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P14061

- DHB1_HUMAN

UniProt

P14061 - DHB1_HUMAN

Protein

Estradiol 17-beta-dehydrogenase 1

Gene

HSD17B1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 3 (30 Nov 2010)
      Previous versions | rss
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    Functioni

    Favors the reduction of estrogens and androgens. Also has 20-alpha-HSD activity. Uses preferentially NADH.

    Catalytic activityi

    17-beta-estradiol + NAD(P)+ = estrone + NAD(P)H.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei66 – 661NADP1 Publication
    Binding sitei143 – 1431Substrate1 Publication
    Active sitei156 – 1561Proton acceptor
    Binding sitei160 – 1601NADP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 3829NADP1 PublicationAdd
    BLAST

    GO - Molecular functioni

    1. catalytic activity Source: ProtInc
    2. estradiol 17-beta-dehydrogenase activity Source: Reactome

    GO - Biological processi

    1. bone development Source: Ensembl
    2. cellular response to metal ion Source: Ensembl
    3. estrogen biosynthetic process Source: Reactome
    4. estrogen metabolic process Source: ProtInc
    5. small molecule metabolic process Source: Reactome
    6. steroid biosynthetic process Source: ProtInc
    7. steroid metabolic process Source: Reactome
    8. testosterone biosynthetic process Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    ReactomeiREACT_11037. Estrogen biosynthesis.
    REACT_160156. The canonical retinoid cycle in rods (twilight vision).
    SABIO-RKP14061.
    UniPathwayiUPA00769.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Estradiol 17-beta-dehydrogenase 1 (EC:1.1.1.62)
    Alternative name(s):
    17-beta-hydroxysteroid dehydrogenase type 1
    Short name:
    17-beta-HSD 1
    20 alpha-hydroxysteroid dehydrogenase
    Short name:
    20-alpha-HSD
    E2DH
    Placental 17-beta-hydroxysteroid dehydrogenase
    Gene namesi
    Name:HSD17B1
    Synonyms:E17KSR, EDH17B1, EDH17B2, EDHB17
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:5210. HSD17B1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. nuclear membrane Source: HPA
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi150 – 1501L → V: Alters substrate specificity. 1 Publication

    Organism-specific databases

    PharmGKBiPA29478.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 328327Estradiol 17-beta-dehydrogenase 1PRO_0000054567Add
    BLAST

    Proteomic databases

    PaxDbiP14061.
    PRIDEiP14061.

    Expressioni

    Gene expression databases

    ArrayExpressiP14061.
    BgeeiP14061.
    CleanExiHS_HSD17B1.
    GenevestigatoriP14061.

    Organism-specific databases

    HPAiHPA021032.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi109525. 1 interaction.
    STRINGi9606.ENSP00000225929.

    Structurei

    Secondary structure

    1
    328
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 96
    Helixi14 – 2411
    Beta strandi31 – 388
    Helixi40 – 423
    Helixi44 – 529
    Beta strandi59 – 646
    Helixi70 – 789
    Beta strandi86 – 905
    Helixi100 – 1023
    Helixi105 – 11511
    Helixi117 – 13317
    Beta strandi136 – 1438
    Helixi144 – 1463
    Helixi154 – 17421
    Helixi175 – 1773
    Beta strandi179 – 1868
    Beta strandi189 – 1924
    Turni193 – 1964
    Helixi201 – 2066
    Helixi210 – 23021
    Helixi234 – 24613
    Beta strandi252 – 2565
    Beta strandi258 – 2603
    Helixi261 – 2699
    Helixi274 – 28512

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A27X-ray1.90A2-290[»]
    1BHSX-ray2.20A2-328[»]
    1DHTX-ray2.24A2-328[»]
    1EQUX-ray3.00A/B2-328[»]
    1FDSX-ray1.70A2-328[»]
    1FDTX-ray2.20A2-328[»]
    1FDUX-ray2.70A/B/C/D2-328[»]
    1FDVX-ray3.10A/B/C/D2-328[»]
    1FDWX-ray2.70A2-328[»]
    1I5RX-ray1.60A2-328[»]
    1IOLX-ray2.30A2-328[»]
    1JTVX-ray1.54A2-328[»]
    1QYVX-ray1.81A2-328[»]
    1QYWX-ray1.63A2-328[»]
    1QYXX-ray1.89A2-328[»]
    3DEYX-ray1.70X2-328[»]
    3DHEX-ray2.30A2-328[»]
    3HB4X-ray2.21X2-328[»]
    3HB5X-ray2.00X2-328[»]
    3KLMX-ray1.70X2-328[»]
    3KLPX-ray2.50X2-328[»]
    3KM0X-ray2.30A/B2-328[»]
    DisProtiDP00023.
    ProteinModelPortaliP14061.
    SMRiP14061. Positions 2-286.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14061.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1028.
    HOVERGENiHBG014077.
    InParanoidiP14061.
    KOiK00044.
    OrthoDBiEOG76T9RW.
    PhylomeDBiP14061.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR011348. 17beta_DH.
    IPR002198. DH_sc/Rdtase_SDR.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view]
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000095. 17beta-HSD. 1 hit.
    PRINTSiPR00081. GDHRDH.
    PR00080. SDRFAMILY.
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P14061-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARTVVLITG CSSGIGLHLA VRLASDPSQS FKVYATLRDL KTQGRLWEAA    50
    RALACPPGSL ETLQLDVRDS KSVAAARERV TEGRVDVLVC NAGLGLLGPL 100
    EALGEDAVAS VLDVNVVGTV RMLQAFLPDM KRRGSGRVLV TGSVGGLMGL 150
    PFNDVYCASK FALEGLCESL AVLLLPFGVH LSLIECGPVH TAFMEKVLGS 200
    PEEVLDRTDI HTFHRFYQYL AHSKQVFREA AQNPEEVAEV FLTALRAPKP 250
    TLRYFTTERF LPLLRMRLDD PSGSNYVTAM HREVFGDVPA KAEAGAEAGG 300
    GAGPGAEDEA GRGAVGDPEL GDPPAAPQ 328
    Length:328
    Mass (Da):34,950
    Last modified:November 30, 2010 - v3
    Checksum:i5B5C8909F9120832
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31R → E AA sequence (PubMed:5045524)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti238 – 2381A → V.1 Publication
    VAR_006951
    Natural varianti313 – 3131G → S.10 Publications
    Corresponds to variant rs605059 [ dbSNP | Ensembl ].
    VAR_006952

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13440 mRNA. Translation: CAA31792.1.
    M36263 mRNA. Translation: AAA35600.1.
    M27138 Genomic DNA. Translation: AAB16941.1.
    M84472 Genomic DNA. Translation: AAB16942.1.
    U34879 Genomic DNA. Translation: AAD05019.1.
    AK127832 mRNA. Translation: BAG54583.1.
    AC067852 Genomic DNA. No translation available.
    CH471152 Genomic DNA. Translation: EAW60836.1.
    BC104752 mRNA. Translation: AAI04753.1.
    BC111935 mRNA. Translation: AAI11936.1.
    CCDSiCCDS11428.1.
    PIRiA36081. DEHUE7.
    RefSeqiNP_000404.2. NM_000413.2.
    UniGeneiHs.654385.
    Hs.655222.

    Genome annotation databases

    EnsembliENST00000585807; ENSP00000466799; ENSG00000108786.
    GeneIDi3292.
    KEGGihsa:3292.
    UCSCiuc002hzw.3. human.

    Polymorphism databases

    DMDMi313104233.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    SHMPD

    The Singapore human mutation and polymorphism database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13440 mRNA. Translation: CAA31792.1 .
    M36263 mRNA. Translation: AAA35600.1 .
    M27138 Genomic DNA. Translation: AAB16941.1 .
    M84472 Genomic DNA. Translation: AAB16942.1 .
    U34879 Genomic DNA. Translation: AAD05019.1 .
    AK127832 mRNA. Translation: BAG54583.1 .
    AC067852 Genomic DNA. No translation available.
    CH471152 Genomic DNA. Translation: EAW60836.1 .
    BC104752 mRNA. Translation: AAI04753.1 .
    BC111935 mRNA. Translation: AAI11936.1 .
    CCDSi CCDS11428.1.
    PIRi A36081. DEHUE7.
    RefSeqi NP_000404.2. NM_000413.2.
    UniGenei Hs.654385.
    Hs.655222.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A27 X-ray 1.90 A 2-290 [» ]
    1BHS X-ray 2.20 A 2-328 [» ]
    1DHT X-ray 2.24 A 2-328 [» ]
    1EQU X-ray 3.00 A/B 2-328 [» ]
    1FDS X-ray 1.70 A 2-328 [» ]
    1FDT X-ray 2.20 A 2-328 [» ]
    1FDU X-ray 2.70 A/B/C/D 2-328 [» ]
    1FDV X-ray 3.10 A/B/C/D 2-328 [» ]
    1FDW X-ray 2.70 A 2-328 [» ]
    1I5R X-ray 1.60 A 2-328 [» ]
    1IOL X-ray 2.30 A 2-328 [» ]
    1JTV X-ray 1.54 A 2-328 [» ]
    1QYV X-ray 1.81 A 2-328 [» ]
    1QYW X-ray 1.63 A 2-328 [» ]
    1QYX X-ray 1.89 A 2-328 [» ]
    3DEY X-ray 1.70 X 2-328 [» ]
    3DHE X-ray 2.30 A 2-328 [» ]
    3HB4 X-ray 2.21 X 2-328 [» ]
    3HB5 X-ray 2.00 X 2-328 [» ]
    3KLM X-ray 1.70 X 2-328 [» ]
    3KLP X-ray 2.50 X 2-328 [» ]
    3KM0 X-ray 2.30 A/B 2-328 [» ]
    DisProti DP00023.
    ProteinModelPortali P14061.
    SMRi P14061. Positions 2-286.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109525. 1 interaction.
    STRINGi 9606.ENSP00000225929.

    Chemistry

    BindingDBi P14061.
    ChEMBLi CHEMBL3181.
    DrugBanki DB00157. NADH.

    Polymorphism databases

    DMDMi 313104233.

    Proteomic databases

    PaxDbi P14061.
    PRIDEi P14061.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000585807 ; ENSP00000466799 ; ENSG00000108786 .
    GeneIDi 3292.
    KEGGi hsa:3292.
    UCSCi uc002hzw.3. human.

    Organism-specific databases

    CTDi 3292.
    GeneCardsi GC17P040701.
    H-InvDB HIX0202506.
    HGNCi HGNC:5210. HSD17B1.
    HPAi HPA021032.
    MIMi 109684. gene.
    neXtProti NX_P14061.
    PharmGKBi PA29478.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1028.
    HOVERGENi HBG014077.
    InParanoidi P14061.
    KOi K00044.
    OrthoDBi EOG76T9RW.
    PhylomeDBi P14061.

    Enzyme and pathway databases

    UniPathwayi UPA00769 .
    Reactomei REACT_11037. Estrogen biosynthesis.
    REACT_160156. The canonical retinoid cycle in rods (twilight vision).
    SABIO-RK P14061.

    Miscellaneous databases

    EvolutionaryTracei P14061.
    GeneWikii HSD17B1.
    GenomeRNAii 3292.
    NextBioi 13059.
    PROi P14061.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P14061.
    Bgeei P14061.
    CleanExi HS_HSD17B1.
    Genevestigatori P14061.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR011348. 17beta_DH.
    IPR002198. DH_sc/Rdtase_SDR.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view ]
    Pfami PF00106. adh_short. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000095. 17beta-HSD. 1 hit.
    PRINTSi PR00081. GDHRDH.
    PR00080. SDRFAMILY.
    PROSITEi PS00061. ADH_SHORT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete amino acid sequence of human placental 17 beta-hydroxysteroid dehydrogenase deduced from cDNA."
      Peltoketo H., Isomaa V., Maeentausta O., Vihko R.
      FEBS Lett. 239:73-77(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-313.
      Tissue: Placenta.
    2. "Characterization of cDNAs for human estradiol 17 beta-dehydrogenase and assignment of the gene to chromosome 17: evidence of two mRNA species with distinct 5'-termini in human placenta."
      Luu-The V., Labrie C., Zhao H.F., Couet J., Lachance Y., Simard J., Leblanc G., Labrie F.
      Mol. Endocrinol. 3:1301-1309(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-313.
      Tissue: Placenta.
    3. "Structure of two in tandem human 17 beta-hydroxysteroid dehydrogenase genes."
      Luu-The V., Labrie C., Simard J., Lachance Y., Zhao H.F., Couet J., Leblanc G., Labrie F.
      Mol. Endocrinol. 4:268-275(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-313.
    4. "Purification, cloning, complementary DNA structure, and predicted amino acid sequence of human estradiol 17 beta-dehydrogenase."
      Luu-The V., Labrie C., Zhao H.F., Couet J., Lachance Y., Simard J., Cote J., Leblanc G., Lagace L., Berube D., Gagne R., Labrie F.
      Ann. N. Y. Acad. Sci. 595:40-52(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-313.
    5. "Genomic organization and DNA sequences of human 17 beta-hydroxysteroid dehydrogenase genes and flanking regions. Localization of multiple Alu sequences and putative cis-acting elements."
      Peltoketo H.E., Isomma V., Vihko R.
      Eur. J. Biochem. 209:459-466(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-313.
    6. Shen Y., Gibbs R.A.
      Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-313.
    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], VARIANT SER-313.
      Tissue: Placenta.
    8. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-313.
    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], VARIANT SER-313.
      Tissue: Brain.
    11. "Amino acid composition and subunit structure. Human placental 17 - estradiol dehydrogenase."
      Burns D.J.W., Engel L.L., Bethune J.L.
      Biochemistry 11:2699-2703(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-6.
    12. "Human placental 17 -oestradiol dehydrogenase. Sequence of a tryptic peptide containing an essential cysteine."
      Nicholas J.C., Harris J.I.
      FEBS Lett. 29:173-176(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 52-68.
    13. "Human placental estradiol 17 beta-dehydrogenase: sequence of a histidine-bearing peptide in the catalytic region."
      Murdock G.L., Chin C.-C., Warren J.C.
      Biochemistry 25:641-646(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 205-224.
    14. "Human placental estradiol 17 beta-dehydrogenase. Identification of a single histidine residue affinity-labeled by both 3-bromoacetoxyestrone and 12 beta-bromoacetoxy-4-estrene-3,17-dione."
      Murdock G.L., Chin C.C., Offord R.E., Bradshaw R.A., Warren J.C.
      J. Biol. Chem. 258:11460-11464(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 220-224.
    15. "Human placental 17 beta-hydroxysteroid dehydrogenase is homologous to NodG protein of Rhizobium meliloti."
      Baker M.E.
      Mol. Endocrinol. 3:881-884(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: SIMILARITY TO SHORT CHAIN DEHYDROGENASES.
    16. "Structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase at 2.20-A resolution."
      Ghosh D., Pletnev V.Z., Zhu D.W., Wawrzak Z., Duax W.L., Pangborn W., Labrie F., Lin S.-X.
      Structure 3:503-513(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
    17. "Crystal structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase complexed with 17 beta-estradiol."
      Azzi A., Rehse P.H., Zhu D.W., Campbell R.L., Labrie F., Lin S.X.
      Nat. Struct. Biol. 3:665-668(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    18. "The structure of a complex of human 17beta-hydroxysteroid dehydrogenase with estradiol and NADP+ identifies two principal targets for the design of inhibitors."
      Breton R., Housset D., Mazza C., Fontecilla-Camps J.-C.
      Structure 4:905-915(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND NADP.
    19. "Unusual charge stabilization of NADP+ in 17beta-hydroxysteroid dehydrogenase."
      Mazza C., Breton R., Housset D., Fontecilla-Camps J.-C.
      J. Biol. Chem. 273:8145-8152(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
    20. "Structure of the ternary complex of human 17beta-hydroxysteroid dehydrogenase type 1 with 3-hydroxyestra-1,3,5,7-tetraen-17-one (equilin) and NADP+."
      Sawicki M.W., Erman M., Puranen T., Vihko P., Ghosh D.
      Proc. Natl. Acad. Sci. U.S.A. 96:840-845(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    21. "Dehydroepiandrosterone and dihydrotestosterone recognition by human estrogenic 17beta-hydroxysteroid dehydrogenase. C-18/c-19 steroid discrimination and enzyme-induced strain."
      Han Q., Campbell R.L., Gangloff A., Huang Y.-W., Lin S.-X.
      J. Biol. Chem. 275:1105-1111(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 39-328, MUTAGENESIS OF LEU-150.
    22. "A concerted, rational design of type 1 17beta-hydroxysteroid dehydrogenase inhibitors: estradiol-adenosine hybrids with high affinity."
      Qiu W., Campbell R.L., Gangloff A., Dupuis P., Boivin R.P., Tremblay M.R., Poirier D., Lin S.X.
      FASEB J. 16:1829-1831(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
    23. "Pseudo-symmetry of C19 steroids, alternative binding orientations, and multispecificity in human estrogenic 17beta-hydroxysteroid dehydrogenase."
      Gangloff A., Shi R., Nahoum V., Lin S.X.
      FASEB J. 17:274-276(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS).
    24. "Cofactor hydrogen bonding onto the protein main chain is conserved in the short chain dehydrogenase/reductase family and contributes to nicotinamide orientation."
      Shi R., Lin S.X.
      J. Biol. Chem. 279:16778-16785(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS).
    25. "Detection of polymorphisms in the estradiol 17 beta-hydroxysteroid dehydrogenase II gene at the EDH17B2 locus on 17q11-q21."
      Normand T., Narod S., Labrie F., Simard J.
      Hum. Mol. Genet. 2:479-483(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VAL-238 AND SER-313.

    Entry informationi

    Entry nameiDHB1_HUMAN
    AccessioniPrimary (citable) accession number: P14061
    Secondary accession number(s): B3KXS1, Q2M2L8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 161 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 17
      Human chromosome 17: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3