CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-032896
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Elongation factor G, mitochondrial 
Protein Synonyms/Alias
  
Gene Name
 GFM1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
82KMHEVKGKDGVGAVMubiquitination[1, 2]
280IPSISDLKLAIRRATubiquitination[1, 2, 3, 4, 5]
302VFLGSALKNKGVQPLubiquitination[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] 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]
 [4] 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]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; GTP-binding; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 591 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 QIVRYGEIPA 240
ELRAAATDHR QELIECVANS DEQLGEMFLE EKIPSISDLK LAIRRATLKR SFTPVFLGSA 300
LKNKGVQPLL DAVLEYLPNP SEVQNYAILN KEDDSKEKTK ILMNSSRDNS HPFVGLAFKL 360
EVGRFGQLTY VRSYQGELKK GDTIYNTRTR KKVRLQRLAR MHADMMEDVE EVYAGDICAL 420
FGIDCASGDT FTDKANSGLS MESIHVPDPV ISIAMKPSNK NDLEKFSKGI GRFTREDPTF 480
KVYFDTENKE TVISGMGELH LEIYAQRLER EYGCPCITGK PKVAFRETIT APVPFDFTHK 540
KQSGGAGQYG KVIGVLEPLD PEDYTKLEFS DETFGSNIPK QFVPAVEKVN F 591 
Gene Ontology
 GO:0005622; C:intracellular; IEA:InterPro.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0003746; F:translation elongation factor activity; IEA:InterPro.
 GO:0006184; P:GTP catabolic process; IEA:GOC. 
Interpro
 IPR000795; EF_GTP-bd_dom.
 IPR009022; EFG_III-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
 PF03764; EFG_IV
 PF00009; GTP_EFTU
 PF03144; GTP_EFTU_D2 
SMART
  
PROSITE
 PS00301; EFACTOR_GTP 
PRINTS
 PR00315; ELONGATNFCT.