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DHPS

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DHPS

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1DHS, 1RLZ, 1ROZ, 1RQD

Identifiers

DHPS, deoxyhypusine synthase, DHS, DS, MIG13, NEDSSWI

External IDs

OMIM: 600944; MGI: 2683592; HomoloGene: 1453; GeneCards: DHPS; OMA:DHPS - orthologs

Gene location (Human)

Chr.	Chromosome 19 (human)^[1]

Band	19p13.13	Start	12,675,717 bp^[1]
Band	19p13.13	End	12,681,880 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 8 (mouse)^[2]

Band	8\|8 C3	Start	85,798,386 bp^[2]
Band	8\|8 C3	End	85,801,791 bp^[2]

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

right hemisphere of cerebellum

ganglionic eminence

primary visual cortex

pituitary gland

anterior pituitary

right uterine tube

left ovary

prostate

muscle of thigh

prefrontal cortex

Top expressed in

embryo

embryo

superior frontal gyrus

neural layer of retina

aortic valve

muscle of thigh

ascending aorta

supraoptic nucleus

epiblast

morula

More reference expression data


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

Species

Human

Mouse


1725


330817


ENSG00000095059


ENSMUSG00000060038


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

^[3]

^[4]

View/Edit Human

View/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 (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.^[6]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000095059 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000060038 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ ^a ^b "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. 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.

PDB gallery

1dhs: CRYSTAL STRUCTURE OF THE NAD COMPLEX OF HUMAN DEOXYHYPUSINE SYNTHASE
1rlz: Deoxyhypusine synthase holoenzyme in its high ionic strength, low pH crystal form
1roz: Deoxyhypusine synthase holoenzyme in its low ionic strength, high pH crystal form
1rqd: deoxyhypusine synthase holoenzyme in its low ionic strength, high pH crystal form with the inhibitor GC7 bound in the active site

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