CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018988
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribosome-releasing factor 2, mitochondrial 
Protein Synonyms/Alias
 RRF2mt; Elongation factor G 2, mitochondrial; EF-G2mt; mEF-G 2; Elongation factor G2; hEFG2 
Gene Name
 GFM2 
Gene Synonyms/Alias
 EFG2; MSTP027 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
196PRICFLNKMDKTGASubiquitination[1]
199CFLNKMDKTGASFKYubiquitination[1]
205DKTGASFKYAVESIRubiquitination[1]
218IREKLKAKPLLLQLPubiquitination[1]
230QLPIGEAKTFKGVVDubiquitination[1]
233IGEAKTFKGVVDVVMacetylation[2]
241GVVDVVMKEKLLWNCubiquitination[1]
243VDVVMKEKLLWNCNSubiquitination[1]
259DGKDFERKPLLEMNDubiquitination[1]
336CGSALKNKGIQPLLDubiquitination[1]
394RIYSGTIKPQLAIHNubiquitination[1]
451GDTIVSSKSSALAAAubiquitination[1, 3, 4, 5]
510PDLEHALKCLQREDPubiquitination[1]
520QREDPSLKVRLDPDSubiquitination[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] 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]
 [3] 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]
 [4] 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]
 [5] 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] 
Functional Description
 Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Acts in collaboration with MRRF. GTP hydrolysis follows the ribosome disassembly and probably occurs on the ribosome large subunit. Not involved in the GTP-dependent ribosomal translocation step during translation elongation. 
Sequence Annotation
 NP_BIND 77 84 GTP (By similarity).
 NP_BIND 141 145 GTP (By similarity).
 NP_BIND 195 198 GTP (By similarity).  
Keyword
 Alternative splicing; Complete proteome; GTP-binding; Mitochondrion; Nucleotide-binding; Polymorphism; Protein biosynthesis; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 779 AA 
Protein Sequence
MLTNLRIFAM SHQTIPSVYI NNICCYKIRA SLKRLKPHVP LGRNCSSLPG LIGNDIKSLH 60
SIINPPIAKI RNIGIMAHID AGKTTTTERI LYYSGYTRSL GDVDDGDTVT DFMAQERERG 120
ITIQSAAVTF DWKGYRVNLI DTPGHVDFTL EVERCLRVLD GAVAVFDASA GVEAQTLTVW 180
RQADKHNIPR ICFLNKMDKT GASFKYAVES IREKLKAKPL LLQLPIGEAK TFKGVVDVVM 240
KEKLLWNCNS NDGKDFERKP LLEMNDPELL KETTEARNAL IEQVADLDDE FADLVLEEFS 300
ENFDLLPAEK LQTAIHRVTL AQTAVPVLCG SALKNKGIQP LLDAVTMYLP SPEERNYEFL 360
QWYKDDLCAL AFKVLHDKQR GPLVFMRIYS GTIKPQLAIH NINGNCTERI SRLLLPFADQ 420
HVEIPSLTAG NIALTVGLKH TATGDTIVSS KSSALAAARR AEREGEKKHR QNNEAERLLL 480
AGVEIPEPVF FCTIEPPSLS KQPDLEHALK CLQREDPSLK VRLDPDSGQT VLCGMGELHI 540
EIIHDRIKRE YGLETYLGPL QVAYRETILN SVRATDTLDR TLGDKRHLVT VEVEARPIET 600
SSVMPVIEFE YAESINEGLL KVSQEAIENG IHSACLQGPL LGSPIQDVAI TLHSLTIHPG 660
TSTTMISACV SRCVQKALKK ADKQVLEPLM NLEVTVARDY LSPVLADLAQ RRGNIQEIQT 720
RQDNKVVIGF VPLAEIMGYS TVLRTLTSGS ATFALELSTY QAMNPQDQNT LLNRRSGLT 779 
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:0032543; P:mitochondrial translation; IDA:UniProtKB.
 GO:0032790; P:ribosome disassembly; 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.
 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.