DHPS

This article is about the gene coding for the enzyme deoxyhypusine synthase. For another enzyme commonly abbreviated DHPS, see Dihydropteroate synthetase. For other uses, see DHPS (disambiguation).

DHPS
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1DHS, 1RLZ, 1ROZ, 1RQD
Identifiers
Aliases	DHPS, deoxyhypusine synthase, DHS, DS, MIG13, NEDSSWI
External IDs	OMIM: 600944 MGI: 2683592 HomoloGene: 1453 GeneCards: DHPS
EC number	2.5.1.46
Gene location (Human) Chr. Chromosome 19 (human) Band 19p13.13 Start 12,675,717 bp End 12,681,880 bp
Gene location (Mouse) Chr. Chromosome 8 (mouse) Band 8|8 C3 Start 85,798,386 bp End 85,801,791 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ganglionic eminence pituitary gland anterior pituitary right uterine tube prostate prefrontal cortex skeletal muscle tissue canal of the cervix fundus left lobe of thyroid gland Top expressed in superior frontal gyrus aortic valve ascending aorta supraoptic nucleus morula fossa facial motor nucleus condyle substantia nigra lip More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity protein binding identical protein binding deoxyhypusine synthase activity Cellular component cytosol cytoplasm Biological process protein homotetramerization protein biosynthesis positive regulation of T cell proliferation glucose homeostasis positive regulation of cell population proliferation spermidine metabolic process spermidine catabolic process peptidyl-lysine modification to peptidyl-hypusine Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1725 330817 Ensembl ENSG00000095059 ENSMUSG00000060038 UniProt P49366 Q3TXU5 RefSeq (mRNA) NM_001206974 NM_001930 NM_013406 NM_001369691 NM_001369692 NM_001369693 NM_001039514 NM_201408 RefSeq (protein) NP_001193903 NP_001921 NP_037538 NP_001356620 NP_001356621 NP_001356622 NP_001034603 Location (UCSC) Chr 19: 12.68 – 12.68 Mb Chr 8: 85.8 – 85.8 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Deoxyhypusine synthase is an enzyme that in humans is encoded by the DHPS gene.

The unusual amino acid hypusine is formed posttranslationally and is only found in a single cellular protein, eukaryotic translation initiation factor 5A (EIF5A, EIF5A2). 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.

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. S2CID 24485865.
• 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. doi:10.1016/S0021-9258(18)47333-4. 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. S2CID 39329481.
• 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. doi:10.1042/bj3150429. 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" (PDF). Gene. 215 (1): 153–7. doi:10.1016/S0378-1119(98)00254-6. hdl:2108/46188. 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• 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.