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Entry version 172 (13 Feb 2019)
Sequence version 2 (08 Feb 2011)
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Protein

Aldo-keto reductase family 1 member B10

Gene

AKR1B10

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 (PubMed:9565553, PubMed:18087047, PubMed:12732097, PubMed:19013440, PubMed:19563777). Displays strong enzymatic activity toward all-trans-retinal, 9-cis-retinal, and 13-cis-retinal (PubMed:12732097, PubMed:18087047). Plays a critical role in detoxifying dietary and lipid-derived unsaturated carbonyls, such as crotonaldehyde, 4-hydroxynonenal, trans-2-hexenal, trans-2,4-hexadienal and their glutathione-conjugates carbonyls (GS-carbonyls) (PubMed:19013440, PubMed:19563777). Displays no reductase activity towards glucose (PubMed:12732097).5 Publications

Miscellaneous

Has no counterpart in murine and rat species.Curated

<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

Retinaldehyde reductase activity is inhibited by tolrestat.2 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 640 min(-1) for glyceraldehyde as substrate (PubMed:12732097). kcat is 185 min(-1) for pyridine-3-aldehyde as substrate (PubMed:12732097). kcat is 116 min(-1) for acrolein as substrate. kcat is 103 min(-1) for 3-methyl-2-butenal as substrate. kcat is 97 min(-1) for(E)-2-hexenal as substrate. kcat is 82 min(-1) for (E,E)-2,4-hexadienal as substrate. kcat is 120 min(-1) for 4-hydroxynonenal as substrate. kcat is 3 min(-1) for GS-acrolein as substrate. kcat is 70 min(-1) for GS-3-methyl-2-butenal as substrate. kcat is 71 min(-1) for GS-(E)-2-hexenal as substrate. kcat is 147 min(-1) for (E,E)-2,4-hexadienal as substrate (PubMed:19563777). kcat is 35 min(-1) for D,L-glyceraldehyde as substrate. kcat is 27 min(-1) for all-trans-retinal as substrate. kcat is 1 min(-1) for 9-cis-retinal as substrate (PubMed:18087047). kcat is 43 min(-1) for 4-hydroxynon-2-enal (PubMed:19013440). kcat is 40 min(-1) for (E)-4-oxonon-2-enal (PubMed:19013440). kcat is 25 min(-1) for 4-methylpentanal (PubMed:19013440).4 Publications
  1. KM=6000 µM for D,L-glyceraldehyde1 Publication
  2. KM=0.6 µM for all-trans-retinal1 Publication
  3. KM=0.7 µM for 9-cis-retinal1 Publication
  4. KM=37 µM for pyridine-3-aldehyde1 Publication
  5. KM=110 µM for acrolein1 Publication
  6. KM=87 µM for 3-methyl-2-butenal1 Publication
  7. KM=30 µM for 4-hydroxynonenal1 Publication
  8. KM=61 µM for (E)-2-hexenal1 Publication
  9. KM=95 µM for (E,E)-2,4-hexadienal1 Publication
  10. KM=532 µM for GS-acrolein1 Publication
  11. KM=245 µM for GS-3-methyl-2-butenal1 Publication
  12. KM=145 µM for GS-(E)-2-hexenal1 Publication
  13. KM=77 µM for GS-(E,E)-2,4-hexadienal1 Publication
  14. KM=330 µM for (E)-4-hydroxynon-2-enal1 Publication
  15. KM=300 µM for (E)-4-oxonon-2-enal1 Publication
  16. KM=50 µM for 4-methylpentanal1 Publication
  1. Vmax=3122 nmol/min/mg enzyme with acrolein1 Publication
  2. Vmax=2647 nmol/min/mg enzyme with 3-methyl-2-butenal as substrate1 Publication
  3. Vmax=2658 nmol/min/mg enzyme with (E)-2-hexenal as substrate1 Publication
  4. Vmax=2160 nmol/min/mg enzyme with (E,E)-2,4-hexadienal as substrate1 Publication
  5. Vmax=3298 nmol/min/mg enzyme with 4-hydroxynonenal1 Publication
  6. Vmax=64 nmol/min/mg enzyme with GS-acrolein1 Publication
  7. Vmax=1960 nmol/min/mg enzyme with GS-3-methyl-2-butenal as substrate1 Publication
  8. Vmax=2049 nmol/min/mg enzyme with GS-(E)-2-hexenal1 Publication
  9. Vmax=4004 nmol/min/mg enzyme with GS-(E,E)-2,4-hexadienal as substrate1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: retinol metabolism

This protein is involved in the pathway retinol metabolism, which is part of Cofactor metabolism.2 Publications
View all proteins of this organism that are known to be involved in the pathway retinol metabolism and in Cofactor metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei44NADP1 Publication1
<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 TyrBy similarity1
Binding sitei111Substrate1 Publication1
Binding sitei184NADP1 Publication1

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 bindingi20 – 22NADP1 Publication3
Nucleotide bindingi160 – 161NADP1 Publication2
Nucleotide bindingi210 – 217NADP1 Publication8
Nucleotide bindingi261 – 273NADP1 PublicationAdd BLAST13

<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: UniProtKB
  • alditol:NADP+ 1-oxidoreductase activity Source: GO_Central
  • aldo-keto reductase (NADP) activity Source: UniProtKB
  • geranylgeranyl reductase activity Source: UniProtKB
  • indanol dehydrogenase activity Source: UniProtKB
  • NADP-retinol dehydrogenase activity Source: UniProtKB
  • oxidoreductase activity Source: GO_Central
  • retinal dehydrogenase activity Source: UniProtKB

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

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.1.1.21 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-975634 Retinoid metabolism and transport

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
O60218

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00912

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001873

<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:
Aldo-keto reductase family 1 member B10 (EC:1.1.1.3001 Publication, EC:1.1.1.541 Publication)
Alternative name(s):
ARL-11 Publication
Aldose reductase-like
Aldose reductase-related protein
Short name:
ARP
Short name:
hARP
Small intestine reductase
Short name:
SI reductase
<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:AKR1B10
Synonyms:AKR1B11
<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:ENSG00000198074.9

Human Gene Nomenclature Database

More...
HGNCi
HGNC:382 AKR1B10

Online Mendelian Inheritance in Man (OMIM)

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MIMi
604707 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O60218

<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

Lysosome, Secreted

<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>Mutagenesisi125K → L: Increased affinity and reduced catalytic activity towards all-trans-retinaldehyde. 1 Publication1
Mutagenesisi299C → S: Decreased affinity and reduced catalytic activity towards 4-hydroxynonenal. 1 Publication1
Mutagenesisi301V → L: Reduced catalytic activity towards all-trans-retinaldehyde. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
57016

Open Targets

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OpenTargetsi
ENSG00000198074

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA24676

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5983

Drug and drug target database

More...
DrugBanki
DB03461 2'-Monophosphoadenosine 5'-Diphosphoribose
DB02383 Tolrestat

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
AKR1B10

<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 ‘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_00001246321 – 316Aldo-keto reductase family 1 member B10Add BLAST316

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 residuei125N6-acetyllysineCombined sources1
Modified residuei263N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O60218

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O60218

MaxQB - The MaxQuant DataBase

More...
MaxQBi
O60218

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

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PaxDbi
O60218

PeptideAtlas

More...
PeptideAtlasi
O60218

PRoteomics IDEntifications database

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PRIDEi
O60218

ProteomicsDB human proteome resource

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ProteomicsDBi
49247

2D gel databases

DOSAC-COBS 2D-PAGE database

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DOSAC-COBS-2DPAGEi
O60218

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O60218

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

More...
PhosphoSitePlusi
O60218

<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

Found in many tissues. Highly expressed in small intestine, colon and adrenal gland.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Overexpressed in certain types of cancers, including hepatocellular carcinoma and lung cancer associated with tobacco smoking.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000198074 Expressed in 137 organ(s), highest expression level in jejunal mucosa

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O60218 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB070163
HPA020280
HPA073633

<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%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
121325, 18 interactors

Protein interaction database and analysis system

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IntActi
O60218, 5 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000352584

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
O60218

<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

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZUAX-ray1.25X1-316[»]
4GA8X-ray1.94A1-316[»]
4GABX-ray1.60A1-316[»]
4GQ0X-ray2.10A1-316[»]
4GQGX-ray1.92A1-316[»]
4I5XX-ray2.10A1-316[»]
4ICCX-ray1.75X1-316[»]
4JIHX-ray2.30A1-316[»]
4JIIX-ray2.20X1-316[»]
4WEVX-ray1.45X1-316[»]
4XZLX-ray1.70X1-316[»]
4XZMX-ray1.75X1-316[»]
4XZNX-ray1.70X1-316[»]
5LIKX-ray2.05X1-316[»]
5LIUX-ray1.75X1-316[»]
5LIWX-ray1.75X1-316[»]
5LIXX-ray1.95X1-316[»]
5LIYX-ray2.05X1-316[»]
5M2FX-ray1.50X1-316[»]
5Y7NX-ray2.50A1-316[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O60218

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

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SMRi
O60218

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
O60218

<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

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eggNOGi
KOG1577 Eukaryota
COG0656 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000154773

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000250272

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG000020

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O60218

KEGG Orthology (KO)

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KOi
K00011

Identification of Orthologs from Complete Genome Data

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OMAi
KKHYPDW

Database of Orthologous Groups

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OrthoDBi
1016440at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O60218

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

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Gene3Di
3.20.20.100, 1 hit

Integrated resource of protein families, domains and functional sites

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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

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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>Sequencei

<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.

O60218-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATFVELSTK AKMPIVGLGT WKSPLGKVKE AVKVAIDAGY RHIDCAYVYQ
60 70 80 90 100
NEHEVGEAIQ EKIQEKAVKR EDLFIVSKLW PTFFERPLVR KAFEKTLKDL
110 120 130 140 150
KLSYLDVYLI HWPQGFKSGD DLFPKDDKGN AIGGKATFLD AWEAMEELVD
160 170 180 190 200
EGLVKALGVS NFSHFQIEKL LNKPGLKYKP VTNQVECHPY LTQEKLIQYC
210 220 230 240 250
HSKGITVTAY SPLGSPDRPW AKPEDPSLLE DPKIKEIAAK HKKTAAQVLI
260 270 280 290 300
RFHIQRNVIV IPKSVTPARI VENIQVFDFK LSDEEMATIL SFNRNWRACN
310
VLQSSHLEDY PFNAEY
Length:316
Mass (Da):36,020
Last modified:February 8, 2011 - v2
<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:i0C2FC0E798955A33
GO

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 conflicti76V → A in AAO13380 (Ref. 3) Curated1
Sequence conflicti100L → P in AAO13380 (Ref. 3) Curated1
Sequence conflicti288T → I in AAO13380 (Ref. 3) 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_02007787P → S. Corresponds to variant dbSNP:rs2303312Ensembl.1
Natural variantiVAR_020078286M → T. Corresponds to variant dbSNP:rs3735042Ensembl.1
Natural variantiVAR_013287313N → DCombined sources6 PublicationsCorresponds to variant dbSNP:rs4728329Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
U37100 mRNA Translation: AAC17469.1
AF052577 mRNA Translation: AAC36465.1
AF524864 mRNA Translation: AAO13380.1
BT006794 mRNA Translation: AAP35440.1
CR541801 mRNA Translation: CAG46600.1
AC078847 Genomic DNA No translation available.
CH236950 Genomic DNA Translation: EAL24069.1
CH471070 Genomic DNA Translation: EAW83816.1
BC008837 mRNA Translation: AAH08837.1
AF044961 mRNA Translation: AAC15671.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS5832.1

NCBI Reference Sequences

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RefSeqi
NP_064695.3, NM_020299.4

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.116724

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000359579; ENSP00000352584; ENSG00000198074

Database of genes from NCBI RefSeq genomes

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GeneIDi
57016

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:57016

UCSC genome browser

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UCSCi
uc003vrr.4 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
U37100 mRNA Translation: AAC17469.1
AF052577 mRNA Translation: AAC36465.1
AF524864 mRNA Translation: AAO13380.1
BT006794 mRNA Translation: AAP35440.1
CR541801 mRNA Translation: CAG46600.1
AC078847 Genomic DNA No translation available.
CH236950 Genomic DNA Translation: EAL24069.1
CH471070 Genomic DNA Translation: EAW83816.1
BC008837 mRNA Translation: AAH08837.1
AF044961 mRNA Translation: AAC15671.1
CCDSiCCDS5832.1
RefSeqiNP_064695.3, NM_020299.4
UniGeneiHs.116724

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZUAX-ray1.25X1-316[»]
4GA8X-ray1.94A1-316[»]
4GABX-ray1.60A1-316[»]
4GQ0X-ray2.10A1-316[»]
4GQGX-ray1.92A1-316[»]
4I5XX-ray2.10A1-316[»]
4ICCX-ray1.75X1-316[»]
4JIHX-ray2.30A1-316[»]
4JIIX-ray2.20X1-316[»]
4WEVX-ray1.45X1-316[»]
4XZLX-ray1.70X1-316[»]
4XZMX-ray1.75X1-316[»]
4XZNX-ray1.70X1-316[»]
5LIKX-ray2.05X1-316[»]
5LIUX-ray1.75X1-316[»]
5LIWX-ray1.75X1-316[»]
5LIXX-ray1.95X1-316[»]
5LIYX-ray2.05X1-316[»]
5M2FX-ray1.50X1-316[»]
5Y7NX-ray2.50A1-316[»]
ProteinModelPortaliO60218
SMRiO60218
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121325, 18 interactors
IntActiO60218, 5 interactors
STRINGi9606.ENSP00000352584

Chemistry databases

BindingDBiO60218
ChEMBLiCHEMBL5983
DrugBankiDB03461 2'-Monophosphoadenosine 5'-Diphosphoribose
DB02383 Tolrestat
SwissLipidsiSLP:000001873

PTM databases

iPTMnetiO60218
PhosphoSitePlusiO60218

Polymorphism and mutation databases

BioMutaiAKR1B10

2D gel databases

DOSAC-COBS-2DPAGEiO60218

Proteomic databases

EPDiO60218
jPOSTiO60218
MaxQBiO60218
PaxDbiO60218
PeptideAtlasiO60218
PRIDEiO60218
ProteomicsDBi49247

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
57016
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359579; ENSP00000352584; ENSG00000198074
GeneIDi57016
KEGGihsa:57016
UCSCiuc003vrr.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
57016
DisGeNETi57016
EuPathDBiHostDB:ENSG00000198074.9

GeneCards: human genes, protein and diseases

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GeneCardsi
AKR1B10

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0007102
HIX0033661
HGNCiHGNC:382 AKR1B10
HPAiCAB070163
HPA020280
HPA073633
MIMi604707 gene
neXtProtiNX_O60218
OpenTargetsiENSG00000198074
PharmGKBiPA24676

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1577 Eukaryota
COG0656 LUCA
GeneTreeiENSGT00940000154773
HOGENOMiHOG000250272
HOVERGENiHBG000020
InParanoidiO60218
KOiK00011
OMAiKKHYPDW
OrthoDBi1016440at2759
PhylomeDBiO60218
TreeFamiTF106492

Enzyme and pathway databases

UniPathwayi
UPA00912

BRENDAi1.1.1.21 2681
ReactomeiR-HSA-975634 Retinoid metabolism and transport
SABIO-RKiO60218

Miscellaneous databases

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

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ChiTaRSi
AKR1B10 human
EvolutionaryTraceiO60218

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
AKR1B10

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

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GenomeRNAii
57016

Protein Ontology

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PROi
PR:O60218

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000198074 Expressed in 137 organ(s), highest expression level in jejunal mucosa
GenevisibleiO60218 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

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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 nameiAK1BA_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: O60218
Secondary accession number(s): A4D1P1
, O75890, Q6FHF3, Q8IWZ1
<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: May 10, 2002
Last sequence update: February 8, 2011
Last modified: February 13, 2019
This is version 172 of the entry and version 2 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, 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 entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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