EIF5A

From Wikipedia, the free encyclopedia
Eukaryotic translation initiation factor 5A

Rendering based on PDB 1FH4.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsEIF5A; EIF-5A; EIF5A1; eIF5AI
External IDsOMIM: 600187 MGI: 106248 HomoloGene: 100947 GeneCards: EIF5A Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez1984276770
EnsemblENSG00000132507ENSMUSG00000078812
UniProtP63241P63242
RefSeq (mRNA)NM_001143760NM_001166589
RefSeq (protein)NP_001137232NP_001160061
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

  1. 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. 
  2. 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): 341350. doi:10.1007/s00726-007-0525-0. PMID 17476569. 
  3. 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): 25792590. doi:10.1074/jbc.M111.309633. PMID 22128152. 
  4. 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. doi:10.1038/nchembio.1001. PMID 22706199?. 

Further reading


This article is issued from Wikipedia. The text is available under the Creative Commons Attribution/Share Alike; additional terms may apply for the media files.