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Aldose reductase (AR) (EC 1.1.1.21) (Aldehyde reductase) (Aldo-keto reductase family 1 member B1)

 ALDR_HUMAN              Reviewed;         316 AA.
P15121; B2R8N3; Q5U031; Q6FGA4; Q6ICP2; Q9BS21; Q9UCI9;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-MAR-2018, entry version 208.
RecName: Full=Aldose reductase;
Short=AR;
EC=1.1.1.21;
AltName: Full=Aldehyde reductase;
AltName: Full=Aldo-keto reductase family 1 member B1;
Name=AKR1B1; Synonyms=ALDR1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2498333;
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;
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;
PubMed=2510130; DOI=10.1093/nar/17.20.8368;
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; DOI=10.1089/dna.1990.9.149;
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;
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;
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].
PubMed=9195951; DOI=10.1074/jbc.272.26.16431;
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;
PubMed=14996095; DOI=10.1111/j.1365-2133.2004.05651.x;
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].
TISSUE=Brain cortex;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[11]
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.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
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).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Eye, and Urinary bladder;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[15]
PROTEIN SEQUENCE OF 131-162, AND TISSUE SPECIFICITY.
PubMed=8435445; DOI=10.1016/0167-4889(93)90218-E;
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).
[16]
PROTEIN SEQUENCE OF 244-275.
PubMed=2492527;
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).
[17]
PROTEIN SEQUENCE OF 276-294, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[18]
PROTEIN SEQUENCE OF 298-316, AND ENZYME REGULATION.
PubMed=8343525; DOI=10.1016/0167-4838(93)90258-S;
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).
[19]
PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT ALA-2.
TISSUE=Muscle;
PubMed=8281941; DOI=10.1111/j.1432-1033.1993.tb18445.x;
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).
[20]
MUTAGENESIS OF ASP-44; TYR-49; LYS-78 AND HIS-111.
PubMed=8245005;
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).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-95; LYS-222 AND LYS-263, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[24]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
PubMed=1621098; DOI=10.1126/science.1621098;
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).
[25]
X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS).
PubMed=1447221;
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).
[26]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=8234324; DOI=10.1073/pnas.90.21.9847;
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).
[27]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=9405046; DOI=10.1021/bi9717136;
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).
[28]
X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) IN COMPLEX WITH NADP AND
SYNTHETIC INHIBITOR, AND ACTIVE SITE.
PubMed=15272156; DOI=10.1107/S0907444904011370;
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).
[29]
X-RAY CRYSTALLOGRAPHY (0.66 ANGSTROMS) IN COMPLEX WITH NADP AND
SYNTHETIC INHIBITOR.
PubMed=15146478; DOI=10.1002/prot.20015;
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).
[30]
X-RAY CRYSTALLOGRAPHY (0.95 ANGSTROMS) IN COMPLEX WITH NADP AND
SUBSTRATE ANALOG.
PubMed=16337231; DOI=10.1016/j.jmb.2005.10.067;
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).
[31]
X-RAY CRYSTALLOGRAPHY (0.82 ANGSTROMS) IN COMPLEX WITH NADP.
PubMed=17505104; DOI=10.1107/S0907444907011997;
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).
[32]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH NADP AND
SYNTHETIC INHIBITOR.
PubMed=17418233; DOI=10.1016/j.jmb.2007.03.021;
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).
[33]
X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) IN COMPLEX WITH NADP AND
SYNTHETIC INHIBITOR.
PubMed=17368668; DOI=10.1016/j.jmb.2006.12.004;
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).
-!- 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.
{ECO:0000269|PubMed:8343525}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15146478,
ECO:0000269|PubMed:15272156, ECO:0000269|PubMed:16337231,
ECO:0000269|PubMed:17368668, ECO:0000269|PubMed:17418233,
ECO:0000269|PubMed:17505104}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Highly expressed in embryonic epithelial cells
(EUE) in response to osmotic stress. {ECO:0000269|PubMed:8435445}.
-!- SIMILARITY: Belongs to the aldo/keto reductase family.
{ECO:0000305}.
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EMBL; J04795; AAA51713.1; -; mRNA.
EMBL; J05017; AAA51714.1; -; mRNA.
EMBL; X15414; CAA33460.1; -; mRNA.
EMBL; M34720; AAA35560.1; -; mRNA.
EMBL; M34721; AAA35561.1; -; Genomic_DNA.
EMBL; J05474; AAA51715.1; -; mRNA.
EMBL; M59783; AAA51712.1; -; Genomic_DNA.
EMBL; M59856; AAA51712.1; JOINED; Genomic_DNA.
EMBL; AF032455; AAB88851.1; -; Genomic_DNA.
EMBL; AF328729; AAN09721.1; -; mRNA.
EMBL; AK313439; BAG36230.1; -; mRNA.
EMBL; CR450351; CAG29347.1; -; mRNA.
EMBL; CR542203; CAG47000.1; -; mRNA.
EMBL; BT019859; AAV38662.1; -; mRNA.
EMBL; CH236950; EAL24070.1; -; Genomic_DNA.
EMBL; CH471070; EAW83814.1; -; Genomic_DNA.
EMBL; BC000260; AAH00260.1; -; mRNA.
EMBL; BC005387; AAH05387.1; -; mRNA.
EMBL; BC010391; AAH10391.1; -; mRNA.
CCDS; CCDS5831.1; -.
PIR; A39763; A39763.
RefSeq; NP_001619.1; NM_001628.3.
UniGene; Hs.521212; -.
PDB; 1ABN; X-ray; 2.40 A; A=2-316.
PDB; 1ADS; X-ray; 1.65 A; A=2-316.
PDB; 1AZ1; X-ray; 1.80 A; A=2-316.
PDB; 1AZ2; X-ray; 2.90 A; A=2-316.
PDB; 1EF3; X-ray; 2.80 A; A/B=2-316.
PDB; 1EL3; X-ray; 1.70 A; A=1-316.
PDB; 1IEI; X-ray; 2.50 A; A=1-316.
PDB; 1MAR; X-ray; 1.80 A; A=2-316.
PDB; 1PWL; X-ray; 1.10 A; A=1-316.
PDB; 1PWM; X-ray; 0.92 A; A=1-316.
PDB; 1T40; X-ray; 1.80 A; A=1-316.
PDB; 1T41; X-ray; 1.05 A; A=1-316.
PDB; 1US0; X-ray; 0.66 A; A=1-316.
PDB; 1X96; X-ray; 1.40 A; A=1-316.
PDB; 1X97; X-ray; 1.40 A; A=1-316.
PDB; 1X98; X-ray; 1.30 A; A=1-316.
PDB; 1XGD; X-ray; 2.10 A; A=2-316.
PDB; 1Z3N; X-ray; 1.04 A; A=1-316.
PDB; 1Z89; X-ray; 1.43 A; A=1-316.
PDB; 1Z8A; X-ray; 0.95 A; A=1-316.
PDB; 2ACQ; X-ray; 1.76 A; A=2-316.
PDB; 2ACR; X-ray; 1.76 A; A=2-316.
PDB; 2ACS; X-ray; 1.76 A; A=2-316.
PDB; 2ACU; X-ray; 1.76 A; A=2-316.
PDB; 2AGT; X-ray; 1.00 A; A=1-316.
PDB; 2DUX; X-ray; 1.60 A; A=1-316.
PDB; 2DUZ; X-ray; 1.60 A; A=1-316.
PDB; 2DV0; X-ray; 1.62 A; A=1-316.
PDB; 2F2K; X-ray; 1.94 A; A=1-316.
PDB; 2FZ8; X-ray; 1.48 A; A=1-316.
PDB; 2FZ9; X-ray; 1.60 A; A=1-316.
PDB; 2FZB; X-ray; 1.50 A; A=6-316.
PDB; 2FZD; X-ray; 1.08 A; A=6-316.
PDB; 2HV5; X-ray; 1.59 A; A=1-316.
PDB; 2HVN; X-ray; 1.58 A; A=1-316.
PDB; 2HVO; X-ray; 1.65 A; A=1-316.
PDB; 2I16; X-ray; 0.81 A; A=1-316.
PDB; 2I17; X-ray; 0.81 A; A=1-316.
PDB; 2IKG; X-ray; 1.43 A; A=1-316.
PDB; 2IKH; X-ray; 1.55 A; A=1-316.
PDB; 2IKI; X-ray; 1.47 A; A=1-316.
PDB; 2IKJ; X-ray; 1.55 A; A=1-316.
PDB; 2INE; X-ray; 1.90 A; A=2-316.
PDB; 2INZ; X-ray; 1.95 A; A=2-316.
PDB; 2IPW; X-ray; 2.00 A; A=2-316.
PDB; 2IQ0; X-ray; 1.95 A; A=2-316.
PDB; 2IQD; X-ray; 2.00 A; A=2-316.
PDB; 2IS7; X-ray; 1.70 A; A=2-316.
PDB; 2ISF; X-ray; 2.00 A; A=2-316.
PDB; 2J8T; X-ray; 0.82 A; A=6-316.
PDB; 2NVC; X-ray; 1.65 A; A=1-316.
PDB; 2NVD; X-ray; 1.55 A; A=1-316.
PDB; 2PD5; X-ray; 1.60 A; A=1-316.
PDB; 2PD9; X-ray; 1.55 A; A=1-316.
PDB; 2PDB; X-ray; 1.60 A; A=1-316.
PDB; 2PDC; X-ray; 1.65 A; A=1-316.
PDB; 2PDF; X-ray; 1.56 A; A=1-316.
PDB; 2PDG; X-ray; 1.42 A; A=1-316.
PDB; 2PDH; X-ray; 1.45 A; A=1-316.
PDB; 2PDI; X-ray; 1.55 A; A=1-316.
PDB; 2PDJ; X-ray; 1.57 A; A=1-316.
PDB; 2PDK; X-ray; 1.55 A; A=1-316.
PDB; 2PDL; X-ray; 1.47 A; A=1-316.
PDB; 2PDM; X-ray; 1.75 A; A=1-316.
PDB; 2PDN; X-ray; 1.70 A; A=1-316.
PDB; 2PDP; X-ray; 1.65 A; A=1-316.
PDB; 2PDQ; X-ray; 1.73 A; A=1-316.
PDB; 2PDU; X-ray; 1.55 A; A=1-316.
PDB; 2PDW; X-ray; 1.55 A; A=1-316.
PDB; 2PDX; X-ray; 1.65 A; A=1-316.
PDB; 2PDY; X-ray; 1.65 A; A=1-316.
PDB; 2PEV; X-ray; 0.90 A; A=1-316.
PDB; 2PF8; X-ray; 0.85 A; A=1-316.
PDB; 2PFH; X-ray; 0.85 A; A=1-316.
PDB; 2PZN; X-ray; 1.00 A; A=1-316.
PDB; 2QXW; X-ray; 0.80 A; A=1-316.
PDB; 2R24; X-ray; 1.75 A; A=1-316.
PDB; 3BCJ; X-ray; 0.78 A; A=1-316.
PDB; 3DN5; X-ray; 1.45 A; A=1-316.
PDB; 3G5E; X-ray; 1.80 A; A=1-316.
PDB; 3GHR; X-ray; 1.00 A; A=1-316.
PDB; 3GHS; X-ray; 1.00 A; A=1-316.
PDB; 3GHT; X-ray; 1.10 A; A=1-316.
PDB; 3GHU; X-ray; 1.20 A; A=1-316.
PDB; 3LBO; X-ray; 1.10 A; A=1-316.
PDB; 3LD5; X-ray; 1.27 A; A=1-316.
PDB; 3LEN; X-ray; 1.21 A; A=1-316.
PDB; 3LEP; X-ray; 0.99 A; A=1-316.
PDB; 3LQG; X-ray; 1.35 A; A=1-316.
PDB; 3LQL; X-ray; 1.13 A; A=1-316.
PDB; 3LZ3; X-ray; 1.03 A; A=1-316.
PDB; 3LZ5; X-ray; 0.95 A; A=1-316.
PDB; 3M0I; X-ray; 1.07 A; A=1-316.
PDB; 3M4H; X-ray; 0.94 A; A=1-316.
PDB; 3M64; X-ray; 1.30 A; A=1-316.
PDB; 3MB9; X-ray; 1.65 A; A=1-316.
PDB; 3MC5; X-ray; 1.14 A; A=1-316.
PDB; 3ONB; X-ray; 1.45 A; A=2-316.
PDB; 3ONC; X-ray; 1.06 A; A=2-316.
PDB; 3P2V; X-ray; 1.69 A; A=1-316.
PDB; 3Q65; X-ray; 2.09 A; A/B=1-316.
PDB; 3Q67; X-ray; 1.55 A; A/B=1-316.
PDB; 3RX2; X-ray; 1.90 A; A=1-316.
PDB; 3RX3; X-ray; 1.90 A; A=1-316.
PDB; 3RX4; X-ray; 2.00 A; A=1-316.
PDB; 3S3G; X-ray; 1.80 A; A=1-316.
PDB; 3T42; X-ray; 1.28 A; A=1-316.
PDB; 3U2C; X-ray; 1.00 A; A=1-316.
PDB; 3V35; X-ray; 1.90 A; A=1-316.
PDB; 3V36; X-ray; 2.00 A; A=1-316.
PDB; 4GCA; X-ray; 0.90 A; A=2-316.
PDB; 4GQ0; X-ray; 2.10 A; A=1-316.
PDB; 4IGS; X-ray; 0.85 A; A=1-316.
PDB; 4JIR; X-ray; 2.00 A; A=1-316.
PDB; 4LAU; X-ray; 0.84 A; A=1-316.
PDB; 4LAZ; X-ray; 0.85 A; A=1-316.
PDB; 4LB3; X-ray; 0.80 A; A=1-316.
PDB; 4LB4; X-ray; 0.80 A; A=1-316.
PDB; 4LBR; X-ray; 0.80 A; A=1-316.
PDB; 4LBS; X-ray; 0.76 A; A=1-316.
PDB; 4NKC; X-ray; 1.12 A; A=2-316.
PDB; 4PR4; X-ray; 1.06 A; A=2-316.
PDB; 4PRR; X-ray; 1.01 A; A=2-316.
PDB; 4PRT; X-ray; 0.96 A; A=1-316.
PDB; 4PUU; X-ray; 1.14 A; A=1-316.
PDB; 4PUW; X-ray; 1.12 A; A=1-316.
PDB; 4Q7B; X-ray; 1.19 A; A=2-316.
PDB; 4QBX; X-ray; 0.98 A; A=1-316.
PDB; 4QR6; X-ray; 1.05 A; A=1-316.
PDB; 4QX4; X-ray; 1.26 A; A=1-316.
PDB; 4QXI; X-ray; 0.87 A; A=1-316.
PDB; 4RPQ; X-ray; 1.20 A; A=2-316.
PDB; 4XZH; X-ray; 1.00 A; A/B=1-316.
PDB; 4XZI; X-ray; 2.45 A; A=1-316.
PDB; 4YS1; X-ray; 1.07 A; A=1-316.
PDB; 4YU1; X-ray; 1.02 A; A=1-316.
PDB; 5HA7; X-ray; 1.65 A; A/B=1-316.
PDBsum; 1ABN; -.
PDBsum; 1ADS; -.
PDBsum; 1AZ1; -.
PDBsum; 1AZ2; -.
PDBsum; 1EF3; -.
PDBsum; 1EL3; -.
PDBsum; 1IEI; -.
PDBsum; 1MAR; -.
PDBsum; 1PWL; -.
PDBsum; 1PWM; -.
PDBsum; 1T40; -.
PDBsum; 1T41; -.
PDBsum; 1US0; -.
PDBsum; 1X96; -.
PDBsum; 1X97; -.
PDBsum; 1X98; -.
PDBsum; 1XGD; -.
PDBsum; 1Z3N; -.
PDBsum; 1Z89; -.
PDBsum; 1Z8A; -.
PDBsum; 2ACQ; -.
PDBsum; 2ACR; -.
PDBsum; 2ACS; -.
PDBsum; 2ACU; -.
PDBsum; 2AGT; -.
PDBsum; 2DUX; -.
PDBsum; 2DUZ; -.
PDBsum; 2DV0; -.
PDBsum; 2F2K; -.
PDBsum; 2FZ8; -.
PDBsum; 2FZ9; -.
PDBsum; 2FZB; -.
PDBsum; 2FZD; -.
PDBsum; 2HV5; -.
PDBsum; 2HVN; -.
PDBsum; 2HVO; -.
PDBsum; 2I16; -.
PDBsum; 2I17; -.
PDBsum; 2IKG; -.
PDBsum; 2IKH; -.
PDBsum; 2IKI; -.
PDBsum; 2IKJ; -.
PDBsum; 2INE; -.
PDBsum; 2INZ; -.
PDBsum; 2IPW; -.
PDBsum; 2IQ0; -.
PDBsum; 2IQD; -.
PDBsum; 2IS7; -.
PDBsum; 2ISF; -.
PDBsum; 2J8T; -.
PDBsum; 2NVC; -.
PDBsum; 2NVD; -.
PDBsum; 2PD5; -.
PDBsum; 2PD9; -.
PDBsum; 2PDB; -.
PDBsum; 2PDC; -.
PDBsum; 2PDF; -.
PDBsum; 2PDG; -.
PDBsum; 2PDH; -.
PDBsum; 2PDI; -.
PDBsum; 2PDJ; -.
PDBsum; 2PDK; -.
PDBsum; 2PDL; -.
PDBsum; 2PDM; -.
PDBsum; 2PDN; -.
PDBsum; 2PDP; -.
PDBsum; 2PDQ; -.
PDBsum; 2PDU; -.
PDBsum; 2PDW; -.
PDBsum; 2PDX; -.
PDBsum; 2PDY; -.
PDBsum; 2PEV; -.
PDBsum; 2PF8; -.
PDBsum; 2PFH; -.
PDBsum; 2PZN; -.
PDBsum; 2QXW; -.
PDBsum; 2R24; -.
PDBsum; 3BCJ; -.
PDBsum; 3DN5; -.
PDBsum; 3G5E; -.
PDBsum; 3GHR; -.
PDBsum; 3GHS; -.
PDBsum; 3GHT; -.
PDBsum; 3GHU; -.
PDBsum; 3LBO; -.
PDBsum; 3LD5; -.
PDBsum; 3LEN; -.
PDBsum; 3LEP; -.
PDBsum; 3LQG; -.
PDBsum; 3LQL; -.
PDBsum; 3LZ3; -.
PDBsum; 3LZ5; -.
PDBsum; 3M0I; -.
PDBsum; 3M4H; -.
PDBsum; 3M64; -.
PDBsum; 3MB9; -.
PDBsum; 3MC5; -.
PDBsum; 3ONB; -.
PDBsum; 3ONC; -.
PDBsum; 3P2V; -.
PDBsum; 3Q65; -.
PDBsum; 3Q67; -.
PDBsum; 3RX2; -.
PDBsum; 3RX3; -.
PDBsum; 3RX4; -.
PDBsum; 3S3G; -.
PDBsum; 3T42; -.
PDBsum; 3U2C; -.
PDBsum; 3V35; -.
PDBsum; 3V36; -.
PDBsum; 4GCA; -.
PDBsum; 4GQ0; -.
PDBsum; 4IGS; -.
PDBsum; 4JIR; -.
PDBsum; 4LAU; -.
PDBsum; 4LAZ; -.
PDBsum; 4LB3; -.
PDBsum; 4LB4; -.
PDBsum; 4LBR; -.
PDBsum; 4LBS; -.
PDBsum; 4NKC; -.
PDBsum; 4PR4; -.
PDBsum; 4PRR; -.
PDBsum; 4PRT; -.
PDBsum; 4PUU; -.
PDBsum; 4PUW; -.
PDBsum; 4Q7B; -.
PDBsum; 4QBX; -.
PDBsum; 4QR6; -.
PDBsum; 4QX4; -.
PDBsum; 4QXI; -.
PDBsum; 4RPQ; -.
PDBsum; 4XZH; -.
PDBsum; 4XZI; -.
PDBsum; 4YS1; -.
PDBsum; 4YU1; -.
PDBsum; 5HA7; -.
ProteinModelPortal; P15121; -.
SMR; P15121; -.
BioGrid; 106732; 44.
IntAct; P15121; 13.
MINT; P15121; -.
STRING; 9606.ENSP00000285930; -.
BindingDB; P15121; -.
ChEMBL; CHEMBL1900; -.
DrugBank; DB07028; (2-{[(4-BROMO-2-FLUOROBENZYL)AMINO]CARBONYL}-5-CHLOROPHENOXY)ACETIC ACID.
DrugBank; DB07030; (5-CHLORO-2-{[(3-NITROBENZYL)AMINO]CARBONYL}PHENOXY)ACETIC ACID.
DrugBank; DB03461; 2'-Monophosphoadenosine 5'-Diphosphoribose.
DrugBank; DB07139; 3-[5-(3-nitrophenyl)thiophen-2-yl]propanoic acid.
DrugBank; DB07187; 6-[(5-CHLORO-3-METHYL-1-BENZOFURAN-2-YL)SULFONYL]PYRIDAZIN-3(2H)-ONE.
DrugBank; DB02007; alpha-D-glucose 6-phosphate.
DrugBank; DB02020; Alrestatin.
DrugBank; DB05327; AS-3201.
DrugBank; DB04272; Citric Acid.
DrugBank; DB02021; Fidarestat.
DrugBank; DB02994; Hydroxydimethylarsine Oxide.
DrugBank; DB02834; IDD552.
DrugBank; DB08084; IDD594.
DrugBank; DB01689; Inhibitor Idd 384.
DrugBank; DB02518; N-Acetylalanine.
DrugBank; DB00157; NADH.
DrugBank; DB05383; pimagedine HCl.
DrugBank; DB02712; Sorbinil.
DrugBank; DB00605; Sulindac.
DrugBank; DB02383; Tolrestat.
GuidetoPHARMACOLOGY; 2768; -.
SwissLipids; SLP:000001112; -.
iPTMnet; P15121; -.
PhosphoSitePlus; P15121; -.
SwissPalm; P15121; -.
BioMuta; AKR1B1; -.
DMDM; 113596; -.
DOSAC-COBS-2DPAGE; P15121; -.
REPRODUCTION-2DPAGE; IPI00413641; -.
REPRODUCTION-2DPAGE; P15121; -.
UCD-2DPAGE; P15121; -.
EPD; P15121; -.
MaxQB; P15121; -.
PaxDb; P15121; -.
PeptideAtlas; P15121; -.
PRIDE; P15121; -.
TopDownProteomics; P15121; -.
DNASU; 231; -.
Ensembl; ENST00000285930; ENSP00000285930; ENSG00000085662.
GeneID; 231; -.
KEGG; hsa:231; -.
UCSC; uc003vrp.2; human.
CTD; 231; -.
DisGeNET; 231; -.
EuPathDB; HostDB:ENSG00000085662.13; -.
GeneCards; AKR1B1; -.
HGNC; HGNC:381; AKR1B1.
HPA; CAB027391; -.
HPA; CAB047353; -.
HPA; HPA026425; -.
HPA; HPA052751; -.
MIM; 103880; gene.
neXtProt; NX_P15121; -.
OpenTargets; ENSG00000085662; -.
PharmGKB; PA24675; -.
eggNOG; KOG1577; Eukaryota.
eggNOG; COG0656; LUCA.
GeneTree; ENSGT00760000119041; -.
HOVERGEN; HBG000020; -.
InParanoid; P15121; -.
KO; K00011; -.
OMA; QIELHPM; -.
OrthoDB; EOG091G0D69; -.
PhylomeDB; P15121; -.
TreeFam; TF106492; -.
BioCyc; MetaCyc:HS01502-MONOMER; -.
BRENDA; 1.1.1.188; 2681.
BRENDA; 1.1.1.21; 2681.
Reactome; R-HSA-196108; Pregnenolone biosynthesis.
Reactome; R-HSA-5652227; Fructose biosynthesis.
SABIO-RK; P15121; -.
ChiTaRS; AKR1B1; human.
EvolutionaryTrace; P15121; -.
GeneWiki; AKR1B1; -.
GenomeRNAi; 231; -.
PRO; PR:P15121; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000085662; -.
CleanEx; HS_AKR1B1; -.
ExpressionAtlas; P15121; baseline and differential.
Genevisible; P15121; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005615; C:extracellular space; TAS:ProtInc.
GO; GO:0042629; C:mast cell granule; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0033010; C:paranodal junction; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0032838; C:plasma membrane bounded cell projection cytoplasm; IEA:Ensembl.
GO; GO:0043220; C:Schmidt-Lanterman incisure; IEA:Ensembl.
GO; GO:0097454; C:Schwann cell microvillus; IEA:Ensembl.
GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IDA:UniProtKB.
GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
GO; GO:0043795; F:glyceraldehyde oxidoreductase activity; IDA:UniProtKB.
GO; GO:0006700; P:C21-steroid hormone biosynthetic process; TAS:Reactome.
GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
GO; GO:0071475; P:cellular hyperosmotic salinity response; IDA:UniProtKB.
GO; GO:0097238; P:cellular response to methylglyoxal; IEA:Ensembl.
GO; GO:1901653; P:cellular response to peptide; IEA:Ensembl.
GO; GO:0044597; P:daunorubicin metabolic process; IMP:UniProtKB.
GO; GO:0044598; P:doxorubicin metabolic process; IMP:UniProtKB.
GO; GO:0046370; P:fructose biosynthetic process; TAS:Reactome.
GO; GO:0072061; P:inner medullary collecting duct development; IEA:Ensembl.
GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
GO; GO:0018931; P:naphthalene metabolic process; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0042415; P:norepinephrine metabolic process; IEA:Ensembl.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
GO; GO:0046427; P:positive regulation of JAK-STAT cascade; IEA:Ensembl.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0035809; P:regulation of urine volume; IEA:Ensembl.
GO; GO:0003091; P:renal water homeostasis; IEA:Ensembl.
GO; GO:0097066; P:response to thyroid hormone; IEA:Ensembl.
GO; GO:0009414; P:response to water deprivation; IEA:Ensembl.
GO; GO:0006061; P:sorbitol biosynthetic process; IEA:Ensembl.
GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IEA:Ensembl.
GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
CDD; cd06660; Aldo_ket_red; 1.
Gene3D; 3.20.20.100; -; 1.
InterPro; IPR018170; Aldo/ket_reductase_CS.
InterPro; IPR020471; Aldo/keto_reductase.
InterPro; IPR023210; NADP_OxRdtase_dom.
InterPro; IPR036812; NADP_OxRdtase_dom_sf.
PANTHER; PTHR11732; PTHR11732; 1.
Pfam; PF00248; Aldo_ket_red; 1.
PIRSF; PIRSF000097; AKR; 1.
PRINTS; PR00069; ALDKETRDTASE.
SUPFAM; SSF51430; SSF51430; 1.
PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; NADP; Oxidoreductase; Phosphoprotein;
Polymorphism; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000269|PubMed:8281941}.
CHAIN 2 316 Aldose reductase.
/FTId=PRO_0000124623.
NP_BIND 10 19 NADP. {ECO:0000255}.
NP_BIND 211 273 NADP. {ECO:0000269|PubMed:15146478,
ECO:0000269|PubMed:15272156,
ECO:0000269|PubMed:16337231,
ECO:0000269|PubMed:17368668,
ECO:0000269|PubMed:17418233,
ECO:0000269|PubMed:17505104}.
ACT_SITE 49 49 Proton donor.
{ECO:0000269|PubMed:15272156}.
BINDING 111 111 Substrate.
SITE 78 78 Lowers pKa of active site Tyr.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000269|PubMed:8281941}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000250|UniProtKB:P07943}.
MOD_RES 95 95 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 222 222 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 263 263 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VARIANT 15 15 I -> F (in dbSNP:rs5054).
/FTId=VAR_014743.
VARIANT 42 42 H -> L (in dbSNP:rs5056).
/FTId=VAR_014744.
VARIANT 73 73 L -> V (in dbSNP:rs5057).
/FTId=VAR_014745.
VARIANT 90 90 K -> E (in dbSNP:rs2229542).
/FTId=VAR_048213.
VARIANT 204 204 G -> S (in dbSNP:rs5061).
/FTId=VAR_014746.
VARIANT 288 288 T -> I (in dbSNP:rs5062).
/FTId=VAR_014747.
MUTAGEN 44 44 D->N: Reduced enzymatic activity.
{ECO:0000269|PubMed:8245005}.
MUTAGEN 49 49 Y->F: Complete loss of enzymatic
activity. {ECO:0000269|PubMed:8245005}.
MUTAGEN 78 78 K->M: Reduced enzymatic activity.
{ECO:0000269|PubMed:8245005}.
MUTAGEN 111 111 H->N: Reduced enzymatic activity.
{ECO:0000269|PubMed:8245005}.
CONFLICT 5 5 L -> I (in Ref. 2; AAA51714).
{ECO:0000305}.
CONFLICT 114 114 T -> I (in Ref. 10; CAG47000).
{ECO:0000305}.
CONFLICT 117 117 K -> R (in Ref. 10; CAG29347).
{ECO:0000305}.
CONFLICT 142 142 W -> R (in Ref. 14; AAH05387).
{ECO:0000305}.
CONFLICT 172 172 N -> S (in Ref. 10; CAG29347).
{ECO:0000305}.
CONFLICT 270 272 IAE -> EAA (in Ref. 16; AA sequence).
{ECO:0000305}.
CONFLICT 307 307 H -> M (in Ref. 18; AA sequence).
{ECO:0000305}.
STRAND 3 6 {ECO:0000244|PDB:1US0}.
STRAND 12 16 {ECO:0000244|PDB:1US0}.
HELIX 25 38 {ECO:0000244|PDB:1US0}.
STRAND 42 44 {ECO:0000244|PDB:1US0}.
HELIX 47 49 {ECO:0000244|PDB:1US0}.
HELIX 52 64 {ECO:0000244|PDB:1US0}.
HELIX 70 72 {ECO:0000244|PDB:1US0}.
STRAND 74 79 {ECO:0000244|PDB:1US0}.
HELIX 81 83 {ECO:0000244|PDB:1US0}.
TURN 86 88 {ECO:0000244|PDB:1US0}.
HELIX 89 100 {ECO:0000244|PDB:1US0}.
STRAND 105 113 {ECO:0000244|PDB:1US0}.
STRAND 118 120 {ECO:0000244|PDB:2PDC}.
STRAND 127 129 {ECO:0000244|PDB:3U2C}.
HELIX 138 150 {ECO:0000244|PDB:1US0}.
STRAND 153 155 {ECO:0000244|PDB:1US0}.
STRAND 157 161 {ECO:0000244|PDB:1US0}.
HELIX 164 171 {ECO:0000244|PDB:1US0}.
STRAND 181 186 {ECO:0000244|PDB:1US0}.
HELIX 194 202 {ECO:0000244|PDB:1US0}.
STRAND 206 211 {ECO:0000244|PDB:1US0}.
STRAND 223 225 {ECO:0000244|PDB:2ACQ}.
TURN 228 230 {ECO:0000244|PDB:1US0}.
HELIX 232 241 {ECO:0000244|PDB:1US0}.
HELIX 245 255 {ECO:0000244|PDB:1US0}.
STRAND 259 261 {ECO:0000244|PDB:1XGD}.
HELIX 267 274 {ECO:0000244|PDB:1US0}.
HELIX 283 290 {ECO:0000244|PDB:1US0}.
HELIX 302 304 {ECO:0000244|PDB:1US0}.
STRAND 307 309 {ECO:0000244|PDB:1IEI}.
STRAND 311 314 {ECO:0000244|PDB:3U2C}.
SEQUENCE 316 AA; 35853 MW; 1852E8616B5DCEAE CRC64;
MASRLLLNNG AKMPILGLGT WKSPPGQVTE AVKVAIDVGY RHIDCAHVYQ NENEVGVAIQ
EKLREQVVKR EELFIVSKLW CTYHEKGLVK GACQKTLSDL KLDYLDLYLI HWPTGFKPGK
EFFPLDESGN VVPSDTNILD TWAAMEELVD EGLVKAIGIS NFNHLQVEMI LNKPGLKYKP
AVNQIECHPY LTQEKLIQYC QSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIAAK
HNKTTAQVLI RFPMQRNLVV IPKSVTPERI AENFKVFDFE LSSQDMTTLL SYNRNWRVCA
LLSCTSHKDY PFHEEF


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201-20-0258 AKR1B1{aldo-keto reductase family 1, member B1 (aldose reductase)}rabbit.pAb 0.1ml
AKR1B15 AKR1B1 Gene aldo-keto reductase family 1, member B1 (aldose reductase)
GWB-DB9900 Anti- AKR1B10 (aldo-keto reductase family 1. member B10 (aldose reductase)) Antibody
CSB-EL001539RA Rat aldo-keto reductase family 1, member B1 (aldose reductase) (AKR1B1) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL001539PI Pig aldo-keto reductase family 1, member B1 (aldose reductase) (AKR1B1) ELISA kit, Species Pig, Sample Type serum, plasma 96T
AKR1B10 AKR1A1 Gene aldo-keto reductase family 1, member A1 (aldehyde reductase)
E1381344 Aldo-Keto Reductase Family 1, Member A1 (Aldehyde Reductase) (AKR1A1) ELISA Kit 1
201-20-0262 AKR7A2{aldo-keto reductase family 7, member A2 (aflatoxin aldehyde reductase)}rabbit.pAb 0.1ml
AKR7L AKR7A2 Gene aldo-keto reductase family 7, member A2 (aflatoxin aldehyde reductase)
AKT1 AKR7A3 Gene aldo-keto reductase family 7, member A3 (aflatoxin aldehyde reductase)
201-20-0263 AKR7A3{aldo-keto reductase family 7, member A3 (aflatoxin aldehyde reductase)}rabbit.pAb 0.1ml
GWB-8A132B Aldo-keto Reductase Family 1 Member A1 (aldehyde reductase) (AKR1A1) Goat anti-Human Polyclonal (C-Terminus) Antibody
CSB-EL001538PI Pig aldo-keto reductase family 1, member A1 (aldehyde reductase) (AKR1A1) ELISA kit, Species Pig, Sample Type serum, plasma 96T
CSB-EL001538RA Rat aldo-keto reductase family 1, member A1 (aldehyde reductase) (AKR1A1) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL001551RA Rat aldo-keto reductase family 7, member A3 (aflatoxin aldehyde reductase) (AKR7A3) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL001550RA Rat aldo-keto reductase family 7, member A2 (aflatoxin aldehyde reductase) (AKR7A2) ELISA kit, Species Rat, Sample Type serum, plasma 96T
AKR1B1-2496H Recombinant Human Aldo-Keto Reductase Family 1, Member B1(aldose reductase), His-tagged species: Human 100
CSB-EL001539RB Rabbit aldo-keto reductase family 1, member B1 (aldose reductase) (AKR1B1) ELISA kit, Species Rabbit, Sample Type serum, plasma 96T
CSB-EL001539BO Bovine aldo-keto reductase family 1, member B1 (aldose reductase) (AKR1B1) ELISA kit, Species Bovine, Sample Type serum, plasma 96T


 

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