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P15121

- ALDR_HUMAN

UniProt

P15121 - ALDR_HUMAN

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Protein

Aldose reductase

Gene

AKR1B1

Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei49 – 491Proton donor1 Publication
Sitei78 – 781Lowers pKa of active site Tyr
Binding sitei111 – 1111Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 1910NADPSequence Analysis
Nucleotide bindingi211 – 27363NADP6 PublicationsAdd
BLAST

GO - Molecular functioni

  1. alditol:NADP+ 1-oxidoreductase activity Source: ProtInc
  2. aldo-keto reductase (NADP) activity Source: UniProtKB
  3. electron carrier activity Source: UniProtKB
  4. glyceraldehyde oxidoreductase activity Source: UniProtKB

GO - Biological processi

  1. C21-steroid hormone biosynthetic process Source: Reactome
  2. carbohydrate metabolic process Source: ProtInc
  3. daunorubicin metabolic process Source: UniProtKB
  4. doxorubicin metabolic process Source: UniProtKB
  5. response to stress Source: UniProtKB
  6. small molecule metabolic process Source: Reactome
  7. steroid metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:HS01502-MONOMER.
BRENDAi1.1.1.21. 2681.
ReactomeiREACT_11038. Pregnenolone biosynthesis.
SABIO-RKP15121.

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
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:381. AKR1B1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. extracellular space Source: ProtInc
  4. extracellular vesicular exosome Source: UniProtKB
  5. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi44 – 441D → N: Reduced enzymatic activity. 1 Publication
Mutagenesisi49 – 491Y → F: Complete loss of enzymatic activity. 1 Publication
Mutagenesisi78 – 781K → M: Reduced enzymatic activity. 1 Publication
Mutagenesisi111 – 1111H → N: Reduced enzymatic activity. 1 Publication

Organism-specific databases

PharmGKBiPA24675.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 316315Aldose reductasePRO_0000124623Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei95 – 951N6-acetyllysine1 Publication
Modified residuei222 – 2221N6-acetyllysine1 Publication
Modified residuei263 – 2631N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP15121.
PaxDbiP15121.
PeptideAtlasiP15121.
PRIDEiP15121.

2D gel databases

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

PTM databases

PhosphoSiteiP15121.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP15121.
CleanExiHS_AKR1B1.
ExpressionAtlasiP15121. baseline and differential.
GenevestigatoriP15121.

Organism-specific databases

HPAiCAB018773.
CAB027391.
CAB047353.
HPA026425.
HPA052751.

Interactioni

Subunit structurei

Monomer.6 Publications

Protein-protein interaction databases

BioGridi106732. 9 interactions.
IntActiP15121. 2 interactions.
MINTiMINT-1196717.
STRINGi9606.ENSP00000285930.

Structurei

Secondary structure

1
316
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64Combined sources
Beta strandi12 – 165Combined sources
Helixi25 – 3814Combined sources
Beta strandi42 – 443Combined sources
Helixi47 – 493Combined sources
Helixi52 – 6413Combined sources
Helixi70 – 723Combined sources
Beta strandi74 – 796Combined sources
Helixi81 – 833Combined sources
Turni86 – 883Combined sources
Helixi89 – 10012Combined sources
Beta strandi105 – 1139Combined sources
Beta strandi118 – 1203Combined sources
Beta strandi127 – 1293Combined sources
Helixi138 – 15013Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi157 – 1615Combined sources
Helixi164 – 1718Combined sources
Beta strandi181 – 1866Combined sources
Helixi194 – 2029Combined sources
Beta strandi206 – 2116Combined sources
Beta strandi223 – 2253Combined sources
Turni228 – 2303Combined sources
Helixi232 – 24110Combined sources
Helixi245 – 25511Combined sources
Beta strandi259 – 2613Combined sources
Helixi267 – 2748Combined sources
Helixi283 – 2908Combined sources
Helixi302 – 3043Combined sources
Beta strandi307 – 3093Combined sources
Beta strandi311 – 3144Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP15121.
SMRiP15121. Positions 1-316.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15121.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

eggNOGiCOG0656.
GeneTreeiENSGT00760000119041.
HOVERGENiHBG000020.
InParanoidiP15121.
KOiK00011.
OMAiDFLDTWT.
OrthoDBiEOG70KGQF.
PhylomeDBiP15121.
TreeFamiTF106492.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51L → I in AAA51714. (PubMed:2504709)Curated
Sequence conflicti114 – 1141T → I in CAG47000. 1 PublicationCurated
Sequence conflicti117 – 1171K → R in CAG29347. 1 PublicationCurated
Sequence conflicti142 – 1421W → R in AAH05387. (PubMed:15489334)Curated
Sequence conflicti172 – 1721N → S in CAG29347. 1 PublicationCurated
Sequence conflicti270 – 2723IAE → EAA AA sequence (PubMed:2492527)Curated
Sequence conflicti307 – 3071H → M AA sequence (PubMed:8343525)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151I → F.
Corresponds to variant rs5054 [ dbSNP | Ensembl ].
VAR_014743
Natural varianti42 – 421H → L.
Corresponds to variant rs5056 [ dbSNP | Ensembl ].
VAR_014744
Natural varianti73 – 731L → V.
Corresponds to variant rs5057 [ dbSNP | Ensembl ].
VAR_014745
Natural varianti90 – 901K → E.
Corresponds to variant rs2229542 [ dbSNP | Ensembl ].
VAR_048213
Natural varianti204 – 2041G → S.
Corresponds to variant rs5061 [ dbSNP | Ensembl ].
VAR_014746
Natural varianti288 – 2881T → I.
Corresponds to variant rs5062 [ dbSNP | Ensembl ].
VAR_014747

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_001628.2.
UniGeneiHs.521212.

Genome annotation databases

EnsembliENST00000285930; ENSP00000285930; ENSG00000085662.
GeneIDi231.
KEGGihsa:231.
UCSCiuc003vrp.1. human.

Polymorphism databases

DMDMi113596.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

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 .
CCDSi CCDS5831.1.
PIRi A39763.
RefSeqi NP_001619.1. NM_001628.2.
UniGenei Hs.521212.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 2-316 [» ]
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 2-316 [» ]
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 2-316 [» ]
2ACR X-ray 1.76 A 2-316 [» ]
2ACS X-ray 1.76 A 2-316 [» ]
2ACU X-ray 1.76 A 2-316 [» ]
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 6-316 [» ]
2FZD X-ray 1.08 A 6-316 [» ]
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 2-316 [» ]
2INZ X-ray 1.95 A 2-316 [» ]
2IPW X-ray 2.00 A 2-316 [» ]
2IQ0 X-ray 1.95 A 2-316 [» ]
2IQD X-ray 2.00 A 2-316 [» ]
2IS7 X-ray 1.70 A 2-316 [» ]
2ISF X-ray 2.00 A 2-316 [» ]
2J8T X-ray 0.82 A 6-316 [» ]
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 [» ]
3LBO X-ray 1.10 A 1-316 [» ]
3LD5 X-ray 1.27 A 1-316 [» ]
3LEN X-ray 1.21 A 1-316 [» ]
3LEP X-ray 0.99 A 1-316 [» ]
3LQG X-ray 1.35 A 1-316 [» ]
3LQL X-ray 1.13 A 1-316 [» ]
3LZ3 X-ray 1.03 A 1-316 [» ]
3LZ5 X-ray 0.95 A 1-316 [» ]
3M0I X-ray 1.07 A 1-316 [» ]
3M4H X-ray 0.94 A 1-316 [» ]
3M64 X-ray 1.30 A 1-316 [» ]
3MB9 X-ray 1.65 A 1-316 [» ]
3MC5 X-ray 1.14 A 1-316 [» ]
3ONB X-ray 1.45 A 2-316 [» ]
3ONC X-ray 1.06 A 2-316 [» ]
3P2V X-ray 1.69 A 1-316 [» ]
3Q65 X-ray 2.09 A/B 1-316 [» ]
3Q67 X-ray 1.55 A/B 1-316 [» ]
3RX2 X-ray 1.90 A 1-316 [» ]
3RX3 X-ray 1.90 A 1-316 [» ]
3RX4 X-ray 2.00 A 1-316 [» ]
3S3G X-ray 1.80 A 1-316 [» ]
3T42 X-ray 1.28 A 1-316 [» ]
3U2C X-ray 1.00 A 1-316 [» ]
3V35 X-ray 1.90 A 1-316 [» ]
3V36 X-ray 2.00 A 1-316 [» ]
4GCA X-ray 0.90 A 2-316 [» ]
4GQ0 X-ray 2.10 A 1-316 [» ]
4IGS X-ray 0.85 A 1-316 [» ]
4JIR X-ray 2.00 A 1-316 [» ]
4LAU X-ray 0.84 A 1-316 [» ]
4LAZ X-ray 0.85 A 1-316 [» ]
4LB3 X-ray 0.80 A 1-316 [» ]
4LB4 X-ray 0.80 A 1-316 [» ]
4LBR X-ray 0.80 A 1-316 [» ]
4LBS X-ray 0.76 A 1-316 [» ]
ProteinModelPortali P15121.
SMRi P15121. Positions 1-316.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106732. 9 interactions.
IntActi P15121. 2 interactions.
MINTi MINT-1196717.
STRINGi 9606.ENSP00000285930.

Chemistry

BindingDBi P15121.
ChEMBLi CHEMBL1900.
DrugBanki DB00605. Sulindac.
GuidetoPHARMACOLOGYi 2768.

PTM databases

PhosphoSitei P15121.

Polymorphism databases

DMDMi 113596.

2D gel databases

DOSAC-COBS-2DPAGE P15121.
REPRODUCTION-2DPAGE IPI00413641.
P15121.
UCD-2DPAGE P15121.

Proteomic databases

MaxQBi P15121.
PaxDbi P15121.
PeptideAtlasi P15121.
PRIDEi P15121.

Protocols and materials databases

DNASUi 231.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000285930 ; ENSP00000285930 ; ENSG00000085662 .
GeneIDi 231.
KEGGi hsa:231.
UCSCi uc003vrp.1. human.

Organism-specific databases

CTDi 231.
GeneCardsi GC07M134127.
HGNCi HGNC:381. AKR1B1.
HPAi CAB018773.
CAB027391.
CAB047353.
HPA026425.
HPA052751.
MIMi 103880. gene.
neXtProti NX_P15121.
PharmGKBi PA24675.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0656.
GeneTreei ENSGT00760000119041.
HOVERGENi HBG000020.
InParanoidi P15121.
KOi K00011.
OMAi DFLDTWT.
OrthoDBi EOG70KGQF.
PhylomeDBi P15121.
TreeFami TF106492.

Enzyme and pathway databases

BioCyci MetaCyc:HS01502-MONOMER.
BRENDAi 1.1.1.21. 2681.
Reactomei REACT_11038. Pregnenolone biosynthesis.
SABIO-RK P15121.

Miscellaneous databases

ChiTaRSi AKR1B1. human.
EvolutionaryTracei P15121.
GeneWikii AKR1B1.
GenomeRNAii 231.
NextBioi 938.
PROi P15121.
SOURCEi Search...

Gene expression databases

Bgeei P15121.
CleanExi HS_AKR1B1.
ExpressionAtlasi P15121. baseline and differential.
Genevestigatori P15121.

Family and domain databases

Gene3Di 3.20.20.100. 1 hit.
InterProi IPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view ]
PANTHERi PTHR11732. PTHR11732. 1 hit.
Pfami PF00248. Aldo_ket_red. 1 hit.
[Graphical view ]
PIRSFi PIRSF000097. AKR. 1 hit.
PRINTSi PR00069. ALDKETRDTASE.
SUPFAMi SSF51430. SSF51430. 1 hit.
PROSITEi PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.
    , 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. 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. 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.

Entry informationi

Entry nameiALDR_HUMAN
AccessioniPrimary (citable) accession number: P15121
Secondary accession number(s): B2R8N3
, Q5U031, Q6FGA4, Q6ICP2, Q9BS21, Q9UCI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 175 of the entry and version 3 of the sequence. [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

External Data

Dasty 3