HSD17B6: Difference between revisions

HSD17B6
Identifiers
Aliases	HSD17B6, HSE, RODH, SDR9C6, hydroxysteroid (17-beta) dehydrogenase 6, hydroxysteroid 17-beta dehydrogenase 6
External IDs	OMIM: 606623; MGI: 1351670; HomoloGene: 20811; GeneCards: HSD17B6; OMA:HSD17B6 - orthologs
Gene location (Human)
Chr.	Chromosome 12 (human)
End	56,787,790 bp
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)
End	127,843,480 bp
RNA expression pattern
	Top expressed in
	right lobe of liver; ; lower lobe of lung; ; seminal vesicula; ; parietal pleura; ; spleen; ; canal of the cervix; ; saphenous vein; ; caudate nucleus; ; nucleus accumbens; ; prostate;
	Top expressed in
	left lobe of liver; ; duodenum; ; olfactory epithelium; ; jejunum; ; morula; ; intestinal villus; ; pyloric antrum; ; blastocyst; ; epithelium of stomach; ; mucous cell of stomach;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	electron transfer activity; oxidoreductase activity; estradiol 17-beta-dehydrogenase activity; catalytic activity; testosterone dehydrogenase (NAD+) activity; NAD-retinol dehydrogenase activity;
Cellular component	organelle membrane; endosome; early endosome membrane; intracellular anatomical structure; endoplasmic reticulum; membrane; intracellular membrane-bounded organelle;
Biological process	androgen biosynthetic process; androgen catabolic process; steroid metabolic process; lipid metabolism; electron transport chain;
	Sources:Amigo / QuickGO
Orthologs
	8630
	27400
	ENSG00000025423
	ENSMUSG00000025396
	O14756
	Q9R092
	NM_003725
	NM_013786; NM_001359377
	NP_003716
	NP_038814; NP_001346306
	Wikidata
View/Edit Human	View/Edit Mouse

Browse history interactively

← Previous edit

Content deleted Content added

VisualWikitext

Inline

Latest revision as of 15:09, 2 April 2024

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

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000025423 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000025396 – 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.
^ 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.
^ 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.
^ ^a ^b "Entrez Gene: HSD17B6 hydroxysteroid (17-beta) dehydrogenase 6 homolog (mouse)".

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

This article on a gene on human chromosome 12 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000025423 – Ensembl, May 2017

[refGRCm38Ensembl-2] 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.

[pmid11165032-5] 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.

[pmid19027726-6] 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.

[entrez-7] "Entrez Gene: HSD17B6 hydroxysteroid (17-beta) dehydrogenase 6 homolog (mouse)".

[1]

[2]

[3]

[4]

[5]

[6]

[7]

@@ Line 1: / Line 1: @@
+{{cs1 config|name-list-style=vanc}}
-{{PBB|geneid=8630}}
+{{Infobox_gene}}
-'''Hydroxysteroid (17-beta) dehydrogenase 6 homolog (mouse)''', also known as '''HSD17B6''', is a human [[gene]].<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>
+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" />
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
-{{PBB_Summary
-| section_title =
-| 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>
-}}
 ==References==
 {{reflist}}
 ==Further reading==
 {{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=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 |pmid= 11165032 |doi=10.1016/S0303-7207(00)00414-7  }}
+*{{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=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=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=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=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=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=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=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=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=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=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=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  | 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}}
-{{gene-12-stub}}
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{gene-12-stub}}
-{{PBB_Controls
-| update_page = yes
-| require_manual_inspection = no
-| update_protein_box = yes
-| update_summary = yes
-| update_citations = yes
-}}