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Protein

Aldose reductase

Gene

AKR1B1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Alditol + NAD(P)+ = aldose + NAD(P)H.

Enzyme regulationi

Cys-299 may regulate the kinetic and inhibition properties of the enzyme, but does not participate in catalysis.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei49Proton donor1 Publication1
Sitei78Lowers pKa of active site Tyr1
Binding sitei111Substrate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 19NADPSequence analysis10
Nucleotide bindingi211 – 273NADP6 PublicationsAdd BLAST63

GO - Molecular functioni

  • alditol:NADP+ 1-oxidoreductase activity Source: Reactome
  • aldo-keto reductase (NADP) activity Source: UniProtKB
  • electron carrier activity Source: UniProtKB
  • glyceraldehyde oxidoreductase activity Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
LigandNADP

Enzyme and pathway databases

BioCyciMetaCyc:HS01502-MONOMER.
BRENDAi1.1.1.188. 2681.
1.1.1.21. 2681.
ReactomeiR-HSA-196108. Pregnenolone biosynthesis.
R-HSA-5652227. Fructose biosynthesis.
SABIO-RKiP15121.

Chemistry databases

SwissLipidsiSLP:000001112.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldose reductase (EC:1.1.1.21)
Short name:
AR
Alternative name(s):
Aldehyde reductase
Aldo-keto reductase family 1 member B1
Gene namesi
Name:AKR1B1
Synonyms:ALDR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

EuPathDBiHostDB:ENSG00000085662.13.
HGNCiHGNC:381. AKR1B1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi44D → N: Reduced enzymatic activity. 1 Publication1
Mutagenesisi49Y → F: Complete loss of enzymatic activity. 1 Publication1
Mutagenesisi78K → M: Reduced enzymatic activity. 1 Publication1
Mutagenesisi111H → N: Reduced enzymatic activity. 1 Publication1

Organism-specific databases

DisGeNETi231.
OpenTargetsiENSG00000085662.
PharmGKBiPA24675.

Chemistry databases

ChEMBLiCHEMBL1900.
DrugBankiDB07028. (2-{[(4-BROMO-2-FLUOROBENZYL)AMINO]CARBONYL}-5-CHLOROPHENOXY)ACETIC ACID.
DB07030. (5-CHLORO-2-{[(3-NITROBENZYL)AMINO]CARBONYL}PHENOXY)ACETIC ACID.
DB03461. 2'-Monophosphoadenosine 5'-Diphosphoribose.
DB07139. 3-[5-(3-nitrophenyl)thiophen-2-yl]propanoic acid.
DB07187. 6-[(5-CHLORO-3-METHYL-1-BENZOFURAN-2-YL)SULFONYL]PYRIDAZIN-3(2H)-ONE.
DB02007. alpha-D-glucose 6-phosphate.
DB02020. Alrestatin.
DB05327. AS-3201.
DB04272. Citric Acid.
DB02021. Fidarestat.
DB02994. Hydroxydimethylarsine Oxide.
DB02834. IDD552.
DB08084. IDD594.
DB01689. Inhibitor Idd 384.
DB02518. N-Acetylalanine.
DB00157. NADH.
DB05383. pimagedine HCl.
DB02712. Sorbinil.
DB00605. Sulindac.
DB02383. Tolrestat.
GuidetoPHARMACOLOGYi2768.

Polymorphism and mutation databases

BioMutaiAKR1B1.
DMDMi113596.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001246232 – 316Aldose reductaseAdd BLAST315

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei3PhosphoserineBy similarity1
Modified residuei95N6-acetyllysineCombined sources1
Modified residuei222N6-acetyllysineCombined sources1
Modified residuei263N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP15121.
MaxQBiP15121.
PaxDbiP15121.
PeptideAtlasiP15121.
PRIDEiP15121.
TopDownProteomicsiP15121.

2D gel databases

DOSAC-COBS-2DPAGEiP15121.
REPRODUCTION-2DPAGEiIPI00413641.
P15121.
UCD-2DPAGEiP15121.

PTM databases

iPTMnetiP15121.
PhosphoSitePlusiP15121.
SwissPalmiP15121.

Expressioni

Tissue specificityi

Highly expressed in embryonic epithelial cells (EUE) in response to osmotic stress.1 Publication

Gene expression databases

BgeeiENSG00000085662.
CleanExiHS_AKR1B1.
ExpressionAtlasiP15121. baseline and differential.
GenevisibleiP15121. HS.

Organism-specific databases

HPAiCAB027391.
CAB047353.
HPA026425.
HPA052751.

Interactioni

Subunit structurei

Monomer.6 Publications

Protein-protein interaction databases

BioGridi106732. 44 interactors.
IntActiP15121. 2 interactors.
MINTiMINT-1196717.
STRINGi9606.ENSP00000285930.

Chemistry databases

BindingDBiP15121.

Structurei

Secondary structure

1316
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 6Combined sources4
Beta strandi12 – 16Combined sources5
Helixi25 – 38Combined sources14
Beta strandi42 – 44Combined sources3
Helixi47 – 49Combined sources3
Helixi52 – 64Combined sources13
Helixi70 – 72Combined sources3
Beta strandi74 – 79Combined sources6
Helixi81 – 83Combined sources3
Turni86 – 88Combined sources3
Helixi89 – 100Combined sources12
Beta strandi105 – 113Combined sources9
Beta strandi118 – 120Combined sources3
Beta strandi127 – 129Combined sources3
Helixi138 – 150Combined sources13
Beta strandi153 – 155Combined sources3
Beta strandi157 – 161Combined sources5
Helixi164 – 171Combined sources8
Beta strandi181 – 186Combined sources6
Helixi194 – 202Combined sources9
Beta strandi206 – 211Combined sources6
Beta strandi223 – 225Combined sources3
Turni228 – 230Combined sources3
Helixi232 – 241Combined sources10
Helixi245 – 255Combined sources11
Beta strandi259 – 261Combined sources3
Helixi267 – 274Combined sources8
Helixi283 – 290Combined sources8
Helixi302 – 304Combined sources3
Beta strandi307 – 309Combined sources3
Beta strandi311 – 314Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4NKCX-ray1.12A2-316[»]
4PR4X-ray1.06A2-316[»]
4PRRX-ray1.01A2-316[»]
4PRTX-ray0.96A1-316[»]
4PUUX-ray1.14A1-316[»]
4PUWX-ray1.12A1-316[»]
4Q7BX-ray1.19A2-316[»]
4QBXX-ray0.98A1-316[»]
4QR6X-ray1.05A1-316[»]
4QX4X-ray1.26A1-316[»]
4QXIX-ray0.87A1-316[»]
4RPQX-ray1.20A2-316[»]
4XZHX-ray1.00A/B1-316[»]
4XZIX-ray2.45A1-316[»]
4YS1X-ray1.07A1-316[»]
4YU1X-ray1.02A1-316[»]
5HA7X-ray1.65A/B1-316[»]
ProteinModelPortaliP15121.
SMRiP15121.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15121.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

eggNOGiKOG1577. Eukaryota.
COG0656. LUCA.
GeneTreeiENSGT00760000119041.
HOVERGENiHBG000020.
InParanoidiP15121.
KOiK00011.
OMAiQIELHPM.
OrthoDBiEOG091G0D69.
PhylomeDBiP15121.
TreeFamiTF106492.

Family and domain databases

CDDicd06660. Aldo_ket_red. 1 hit.
Gene3Di3.20.20.100. 1 hit.
InterProiView protein in InterPro
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
IPR036812. NADP_OxRdtase_dom_sf.
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiView protein in Pfam
PF00248. Aldo_ket_red. 1 hit.
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiView protein in PROSITE
PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15121-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASRLLLNNG AKMPILGLGT WKSPPGQVTE AVKVAIDVGY RHIDCAHVYQ
60 70 80 90 100
NENEVGVAIQ EKLREQVVKR EELFIVSKLW CTYHEKGLVK GACQKTLSDL
110 120 130 140 150
KLDYLDLYLI HWPTGFKPGK EFFPLDESGN VVPSDTNILD TWAAMEELVD
160 170 180 190 200
EGLVKAIGIS NFNHLQVEMI LNKPGLKYKP AVNQIECHPY LTQEKLIQYC
210 220 230 240 250
QSKGIVVTAY SPLGSPDRPW AKPEDPSLLE DPRIKAIAAK HNKTTAQVLI
260 270 280 290 300
RFPMQRNLVV IPKSVTPERI AENFKVFDFE LSSQDMTTLL SYNRNWRVCA
310
LLSCTSHKDY PFHEEF
Length:316
Mass (Da):35,853
Last modified:January 23, 2007 - v3
Checksum:i1852E8616B5DCEAE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti5L → I in AAA51714 (PubMed:2504709).Curated1
Sequence conflicti114T → I in CAG47000 (Ref. 10) Curated1
Sequence conflicti117K → R in CAG29347 (Ref. 10) Curated1
Sequence conflicti142W → R in AAH05387 (PubMed:15489334).Curated1
Sequence conflicti172N → S in CAG29347 (Ref. 10) Curated1
Sequence conflicti270 – 272IAE → EAA AA sequence (PubMed:2492527).Curated3
Sequence conflicti307H → M AA sequence (PubMed:8343525).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01474315I → F. Corresponds to variant dbSNP:rs5054Ensembl.1
Natural variantiVAR_01474442H → L. Corresponds to variant dbSNP:rs5056Ensembl.1
Natural variantiVAR_01474573L → V. Corresponds to variant dbSNP:rs5057Ensembl.1
Natural variantiVAR_04821390K → E. Corresponds to variant dbSNP:rs2229542Ensembl.1
Natural variantiVAR_014746204G → S. Corresponds to variant dbSNP:rs5061Ensembl.1
Natural variantiVAR_014747288T → I. Corresponds to variant dbSNP:rs5062Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5831.1.
PIRiA39763.
RefSeqiNP_001619.1. NM_001628.3.
UniGeneiHs.521212.

Genome annotation databases

EnsembliENST00000285930; ENSP00000285930; ENSG00000085662.
GeneIDi231.
KEGGihsa:231.
UCSCiuc003vrp.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiALDR_HUMAN
AccessioniPrimary (citable) accession number: P15121
Secondary accession number(s): B2R8N3
, Q5U031, Q6FGA4, Q6ICP2, Q9BS21, Q9UCI9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: October 25, 2017
This is version 204 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families