DHPS

DHPS
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesDHPS, deoxyhypusine synthase, DHS, DS, MIG13
External IDsMGI: 2683592 HomoloGene: 1453 GeneCards: DHPS
EC number2.5.1.46
Gene location (Human)
Chr.Chromosome 19 (human)[1]
Band19p13.13Start12,675,717 bp[1]
End12,681,902 bp[1]
RNA expression pattern




More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

1725

330817

Ensembl

ENSG00000095059

ENSMUSG00000060038

UniProt

P49366

Q3TXU5

RefSeq (mRNA)

NM_001206974
NM_001930
NM_013406
NM_013407

NM_001039514
NM_201408

RefSeq (protein)

NP_001193903
NP_001921
NP_037538

NP_001034603

Location (UCSC)Chr 19: 12.68 – 12.68 MbChr 8: 85.07 – 85.08 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Deoxyhypusine synthase is an enzyme that in humans is encoded by the DHPS gene.[5][6]

The unusual amino acid hypusine is formed posttranslationally and is only found in a single cellular protein, eukaryotic translation initiation factor 5A. In the first step of hypusine biosynthesis, deoxyhypusine synthase catalyzes the NAD-dependent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the EIF5A precursor protein to form the intermediate deoxyhypusine residue. This gene consists of nine exons spanning 6.6 kb. Three transcript variants have been isolated. However, only transcript variant 1 encodes an active protein. The shorter variants may act as modulating factors of DHPS activity.[6]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000095059 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000060038 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ Joe YA, Wolff EC, Park MH (Oct 1995). "Cloning and expression of human deoxyhypusine synthase cDNA. Structure-function studies with the recombinant enzyme and mutant proteins". J Biol Chem. 270 (38): 22386–92. doi:10.1074/jbc.270.38.22386. PMID 7673224.
  6. 1 2 "Entrez Gene: DHPS deoxyhypusine synthase".

Further reading

  • Klier H, Csonga R, Steinkasserer A, et al. (1995). "Purification and characterization of human deoxyhypusine synthase from HeLa cells". FEBS Lett. 364 (2): 207–10. doi:10.1016/0014-5793(95)00394-O. PMID 7750572.
  • 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, Kappel B, Jaksche H, et al. (1996). "Molecular characterization of a cDNA encoding functional human deoxyhypusine synthase and chromosomal mapping of the corresponding gene locus". FEBS Lett. 378 (2): 195–8. doi:10.1016/0014-5793(95)01456-X. PMID 8549832.
  • Yan YP, Tao Y, Chen KY (1996). "Molecular cloning and functional expression of human deoxyhypusine synthase cDNA based on expressed sequence tag information". Biochem. J. 315 (2): 429–34. PMC 1217213. PMID 8615810.
  • Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
  • Jones T, Sheer D, Kapetanopoulos A, et al. (1996). "The gene coding for human deoxyhypusine synthase (DHPS) maps to chromosome 19p13.11-p13.12". Genomics. 35 (3): 635–7. doi:10.1006/geno.1996.0416. PMID 8812510.
  • Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
  • Liao DI, Wolff EC, Park MH, Davies DR (1998). "Crystal structure of the NAD complex of human deoxyhypusine synthase: an enzyme with a ball-and-chain mechanism for blocking the active site". Structure. 6 (1): 23–32. doi:10.1016/S0969-2126(98)00004-5. PMID 9493264.
  • Mantuano E, Trettel F, Olsen AS, et al. (1998). "Localization and genomic structure of human deoxyhypusine synthase gene on chromosome 19p13.2-distal 19p13.1". Gene. 215 (1): 153–7. doi:10.1016/S0378-1119(98)00254-6. PMID 9666110.
  • 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.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Ober D, Harms R, Witte L, Hartmann T (2003). "Molecular evolution by change of function. Alkaloid-specific homospermidine synthase retained all properties of deoxyhypusine synthase except binding the eIF5A precursor protein". J. Biol. Chem. 278 (15): 12805–12. doi:10.1074/jbc.M207112200. PMID 12562768.
  • Park JH, Wolff EC, Folk JE, Park MH (2003). "Reversal of the deoxyhypusine synthesis reaction. Generation of spermidine or homospermidine from deoxyhypusine by deoxyhypusine synthase". J. Biol. Chem. 278 (35): 32683–91. doi:10.1074/jbc.M304247200. PMID 12788913.
  • Kang KR, Chung SI (2004). "Protein kinase CK2 phosphorylates and interacts with deoxyhypusine synthase in HeLa cells". Exp. Mol. Med. 35 (6): 556–64. doi:10.1038/emm.2003.73. PMID 14749535.
  • Umland TC, Wolff EC, Park MH, Davies DR (2004). "A new crystal structure of deoxyhypusine synthase reveals the configuration of the active enzyme and of an enzyme.NAD.inhibitor ternary complex". J. Biol. Chem. 279 (27): 28697–705. doi:10.1074/jbc.M404095200. PMID 15100216.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
  • Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.


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