Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Aldose reductase

Gene

AKR1B1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei49Proton donor1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei78Lowers pKa of active site Tyr1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei111Substrate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi10 – 19NADPSequence analysis10
Nucleotide bindingi211 – 273NADP6 PublicationsAdd BLAST63

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • alcohol dehydrogenase (NADP+) activity Source: GO_Central
  • alditol:NADP+ 1-oxidoreductase activity Source: UniProtKB
  • electron transfer activity Source: UniProtKB
  • glyceraldehyde oxidoreductase activity Source: UniProtKB
  • oxidoreductase activity Source: GO_Central

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
LigandNADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:HS01502-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.1.1.188 2681
1.1.1.21 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-196108 Pregnenolone biosynthesis
R-HSA-5652227 Fructose biosynthesis

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P15121

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001112

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:AKR1B1
Synonyms:ALDR1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000085662.13

Human Gene Nomenclature Database

More...
HGNCi
HGNC:381 AKR1B1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
103880 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P15121

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

More...
DisGeNETi
231

Open Targets

More...
OpenTargetsi
ENSG00000085662

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA24675

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1900

Drug and drug target database

More...
DrugBanki
DB07028 (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

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
2768

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
AKR1B1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
113596

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001246232 – 316Aldose reductaseAdd BLAST315

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

More...
EPDi
P15121

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P15121

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P15121

PeptideAtlas

More...
PeptideAtlasi
P15121

PRoteomics IDEntifications database

More...
PRIDEi
P15121

ProteomicsDB human proteome resource

More...
ProteomicsDBi
53108

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P15121

2D gel databases

DOSAC-COBS 2D-PAGE database

More...
DOSAC-COBS-2DPAGEi
P15121

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
IPI00413641
P15121

University College Dublin 2-DE Proteome Database

More...
UCD-2DPAGEi
P15121

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P15121

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P15121

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P15121

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000085662 Expressed in 238 organ(s), highest expression level in adrenal gland

CleanEx database of gene expression profiles

More...
CleanExi
HS_AKR1B1

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P15121 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P15121 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB027391
CAB047353
HPA026425
HPA052751

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.6 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
106732, 44 interactors

Protein interaction database and analysis system

More...
IntActi
P15121, 3 interactors

Molecular INTeraction database

More...
MINTi
P15121

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000285930

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P15121

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1316
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P15121

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P15121

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P15121

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1577 Eukaryota
COG0656 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000153272

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG000020

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P15121

KEGG Orthology (KO)

More...
KOi
K00011

Identification of Orthologs from Complete Genome Data

More...
OMAi
QIELHPM

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0D69

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P15121

TreeFam database of animal gene trees

More...
TreeFami
TF106492

Family and domain databases

Conserved Domains Database

More...
CDDi
cd06660 Aldo_ket_red, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.100, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR018170 Aldo/ket_reductase_CS
IPR020471 Aldo/keto_reductase
IPR023210 NADP_OxRdtase_dom
IPR036812 NADP_OxRdtase_dom_sf

The PANTHER Classification System

More...
PANTHERi
PTHR11732 PTHR11732, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00248 Aldo_ket_red, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000097 AKR, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00069 ALDKETRDTASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51430 SSF51430, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00798 ALDOKETO_REDUCTASE_1, 1 hit
PS00062 ALDOKETO_REDUCTASE_2, 1 hit
PS00063 ALDOKETO_REDUCTASE_3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i1852E8616B5DCEAE
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PCX2E9PCX2_HUMAN
Aldose reductase
AKR1B1
263Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PEF9E9PEF9_HUMAN
Aldose reductase
AKR1B1
102Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS5831.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A39763

NCBI Reference Sequences

More...
RefSeqi
NP_001619.1, NM_001628.3

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.521212

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000285930; ENSP00000285930; ENSG00000085662

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
231

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:231

UCSC genome browser

More...
UCSCi
uc003vrp.2 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
CCDSiCCDS5831.1
PIRiA39763
RefSeqiNP_001619.1, NM_001628.3
UniGeneiHs.521212

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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...

Protein-protein interaction databases

BioGridi106732, 44 interactors
IntActiP15121, 3 interactors
MINTiP15121
STRINGi9606.ENSP00000285930

Chemistry databases

BindingDBiP15121
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
SwissLipidsiSLP:000001112

PTM databases

iPTMnetiP15121
PhosphoSitePlusiP15121
SwissPalmiP15121

Polymorphism and mutation databases

BioMutaiAKR1B1
DMDMi113596

2D gel databases

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

Proteomic databases

EPDiP15121
MaxQBiP15121
PaxDbiP15121
PeptideAtlasiP15121
PRIDEiP15121
ProteomicsDBi53108
TopDownProteomicsiP15121

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
231
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
231
DisGeNETi231
EuPathDBiHostDB:ENSG00000085662.13

GeneCards: human genes, protein and diseases

More...
GeneCardsi
AKR1B1
HGNCiHGNC:381 AKR1B1
HPAiCAB027391
CAB047353
HPA026425
HPA052751
MIMi103880 gene
neXtProtiNX_P15121
OpenTargetsiENSG00000085662
PharmGKBiPA24675

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1577 Eukaryota
COG0656 LUCA
GeneTreeiENSGT00940000153272
HOVERGENiHBG000020
InParanoidiP15121
KOiK00011
OMAiQIELHPM
OrthoDBiEOG091G0D69
PhylomeDBiP15121
TreeFamiTF106492

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

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
AKR1B1 human
EvolutionaryTraceiP15121

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
AKR1B1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
231

Protein Ontology

More...
PROi
PR:P15121

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000085662 Expressed in 238 organ(s), highest expression level in adrenal gland
CleanExiHS_AKR1B1
ExpressionAtlasiP15121 baseline and differential
GenevisibleiP15121 HS

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiALDR_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P15121
Secondary accession number(s): B2R8N3
, Q5U031, Q6FGA4, Q6ICP2, Q9BS21, Q9UCI9
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 214 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again