Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Hematopoietic prostaglandin D synthase

Gene

HPGDS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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
  1. Vmax=8.6 µmol/min/mg enzyme with 1-bromo-2,4-dinitrobenzene as substrate3 Publications
  2. Vmax=5.1 µmol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as substrate3 Publications
  3. Vmax=44.3 µmol/min/mg enzyme with 1-fluoro-2,4-dinitrobenzene as substrate3 Publications
  4. Vmax=10.7 µmol/min/mg enzyme with 1-iodo-2,4-dinitrobenzene as substrate3 Publications
  5. Vmax=6.8 µmol/min/mg enzyme with allyl isothiocyanate as substrate3 Publications
  6. Vmax=6.3 µmol/min/mg enzyme with benzyl isothiocyanate as substrate3 Publications
  7. 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

  • calcium ion binding Source: UniProtKB
  • glutathione transferase activity Source: UniProtKB-EC
  • magnesium ion binding Source: UniProtKB
  • prostaglandin-D synthase activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • arachidonic acid metabolic process Source: Reactome
  • cyclooxygenase pathway Source: Reactome
  • glutathione derivative biosynthetic process Source: Reactome
  • locomotory behavior Source: ProtInc
  • prostaglandin metabolic process Source: UniProtKB
  • signal transduction Source: ProtInc
  • small molecule metabolic process Source: Reactome
  • 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.
BRENDAi2.5.1.18. 2681.
5.3.99.2. 2681.
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 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:17890. HPGDS.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: ProtInc
  • 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.

Chemistry

DrugBankiDB00143. Glutathione.

Polymorphism and mutation databases

BioMutaiHPGDS.

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.
GenevisibleiO60760. HS.

Organism-specific databases

HPAiCAB020805.
HPA024035.

Interactioni

Subunit structurei

Homodimer.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABHD17AQ96GS63EBI-10187349,EBI-2870273
ARRDC3Q96B673EBI-10187349,EBI-2875665
MFI2P08582-23EBI-10187349,EBI-10195914

Protein-protein interaction databases

BioGridi118128. 4 interactions.
IntActiO60760. 3 interactions.
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.
CCDSiCCDS3640.1.
RefSeqiNP_055300.1. NM_014485.2.
UniGeneiHs.128433.

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...

Protein-protein interaction databases

BioGridi118128. 4 interactions.
IntActiO60760. 3 interactions.
STRINGi9606.ENSP00000295256.

Chemistry

BindingDBiO60760.
ChEMBLiCHEMBL5879.
DrugBankiDB00143. Glutathione.
GuidetoPHARMACOLOGYi1381.

PTM databases

PhosphoSiteiO60760.

Polymorphism and mutation databases

BioMutaiHPGDS.

Proteomic databases

PaxDbiO60760.
PRIDEiO60760.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi27306.
GeneCardsiGC04M095219.
HGNCiHGNC:17890. HPGDS.
HPAiCAB020805.
HPA024035.
MIMi602598. gene.
neXtProtiNX_O60760.
PharmGKBiPA165664133.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG122057.
GeneTreeiENSGT00670000097856.
HOGENOMiHOG000115733.
HOVERGENiHBG105321.
InParanoidiO60760.
KOiK01830.
OMAiMSCFPWA.
OrthoDBiEOG78WKT1.
PhylomeDBiO60760.
TreeFamiTF105321.

Enzyme and pathway databases

BioCyciMetaCyc:HS08788-MONOMER.
BRENDAi2.5.1.18. 2681.
5.3.99.2. 2681.
ReactomeiREACT_150149. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
REACT_6926. Glutathione conjugation.
SABIO-RKO60760.

Miscellaneous databases

EvolutionaryTraceiO60760.
GeneWikiiPGDS.
GenomeRNAii27306.
NextBioi50305.
PROiO60760.
SOURCEiSearch...

Gene expression databases

BgeeiO60760.
GenevisibleiO60760. HS.

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]
ProtoNetiSearch...

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: June 24, 2015
This is version 147 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.