CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016357
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation factor Tu, mitochondrial 
Protein Synonyms/Alias
  
Gene Name
 Tufm 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
88LAEGGGAKFKKYEEIacetylation[1]
88LAEGGGAKFKKYEEIubiquitination[2]
90EGGGAKFKKYEEIDNacetylation[1]
91GGGAKFKKYEEIDNAacetylation[1]
238LGVKSVQKLLDAVDTacetylation[1]
256VPTRDLDKPFLLPVEacetylation[1]
297CELLGHNKNIRTVVTacetylation[1]
361AQVYILSKEEGGRHKacetylation[1]
Reference
 [1] 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]
 [2] 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
Functional Description
 This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis (By similarity). 
Sequence Annotation
 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 (By similarity).
 MOD_RES 88 88 N6-acetyllysine (By similarity).
 MOD_RES 256 256 N6-acetyllysine (By similarity).
 MOD_RES 418 418 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Elongation factor; GTP-binding; Mitochondrion; Nucleotide-binding; Protein biosynthesis; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 452 AA 
Protein Sequence
MAAATLLRAT PRFSGLCASP TPFLQGRLRP LKAPASPFLC RGLAVEAKKT YVRDKPHVNV 60
GTIGHVDHGK TTLTAAITKI LAEGGGAKFK KYEEIDNAPE ERARGITINA AHVEYSTAAR 120
HYAHTDCPGH ADYVKNMITG TAPLDGCILV VAANDGPMPQ TREHLLLAKQ IGVEHVVVYV 180
NKADAVQDSE MVELVELEIR ELLTEFGYKG EETPVIVGSA LCALEQRDPE LGVKSVQKLL 240
DAVDTYIPVP TRDLDKPFLL PVESVYSIPG RGTVVTGTLE RGILKKGDEC ELLGHNKNIR 300
TVVTGIEMFH KSLERAEAGD NLGALVRGLK REDLRRGLVM VKPGSIQPHQ KVEAQVYILS 360
KEEGGRHKPF VSHFMPVMFS LTWDMACRVI LPPGKELAMP GEDLKLSLIL RQPMILEKGQ 420
RFTLRDGNKT IGTGLVTDVP AMTEEDKNIK WS 452 
Gene Ontology
 GO:0005743; C:mitochondrial inner 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; ISS:UniProtKB.
 GO:0006184; P:GTP catabolic process; IEA:GOC. 
Interpro
 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. 
Pfam
 PF00009; GTP_EFTU
 PF03144; GTP_EFTU_D2
 PF03143; GTP_EFTU_D3 
SMART
  
PROSITE
 PS00301; EFACTOR_GTP 
PRINTS
 PR00315; ELONGATNFCT.