AKR7A2

AKR7A2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2BP1
Identifiers
Aliases	AKR7A2 , AFAR, AFAR1, AFB1-AR1, AKR7, aldo-keto reductase family 7, member A2, aldo-keto reductase family 7 member A2
External IDs	OMIM: 603418; MGI: 107796; HomoloGene: 2737; GeneCards: AKR7A2; OMA:AKR7A2 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1p36.13 Start 19,303,965 bp [1] End 19,312,144 bp [1]
Gene location (Mouse) Chr. Chromosome 4 (mouse) [2] Band 4 D3|4 70.64 cM Start 139,038,055 bp [2] End 139,045,737 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of transverse colon duodenum right adrenal gland right adrenal cortex right uterine tube left adrenal gland jejunal mucosa left adrenal cortex human kidney canal of the cervix Top expressed in right kidney proximal tubule left lobe of liver Paneth cell human kidney internal carotid artery crypt of lieberkuhn of small intestine external carotid artery right ventricle motor neuron More reference expression data BioGPS More reference expression data
Gene ontology Molecular function alditol:NADP+ 1-oxidoreductase activity electron transfer activity oxidoreductase activity phenanthrene-9,10-epoxide hydrolase activity aldo-keto reductase (NADP) activity protein binding Cellular component cytoplasm Golgi apparatus extracellular exosome cytosol Biological process xenobiotic metabolic process cellular aldehyde metabolic process daunorubicin metabolic process doxorubicin metabolic process carbohydrate metabolic process electron transport chain Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8574 110198 Ensembl ENSG00000053371 ENSMUSG00000028743 UniProt O43488 Q8CG76 RefSeq (mRNA) NM_003689 NM_001320979 NM_025337 RefSeq (protein) NP_001307908 NP_003680 NP_079613 Location (UCSC) Chr 1: 19.3 – 19.31 Mb Chr 4: 139.04 – 139.05 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Aflatoxin B1 aldehyde reductase member 2 is an enzyme that in humans is encoded by the AKR7A2 gene. ^{[5] [6]}

Function

Aldo-keto reductases, such as AKR7A2, are involved in the detoxification of aldehydes and ketones.[supplied by OMIM] ^[6]

References

1. GRCh38: Ensembl release 89: ENSG00000053371 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000028743 – 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. Ireland LS, Harrison DJ, Neal GE, Hayes JD (Aug 1998). "Molecular cloning, expression and catalytic activity of a human AKR7 member of the aldo-keto reductase superfamily: evidence that the major 2-carboxybenzaldehyde reductase from human liver is a homologue of rat aflatoxin B1-aldehyde reductase". Biochem J. 332 (1): 21–34. doi:10.1042/bj3320021. PMC   1219447 . PMID   9576847.
6. "Entrez Gene: AKR7A2 aldo-keto reductase family 7, member A2 (aflatoxin aldehyde reductase)".

External links

• Human AKR7A2 genome location and AKR7A2 gene details page in the UCSC Genome Browser .
• Overview of all the structural information available in the PDB for UniProt : O43488 (Human Aflatoxin B1 aldehyde reductase member 2 (AKR7A2)) at the PDBe-KB .

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.
• Praml C, Savelyeva L, Perri P, Schwab M (1998). "Cloning of the human aflatoxin B1-aldehyde reductase gene at 1p35-1p36.1 in a region frequently altered in human tumor cells". Cancer Res. 58 (22): 5014–8. PMID   9823300.
• Kelly VP, Sherratt PJ, Crouch DH, Hayes JD (2002). "Novel homodimeric and heterodimeric rat gamma-hydroxybutyrate synthases that associate with the Golgi apparatus define a distinct subclass of aldo-keto reductase 7 family proteins". Biochem. J. 366 (Pt 3): 847–61. doi:10.1042/BJ20020342. PMC   1222835 . PMID   12071861.
• 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.
• Praml C, Savelyeva L, Schwab M (2003). "Aflatoxin B1 aldehyde reductase (AFAR) genes cluster at 1p35-1p36.1 in a region frequently altered in human tumour cells". Oncogene. 22 (30): 4765–73. doi: 10.1038/sj.onc.1206684 . PMID   12879023.
• 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.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
• Jordanova A, Irobi J, Thomas FP, et al. (2006). "Disrupted function and axonal distribution of mutant tyrosyl-tRNA synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy" . Nat. Genet. 38 (2): 197–202. doi:10.1038/ng1727. PMID   16429158. S2CID   16668375.
• Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi: 10.1038/nature04727 . PMID   16710414.
• Lyon RC, Johnston SM, Watson DG, et al. (2007). "Synthesis and catabolism of gamma-hydroxybutyrate in SH-SY5Y human neuroblastoma cells: role of the aldo-keto reductase AKR7A2". J. Biol. Chem. 282 (36): 25986–92. doi: 10.1074/jbc.M702465200 . PMID   17591773.