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edited opening sentence to make clear that article is about both protein and the gene that encodes it
Added the cs1 style template to denote Vancouver ("vanc") citation style, because references contain "vauthors" attribute to specify the list of authors. Added bibcode. | Use this tool. Report bugs. | #UCB_Gadget
 
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'''Hydroxysteroid 17-beta dehydrogenase 6''' is an [[enzyme]] that in humans is encoded by the ''HSD17B6'' [[gene]].<ref name="pmid11165032">{{cite journal | author = Baker ME | title = Evolution of 17beta-hydroxysteroid dehydrogenases and their role in androgen, estrogen and retinoid action | journal = Mol Cell Endocrinol | volume = 171 | issue = 1-2 | pages = 211-5 | year = 2001 | month = Feb | pmid = 11165032 | pmc = | doi = }}</ref><ref name="pmid19027726">{{cite journal | author = Persson B, Kallberg Y, Bray JE, Bruford E, Dellaporta SL, Favia AD, Duarte RG, Jornvall H, Kavanagh KL, Kedishvili N, Kisiela M, Maser E, Mindnich R, Orchard S, Penning TM, Thornton JM, Adamski J, Oppermann U | title = The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative | journal = Chem Biol Interact | volume = 178 | issue = 1-3 | pages = 94-8 | year = 2009 | month = Feb | pmid = 19027726 | pmc = | doi = 10.1016/j.cbi.2008.10.040 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: HSD17B6 hydroxysteroid (17-beta) dehydrogenase 6 homolog (mouse)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8630| accessdate = }}</ref>
'''Hydroxysteroid 17-beta dehydrogenase 6''' is an [[enzyme]] that in humans is encoded by the ''HSD17B6'' [[gene]].<ref name="pmid11165032">{{cite journal | author = Baker ME | title = Evolution of 17beta-hydroxysteroid dehydrogenases and their role in androgen, estrogen and retinoid action | journal = Mol Cell Endocrinol | volume = 171 | issue = 1–2 | pages = 211–5 |date=Feb 2001 | pmid = 11165032 | doi =10.1016/S0303-7207(00)00414-7 | s2cid = 42947381 }}</ref><ref name="pmid19027726">{{cite journal |vauthors=Persson B, Kallberg Y, Bray JE, Bruford E, Dellaporta SL, Favia AD, Duarte RG, Jornvall H, Kavanagh KL, Kedishvili N, Kisiela M, Maser E, Mindnich R, Orchard S, Penning TM, Thornton JM, Adamski J, Oppermann U | title = The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative | journal = Chem Biol Interact | volume = 178 | issue = 1–3 | pages = 94–8 |date=Feb 2009 | pmid = 19027726 | pmc = 2896744| doi = 10.1016/j.cbi.2008.10.040 | bibcode = 2009CBI...178...94P }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: HSD17B6 hydroxysteroid (17-beta) dehydrogenase 6 homolog (mouse)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8630}}</ref>


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The protein encoded by this gene has both oxidoreductase and epimerase activities and is involved in androgen catabolism. The oxidoreductase activity can convert 3 alpha-adiol to dihydrotestosterone, while the epimerase activity can convert androsterone to epi-androsterone. Both reactions use NAD+ as the preferred cofactor. This gene is a member of the retinol dehydrogenase family. Transcript variants utilizing alternative polyadenylation signals exist.<ref name="entrez" />
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| summary_text = The protein encoded by this gene has both oxidoreductase and epimerase activities and is involved in androgen catabolism. The oxidoreductase activity can convert 3 alpha-adiol to dihydrotestosterone, while the epimerase activity can convert androsterone to epi-androsterone. Both reactions use NAD+ as the preferred cofactor. This gene is a member of the retinol dehydrogenase family. Transcript variants utilizing alternative polyadenylation signals exist.<ref name="entrez">{{cite web | title = Entrez Gene: HSD17B6 hydroxysteroid (17-beta) dehydrogenase 6 homolog (mouse)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8630| accessdate = }}</ref>
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==References==
==References==
{{reflist}}
{{reflist}}

==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
*{{cite journal |vauthors=Biswas MG, Russell DW |title=Expression cloning and characterization of oxidative 17beta- and 3alpha-hydroxysteroid dehydrogenases from rat and human prostate |journal=J. Biol. Chem. |volume=272 |issue= 25 |pages= 15959–66 |year= 1997 |pmid= 9188497 |doi=10.1074/jbc.272.25.15959 |doi-access=free }}
{{PBB_Further_reading
*{{cite journal |vauthors=Huang XF, Luu-The V |title=Molecular characterization of a first human 3(alpha-->beta)-hydroxysteroid epimerase |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29452–7 |year= 2000 |pmid= 10896656 |doi= 10.1074/jbc.M000562200 |doi-access= free }}
| citations =
*{{cite journal | author=Biswas MG, Russell DW |title=Expression cloning and characterization of oxidative 17beta- and 3alpha-hydroxysteroid dehydrogenases from rat and human prostate. |journal=J. Biol. Chem. |volume=272 |issue= 25 |pages= 15959–66 |year= 1997 |pmid= 9188497 |doi=10.1074/jbc.272.25.15959 }}
*{{cite journal |vauthors=Kedishvili NY, Belyaeva OV, Gough WH |title=Cloning of the human RoDH-related short chain dehydrogenase gene and analysis of its structure |journal=Chem. Biol. Interact. |volume=130-132 |issue= 1–3 |pages= 457–67 |year= 2001 |pmid= 11306067 |doi=10.1016/S0009-2797(00)00291-X }}
*{{cite journal | author=Huang XF, Luu-The V |title=Molecular characterization of a first human 3(alpha-->beta)-hydroxysteroid epimerase. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29452–7 |year= 2000 |pmid= 10896656 |doi= 10.1074/jbc.M000562200 }}
*{{cite journal |vauthors=Chetyrkin SV, Hu J, Gough WH, etal |title=Further characterization of human microsomal 3alpha-hydroxysteroid dehydrogenase |journal=Arch. Biochem. Biophys. |volume=386 |issue= 1 |pages= 1–10 |year= 2001 |pmid= 11360992 |doi= 10.1006/abbi.2000.2203 }}
*{{cite journal | author=Kedishvili NY, Belyaeva OV, Gough WH |title=Cloning of the human RoDH-related short chain dehydrogenase gene and analysis of its structure. |journal=Chem. Biol. Interact. |volume=130-132 |issue= 1-3 |pages= 457–67 |year= 2001 |pmid= 11306067 |doi=10.1016/S0009-2797(00)00291-X }}
*{{cite journal |vauthors=Huang XF, Luu-The V |title=Gene structure, chromosomal localization and analysis of 3-ketosteroid reductase activity of the human 3(alpha-->beta)-hydroxysteroid epimerase |journal=Biochim. Biophys. Acta |volume=1520 |issue= 2 |pages= 124–30 |year= 2001 |pmid= 11513953 |doi= 10.1016/s0167-4781(01)00247-0}}
*{{cite journal | author=Chetyrkin SV, Hu J, Gough WH, ''et al.'' |title=Further characterization of human microsomal 3alpha-hydroxysteroid dehydrogenase. |journal=Arch. Biochem. Biophys. |volume=386 |issue= 1 |pages= 1–10 |year= 2001 |pmid= 11360992 |doi= 10.1006/abbi.2000.2203 }}
*{{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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 |bibcode=2002PNAS...9916899M |doi-access=free }}
*{{cite journal | author=Huang XF, Luu-The V |title=Gene structure, chromosomal localization and analysis of 3-ketosteroid reductase activity of the human 3(alpha-->beta)-hydroxysteroid epimerase. |journal=Biochim. Biophys. Acta |volume=1520 |issue= 2 |pages= 124–30 |year= 2001 |pmid= 11513953 |doi= }}
*{{cite journal |vauthors=Jones MR, Italiano L, Wilson SG, etal |title=Polymorphism in HSD17B6 is associated with key features of polycystic ovary syndrome |journal=Fertil. Steril. |volume=86 |issue= 5 |pages= 1438–46 |year= 2006 |pmid= 17070195 |doi= 10.1016/j.fertnstert.2006.04.027 |doi-access= free }}
*{{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=Belyaeva OV, Chetyrkin SV, Clark AL, etal |title=Role of microsomal retinol/sterol dehydrogenase-like short-chain dehydrogenases/reductases in the oxidation and epimerization of 3alpha-hydroxysteroids in human tissues |journal=Endocrinology |volume=148 |issue= 5 |pages= 2148–56 |year= 2007 |pmid= 17289849 |doi= 10.1210/en.2006-1491 | pmc=2571913 }}
*{{cite journal | author=Jones MR, Italiano L, Wilson SG, ''et al.'' |title=Polymorphism in HSD17B6 is associated with key features of polycystic ovary syndrome. |journal=Fertil. Steril. |volume=86 |issue= 5 |pages= 1438–46 |year= 2006 |pmid= 17070195 |doi= 10.1016/j.fertnstert.2006.04.027 }}
*{{cite journal | author=Belyaeva OV, Chetyrkin SV, Clark AL, ''et al.'' |title=Role of microsomal retinol/sterol dehydrogenase-like short-chain dehydrogenases/reductases in the oxidation and epimerization of 3alpha-hydroxysteroids in human tissues. |journal=Endocrinology |volume=148 |issue= 5 |pages= 2148–56 |year= 2007 |pmid= 17289849 |doi= 10.1210/en.2006-1491 }}
}}
{{refend}}
{{refend}}


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Latest revision as of 15:09, 2 April 2024

HSD17B6
Identifiers
AliasesHSD17B6, HSE, RODH, SDR9C6, hydroxysteroid (17-beta) dehydrogenase 6, hydroxysteroid 17-beta dehydrogenase 6
External IDsOMIM: 606623; MGI: 1351670; HomoloGene: 20811; GeneCards: HSD17B6; OMA:HSD17B6 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

8630

27400

Ensembl

ENSG00000025423

ENSMUSG00000025396

UniProt

O14756

Q9R092

RefSeq (mRNA)

NM_003725

NM_013786
NM_001359377

RefSeq (protein)

NP_003716

NP_038814
NP_001346306

Location (UCSC)Chr 12: 56.75 – 56.79 MbChr 10: 127.83 – 127.84 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Hydroxysteroid 17-beta dehydrogenase 6 is an enzyme that in humans is encoded by the HSD17B6 gene.[5][6][7]

The protein encoded by this gene has both oxidoreductase and epimerase activities and is involved in androgen catabolism. The oxidoreductase activity can convert 3 alpha-adiol to dihydrotestosterone, while the epimerase activity can convert androsterone to epi-androsterone. Both reactions use NAD+ as the preferred cofactor. This gene is a member of the retinol dehydrogenase family. Transcript variants utilizing alternative polyadenylation signals exist.[7]

References

[edit]
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000025423 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025396 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Baker ME (Feb 2001). "Evolution of 17beta-hydroxysteroid dehydrogenases and their role in androgen, estrogen and retinoid action". Mol Cell Endocrinol. 171 (1–2): 211–5. doi:10.1016/S0303-7207(00)00414-7. PMID 11165032. S2CID 42947381.
  6. ^ Persson B, Kallberg Y, Bray JE, Bruford E, Dellaporta SL, Favia AD, Duarte RG, Jornvall H, Kavanagh KL, Kedishvili N, Kisiela M, Maser E, Mindnich R, Orchard S, Penning TM, Thornton JM, Adamski J, Oppermann U (Feb 2009). "The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative". Chem Biol Interact. 178 (1–3): 94–8. Bibcode:2009CBI...178...94P. doi:10.1016/j.cbi.2008.10.040. PMC 2896744. PMID 19027726.
  7. ^ a b "Entrez Gene: HSD17B6 hydroxysteroid (17-beta) dehydrogenase 6 homolog (mouse)".

Further reading

[edit]


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