VRVAVEAKNPADLPK	succinylation	[2]
512	VRVAVEAKNPADLPK	ubiquitination	[3]
571	DHACIPIKKSDPVVS	acetylation	[1]
571	DHACIPIKKSDPVVS	ubiquitination	[3]
572	HACIPIKKSDPVVSY	acetylation	[2]
572	HACIPIKKSDPVVSY	succinylation	[2]
572	HACIPIKKSDPVVSY	ubiquitination	[3]
594	SNVLCLSKSPNKHNR	acetylation	[2]
594	SNVLCLSKSPNKHNR	succinylation	[2]
594	SNVLCLSKSPNKHNR	ubiquitination	[3]
605	KHNRLYMKARPFPDG	ubiquitination	[3]
619	GLAEDIDKGEVSARQ	acetylation	[2]
638	RARYLAEKYEWDVAE	acetylation	[1, 2]
638	RARYLAEKYEWDVAE	ubiquitination	[3]
648	WDVAEARKIWCFGPD	acetylation	[1, 6]
648	WDVAEARKIWCFGPD	ubiquitination	[3]
845	TRKRKGLKEGIPALD	ubiquitination	[3]
857	ALDNFLDKL******	acetylation	[2, 6]

[1] 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]
[2] 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]
[3] 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]
[4] 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]
[5] 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]
[6] 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]

Functional Description

Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.

NP_BIND 26 33 GTP (By similarity).
NP_BIND 104 108 GTP (By similarity).
NP_BIND 158 161 GTP (By similarity).
MOD_RES 54 54 Phosphothreonine.
MOD_RES 57 57 Phosphothreonine.
MOD_RES 59 59 Phosphothreonine.
MOD_RES 235 235 N6-acetyllysine (By similarity).
MOD_RES 239 239 N6-acetyllysine (By similarity).
MOD_RES 272 272 N6-acetyllysine (By similarity).
MOD_RES 275 275 N6-acetyllysine (By similarity).
MOD_RES 435 435 Phosphothreonine (By similarity).
MOD_RES 445 445 N6-acetyllysine (By similarity).
MOD_RES 502 502 Phosphoserine (By similarity).
MOD_RES 715 715 Diphthamide (By similarity).

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

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005844; C:polysome; IDA:MGI.
GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO:0003924; F:GTPase activity; IDA:MGI.
GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
GO:0006414; P:translational elongation; IDA:MGI.

IPR000795; EF_GTP-bd_dom.
IPR009022; EFG_III-V.
IPR000640; EFG_V.
IPR027417; P-loop_NTPase.
IPR020568; Ribosomal_S5_D2-typ_fold.
IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
IPR005225; Small_GTP-bd_dom.
IPR005517; Transl_elong_EFG/EF2_IV.
IPR004161; Transl_elong_EFTu/EF1A_2.
IPR009000; Transl_elong_init/rib_B-barrel.

PF00679; EFG_C
PF03764; EFG_IV
PF00009; GTP_EFTU
PF03144; GTP_EFTU_D2

SM00838; EFG_C
SM00889; EFG_IV

PS00301; EFACTOR_GTP

PR00315; ELONGATNFCT.