UniProt Accession

 IF5A1_HUMAN; P63241; A8K9A0; D3DTP2; P10159; Q16182; Q7L7L3; Q7Z4L1; Q9D0G2 

Genbank Protein ID

 M23419; S72024; U17969; AY129319; AY129320; AY129321; AY129322; AK292615; CH471108; CH471108; CH471108; CH471108; BC000751; BC001832; BC030160; BC080196; BC085015; BC107779 

Genbank Nucleotide ID

 AAA58453.1; AAD14095.1; AAA86989.1; AAN17514.1; AAN17515.1; AAN17516.1; AAN17518.1; BAF85304.1; EAW90219.1; EAW90220.1; EAW90221.1; EAW90222.1; AAH00751.1; AAH01832.1; AAH30160.1; AAH80196.1; AAH85015.1; AAI07780.1 

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
57	MQCSALRKNGFVVLK	ubiquitination	[1, 2, 3]
64	KNGFVVLKGRPCKIV	ubiquitination	[2]
69	VLKGRPCKIVEMSTS	ubiquitination	[1, 2]
97	GIDIFTGKKYEDICP	ubiquitination	[1, 2, 3]
98	IDIFTGKKYEDICPS	ubiquitination	[2, 3, 4]
115	NMDVPNIKRNDFQLI	ubiquitination	[1, 2, 3, 4]
151	LPEGDLGKEIEQKYD	ubiquitination	[2, 3]

Reference

 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [2] 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]
 [3] 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]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 

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

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