CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017397
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Translation factor GUF1, mitochondrial 
Protein Synonyms/Alias
 Elongation factor 4 homolog; EF-4; GTPase GUF1; Ribosomal back-translocase 
Gene Name
 GUF1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
99TGTIDKTKNNKQVLDubiquitination[1]
102IDKTKNNKQVLDKLQubiquitination[2]
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] 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
 Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one- codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner (By similarity). 
Sequence Annotation
 NP_BIND 75 82 GTP (By similarity).
 NP_BIND 140 144 GTP (By similarity).
 NP_BIND 194 197 GTP (By similarity).
 CROSSLNK 102 102 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Complete proteome; GTP-binding; Hydrolase; Isopeptide bond; Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding; Polymorphism; Protein biosynthesis; Reference proteome; Transit peptide; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 669 AA 
Protein Sequence
MWTLVGRGWG CARALAPRAT GAALLVAPGP RSAPTLGAAP ESWATDRLYS SAEFKEKLDM 60
SRFPVENIRN FSIVAHVDHG KSTLADRLLE LTGTIDKTKN NKQVLDKLQV ERERGITVKA 120
QTASLFYNCE GKQYLLNLID TPGHVDFSYE VSRSLSACQG VLLVVDANEG IQAQTVANFF 180
LAFEAQLSVI PVINKIDLKN ADPERVENQI EKVFDIPSDE CIKISAKLGT NVESVLQAII 240
ERIPPPKVHR KNPLRALVFD STFDQYRGVI ANVALFDGVV SKGDKIVSAH TQKTYEVNEV 300
GVLNPNEQPT HKLYAGQVGY LIAGMKDVTE AQIGDTLCLH KQPVEPLPGF KSAKPMVFAG 360
MYPLDQSEYN NLKSAIEKLT LNDSSVTVHR DSSLALGAGW RLGFLGLLHM EVFNQRLEQE 420
YNASVILTTP TVPYKAVLSS SKLIKEHREK EITIINPAQF PDKSKVTEYL EPVVLGTIIT 480
PDEYTGKIMM LCEARRAVQK NMIFIDQNRV MLKYLFPLNE IVVDFYDSLK SLSSGYASFD 540
YEDAGYQTAE LVKMDILLNG NTVEELVTVV HKDKAHSIGK AICERLKDSL PRQLFEIAIQ 600
AAIGSKIIAR ETVKAYRKNV LAKCYGGDIT RKMKLLKRQA EGKKKLRKIG NVEVPKDAFI 660
KVLKTQSSK 669 
Gene Ontology
 GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
 GO:0005759; C:mitochondrial matrix; IEA:HAMAP.
 GO:0005525; F:GTP binding; IEA:HAMAP.
 GO:0003924; F:GTPase activity; IEA:HAMAP.
 GO:0043022; F:ribosome binding; IEA:HAMAP.
 GO:0006184; P:GTP catabolic process; IEA:GOC.
 GO:0045727; P:positive regulation of translation; IEA:HAMAP.
 GO:0006412; P:translation; IEA:UniProtKB-KW. 
Interpro
 IPR006297; EF-4.
 IPR000795; EF_GTP-bd_dom.
 IPR009022; EFG_III-V.
 IPR000640; EFG_V.
 IPR013842; LepA_GTP-bd_C.
 IPR027417; P-loop_NTPase.
 IPR005225; Small_GTP-bd_dom.
 IPR004161; Transl_elong_EFTu/EF1A_2.
 IPR009000; Transl_elong_init/rib_B-barrel. 
Pfam
 PF00679; EFG_C
 PF00009; GTP_EFTU
 PF03144; GTP_EFTU_D2
 PF06421; LepA_C 
SMART
 SM00838; EFG_C 
PROSITE
 PS00301; EFACTOR_GTP 
PRINTS
 PR00315; ELONGATNFCT.