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UniProtKB/Swiss-Prot entry P15121


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ALDR_HUMAN
Primary accession number P15121
Secondary accession numbers Q5U031 Q9BS21 Q9UCI9
Integrated into Swiss-Prot on April 1, 1990
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    September 23, 2008 (Entry version 110)
Name and origin of the protein
Protein name Aldose reductase
Synonyms AR
EC 1.1.1.21
Aldehyde reductase
Gene name
Name: AKR1B1
Synonyms: ALDR1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2498333 [NCBI, ExPASy, EBI, Israel, Japan]
Bohren K.M., Bullock B., Wermuth B., Gabbay K.H.;
"The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases.";
J. Biol. Chem. 264:9547-9551(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=2504709 [NCBI, ExPASy, EBI, Israel, Japan]
Chung S., Lamendola J.;
"Cloning and sequence determination of human placental aldose reductase gene.";
J. Biol. Chem. 264:14775-14777(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fetus;
DOI=10.1093/nar/17.20.8368; PubMed=2510130 [NCBI, ExPASy, EBI, Israel, Japan]
Graham A., Hedge P.J., Powell S.J., Riley J., Brown L., Gammack A., Carey F., Markham A.F.;
"Nucleotide sequence of cDNA for human aldose reductase.";
Nucleic Acids Res. 17:8368-8368(1989).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Placenta;
PubMed=2111143 [NCBI, ExPASy, EBI, Israel, Japan]
Grundmann U., Bohn H., Obermeier R., Amann E.;
"Cloning and prokaryotic expression of a biologically active human placental aldose reductase.";
DNA Cell Biol. 9:149-157(1990).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2112546 [NCBI, ExPASy, EBI, Israel, Japan]
Nishimura C., Matsuura Y., Kokai Y., Akera T., Carper D., Morjana N., Lyons C., Flynn T.G.;
"Cloning and expression of human aldose reductase.";
J. Biol. Chem. 265:9788-9792(1990).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1901857 [NCBI, ExPASy, EBI, Israel, Japan]
Graham A., Brown L., Hedge P.J., Gammack A.J., Markham A.F.;
"Structure of the human aldose reductase gene.";
J. Biol. Chem. 266:6872-6877(1991).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1074/jbc.272.26.16431; PubMed=9195951 [NCBI, ExPASy, EBI, Israel, Japan]
Ko B.C.B., Ruepp B., Bohren K.M., Gabbay K.H., Chung S.S.;
"Identification and characterization of multiple osmotic response sequences in the human aldose reductase gene.";
J. Biol. Chem. 272:16431-16437(1997).
[8]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lymphoma;
DOI=10.1111/j.1365-2133.2004.05651.x; PubMed=14996095 [NCBI, ExPASy, EBI, Israel, Japan]
Hartmann T.B., Thiel D., Dummer R., Schadendorf D., Eichmueller S.;
"SEREX identification of new tumour-associated antigens in cutaneous T-cell lymphoma.";
Br. J. Dermatol. 150:252-258(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1083423; PubMed=12690205 [NCBI, ExPASy, EBI, Israel, Japan]
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Eye, and Urinary bladder;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
PROTEIN SEQUENCE OF 131-162, AND TISSUE SPECIFICITY.
DOI=10.1016/0167-4889(93)90218-E; PubMed=8435445 [NCBI, ExPASy, EBI, Israel, Japan]
Ferraretto A., Negri A., Giuliani A., De Grada L., Fuhrman Conti A.M., Ronchi S.;
"Aldose reductase is involved in long-term adaptation of EUE cells to hyperosmotic stress.";
Biochim. Biophys. Acta 1175:283-288(1993).
[13]
PROTEIN SEQUENCE OF 244-275.
PubMed=2492527 [NCBI, ExPASy, EBI, Israel, Japan]
Morjana N.A., Lyons C., Flynn T.G.;
"Aldose reductase from human psoas muscle. Affinity labeling of an active site lysine by pyridoxal 5'-phosphate and pyridoxal 5'-diphospho-5'-adenosine.";
J. Biol. Chem. 264:2912-2919(1989).
[14]
PROTEIN SEQUENCE OF 276-294, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[15]
PROTEIN SEQUENCE OF 298-316, AND ENZYME REGULATION.
DOI=10.1016/0167-4838(93)90258-S; PubMed=8343525 [NCBI, ExPASy, EBI, Israel, Japan]
Liu S.Q., Bhatnagar A., Ansari N.H., Srivastava S.K.;
"Identification of the reactive cysteine residue in human placenta aldose reductase.";
Biochim. Biophys. Acta 1164:268-272(1993).
[16]
PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT ALA-2.
TISSUE=Muscle;
PubMed=8281941 [NCBI, ExPASy, EBI, Israel, Japan]
Jaquinod M., Potier N., Klarskov K., Reymann J.-M., Sorokine O., Kieffer S., Barth P., Andriantomanga V., Biellmann J.-F., van Dorsselaer A.;
"Sequence of pig lens aldose reductase and electrospray mass spectrometry of non-covalent and covalent complexes.";
Eur. J. Biochem. 218:893-903(1993).
[17]
MUTAGENESIS OF ASP-44; TYR-49; LYS-78 AND HIS-111.
PubMed=8245005 [NCBI, ExPASy, EBI, Israel, Japan]
Tarle I., Borhani D.W., Wilson D.K., Quiocho F.A., Petrash J.M.;
"Probing the active site of human aldose reductase. Site-directed mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110.";
J. Biol. Chem. 268:25687-25693(1993).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND TYR-40, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[19]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
PubMed=1621098 [NCBI, ExPASy, EBI, Israel, Japan]
Wilson D.K., Bohren K.M., Gabbay K.H., Quiocho F.A.;
"An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications.";
Science 257:81-84(1992).
[20]
X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS).
PubMed=1447221 [NCBI, ExPASy, EBI, Israel, Japan]
Borhani D.W., Harter T.M., Pertrash J.M.;
"The crystal structure of the aldose reductase.NADPH binary complex.";
J. Biol. Chem. 267:24841-24847(1992).
[21]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=8234324 [NCBI, ExPASy, EBI, Israel, Japan]
Wilson D.K., Tarle I., Petrash J.M., Quiocho F.A.;
"Refined 1.8-A structure of human aldose reductase complexed with the potent inhibitor zopolrestat.";
Proc. Natl. Acad. Sci. U.S.A. 90:9847-9851(1993).
[22]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
DOI=10.1021/bi9717136; PubMed=9405046 [NCBI, ExPASy, EBI, Israel, Japan]
Harrison D.H., Bohren K.M., Petsko G.A., Ringe D., Gabbay K.H.;
"The alrestatin double-decker: binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant.";
Biochemistry 36:16134-16140(1997).
[23]
X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) IN COMPLEX WITH NADP AND SYNTHETIC INHIBITOR, AND ACTIVE SITE.
DOI=10.1107/S0907444904011370; PubMed=15272156 [NCBI, ExPASy, EBI, Israel, Japan]
Ruiz F., Hazemann I., Mitschler A., Joachimiak A., Schneider T., Karplus M., Podjarny A.;
"The crystallographic structure of the aldose reductase-IDD552 complex shows direct proton donation from tyrosine 48.";
Acta Crystallogr. D 60:1347-1354(2004).
[24]
X-RAY CRYSTALLOGRAPHY (0.66 ANGSTROMS) IN COMPLEX WITH NADP AND SYNTHETIC INHIBITOR.
DOI=10.1002/prot.20015; PubMed=15146478 [NCBI, ExPASy, EBI, Israel, Japan]
Howard E.I., Sanishvili R., Cachau R.E., Mitschler A., Chevrier B., Barth P., Lamour V., Van Zandt M., Sibley E., Bon C., Moras D., Schneider T.R., Joachimiak A., Podjarny A.;
"Ultrahigh resolution drug design I: details of interactions in human aldose reductase-inhibitor complex at 0.66 A.";
Proteins 55:792-804(2004).
[25]
X-RAY CRYSTALLOGRAPHY (0.95 ANGSTROMS) IN COMPLEX WITH NADP AND SUBSTRATE ANALOG.
DOI=10.1016/j.jmb.2005.10.067; PubMed=16337231 [NCBI, ExPASy, EBI, Israel, Japan]
Steuber H., Zentgraf M., Podjarny A., Heine A., Klebe G.;
"High-resolution crystal structure of aldose reductase complexed with the novel sulfonyl-pyridazinone inhibitor exhibiting an alternative active site anchoring group.";
J. Mol. Biol. 356:45-56(2006).
[26]
X-RAY CRYSTALLOGRAPHY (0.82 ANGSTROMS) IN COMPLEX WITH NADP.
DOI=10.1107/S0907444907011997; PubMed=17505104 [NCBI, ExPASy, EBI, Israel, Japan]
Biadene M., Hazemann I., Cousido A., Ginell S., Joachimiak A., Sheldrick G.M., Podjarny A., Schneider T.R.;
"The atomic resolution structure of human aldose reductase reveals that rearrangement of a bound ligand allows the opening of the safety-belt loop.";
Acta Crystallogr. D 63:665-672(2007).
[27]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH NADP AND SYNTHETIC INHIBITOR.
DOI=10.1016/j.jmb.2007.03.021; PubMed=17418233 [NCBI, ExPASy, EBI, Israel, Japan]
Steuber H., Zentgraf M., La Motta C., Sartini S., Heine A., Klebe G.;
"Evidence for a novel binding site conformer of aldose reductase in ligand-bound state.";
J. Mol. Biol. 369:186-197(2007).
[28]
X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) IN COMPLEX WITH NADP AND SYNTHETIC INHIBITOR.
DOI=10.1016/j.jmb.2006.12.004; PubMed=17368668 [NCBI, ExPASy, EBI, Israel, Japan]
Steuber H., Heine A., Klebe G.;
"Structural and thermodynamic study on aldose reductase: nitro-substituted inhibitors with strong enthalpic binding contribution.";
J. Mol. Biol. 368:618-638(2007).
Comments
  • FUNCTION: Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
  • CATALYTIC ACTIVITY: Alditol + NAD(P)+ = aldose + NAD(P)H.
  • ENZYME REGULATION: Cys-299 may regulate the kinetic and inhibition properties of the enzyme, but does not participate in catalysis.
  • SUBUNIT: Monomer.
  • INTERACTION:
    P19532:TFE3; NbExp=1; IntAct=EBI-1052491, EBI-1048957;
  • SUBCELLULAR LOCATION: Cytoplasm.
  • TISSUE SPECIFICITY: Highly expressed in embryonic epithelial cells (EUE) in response to osmotic stress.
  • DISEASE: In diabetes and galactosemia, increased AR activity leads to high levels of sorbitol and galactitol, respectively, in the cells of many tissues. Accumulation of sugar alcohols has been shown to cause osmotic cataracts in the lens. AR is also thought to play a key role in diabetic complications of three other target tissues, namely, nerve, kidney and retina.
  • SIMILARITY: Belongs to the aldo/keto reductase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J04795; AAA51713.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J05017; AAA51714.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X15414; CAA33460.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M34720; AAA35560.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M34721; AAA35561.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J05474; AAA51715.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M59783; AAA51712.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M59856; AAA51712.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF032455; AAB88851.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF328729; AAN09721.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT019859; AAV38662.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH236950; EAL24070.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000260; AAH00260.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005387; AAH05387.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010391; AAH10391.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A39763; A39763.
RefSeq NP_001619.1; -.
UniGene Hs.521212
3D structure databases
PDB
1ABN; X-ray; 2.40 A; A=1-316.[ExPASy / RCSB / EBI]
1ADS; X-ray; 1.65 A; A=1-316.[ExPASy / RCSB / EBI]
1AZ1; X-ray; 1.80 A; A=1-316.[ExPASy / RCSB / EBI]
1AZ2; X-ray; 2.90 A; A=1-316.[ExPASy / RCSB / EBI]
1EF3; X-ray; 2.80 A; A/B=1-316.[ExPASy / RCSB / EBI]
1EL3; X-ray; 1.70 A; A=1-316.[ExPASy / RCSB / EBI]
1IEI; X-ray; 2.50 A; A=1-316.[ExPASy / RCSB / EBI]
1MAR; X-ray; 1.80 A; A=1-316.[ExPASy / RCSB / EBI]
1PWL; X-ray; 1.10 A; A=1-316.[ExPASy / RCSB / EBI]
1PWM; X-ray; 0.92 A; A=1-316.[ExPASy / RCSB / EBI]
1T40; X-ray; 1.80 A; A=1-316.[ExPASy / RCSB / EBI]
1T41; X-ray; 1.05 A; A=1-316.[ExPASy / RCSB / EBI]
1US0; X-ray; 0.66 A; A=1-316.[ExPASy / RCSB / EBI]
1X96; X-ray; 1.40 A; A=1-316.[ExPASy / RCSB / EBI]
1X97; X-ray; 1.40 A; A=1-316.[ExPASy / RCSB / EBI]
1X98; X-ray; 1.30 A; A=1-316.[ExPASy / RCSB / EBI]
1XGD; X-ray; 2.10 A; A=2-316.[ExPASy / RCSB / EBI]
1Z3N; X-ray; 1.04 A; A=1-316.[ExPASy / RCSB / EBI]
1Z89; X-ray; 1.43 A; A=1-316.[ExPASy / RCSB / EBI]
1Z8A; X-ray; 0.95 A; A=1-316.[ExPASy / RCSB / EBI]
2ACQ; X-ray; 1.76 A; A=1-316.[ExPASy / RCSB / EBI]
2ACR; X-ray; 1.76 A; A=1-316.[ExPASy / RCSB / EBI]
2ACS; X-ray; 1.76 A; A=1-316.[ExPASy / RCSB / EBI]
2ACU; X-ray; 1.76 A; A=1-316.[ExPASy / RCSB / EBI]
2AGT; X-ray; 1.00 A; A=1-316.[ExPASy / RCSB / EBI]
2DUX; X-ray; 1.60 A; A=1-316.[ExPASy / RCSB / EBI]
2DUZ; X-ray; 1.60 A; A=1-316.[ExPASy / RCSB / EBI]
2DV0; X-ray; 1.62 A; A=1-316.[ExPASy / RCSB / EBI]
2F2K; X-ray; 1.94 A; A=1-316.[ExPASy / RCSB / EBI]
2FZ8; X-ray; 1.48 A; A=1-316.[ExPASy / RCSB / EBI]
2FZ9; X-ray; 1.60 A; A=1-316.[ExPASy / RCSB / EBI]
2FZB; X-ray; 1.50 A; A=1-316.[ExPASy / RCSB / EBI]
2FZD; X-ray; 1.08 A; A=1-316.[ExPASy / RCSB / EBI]
2HV5; X-ray; 1.59 A; A=1-316.[ExPASy / RCSB / EBI]
2HVN; X-ray; 1.58 A; A=1-316.[ExPASy / RCSB / EBI]
2HVO; X-ray; 1.65 A; A=1-316.[ExPASy / RCSB / EBI]
2I16; X-ray; 0.81 A; A=1-316.[ExPASy / RCSB / EBI]
2I17; X-ray; 0.81 A; A=1-316.[ExPASy / RCSB / EBI]
2IKG; X-ray; 1.43 A; A=1-316.[ExPASy / RCSB / EBI]
2IKH; X-ray; 1.55 A; A=1-316.[ExPASy / RCSB / EBI]
2IKI; X-ray; 1.47 A; A=1-316.[ExPASy / RCSB / EBI]
2IKJ; X-ray; 1.55 A; A=1-316.[ExPASy / RCSB / EBI]
2INE; X-ray; 1.90 A; A=1-316.[ExPASy / RCSB / EBI]
2INZ; X-ray; 1.95 A; A=1-316.[ExPASy / RCSB / EBI]
2IPW; X-ray; 2.00 A; A=2-316.[ExPASy / RCSB / EBI]
2IQ0; X-ray; 1.95 A; A=2-316.[ExPASy / RCSB / EBI]
2IQD; X-ray; 2.00 A; A=2-316.[ExPASy / RCSB / EBI]
2IS7; X-ray; 1.70 A; A=1-316.[ExPASy / RCSB / EBI]
2ISF; X-ray; 2.00 A; A=2-316.[ExPASy / RCSB / EBI]
2J8T; X-ray; 0.82 A; A=1-316.[ExPASy / RCSB / EBI]
2NVC; X-ray; 1.65 A; A=1-316.[ExPASy / RCSB / EBI]
2NVD; X-ray; 1.55 A; A=1-316.[ExPASy / RCSB / EBI]
2PD5; X-ray; 1.60 A; A=1-316.[ExPASy / RCSB / EBI]
2PD9; X-ray; 1.55 A; A=1-316.[ExPASy / RCSB / EBI]
2PDB; X-ray; 1.60 A; A=1-316.[ExPASy / RCSB / EBI]
2PDC; X-ray; 1.65 A; A=1-316.[ExPASy / RCSB / EBI]
2PDF; X-ray; 1.56 A; A=1-316.[ExPASy / RCSB / EBI]
2PDG; X-ray; 1.42 A; A=1-316.[ExPASy / RCSB / EBI]
2PDH; X-ray; 1.45 A; A=1-316.[ExPASy / RCSB / EBI]
2PDI; X-ray; 1.55 A; A=1-316.[ExPASy / RCSB / EBI]
2PDJ; X-ray; 1.57 A; A=1-316.[ExPASy / RCSB / EBI]
2PDK; X-ray; 1.55 A; A=1-316.[ExPASy / RCSB / EBI]
2PDL; X-ray; 1.47 A; A=1-316.[ExPASy / RCSB / EBI]
2PDM; X-ray; 1.75 A; A=1-316.[ExPASy / RCSB / EBI]
2PDN; X-ray; 1.70 A; A=1-316.[ExPASy / RCSB / EBI]
2PDP; X-ray; 1.65 A; A=1-316.[ExPASy / RCSB / EBI]
2PDQ; X-ray; 1.73 A; A=1-316.[ExPASy / RCSB / EBI]
2PDU; X-ray; 1.55 A; A=1-316.[ExPASy / RCSB / EBI]
2PDW; X-ray; 1.55 A; A=1-316.[ExPASy / RCSB / EBI]
2PDX; X-ray; 1.65 A; A=1-316.[ExPASy / RCSB / EBI]
2PDY; X-ray; 1.65 A; A=1-316.[ExPASy / RCSB / EBI]
2PEV; X-ray; 0.90 A; A=1-316.[ExPASy / RCSB / EBI]
2PF8; X-ray; 0.85 A; A=1-316.[ExPASy / RCSB / EBI]
2PFH; X-ray; 0.85 A; A=1-315.[ExPASy / RCSB / EBI]
2PZN; X-ray; 1.00 A; A=1-316.[ExPASy / RCSB / EBI]
2QXW; X-ray; 0.80 A; A=1-316.[ExPASy / RCSB / EBI]
3BCJ; X-ray; 0.78 A; A=1-316.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1ABN; -.
1ADS; -.
1AZ1; -.
1AZ2; -.
1EF3; -.
1EL3; -.
1IEI; -.
1MAR; -.
1PWL; -.
1PWM; -.
1T40; -.
1T41; -.
1US0; -.
1X96; -.
1X97; -.
1X98; -.
1XGD; -.
1Z3N; -.
1Z89; -.
1Z8A; -.
2ACQ; -.
2ACR; -.
2ACS; -.
2ACU; -.
2AGT; -.
2DUX; -.
2DUZ; -.
2DV0; -.
2F2K; -.
2FZ8; -.
2FZ9; -.
2FZB; -.
2FZD; -.
2HV5; -.
2HVN; -.
2HVO; -.
2I16; -.
2I17; -.
2IKG; -.
2IKH; -.
2IKI; -.
2IKJ; -.
2INE; -.
2INZ; -.
2IPW; -.
2IQ0; -.
2IQD; -.
2IS7; -.
2ISF; -.
2J8T; -.
2NVC; -.
2NVD; -.
2PD5; -.
2PD9; -.
2PDB; -.
2PDC; -.
2PDF; -.
2PDG; -.
2PDH; -.
2PDI; -.
2PDJ; -.
2PDK; -.
2PDL; -.
2PDM; -.
2PDN; -.
2PDP; -.
2PDQ; -.
2PDU; -.
2PDW; -.
2PDX; -.
2PDY; -.
2PEV; -.
2PF8; -.
2PFH; -.
2PZN; -.
2QXW; -.
3BCJ; -.
ModBase P15121.
Protein-protein interaction databases
IntAct P15121; -.
PTM databases
PhosphoSite P15121; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-12905; -.
2D gel databases
Aarhus/Ghent-2DPAGE 1202; IEF.
DOSAC-COBS-2DPAGE P15121; -.
REPRODUCTION-2DPAGE IPI00413641; -.
P15121; -.
Organism-specific databases
H-InvDB HIX0007101; -.
HGNC HGNC:381; AKR1B1.
GenAtlas AKR1B1.
HPA CAB018773; -.
MIM 103880; gene. [NCBI / EBI]
PharmGKB PA24675; -.
GeneCards P15121.
Gene expression databases
ArrayExpress P15121; -.
CleanEx HS_AKR1B1; -.
GermOnline ENSG00000085662; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005615; Cellular component: extracellular space (traceable author statement from ProtInc).
GO:0004032; Molecular function: aldehyde reductase activity (traceable author statement from ProtInc).
GO:0009055; Molecular function: electron carrier activity (traceable author statement from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0005975; Biological process: carbohydrate metabolic process (traceable author statement from ProtInc).
GO:0006950; Biological process: response to stress (traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001395; Aldo/ket_red.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.100; Aldo/ket_red; 1.
PANTHER PTHR11732; Aldo/ket_red; 1.
Pfam PF00248; Aldo_ket_red; 1.
Pfam graphical view of domain structure.
PRINTS PR00069; ALDKETRDTASE.
ProDom PD000288; Aldo/ket_red; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00798; ALDOKETO_REDUCTASE_1; 1.
PS00062; ALDOKETO_REDUCTASE_2; 1.
PS00063; ALDOKETO_REDUCTASE_3; 1.
BLOCKS P15121.
Other
SWISS-3DIMAGE P15121.
Proteomic databases
PeptideAtlas P15121; -.
Genome annotation databases
Ensembl ENSG00000085662; Homo sapiens. [Contig view]
GeneID 231; -.
KEGG hsa:231; -.
Phylogenomic databases
HOGENOM P15121; -.
HOVERGEN P15121; -.
Other
DrugBank DB00157; NADH.
DB00605; Sulindac.
LinkHub P15121; -.
SOURCE AKR1B1; Homo sapiens.
ProtoNet P15121.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Cataract; Cytoplasm; Direct protein sequencing; NADP; Oxidoreductase; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   316  315     Aldose reductase. PRO_0000124623
NP_BIND   10    19  10     NADP (Potential). 
NP_BIND   211   273  63     NADP. 
ACT_SITE   49    49        Proton donor. 
BINDING   111   111        Substrate. 
SITE   78    78  1     Lowers pKa of active site Tyr. 
MOD_RES   2     2        N-acetylalanine. 
MOD_RES   23    23        Phosphoserine. 
MOD_RES   40    40        Phosphotyrosine. 
VARIANT   15    15  1     I -> F (in dbSNP:rs5054 [NCBI]). VAR_014743 [3D]
VARIANT   42    42  1     H -> L (in dbSNP:rs5056 [NCBI]). VAR_014744 [3D]
VARIANT   73    73  1     L -> V (in dbSNP:rs5057 [NCBI]). VAR_014745 [3D]
VARIANT   204   204  1     G -> S (in dbSNP:rs5061 [NCBI]). VAR_014746 [3D]
VARIANT   288   288  1     T -> I (in dbSNP:rs5062 [NCBI]). VAR_014747 [3D]
MUTAGEN   44    44        D->N: Reduced enzymatic activity. 
MUTAGEN   49    49        Y->F: Complete loss of enzymatic activity. 
MUTAGEN   78    78        K->M: Reduced enzymatic activity. 
MUTAGEN   111   111        H->N: Reduced enzymatic activity. 
CONFLICT   5     5        L -> I (in Ref. 2; AAA51714). 
CONFLICT   142   142        W -> R (in Ref. 11; AAH05387). 
CONFLICT   270   272        IAE -> EAA (in Ref. 13; AA sequence).