CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009722
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Eukaryotic translation initiation factor 5A-1 
Protein Synonyms/Alias
 eIF-5A-1; eIF-5A1; Eukaryotic initiation factor 5A isoform 1; eIF-5A; Rev-binding factor; eIF-4D 
Gene Name
 EIF5A 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
27MQCSALRKNGFVVLKacetylation[1]
27MQCSALRKNGFVVLKubiquitination[2, 3]
34KNGFVVLKGRPCKIVubiquitination[3]
39VLKGRPCKIVEMSTSubiquitination[3]
47IVEMSTSKTGKHGHAacetylation[1, 4]
67GIDIFTGKKYEDICPubiquitination[2, 3, 5]
68IDIFTGKKYEDICPSacetylation[6]
68IDIFTGKKYEDICPSubiquitination[2, 3, 7]
85NMDVPNIKRNDFQLIubiquitination[2, 7]
121LPEGDLGKEIEQKYDubiquitination[2, 3, 5]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [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] The effect of hypusine modification on the intracellular localization of eIF5A.
 Lee SB, Park JH, Kaevel J, Sramkova M, Weigert R, Park MH.
 Biochem Biophys Res Commun. 2009 Jun 12;383(4):497-502. [PMID: 19379712]
 [5] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [6] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [7] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865
Functional Description
 mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. With syntenin SDCBP, functions as a regulator of p53/TP53 and p53/TP53-dependent apoptosis. Regulates also TNF- alpha-mediated apoptosis. Mediates effects of polyamines on neuronal process extension and survival. May play an important role in brain development and function, and in skeletal muscle stem cell differentiation. Also described as a cellular cofactor of human T-cell leukemia virus type I (HTLV-1) Rex protein and of human immunodeficiency virus type 1 (HIV-1) Rev protein, essential for mRNA export of retroviral transcripts. 
Sequence Annotation
 REGION 20 90 DOHH-binding.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 47 47 N6-acetyllysine.
 MOD_RES 50 50 Hypusine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Elongation factor; Endoplasmic reticulum; Hypusine; Membrane; mRNA transport; Nuclear pore complex; Nucleus; Protein biosynthesis; Protein transport; Reference proteome; RNA-binding; Translocation; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 154 AA 
Protein Sequence
MADDLDFETG DAGASATFPM QCSALRKNGF VVLKGRPCKI VEMSTSKTGK HGHAKVHLVG 60
IDIFTGKKYE DICPSTHNMD VPNIKRNDFQ LIGIQDGYLS LLQDSGEVRE DLRLPEGDLG 120
KEIEQKYDCG EEILITVLSA MTEEAAVAIK AMAK 154 
Gene Ontology
 GO:0005642; C:annulate lamellae; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0005643; C:nuclear pore; IDA:UniProtKB.
 GO:0043022; F:ribosome binding; IEA:InterPro.
 GO:0003746; F:translation elongation factor activity; ISS:UniProtKB.
 GO:0017070; F:U6 snRNA binding; IDA:UniProtKB.
 GO:0006917; P:induction of apoptosis; IDA:UniProtKB.
 GO:0006406; P:mRNA export from nucleus; IMP:UniProtKB.
 GO:0008612; P:peptidyl-lysine modification to hypusine; TAS:Reactome.
 GO:0008284; P:positive regulation of cell proliferation; IGI:UniProtKB.
 GO:0045901; P:positive regulation of translational elongation; ISS:UniProtKB.
 GO:0045905; P:positive regulation of translational termination; IEA:InterPro.
 GO:0043687; P:post-translational protein modification; TAS:Reactome.
 GO:0006611; P:protein export from nucleus; IMP:UniProtKB.
 GO:0006452; P:translational frameshifting; IEA:InterPro. 
Interpro
 IPR005824; KOW.
 IPR012340; NA-bd_OB-fold.
 IPR014722; Rib_L2_dom2.
 IPR019769; Trans_elong_IF5A_hypusine_site.
 IPR001884; Transl_elong_IF5A.
 IPR020189; Transl_elong_IF5A_C.
 IPR008991; Translation_prot_SH3-like. 
Pfam
 PF01287; eIF-5a
 PF00467; KOW 
SMART
  
PROSITE
 PS00302; IF5A_HYPUSINE 
PRINTS