CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016682
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation factor Tu GTP-binding domain-containing protein 1 
Protein Synonyms/Alias
  
Gene Name
 Eftud1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
429VKALPQNKPRPLTQEubiquitination[1]
635SEMPQLVKGMKLLNQubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 Involved in the biogenesis of the 60S ribosomal subunit and translational activation of ribosomes. Together with SBDS, triggers the GTP-dependent release of EIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating EIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export. Has low intrinsic GTPase activity. GTPase activity is increased by contact with 60S ribosome subunits (By similarity). 
Sequence Annotation
 NP_BIND 26 33 GTP (By similarity).
 NP_BIND 92 96 GTP (By similarity).
 NP_BIND 146 149 GTP (By similarity).
 MOD_RES 528 528 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Complete proteome; Elongation factor; GTP-binding; Nucleotide-binding; Protein biosynthesis; Reference proteome; Ribosome biogenesis. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1127 AA 
Protein Sequence
MVLSGVDKMI RLQKNTANIR NICVLAHVDH GKTTLADCLI SSNGIISSRL AGKLRYMDSR 60
EDEQVRGITM KSSAISLHYA EGHEEYLINL IDSPGHVDFS SEVSTAVRIC DGCIIVVDAV 120
EGVCPQTQAV LRQAWLENIR PVLVINKIDR LIVELKFTPQ EAYSHLKNIL EQINALTGTL 180
FTSKVLEERA ERETESQAKP HSEQGEQVYD WSAGLEDVDD SQLYFSPEQG NVVFTSAIDG 240
WGFGIEHFAR IYSQKIGIKK EVLLKTLWGD YYINMKAKKI MKVDQAKGKK PLFVQLILEN 300
IWSLYDAVLK KDKEKIDKIV TSLGLKIGAR EARHSDPKVQ INAICSQWLP ISHAVLAMVC 360
HKLPSPLDMT SERVEKLLCT GSQTFESLPP ETQALKAAFM KCGSEDTAPV IIFVSKMFAV 420
DVKALPQNKP RPLTQEEMAQ RRERARQRHA EKLAAAQGQT SQGPTQDGGA LETSPHEDEP 480
RGDEPDVASV SRQPVSQEES SQEAFIAFAR VFSGIARRGK KIFVLGPKYS PVDFLQRVPL 540
GFSAPLEDLP PVPHMACCTL ENLYLLMGRE LEDLEEVPPG NVLGIGGLQD FVLKSATLCS 600
LPSCPPFIPL NFEATPIVRV AVEPKHPSEM PQLVKGMKLL NQADPCVQVL IQETGEHVLV 660
TAGEVHLQRC LDDLRERFAK IHISVSEPII PFRETITKPP KVDMVNEEIG RQQKVAVIHQ 720
TKEEQSKIPE GIHVDSDGLI TIPTPNKLAT LSVRAIPLPE EVTRILEENS DLIRSMELLT 780
SSLNEGRNTQ AIHQKTQEKI WEFKGKLEKH LTGRKWRNTV DQIWSFGPRK CGPNILVSRS 840
EDFQNSVWSG PAGRESKEAS RFRDFGNSIV SGFQLATLSG PMCEEPLMGV CFVLEKWELN 900
KCAEQGASDK QHQGQCDLAG EGQGGGKTCH VGDENQEQQD VCSEPFEETS QKGDSPVIDC 960
YGPFSGQLIA TMKEACRYAL QVKPQRLMAA MYTCDIMATS DVLGRVYAVL SKREGRVLQE 1020
EMKEGTDMFI IKAVLPVAES FGFADEIRKR TSGLASPQLV FSHWEVIPSD PFWVPTTEEE 1080
YLHFGEKADS ENQARKYMNA VRKRKGLYVE EKIVEHAEKQ RTLSKNK 1127 
Gene Ontology
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; ISS:UniProtKB.
 GO:0043022; F:ribosome binding; ISS:UniProtKB.
 GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
 GO:0042256; P:mature ribosome assembly; 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.
 IPR004161; Transl_elong_EFTu/EF1A_2.
 IPR009000; Transl_elong_init/rib_B-barrel. 
Pfam
 PF00679; EFG_C
 PF00009; GTP_EFTU
 PF03144; GTP_EFTU_D2 
SMART
 SM00838; EFG_C 
PROSITE
 PS00301; EFACTOR_GTP 
PRINTS
 PR00315; ELONGATNFCT.