HSD17B12

Protein-coding gene in the species Homo sapiens

HSD17B12
Identifiers
AliasesHSD17B12, KAR, SDR12C1, hydroxysteroid (17-beta) dehydrogenase 12, hydroxysteroid 17-beta dehydrogenase 12
External IDsOMIM: 609574; MGI: 1926967; HomoloGene: 95094; GeneCards: HSD17B12; OMA:HSD17B12 - orthologs
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for HSD17B12
Genomic location for HSD17B12
Band11p11.2Start43,680,680 bp[1]
End43,856,617 bp[1]
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)[2]
Chromosome 2 (mouse)
Genomic location for HSD17B12
Genomic location for HSD17B12
Band2|2 E1Start93,863,034 bp[2]
End93,988,309 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • endothelial cell

  • retinal pigment epithelium

  • pancreatic ductal cell

  • optic nerve

  • pars reticulata

  • inferior ganglion of vagus nerve

  • cardia

  • renal medulla

  • spinal ganglia

  • Pars compacta
Top expressed in
  • skin of external ear

  • brown adipose tissue

  • transitional epithelium of urinary bladder

  • cumulus cell

  • tunica adventitia of aorta

  • left lobe of liver

  • ciliary body

  • iris

  • sciatic nerve

  • lip
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • heparin binding
  • estradiol 17-beta-dehydrogenase activity
  • oxidoreductase activity
  • collagen binding
  • fibronectin binding
  • protein binding
  • 3-oxo-lignoceroyl-CoA reductase activity
  • 3-oxo-behenoyl-CoA reductase activity
  • long-chain-3-hydroxyacyl-CoA dehydrogenase activity
  • 3-oxo-arachidoyl-CoA reductase activity
  • 3-oxo-cerotoyl-CoA reductase activity
Cellular component
  • integral component of membrane
  • membrane
  • endoplasmic reticulum
  • endoplasmic reticulum membrane
  • extracellular matrix
Biological process
  • lipid metabolism
  • extracellular matrix organization
  • long-chain fatty-acyl-CoA biosynthetic process
  • positive regulation of cell-substrate adhesion
  • fatty acid biosynthetic process
  • estrogen biosynthetic process
  • steroid biosynthetic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

51144

56348

Ensembl

ENSG00000149084

ENSMUSG00000027195

UniProt

Q53GQ0

O70503

RefSeq (mRNA)

NM_016142

NM_019657

RefSeq (protein)

NP_057226

NP_062631

Location (UCSC)Chr 11: 43.68 – 43.86 MbChr 2: 93.86 – 93.99 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Estradiol 17-beta-dehydrogenase 12 is an enzyme that in humans is encoded by the HSD17B12 gene.[5][6][7]

The enzyme 17-beta hydroxysteroid dehydrogenase-12 (HSD17B12) uses NADPH to reduce 3-ketoacyl-CoA to 3-hydroxyacyl-CoA during the second step of fatty acid elongation.[supplied by OMIM][7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000149084 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027195 – 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. ^ Moon YA, Horton JD (Feb 2003). "Identification of two mammalian reductases involved in the two-carbon fatty acyl elongation cascade". J Biol Chem. 278 (9): 7335–43. doi:10.1074/jbc.M211684200. PMID 12482854.
  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: HSD17B12 hydroxysteroid (17-beta) dehydrogenase 12".

Further reading

  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • 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.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Suzuki Y, Yamashita R, Shirota M, et al. (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.
  • 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.
  • Gnatenko DV, Cupit LD, Huang EC, et al. (2005). "Platelets express steroidogenic 17beta-hydroxysteroid dehydrogenases. Distinct profiles predict the essential thrombocythemic phenotype". Thromb. Haemost. 94 (2): 412–21. doi:10.1160/TH05-01-0037. PMID 16113833. S2CID 257259321.
  • Luu-The V, Tremblay P, Labrie F (2006). "Characterization of type 12 17beta-hydroxysteroid dehydrogenase, an isoform of type 3 17beta-hydroxysteroid dehydrogenase responsible for estradiol formation in women". Mol. Endocrinol. 20 (2): 437–43. doi:10.1210/me.2005-0058. PMID 16166196.
  • Sakurai N, Miki Y, Suzuki T, et al. (2006). "Systemic distribution and tissue localizations of human 17beta-hydroxysteroid dehydrogenase type 12". J. Steroid Biochem. Mol. Biol. 99 (4–5): 174–81. doi:10.1016/j.jsbmb.2006.01.010. PMID 16621523. S2CID 22249124.


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