LOCUS NP_006057 325 aa linear PRI 22-OCT-2008
DEFINITION aldo-keto reductase family 1, member A1 [Homo sapiens].
ACCESSION NP_006057
VERSION NP_006057.1 GI:5174391
DBSOURCE REFSEQ: accession NM_006066.2
KEYWORDS .
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 325)
AUTHORS Hosgood,H.D. III, Menashe,I., Shen,M., Yeager,M., Yuenger,J.,
Rajaraman,P., He,X., Chatterjee,N., Caporaso,N.E., Zhu,Y.,
Chanock,S.J., Zheng,T. and Lan,Q.
TITLE Pathway-based evaluation of 380 candidate genes and lung cancer
susceptibility suggests the importance of the cell cycle pathway
JOURNAL Carcinogenesis 29 (10), 1938-1943 (2008)
PUBMED 18676680
REMARK GeneRIF: Observational study of gene-disease association. (HuGE
Navigator)
REFERENCE 2 (residues 1 to 325)
AUTHORS Steuber,H., Heine,A., Podjarny,A. and Klebe,G.
TITLE Merging the binding sites of aldose and aldehyde reductase for
detection of inhibitor selectivity-determining features
JOURNAL J. Mol. Biol. 379 (5), 991-1016 (2008)
PUBMED 18495158
REMARK GeneRIF: the binding site residues deviating between ALR1 and ALR2
influence ligand affinity in a complex interplay, presumably
involving changes of dynamic properties and differences of the
solvation/desolvation balance upon ligand binding
REFERENCE 3 (residues 1 to 325)
AUTHORS Lan,Q., Zheng,T., Shen,M., Zhang,Y., Wang,S.S., Zahm,S.H.,
Holford,T.R., Leaderer,B., Boyle,P. and Chanock,S.
TITLE Genetic polymorphisms in the oxidative stress pathway and
susceptibility to non-Hodgkin lymphoma
JOURNAL Hum. Genet. 121 (2), 161-168 (2007)
PUBMED 17149600
REMARK GeneRIF: Observational study of gene-disease association. (HuGE
Navigator)
REFERENCE 4 (residues 1 to 325)
AUTHORS Wang,S.S., Davis,S., Cerhan,J.R., Hartge,P., Severson,R.K.,
Cozen,W., Lan,Q., Welch,R., Chanock,S.J. and Rothman,N.
TITLE Polymorphisms in oxidative stress genes and risk for non-Hodgkin
lymphoma
JOURNAL Carcinogenesis 27 (9), 1828-1834 (2006)
PUBMED 16543247
REMARK GeneRIF: Observational study of gene-disease association. (HuGE
Navigator)
REFERENCE 5 (residues 1 to 325)
AUTHORS Bohren,K.M., Brownlee,J.M., Milne,A.C., Gabbay,K.H. and
Harrison,D.H.
TITLE The structure of Apo R268A human aldose reductase: hinges and
latches that control the kinetic mechanism
JOURNAL Biochim. Biophys. Acta 1748 (2), 201-212 (2005)
PUBMED 15769597
REMARK GeneRIF: structure of Apo R268A human aldose reductase reveals
hinges and latches that control the kinetic mechanism
REFERENCE 6 (sites)
AUTHORS Takahashi,M., Lu,Y.B., Myint,T., Fujii,J., Wada,Y. and Taniguchi,N.
TITLE In vivo glycation of aldehyde reductase, a major 3-deoxyglucosone
reducing enzyme: identification of glycation sites
JOURNAL Biochemistry 34 (4), 1433-1438 (1995)
PUBMED 7827091
REFERENCE 7 (residues 1 to 325)
AUTHORS Dawson,S.J. and White,L.A.
TITLE Treatment of Haemophilus aphrophilus endocarditis with
ciprofloxacin
JOURNAL J. Infect. 24 (3), 317-320 (1992)
PUBMED 1602151
REFERENCE 8 (residues 1 to 325)
AUTHORS Tanimoto,T., Ohta,M., Tanaka,A., Ikemoto,I. and Machida,T.
TITLE Purification and characterization of human testis aldose and
aldehyde reductase
JOURNAL Int. J. Biochem. 23 (4), 421-428 (1991)
PUBMED 1901806
REFERENCE 9 (residues 1 to 325)
AUTHORS Vander Jagt,D.L., Hunsaker,L.A., Robinson,B., Stangebye,L.A. and
Deck,L.M.
TITLE Aldehyde and aldose reductases from human placenta. Heterogeneous
expression of multiple enzyme forms
JOURNAL J. Biol. Chem. 265 (19), 10912-10918 (1990)
PUBMED 2113526
REFERENCE 10 (residues 1 to 325)
AUTHORS Bohren,K.M., Bullock,B., Wermuth,B. and Gabbay,K.H.
TITLE The aldo-keto reductase superfamily. cDNAs and deduced amino acid
sequences of human aldehyde and aldose reductases
JOURNAL J. Biol. Chem. 264 (16), 9547-9551 (1989)
PUBMED 2498333
REFERENCE 11 (residues 1 to 325)
AUTHORS Wermuth,B., Omar,A., Forster,A., di Francesco,C., Wolf,M., von
Wartburg,J.P., Bullock,B. and Gabbay,K.H.
TITLE Primary structure of aldehyde reductase from human liver
JOURNAL Prog. Clin. Biol. Res. 232, 297-307 (1987)
PUBMED 3615425
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from BC000670.2 and AF112482.1.
Summary: This gene encodes a member of the aldo/keto reductase
superfamily, which consists of more than 40 known enzymes and
proteins. This member, also known as aldehyde reductase, is
involved in the reduction of biogenic and xenobiotic aldehydes and
is present in virtually every tissue. Alternative splicing of this
gene results in two transcript variants encoding the same protein.
[provided by RefSeq].
Transcript Variant: This variant (1) is the minor and longer
transcript.
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the
Entrez Gene record to access additional publications.
FEATURES Location/Qualifiers
source 1..325
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="1"
/map="1p33-p32"
Protein 1..325
/product="aldo-keto reductase family 1, member A1"
/EC_number="1.1.1.2"
/note="aldehyde reductase; alcohol dehydrogenase;
dihydrodiol dehydrogenase 3"
/calculated_mol_wt=36442
Site 68
/site_type="glycosylation"
/experiment="experimental evidence, no additional details
recorded"
/note="glycation site"
/citation=[6]
Site 85
/site_type="glycosylation"
/experiment="experimental evidence, no additional details
recorded"
/note="glycation site"
/citation=[6]
Site 141
/site_type="glycosylation"
/experiment="experimental evidence, no additional details
recorded"
/note="glycation site"
/citation=[6]
CDS 1..325
/gene="AKR1A1"
/gene_synonym="ALR"
/gene_synonym="ARM"
/gene_synonym="DD3"
/gene_synonym="ALDR1"
/gene_synonym="MGC1380"
/gene_synonym="MGC12529"
/coded_by="NM_006066.2:465..1442"
/db_xref="CCDS:CCDS523.1"
/db_xref="GeneID:10327"
/db_xref="HGNC:380"
/db_xref="HPRD:00069"
/db_xref="MIM:103830"
ORIGIN
1 maascvllht gqkmpliglg twksepgqvk aavkyalsvg yrhidcaaiy gnepeigeal
61 kedvgpgkav preelfvtsk lwntkhhped vepalrktla dlqleyldly lmhwpyafer
121 gdnpfpknad gticydsthy ketwkaleal vakglvqalg lsnfnsrqid dilsvasvrp
181 avlqvechpy laqneliahc qarglevtay splgssdraw rdpdepvlle epvvlalaek
241 ygrspaqill rwqvqrkvic ipksitpsri lqnikvfdft fspeemkqln alnknwryiv
301 pmltvdgkrv prdaghplyp fndpy
//