AKR1B10

Protein-coding gene in the species Homo sapiens
AKR1B10
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1ZUA, 4GA8, 4GAB, 4GQ0, 4GQG, 4I5X, 4ICC, 4JIH, 4JII, 4WEV, 4XZL, 4XZN, 4XZM

Identifiers
AliasesAKR1B10, AKR1B11, AKR1B12, ALDRLn, ARL-1, ARL1, HIS, HSI, aldo-keto reductase family 1, member B10 (aldose reductase), aldo-keto reductase family 1 member B10
External IDsOMIM: 604707; MGI: 107673; HomoloGene: 116462; GeneCards: AKR1B10; OMA:AKR1B10 - orthologs
Gene location (Human)
Chromosome 7 (human)
Chr.Chromosome 7 (human)[1]
Chromosome 7 (human)
Genomic location for AKR1B10
Genomic location for AKR1B10
Band7q33Start134,527,567 bp[1]
End134,541,412 bp[1]
Gene location (Mouse)
Chromosome 6 (mouse)
Chr.Chromosome 6 (mouse)[2]
Chromosome 6 (mouse)
Genomic location for AKR1B10
Genomic location for AKR1B10
Band6 B1|6 14.91 cMStart34,331,054 bp[2]
End34,345,398 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • jejunal mucosa

  • mucosa of ileum

  • gums

  • gingival epithelium

  • mucosa of transverse colon

  • gallbladder

  • pancreatic ductal cell

  • gastric mucosa

  • islet of Langerhans

  • mucosa of sigmoid colon
Top expressed in
  • pyloric antrum

  • mucous cell of stomach

  • adrenal gland

  • Scarpa's ganglion

  • epithelium of stomach

  • blastocyst

  • endothelial cell of lymphatic vessel

  • Gonadal ridge

  • stroma of bone marrow

  • duodenum
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • retinal dehydrogenase activity
  • geranylgeranyl reductase activity
  • indanol dehydrogenase activity
  • aldo-keto reductase (NADP) activity
  • protein binding
  • oxidoreductase activity
  • alditol:NADP+ 1-oxidoreductase activity
  • alcohol dehydrogenase (NADP+) activity
  • NADP-retinol dehydrogenase activity
  • allyl-alcohol dehydrogenase activity
Cellular component
  • cytosol
  • extracellular region
  • lysosome
  • mitochondrion
Biological process
  • daunorubicin metabolic process
  • doxorubicin metabolic process
  • retinoid metabolic process
  • farnesol catabolic process
  • retinol metabolic process
  • cellular detoxification of aldehyde
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

57016

14187

Ensembl

ENSG00000198074

ENSMUSG00000029762

UniProt

O60218

P45377

RefSeq (mRNA)

NM_020299

NM_008012

RefSeq (protein)

NP_064695

NP_032038

Location (UCSC)Chr 7: 134.53 – 134.54 MbChr 6: 34.33 – 34.35 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Aldo-keto reductase family 1 member B10 is an enzyme that in humans is encoded by the AKR1B10 gene.[5][6][7]

This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. This member can efficiently reduce aliphatic and aromatic aldehydes, and it is less active on hexoses. It is highly expressed in adrenal gland, small intestine, and colon, and may play an important role in liver carcinogenesis.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000198074 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029762 – 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. ^ Hyndman DJ, Flynn TG (August 1998). "Sequence and expression levels in human tissues of a new member of the aldo-keto reductase family". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1399 (2–3): 198–202. doi:10.1016/s0167-4781(98)00109-2. PMID 9765596.
  6. ^ Cao D, Fan ST, Chung SS (May 1998). "Identification and characterization of a novel human aldose reductase-like gene". The Journal of Biological Chemistry. 273 (19): 11429–35. doi:10.1074/jbc.273.19.11429. PMID 9565553.
  7. ^ a b "Entrez Gene: AKR1B10 aldo-keto reductase family 1, member B10 (aldose reductase)".

External links

Further reading

  • Scuric Z, Stain SC, Anderson WF, Hwang JJ (April 1998). "New member of aldose reductase family proteins overexpressed in human hepatocellular carcinoma". Hepatology. 27 (4): 943–50. doi:10.1002/hep.510270408. PMID 9537432. S2CID 23740299.
  • Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, et al. (December 2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proceedings of the National Academy of Sciences of the United States of America. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Crosas B, Hyndman DJ, Gallego O, Martras S, Parés X, Flynn TG, Farrés J (August 2003). "Human aldose reductase and human small intestine aldose reductase are efficient retinal reductases: consequences for retinoid metabolism". The Biochemical Journal. 373 (Pt 3): 973–9. doi:10.1042/BJ20021818. PMC 1223539. PMID 12732097.
  • Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, et al. (October 2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Research. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Petrovic MG, Peterlin B, Hawlina M, Petrovic D (2005). "Aldose reductase (AC)n gene polymorphism and susceptibility to diabetic retinopathy in Type 2 diabetes in Caucasians". Journal of Diabetes and Its Complications. 19 (2): 70–3. doi:10.1016/j.jdiacomp.2004.08.004. PMID 15745835.
  • Kang ES, Kim HJ, Paek KS, Jang HS, Chang KC, Lee JH, et al. (May 2005). "Phorbol ester up-regulates aldose reductase expression in A549 cells: a potential role for aldose reductase in cell cycle modulation". Cellular and Molecular Life Sciences. 62 (10): 1146–55. doi:10.1007/s00018-005-5024-4. PMID 15928807. S2CID 13502923.
  • Lee YS, Paek KS, Kang ES, Jang HS, Kim HJ, Kang YJ, et al. (November 2005). "Involvement of nuclear factor kappaB in up-regulation of aldose reductase gene expression by 12-O-tetradecanoylphorbol-13-acetate in HeLa cells". The International Journal of Biochemistry & Cell Biology. 37 (11): 2297–309. doi:10.1016/j.biocel.2005.04.016. PMID 15936242.
  • Vikramadithyan RK, Hu Y, Noh HL, Liang CP, Hallam K, Tall AR, et al. (September 2005). "Human aldose reductase expression accelerates diabetic atherosclerosis in transgenic mice". The Journal of Clinical Investigation. 115 (9): 2434–43. doi:10.1172/JCI24819. PMC 1190371. PMID 16127462.
  • Hazemann I, Dauvergne MT, Blakeley MP, Meilleur F, Haertlein M, Van Dorsselaer A, et al. (October 2005). "High-resolution neutron protein crystallography with radically small crystal volumes: application of perdeuteration to human aldose reductase". Acta Crystallographica. Section D, Biological Crystallography. 61 (Pt 10): 1413–7. Bibcode:2005AcCrD..61.1413H. doi:10.1107/S0907444905024285. PMID 16204895.
  • Mashkova TD, Oparina NI, Zinov'eva OL, Kropotova ES, Dubovaia VI, Poltaraus AB, et al. (2007). "[Transcription TIMP3, DAPk1 and AKR1B10 genes in squamous cell lung cancer]". Molekuliarnaia Biologiia. 40 (6): 1047–54. doi:10.1134/s0026893306060148. PMID 17209433. S2CID 39287274.
  • Tammali R, Ramana KV, Srivastava SK (July 2007). "Aldose reductase regulates TNF-alpha-induced PGE2 production in human colon cancer cells". Cancer Letters. 252 (2): 299–306. doi:10.1016/j.canlet.2007.01.001. PMC 1945127. PMID 17300864.
  • Yan R, Zu X, Ma J, Liu Z, Adeyanju M, Cao D (November 2007). "Aldo-keto reductase family 1 B10 gene silencing results in growth inhibition of colorectal cancer cells: Implication for cancer intervention". International Journal of Cancer. 121 (10): 2301–6. doi:10.1002/ijc.22933. PMID 17597105. S2CID 1546354.

External links

  • PDBe-KB provides an overview of all the structure information available in the PDB for Human Aldo-keto reductase family 1 member B10 (AKR1B10)]
  • v
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  • 1zua: Crystal Structure Of AKR1B10 Complexed With NADP+ And Tolrestat
    1zua: Crystal Structure Of AKR1B10 Complexed With NADP+ And Tolrestat
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1.1.1: NAD/NADP acceptor
1.1.2: cytochrome acceptor
  • D-lactate dehydrogenase (cytochrome)
  • D-lactate dehydrogenase (cytochrome c-553)
  • Mannitol dehydrogenase (cytochrome)
1.1.3: oxygen acceptor
1.1.4: disulfide as acceptor
1.1.5: quinone/similar acceptor
1.1.99: other acceptors
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