EIF5A

Eukaryotic translation initiation factor 5A

Rendering based on PDB 1FH4.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1FH4, 3CPF

Identifiers

Symbols

EIF5A ; EIF-5A; EIF5A1; eIF5AI

External IDs

OMIM: 600187 MGI: 106248 HomoloGene: 133803 GeneCards: EIF5A Gene

Gene ontology
Molecular function	• RNA binding • translation elongation factor activity • protein binding • U6 snRNA binding • ribosome binding • poly(A) RNA binding • protein N-terminus binding
Cellular component	• nucleus • annulate lamellae • nuclear pore • cytoplasm • endoplasmic reticulum membrane • cytosol • membrane • extracellular vesicular exosome
Biological process	• mRNA export from nucleus • translational frameshifting • protein export from nucleus • nucleocytoplasmic transport • apoptotic process • positive regulation of cell proliferation • peptidyl-lysine modification to peptidyl-hypusine • post-translational protein modification • cellular protein metabolic process • positive regulation of translational elongation • positive regulation of translational termination
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 17:
7.21 – 7.22 Mb

Chr 11:
69.92 – 69.92 Mb

PubMed search

Eukaryotic translation initiation factor 5A-1 is a protein that in humans is encoded by the EIF5A gene.^[1]

It is the only known protein to contain the unusual amino acid hypusine [N (ε)- (4-amino-2-hydroxybutyl)-lysine], which is synthesized on eIF5A at a specific lysine residue from the polyamine spermidine by two catalytic steps.^[2]

EF-P is the prokaryotic homolog of eIF5A, which is also modified post-translationally in a similar but distinct way.^[3]^[4]

References

↑ Steinkasserer A, Jones T, Sheer D, Koettnitz K, Hauber J, Bevec D (Jun 1995). "The eukaryotic cofactor for the human immunodeficiency virus type 1 (HIV-1) rev protein, eIF-5A, maps to chromosome 17p12-p13: three eIF-5A pseudogenes map to 10q23.3, 17q25, and 19q13.2". Genomics 25 (3): 749–52. doi:10.1016/0888-7543(95)80025-H. PMID 7759117.
↑ Wolff EC, Kang KR, Kim YS, Park MH (May 2007). "Posttranslational synthesis of hypusine: evolutionary progression and specificity of the hypusine modification". Amino Acids 33 (2): 341–350. doi:10.1007/s00726-007-0525-0. PMC 2572820. PMID 17476569.
↑ Park JH, Johansson HE, Aoki H, Huang BX, Kim HY, Ganoza MC, Park MH (Nov 2011). "Post-translational modification by β-lysylation is required for activity of Escherichia coli elongation factor P (EF-P)". Journal of Biological Chemistry 287 (4): 2579–2590. doi:10.1074/jbc.M111.309633. PMC 3268417. PMID 22128152.
↑ Peil L, Starosta AL, Virumäe K, Atkinson GC, Tenson T, Remme J, Wilson DN (2012). "Lys34 of translation elongation factor EF-P is hydroxylated by YfcM". Nature Chemical Biology Epub (8): 695–7. doi:10.1038/nchembio.1001. PMID 22706199.

Bevec D, Hauber J (1997). "Eukaryotic initiation factor 5A activity and HIV-1 Rev function.". Biol. Signals 6 (3): 124–33. doi:10.1159/000109118. PMID 9285095.
Li L, Li HS, Pauza CD et al. (2006). "Roles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactions.". Cell Res. 15 (11–12): 923–34. doi:10.1038/sj.cr.7290370. PMID 16354571.
Rasmussen HH, van Damme J, Puype M et al. (1993). "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes". Electrophoresis 13 (12): 960–9. doi:10.1002/elps.11501301199. PMID 1286667.
Chung SI, Park MH, Folk JE, Lewis MS (1991). "Eukaryotic initiation factor 5A: the molecular form of the hypusine-containing protein from human erythrocytes". Biochim. Biophys. Acta 1076 (3): 448–51. doi:10.1016/0167-4838(91)90490-q. PMID 1900436.
Smit-McBride Z, Dever TE, Hershey JW, Merrick WC (1989). "Sequence determination and cDNA cloning of eukaryotic initiation factor 4D, the hypusine-containing protein". J. Biol. Chem. 264 (3): 1578–83. PMID 2492279.
Park MH, Liu TY, Neece SH, Swiggard WJ (1986). "Eukaryotic initiation factor 4D. Purification from human red blood cells and the sequence of amino acids around its single hypusine residue". J. Biol. Chem. 261 (31): 14515–9. PMID 3095320.
Koettnitz K, Kappel B, Baumruker T et al. (1994). "The genomic structure encoding human initiation factor eIF-5A". Gene 144 (2): 249–52. doi:10.1016/0378-1119(94)90385-9. PMID 7545941.
Klier H, Csonga R, Joäo HC et al. (1995). "Isolation and structural characterization of different isoforms of the hypusine-containing protein eIF-5A from HeLa cells". Biochemistry 34 (45): 14693–702. doi:10.1021/bi00045a010. PMID 7578077.
Koettnitz K, Wöhl T, Kappel B et al. (1995). "Identification of a new member of the human eIF-5A gene family". Gene 159 (2): 283–4. doi:10.1016/0378-1119(95)00136-T. PMID 7622067.
Joe YA, Park MH (1994). "Structural features of the eIF-5A precursor required for posttranslational synthesis of deoxyhypusine". J. Biol. Chem. 269 (41): 25916–21. PMID 7929297.
Bevec D, Klier H, Holter W et al. (1994). "Induced gene expression of the hypusine-containing protein eukaryotic initiation factor 5A in activated human T lymphocytes". Proc. Natl. Acad. Sci. U.S.A. 91 (23): 10829–33. doi:10.1073/pnas.91.23.10829. PMC 45119. PMID 7971969.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Ruhl M, Himmelspach M, Bahr GM et al. (1994). "Eukaryotic initiation factor 5A is a cellular target of the human immunodeficiency virus type 1 Rev activation domain mediating trans-activation". J. Cell Biol. 123 (6 Pt 1): 1309–20. doi:10.1083/jcb.123.6.1309. PMC 2290910. PMID 8253832.
Liu YP, Nemeroff M, Yan YP, Chen KY (1997). "Interaction of eukaryotic initiation factor 5A with the human immunodeficiency virus type 1 Rev response element RNA and U6 snRNA requires deoxyhypusine or hypusine modification". Biol. Signals 6 (3): 166–74. doi:10.1159/000109123. PMID 9285100.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Singh US, Li Q, Cerione R (1998). "Identification of the eukaryotic initiation factor 5A as a retinoic acid-stimulated cellular binding partner for tissue transglutaminase II". J. Biol. Chem. 273 (4): 1946–50. doi:10.1074/jbc.273.4.1946. PMID 9442029.
Schatz O, Oft M, Dascher C et al. (1998). "Interaction of the HIV-1 rev cofactor eukaryotic initiation factor 5A with ribosomal protein L5". Proc. Natl. Acad. Sci. U.S.A. 95 (4): 1607–12. doi:10.1073/pnas.95.4.1607. PMC 19115. PMID 9465063.
Lee YB, Joe YA, Wolff EC et al. (1999). "Complex formation between deoxyhypusine synthase and its protein substrate, the eukaryotic translation initiation factor 5A (eIF5A) precursor". Biochem. J. 340 (1): 273–81. doi:10.1042/0264-6021:3400273. PMC 1220246. PMID 10229683.

Protein biosynthesis: translation (prokaryotic, eukaryotic)

Ribosomal proteins

Initiation factor

Prokaryotic

Archaeal

aIF1
aIF2
aIF5
aIF6

Eukaryotic

eIF1	EIF1AX AY 1B

eIF2	EIF2S1 EIF2S2 EIF2S3 EIF2B1 EIF2B2 EIF2B3 EIF2B4 EIF2B5 EIF-2 kinase

eIF3	EIF3A B C D F G H I J K M S6

eIF4	EIF4A2 A3 B E1 E2 G1 G2 G3 H

eIF5	EIF5A A2 B

eIF6	EIF6

Elongation factor

Prokaryotic	EF-Tu EF-Ts EF-G

Archaeal	aEF-1, aEF-2

Eukaryotic	EEF-1 EEF1A1 EEF1A2 EEF1A3 EEF1B1 EEF1B2 EEF1B3 EEF1B4 EEF1D EEF1E1 EEF1G EEF2

Release factor

Other

Other concepts

Index of genetics

Description	Gene expression DNA replication cycle recombination repair binding proteins Transcription factors regulators nucleic acids RNA RNA binding proteins ribonucleoproteins repeated sequence modification Translation ribosome modification nexins Proteins domains Structure primary secondary tertiary quaternary

Disease	Replication and repair Transcription factor Transcription Translation

EIF5A

References

Further reading