CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017827
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 
Gene Name
 Gfm2 
Gene Synonyms/Alias
 Efg2 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
378AFKVLHDKQRGPLVFacetylation[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] 
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 (By similarity). 
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; Protein biosynthesis; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 779 AA 
Protein Sequence
MFTKWRIFAV NHQRTFSVHL NTMCYCKIKA NLKRLKTQLP LTRNYSSAPG IAGSDVKSLH 60
SVINPPVAKI RNIGIMAHID AGKTTTTERI LYYSGYTRSL GDVDDGDTVT DFMAQERERG 120
ITIQSAAVTL DWKGYRVNLI DTPGHVDFTL EVERCLRVLD GAVAVFDASA GVEAQTLTVW 180
RQADKHKIPR ICFLNKMDKT GASFNYAVES IREKLKAKPL ILQLPIGEAR TFQGVVDVVN 240
KEKLLWNSNS DDGKDFERMP LSEASDRELL KETIEARNSL IEQVADLDDE FADLVLGEFS 300
ENFDLVPAEK LQAAVHRVTL AQAAVPVLCG SALKNKGVQP LLDAVTTYLP SPEEREDRFL 360
QWYEGDLCAL AFKVLHDKQR GPLVFLRIYS GTLTPQLAVH NINRNCTERM SRLLLPFADQ 420
HVEIPSLTAG NIALTVGLKQ TATGDTIVSS KSSALAAARR AGRGEREHGK KREAESLLLA 480
GVEVPEPVFF CTIEPPSVAK QPDLDHALER LQREDPSLKV KLDPDSGQTV LCGMGELHIE 540
IIHDRIKREY GLETYLGPLQ VAYRETILNS VRATDTLDRV LGDKRHLVSA ELEVRPAEEP 600
CAVAKIEYAD CVGEDLLQAS REAIESAVHS ACLQGPLLGS PVQDVAMTLH SLMIHPGTST 660
TMVTACISRC MQKALKKADK QVLEPLMSLE VTVSREYLSP VLADLAQRRG NIQEIQTRQD 720
NRVVLGFVPL AEIMGYSTVL RTLTSGSATF ALELSTYQAM SPQDQSALLN QRSGLAHVL 779 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; ISS:UniProtKB.
 GO:0032543; P:mitochondrial translation; ISS:UniProtKB.
 GO:0032790; P:ribosome disassembly; ISS: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.