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P52895

- AK1C2_HUMAN

UniProt

P52895 - AK1C2_HUMAN

Protein

Aldo-keto reductase family 1 member C2

Gene

AKR1C2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 3 (10 May 2002)
      Previous versions | rss
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    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

    1. alditol:NADP+ 1-oxidoreductase activity Source: UniProtKB
    2. bile acid binding Source: UniProtKB
    3. carboxylic acid binding Source: UniProtKB
    4. ketosteroid monooxygenase activity Source: UniProtKB
    5. oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor Source: UniProtKB
    6. phenanthrene 9,10-monooxygenase activity Source: UniProtKB
    7. prostaglandin F receptor activity Source: UniProtKB
    8. trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity Source: UniProtKB

    GO - Biological processi

    1. cellular response to jasmonic acid stimulus Source: UniProtKB
    2. daunorubicin metabolic process Source: UniProtKB
    3. digestion Source: UniProtKB
    4. doxorubicin metabolic process Source: UniProtKB
    5. epithelial cell differentiation Source: UniProt
    6. G-protein coupled receptor signaling pathway Source: UniProtKB
    7. oxidation-reduction process Source: UniProtKB
    8. positive regulation of cell proliferation Source: UniProtKB
    9. positive regulation of protein kinase B signaling Source: UniProtKB
    10. progesterone metabolic process Source: UniProtKB
    11. prostaglandin metabolic process Source: UniProtKB
    12. response to prostaglandin Source: UniProtKB
    13. steroid metabolic process Source: UniProtKB

    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.
    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: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:385. AKR1C2.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    46,XY sex reversal 8 (SRXY8) [MIM:614279]: A disorder of sex development. Affected individuals have a 46,XY karyotype but present as phenotypically normal females.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.

    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

    ArrayExpressiP52895.
    BgeeiP52895.
    CleanExiHS_AKR1C2.
    GenevestigatoriP52895.

    Organism-specific databases

    HPAiCAB047304.

    Interactioni

    Protein-protein interaction databases

    BioGridi108013. 2 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 – 93
    Beta strandi15 – 228
    Helixi32 – 4413
    Beta strandi48 – 503
    Helixi53 – 553
    Helixi58 – 7013
    Helixi76 – 783
    Beta strandi80 – 856
    Helixi87 – 893
    Helixi92 – 943
    Helixi95 – 10612
    Beta strandi111 – 1166
    Beta strandi119 – 1224
    Beta strandi124 – 1263
    Helixi144 – 15613
    Beta strandi159 – 1679
    Helixi170 – 1778
    Beta strandi187 – 1926
    Helixi200 – 2089
    Beta strandi212 – 2176
    Turni225 – 2273
    Helixi235 – 2373
    Helixi239 – 24810
    Helixi252 – 26211
    Beta strandi266 – 2705
    Helixi274 – 2807
    Helixi281 – 2855
    Helixi290 – 2978
    Helixi309 – 3113
    Beta strandi318 – 3214

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    InParanoidiP52895.
    KOiK00089.
    K00212.
    OMAiYTSKLWI.
    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. Align

    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

    MDSKYQCVKL NDGHFMPVLG FGTYAPAEVP KSKALEAVKL AIEAGFHHID    50
    SAHVYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWSNSH RPELVRPALE 100
    RSLKNLQLDY VDLYLIHFPV SVKPGEEVIP KDENGKILFD TVDLCATWEA 150
    MEKCKDAGLA KSIGVSNFNH RLLEMILNKP GLKYKPVCNQ VECHPYFNQR 200
    KLLDFCKSKD IVLVAYSALG SHREEPWVDP NSPVLLEDPV LCALAKKHKR 250
    TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTS EEMKAIDGLN 300
    RNVRYLTLDI FAGPPNYPFS DEY 323
    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:
    EMBL
    GenBank
    DDBJ
    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. [P52895-1]
    ENST00000407674; ENSP00000385221; ENSG00000151632. [P52895-1]
    ENST00000455190; ENSP00000408440; ENSG00000151632. [P52895-2]
    GeneIDi1646.
    KEGGihsa:1646.
    UCSCiuc001ihs.3. human. [P52895-1]
    uc010qao.2. human. [P52895-2]

    Polymorphism databases

    DMDMi20532374.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS44350.1. [P52895-2 ]
    CCDS7062.1. [P52895-1 ]
    PIRi I73676.
    JC5240.
    S61516.
    RefSeqi NP_001128713.1. NM_001135241.2. [P52895-2 ]
    NP_001345.1. NM_001354.5. [P52895-1 ]
    NP_995317.1. NM_205845.2. [P52895-1 ]
    UniGenei Hs.460260.
    Hs.567256.
    Hs.734597.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IHI X-ray 3.00 A/B 1-323 [» ]
    1J96 X-ray 1.25 A/B 2-323 [» ]
    1XJB X-ray 1.90 A/B 2-323 [» ]
    2HDJ X-ray 2.00 A/B 1-323 [» ]
    2IPJ X-ray 1.80 A/B 3-323 [» ]
    4JQ1 X-ray 1.60 A/B 1-323 [» ]
    4JQ2 X-ray 1.75 A/B 1-323 [» ]
    4JQ3 X-ray 1.75 A/B 1-323 [» ]
    4JQ4 X-ray 1.52 A/B 1-323 [» ]
    4JQA X-ray 1.45 A/B 1-323 [» ]
    4JTQ X-ray 1.60 A/B 1-323 [» ]
    4JTR X-ray 1.30 A/B 1-323 [» ]
    4L1W X-ray 2.20 A/B 2-323 [» ]
    4L1X X-ray 2.00 A/B 2-323 [» ]
    ProteinModelPortali P52895.
    SMRi P52895. Positions 2-323.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108013. 2 interactions.
    IntActi P52895. 1 interaction.
    STRINGi 9606.ENSP00000370129.

    Chemistry

    BindingDBi P52895.
    ChEMBLi CHEMBL5847.
    DrugBanki DB01586. Ursodeoxycholic acid.

    PTM databases

    PhosphoSitei P52895.

    Polymorphism databases

    DMDMi 20532374.

    Proteomic databases

    MaxQBi P52895.
    PaxDbi P52895.
    PRIDEi P52895.

    Protocols and materials databases

    DNASUi 1646.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000380753 ; ENSP00000370129 ; ENSG00000151632 . [P52895-1 ]
    ENST00000407674 ; ENSP00000385221 ; ENSG00000151632 . [P52895-1 ]
    ENST00000455190 ; ENSP00000408440 ; ENSG00000151632 . [P52895-2 ]
    GeneIDi 1646.
    KEGGi hsa:1646.
    UCSCi uc001ihs.3. human. [P52895-1 ]
    uc010qao.2. human. [P52895-2 ]

    Organism-specific databases

    CTDi 1646.
    GeneCardsi GC10M005021.
    HGNCi HGNC:385. AKR1C2.
    HPAi CAB047304.
    MIMi 600450. gene.
    614279. phenotype.
    neXtProti NX_P52895.
    Orphaneti 90796. 46,XY disorder of sex development due to isolated 17, 20 lyase deficiency.
    PharmGKBi PA24678.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0656.
    HOGENOMi HOG000250272.
    HOVERGENi HBG000020.
    InParanoidi P52895.
    KOi K00089.
    K00212.
    OMAi YTSKLWI.
    PhylomeDBi P52895.
    TreeFami TF106492.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS07754-MONOMER.
    BRENDAi 1.1.1.213. 2681.
    Reactomei REACT_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-RK P52895.
    SignaLinki P52895.

    Miscellaneous databases

    EvolutionaryTracei P52895.
    NextBioi 6772.
    PROi P52895.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P52895.
    Bgeei P52895.
    CleanExi HS_AKR1C2.
    Genevestigatori P52895.

    Family and domain databases

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

    Publicationsi

    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: October 1, 2014
    This is version 149 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