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O60760

- HPGDS_HUMAN

UniProt

O60760 - HPGDS_HUMAN

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Protein

Hematopoietic prostaglandin D synthase

Gene

HPGDS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

glutathione4 PublicationsNote: Glutathione is 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
Complete GO annotation...

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.
SABIO-RKO60760.

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
Complete GO annotation...

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

BgeeiO60760.
ExpressionAtlasiO60760. baseline and differential.
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 – 129Combined sources
Helixi13 – 153Combined sources
Helixi16 – 249Combined sources
Beta strandi30 – 345Combined sources
Helixi36 – 383Combined sources
Helixi39 – 435Combined sources
Beta strandi46 – 494Combined sources
Beta strandi53 – 564Combined sources
Beta strandi59 – 624Combined sources
Helixi64 – 729Combined sources
Helixi76 – 783Combined sources
Helixi82 – 10019Combined sources
Helixi109 – 12113Combined sources
Helixi123 – 13513Combined sources
Beta strandi139 – 1424Combined sources
Helixi148 – 16316Combined sources
Turni165 – 1706Combined sources
Helixi172 – 18211Combined sources
Helixi185 – 1939Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00670000097856.
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

        10         20         30         40         50
MPNYKLTYFN MRGRAEIIRY IFAYLDIQYE DHRIEQADWP EIKSTLPFGK
60 70 80 90 100
IPILEVDGLT LHQSLAIARY LTKNTDLAGN TEMEQCHVDA IVDTLDDFMS
110 120 130 140 150
CFPWAEKKQD VKEQMFNELL TYNAPHLMQD LDTYLGGREW LIGNSVTWAD
160 170 180 190
FYWEICSTTL LVFKPDLLDN HPRLVTLRKK VQAIPAVANW IKRRPQTKL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00670000097856.
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.
SABIO-RK O60760.

Miscellaneous databases

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

Gene expression databases

Bgeei O60760.
ExpressionAtlasi O60760. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 141 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

Dasty 3