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P15121 (ALDR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 171. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aldose reductase

Short name=AR
EC=1.1.1.21
Alternative name(s):
Aldehyde reductase
Aldo-keto reductase family 1 member B1
Gene names
Name:AKR1B1
Synonyms:ALDR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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. Ref.18

Subunit structure

Monomer.

Subcellular location

Cytoplasm.

Tissue specificity

Highly expressed in embryonic epithelial cells (EUE) in response to osmotic stress. Ref.15

Sequence similarities

Belongs to the aldo/keto reductase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandNADP
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processC21-steroid hormone biosynthetic process

Traceable author statement. Source: Reactome

carbohydrate metabolic process

Traceable author statement Ref.5. Source: ProtInc

daunorubicin metabolic process

Inferred from mutant phenotype PubMed 20837989. Source: UniProtKB

doxorubicin metabolic process

Inferred from mutant phenotype PubMed 20837989. Source: UniProtKB

response to stress

Traceable author statement Ref.15. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

steroid metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

extracellular space

Traceable author statement Ref.5. Source: ProtInc

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337PubMed 23376485. Source: UniProt

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionalditol:NADP+ 1-oxidoreductase activity

Traceable author statement Ref.5. Source: ProtInc

aldo-keto reductase (NADP) activity

Traceable author statement Ref.15. Source: UniProtKB

electron carrier activity

Traceable author statement Ref.5. Source: UniProtKB

glyceraldehyde oxidoreductase activity

Inferred from direct assay PubMed 20837989. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 316315Aldose reductase
PRO_0000124623

Regions

Nucleotide binding10 – 1910NADP Potential
Nucleotide binding211 – 27363NADP

Sites

Active site491Proton donor Ref.28
Binding site1111Substrate
Site781Lowers pKa of active site Tyr

Amino acid modifications

Modified residue21N-acetylalanine Ref.19 Ref.21
Modified residue951N6-acetyllysine Ref.22
Modified residue2221N6-acetyllysine Ref.22
Modified residue2631N6-acetyllysine Ref.22

Natural variations

Natural variant151I → F.
Corresponds to variant rs5054 [ dbSNP | Ensembl ].
VAR_014743
Natural variant421H → L.
Corresponds to variant rs5056 [ dbSNP | Ensembl ].
VAR_014744
Natural variant731L → V.
Corresponds to variant rs5057 [ dbSNP | Ensembl ].
VAR_014745
Natural variant901K → E.
Corresponds to variant rs2229542 [ dbSNP | Ensembl ].
VAR_048213
Natural variant2041G → S.
Corresponds to variant rs5061 [ dbSNP | Ensembl ].
VAR_014746
Natural variant2881T → I.
Corresponds to variant rs5062 [ dbSNP | Ensembl ].
VAR_014747

Experimental info

Mutagenesis441D → N: Reduced enzymatic activity. Ref.20
Mutagenesis491Y → F: Complete loss of enzymatic activity. Ref.20
Mutagenesis781K → M: Reduced enzymatic activity. Ref.20
Mutagenesis1111H → N: Reduced enzymatic activity. Ref.20
Sequence conflict51L → I in AAA51714. Ref.2
Sequence conflict1141T → I in CAG47000. Ref.10
Sequence conflict1171K → R in CAG29347. Ref.10
Sequence conflict1421W → R in AAH05387. Ref.14
Sequence conflict1721N → S in CAG29347. Ref.10
Sequence conflict270 – 2723IAE → EAA AA sequence Ref.16
Sequence conflict3071H → M AA sequence Ref.18

Secondary structure

.............................................................. 316
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15121 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 1852E8616B5DCEAE

FASTA31635,853
        10         20         30         40         50         60 
MASRLLLNNG AKMPILGLGT WKSPPGQVTE AVKVAIDVGY RHIDCAHVYQ NENEVGVAIQ 

        70         80         90        100        110        120 
EKLREQVVKR EELFIVSKLW CTYHEKGLVK GACQKTLSDL KLDYLDLYLI HWPTGFKPGK 

       130        140        150        160        170        180 
EFFPLDESGN VVPSDTNILD TWAAMEELVD EGLVKAIGIS NFNHLQVEMI LNKPGLKYKP 

       190        200        210        220        230        240 
AVNQIECHPY LTQEKLIQYC QSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIAAK 

       250        260        270        280        290        300 
HNKTTAQVLI RFPMQRNLVV IPKSVTPERI AENFKVFDFE LSSQDMTTLL SYNRNWRVCA 

       310 
LLSCTSHKDY PFHEEF 

« Hide

References

« Hide 'large scale' references
[1]"The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases."
Bohren K.M., Bullock B., Wermuth B., Gabbay K.H.
J. Biol. Chem. 264:9547-9551(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Cloning and sequence determination of human placental aldose reductase gene."
Chung S., Lamendola J.
J. Biol. Chem. 264:14775-14777(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[3]"Nucleotide sequence of cDNA for human aldose reductase."
Graham A., Hedge P.J., Powell S.J., Riley J., Brown L., Gammack A., Carey F., Markham A.F.
Nucleic Acids Res. 17:8368-8368(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fetus.
[4]"Cloning and prokaryotic expression of a biologically active human placental aldose reductase."
Grundmann U., Bohn H., Obermeier R., Amann E.
DNA Cell Biol. 9:149-157(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Tissue: Placenta.
[5]"Cloning and expression of human aldose reductase."
Nishimura C., Matsuura Y., Kokai Y., Akera T., Carper D., Morjana N., Lyons C., Flynn T.G.
J. Biol. Chem. 265:9788-9792(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]"Structure of the human aldose reductase gene."
Graham A., Brown L., Hedge P.J., Gammack A.J., Markham A.F.
J. Biol. Chem. 266:6872-6877(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"Identification and characterization of multiple osmotic response sequences in the human aldose reductase gene."
Ko B.C.B., Ruepp B., Bohren K.M., Gabbay K.H., Chung S.S.
J. Biol. Chem. 272:16431-16437(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"SEREX identification of new tumour-associated antigens in cutaneous T-cell lymphoma."
Hartmann T.B., Thiel D., Dummer R., Schadendorf D., Eichmueller S.
Br. J. Dermatol. 150:252-258(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lymphoma.
[9]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.
[10]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[11]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[12]"Human chromosome 7: DNA sequence and biology."
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. expand/collapse author list , 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.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[14]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain, Eye and Urinary bladder.
[15]"Aldose reductase is involved in long-term adaptation of EUE cells to hyperosmotic stress."
Ferraretto A., Negri A., Giuliani A., De Grada L., Fuhrman Conti A.M., Ronchi S.
Biochim. Biophys. Acta 1175:283-288(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 131-162, TISSUE SPECIFICITY.
[16]"Aldose reductase from human psoas muscle. Affinity labeling of an active site lysine by pyridoxal 5'-phosphate and pyridoxal 5'-diphospho-5'-adenosine."
Morjana N.A., Lyons C., Flynn T.G.
J. Biol. Chem. 264:2912-2919(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 244-275.
[17]Lubec G., Vishwanath V.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 276-294, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[18]"Identification of the reactive cysteine residue in human placenta aldose reductase."
Liu S.Q., Bhatnagar A., Ansari N.H., Srivastava S.K.
Biochim. Biophys. Acta 1164:268-272(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 298-316, ENZYME REGULATION.
[19]"Sequence of pig lens aldose reductase and electrospray mass spectrometry of non-covalent and covalent complexes."
Jaquinod M., Potier N., Klarskov K., Reymann J.-M., Sorokine O., Kieffer S., Barth P., Andriantomanga V., Biellmann J.-F., van Dorsselaer A.
Eur. J. Biochem. 218:893-903(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, ACETYLATION AT ALA-2.
Tissue: Muscle.
[20]"Probing the active site of human aldose reductase. Site-directed mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110."
Tarle I., Borhani D.W., Wilson D.K., Quiocho F.A., Petrash J.M.
J. Biol. Chem. 268:25687-25693(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASP-44; TYR-49; LYS-78 AND HIS-111.
[21]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-95; LYS-222 AND LYS-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications."
Wilson D.K., Bohren K.M., Gabbay K.H., Quiocho F.A.
Science 257:81-84(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
[25]"The crystal structure of the aldose reductase.NADPH binary complex."
Borhani D.W., Harter T.M., Pertrash J.M.
J. Biol. Chem. 267:24841-24847(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS).
[26]"Refined 1.8-A structure of human aldose reductase complexed with the potent inhibitor zopolrestat."
Wilson D.K., Tarle I., Petrash J.M., Quiocho F.A.
Proc. Natl. Acad. Sci. U.S.A. 90:9847-9851(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[27]"The alrestatin double-decker: binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant."
Harrison D.H., Bohren K.M., Petsko G.A., Ringe D., Gabbay K.H.
Biochemistry 36:16134-16140(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[28]"The crystallographic structure of the aldose reductase-IDD552 complex shows direct proton donation from tyrosine 48."
Ruiz F., Hazemann I., Mitschler A., Joachimiak A., Schneider T., Karplus M., Podjarny A.
Acta Crystallogr. D 60:1347-1354(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) IN COMPLEX WITH NADP AND SYNTHETIC INHIBITOR, ACTIVE SITE.
[29]"Ultrahigh resolution drug design I: details of interactions in human aldose reductase-inhibitor complex at 0.66 A."
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.
Proteins 55:792-804(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (0.66 ANGSTROMS) IN COMPLEX WITH NADP AND SYNTHETIC INHIBITOR.
[30]"High-resolution crystal structure of aldose reductase complexed with the novel sulfonyl-pyridazinone inhibitor exhibiting an alternative active site anchoring group."
Steuber H., Zentgraf M., Podjarny A., Heine A., Klebe G.
J. Mol. Biol. 356:45-56(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (0.95 ANGSTROMS) IN COMPLEX WITH NADP AND SUBSTRATE ANALOG.
[31]"The atomic resolution structure of human aldose reductase reveals that rearrangement of a bound ligand allows the opening of the safety-belt loop."
Biadene M., Hazemann I., Cousido A., Ginell S., Joachimiak A., Sheldrick G.M., Podjarny A., Schneider T.R.
Acta Crystallogr. D 63:665-672(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (0.82 ANGSTROMS) IN COMPLEX WITH NADP.
[32]"Evidence for a novel binding site conformer of aldose reductase in ligand-bound state."
Steuber H., Zentgraf M., La Motta C., Sartini S., Heine A., Klebe G.
J. Mol. Biol. 369:186-197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH NADP AND SYNTHETIC INHIBITOR.
[33]"Structural and thermodynamic study on aldose reductase: nitro-substituted inhibitors with strong enthalpic binding contribution."
Steuber H., Heine A., Klebe G.
J. Mol. Biol. 368:618-638(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) IN COMPLEX WITH NADP AND SYNTHETIC INHIBITOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04795 mRNA. Translation: AAA51713.1.
J05017 mRNA. Translation: AAA51714.1.
X15414 mRNA. Translation: CAA33460.1.
M34720 mRNA. Translation: AAA35560.1.
M34721 Genomic DNA. Translation: AAA35561.1.
J05474 mRNA. Translation: AAA51715.1.
M59783, M59856 Genomic DNA. Translation: AAA51712.1.
AF032455 Genomic DNA. Translation: AAB88851.1.
AF328729 mRNA. Translation: AAN09721.1.
AK313439 mRNA. Translation: BAG36230.1.
CR450351 mRNA. Translation: CAG29347.1.
CR542203 mRNA. Translation: CAG47000.1.
BT019859 mRNA. Translation: AAV38662.1.
CH236950 Genomic DNA. Translation: EAL24070.1.
CH471070 Genomic DNA. Translation: EAW83814.1.
BC000260 mRNA. Translation: AAH00260.1.
BC005387 mRNA. Translation: AAH05387.1.
BC010391 mRNA. Translation: AAH10391.1.
CCDSCCDS5831.1.
PIRA39763.
RefSeqNP_001619.1. NM_001628.2.
UniGeneHs.521212.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ABNX-ray2.40A2-316[»]
1ADSX-ray1.65A2-316[»]
1AZ1X-ray1.80A2-316[»]
1AZ2X-ray2.90A2-316[»]
1EF3X-ray2.80A/B2-316[»]
1EL3X-ray1.70A1-316[»]
1IEIX-ray2.50A1-316[»]
1MARX-ray1.80A2-316[»]
1PWLX-ray1.10A1-316[»]
1PWMX-ray0.92A1-316[»]
1T40X-ray1.80A1-316[»]
1T41X-ray1.05A1-316[»]
1US0X-ray0.66A1-316[»]
1X96X-ray1.40A1-316[»]
1X97X-ray1.40A1-316[»]
1X98X-ray1.30A1-316[»]
1XGDX-ray2.10A2-316[»]
1Z3NX-ray1.04A1-316[»]
1Z89X-ray1.43A1-316[»]
1Z8AX-ray0.95A1-316[»]
2ACQX-ray1.76A2-316[»]
2ACRX-ray1.76A2-316[»]
2ACSX-ray1.76A2-316[»]
2ACUX-ray1.76A2-316[»]
2AGTX-ray1.00A1-316[»]
2DUXX-ray1.60A1-316[»]
2DUZX-ray1.60A1-316[»]
2DV0X-ray1.62A1-316[»]
2F2KX-ray1.94A1-316[»]
2FZ8X-ray1.48A1-316[»]
2FZ9X-ray1.60A1-316[»]
2FZBX-ray1.50A6-316[»]
2FZDX-ray1.08A6-316[»]
2HV5X-ray1.59A1-316[»]
2HVNX-ray1.58A1-316[»]
2HVOX-ray1.65A1-316[»]
2I16X-ray0.81A1-316[»]
2I17X-ray0.81A1-316[»]
2IKGX-ray1.43A1-316[»]
2IKHX-ray1.55A1-316[»]
2IKIX-ray1.47A1-316[»]
2IKJX-ray1.55A1-316[»]
2INEX-ray1.90A2-316[»]
2INZX-ray1.95A2-316[»]
2IPWX-ray2.00A2-316[»]
2IQ0X-ray1.95A2-316[»]
2IQDX-ray2.00A2-316[»]
2IS7X-ray1.70A2-316[»]
2ISFX-ray2.00A2-316[»]
2J8TX-ray0.82A6-316[»]
2NVCX-ray1.65A1-316[»]
2NVDX-ray1.55A1-316[»]
2PD5X-ray1.60A1-316[»]
2PD9X-ray1.55A1-316[»]
2PDBX-ray1.60A1-316[»]
2PDCX-ray1.65A1-316[»]
2PDFX-ray1.56A1-316[»]
2PDGX-ray1.42A1-316[»]
2PDHX-ray1.45A1-316[»]
2PDIX-ray1.55A1-316[»]
2PDJX-ray1.57A1-316[»]
2PDKX-ray1.55A1-316[»]
2PDLX-ray1.47A1-316[»]
2PDMX-ray1.75A1-316[»]
2PDNX-ray1.70A1-316[»]
2PDPX-ray1.65A1-316[»]
2PDQX-ray1.73A1-316[»]
2PDUX-ray1.55A1-316[»]
2PDWX-ray1.55A1-316[»]
2PDXX-ray1.65A1-316[»]
2PDYX-ray1.65A1-316[»]
2PEVX-ray0.90A1-316[»]
2PF8X-ray0.85A1-316[»]
2PFHX-ray0.85A1-316[»]
2PZNX-ray1.00A1-316[»]
2QXWX-ray0.80A1-316[»]
2R24X-ray1.75A1-316[»]
3BCJX-ray0.78A1-316[»]
3DN5X-ray1.45A1-316[»]
3G5EX-ray1.80A1-316[»]
3GHRX-ray1.00A1-316[»]
3GHSX-ray1.00A1-316[»]
3GHTX-ray1.10A1-316[»]
3GHUX-ray1.20A1-316[»]
3LBOX-ray1.10A1-316[»]
3LD5X-ray1.27A1-316[»]
3LENX-ray1.21A1-316[»]
3LEPX-ray0.99A1-316[»]
3LQGX-ray1.35A1-316[»]
3LQLX-ray1.13A1-316[»]
3LZ3X-ray1.03A1-316[»]
3LZ5X-ray0.95A1-316[»]
3M0IX-ray1.07A1-316[»]
3M4HX-ray0.94A1-316[»]
3M64X-ray1.30A1-316[»]
3MB9X-ray1.65A1-316[»]
3MC5X-ray1.14A1-316[»]
3ONBX-ray1.45A2-316[»]
3ONCX-ray1.06A2-316[»]
3P2VX-ray1.69A1-316[»]
3Q65X-ray2.09A/B1-316[»]
3Q67X-ray1.55A/B1-316[»]
3RX2X-ray1.90A1-316[»]
3RX3X-ray1.90A1-316[»]
3RX4X-ray2.00A1-316[»]
3S3GX-ray1.80A1-316[»]
3T42X-ray1.28A1-316[»]
3U2CX-ray1.00A1-316[»]
3V35X-ray1.90A1-316[»]
3V36X-ray2.00A1-316[»]
4GCAX-ray0.90A2-316[»]
4GQ0X-ray2.10A1-316[»]
4IGSX-ray0.85A1-316[»]
4JIRX-ray2.00A1-316[»]
4LAUX-ray0.84A1-316[»]
4LAZX-ray0.85A1-316[»]
4LB3X-ray0.80A1-316[»]
4LB4X-ray0.80A1-316[»]
4LBRX-ray0.80A1-316[»]
4LBSX-ray0.76A1-316[»]
ProteinModelPortalP15121.
SMRP15121. Positions 1-316.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106732. 8 interactions.
IntActP15121. 2 interactions.
MINTMINT-1196717.
STRING9606.ENSP00000285930.

Chemistry

BindingDBP15121.
ChEMBLCHEMBL1900.
DrugBankDB00157. NADH.
DB00605. Sulindac.

PTM databases

PhosphoSiteP15121.

Polymorphism databases

DMDM113596.

2D gel databases

DOSAC-COBS-2DPAGEP15121.
REPRODUCTION-2DPAGEIPI00413641.
P15121.
UCD-2DPAGEP15121.

Proteomic databases

MaxQBP15121.
PaxDbP15121.
PeptideAtlasP15121.
PRIDEP15121.

Protocols and materials databases

DNASU231.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000285930; ENSP00000285930; ENSG00000085662.
GeneID231.
KEGGhsa:231.
UCSCuc003vrp.1. human.

Organism-specific databases

CTD231.
GeneCardsGC07M134127.
HGNCHGNC:381. AKR1B1.
HPACAB018773.
CAB027391.
CAB047353.
HPA026425.
HPA052751.
MIM103880. gene.
neXtProtNX_P15121.
PharmGKBPA24675.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0656.
HOVERGENHBG000020.
InParanoidP15121.
KOK00011.
OMADFLDTWT.
OrthoDBEOG70KGQF.
PhylomeDBP15121.
TreeFamTF106492.

Enzyme and pathway databases

BioCycMetaCyc:HS01502-MONOMER.
BRENDA1.1.1.21. 2681.
ReactomeREACT_111217. Metabolism.
REACT_15493. Steroid hormones.
SABIO-RKP15121.

Gene expression databases

ArrayExpressP15121.
BgeeP15121.
CleanExHS_AKR1B1.
GenevestigatorP15121.

Family and domain databases

Gene3D3.20.20.100. 1 hit.
InterProIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERPTHR11732. PTHR11732. 1 hit.
PfamPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFPIRSF000097. AKR. 1 hit.
PRINTSPR00069. ALDKETRDTASE.
SUPFAMSSF51430. SSF51430. 1 hit.
PROSITEPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAKR1B1. human.
EvolutionaryTraceP15121.
GeneWikiAKR1B1.
GenomeRNAi231.
NextBio938.
PROP15121.
SOURCESearch...

Entry information

Entry nameALDR_HUMAN
AccessionPrimary (citable) accession number: P15121
Secondary accession number(s): B2R8N3 expand/collapse secondary AC list , Q5U031, Q6FGA4, Q6ICP2, Q9BS21, Q9UCI9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 171 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM