DHPS: Difference between revisions

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{{about|the gene coding for the enzyme deoxyhypusine synthase|another enzyme commonly abbreviated DHPS|Dihydropteroate synthetase|other uses|DHPS (disambiguation)}}
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{{Infobox_gene}}
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'''Deoxyhypusine synthase''' is an [[enzyme]] that in humans is encoded by the ''DHPS'' [[gene]].<ref name="pmid7673224">{{cite journal | vauthors = Joe YA, Wolff EC, Park MH | title = Cloning and expression of human deoxyhypusine synthase cDNA. Structure-function studies with the recombinant enzyme and mutant proteins | journal = J Biol Chem | volume = 270 | issue = 38 | pages = 22386–92 |date=Oct 1995 | pmid = 7673224 | pmc =  | doi =  10.1074/jbc.270.38.22386}}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DHPS deoxyhypusine synthase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1725| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_DHPS_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dhs.
| PDB = {{PDB2|1dhs}}, {{PDB2|1rlz}}, {{PDB2|1roz}}, {{PDB2|1rqd}}
| Name = Deoxyhypusine synthase
| HGNCid = 2869
| Symbol = DHPS
| AltSymbols =; MIG13
| OMIM = 600944
| ECnumber = 
| Homologene = 1453
| MGIid = 2683592
| GeneAtlas_image1 = PBB_GE_DHPS_211558_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_DHPS_202802_at_tn.png
| GeneAtlas_image3 = PBB_GE_DHPS_207831_x_at_tn.png
| Function = {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006412 |text = translation}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0008612 |text = hypusine biosynthetic process from peptidyl-lysine}} {{GNF_GO|id=GO:0050983 |text = spermidine catabolic process to deoxyhypusine, using deoxyhypusine synthase}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1725
    | Hs_Ensembl = ENSG00000095059
    | Hs_RefseqProtein = NP_001921
    | Hs_RefseqmRNA = NM_001930
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 12647565
    | Hs_GenLoc_end = 12653716
    | Hs_Uniprot = P49366
    | Mm_EntrezGene = 330817
    | Mm_Ensembl = ENSMUSG00000060038
    | Mm_RefseqmRNA = NM_001039514
    | Mm_RefseqProtein = NP_001034603
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 87961862
    | Mm_GenLoc_end = 87965266
    | Mm_Uniprot =   
  }}
}}
'''Deoxyhypusine synthase''', also known as '''DHPS''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DHPS deoxyhypusine synthase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1725| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: DHPS deoxyhypusine synthase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1725| accessdate = }}</ref>
| summary_text = 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.<ref name="entrez"/>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Joe YA, Wolff EC, Park MH |title=Cloning and expression of human deoxyhypusine synthase cDNA. Structure-function studies with the recombinant enzyme and mutant proteins. |journal=J. Biol. Chem. |volume=270 |issue= 38 |pages= 22386-92 |year= 1995 |pmid= 7673224 |doi= }}
*{{cite journal  | author=Klier H |title=Purification and characterization of human deoxyhypusine synthase from HeLa cells |journal=FEBS Lett. |volume=364 |issue= 2 |pages= 207–10 |year= 1995 |pmid= 7750572 |doi=10.1016/0014-5793(95)00394-O |name-list-format=vanc| author2=Csonga R | author3=Steinkasserer A | display-authors=3  | last4=Wohl  | first4=T  | last5=Lottspeich  | first5=F  | last6=Eder  | first6=J  }}
*{{cite journal | author=Klier H, Csonga R, Steinkasserer A, ''et al.'' |title=Purification and characterization of human deoxyhypusine synthase from HeLa cells. |journal=FEBS Lett. |volume=364 |issue= 2 |pages= 207-10 |year= 1995 |pmid= 7750572 |doi=  }}
*{{cite journal  | vauthors=Joe YA, Park MH |title=Structural features of the eIF-5A precursor required for posttranslational synthesis of deoxyhypusine |journal=J. Biol. Chem. |volume=269 |issue= 41 |pages= 25916–21 |year= 1994 |pmid= 7929297 |doi=  }}
*{{cite journal  | author=Joe YA, Park MH |title=Structural features of the eIF-5A precursor required for posttranslational synthesis of deoxyhypusine. |journal=J. Biol. Chem. |volume=269 |issue= 41 |pages= 25916-21 |year= 1994 |pmid= 7929297 |doi=  }}
*{{cite journal  | author=Bevec D |title=Molecular characterization of a cDNA encoding functional human deoxyhypusine synthase and chromosomal mapping of the corresponding gene locus |journal=FEBS Lett. |volume=378 |issue= 2 |pages= 195–8 |year= 1996 |pmid= 8549832 |doi=10.1016/0014-5793(95)01456-X |name-list-format=vanc| author2=Kappel B  | author3=Jaksche H  | display-authors=3  | last4=Csonga | first4=R  | last5=Hauber  | first5=J  | last6=Klier | first6=H  | last7=Steinkasserer  | first7=A }}
*{{cite journal  | author=Bevec D, Kappel B, Jaksche H, ''et al.'' |title=Molecular characterization of a cDNA encoding functional human deoxyhypusine synthase and chromosomal mapping of the corresponding gene locus. |journal=FEBS Lett. |volume=378 |issue= 2 |pages= 195-8 |year= 1996 |pmid= 8549832 |doi= }}
*{{cite journal | vauthors=Yan YP, Tao Y, Chen KY |title=Molecular cloning and functional expression of human deoxyhypusine synthase cDNA based on expressed sequence tag information |journal=Biochem. J. |volume=315 |issue=  2|pages= 429–34 |year= 1996 |pmid= 8615810 |doi= | pmc=1217213  }}
*{{cite journal | author=Yan YP, Tao Y, Chen KY |title=Molecular cloning and functional expression of human deoxyhypusine synthase cDNA based on expressed sequence tag information. |journal=Biochem. J. |volume=315 ( Pt 2) |issue=  |pages= 429-34 |year= 1996 |pmid= 8615810 |doi= }}
*{{cite journal  | author=Andersson B |title=A "double adaptor" method for improved shotgun library construction |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107–13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 |name-list-format=vanc| author2=Wentland MA  | author3=Ricafrente JY  | display-authors=3  | last4=Liu  | first4=W  | last5=Gibbs  | first5=RA }}
*{{cite journal | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal  | author=Jones T |title=The gene coding for human deoxyhypusine synthase (DHPS) maps to chromosome 19p13.11-p13.12 |journal=Genomics |volume=35 |issue= 3 |pages= 635–7 |year= 1996 |pmid= 8812510 |doi= 10.1006/geno.1996.0416 |name-list-format=vanc| author2=Sheer D | author3=Kapetanopoulos A  | display-authors=3  | last4=Hauber  | first4=Joachim  | last5=Bevec  | first5=Dorian  | last6=Steinkasserer  | first6=Alexander }}
*{{cite journal  | author=Jones T, Sheer D, Kapetanopoulos A, ''et al.'' |title=The gene coding for human deoxyhypusine synthase (DHPS) maps to chromosome 19p13.11-p13.12. |journal=Genomics |volume=35 |issue= 3 |pages= 635-7 |year= 1996 |pmid= 8812510 |doi= 10.1006/geno.1996.0416 }}
*{{cite journal  | author=Yu W |title=Large-scale concatenation cDNA sequencing |journal=Genome Res. |volume=7 |issue= 4 |pages= 353–8 |year= 1997 |pmid= 9110174 |doi=  10.1101/gr.7.4.353| pmc=139146  |name-list-format=vanc| author2=Andersson B  | author3=Worley KC  | display-authors=3  | last4=Muzny  | first4=DM | last5=Ding | first5=Y  | last6=Liu  | first6=W  | last7=Ricafrente  | first7=JY  | last8=Wentland  | first8=MA  | last9=Lennon  | first9=G  }}
*{{cite journal | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi= }}
*{{cite journal  | vauthors=Liao DI, Wolff EC, Park MH, Davies DR |title=Crystal structure of the NAD complex of human deoxyhypusine synthase: an enzyme with a ball-and-chain mechanism for blocking the active site |journal=Structure |volume=6 |issue= 1 |pages= 23–32 |year= 1998 |pmid= 9493264 |doi=10.1016/S0969-2126(98)00004-5  }}
*{{cite journal  | author=Liao DI, Wolff EC, Park MH, Davies DR |title=Crystal structure of the NAD complex of human deoxyhypusine synthase: an enzyme with a ball-and-chain mechanism for blocking the active site. |journal=Structure |volume=6 |issue= 1 |pages= 23-32 |year= 1998 |pmid= 9493264 |doi=  }}
*{{cite journal  | author=Mantuano E |title=Localization and genomic structure of human deoxyhypusine synthase gene on chromosome 19p13.2-distal 19p13.1 |journal=Gene |volume=215 |issue= 1 |pages= 153–7 |year= 1998 |pmid= 9666110 |doi=10.1016/S0378-1119(98)00254-6 |name-list-format=vanc| author2=Trettel F  | author3=Olsen AS  | display-authors=3  | last4=Lennon  | first4=G  | last5=Frontali  | first5=M  | last6=Jodice  | first6=C  }}
*{{cite journal | author=Mantuano E, Trettel F, Olsen AS, ''et al.'' |title=Localization and genomic structure of human deoxyhypusine synthase gene on chromosome 19p13.2-distal 19p13.1. |journal=Gene |volume=215 |issue= 1 |pages= 153-7 |year= 1998 |pmid= 9666110 |doi=  }}
*{{cite journal  | author=Lee YB |title=Complex formation between deoxyhypusine synthase and its protein substrate, the eukaryotic translation initiation factor 5A (eIF5A) precursor |journal=Biochem. J. |volume=340 |issue= 1|pages= 273–81 |year= 1999 |pmid= 10229683 |doi=10.1042/0264-6021:3400273 | pmc=1220246 |name-list-format=vanc| author2=Joe YA  | author3=Wolff EC | display-authors=3  | last4=Dimitriadis  | first4=Emilios K. | last5=Park  | first5=Myung Hee  }}
*{{cite journal  | author=Lee YB, Joe YA, Wolff EC, ''et al.'' |title=Complex formation between deoxyhypusine synthase and its protein substrate, the eukaryotic translation initiation factor 5A (eIF5A) precursor. |journal=Biochem. J. |volume=340 ( Pt 1) |issue=  |pages= 273-81 |year= 1999 |pmid= 10229683 |doi=  }}
*{{cite journal  | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | vauthors=Ober D, Harms R, Witte L, Hartmann T |title=Molecular evolution by change of function. Alkaloid-specific homospermidine synthase retained all properties of deoxyhypusine synthase except binding the eIF5A precursor protein |journal=J. Biol. Chem. |volume=278 |issue= 15 |pages= 12805–12 |year= 2003 |pmid= 12562768 |doi= 10.1074/jbc.M207112200 }}
*{{cite journal | author=Ober D, Harms R, Witte L, Hartmann T |title=Molecular evolution by change of function. Alkaloid-specific homospermidine synthase retained all properties of deoxyhypusine synthase except binding the eIF5A precursor protein. |journal=J. Biol. Chem. |volume=278 |issue= 15 |pages= 12805-12 |year= 2003 |pmid= 12562768 |doi= 10.1074/jbc.M207112200 }}
*{{cite journal  | vauthors=Park JH, Wolff EC, Folk JE, Park MH |title=Reversal of the deoxyhypusine synthesis reaction. Generation of spermidine or homospermidine from deoxyhypusine by deoxyhypusine synthase |journal=J. Biol. Chem. |volume=278 |issue= 35 |pages= 32683–91 |year= 2003 |pmid= 12788913 |doi= 10.1074/jbc.M304247200 }}
*{{cite journal | author=Park JH, Wolff EC, Folk JE, Park MH |title=Reversal of the deoxyhypusine synthesis reaction. Generation of spermidine or homospermidine from deoxyhypusine by deoxyhypusine synthase. |journal=J. Biol. Chem. |volume=278 |issue= 35 |pages= 32683-91 |year= 2003 |pmid= 12788913 |doi= 10.1074/jbc.M304247200 }}
*{{cite journal  | vauthors=Kang KR, Chung SI |title=Protein kinase CK2 phosphorylates and interacts with deoxyhypusine synthase in HeLa cells |journal=Exp. Mol. Med. |volume=35 |issue= 6 |pages= 556–64 |year= 2004 |pmid= 14749535 |doi=  10.1038/emm.2003.73}}
*{{cite journal  | author=Kang KR, Chung SI |title=Protein kinase CK2 phosphorylates and interacts with deoxyhypusine synthase in HeLa cells. |journal=Exp. Mol. Med. |volume=35 |issue= 6 |pages= 556-64 |year= 2004 |pmid= 14749535 |doi=  }}
*{{cite journal  | vauthors=Umland TC, Wolff EC, Park MH, Davies DR |title=A new crystal structure of deoxyhypusine synthase reveals the configuration of the active enzyme and of an enzyme.NAD.inhibitor ternary complex |journal=J. Biol. Chem. |volume=279 |issue= 27 |pages= 28697–705 |year= 2004 |pmid= 15100216 |doi= 10.1074/jbc.M404095200 }}
*{{cite journal | author=Umland TC, Wolff EC, Park MH, Davies DR |title=A new crystal structure of deoxyhypusine synthase reveals the configuration of the active enzyme and of an enzyme.NAD.inhibitor ternary complex. |journal=J. Biol. Chem. |volume=279 |issue= 27 |pages= 28697-705 |year= 2004 |pmid= 15100216 |doi= 10.1074/jbc.M404095200 }}
*{{cite journal  | author=Gerhard DS |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928  |name-list-format=vanc| author2=Wagner L  | author3=Feingold EA  | display-authors=3  | last4=Shenmen  | first4=CM  | last5=Grouse  | first5=LH  | last6=Schuler  | first6=G  | last7=Klein  | first7=SL  | last8=Old  | first8=S  | last9=Rasooly  | first9=R }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Rual JF |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209  |name-list-format=vanc| author2=Venkatesan K  | author3=Hao T  | display-authors=3  | last4=Hirozane-Kishikawa  | first4=Tomoko  | last5=Dricot  | first5=Amélie  | last6=Li  | first6=Ning  | last7=Berriz  | first7=Gabriel F.  | last8=Gibbons  | first8=Francis D.  | last9=Dreze  | first9=Matija }}
*{{cite journal | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal  | author=Ewing RM |title=Large-scale mapping of human protein-protein interactions by mass spectrometry |journal=Mol. Syst. Biol. |volume=3 |issue=  1|pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134  | pmc=1847948  |name-list-format=vanc| author2=Chu P  | author3=Elisma F  | display-authors=3  | last4=Li  | first4=Hongyan  | last5=Taylor  | first5=Paul  | last6=Climie  | first6=Shane  | last7=McBroom-Cerajewski  | first7=Linda  | last8=Robinson  | first8=Mark D | last9=O'Connor | first9=Liam }}
*{{cite journal | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue= |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 }}
}}
}}
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{{refend}}
{{PDB Gallery|geneid=1725}}
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Latest revision as of 18:25, 30 August 2017

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).
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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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Wikidata
View/Edit Human

Deoxyhypusine synthase is an enzyme that in humans is encoded by the DHPS gene.[1][2]

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.[2]

References

  1. ↑ 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.
  2. ↑ 2.0 2.1 "Entrez Gene: DHPS deoxyhypusine synthase".

Further reading



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