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Entry version 143 (16 Oct 2019)
Sequence version 2 (23 Jan 2007)
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Protein

Aldo-keto reductase family 1 member A1

Gene

Akr1a1

Organism
Rattus norvegicus (Rat)
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. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides and bile acids (By similarity) (PubMed:22820017, PubMed:25152401). Plays an important role in ascorbic acid biosynthesis by catalyzing the reduction of D-glucuronic acid and D-glucurono-gamma-lactone (PubMed:22820017). Functions as a detoxifiying enzyme by reducing a range of toxic aldehydes. Reduces methylglyoxal and 3-deoxyglucosone, which are present at elevated levels under hyperglycemic conditions and are cytotoxic (PubMed:8500767, PubMed:25152401). Involved also in the detoxification of lipid-derived aldehydes like acrolein (PubMed:25152401). Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs (By similarity). Displays no reductase activity towards retinoids (By similarity).By similarity3 Publications

<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 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 3.0 sec(-1) for D,L glyceraldehyde as substrate (PubMed:22820017). kcat is 3.0 sec(-1) for methylglyoxal as substrate (PubMed:22820017). kcat is 3.4 sec(-1) for 3-deoxyglucosone as substrate (PubMed:22820017). kcat is 3.1 sec(-1) for D-glucuronic acid as substrate (PubMed:22820017). kcat is 3.7 sec(-1) for D-glucurono-gamma-lactone acid as substrate (PubMed:22820017).1 Publication
  1. KM=2.9 mM for D,L glyceraldehyde1 Publication
  2. KM=1.8 mM for D-glucuronic acid1 Publication
  3. KM=0.31 mM for methylglyoxal1 Publication
  4. KM=0.63 mM for 3-deoxyglucosone1 Publication
  5. KM=11 mM for D-glucurono-gamma-lactone1 Publication
  6. KM=2.4 mM for acrolein1 Publication
  7. KM=0.260 mM for mevaldate1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei50Proton donorBy similarity1
    <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>Sitei80Lowers pKa of active site TyrBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei113SubstrateBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi11 – 20NADPSequence analysis10
    Nucleotide bindingi211 – 273NADPBy similarityAdd 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

    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

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-RNO-156590 Glutathione conjugation
    R-RNO-5661270 Formation of xylulose-5-phosphate

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P51635

    <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 A1 (EC:1.1.1.22 Publications, EC:1.1.1.331 Publication, EC:1.1.1.3721 Publication, EC:1.1.1.541 Publication)
    Alternative name(s):
    3-DG-reducing enzyme1 Publication
    Alcohol dehydrogenase [NADP(+)]
    Aldehyde reductase1 Publication
    Glucuronate reductase1 Publication (EC:1.1.1.191 Publication)
    Glucuronolactone reductase1 Publication (EC:1.1.1.201 Publication)
    <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:Akr1a1
    Synonyms:Alr
    <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>OrganismiRattus norvegicus (Rat)
    <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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
    <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
    • UP000002494 <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 5

    Organism-specific databases

    Rat genome database

    More...
    RGDi
    68346 Akr1a1

    <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 & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    <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

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3871

    DrugCentral

    More...
    DrugCentrali
    P51635

    <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 methionineiRemoved1 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_00001246202 – 325Aldo-keto reductase family 1 member A1Add BLAST324

    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-acetylthreonine1 Publication1
    Modified residuei4PhosphoserineCombined sources1
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi23N-linked (Glc) (glycation) lysine1 Publication1
    Modified residuei38PhosphoserineBy similarity1
    Glycosylationi68N-linked (Glc) (glycation) lysine1 Publication1
    Glycosylationi85N-linked (Glc) (glycation) lysine1 Publication1
    Modified residuei127N6-acetyllysine; alternateBy similarity1
    Modified residuei127N6-succinyllysine; alternateBy similarity1
    Glycosylationi141N-linked (Glc) (glycation) lysine1 Publication1
    Modified residuei145N6-succinyllysineBy similarity1
    Glycosylationi153N-linked (Glc) (glycation) lysine1 Publication1
    Modified residuei211PhosphoserineBy similarity1

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei13Not glycated1 Publication1
    Sitei30Not glycated1 Publication1
    Sitei34Not glycated1 Publication1
    Sitei61Not glycated1 Publication1
    Sitei80Not glycated1 Publication1
    Sitei97Not glycated1 Publication1
    Sitei127Not glycated1 Publication1
    Sitei134Not glycated1 Publication1
    Sitei145Not glycated1 Publication1
    Sitei157Not glycated1 Publication1
    Sitei240Not glycated1 Publication1
    Sitei257Not glycated1 Publication1
    Sitei263Not glycated1 Publication1
    Sitei287Not glycated1 Publication1
    Sitei294Not glycated1 Publication1
    Sitei308Not glycated1 Publication1

    Keywords - PTMi

    Acetylation, Glycation, Glycoprotein, Phosphoprotein

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P51635

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

    More...
    PaxDbi
    P51635

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P51635

    2D gel databases

    The World-2DPAGE database

    More...
    World-2DPAGEi
    0004:P51635

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P51635

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

    More...
    PhosphoSitePlusi
    P51635

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    P51635

    <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

    Widely expressed.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSRNOG00000016727 Expressed in 10 organ(s), highest expression level in adult mammalian kidney

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P51635 RN

    <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.

    By similarity

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    10116.ENSRNOP00000023072

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P51635

    <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

    3D structure databases

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

    More...
    SMRi
    P51635

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <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
    ENSGT00940000156539

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000250272

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P51635

    KEGG Orthology (KO)

    More...
    KOi
    K00002

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    WATYNTR

    Database of Orthologous Groups

    More...
    OrthoDBi
    1016440at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P51635

    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>. The information is filed in different subsections. The current subsections and their content are listed below:<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.

    <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.

    P51635-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTASSVLLHT GQKMPLIGLG TWKSEPGQVK AAIKYALSVG YRHIDCASVY
    60 70 80 90 100
    GNETEIGEAL KESVGAGKAV PREELFVTSK LWNTKHHPED VEPAVRKTLA
    110 120 130 140 150
    DLQLEYLDLY LMHWPYAFER GDNPFPKNAD GTVKYDSTHY KETWKALEAL
    160 170 180 190 200
    VAKGLVKALG LSNFSSRQID DVLSVASVRP AVLQVECHPY LAQNELIAHC
    210 220 230 240 250
    QARGLEVTAY SPLGSSDRAW RHPDEPVLLE EPVVLALAEK HGRSPAQILL
    260 270 280 290 300
    RWQVQRKVIC IPKSITPSRI LQNIQVFDFT FSPEEMKQLD ALNKNWRYIV
    310 320
    PMITVDGKRV PRDAGHPLYP FNDPY
    Length:325
    Mass (Da):36,506
    Last modified:January 23, 2007 - 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:iF95573B7411884DA
    GO

    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
    D10854 mRNA Translation: BAA01627.1
    BC059133 mRNA Translation: AAH59133.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    JN0629

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_112262.1, NM_031000.3

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENSRNOT00000023072; ENSRNOP00000023072; ENSRNOG00000016727

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    78959

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    rno:78959

    UCSC genome browser

    More...
    UCSCi
    RGD:68346 rat

    <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
    D10854 mRNA Translation: BAA01627.1
    BC059133 mRNA Translation: AAH59133.1
    PIRiJN0629
    RefSeqiNP_112262.1, NM_031000.3

    3D structure databases

    SMRiP51635
    ModBaseiSearch...

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000023072

    Chemistry databases

    BindingDBiP51635
    ChEMBLiCHEMBL3871
    DrugCentraliP51635

    PTM databases

    iPTMnetiP51635
    PhosphoSitePlusiP51635
    SwissPalmiP51635

    2D gel databases

    World-2DPAGEi0004:P51635

    Proteomic databases

    jPOSTiP51635
    PaxDbiP51635
    PRIDEiP51635

    Genome annotation databases

    EnsembliENSRNOT00000023072; ENSRNOP00000023072; ENSRNOG00000016727
    GeneIDi78959
    KEGGirno:78959
    UCSCiRGD:68346 rat

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    10327
    RGDi68346 Akr1a1

    Phylogenomic databases

    eggNOGiKOG1577 Eukaryota
    COG0656 LUCA
    GeneTreeiENSGT00940000156539
    HOGENOMiHOG000250272
    InParanoidiP51635
    KOiK00002
    OMAiWATYNTR
    OrthoDBi1016440at2759
    PhylomeDBiP51635
    TreeFamiTF106492

    Enzyme and pathway databases

    ReactomeiR-RNO-156590 Glutathione conjugation
    R-RNO-5661270 Formation of xylulose-5-phosphate
    SABIO-RKiP51635

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P51635

    Gene expression databases

    BgeeiENSRNOG00000016727 Expressed in 10 organ(s), highest expression level in adult mammalian kidney
    GenevisibleiP51635 RN

    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
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    MobiDB: a database of protein disorder and mobility annotations

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    MobiDBi
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    <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 nameiAK1A1_RAT
    <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: P51635
    <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: October 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 16, 2019
    This is version 143 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

    <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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

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