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P28845

- DHI1_HUMAN

UniProt

P28845 - DHI1_HUMAN

Protein

Corticosteroid 11-beta-dehydrogenase isozyme 1

Gene

HSD11B1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes reversibly the conversion of cortisol to the inactive metabolite cortisone. Catalyzes reversibly the conversion of 7-ketocholesterol to 7-beta-hydroxycholesterol. In intact cells, the reaction runs only in one direction, from 7-ketocholesterol to 7-beta-hydroxycholesterol By similarity.By similarity

    Catalytic activityi

    An 11-beta-hydroxysteroid + NADP+ = an 11-oxosteroid + NADPH.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei170 – 1701Substrate
    Active sitei183 – 1831Proton acceptor

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi41 – 6727NADP6 PublicationsAdd
    BLAST
    Nucleotide bindingi92 – 932NADP6 Publications
    Nucleotide bindingi119 – 1213NADP6 Publications
    Nucleotide bindingi183 – 1875NADP6 Publications
    Nucleotide bindingi218 – 2225NADP6 Publications

    GO - Molecular functioni

    1. 11-beta-hydroxysteroid dehydrogenase (NADP+) activity Source: UniProtKB-EC
    2. 11-beta-hydroxysteroid dehydrogenase [NAD(P)] activity Source: Reactome

    GO - Biological processi

    1. glucocorticoid biosynthetic process Source: Reactome
    2. lung development Source: Ensembl
    3. small molecule metabolic process Source: Reactome
    4. steroid metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Lipid metabolism, Steroid metabolism

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04154-MONOMER.
    BRENDAi1.1.1.146. 2681.
    ReactomeiREACT_11036. Glucocorticoid biosynthesis.
    SABIO-RKP28845.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Corticosteroid 11-beta-dehydrogenase isozyme 1 (EC:1.1.1.146)
    Alternative name(s):
    11-beta-hydroxysteroid dehydrogenase 1
    Short name:
    11-DH
    Short name:
    11-beta-HSD1
    Gene namesi
    Name:HSD11B1
    Synonyms:HSD11, HSD11L
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:5208. HSD11B1.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Single-pass type II membrane protein 1 Publication

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: Reactome
    2. integral component of membrane Source: UniProtKB-KW
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Cortisone reductase deficiency (CRD) [MIM:604931]: In CRD, activation of cortisone to cortisol does not occur, resulting in adrenocorticotropin-mediated androgen excess and a phenotype resembling polycystic ovary syndrome (PCOS).
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi5 – 62KK → RR: Predominantly inverted topology. No effect on activity. 1 Publication
    Mutagenesisi5 – 62KK → SS: Inverted topology. Reduced Vmax. 1 Publication
    Mutagenesisi5 – 51K → R: Predominantly inverted topology. No effect on activity. 1 Publication
    Mutagenesisi5 – 51K → S: Inverted topology. No effect on activity. 1 Publication
    Mutagenesisi6 – 61K → R: No effect on topology. Increased Km for corticosterone. 1 Publication
    Mutagenesisi6 – 61K → S: No effect on topology or activity. 1 Publication
    Mutagenesisi18 – 214YYYY → AAAA: No effect on topology. Reduced Vmax.
    Mutagenesisi18 – 214YYYY → FFFF: No effect on topology or activity.
    Mutagenesisi19 – 213YYY → AYA: No effect on topology. Reduced Vmax.
    Mutagenesisi25 – 262EE → KK: Inverted topology. Reduced Vmax. 1 Publication
    Mutagenesisi25 – 262EE → KQ: No effect on topology. Reduced Vmax. 1 Publication
    Mutagenesisi25 – 262EE → QQ: Reduced Vmax. 1 Publication
    Mutagenesisi25 – 251E → K or Q: No effect on activity. 1 Publication
    Mutagenesisi26 – 261E → K: No effect on activity. 1 Publication
    Mutagenesisi35 – 362KK → SS: Complete loss of activity.

    Organism-specific databases

    MIMi604931. phenotype.
    Orphaneti168588. Hyperandrogenism due to cortisone reductase deficiency.
    PharmGKBiPA29476.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 292291Corticosteroid 11-beta-dehydrogenase isozyme 1PRO_0000054619Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi123 – 1231N-linked (GlcNAc...)2 Publications
    Glycosylationi162 – 1621N-linked (GlcNAc...)2 Publications
    Glycosylationi207 – 2071N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Glycosylated.2 Publications

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiP28845.
    PaxDbiP28845.
    PRIDEiP28845.

    PTM databases

    PhosphoSiteiP28845.

    Expressioni

    Tissue specificityi

    Widely expressed. Highest expression in liver.

    Gene expression databases

    BgeeiP28845.
    CleanExiHS_HSD11B1.
    GenevestigatoriP28845.

    Organism-specific databases

    HPAiHPA047729.

    Interactioni

    Subunit structurei

    Homodimer.6 Publications

    Protein-protein interaction databases

    BioGridi109523. 2 interactions.
    DIPiDIP-59618N.
    IntActiP28845. 1 interaction.
    STRINGi9606.ENSP00000261465.

    Structurei

    Secondary structure

    1
    292
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi29 – 324
    Beta strandi36 – 416
    Helixi45 – 5612
    Beta strandi60 – 667
    Helixi68 – 8114
    Beta strandi84 – 907
    Helixi96 – 11015
    Beta strandi114 – 1185
    Helixi133 – 14311
    Helixi145 – 16117
    Beta strandi164 – 1707
    Helixi171 – 1733
    Helixi181 – 20424
    Beta strandi209 – 2157
    Helixi221 – 2266
    Helixi229 – 2346
    Helixi238 – 25013
    Beta strandi254 – 2585
    Helixi262 – 2676
    Helixi271 – 28010
    Helixi281 – 2833
    Turni287 – 2893

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XU7X-ray1.80A/B/C/D24-292[»]
    1XU9X-ray1.55A/B/C/D24-292[»]
    2BELX-ray2.11A/B/C/D26-284[»]
    2ILTX-ray2.30A24-285[»]
    2IRWX-ray3.10A/B/C/D/E/F/G/H26-289[»]
    2RBEX-ray1.90A/B/C/D25-292[»]
    3BYZX-ray2.69A/B/C/D25-292[»]
    3BZUX-ray2.25A/B/C/D24-292[»]
    3CH6X-ray2.35A/B/D/E24-292[»]
    3CZRX-ray2.35A/B24-292[»]
    3D3EX-ray2.60A/B/C/D24-292[»]
    3D4NX-ray2.50A/B/C/D24-292[»]
    3D5QX-ray2.55A/B/C/D24-292[»]
    3EY4X-ray3.00A/B/C/D25-292[»]
    3FCOX-ray2.65A/B24-291[»]
    3FRJX-ray2.30A/B24-292[»]
    3H6KX-ray2.19A/B/C/D24-292[»]
    3HFGX-ray2.30A/B/C/D24-292[»]
    3OQ1X-ray2.60A/B/C/D24-292[»]
    3PDJX-ray2.30A/B24-292[»]
    3QQPX-ray2.72A/B/C/D24-292[»]
    3TFQX-ray1.80A/B/D/E24-292[»]
    4BB5X-ray2.20A/B/C/D1-292[»]
    4BB6X-ray2.55A/B1-292[»]
    4C7KX-ray1.91A/B/C/D24-292[»]
    4HFRX-ray2.73A/B24-292[»]
    4HX5X-ray2.19A/B/C/D24-292[»]
    4IJUX-ray2.35A/B/D/E24-292[»]
    4IJVX-ray2.35A/B/D/E24-292[»]
    4IJWX-ray2.35A/B/D/E24-292[»]
    4K1LX-ray1.96A/B/C/D24-292[»]
    4P38X-ray2.80A/B26-290[»]
    ProteinModelPortaliP28845.
    SMRiP28845. Positions 26-277.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP28845.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 76CytoplasmicSequence Analysis
    Topological domaini25 – 292268LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei8 – 2417Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1028.
    HOGENOMiHOG000010276.
    HOVERGENiHBG005481.
    InParanoidiP28845.
    KOiK15680.
    OMAiWGGLDML.
    OrthoDBiEOG7353X9.
    PhylomeDBiP28845.
    TreeFamiTF329114.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002198. 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]
    PRINTSiPR00081. GDHRDH.
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P28845-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAFMKKYLLP ILGLFMAYYY YSANEEFRPE MLQGKKVIVT GASKGIGREM    50
    AYHLAKMGAH VVVTARSKET LQKVVSHCLE LGAASAHYIA GTMEDMTFAE 100
    QFVAQAGKLM GGLDMLILNH ITNTSLNLFH DDIHHVRKSM EVNFLSYVVL 150
    TVAALPMLKQ SNGSIVVVSS LAGKVAYPMV AAYSASKFAL DGFFSSIRKE 200
    YSVSRVNVSI TLCVLGLIDT ETAMKAVSGI VHMQAAPKEE CALEIIKGGA 250
    LRQEEVYYDS SLWTTLLIRN PCRKILEFLY STSYNMDRFI NK 292
    Length:292
    Mass (Da):32,401
    Last modified:January 23, 2007 - v3
    Checksum:i4632D0F3BBEFC474
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti148 – 1481V → E in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035845

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M76665
    , M76661, M76662, M76663, M76664 Genomic DNA. Translation: AAC31757.1.
    AY044084, AY044083 Genomic DNA. Translation: AAK83653.1.
    AK313973 mRNA. Translation: BAG36688.1.
    AL022398, AL031316 Genomic DNA. Translation: CAA18541.2.
    AL031316, AL022398 Genomic DNA. Translation: CAI20063.1.
    CH471100 Genomic DNA. Translation: EAW93445.1.
    CH471100 Genomic DNA. Translation: EAW93446.1.
    BC012593 mRNA. Translation: AAH12593.1.
    CCDSiCCDS1489.1.
    PIRiA41173. DXHUBH.
    RefSeqiNP_001193670.1. NM_001206741.1.
    NP_005516.1. NM_005525.3.
    NP_861420.1. NM_181755.2.
    UniGeneiHs.195040.

    Genome annotation databases

    EnsembliENST00000261465; ENSP00000261465; ENSG00000117594.
    ENST00000367027; ENSP00000355994; ENSG00000117594.
    ENST00000367028; ENSP00000355995; ENSG00000117594.
    GeneIDi3290.
    KEGGihsa:3290.
    UCSCiuc001hhj.3. human.

    Polymorphism databases

    DMDMi118569.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M76665
    , M76661 , M76662 , M76663 , M76664 Genomic DNA. Translation: AAC31757.1 .
    AY044084 , AY044083 Genomic DNA. Translation: AAK83653.1 .
    AK313973 mRNA. Translation: BAG36688.1 .
    AL022398 , AL031316 Genomic DNA. Translation: CAA18541.2 .
    AL031316 , AL022398 Genomic DNA. Translation: CAI20063.1 .
    CH471100 Genomic DNA. Translation: EAW93445.1 .
    CH471100 Genomic DNA. Translation: EAW93446.1 .
    BC012593 mRNA. Translation: AAH12593.1 .
    CCDSi CCDS1489.1.
    PIRi A41173. DXHUBH.
    RefSeqi NP_001193670.1. NM_001206741.1.
    NP_005516.1. NM_005525.3.
    NP_861420.1. NM_181755.2.
    UniGenei Hs.195040.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XU7 X-ray 1.80 A/B/C/D 24-292 [» ]
    1XU9 X-ray 1.55 A/B/C/D 24-292 [» ]
    2BEL X-ray 2.11 A/B/C/D 26-284 [» ]
    2ILT X-ray 2.30 A 24-285 [» ]
    2IRW X-ray 3.10 A/B/C/D/E/F/G/H 26-289 [» ]
    2RBE X-ray 1.90 A/B/C/D 25-292 [» ]
    3BYZ X-ray 2.69 A/B/C/D 25-292 [» ]
    3BZU X-ray 2.25 A/B/C/D 24-292 [» ]
    3CH6 X-ray 2.35 A/B/D/E 24-292 [» ]
    3CZR X-ray 2.35 A/B 24-292 [» ]
    3D3E X-ray 2.60 A/B/C/D 24-292 [» ]
    3D4N X-ray 2.50 A/B/C/D 24-292 [» ]
    3D5Q X-ray 2.55 A/B/C/D 24-292 [» ]
    3EY4 X-ray 3.00 A/B/C/D 25-292 [» ]
    3FCO X-ray 2.65 A/B 24-291 [» ]
    3FRJ X-ray 2.30 A/B 24-292 [» ]
    3H6K X-ray 2.19 A/B/C/D 24-292 [» ]
    3HFG X-ray 2.30 A/B/C/D 24-292 [» ]
    3OQ1 X-ray 2.60 A/B/C/D 24-292 [» ]
    3PDJ X-ray 2.30 A/B 24-292 [» ]
    3QQP X-ray 2.72 A/B/C/D 24-292 [» ]
    3TFQ X-ray 1.80 A/B/D/E 24-292 [» ]
    4BB5 X-ray 2.20 A/B/C/D 1-292 [» ]
    4BB6 X-ray 2.55 A/B 1-292 [» ]
    4C7K X-ray 1.91 A/B/C/D 24-292 [» ]
    4HFR X-ray 2.73 A/B 24-292 [» ]
    4HX5 X-ray 2.19 A/B/C/D 24-292 [» ]
    4IJU X-ray 2.35 A/B/D/E 24-292 [» ]
    4IJV X-ray 2.35 A/B/D/E 24-292 [» ]
    4IJW X-ray 2.35 A/B/D/E 24-292 [» ]
    4K1L X-ray 1.96 A/B/C/D 24-292 [» ]
    4P38 X-ray 2.80 A/B 26-290 [» ]
    ProteinModelPortali P28845.
    SMRi P28845. Positions 26-277.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109523. 2 interactions.
    DIPi DIP-59618N.
    IntActi P28845. 1 interaction.
    STRINGi 9606.ENSP00000261465.

    Chemistry

    BindingDBi P28845.
    ChEMBLi CHEMBL4235.
    DrugBanki DB00157. NADH.
    GuidetoPHARMACOLOGYi 2763.

    PTM databases

    PhosphoSitei P28845.

    Polymorphism databases

    DMDMi 118569.

    Proteomic databases

    MaxQBi P28845.
    PaxDbi P28845.
    PRIDEi P28845.

    Protocols and materials databases

    DNASUi 3290.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261465 ; ENSP00000261465 ; ENSG00000117594 .
    ENST00000367027 ; ENSP00000355994 ; ENSG00000117594 .
    ENST00000367028 ; ENSP00000355995 ; ENSG00000117594 .
    GeneIDi 3290.
    KEGGi hsa:3290.
    UCSCi uc001hhj.3. human.

    Organism-specific databases

    CTDi 3290.
    GeneCardsi GC01P209859.
    HGNCi HGNC:5208. HSD11B1.
    HPAi HPA047729.
    MIMi 600713. gene.
    604931. phenotype.
    neXtProti NX_P28845.
    Orphaneti 168588. Hyperandrogenism due to cortisone reductase deficiency.
    PharmGKBi PA29476.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1028.
    HOGENOMi HOG000010276.
    HOVERGENi HBG005481.
    InParanoidi P28845.
    KOi K15680.
    OMAi WGGLDML.
    OrthoDBi EOG7353X9.
    PhylomeDBi P28845.
    TreeFami TF329114.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS04154-MONOMER.
    BRENDAi 1.1.1.146. 2681.
    Reactomei REACT_11036. Glucocorticoid biosynthesis.
    SABIO-RK P28845.

    Miscellaneous databases

    EvolutionaryTracei P28845.
    GeneWikii 11%CE%B2-hydroxysteroid_dehydrogenase_type_1.
    GenomeRNAii 3290.
    NextBioi 13049.
    PROi P28845.
    SOURCEi Search...

    Gene expression databases

    Bgeei P28845.
    CleanExi HS_HSD11B1.
    Genevestigatori P28845.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi 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 ]
    PRINTSi PR00081. GDHRDH.
    PROSITEi PS00061. ADH_SHORT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human gene for 11 beta-hydroxysteroid dehydrogenase. Structure, tissue distribution, and chromosomal localization."
      Tannin G.M., Agarwal A.K., Monder C., New M.I., White P.C.
      J. Biol. Chem. 266:16653-16658(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Testis.
    2. "Association studies between microsatellite markers within the gene encoding human 11beta-hydroxysteroid dehydrogenase type 1 and body mass index, waist to hip ratio, and glucocorticoid metabolism."
      Draper N., Echwald S.M., Lavery G.G., Walker E.A., Fraser R., Davies E., Soerensen T.I.A., Astrup A., Adamski J., Hewison M., Connell J.M., Pedersen O., Stewart P.M.
      J. Clin. Endocrinol. Metab. 87:4984-4990(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "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].
      Tissue: Liver.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Brain.
    7. "The N-terminal anchor sequences of 11beta-hydroxysteroid dehydrogenases determine their orientation in the endoplasmic reticulum membrane."
      Odermatt A., Arnold P., Stauffer A., Frey B.M., Frey F.J.
      J. Biol. Chem. 274:28762-28770(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION, MUTAGENESIS OF LYS-5; 5-LYS-LYS-6; LYS-6; 18-TYR--TYR-21 AND 19-TYR--TYR-21.
    8. "Mutations in the genes encoding 11beta-hydroxysteroid dehydrogenase type 1 and hexose-6-phosphate dehydrogenase interact to cause cortisone reductase deficiency."
      Draper N., Walker E.A., Bujalska I.J., Tomlinson J.W., Chalder S.M., Arlt W., Lavery G.G., Bedendo O., Ray D.W., Laing I., Malunowicz E., White P.C., Hewison M., Mason P.J., Connell J.M., Shackleton C.H.L., Stewart P.M.
      Nat. Genet. 34:434-439(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CDR.
    9. "Appropriate function of 11beta-hydroxysteroid dehydrogenase type 1 in the endoplasmic reticulum lumen is dependent on its N-terminal region sharing similar topological determinants with 50-kDa esterase."
      Frick C., Atanasov A.G., Arnold P., Ozols J., Odermatt A.
      J. Biol. Chem. 279:31131-31138(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, TOPOLOGY, MUTAGENESIS OF 5-LYS-LYS-6; GLU-25; 25-GLU-GLU-26; GLU-26 AND 35-LYS-LYS-36.
    10. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-123 AND ASN-162.
      Tissue: Liver.
    11. "Conformational flexibility in crystal structures of human 11beta-hydroxysteroid dehydrogenase type I provide insights into glucocorticoid interconversion and enzyme regulation."
      Hosfield D.J., Wu Y., Skene R.J., Hilgers M., Jennings A., Snell G.P., Aertgeerts K.
      J. Biol. Chem. 280:4639-4648(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 24-292 IN COMPLEX WITH NADP AND SUBSTRATE ANALOG, SUBUNIT.
    12. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 24-284 IN COMPLEXES WITH ADAMANTANE SULFONE AND SULFONAMIDE INHIBITORS, CATALYTIC ACTIVITY.
    13. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-292 IN COMPLEX WITH NADP AND INHIBITOR, SUBUNIT, CATALYTIC ACTIVITY.
    14. Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 24-292 IN COMPLEX WITH NADP AND INHIBITOR.
    15. "Structural characterization and pharmacodynamic effects of an orally active 11beta-hydroxysteroid dehydrogenase type 1 inhibitor."
      Hale C., Veniant M., Wang Z., Chen M., McCormick J., Cupples R., Hickman D., Min X., Sudom A., Xu H., Matsumoto G., Fotsch C., St Jean D.J. Jr., Wang M.
      Chem. Biol. Drug Des. 71:36-44(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 24-292 IN COMPLEX WITH NADP AND INHIBITOR.
    16. "Discovery of novel, potent benzamide inhibitors of 11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1) exhibiting oral activity in an enzyme inhibition ex vivo model."
      Julian L.D., Wang Z., Bostick T., Caille S., Choi R., DeGraffenreid M., Di Y., He X., Hungate R.W., Jaen J.C., Liu J., Monshouwer M., McMinn D., Rew Y., Sudom A., Sun D., Tu H., Ursu S.
      , Walker N., Yan X., Ye Q., Powers J.P.
      J. Med. Chem. 51:3953-3960(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 24-292 IN COMPLEX WITH NADP AND INHIBITOR.
    17. "Discovery and optimization of piperidyl benzamide derivatives as a novel class of 11beta-HSD1 inhibitors."
      Rew Y., McMinn D.L., Wang Z., He X., Hungate R.W., Jaen J.C., Sudom A., Sun D., Tu H., Ursu S., Villemure E., Walker N.P.C., Yan X., Ye Q., Powers J.P.
      Bioorg. Med. Chem. Lett. 19:1797-1801(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 24-292 IN COMPLEX WITH NADP AND INHIBITOR.
    18. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-148.

    Entry informationi

    Entry nameiDHI1_HUMAN
    AccessioniPrimary (citable) accession number: P28845
    Secondary accession number(s): B2R9Z1, D3DT89
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 153 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, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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