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P17516

- AK1C4_HUMAN

UniProt

P17516 - AK1C4_HUMAN

Protein

Aldo-keto reductase family 1 member C4

Gene

AKR1C4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 3 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Catalyzes the transformation of the potent androgen dihydrotestosterone (DHT) into the less active form, 5-alpha-androstan-3-alpha,17-beta-diol (3-alpha-diol). Also has some 20-alpha-hydroxysteroid dehydrogenase activity. The biotransformation of the pesticide chlordecone (kepone) to its corresponding alcohol leads to increased biliary excretion of the pesticide and concomitant reduction of its neurotoxicity since bile is the major excretory route.

    Catalytic activityi

    Chlordecone alcohol + NADP+ = chlordecone + NADPH.
    A 3-alpha-hydroxysteroid + NAD(P)+ = a 3-oxosteroid + NAD(P)H.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei50 – 501NADP1 Publication
    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 – 1901NADP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi20 – 245NADP1 Publication
    Nucleotide bindingi166 – 1672NADP1 Publication
    Nucleotide bindingi216 – 2216NADP1 Publication
    Nucleotide bindingi270 – 28011NADP1 PublicationAdd
    BLAST

    GO - Molecular functioni

    1. aldo-keto reductase (NADP) activity Source: ProtInc
    2. androsterone dehydrogenase activity Source: UniProtKB
    3. bile acid transmembrane transporter activity Source: ProtInc
    4. chlordecone reductase activity Source: UniProtKB-EC
    5. electron carrier activity Source: UniProtKB
    6. oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor Source: UniProtKB
    7. retinal dehydrogenase activity Source: UniProtKB

    GO - Biological processi

    1. androgen metabolic process Source: ProtInc
    2. bile acid and bile salt transport Source: ProtInc
    3. bile acid biosynthetic process Source: Reactome
    4. bile acid metabolic process Source: Reactome
    5. cellular response to jasmonic acid stimulus Source: UniProtKB
    6. daunorubicin metabolic process Source: UniProtKB
    7. doxorubicin metabolic process Source: UniProtKB
    8. phototransduction, visible light Source: Reactome
    9. retinoid metabolic process Source: Reactome
    10. small molecule metabolic process Source: Reactome
    11. steroid metabolic process Source: ProtInc

    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-RKP17516.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aldo-keto reductase family 1 member C4 (EC:1.1.1.-)
    Alternative name(s):
    3-alpha-HSD1
    3-alpha-hydroxysteroid dehydrogenase type I (EC:1.1.1.357)
    Chlordecone reductase (EC:1.1.1.225)
    Short name:
    CDR
    Dihydrodiol dehydrogenase 4
    Short name:
    DD-4
    Short name:
    DD4
    HAKRA
    Gene namesi
    Name:AKR1C4
    Synonyms:CHDR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:387. AKR1C4.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. cytosol Source: Reactome

    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 gene represented in this entry may act as a disease modifier. A splicing mutation resulting in loss of AKR1C4 exon 2 has been found in affected individuals carrying a causative mutation in AKR1C2 (PubMed:21802064). These patients manifest a more severe disease phenotype than individuals only carrying mutations in AKR1C2.1 Publication

    Organism-specific databases

    MIMi614279. phenotype.
    Orphaneti90796. 46,XY disorder of sex development due to isolated 17, 20 lyase deficiency.
    PharmGKBiPA24680.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 323323Aldo-keto reductase family 1 member C4PRO_0000124640Add
    BLAST

    Post-translational modificationi

    The N-terminus is blocked.

    Proteomic databases

    MaxQBiP17516.
    PaxDbiP17516.
    PRIDEiP17516.

    PTM databases

    PhosphoSiteiP17516.

    Expressioni

    Tissue specificityi

    Liver specific.2 Publications

    Gene expression databases

    ArrayExpressiP17516.
    BgeeiP17516.
    CleanExiHS_AKR1C4.
    GenevestigatoriP17516.

    Organism-specific databases

    HPAiHPA044720.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi107534. 2 interactions.
    STRINGi9606.ENSP00000263126.

    Structurei

    Secondary structure

    1
    323
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 53
    Beta strandi7 – 93
    Beta strandi15 – 228
    Helixi33 – 4412
    Beta strandi48 – 503
    Helixi53 – 553
    Helixi58 – 7114
    Helixi76 – 783
    Beta strandi80 – 856
    Helixi87 – 893
    Helixi92 – 10615
    Beta strandi111 – 1177
    Beta strandi124 – 1263
    Helixi144 – 15613
    Beta strandi159 – 1679
    Helixi170 – 1778
    Beta strandi187 – 1926
    Helixi200 – 2089
    Beta strandi212 – 2176
    Turni225 – 2273
    Helixi235 – 2373
    Helixi239 – 2479
    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
    2FVLX-ray2.40A/B/C1-323[»]
    ProteinModelPortaliP17516.
    SMRiP17516. Positions 1-323.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP17516.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldo/keto reductase family.Curated

    Phylogenomic databases

    eggNOGiCOG0656.
    HOGENOMiHOG000250272.
    HOVERGENiHBG000020.
    InParanoidiP17516.
    KOiK00037.
    K00089.
    K00092.
    K00212.
    OMAiLLHFPMA.
    OrthoDBiEOG70KGQF.
    PhylomeDBiP17516.
    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.

    P17516-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDPKYQRVEL NDGHFMPVLG FGTYAPPEVP RNRAVEVTKL AIEAGFRHID    50
    SAYLYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWCTFF QPQMVQPALE 100
    SSLKKLQLDY VDLYLLHFPM ALKPGETPLP KDENGKVIFD TVDLSATWEV 150
    MEKCKDAGLA KSIGVSNFNC RQLEMILNKP GLKYKPVCNQ VECHPYLNQS 200
    KLLDFCKSKD IVLVAHSALG TQRHKLWVDP NSPVLLEDPV LCALAKKHKQ 250
    TPALIALRYQ LQRGVVVLAK SYNEQRIREN IQVFEFQLTS EDMKVLDGLN 300
    RNYRYVVMDF LMDHPDYPFS DEY 323
    Length:323
    Mass (Da):37,067
    Last modified:October 5, 2010 - v3
    Checksum:iE728CE4B420E8C58
    GO

    Sequence cautioni

    The sequence AAA35658.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Polymorphismi

    The allele with Cys-145/Val-311 shows a three- to five-fold decrease in catalytic efficiency for xenobiotic and steroidal substrates compared to the Ser-145/Leu-311 allele.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti135 – 1351G → E.
    Corresponds to variant rs11253043 [ dbSNP | Ensembl ].
    VAR_028240
    Natural varianti145 – 1451S → C.1 Publication
    Corresponds to variant rs3829125 [ dbSNP | Ensembl ].
    VAR_013290
    Natural varianti170 – 1701C → Y.1 Publication
    Corresponds to variant rs17851824 [ dbSNP | Ensembl ].
    VAR_028241
    Natural varianti250 – 2501Q → R.9 Publications
    Corresponds to variant rs4880718 [ dbSNP | Ensembl ].
    VAR_028242
    Natural varianti311 – 3111L → V.1 Publication
    Corresponds to variant rs17134592 [ dbSNP | Ensembl ].
    VAR_013291

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S68287 mRNA. Translation: AAD14010.1.
    AB045829 mRNA. Translation: BAA99542.1.
    AB031085 mRNA. Translation: BAA92885.1.
    AB032163 Genomic DNA. Translation: BAA92893.1.
    AL355303 Genomic DNA. No translation available.
    BC020744 mRNA. Translation: AAH20744.1.
    M33375 mRNA. Translation: AAA35658.1. Different initiation.
    D26125 mRNA. Translation: BAA05122.1.
    CCDSiCCDS7064.1.
    PIRiA57407.
    S59620.
    RefSeqiNP_001809.3. NM_001818.3.
    UniGeneiHs.567245.

    Genome annotation databases

    EnsembliENST00000263126; ENSP00000263126; ENSG00000198610.
    ENST00000380448; ENSP00000369814; ENSG00000198610.
    GeneIDi1109.
    KEGGihsa:1109.
    UCSCiuc001ihw.2. human.

    Polymorphism databases

    DMDMi308153631.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S68287 mRNA. Translation: AAD14010.1 .
    AB045829 mRNA. Translation: BAA99542.1 .
    AB031085 mRNA. Translation: BAA92885.1 .
    AB032163 Genomic DNA. Translation: BAA92893.1 .
    AL355303 Genomic DNA. No translation available.
    BC020744 mRNA. Translation: AAH20744.1 .
    M33375 mRNA. Translation: AAA35658.1 . Different initiation.
    D26125 mRNA. Translation: BAA05122.1 .
    CCDSi CCDS7064.1.
    PIRi A57407.
    S59620.
    RefSeqi NP_001809.3. NM_001818.3.
    UniGenei Hs.567245.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FVL X-ray 2.40 A/B/C 1-323 [» ]
    ProteinModelPortali P17516.
    SMRi P17516. Positions 1-323.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107534. 2 interactions.
    STRINGi 9606.ENSP00000263126.

    Chemistry

    BindingDBi P17516.
    ChEMBLi CHEMBL4999.

    PTM databases

    PhosphoSitei P17516.

    Polymorphism databases

    DMDMi 308153631.

    Proteomic databases

    MaxQBi P17516.
    PaxDbi P17516.
    PRIDEi P17516.

    Protocols and materials databases

    DNASUi 1109.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263126 ; ENSP00000263126 ; ENSG00000198610 .
    ENST00000380448 ; ENSP00000369814 ; ENSG00000198610 .
    GeneIDi 1109.
    KEGGi hsa:1109.
    UCSCi uc001ihw.2. human.

    Organism-specific databases

    CTDi 1109.
    GeneCardsi GC10P005228.
    HGNCi HGNC:387. AKR1C4.
    HPAi HPA044720.
    MIMi 600451. gene.
    614279. phenotype.
    neXtProti NX_P17516.
    Orphaneti 90796. 46,XY disorder of sex development due to isolated 17, 20 lyase deficiency.
    PharmGKBi PA24680.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0656.
    HOGENOMi HOG000250272.
    HOVERGENi HBG000020.
    InParanoidi P17516.
    KOi K00037.
    K00089.
    K00092.
    K00212.
    OMAi LLHFPMA.
    OrthoDBi EOG70KGQF.
    PhylomeDBi P17516.
    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 P17516.

    Miscellaneous databases

    EvolutionaryTracei P17516.
    GeneWikii 3-alpha-HSD.
    GenomeRNAii 1109.
    NextBioi 4602.
    PROi P17516.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P17516.
    Bgeei P17516.
    CleanExi HS_AKR1C4.
    Genevestigatori P17516.

    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. "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], VARIANT ARG-250.
      Tissue: Liver.
    2. "Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases."
      Khanna M., Qin K.-N., Wang R.W., Cheng K.-C.
      J. Biol. Chem. 270:20162-20168(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, VARIANT ARG-250.
    3. "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], VARIANT ARG-250.
    4. "Characterization of a novel variant (S145C/L311V) of 3alpha-hydroxysteroid/dihydrodiol dehydrogenase in human liver."
      Kume T., Iwasa H., Shiraishi H., Yokoi T., Nagashima K., Otsuka M., Terada T., Takagi T., Hara A., Kamataki T.
      Pharmacogenetics 9:763-771(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS CYS-145; ARG-250 AND VAL-311.
      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 [GENOMIC DNA / MRNA], VARIANT ARG-250.
      Tissue: Liver.
    6. "Human types 1 and 3 3 alpha-hydroxysteroid dehydrogenases: differential lability and tissue distribution."
      Dufort I., Labrie F., Luu-The V.
      J. Clin. Endocrinol. Metab. 86:841-846(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION OF 3-ALPHA-HSD ACTIVITY, TISSUE SPECIFICITY, VARIANT ARG-250.
      Tissue: Liver.
    7. "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].
    8. "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], VARIANTS TYR-170 AND ARG-250.
      Tissue: Liver.
    9. "Isolation and characterization of cloned cDNAs encoding human liver chlordecone reductase."
      Winters C.J., Molowa D.T., Guzelian P.S.
      Biochemistry 29:1080-1087(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-323, VARIANT ARG-250.
      Tissue: Liver.
    10. "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 3-323, PROTEIN SEQUENCE OF 5-29; 76-131; 184-201 AND 271-294, VARIANT ARG-250.
      Tissue: Liver.
    11. "Human hepatic 3 alpha-hydroxysteroid dehydrogenase: possible identity with human hepatic chlordecone reductase."
      Binstock J.M., Iyer R.B., Hamby C.V., Fried V.A., Schwartz I.S., Weinstein B.I., Southren A.L.
      Biochem. Biophys. Res. Commun. 187:760-766(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 40-54; 105-121; 162-175; 184-196; 277-291 AND 307-321, CHARACTERIZATION AS 3-ALPHA-HSD.
    12. "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: INVOLVEMENT IN SRXY8.
    13. "Crystal structure of human 3-alpha hydroxysteroid/dihydrodiol dehydrogenase (AKR1C4) complexed with NADP+."
      Structural genomics consortium (SGC)
      Submitted (FEB-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NADP.

    Entry informationi

    Entry nameiAK1C4_HUMAN
    AccessioniPrimary (citable) accession number: P17516
    Secondary accession number(s): Q5T6A3, Q8WW84, Q9NS54
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 164 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