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Protein

Aldo-keto reductase family 1 member C1

Gene

AKR1C1

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

Functioni

Converts progesterone to its inactive form, 20-alpha-dihydroxyprogesterone (20-alpha-OHP). In the liver and intestine, may have a role in the transport of bile. May have a role in monitoring the intrahepatic bile acid concentration. Has a low bile-binding ability. May play a role in myelin formation.2 Publications

Catalytic activityi

17-alpha,20-alpha-dihydroxypregn-4-en-3-one + NAD(P)+ = 17-alpha-hydroxyprogesterone + NAD(P)H.
Trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH.
Indan-1-ol + NAD(P)+ = indanone + NAD(P)H.

Enzyme regulationi

Inhibited by hexestrol with an IC50 of 9.5 µM, 1,10-phenanthroline with an IC50 of 55 µM, 1,7-phenanthroline with an IC50 of 72 µM, flufenamic acid with an IC50 of 6.0 µM, indomethacin with an IC50 of 140 µM, ibuprofen with an IC50 of 950 µM, lithocholic acid with an IC50 of 25 µM, ursodeoxycholic acid with an IC50 of 340 µM and chenodeoxycholic acid with an IC50 of 570 µM.1 Publication

Kineticsi

  1. KM=5 µM for (s)-tetralol2 Publications
  2. KM=38 µM for (s)-indan-1-ol2 Publications
  3. KM=580 µM for benzene dihydrodiol2 Publications
  4. KM=3 µM for 5-beta-pregnane-3-alpha,20-alpha-diol2 Publications
  5. KM=3 µM for 5-beta-pregnan-20-alpha-ol-3-one2 Publications
  6. KM=12 µM for 4-pregnen-20-alpha-ol-3-one2 Publications
  7. KM=133 µM for 9-alpha,11-beta-PGF22 Publications
  8. KM=2 µM for 5-beta-pregnan-3-alpha-ol-20-one2 Publications
  9. KM=1 µM for 5-beta-androstane-3,17-dione2 Publications
  10. KM=12 µM for PGD22 Publications
  11. KM=0.6 µM for 20-alpha-hydroxyprogesterone (with NADH)2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei24 – 241Substrate
    Binding sitei50 – 501NADP2 Publications
    Sitei54 – 541Important for substrate specificityBy similarity
    Active sitei55 – 551Proton donorBy similarity
    Sitei84 – 841Lowers pKa of active site TyrBy similarity
    Binding sitei117 – 1171SubstrateBy similarity
    Binding sitei190 – 1901NADP2 Publications
    Binding sitei222 – 2221Substrate
    Sitei222 – 2221May be involved in the mediating step between the transformation of progesterone and the release of the cofactor
    Binding sitei227 – 2271Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi20 – 245NADP2 Publications
    Nucleotide bindingi166 – 1672NADP2 Publications
    Nucleotide bindingi216 – 2227NADP2 Publications
    Nucleotide bindingi270 – 28011NADP2 PublicationsAdd
    BLAST

    GO - Molecular functioni

    • 17-alpha,20-alpha-dihydroxypregn-4-en-3-one dehydrogenase activity Source: UniProtKB-EC
    • alditol:NADP+ 1-oxidoreductase activity Source: UniProtKB
    • aldo-keto reductase (NADP) activity Source: UniProtKB
    • androsterone dehydrogenase (B-specific) activity Source: UniProtKB
    • bile acid binding Source: UniProtKB
    • carboxylic acid binding Source: UniProtKB
    • indanol dehydrogenase activity Source: UniProtKB-EC
    • 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

    • bile acid and bile salt transport Source: UniProtKB
    • bile acid metabolic process Source: UniProtKB
    • cellular response to jasmonic acid stimulus Source: UniProtKB
    • cholesterol homeostasis Source: UniProtKB
    • daunorubicin metabolic process Source: UniProtKB
    • digestion Source: UniProtKB
    • doxorubicin metabolic process Source: UniProtKB
    • epithelial cell differentiation Source: UniProtKB
    • intestinal cholesterol absorption Source: UniProtKB
    • oxidation-reduction process Source: UniProtKB
    • phototransduction, visible light Source: Reactome
    • progesterone metabolic process Source: UniProtKB
    • protein homooligomerization Source: UniProtKB
    • response to organophosphorus Source: UniProtKB
    • retinal metabolic process Source: UniProtKB
    • retinoid metabolic process Source: Reactome
    • xenobiotic metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BRENDAi1.1.1.149. 2681.
    1.1.1.270. 2681.
    1.1.1.50. 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.
    REACT_24968. Retinoid metabolism and transport.
    SABIO-RKQ04828.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aldo-keto reductase family 1 member C1 (EC:1.1.1.-)
    Alternative name(s):
    20-alpha-hydroxysteroid dehydrogenase (EC:1.1.1.149)
    Short name:
    20-alpha-HSD
    Chlordecone reductase homolog HAKRC
    Dihydrodiol dehydrogenase 1/2
    Short name:
    DD1/DD2
    High-affinity hepatic bile acid-binding protein
    Short name:
    HBAB
    Indanol dehydrogenase (EC:1.1.1.112)
    Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase (EC:1.3.1.20)
    Gene namesi
    Name:AKR1C1
    Synonyms:DDH, DDH1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:384. AKR1C1.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    • extracellular exosome Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi127 – 1271E → D: 30-fold decrease in k(cat)/K(m) value for progesterone reduction; no effect on the K(m) value. 1 Publication
    Mutagenesisi222 – 2221H → I: Marked decrease in k(cat)/K(m) value for progesterone; 24-fold decrease for progesterone reduction; 18-fold decrease for 20alpha-OHProg oxidation. 95-fold decrease in K(m) value for NADPH. 1 Publication
    Mutagenesisi222 – 2221H → S: Marked decrease in k(cat)/K(m) value for progesterone; 10-fold decrease for progesterone reduction; 3-fold decrease for 20alpha-OHProg oxidation. 10-fold decrease in K(m) value for NADPH. 1 Publication
    Mutagenesisi304 – 3041R → L: 70-fold decrease in progesterone reduction. No effect on DHT reduction. 1 Publication
    Mutagenesisi305 – 3051Y → F: No effect on progesterone reduction. 1 Publication
    Mutagenesisi307 – 3071T → V: No effect on progesterone reduction. 1 Publication
    Mutagenesisi309 – 3091D → V: No effect on progesterone reduction. 1 Publication

    Organism-specific databases

    PharmGKBiPA24677.

    Chemistry

    DrugBankiDB00945. Acetylsalicylic acid.
    DB00936. Salicylic acid.

    Polymorphism and mutation databases

    BioMutaiAKR1C1.
    DMDMi416877.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 323323Aldo-keto reductase family 1 member C1PRO_0000124633Add
    BLAST

    Proteomic databases

    MaxQBiQ04828.
    PaxDbiQ04828.
    PRIDEiQ04828.

    PTM databases

    PhosphoSiteiQ04828.

    Expressioni

    Tissue specificityi

    Expressed in all tissues tested including liver, prostate, testis, adrenal gland, brain, uterus, mammary gland and keratinocytes. Highest levels found in liver, mammary gland and brain.1 Publication

    Gene expression databases

    BgeeiQ04828.
    CleanExiHS_AKR1C1.
    ExpressionAtlasiQ04828. baseline and differential.
    GenevisibleiQ04828. HS.

    Organism-specific databases

    HPAiCAB047303.

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PTPN3P260453EBI-2116455,EBI-1047946

    Protein-protein interaction databases

    BioGridi108012. 9 interactions.
    IntActiQ04828. 4 interactions.
    MINTiMINT-5001209.

    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
    Helixi33 – 4412Combined sources
    Beta strandi48 – 503Combined sources
    Helixi53 – 553Combined sources
    Helixi58 – 7013Combined sources
    Helixi76 – 783Combined sources
    Beta strandi80 – 856Combined sources
    Helixi87 – 893Combined sources
    Helixi92 – 10615Combined sources
    Beta strandi111 – 1166Combined sources
    Beta strandi124 – 1263Combined sources
    Helixi144 – 15613Combined sources
    Beta strandi159 – 1679Combined sources
    Helixi170 – 1778Combined sources
    Beta strandi187 – 1926Combined sources
    Beta strandi194 – 1974Combined 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

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MRQX-ray1.59A2-323[»]
    3C3UX-ray1.80A1-323[»]
    3GUGX-ray1.90A1-323[»]
    3NTYX-ray1.87A1-323[»]
    ProteinModelPortaliQ04828.
    SMRiQ04828. Positions 2-323.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ04828.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Phylogenomic databases

    eggNOGiCOG0656.
    GeneTreeiENSGT00760000119041.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    InParanoidiQ04828.
    KOiK00089.
    K00212.
    OMAiRYITADF.
    PhylomeDBiQ04828.
    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.
    PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q04828-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDSKYQCVKL NDGHFMPVLG FGTYAPAEVP KSKALEATKL AIEAGFRHID
    60 70 80 90 100
    SAHLYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWCNSH RPELVRPALE
    110 120 130 140 150
    RSLKNLQLDY VDLYLIHFPV SVKPGEEVIP KDENGKILFD TVDLCATWEA
    160 170 180 190 200
    VEKCKDAGLA KSIGVSNFNR RQLEMILNKP 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):36,788
    Last modified:October 1, 1993 - v1
    Checksum:i9CB215478FBD29D5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31S → A no nucleotide entry (PubMed:7626489).Curated
    Sequence conflicti95 – 951V → D no nucleotide entry (PubMed:7626489).Curated
    Sequence conflicti95 – 951V → D in AAD14012 (PubMed:8274401).Curated
    Sequence conflicti158 – 1581G → E no nucleotide entry (PubMed:7626489).Curated
    Sequence conflicti158 – 1581G → E in AAD14012 (PubMed:8274401).Curated
    Sequence conflicti171 – 1722RQ → ST no nucleotide entry (PubMed:7626489).Curated
    Sequence conflicti171 – 1722RQ → ST in AAD14012 (PubMed:8274401).Curated
    Sequence conflicti183 – 1842KY → QV no nucleotide entry (PubMed:7626489).Curated
    Sequence conflicti183 – 1842KY → QV in AAD14012 (PubMed:8274401).Curated
    Sequence conflicti222 – 2221H → L no nucleotide entry (PubMed:7626489).Curated
    Sequence conflicti222 – 2221H → L in AAD14012 (PubMed:8274401).Curated
    Sequence conflicti319 – 3191F → I no nucleotide entry (PubMed:7626489).Curated
    Sequence conflicti319 – 3191F → I in AAD14012 (PubMed:8274401).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti170 – 1701R → H.
    Corresponds to variant rs17295755 [ dbSNP | Ensembl ].
    VAR_048214
    Natural varianti172 – 1721Q → L.
    Corresponds to variant rs17354444 [ dbSNP | Ensembl ].
    VAR_048215

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M86609 mRNA. Translation: AAB02880.1.
    U05861
    , U05853, U05854, U05855, U05857, U05858, U05859, U05860 Genomic DNA. Translation: AAA18115.1.
    U05684 mRNA. Translation: AAA16227.1.
    AB031083 mRNA. Translation: BAA92883.1.
    AB032150 Genomic DNA. Translation: BAA92886.1.
    BT007197 mRNA. Translation: AAP35861.1.
    AL713867, AC091817 Genomic DNA. Translation: CAI16409.1.
    BC015490 mRNA. Translation: AAH15490.1.
    BC020216 mRNA. Translation: AAH20216.1.
    BC040210 mRNA. Translation: AAH40210.1.
    S68290 mRNA. Translation: AAD14012.1.
    D26124 mRNA. Translation: BAA05121.1.
    CCDSiCCDS7061.1.
    PIRiA53436.
    I73675.
    S59619.
    S61515.
    RefSeqiNP_001344.2. NM_001353.5.
    UniGeneiHs.460260.

    Genome annotation databases

    EnsembliENST00000380872; ENSP00000370254; ENSG00000187134.
    GeneIDi1645.
    KEGGihsa:1645.
    UCSCiuc001iho.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M86609 mRNA. Translation: AAB02880.1.
    U05861
    , U05853, U05854, U05855, U05857, U05858, U05859, U05860 Genomic DNA. Translation: AAA18115.1.
    U05684 mRNA. Translation: AAA16227.1.
    AB031083 mRNA. Translation: BAA92883.1.
    AB032150 Genomic DNA. Translation: BAA92886.1.
    BT007197 mRNA. Translation: AAP35861.1.
    AL713867, AC091817 Genomic DNA. Translation: CAI16409.1.
    BC015490 mRNA. Translation: AAH15490.1.
    BC020216 mRNA. Translation: AAH20216.1.
    BC040210 mRNA. Translation: AAH40210.1.
    S68290 mRNA. Translation: AAD14012.1.
    D26124 mRNA. Translation: BAA05121.1.
    CCDSiCCDS7061.1.
    PIRiA53436.
    I73675.
    S59619.
    S61515.
    RefSeqiNP_001344.2. NM_001353.5.
    UniGeneiHs.460260.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MRQX-ray1.59A2-323[»]
    3C3UX-ray1.80A1-323[»]
    3GUGX-ray1.90A1-323[»]
    3NTYX-ray1.87A1-323[»]
    ProteinModelPortaliQ04828.
    SMRiQ04828. Positions 2-323.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi108012. 9 interactions.
    IntActiQ04828. 4 interactions.
    MINTiMINT-5001209.

    Chemistry

    BindingDBiQ04828.
    ChEMBLiCHEMBL5905.
    DrugBankiDB00945. Acetylsalicylic acid.
    DB00936. Salicylic acid.

    PTM databases

    PhosphoSiteiQ04828.

    Polymorphism and mutation databases

    BioMutaiAKR1C1.
    DMDMi416877.

    Proteomic databases

    MaxQBiQ04828.
    PaxDbiQ04828.
    PRIDEiQ04828.

    Protocols and materials databases

    DNASUi1645.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000380872; ENSP00000370254; ENSG00000187134.
    GeneIDi1645.
    KEGGihsa:1645.
    UCSCiuc001iho.3. human.

    Organism-specific databases

    CTDi1645.
    GeneCardsiGC10P004934.
    HGNCiHGNC:384. AKR1C1.
    HPAiCAB047303.
    MIMi600449. gene.
    neXtProtiNX_Q04828.
    PharmGKBiPA24677.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0656.
    GeneTreeiENSGT00760000119041.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    InParanoidiQ04828.
    KOiK00089.
    K00212.
    OMAiRYITADF.
    PhylomeDBiQ04828.
    TreeFamiTF106492.

    Enzyme and pathway databases

    BRENDAi1.1.1.149. 2681.
    1.1.1.270. 2681.
    1.1.1.50. 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.
    REACT_24968. Retinoid metabolism and transport.
    SABIO-RKQ04828.

    Miscellaneous databases

    EvolutionaryTraceiQ04828.
    GeneWikiiAKR1C1.
    GenomeRNAii1645.
    NextBioi6768.
    PROiQ04828.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ04828.
    CleanExiHS_AKR1C1.
    ExpressionAtlasiQ04828. baseline and differential.
    GenevisibleiQ04828. 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.
    PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "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: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Genomic organization and chromosomal localization of a novel human hepatic dihydrodiol dehydrogenase with high affinity bile acid binding."
      Lou H., Hammond L., Sharma V., Sparkes R.S., Lusis A.J., Stolz A.
      J. Biol. Chem. 269:8416-8422(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Blood.
    3. "Regulation of human dihydrodiol dehydrogenase by Michael acceptor xenobiotics."
      Ciaccio P.J., Jaiswal A.K., Tew K.D.
      J. Biol. Chem. 269:15558-15562(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Colon.
    4. "Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans."
      Khanna M., Qin K.-N., Cheng K.-C.
      J. Steroid Biochem. Mol. Biol. 53:41-46(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    5. "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 [MRNA].
      Tissue: Liver.
    6. "Characterization of a human 20alpha-hydroxysteroid dehydrogenase."
      Zhang Y., Dufort I., Rheault P., Luu-The V.
      J. Mol. Endocrinol. 25:221-228(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
      Tissue: Skin fibroblast.
    7. "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].
    8. "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].
    9. "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].
      Tissue: Lung and Testis.
    10. "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] OF 4-323.
      Tissue: Liver.
    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 10-31; 40-61; 69-126; 137-153; 162-206; 209-230; 250-267; 271-289 AND 295-323, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    12. "Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder."
      Deyashiki Y., Ogasawara A., Nakayama T., Nakanishi M., Miyabe Y., Sato K., Hara A.
      Biochem. J. 299:545-552(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-323, PROTEIN SEQUENCE OF 18-31; 105-131; 176-193 AND 271-294.
      Tissue: Liver.
    13. "Human 20alpha-hydroxysteroid dehydrogenase: crystallographic and site-directed mutagenesis studies lead to the identification of an alternative binding site for C21-steroids."
      Couture J.-F., Legrand P., Cantin L., Luu-The V., Labrie F., Breton R.
      J. Mol. Biol. 331:593-604(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH NADP AND 20ALPHA-HYDROXY-PROGESTERONE, MUTAGENESIS OF GLU-127; HIS-222; ARG-304; TYR-305; THR-307 AND ASP-309.
    14. "Probing the inhibitor selectivity pocket of human 20alpha-hydroxysteroid dehydrogenase (AKR1C1) with X-ray crystallography and site-directed mutagenesis."
      El-Kabbani O., Dhagat U., Soda M., Endo S., Matsunaga T., Hara A.
      Bioorg. Med. Chem. Lett. 21:2564-2567(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) IN COMPLEX WITH NADP AND 3-CHLORO-5-PHENYLSALICYLIC ACID.

    Entry informationi

    Entry nameiAK1C1_HUMAN
    AccessioniPrimary (citable) accession number: Q04828
    Secondary accession number(s): P52896
    , Q5SR15, Q7M4N2, Q9UCX2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: June 24, 2015
    This is version 165 of the entry and version 1 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.