Reviewed, UniProtKB/Swiss-Prot P15121 (ALDR_HUMAN)

Names and originHide

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributesHide

Sequence length	316 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)Hide

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.

OntologiesHide

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Traceable author statement. Source: ProtInc oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to stress Ref.15 Traceable author statement. Source: UniProtKB
Cellular component	cytosol Inferred from Experiment. Source: Reactome extracellular space Traceable author statement. Source: ProtInc
Molecular function	aldehyde reductase activity Inferred from Experiment. Source: Reactome electron carrier activity Ref.5 Traceable author statement. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactionsHide

With	Entry	#Exp.	IntAct	Notes
TFE3	P19532	1	EBI-1052491,EBI-1048957

Sequence annotation (Features)Hide

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 316

315

Aldose reductase

PRO_0000124623

Regions

Nucleotide binding

10 – 19

10

NADP Potential

Nucleotide binding

211 – 273

63

NADP

Sites

Active site

49

1

Proton donor Ref.29

Binding site

111

1

Substrate

Site

78

1

Lowers pKa of active site Tyr

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.19 Ref.23

Modified residue

23

1

Phosphoserine Ref.21

Modified residue

40

1

Phosphotyrosine Ref.21

Modified residue

95

1

N6-acetyllysine Ref.24

Modified residue

222

1

N6-acetyllysine Ref.24

Modified residue

263

1

N6-acetyllysine Ref.24

Natural variations

Natural variant

15

1

I → F. [dbSNP:rs5054]

VAR_014743

Natural variant

42

1

H → L. [dbSNP:rs5056]

VAR_014744

Natural variant

73

1

L → V. [dbSNP:rs5057]

VAR_014745

Natural variant

90

1

K → E. [dbSNP:rs2229542]

VAR_048213

Natural variant

204

1

G → S. [dbSNP:rs5061]

VAR_014746

Natural variant

288

1

T → I. [dbSNP:rs5062]

VAR_014747

Experimental info

Mutagenesis

44

1

D → N: Reduced enzymatic activity. Ref.20

Mutagenesis

49

1

Y → F: Complete loss of enzymatic activity. Ref.20

Mutagenesis

78

1

K → M: Reduced enzymatic activity. Ref.20

Mutagenesis

111

1

H → N: Reduced enzymatic activity. Ref.20

Sequence conflict

5

1

L → I in AAA51714. Ref.2

Sequence conflict

114

1

T → I in CAG47000. Ref.10

Sequence conflict

117

1

K → R in CAG29347. Ref.10

Sequence conflict

142

1

W → R in AAH05387. Ref.14

Sequence conflict

172

1

N → S in CAG29347. Ref.10

Sequence conflict

270 – 272

3

IAE → EAA AA sequence Ref.16

Sequence conflict

307

1

H → M AA sequence Ref.18

Secondary structure

1

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316

Helix Strand Turn

Details...

Beta strand

3 – 6

4

Beta strand

12 – 16

5

Helix

25 – 38

14

Beta strand

42 – 44

3

Helix

47 – 49

3

Helix

52 – 64

13

Helix

70 – 72

3

Beta strand

74 – 79

6

Helix

81 – 83

3

Helix

86 – 88

3

Helix

89 – 100

12

Beta strand

105 – 111

7

Helix

138 – 150

13

Beta strand

153 – 155

3

Beta strand

157 – 161

5

Helix

164 – 171

8

Beta strand

181 – 186

6

Helix

194 – 202

9

Beta strand

206 – 210

5

Helix

228 – 230

3

Helix

232 – 240

9

Helix

245 – 254

10

Turn

255 – 257

3

Helix

267 – 274

8

Helix

283 – 290

8

Helix

302 – 304

3

SequencesHide

	Sequence		Length	Mass (Da)
	P15121-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 1852E8616B5DCEAE	FASTA	316	35,853
	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

ReferencesHide

	« Hide 'large scale' referencesShow '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: 2498333] [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: 2504709] [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: 2510130] [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: 2111143] [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: 2112546] [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: 1901857] [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: 9195951] [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: 14996095] [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. , 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: 14702039] [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. , 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: 12690205] [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. , 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: 15489334] [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: 8435445] [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: 2492527] [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, 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: 8343525] [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: 8281941] [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: 8245005] [Abstract] Cited for: MUTAGENESIS OF ASP-44; TYR-49; LYS-78 AND HIS-111.
[21]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND TYR-40, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[24]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-95; LYS-222 AND LYS-263, MASS SPECTROMETRY.
[25]	"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: 1621098] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
[26]	"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: 1447221] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS).
[27]	"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: 8234324] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[28]	"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: 9405046] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[29]	"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: 15272156] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) IN COMPLEX WITH NADP AND SYNTHETIC INHIBITOR, ACTIVE SITE.
[30]	"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: 15146478] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (0.66 ANGSTROMS) IN COMPLEX WITH NADP AND SYNTHETIC INHIBITOR.
[31]	"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: 16337231] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (0.95 ANGSTROMS) IN COMPLEX WITH NADP AND SUBSTRATE ANALOG.
[32]	"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: 17505104] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (0.82 ANGSTROMS) IN COMPLEX WITH NADP.
[33]	"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: 17418233] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH NADP AND SYNTHETIC INHIBITOR.
[34]	"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: 17368668] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) IN COMPLEX WITH NADP AND SYNTHETIC INHIBITOR.
+	Additional computationally mapped references.

Cross-referencesHide

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.

IPI

IPI00413641.

PIR

A39763.

RefSeq

NP_001619.1.

UniGene

Hs.521212

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ABN	X-ray	2.40	A	2-316	[»]
1ADS	X-ray	1.65	A	2-316	[»]
1AZ1	X-ray	1.80	A	2-316	[»]
1AZ2	X-ray	2.90	A	2-316	[»]
1EF3	X-ray	2.80	A/B	2-315	[»]
1EL3	X-ray	1.70	A	1-316	[»]
1IEI	X-ray	2.50	A	1-316	[»]
1MAR	X-ray	1.80	A	2-316	[»]
1PWL	X-ray	1.10	A	1-316	[»]
1PWM	X-ray	0.92	A	1-316	[»]
1T40	X-ray	1.80	A	1-316	[»]
1T41	X-ray	1.05	A	1-316	[»]
1US0	X-ray	0.66	A	1-316	[»]
1X96	X-ray	1.40	A	1-316	[»]
1X97	X-ray	1.40	A	1-316	[»]
1X98	X-ray	1.30	A	1-316	[»]
1XGD	X-ray	2.10	A	2-315	[»]
1Z3N	X-ray	1.04	A	1-316	[»]
1Z89	X-ray	1.43	A	1-316	[»]
1Z8A	X-ray	0.95	A	1-316	[»]
2ACQ	X-ray	1.76	A	2-315	[»]
2ACR	X-ray	1.76	A	2-315	[»]
2ACS	X-ray	1.76	A	2-315	[»]
2ACU	X-ray	1.76	A	2-315	[»]
2AGT	X-ray	1.00	A	1-316	[»]
2DUX	X-ray	1.60	A	1-316	[»]
2DUZ	X-ray	1.60	A	1-316	[»]
2DV0	X-ray	1.62	A	1-316	[»]
2F2K	X-ray	1.94	A	1-316	[»]
2FZ8	X-ray	1.48	A	1-316	[»]
2FZ9	X-ray	1.60	A	1-316	[»]
2FZB	X-ray	1.50	A	1-316	[»]
2FZD	X-ray	1.08	A	1-316	[»]
2HV5	X-ray	1.59	A	1-316	[»]
2HVN	X-ray	1.58	A	1-316	[»]
2HVO	X-ray	1.65	A	1-316	[»]
2I16	X-ray	0.81	A	1-316	[»]
2I17	X-ray	0.81	A	1-316	[»]
2IKG	X-ray	1.43	A	1-316	[»]
2IKH	X-ray	1.55	A	1-316	[»]
2IKI	X-ray	1.47	A	1-316	[»]
2IKJ	X-ray	1.55	A	1-316	[»]
2INE	X-ray	1.90	A	2-315	[»]
2INZ	X-ray	1.95	A	2-315	[»]
2IPW	X-ray	2.00	A	2-315	[»]
2IQ0	X-ray	1.95	A	2-315	[»]
2IQD	X-ray	2.00	A	2-315	[»]
2IS7	X-ray	1.70	A	2-315	[»]
2ISF	X-ray	2.00	A	2-315	[»]
2J8T	X-ray	0.82	A	1-316	[»]
2NVC	X-ray	1.65	A	1-316	[»]
2NVD	X-ray	1.55	A	1-316	[»]
2PD5	X-ray	1.60	A	1-316	[»]
2PD9	X-ray	1.55	A	1-316	[»]
2PDB	X-ray	1.60	A	1-316	[»]
2PDC	X-ray	1.65	A	1-316	[»]
2PDF	X-ray	1.56	A	1-316	[»]
2PDG	X-ray	1.42	A	1-316	[»]
2PDH	X-ray	1.45	A	1-316	[»]
2PDI	X-ray	1.55	A	1-316	[»]
2PDJ	X-ray	1.57	A	1-316	[»]
2PDK	X-ray	1.55	A	1-316	[»]
2PDL	X-ray	1.47	A	1-316	[»]
2PDM	X-ray	1.75	A	1-316	[»]
2PDN	X-ray	1.70	A	1-316	[»]
2PDP	X-ray	1.65	A	1-316	[»]
2PDQ	X-ray	1.73	A	1-316	[»]
2PDU	X-ray	1.55	A	1-316	[»]
2PDW	X-ray	1.55	A	1-316	[»]
2PDX	X-ray	1.65	A	1-316	[»]
2PDY	X-ray	1.65	A	1-316	[»]
2PEV	X-ray	0.90	A	1-316	[»]
2PF8	X-ray	0.85	A	1-316	[»]
2PFH	X-ray	0.85	A	1-316	[»]
2PZN	X-ray	1.00	A	1-316	[»]
2QXW	X-ray	0.80	A	1-316	[»]
2R24	X-ray	1.75	A	1-316	[»]
3BCJ	X-ray	0.78	A	1-316	[»]
3DN5	X-ray	1.45	A	1-316	[»]
3G5E	X-ray	1.80	A	1-316	[»]
3GHR	X-ray	1.00	A	1-316	[»]
3GHS	X-ray	1.00	A	1-316	[»]
3GHT	X-ray	1.10	A	1-316	[»]
3GHU	X-ray	1.20	A	1-316	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P15121. 12 interactions.

MINT

MINT-1196717.

STRING

P15121.

PTM databases

PhosphoSite

P15121.

2-D gel databases

Aarhus/Ghent-2DPAGE

1202. IEF.

DOSAC-COBS-2DPAGE

P15121.

REPRODUCTION-2DPAGE

IPI00413641.
P15121.

UCD-2DPAGE

P15121.

Proteomic databases

PeptideAtlas

P15121.

PRIDE

P15121.

Genome annotation databases

Ensembl

ENST00000285930; ENSP00000285930; ENSG00000085662; Homo sapiens. [Genome view]

GeneID

231.

KEGG

hsa:231.

UCSC

uc003vrp.1. human.

Organism-specific databases

CTD

231.

GeneCards

GC07M133778.

H-InvDB

HIX0007101.

HGNC

HGNC:381. AKR1B1.

HPA

CAB018773.
CAB027391.
HPA026425.

MIM

103880. gene.

PharmGKB

PA24675.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG605727.

HOVERGEN

HBG000020.

InParanoid

P15121.

OMA

CEAMATY.

OrthoDB

EOG96MF48.

PhylomeDB

P15121.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-12905.

BRENDA

1.1.1.21. 247.

Gene expression databases

ArrayExpress

P15121.

Bgee

P15121.

CleanEx

HS_AKR1B1.

Genevestigator

P15121.

GermOnline

ENSG00000085662. Homo sapiens.

Family and domain databases

InterPro

IPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_sg.
[Graphical view]

Gene3D

G3DSA:3.20.20.100. Aldo/ket_red. 1 hit.

PANTHER

PTHR11732. Aldo/ket_red. 1 hit.

Pfam

PF00248. Aldo_ket_red. 1 hit.
[Graphical view]

PRINTS

PR00069. ALDKETRDTASE.

SUPFAM

SSF51430. Aldo/ket_red. 1 hit.

PROSITE

PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00157. NADH.
DB00605. Sulindac.

NextBio

938.

SOURCE

Search...

Entry informationHide

Entry name

ALDR_HUMAN

Accession

Primary (citable) accession number: P15121
Secondary accession number(s): B2R8N3 , Q5U031, Q6FGA4, Q6ICP2, Q9BS21, Q9UCI9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	January 23, 2007
Last modified:	July 13, 2010
This is version 133 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.