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Q04828

- AK1C1_HUMAN

UniProt

Q04828 - AK1C1_HUMAN

Protein

Aldo-keto reductase family 1 member C1

Gene

AKR1C1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    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

    1. 17-alpha,20-alpha-dihydroxypregn-4-en-3-one dehydrogenase activity Source: UniProtKB-EC
    2. alditol:NADP+ 1-oxidoreductase activity Source: UniProtKB
    3. aldo-keto reductase (NADP) activity Source: UniProtKB
    4. androsterone dehydrogenase (B-specific) activity Source: UniProtKB
    5. bile acid binding Source: UniProtKB
    6. carboxylic acid binding Source: UniProtKB
    7. indanol dehydrogenase activity Source: UniProtKB-EC
    8. ketosteroid monooxygenase activity Source: UniProtKB
    9. oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor Source: UniProtKB
    10. phenanthrene 9,10-monooxygenase activity Source: UniProtKB
    11. trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity Source: UniProtKB

    GO - Biological processi

    1. bile acid and bile salt transport Source: UniProtKB
    2. bile acid metabolic process Source: UniProtKB
    3. cellular response to jasmonic acid stimulus Source: UniProtKB
    4. cholesterol homeostasis Source: UniProtKB
    5. daunorubicin metabolic process Source: UniProtKB
    6. digestion Source: UniProtKB
    7. doxorubicin metabolic process Source: UniProtKB
    8. epithelial cell differentiation Source: UniProt
    9. intestinal cholesterol absorption Source: UniProtKB
    10. oxidation-reduction process Source: UniProtKB
    11. phototransduction, visible light Source: Reactome
    12. progesterone metabolic process Source: UniProtKB
    13. protein homooligomerization Source: UniProtKB
    14. response to organophosphorus Source: UniProtKB
    15. retinal metabolic process Source: UniProtKB
    16. retinoid metabolic process Source: Reactome
    17. xenobiotic metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    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: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:384. AKR1C1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt

    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.

    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

    ArrayExpressiQ04828.
    BgeeiQ04828.
    CleanExiHS_AKR1C1.
    GenevestigatoriQ04828.

    Organism-specific databases

    HPAiCAB010874.
    CAB047303.

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Protein-protein interaction databases

    BioGridi108012. 4 interactions.
    IntActiQ04828. 3 interactions.
    MINTiMINT-5001209.
    STRINGi9606.ENSP00000370254.

    Structurei

    Secondary structure

    1
    323
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 93
    Beta strandi15 – 228
    Helixi33 – 4412
    Beta strandi48 – 503
    Helixi53 – 553
    Helixi58 – 7013
    Helixi76 – 783
    Beta strandi80 – 856
    Helixi87 – 893
    Helixi92 – 10615
    Beta strandi111 – 1166
    Beta strandi124 – 1263
    Helixi144 – 15613
    Beta strandi159 – 1679
    Helixi170 – 1778
    Beta strandi187 – 1926
    Beta strandi194 – 1974
    Helixi200 – 2089
    Beta strandi212 – 2176
    Turni225 – 2273
    Helixi235 – 2373
    Helixi239 – 24810
    Helixi252 – 26211
    Beta strandi266 – 2705
    Helixi274 – 2807
    Helixi281 – 2855
    Helixi290 – 2978
    Helixi309 – 3113

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    InParanoidiQ04828.
    KOiK00089.
    K00212.
    OMAiEMREDED.
    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

    MDSKYQCVKL NDGHFMPVLG FGTYAPAEVP KSKALEATKL AIEAGFRHID    50
    SAHLYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWCNSH RPELVRPALE 100
    RSLKNLQLDY VDLYLIHFPV SVKPGEEVIP KDENGKILFD TVDLCATWEA 150
    VEKCKDAGLA KSIGVSNFNR RQLEMILNKP GLKYKPVCNQ VECHPYFNQR 200
    KLLDFCKSKD IVLVAYSALG SHREEPWVDP NSPVLLEDPV LCALAKKHKR 250
    TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTS EEMKAIDGLN 300
    RNVRYLTLDI FAGPPNYPFS DEY 323
    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:
    EMBL
    GenBank
    DDBJ
    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.
    ENST00000434459; ENSP00000412248; ENSG00000187134.
    GeneIDi1645.
    KEGGihsa:1645.
    UCSCiuc001iho.3. human.

    Polymorphism databases

    DMDMi416877.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS7061.1.
    PIRi A53436.
    I73675.
    S59619.
    S61515.
    RefSeqi NP_001344.2. NM_001353.5.
    UniGenei Hs.460260.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MRQ X-ray 1.59 A 2-323 [» ]
    3C3U X-ray 1.80 A 1-323 [» ]
    3GUG X-ray 1.90 A 1-323 [» ]
    3NTY X-ray 1.87 A 1-323 [» ]
    ProteinModelPortali Q04828.
    SMRi Q04828. Positions 2-323.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108012. 4 interactions.
    IntActi Q04828. 3 interactions.
    MINTi MINT-5001209.
    STRINGi 9606.ENSP00000370254.

    Chemistry

    BindingDBi Q04828.
    ChEMBLi CHEMBL5905.
    DrugBanki DB00945. Acetylsalicylic acid.
    DB00936. Salicylic acid.

    PTM databases

    PhosphoSitei Q04828.

    Polymorphism databases

    DMDMi 416877.

    Proteomic databases

    MaxQBi Q04828.
    PaxDbi Q04828.
    PRIDEi Q04828.

    Protocols and materials databases

    DNASUi 1645.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000380872 ; ENSP00000370254 ; ENSG00000187134 .
    ENST00000434459 ; ENSP00000412248 ; ENSG00000187134 .
    GeneIDi 1645.
    KEGGi hsa:1645.
    UCSCi uc001iho.3. human.

    Organism-specific databases

    CTDi 1645.
    GeneCardsi GC10P004995.
    HGNCi HGNC:384. AKR1C1.
    HPAi CAB010874.
    CAB047303.
    MIMi 600449. gene.
    neXtProti NX_Q04828.
    PharmGKBi PA24677.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0656.
    HOGENOMi HOG000250272.
    HOVERGENi HBG000020.
    InParanoidi Q04828.
    KOi K00089.
    K00212.
    OMAi EMREDED.
    PhylomeDBi Q04828.
    TreeFami TF106492.

    Enzyme and pathway databases

    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.
    REACT_24968. Retinoid metabolism and transport.
    SABIO-RK Q04828.

    Miscellaneous databases

    EvolutionaryTracei Q04828.
    GeneWikii AKR1C1.
    GenomeRNAii 1645.
    NextBioi 6768.
    PROi Q04828.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q04828.
    Bgeei Q04828.
    CleanExi HS_AKR1C1.
    Genevestigatori Q04828.

    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 PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
    PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
    PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 156 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