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O60760

- HPGDS_HUMAN

UniProt

O60760 - HPGDS_HUMAN

Protein

Hematopoietic prostaglandin D synthase

Gene

HPGDS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Bifunctional enzyme which catalyzes both the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation, and the conjugation of glutathione with a wide range of aryl halides and organic isothiocyanates. Also exhibits low glutathione-peroxidase activity towards cumene hydroperoxide.8 Publications

    Catalytic activityi

    (5Z,13E,15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E,15S)-9-alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate.
    RX + glutathione = HX + R-S-glutathione.

    Cofactori

    Glutathione. Required for the prostaglandin D synthase activity.4 Publications

    Enzyme regulationi

    Prostaglandin PGD2 synthesis is stimulated by calcium and magnesium ions. One calcium or magnesium ion is bound between the subunits of the homodimer. The interactions with the protein are for the most part mediated via water molecules. Magnesium increases the affinity for glutathione, while calcium has no effect on the affinity for glutathione.1 Publication

    Kineticsi

    1. KM=8 mM for glutathione for the glutathione-conjugating activity3 Publications
    2. KM=0.6 mM for glutathione for the prostaglandin D synthase activity in the presence of EDTA3 Publications
    3. KM=0.14 mM for glutathione for the prostaglandin D synthase activity in the presence of magnesium ions3 Publications

    Vmax=8.6 µmol/min/mg enzyme with 1-bromo-2,4-dinitrobenzene as substrate3 Publications

    Vmax=5.1 µmol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as substrate3 Publications

    Vmax=44.3 µmol/min/mg enzyme with 1-fluoro-2,4-dinitrobenzene as substrate3 Publications

    Vmax=10.7 µmol/min/mg enzyme with 1-iodo-2,4-dinitrobenzene as substrate3 Publications

    Vmax=6.8 µmol/min/mg enzyme with allyl isothiocyanate as substrate3 Publications

    Vmax=6.3 µmol/min/mg enzyme with benzyl isothiocyanate as substrate3 Publications

    Vmax=0.05 µmol/min/mg enzyme with cumene hydroperoxide as substrate3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei8 – 81Glutathione1 Publication
    Binding sitei14 – 141Glutathione1 Publication
    Binding sitei39 – 391Glutathione1 Publication
    Binding sitei51 – 511Glutathione; via amide nitrogen and carbonyl oxygen1 Publication

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. glutathione transferase activity Source: UniProtKB-EC
    3. magnesium ion binding Source: UniProtKB
    4. prostaglandin-D synthase activity Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. arachidonic acid metabolic process Source: Reactome
    2. cyclooxygenase pathway Source: Reactome
    3. glutathione derivative biosynthetic process Source: Reactome
    4. locomotory behavior Source: ProtInc
    5. prostaglandin metabolic process Source: UniProtKB
    6. signal transduction Source: ProtInc
    7. small molecule metabolic process Source: Reactome
    8. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Isomerase, Transferase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism

    Keywords - Ligandi

    Calcium, Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08788-MONOMER.
    ReactomeiREACT_150149. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
    REACT_6926. Glutathione conjugation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hematopoietic prostaglandin D synthase (EC:5.3.99.2)
    Short name:
    H-PGDS
    Alternative name(s):
    GST class-sigma
    Glutathione S-transferase (EC:2.5.1.18)
    Glutathione-dependent PGD synthase
    Glutathione-requiring prostaglandin D synthase
    Prostaglandin-H2 D-isomerase
    Gene namesi
    Name:HPGDS
    Synonyms:GSTS, PGDS, PTGDS2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:17890. HPGDS.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi93 – 931D → N: Loss of activation by calcium or magnesium ions. 1 Publication
    Mutagenesisi96 – 961D → N: Increases PGD2 synthesis. Loss of activation by calcium or magnesium ions. 1 Publication
    Mutagenesisi97 – 971D → N: Reduces PGD2 synthesis by 99%. Loss of activation by calcium or magnesium ions. 1 Publication

    Organism-specific databases

    PharmGKBiPA165664133.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 199199Hematopoietic prostaglandin D synthasePRO_0000185934Add
    BLAST

    Proteomic databases

    PaxDbiO60760.
    PRIDEiO60760.

    PTM databases

    PhosphoSiteiO60760.

    Expressioni

    Tissue specificityi

    Expressed in a number of megakaryocytic cell lines but not in platelets. Highly expressed in adipose tissue, macrophages and placenta. Also expressed at lower levels in lung, heart, lymph nodes, appendix, bone marrow and fetal liver.4 Publications

    Developmental stagei

    Highest levels in immature megakaryocytic cells. Disappears after final differentiation to platelets.1 Publication

    Inductioni

    By 12-O-tetradecanoylphorbol-13-acetate (TPA).1 Publication

    Gene expression databases

    ArrayExpressiO60760.
    BgeeiO60760.
    GenevestigatoriO60760.

    Organism-specific databases

    HPAiCAB020805.
    HPA024035.

    Interactioni

    Subunit structurei

    Homodimer.5 Publications

    Protein-protein interaction databases

    BioGridi118128. 1 interaction.
    STRINGi9606.ENSP00000295256.

    Structurei

    Secondary structure

    1
    199
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 129
    Helixi13 – 153
    Helixi16 – 249
    Beta strandi30 – 345
    Helixi36 – 383
    Helixi39 – 435
    Beta strandi46 – 494
    Beta strandi53 – 564
    Beta strandi59 – 624
    Helixi64 – 729
    Helixi76 – 783
    Helixi82 – 10019
    Helixi109 – 12113
    Helixi123 – 13513
    Beta strandi139 – 1424
    Helixi148 – 16316
    Turni165 – 1706
    Helixi172 – 18211
    Helixi185 – 1939

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IYHX-ray1.70A/B/C/D2-199[»]
    1IYIX-ray1.80A/B/C/D2-199[»]
    1V40X-ray1.90A/B/C/D2-199[»]
    2CVDX-ray1.45A/B/C/D2-199[»]
    2VCQX-ray1.95A/B/C/D1-199[»]
    2VCWX-ray1.95A/B/C/D1-199[»]
    2VCXX-ray2.10A/B/C/D1-199[»]
    2VCZX-ray1.95A/B/C/D1-199[»]
    2VD0X-ray2.20A/B/C/D1-199[»]
    2VD1X-ray2.25A/B/C/D1-199[»]
    3EE2X-ray1.91A/B1-199[»]
    3KXOX-ray2.10A/B1-199[»]
    3VI5X-ray2.00A/B/C/D2-199[»]
    3VI7X-ray2.00A/B/C/D2-199[»]
    4EC0X-ray1.85A/B1-199[»]
    4EDYX-ray1.72A/B2-199[»]
    4EDZX-ray2.00A/B/C/D2-199[»]
    4EE0X-ray1.75A/B2-199[»]
    ProteinModelPortaliO60760.
    SMRiO60760. Positions 2-199.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60760.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 7978GST N-terminalAdd
    BLAST
    Domaini81 – 199119GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni63 – 642Glutathione binding

    Sequence similaritiesi

    Belongs to the GST superfamily. Sigma family.Curated
    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Phylogenomic databases

    eggNOGiNOG122057.
    HOGENOMiHOG000115733.
    HOVERGENiHBG105321.
    InParanoidiO60760.
    KOiK01830.
    OMAiMSCFPWA.
    OrthoDBiEOG78WKT1.
    PhylomeDBiO60760.
    TreeFamiTF105321.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O60760-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPNYKLTYFN MRGRAEIIRY IFAYLDIQYE DHRIEQADWP EIKSTLPFGK    50
    IPILEVDGLT LHQSLAIARY LTKNTDLAGN TEMEQCHVDA IVDTLDDFMS 100
    CFPWAEKKQD VKEQMFNELL TYNAPHLMQD LDTYLGGREW LIGNSVTWAD 150
    FYWEICSTTL LVFKPDLLDN HPRLVTLRKK VQAIPAVANW IKRRPQTKL 199
    Length:199
    Mass (Da):23,344
    Last modified:January 23, 2007 - v3
    Checksum:iA4ED2476B16CC5C3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti187 – 1871V → I no nucleotide entry (PubMed:11672424)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D82073 mRNA. Translation: BAA25545.1.
    AB008830 Genomic DNA. Translation: BAA96854.1.
    AK290075 mRNA. Translation: BAF82764.1.
    CR541662 mRNA. Translation: CAG46463.1.
    CR541679 mRNA. Translation: CAG46480.1.
    CH471057 Genomic DNA. Translation: EAX06052.1.
    BC020734 mRNA. Translation: AAH20734.1.
    CCDSiCCDS3640.1.
    RefSeqiNP_055300.1. NM_014485.2.
    UniGeneiHs.128433.

    Genome annotation databases

    EnsembliENST00000295256; ENSP00000295256; ENSG00000163106.
    GeneIDi27306.
    KEGGihsa:27306.
    UCSCiuc003hte.1. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D82073 mRNA. Translation: BAA25545.1 .
    AB008830 Genomic DNA. Translation: BAA96854.1 .
    AK290075 mRNA. Translation: BAF82764.1 .
    CR541662 mRNA. Translation: CAG46463.1 .
    CR541679 mRNA. Translation: CAG46480.1 .
    CH471057 Genomic DNA. Translation: EAX06052.1 .
    BC020734 mRNA. Translation: AAH20734.1 .
    CCDSi CCDS3640.1.
    RefSeqi NP_055300.1. NM_014485.2.
    UniGenei Hs.128433.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IYH X-ray 1.70 A/B/C/D 2-199 [» ]
    1IYI X-ray 1.80 A/B/C/D 2-199 [» ]
    1V40 X-ray 1.90 A/B/C/D 2-199 [» ]
    2CVD X-ray 1.45 A/B/C/D 2-199 [» ]
    2VCQ X-ray 1.95 A/B/C/D 1-199 [» ]
    2VCW X-ray 1.95 A/B/C/D 1-199 [» ]
    2VCX X-ray 2.10 A/B/C/D 1-199 [» ]
    2VCZ X-ray 1.95 A/B/C/D 1-199 [» ]
    2VD0 X-ray 2.20 A/B/C/D 1-199 [» ]
    2VD1 X-ray 2.25 A/B/C/D 1-199 [» ]
    3EE2 X-ray 1.91 A/B 1-199 [» ]
    3KXO X-ray 2.10 A/B 1-199 [» ]
    3VI5 X-ray 2.00 A/B/C/D 2-199 [» ]
    3VI7 X-ray 2.00 A/B/C/D 2-199 [» ]
    4EC0 X-ray 1.85 A/B 1-199 [» ]
    4EDY X-ray 1.72 A/B 2-199 [» ]
    4EDZ X-ray 2.00 A/B/C/D 2-199 [» ]
    4EE0 X-ray 1.75 A/B 2-199 [» ]
    ProteinModelPortali O60760.
    SMRi O60760. Positions 2-199.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118128. 1 interaction.
    STRINGi 9606.ENSP00000295256.

    Chemistry

    BindingDBi O60760.
    ChEMBLi CHEMBL5879.
    DrugBanki DB00143. Glutathione.
    GuidetoPHARMACOLOGYi 1381.

    PTM databases

    PhosphoSitei O60760.

    Proteomic databases

    PaxDbi O60760.
    PRIDEi O60760.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295256 ; ENSP00000295256 ; ENSG00000163106 .
    GeneIDi 27306.
    KEGGi hsa:27306.
    UCSCi uc003hte.1. human.

    Organism-specific databases

    CTDi 27306.
    GeneCardsi GC04M095219.
    HGNCi HGNC:17890. HPGDS.
    HPAi CAB020805.
    HPA024035.
    MIMi 602598. gene.
    neXtProti NX_O60760.
    PharmGKBi PA165664133.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG122057.
    HOGENOMi HOG000115733.
    HOVERGENi HBG105321.
    InParanoidi O60760.
    KOi K01830.
    OMAi MSCFPWA.
    OrthoDBi EOG78WKT1.
    PhylomeDBi O60760.
    TreeFami TF105321.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS08788-MONOMER.
    Reactomei REACT_150149. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
    REACT_6926. Glutathione conjugation.

    Miscellaneous databases

    EvolutionaryTracei O60760.
    GeneWikii PGDS.
    GenomeRNAii 27306.
    NextBioi 50305.
    PROi O60760.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60760.
    Bgeei O60760.
    Genevestigatori O60760.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEi PS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure and chromosomal localization of human and mouse genes for hematopoietic prostaglandin D synthase."
      Kanaoka Y., Fujimori K., Kikuno R., Sakaguchi Y., Urade Y., Hayaishi O.
      Eur. J. Biochem. 267:3315-3322(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, TISSUE SPECIFICITY.
      Tissue: Placenta.
    2. "Mammalian class Sigma glutathione S-transferases: catalytic properties and tissue-specific expression of human and rat GSH-dependent prostaglandin D2 synthases."
      Jowsey I.R., Thomson A.M., Flanagan J.U., Murdock P.R., Moore G.B., Meyer D.J., Murphy G.J., Smith S.A., Hayes J.D.
      Biochem. J. 359:507-516(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
      Tissue: Placenta.
    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: Substantia nigra.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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: Placenta.
    7. "Induction of hematopoietic prostaglandin D synthase in human megakaryocytic cells by phorbol ester."
      Suzuki T., Watanabe K., Kanaoka Y., Sato T., Hayaishi O.
      Biochem. Biophys. Res. Commun. 241:288-293(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
      Tissue: Megakaryocyte.
    8. Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Megakaryocyte.
    9. Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH CALCIUM IONS; MAGNESIUM IONS AND GLUTATHIONE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-93; ASP-96 AND ASP-97.
    10. "First determination of the inhibitor complex structure of human hematopoietic prostaglandin D synthase."
      Inoue T., Okano Y., Kado Y., Aritake K., Irikura D., Uodome N., Okazaki N., Kinugasa S., Shishitani H., Matsumura H., Kai Y., Urade Y.
      J. Biochem. 135:279-283(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND THE SYNTHETIC INHIBITOR BSBT, FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    11. "Structural and functional characterization of HQL-79, an orally selective inhibitor of human hematopoietic prostaglandin D synthase."
      Aritake K., Kado Y., Inoue T., Miyano M., Urade Y.
      J. Biol. Chem. 281:15277-15286(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE; MAGNESIUM IONS AND THE SYNTHETIC INHIBITOR HQL-79, FUNCTION, CATALYTIC ACTIVITY.
    12. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH SYNTHETIC INHIBITORS, SUBUNIT.
    13. "Identification and characterisation of new inhibitors for the human hematopoietic prostaglandin D2 synthase."
      Weber J.E., Oakley A.J., Christ A.N., Clark A.G., Hayes J.D., Hall R., Hume D.A., Board P.G., Smythe M.L., Flanagan J.U.
      Eur. J. Med. Chem. 45:447-454(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR, CATALYTIC ACTIVITY, FUNCTION.

    Entry informationi

    Entry nameiHPGDS_HUMAN
    AccessioniPrimary (citable) accession number: O60760
    Secondary accession number(s): Q6FHT9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 139 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 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

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