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Wikipedia

AKR7A2

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

AKR7A2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesAKR7A2, AFAR, AFAR1, AFB1-AR1, AKR7, aldo-keto reductase family 7, member A2, aldo-keto reductase family 7 member A2
External IDsOMIM: 603418; MGI: 107796; HomoloGene: 2737; GeneCards: AKR7A2; OMA:AKR7A2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003689
NM_001320979

NM_025337

RefSeq (protein)

NP_001307908
NP_003680

NP_079613

Location (UCSC)Chr 1: 19.3 – 19.31 MbChr 4: 139.04 – 139.05 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function edit

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

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000053371 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b "Entrez Gene: AKR7A2 aldo-keto reductase family 7, member A2 (aflatoxin aldehyde reductase)".

External links edit

  • 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 edit

  • 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.


akr7a2, aflatoxin, aldehyde, reductase, member, enzyme, that, humans, encoded, gene, available, structurespdbortholog, search, pdbe, rcsblist, codes2bp1identifiersaliases, afar, afar1, afb1, akr7, aldo, keto, reductase, family, member, aldo, keto, reductase, f. Aflatoxin B1 aldehyde reductase member 2 is an enzyme that in humans is encoded by the AKR7A2 gene 5 6 AKR7A2Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes2BP1IdentifiersAliasesAKR7A2 AFAR AFAR1 AFB1 AR1 AKR7 aldo keto reductase family 7 member A2 aldo keto reductase family 7 member A2External IDsOMIM 603418 MGI 107796 HomoloGene 2737 GeneCards AKR7A2 OMA AKR7A2 orthologsGene location Human Chr Chromosome 1 human 1 Band1p36 13Start19 303 965 bp 1 End19 312 144 bp 1 Gene location Mouse Chr Chromosome 4 mouse 2 Band4 D3 4 70 64 cMStart139 038 055 bp 2 End139 045 737 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed induodenumright adrenal glandright uterine tubeleft adrenal glandjejunal mucosakidneycanal of the cervixright lobe of liverbody of stomachbody of pancreasTop expressed inproximal tubuleleft lobe of liverPaneth cellkidneyinternal carotid arterycrypt of lieberkuhn of small intestineexternal carotid arteryright ventriclemotor neuronmaxillary prominenceMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionalditol NADP 1 oxidoreductase activity electron transfer activity oxidoreductase activity phenanthrene 9 10 epoxide hydrolase activity aldo keto reductase NADP activity protein bindingCellular componentcytoplasm Golgi apparatus extracellular exosome cytosolBiological processxenobiotic metabolic process cellular aldehyde metabolic process daunorubicin metabolic process doxorubicin metabolic process carbohydrate metabolic process electron transport chainSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez8574110198EnsemblENSG00000053371ENSMUSG00000028743UniProtO43488Q8CG76RefSeq mRNA NM 003689NM 001320979NM 025337RefSeq protein NP 001307908NP 003680NP 079613Location UCSC Chr 1 19 3 19 31 MbChr 4 139 04 139 05 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Function 2 References 3 External links 4 Further readingFunction editAldo keto reductases such as AKR7A2 are involved in the detoxification of aldehydes and ketones supplied by OMIM 6 References edit a b c GRCh38 Ensembl release 89 ENSG00000053371 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000028743 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 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 a b Entrez Gene AKR7A2 aldo keto reductase family 7 member A2 aflatoxin aldehyde reductase External links editHuman 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 editMaruyama 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 Portal nbsp Biology nbsp This article on a gene on human chromosome 1 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title AKR7A2 amp oldid 1115436101, wikipedia, wiki, book, books, library,

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