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Protein

Aldo-keto reductase family 1 member C2

Gene

AKR1C2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Works in concert with the 5-alpha/5-beta-steroid reductases to convert steroid hormones into the 3-alpha/5-alpha and 3-alpha/5-beta-tetrahydrosteroids. Catalyzes the inactivation of the most potent androgen 5-alpha-dihydrotestosterone (5-alpha-DHT) to 5-alpha-androstane-3-alpha,17-beta-diol (3-alpha-diol). Has a high bile-binding ability.4 Publications

Catalytic activityi

Trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH.
A 3-alpha-hydroxysteroid + NAD(P)+ = a 3-oxosteroid + NAD(P)H.

Enzyme regulationi

Inhibited by hexestrol with an IC50 of 2.8 µM, 1,10-phenanthroline with an IC50 of 2100 µM, 1,7-phenanthroline with an IC50 of 1500 µM, flufenamic acid with an IC50 of 0.9 µM, indomethacin with an IC50 of 75 µM, ibuprofen with an IC50 of 6.9 µM, lithocholic acid with an IC50 of 0.07 µM, ursodeoxycholic acid with an IC50 of 0.08 µM and chenodeoxycholic acid with an IC50 of 0.13 µM.1 Publication

Kineticsi

  1. KM=260 µM for (s)-tetralol1 Publication
  2. KM=520 µM for (s)-indan-1-ol1 Publication
  3. KM=5000 µM for benzene dihydrodiol1 Publication
  4. KM=1 µM for 5-beta-pregnane-3-alpha,20-alpha-diol1 Publication
  5. KM=208 µM for 9-alpha,11-beta-PGF21 Publication
  6. KM=0.3 µM for 5-beta-androstane-3,17-dione1 Publication
  7. KM=79 µM for PGD21 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei24 – 241SubstrateBy similarity
    Binding sitei50 – 501NADP5 Publications
    Active sitei55 – 551Proton donor
    Sitei84 – 841Lowers pKa of active site TyrBy similarity
    Binding sitei117 – 1171Substrate
    Binding sitei190 – 1901NADP5 Publications
    Binding sitei222 – 2221SubstrateBy similarity
    Binding sitei227 – 2271Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi20 – 245NADP5 Publications
    Nucleotide bindingi166 – 1672NADP5 Publications
    Nucleotide bindingi216 – 2227NADP5 Publications
    Nucleotide bindingi270 – 28011NADP5 PublicationsAdd
    BLAST

    GO - Molecular functioni

    • alditol:NADP+ 1-oxidoreductase activity Source: UniProtKB
    • bile acid binding Source: UniProtKB
    • carboxylic acid binding Source: UniProtKB
    • ketosteroid monooxygenase activity Source: UniProtKB
    • oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor Source: UniProtKB
    • phenanthrene 9,10-monooxygenase activity Source: UniProtKB
    • trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity Source: UniProtKB

    GO - Biological processi

    • cellular response to jasmonic acid stimulus Source: UniProtKB
    • cellular response to prostaglandin D stimulus Source: UniProtKB
    • daunorubicin metabolic process Source: UniProtKB
    • digestion Source: UniProtKB
    • doxorubicin metabolic process Source: UniProtKB
    • epithelial cell differentiation Source: UniProtKB
    • G-protein coupled receptor signaling pathway Source: UniProtKB
    • oxidation-reduction process Source: UniProtKB
    • positive regulation of cell proliferation Source: UniProtKB
    • positive regulation of protein kinase B signaling Source: UniProtKB
    • progesterone metabolic process Source: UniProtKB
    • prostaglandin metabolic process Source: UniProtKB
    • steroid metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Lipid metabolism, Steroid metabolism

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:HS07754-MONOMER.
    BRENDAi1.1.1.213. 2681.
    1.1.1.357. 2681.
    1.3.1.20. 2681.
    ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    REACT_11048. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
    REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
    SABIO-RKP52895.
    SignaLinkiP52895.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aldo-keto reductase family 1 member C2 (EC:1.-.-.-)
    Alternative name(s):
    3-alpha-HSD3
    Chlordecone reductase homolog HAKRD
    Dihydrodiol dehydrogenase 2
    Short name:
    DD-2
    Short name:
    DD2
    Dihydrodiol dehydrogenase/bile acid-binding protein
    Short name:
    DD/BABP
    Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase (EC:1.3.1.20)
    Type III 3-alpha-hydroxysteroid dehydrogenase (EC:1.1.1.357)
    Gene namesi
    Name:AKR1C2
    Synonyms:DDH2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:385. AKR1C2.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    46,XY sex reversal 8 (SRXY8)1 Publication

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA disorder of sex development. Affected individuals have a 46,XY karyotype but present as phenotypically normal females.

    See also OMIM:614279
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti79 – 791I → V in SRXY8; partially impaired activity. 1 Publication
    VAR_066632
    Natural varianti90 – 901H → Q in SRXY8; partially impaired activity. 1 Publication
    VAR_066633
    Natural varianti222 – 2221H → Q in SRXY8; partially impaired activity. 1 Publication
    VAR_066634
    Natural varianti300 – 3001N → T in SRXY8; partially impaired activity. 1 Publication
    VAR_066635

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi24 – 241Y → A: Strongly decreases affinity for androstenedione. Decreases androstenedione reductase activity about 60-fold. 1 Publication
    Mutagenesisi31 – 311K → A or M: Increases the low androstenedione reductase activity. 1 Publication
    Mutagenesisi301 – 3011R → A: Decreases 3-alpha-hydroxysteroid reductase activity about 50-fold. 1 Publication
    Mutagenesisi304 – 3041R → A: Decreases 3-alpha-hydroxysteroid reductase activity about 500-fold. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi614279. phenotype.
    Orphaneti90796. 46,XY disorder of sex development due to isolated 17,20 lyase deficiency.
    PharmGKBiPA24678.

    Chemistry

    DrugBankiDB01586. Ursodeoxycholic acid.

    Polymorphism and mutation databases

    BioMutaiAKR1C2.
    DMDMi20532374.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 323323Aldo-keto reductase family 1 member C2PRO_0000124637Add
    BLAST

    Proteomic databases

    MaxQBiP52895.
    PaxDbiP52895.
    PRIDEiP52895.

    PTM databases

    PhosphoSiteiP52895.

    Expressioni

    Tissue specificityi

    Expressed in fetal testes. Expressed in fetal and adult adrenal glands.1 Publication

    Gene expression databases

    BgeeiP52895.
    CleanExiHS_AKR1C2.
    ExpressionAtlasiP52895. baseline and differential.
    GenevisibleiP52895. HS.

    Organism-specific databases

    HPAiCAB047304.

    Interactioni

    Protein-protein interaction databases

    BioGridi108013. 7 interactions.
    IntActiP52895. 1 interaction.
    STRINGi9606.ENSP00000370129.

    Structurei

    Secondary structure

    1
    323
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 93Combined sources
    Beta strandi15 – 228Combined sources
    Helixi32 – 4413Combined sources
    Beta strandi48 – 503Combined sources
    Helixi53 – 553Combined sources
    Helixi58 – 7013Combined sources
    Helixi76 – 783Combined sources
    Beta strandi80 – 856Combined sources
    Helixi87 – 893Combined sources
    Helixi92 – 943Combined sources
    Helixi95 – 10612Combined sources
    Beta strandi111 – 1166Combined sources
    Beta strandi119 – 1224Combined sources
    Beta strandi124 – 1263Combined sources
    Helixi144 – 15613Combined sources
    Beta strandi159 – 1679Combined sources
    Helixi170 – 1778Combined sources
    Beta strandi187 – 1926Combined sources
    Helixi200 – 2089Combined sources
    Beta strandi212 – 2176Combined sources
    Turni225 – 2273Combined sources
    Helixi235 – 2373Combined sources
    Helixi239 – 24810Combined sources
    Helixi252 – 26211Combined sources
    Beta strandi266 – 2705Combined sources
    Helixi274 – 2807Combined sources
    Helixi281 – 2855Combined sources
    Helixi290 – 2978Combined sources
    Helixi309 – 3113Combined sources
    Beta strandi318 – 3214Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IHIX-ray3.00A/B1-323[»]
    1J96X-ray1.25A/B2-323[»]
    1XJBX-ray1.90A/B2-323[»]
    2HDJX-ray2.00A/B1-323[»]
    2IPJX-ray1.80A/B3-323[»]
    4JQ1X-ray1.60A/B1-323[»]
    4JQ2X-ray1.75A/B1-323[»]
    4JQ3X-ray1.75A/B1-323[»]
    4JQ4X-ray1.52A/B1-323[»]
    4JQAX-ray1.45A/B1-323[»]
    4JTQX-ray1.60A/B1-323[»]
    4JTRX-ray1.30A/B1-323[»]
    4L1WX-ray2.20A/B2-323[»]
    4L1XX-ray2.00A/B2-323[»]
    ProteinModelPortaliP52895.
    SMRiP52895. Positions 2-323.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52895.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Phylogenomic databases

    eggNOGiCOG0656.
    GeneTreeiENSGT00760000119041.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    InParanoidiP52895.
    KOiK00089.
    K00212.
    OMAiRHIDIAY.
    PhylomeDBiP52895.
    TreeFamiTF106492.

    Family and domain databases

    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase_subgr.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 1 hit.
    PfamiPF00248. Aldo_ket_red. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000097. AKR. 1 hit.
    PRINTSiPR00069. ALDKETRDTASE.
    SUPFAMiSSF51430. SSF51430. 1 hit.
    PROSITEiPS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: P52895-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MDSKYQCVKL NDGHFMPVLG FGTYAPAEVP KSKALEAVKL AIEAGFHHID
    60 70 80 90 100
    SAHVYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWSNSH RPELVRPALE
    110 120 130 140 150
    RSLKNLQLDY VDLYLIHFPV SVKPGEEVIP KDENGKILFD TVDLCATWEA
    160 170 180 190 200
    MEKCKDAGLA KSIGVSNFNH RLLEMILNKP GLKYKPVCNQ VECHPYFNQR
    210 220 230 240 250
    KLLDFCKSKD IVLVAYSALG SHREEPWVDP NSPVLLEDPV LCALAKKHKR
    260 270 280 290 300
    TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTS EEMKAIDGLN
    310 320
    RNVRYLTLDI FAGPPNYPFS DEY
    Length:323
    Mass (Da):36,735
    Last modified:May 10, 2002 - v3
    Checksum:i0D7B6F983FCE85E1
    GO
    Isoform 2 (identifier: P52895-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         124-139: PGEEVIPKDENGKILF → EDIGILTWKKSPKHNS
         140-323: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:139
    Mass (Da):15,748
    Checksum:i11CAE1B299B378AC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti76 – 761R → S AA sequence (PubMed:8486699).Curated
    Sequence conflicti87 – 871S → C AA sequence (PubMed:8486699).Curated
    Sequence conflicti93 – 931E → EE AA sequence (PubMed:8486699).Curated
    Sequence conflicti111 – 1111V → A in AAB38486 (PubMed:7959017).Curated
    Sequence conflicti164 – 1641G → R in BAF82993 (PubMed:14702039).Curated
    Sequence conflicti179 – 1791K → E in AAD14013 (PubMed:8274401).Curated
    Sequence conflicti179 – 1791K → E in AAB38486 (PubMed:7959017).Curated
    Sequence conflicti185 – 1851K → E in AAD14013 (PubMed:8274401).Curated
    Sequence conflicti185 – 1851K → E in AAB38486 (PubMed:7959017).Curated
    Sequence conflicti188 – 1881C → H AA sequence (PubMed:8486699).Curated
    Sequence conflicti193 – 1931C → H AA sequence (PubMed:8486699).Curated
    Sequence conflicti319 – 3191F → I in AAD14013 (PubMed:8274401).Curated
    Sequence conflicti319 – 3191F → I in AAB38486 (PubMed:7959017).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti46 – 461F → Y.1 Publication
    Corresponds to variant rs2854482 [ dbSNP | Ensembl ].
    VAR_048216
    Natural varianti79 – 791I → V in SRXY8; partially impaired activity. 1 Publication
    VAR_066632
    Natural varianti90 – 901H → Q in SRXY8; partially impaired activity. 1 Publication
    VAR_066633
    Natural varianti172 – 1721L → Q.
    Corresponds to variant rs11474 [ dbSNP | Ensembl ].
    VAR_014748
    Natural varianti222 – 2221H → Q in SRXY8; partially impaired activity. 1 Publication
    VAR_066634
    Natural varianti300 – 3001N → T in SRXY8; partially impaired activity. 1 Publication
    VAR_066635

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei124 – 13916PGEEV…GKILF → EDIGILTWKKSPKHNS in isoform 2. 1 PublicationVSP_043779Add
    BLAST
    Alternative sequencei140 – 323184Missing in isoform 2. 1 PublicationVSP_043780Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    S68330 mRNA. Translation: AAD14013.1.
    U05598 mRNA. Translation: AAA20937.1.
    L32592 Genomic DNA. Translation: AAB38486.1.
    AB021654 mRNA. Translation: BAA36169.1.
    AB031084 mRNA. Translation: BAA92884.1.
    AB032153 Genomic DNA. Translation: BAA92891.1.
    AK290304 mRNA. Translation: BAF82993.1.
    AK296686 mRNA. Translation: BAG59281.1.
    BT006653 mRNA. Translation: AAP35299.1.
    AL713867, AL391427 Genomic DNA. Translation: CAI16408.1.
    BC007024 mRNA. Translation: AAH07024.1.
    BC063574 mRNA. Translation: AAH63574.1.
    CCDSiCCDS44350.1. [P52895-2]
    CCDS7062.1. [P52895-1]
    PIRiI73676.
    JC5240.
    S61516.
    RefSeqiNP_001128713.1. NM_001135241.2. [P52895-2]
    NP_001345.1. NM_001354.5. [P52895-1]
    NP_995317.1. NM_205845.2. [P52895-1]
    UniGeneiHs.460260.
    Hs.567256.
    Hs.734597.

    Genome annotation databases

    EnsembliENST00000380753; ENSP00000370129; ENSG00000151632.
    ENST00000455190; ENSP00000408440; ENSG00000151632. [P52895-2]
    GeneIDi1646.
    KEGGihsa:1646.
    UCSCiuc001ihs.3. human. [P52895-1]
    uc010qao.2. human. [P52895-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    S68330 mRNA. Translation: AAD14013.1.
    U05598 mRNA. Translation: AAA20937.1.
    L32592 Genomic DNA. Translation: AAB38486.1.
    AB021654 mRNA. Translation: BAA36169.1.
    AB031084 mRNA. Translation: BAA92884.1.
    AB032153 Genomic DNA. Translation: BAA92891.1.
    AK290304 mRNA. Translation: BAF82993.1.
    AK296686 mRNA. Translation: BAG59281.1.
    BT006653 mRNA. Translation: AAP35299.1.
    AL713867, AL391427 Genomic DNA. Translation: CAI16408.1.
    BC007024 mRNA. Translation: AAH07024.1.
    BC063574 mRNA. Translation: AAH63574.1.
    CCDSiCCDS44350.1. [P52895-2]
    CCDS7062.1. [P52895-1]
    PIRiI73676.
    JC5240.
    S61516.
    RefSeqiNP_001128713.1. NM_001135241.2. [P52895-2]
    NP_001345.1. NM_001354.5. [P52895-1]
    NP_995317.1. NM_205845.2. [P52895-1]
    UniGeneiHs.460260.
    Hs.567256.
    Hs.734597.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IHIX-ray3.00A/B1-323[»]
    1J96X-ray1.25A/B2-323[»]
    1XJBX-ray1.90A/B2-323[»]
    2HDJX-ray2.00A/B1-323[»]
    2IPJX-ray1.80A/B3-323[»]
    4JQ1X-ray1.60A/B1-323[»]
    4JQ2X-ray1.75A/B1-323[»]
    4JQ3X-ray1.75A/B1-323[»]
    4JQ4X-ray1.52A/B1-323[»]
    4JQAX-ray1.45A/B1-323[»]
    4JTQX-ray1.60A/B1-323[»]
    4JTRX-ray1.30A/B1-323[»]
    4L1WX-ray2.20A/B2-323[»]
    4L1XX-ray2.00A/B2-323[»]
    ProteinModelPortaliP52895.
    SMRiP52895. Positions 2-323.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi108013. 7 interactions.
    IntActiP52895. 1 interaction.
    STRINGi9606.ENSP00000370129.

    Chemistry

    BindingDBiP52895.
    ChEMBLiCHEMBL5847.
    DrugBankiDB01586. Ursodeoxycholic acid.

    PTM databases

    PhosphoSiteiP52895.

    Polymorphism and mutation databases

    BioMutaiAKR1C2.
    DMDMi20532374.

    Proteomic databases

    MaxQBiP52895.
    PaxDbiP52895.
    PRIDEiP52895.

    Protocols and materials databases

    DNASUi1646.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000380753; ENSP00000370129; ENSG00000151632.
    ENST00000455190; ENSP00000408440; ENSG00000151632. [P52895-2]
    GeneIDi1646.
    KEGGihsa:1646.
    UCSCiuc001ihs.3. human. [P52895-1]
    uc010qao.2. human. [P52895-2]

    Organism-specific databases

    CTDi1646.
    GeneCardsiGC10M005021.
    HGNCiHGNC:385. AKR1C2.
    HPAiCAB047304.
    MIMi600450. gene.
    614279. phenotype.
    neXtProtiNX_P52895.
    Orphaneti90796. 46,XY disorder of sex development due to isolated 17,20 lyase deficiency.
    PharmGKBiPA24678.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0656.
    GeneTreeiENSGT00760000119041.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    InParanoidiP52895.
    KOiK00089.
    K00212.
    OMAiRHIDIAY.
    PhylomeDBiP52895.
    TreeFamiTF106492.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS07754-MONOMER.
    BRENDAi1.1.1.213. 2681.
    1.1.1.357. 2681.
    1.3.1.20. 2681.
    ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    REACT_11048. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
    REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
    SABIO-RKP52895.
    SignaLinkiP52895.

    Miscellaneous databases

    EvolutionaryTraceiP52895.
    GenomeRNAii1646.
    NextBioi6772.
    PROiP52895.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP52895.
    CleanExiHS_AKR1C2.
    ExpressionAtlasiP52895. baseline and differential.
    GenevisibleiP52895. HS.

    Family and domain databases

    Gene3Di3.20.20.100. 1 hit.
    InterProiIPR001395. Aldo/ket_red.
    IPR018170. Aldo/ket_reductase_CS.
    IPR020471. Aldo/keto_reductase_subgr.
    IPR023210. NADP_OxRdtase_dom.
    [Graphical view]
    PANTHERiPTHR11732. PTHR11732. 1 hit.
    PfamiPF00248. Aldo_ket_red. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000097. AKR. 1 hit.
    PRINTSiPR00069. ALDKETRDTASE.
    SUPFAMiSSF51430. SSF51430. 1 hit.
    PROSITEiPS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase."
      Qin K.-N., New M.I., Cheng K.-C.
      J. Steroid Biochem. Mol. Biol. 46:673-679(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    2. "cDNA and deduced amino acid sequences of a human colon dihydrodiol dehydrogenase."
      Ciaccio P.J., Tew K.D.
      Biochim. Biophys. Acta 1186:129-132(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Colon.
    3. "Structure of a gene coding for human dihydrodiol dehydrogenase/bile acid-binding protein."
      Qin K.-N., Khanna M., Cheng K.-C.
      Gene 149:357-361(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT TYR-46.
    4. "Molecular cloning of human type 3 3 alpha-hydroxysteroid dehydrogenase that differs from 20 alpha-hydroxysteroid dehydrogenase by seven amino acids."
      Dufort I., Soucy P., Labrie F., Luu-The V.
      Biochem. Biophys. Res. Commun. 228:474-479(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
      Tissue: Prostate.
    5. "Sequence of the cDNA of a human dihydrodiol dehydrogenase isoform (AKR1C2) and tissue distribution of its mRNA."
      Shiraishi H., Ishikura S., Matsuura K., Deyashiki Y., Ninomiya M., Sakai S., Hara A.
      Biochem. J. 334:399-405(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    6. "Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes."
      Nishizawa M., Nakajima T., Yasuda K., Kanzaki H., Sasaguri Y., Watanabe K., Ito S.
      Genes Cells 5:111-125(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
      Tissue: Liver.
    7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Tongue.
    8. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    9. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Lung and Urinary bladder.
    11. "Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells."
      Hara A., Matsuura K., Tamada Y., Sato K., Miyabe Y., Deyashiki Y., Ishida N.
      Biochem. J. 313:373-376(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-31; 40-62; 69-100; 105-131; 137-153; 162-206; 209-231; 250-269 AND 271-323, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    12. "cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family."
      Stolz A., Hammond L., Lou H., Takikawa H., Ronk M., Shively J.E.
      J. Biol. Chem. 268:10448-10457(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 10-29; 40-55; 76-101; 105-128; 137-146; 162-197; 208-223; 259-270 AND 305-322.
      Tissue: Liver.
    13. "Why boys will be boys: two pathways of fetal testicular androgen biosynthesis are needed for male sexual differentiation."
      Fluck C.E., Meyer-Boni M., Pandey A.V., Kempna P., Miller W.L., Schoenle E.J., Biason-Lauber A.
      Am. J. Hum. Genet. 89:201-218(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, VARIANTS SRXY8 VAL-79; GLN-90; GLN-222 AND THR-300, CHARACTERIZATION OF VARIANTS SRXY8 VAL-79; GLN-90; GLN-222 AND THR-300.
    14. "Crystal structure of human type III 3alpha-hydroxysteroid dehydrogenase/bile acid binding protein complexed with NADP(+) and ursodeoxycholate."
      Jin Y., Stayrook S.E., Albert R.H., Palackal N.T., Penning T.M., Lewis M.
      Biochemistry 40:10161-10168(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH NADP AND URSODEOXYCHOLATE.
    15. "Structure of the human 3alpha-hydroxysteroid dehydrogenase type 3 in complex with testosterone and NADP at 1.25-A resolution."
      Nahoum V., Gangloff A., Legrand P., Zhu D.-W., Cantin L., Zhorov B.S., Luu-The V., Labrie F., Breton R., Lin S.X.
      J. Biol. Chem. 276:42091-42098(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH NADP AND TESTOSTERONE.
    16. "Comparison of crystal structures of human type 3 3alpha-hydroxysteroid dehydrogenase reveals an 'induced-fit' mechanism and a conserved basic motif involved in the binding of androgen."
      Couture J.F., de Jesus-Tran K.P., Roy A.M., Cantin L., Cote P.L., Legrand P., Luu-The V., Labrie F., Breton R.
      Protein Sci. 14:1485-1497(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-323 IN COMPLEX WITH NADP, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-301 AND ARG-304.
    17. "Crystal structures of mouse 17alpha-hydroxysteroid dehydrogenase (apoenzyme and enzyme-NADP(H) binary complex): identification of molecular determinants responsible for the unique 17alpha-reductive activity of this enzyme."
      Faucher F., Pereira de Jesus-Tran K., Cantin L., Luu-The V., Labrie F., Breton R.
      J. Mol. Biol. 364:747-763(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH NADP, FUNCTION, CATALYTIC ACTIVITY.
    18. "Mouse 17alpha-hydroxysteroid dehydrogenase (AKR1C21) binds steroids differently from other aldo-keto reductases: identification and characterization of amino acid residues critical for substrate binding."
      Faucher F., Cantin L., Pereira de Jesus-Tran K., Lemieux M., Luu-The V., Labrie F., Breton R.
      J. Mol. Biol. 369:525-540(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 3-323 IN COMPLEX WITH NADP AND HYDROXYANDROSTERONE, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-24 AND LYS-31.

    Entry informationi

    Entry nameiAK1C2_HUMAN
    AccessioniPrimary (citable) accession number: P52895
    Secondary accession number(s): A8K2N9
    , B4DKR9, Q14133, Q5SR16, Q7M4N1, Q96A71
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: May 10, 2002
    Last modified: July 22, 2015
    This is version 156 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.