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Protein

Aldose reductase

Gene

AKR1B1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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: UniProtKB
  • electron transfer 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
MIMi103880 gene
neXtProtiNX_P15121

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
ProteomicsDBi53108
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
MINTiP15121
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[»]
5OU0X-ray0.94A1-316[»]
5OUJX-ray0.96A1-316[»]
5OUKX-ray0.96A1-316[»]
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: June 20, 2018
This is version 210 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

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