CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014763
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation factor 1-delta 
Protein Synonyms/Alias
 EF-1-delta 
Gene Name
 Eef1d 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
240VREVWLEKPRYDAAEacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
Functional Description
 Isoform 1: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1- alpha for another round of transfer of aminoacyl-tRNAs to the ribosome (By similarity). 
Sequence Annotation
 REGION 80 115 Leucine-zipper (By similarity).
 REGION 173 281 Catalytic (GEF) (By similarity).
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 17 17 N6-acetyllysine (By similarity).
 MOD_RES 107 107 N6-acetyllysine (By similarity).
 MOD_RES 117 117 N6-acetyllysine (By similarity).
 MOD_RES 129 129 Phosphothreonine (By similarity).
 MOD_RES 133 133 Phosphoserine (By similarity).
 MOD_RES 147 147 Phosphothreonine (By similarity).
 MOD_RES 162 162 Phosphoserine; by CK2.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; DNA-binding; Elongation factor; Nucleus; Phosphoprotein; Protein biosynthesis; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 281 AA 
Protein Sequence
MRSGKASCAL ETVWEDKHKY EEAERRFHEH EATQAAAASV QQLLAEVPAV NGPSSQEDAE 60
DTDEAETPNT SSRSDPRKSH ECKKPLQKKR KRSPKSWLGQ ADLALVGLSA DHVWLDKPLF 120
DQAESSYRQR LADVAAQAAQ SPALAPRGPC THGSHVACHH VTWGIWVNKS CFDQAERAFV 180
EWSQALLLAA EGSHREGTPD TGQQAVTPDL ALACQPCPPA NGQPPLGSLQ ALVREVWLEK 240
PRYDAAERGF YEALFDGHPP GKVRLQERAS QAEGTRRGRR DRRSRNTVGN KRAGSKRADG 300
EAPSALPYWY FLHKDAEAPW LSKPTYDSAE CRHHAAEALR IAWRLEAASL AHRPTPRSGP 360
SMSSLRPKKM ATNFLMHEKI WFDKFKYDDA ERRFYEQMNG PVTAGSRQEN GASVILRDIA 420
RARENIQKSL AGSSGPGASS GPGGDHSDLI VRIASLEVEN QNLRGVVQDL QQAISKLEVR 480
LSTLEKSSPT HRATAPQTQH VSPMRQVEPP AKKGATPAED DEDNDIDLFG SDEEEEDKEA 540
ARLREERLRQ YAEKKAKKPT LVAKSSILLD VKPWDDETDM AQLETCVRSI QLDGLVWGAS 600
KLVPVGYGIR KLQIQCVVED DKVGTDLLEE EITKFEEHVQ SVDIAAFNKI 650 
Gene Ontology
 GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0004871; F:signal transducer activity; IEA:Compara.
 GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IEA:Compara.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR018940; EF-1_beta_acid_region_euk.
 IPR014717; Transl_elong_EF1B/ribosomal_S6.
 IPR001326; Transl_elong_EF1B_B/D_CS.
 IPR014038; Transl_elong_fac_EF1B_bsu/dsu. 
Pfam
 PF10587; EF-1_beta_acid
 PF00736; EF1_GNE 
SMART
 SM00888; EF1_GNE 
PROSITE
 PS00825; EF1BD_2 
PRINTS