CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019591
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation factor G, mitochondrial 
Protein Synonyms/Alias
 EF-Gmt; Elongation factor G 1, mitochondrial; mEF-G 1; Elongation factor G1; hEFG1 
Gene Name
 GFM1 
Gene Synonyms/Alias
 EFG; EFG1; GFM 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
82KMHEVKGKDGVGAVMubiquitination[1, 2]
299IPSISDLKLAIRRATubiquitination[1, 2, 3]
321VFLGSALKNKGVQPLubiquitination[1]
323LGSALKNKGVQPLLDubiquitination[1]
Reference
 [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] 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]
 [3] 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
Functional Description
 Mitochondrial GTPase that 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. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. 
Sequence Annotation
 NP_BIND 53 60 GTP (By similarity).
 NP_BIND 120 124 GTP (By similarity).
 NP_BIND 174 177 GTP (By similarity).
 MOD_RES 175 175 N6-acetyllysine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Elongation factor; GTP-binding; Mitochondrion; Nucleotide-binding; Polymorphism; Protein biosynthesis; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 751 AA 
Protein Sequence
MRLLGAAAVA ALGRGRAPAS LGWQRKQVNW KACRWSSSGV IPNEKIRNIG ISAHIDSGKT 60
TLTERVLYYT GRIAKMHEVK GKDGVGAVMD SMELERQRGI TIQSAATYTM WKDVNINIID 120
TPGHVDFTIE VERALRVLDG AVLVLCAVGG VQCQTMTVNR QMKRYNVPFL TFINKLDRMG 180
SNPARALQQM RSKLNHNAAF MQIPMGLEGN FKGIVDLIEE RAIYFDGDFG HFLRDFLPLL 240
WNWDRRSGSQ IVRYGEIPAE LRAAATDHRQ ELIECVANSD EQLGEMFLEE KIPSISDLKL 300
AIRRATLKRS FTPVFLGSAL KNKGVQPLLD AVLEYLPNPS EVQNYAILNK EDDSKEKTKI 360
LMNSSRDNSH PFVGLAFKLE VGRFGQLTYV RSYQGELKKG DTIYNTRTRK KVRLQRLARM 420
HADMMEDVEE VYAGDICALF GIDCASGDTF TDKANSGLSM ESIHVPDPVI SIAMKPSNKN 480
DLEKFSKGIG RFTREDPTFK VYFDTENKET VISGMGELHL EIYAQRLERE YGCPCITGKP 540
KVAFRETITA PVPFDFTHKK QSGGAGQYGK VIGVLEPLDP EDYTKLEFSD ETFGSNIPKQ 600
FVPAVEKGFL DACEKGPLSG HKLSGLRFVL QDGAHHMVDS NEISFIRAGE GALKQALANA 660
TLCILEPIMA VEVVAPNEFQ GQVIAGINRR HGVITGQDGV EDYFTLYADV PLNDMFGYST 720
ELRSCTEGKG EYTMEYSRYQ PCLPSTQEDV INKYLEATGQ LPVKKGKAKN 770 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IDA:UniProtKB.
 GO:0003746; F:translation elongation factor activity; IDA:UniProtKB.
 GO:0070125; P:mitochondrial translational elongation; IDA:UniProtKB. 
Interpro
 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.
 IPR004540; Transl_elong_EFG/EF2.
 IPR005517; Transl_elong_EFG/EF2_IV.
 IPR004161; Transl_elong_EFTu/EF1A_2.
 IPR009000; Transl_elong_init/rib_B-barrel. 
Pfam
 PF00679; EFG_C
 PF03764; EFG_IV
 PF00009; GTP_EFTU
 PF03144; GTP_EFTU_D2 
SMART
 SM00838; EFG_C
 SM00889; EFG_IV 
PROSITE
 PS00301; EFACTOR_GTP 
PRINTS
 PR00315; ELONGATNFCT.