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Q05769

- PGH2_MOUSE

UniProt

Q05769 - PGH2_MOUSE

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Protein
Prostaglandin G/H synthase 2
Gene
Ptgs2, Cox-2, Cox2, Pghs-b, Tis10
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Converts arachidonate to prostaglandin H2 (PGH2), a committed step in prostanoid synthesis. Constitutively expressed in some tissues in physiological conditions, such as the endothelium, kidney and brain, and in pathological conditions, such as in cancer. PTGS2 is responsible for production of inflammatory prostaglandins. Up-regulation of PTGS2 is also associated with increased cell adhesion, phenotypic changes, resistance to apoptosis and tumor angiogenesis. In cancer cells, PTGS2 is a key step in the production of prostaglandin E2 (PGE2), which plays important roles in modulating motility, proliferation and resistance to apoptosis.5 Publications

Catalytic activityi

Arachidonate + AH2 + 2 O2 = prostaglandin H2 + A + H2O.4 Publications

Cofactori

Binds 1 heme B (iron-protoporphyrin IX) group per subunit.3 Publications

Enzyme regulationi

Inhibited by the nonsteroidal anti-inflammatory drugs aspirin, naproxen, diclofenac, meclofenamic acid, indomethacin and their analogs.2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei106 – 1061Substrate
Active sitei193 – 1931Proton acceptor1 Publication
Binding sitei341 – 3411Substrate
Active sitei371 – 3711For cyclooxygenase activity1 Publication
Binding sitei371 – 3711Substrate
Metal bindingi374 – 3741Iron (heme axial ligand)
Sitei516 – 5161Aspirin-acetylated serine
Sitei592 – 5921Not glycosylated

GO - Molecular functioni

  1. heme binding Source: UniProtKB
  2. lipid binding Source: Ensembl
  3. metal ion binding Source: UniProtKB-KW
  4. oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Source: Ensembl
  5. peroxidase activity Source: UniProtKB-KW
  6. prostaglandin-endoperoxide synthase activity Source: UniProtKB
  7. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. anagen Source: MGI
  2. angiogenesis Source: Ensembl
  3. bone mineralization Source: MGI
  4. brown fat cell differentiation Source: BHF-UCL
  5. cellular response to ATP Source: Ensembl
  6. cellular response to UV Source: Ensembl
  7. cellular response to hypoxia Source: Ensembl
  8. cellular response to mechanical stimulus Source: Ensembl
  9. cyclooxygenase pathway Source: UniProtKB
  10. decidualization Source: Ensembl
  11. embryo implantation Source: Ensembl
  12. inflammatory response Source: Ensembl
  13. keratinocyte differentiation Source: UniProtKB
  14. learning Source: Ensembl
  15. maintenance of blood-brain barrier Source: Ensembl
  16. memory Source: Ensembl
  17. negative regulation of calcium ion transport Source: Ensembl
  18. negative regulation of cell cycle Source: Ensembl
  19. negative regulation of cell proliferation Source: Ensembl
  20. negative regulation of smooth muscle contraction Source: Ensembl
  21. negative regulation of synaptic transmission, dopaminergic Source: Ensembl
  22. ovulation Source: Ensembl
  23. positive regulation of NF-kappaB import into nucleus Source: Ensembl
  24. positive regulation of apoptotic process Source: Ensembl
  25. positive regulation of brown fat cell differentiation Source: BHF-UCL
  26. positive regulation of cell migration involved in sprouting angiogenesis Source: Ensembl
  27. positive regulation of fever generation Source: BHF-UCL
  28. positive regulation of fibroblast growth factor production Source: Ensembl
  29. positive regulation of nitric oxide biosynthetic process Source: Ensembl
  30. positive regulation of platelet-derived growth factor production Source: Ensembl
  31. positive regulation of smooth muscle cell proliferation Source: Ensembl
  32. positive regulation of smooth muscle contraction Source: Ensembl
  33. positive regulation of synaptic plasticity Source: Ensembl
  34. positive regulation of synaptic transmission, glutamatergic Source: Ensembl
  35. positive regulation of transforming growth factor beta production Source: Ensembl
  36. positive regulation of vasoconstriction Source: Ensembl
  37. positive regulation vascular endothelial growth factor production Source: Ensembl
  38. prostaglandin biosynthetic process Source: UniProtKB
  39. regulation of blood pressure Source: MGI
  40. regulation of cell proliferation Source: MGI
  41. response to drug Source: Ensembl
  42. response to estradiol Source: Ensembl
  43. response to fatty acid Source: Ensembl
  44. response to fructose Source: Ensembl
  45. response to glucocorticoid Source: Ensembl
  46. response to lipopolysaccharide Source: Ensembl
  47. response to lithium ion Source: Ensembl
  48. response to manganese ion Source: Ensembl
  49. response to oxidative stress Source: InterPro
  50. response to tumor necrosis factor Source: Ensembl
  51. response to vitamin D Source: Ensembl
  52. sensory perception of pain Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase, Peroxidase

Keywords - Biological processi

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

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_188623. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
REACT_196559. Synthesis of 15-eicosatetraenoic acid derivatives.
UniPathwayiUPA00662.

Protein family/group databases

PeroxiBasei3360. MmPGHS02.

Names & Taxonomyi

Protein namesi
Recommended name:
Prostaglandin G/H synthase 2 (EC:1.14.99.1)
Alternative name(s):
Cyclooxygenase-2
Short name:
COX-2
Glucocorticoid-regulated inflammatory cyclooxygenase
Gripghs
Macrophage activation-associated marker protein P71/73
PES-2
PHS II
Prostaglandin H2 synthase 2
Short name:
PGH synthase 2
Short name:
PGHS-2
Prostaglandin-endoperoxide synthase 2
TIS10 protein
Gene namesi
Name:Ptgs2
Synonyms:Cox-2, Cox2, Pghs-b, Tis10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:97798. Ptgs2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. neuron projection Source: MGI
  4. protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Disruption phenotypei

Mutant mice exhibit defects in colonic mucosal wound repair.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi517 – 5171L → A, F, P or T: Slightly reduced activity. 1 Publication
Mutagenesisi580 – 5801N → A: Loss of glycosylation site. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717
Add
BLAST
Chaini18 – 604587Prostaglandin G/H synthase 2
PRO_0000023876Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi21 ↔ 323 Publications
Disulfide bondi22 ↔ 1453 Publications
Disulfide bondi26 ↔ 423 Publications
Disulfide bondi44 ↔ 543 Publications
Glycosylationi53 – 531N-linked (GlcNAc...)7 Publications
CAR_000222
Glycosylationi130 – 1301N-linked (GlcNAc...)7 Publications
CAR_000223
Glycosylationi396 – 3961N-linked (GlcNAc...)7 Publications
CAR_000224
Modified residuei526 – 5261S-nitrosocysteine By similarity
Disulfide bondi555 ↔ 5613 Publications
Glycosylationi580 – 5801N-linked (GlcNAc...)2 Publications
CAR_000225

Post-translational modificationi

S-nitrosylation by NOS2 (iNOS) activates enzyme activity. S-nitrosylation may take place on different Cys residues in addition to Cys-526 By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, S-nitrosylation

Proteomic databases

PaxDbiQ05769.
PRIDEiQ05769.

PTM databases

PhosphoSiteiQ05769.
UniCarbKBiQ05769.

Expressioni

Tissue specificityi

Following colon injury, expressed in the wound bed mesenchyme during the first phase of repair, probably by colonic mesenchymal stem cells (at protein level).1 Publication

Developmental stagei

During colonic wound repair, highly up-regulated (more than 1600-fold) in the mesenchyme of the wound bed 2 days after injury as compared to uninjured mucosa. Further increase in expression is observed at day 4 following injury (close to 2200-fold). Down-regulated at day 6 (only 93-fold increase as compared to uninjured mucosa).1 Publication

Inductioni

By cytokines and mitogens.2 Publications

Gene expression databases

BgeeiQ05769.
CleanExiMM_PTGS2.
GenevestigatoriQ05769.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi202463. 5 interactions.
DIPiDIP-31082N.
IntActiQ05769. 1 interaction.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni20 – 234
Helixi27 – 293
Beta strandi31 – 366
Beta strandi39 – 435
Beta strandi47 – 504
Turni51 – 544
Helixi59 – 679
Helixi71 – 788
Helixi82 – 898
Helixi92 – 10716
Beta strandi117 – 1193
Beta strandi120 – 1223
Helixi125 – 1295
Beta strandi131 – 1333
Beta strandi135 – 1384
Beta strandi145 – 1473
Beta strandi150 – 1534
Helixi160 – 1678
Helixi182 – 19211
Turni193 – 1953
Turni200 – 2023
Beta strandi206 – 2083
Beta strandi213 – 2153
Helixi217 – 2204
Helixi224 – 2307
Beta strandi241 – 2433
Beta strandi246 – 2483
Helixi252 – 2554
Beta strandi263 – 2653
Helixi267 – 2693
Turni276 – 2794
Helixi282 – 30524
Helixi311 – 33222
Helixi334 – 3396
Helixi349 – 3524
Helixi365 – 3706
Helixi374 – 3763
Beta strandi379 – 3835
Beta strandi386 – 3883
Helixi390 – 3934
Helixi398 – 41417
Beta strandi420 – 4245
Helixi428 – 4303
Helixi431 – 44313
Helixi449 – 4557
Helixi464 – 4685
Beta strandi469 – 4713
Helixi472 – 48110
Helixi484 – 4863
Helixi489 – 4957
Beta strandi503 – 5053
Helixi506 – 52116
Helixi524 – 5263
Turni528 – 5303
Helixi533 – 5364
Helixi539 – 5468
Helixi550 – 5578
Beta strandi558 – 5603

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CVUX-ray2.40A/B18-569[»]
1CX2X-ray3.00A/B/C/D18-604[»]
1DCXmodel-A/B18-569[»]
1DD0model-A/B18-569[»]
1DDXX-ray3.00A/B/C/D18-569[»]
1PXXX-ray2.90A/B/C/D1-604[»]
3HS5X-ray2.10A/B20-604[»]
3HS6X-ray2.40A/B20-604[»]
3HS7X-ray2.65A/B20-604[»]
3KRKX-ray2.40A/B20-604[»]
3LN0X-ray2.20A/B/C/D18-604[»]
3LN1X-ray2.40A/B/C/D18-604[»]
3MDLX-ray2.20A/B20-599[»]
3MQEX-ray2.80A/B/C/D18-604[»]
3NT1X-ray1.73A/B18-604[»]
3NTBX-ray2.27A/B/C/D18-604[»]
3NTGX-ray2.19A/B/C/D18-569[»]
3OLTX-ray2.45A/B20-604[»]
3OLUX-ray2.35A/B20-604[»]
3PGHX-ray2.50A/B/C/D18-604[»]
3Q7DX-ray2.40A/B18-604[»]
3QH0X-ray2.10A/B1-604[»]
3QMOX-ray3.00A/B1-604[»]
3RR3X-ray2.84A/B/C/D18-577[»]
3TZIX-ray2.15A/B20-604[»]
4COXX-ray2.90A/B/C/D18-604[»]
4E1GX-ray2.10A/B1-604[»]
4FM5X-ray2.81A/B/C/D1-604[»]
4M10X-ray2.01A/B/C/D18-604[»]
4M11X-ray2.45A/B/C/D18-569[»]
4OTYX-ray2.35A/B18-604[»]
5COXX-ray3.00A/B/C/D18-604[»]
6COXX-ray2.80A/B18-604[»]
ProteinModelPortaliQ05769.
SMRiQ05769. Positions 18-569.

Miscellaneous databases

EvolutionaryTraceiQ05769.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 5538EGF-like
Add
BLAST

Sequence similaritiesi

Contains 1 EGF-like domain.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG39991.
GeneTreeiENSGT00390000010743.
HOGENOMiHOG000013149.
HOVERGENiHBG000366.
InParanoidiQ05769.
KOiK11987.
OMAiICNNVKG.
OrthoDBiEOG7RFTHC.
PhylomeDBiQ05769.
TreeFamiTF329675.

Family and domain databases

Gene3Di1.10.640.10. 1 hit.
InterProiIPR029576. COX-2.
IPR000742. EG-like_dom.
IPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
[Graphical view]
PANTHERiPTHR11903:SF8. PTHR11903:SF8. 1 hit.
PfamiPF03098. An_peroxidase. 2 hits.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SMARTiSM00181. EGF. 1 hit.
[Graphical view]
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS50026. EGF_3. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q05769-1 [UniParc]FASTAAdd to Basket

« Hide

MLFRAVLLCA ALGLSQAANP CCSNPCQNRG ECMSTGFDQY KCDCTRTGFY    50
GENCTTPEFL TRIKLLLKPT PNTVHYILTH FKGVWNIVNN IPFLRSLIMK 100
YVLTSRSYLI DSPPTYNVHY GYKSWEAFSN LSYYTRALPP VADDCPTPMG 150
VKGNKELPDS KEVLEKVLLR REFIPDPQGS NMMFAFFAQH FTHQFFKTDH 200
KRGPGFTRGL GHGVDLNHIY GETLDRQHKL RLFKDGKLKY QVIGGEVYPP 250
TVKDTQVEMI YPPHIPENLQ FAVGQEVFGL VPGLMMYATI WLREHNRVCD 300
ILKQEHPEWG DEQLFQTSRL ILIGETIKIV IEDYVQHLSG YHFKLKFDPE 350
LLFNQQFQYQ NRIASEFNTL YHWHPLLPDT FNIEDQEYSF KQFLYNNSIL 400
LEHGLTQFVE SFTRQIAGRV AGGRNVPIAV QAVAKASIDQ SREMKYQSLN 450
EYRKRFSLKP YTSFEELTGE KEMAAELKAL YSDIDVMELY PALLVEKPRP 500
DAIFGETMVE LGAPFSLKGL MGNPICSPQY WKPSTFGGEV GFKIINTASI 550
QSLICNNVKG CPFTSFNVQD PQPTKTATIN ASASHSRLDD INPTVLIKRR 600
STEL 604
Length:604
Mass (Da):69,013
Last modified:June 1, 1994 - v1
Checksum:iDFE1658295C92064
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti98 – 981I → T in AAA39924. 1 Publication
Sequence conflicti142 – 1421A → R in AAA39918. 1 Publication
Sequence conflicti301 – 3011I → L no nucleotide entry 1 Publication
Sequence conflicti585 – 5851H → R in AAA39918. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64291 mRNA. Translation: AAA39924.1.
M94967 mRNA. Translation: AAA39918.1.
M82866
, M82862, M82863, M82864, M82865 Genomic DNA. Translation: AAA40448.1.
M88242 mRNA. Translation: AAA37740.1.
AK049923 mRNA. Translation: BAC33986.1.
AK144956 mRNA. Translation: BAE26154.1.
AK166221 mRNA. Translation: BAE38639.1.
AK172161 mRNA. Translation: BAE42855.1.
CH466520 Genomic DNA. Translation: EDL39487.1.
CCDSiCCDS15353.1.
PIRiA49010.
RefSeqiNP_035328.2. NM_011198.3.
UniGeneiMm.292547.

Genome annotation databases

EnsembliENSMUST00000035065; ENSMUSP00000035065; ENSMUSG00000032487.
GeneIDi19225.
KEGGimmu:19225.
UCSCiuc007cxv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64291 mRNA. Translation: AAA39924.1 .
M94967 mRNA. Translation: AAA39918.1 .
M82866
, M82862 , M82863 , M82864 , M82865 Genomic DNA. Translation: AAA40448.1 .
M88242 mRNA. Translation: AAA37740.1 .
AK049923 mRNA. Translation: BAC33986.1 .
AK144956 mRNA. Translation: BAE26154.1 .
AK166221 mRNA. Translation: BAE38639.1 .
AK172161 mRNA. Translation: BAE42855.1 .
CH466520 Genomic DNA. Translation: EDL39487.1 .
CCDSi CCDS15353.1.
PIRi A49010.
RefSeqi NP_035328.2. NM_011198.3.
UniGenei Mm.292547.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CVU X-ray 2.40 A/B 18-569 [» ]
1CX2 X-ray 3.00 A/B/C/D 18-604 [» ]
1DCX model - A/B 18-569 [» ]
1DD0 model - A/B 18-569 [» ]
1DDX X-ray 3.00 A/B/C/D 18-569 [» ]
1PXX X-ray 2.90 A/B/C/D 1-604 [» ]
3HS5 X-ray 2.10 A/B 20-604 [» ]
3HS6 X-ray 2.40 A/B 20-604 [» ]
3HS7 X-ray 2.65 A/B 20-604 [» ]
3KRK X-ray 2.40 A/B 20-604 [» ]
3LN0 X-ray 2.20 A/B/C/D 18-604 [» ]
3LN1 X-ray 2.40 A/B/C/D 18-604 [» ]
3MDL X-ray 2.20 A/B 20-599 [» ]
3MQE X-ray 2.80 A/B/C/D 18-604 [» ]
3NT1 X-ray 1.73 A/B 18-604 [» ]
3NTB X-ray 2.27 A/B/C/D 18-604 [» ]
3NTG X-ray 2.19 A/B/C/D 18-569 [» ]
3OLT X-ray 2.45 A/B 20-604 [» ]
3OLU X-ray 2.35 A/B 20-604 [» ]
3PGH X-ray 2.50 A/B/C/D 18-604 [» ]
3Q7D X-ray 2.40 A/B 18-604 [» ]
3QH0 X-ray 2.10 A/B 1-604 [» ]
3QMO X-ray 3.00 A/B 1-604 [» ]
3RR3 X-ray 2.84 A/B/C/D 18-577 [» ]
3TZI X-ray 2.15 A/B 20-604 [» ]
4COX X-ray 2.90 A/B/C/D 18-604 [» ]
4E1G X-ray 2.10 A/B 1-604 [» ]
4FM5 X-ray 2.81 A/B/C/D 1-604 [» ]
4M10 X-ray 2.01 A/B/C/D 18-604 [» ]
4M11 X-ray 2.45 A/B/C/D 18-569 [» ]
4OTY X-ray 2.35 A/B 18-604 [» ]
5COX X-ray 3.00 A/B/C/D 18-604 [» ]
6COX X-ray 2.80 A/B 18-604 [» ]
ProteinModelPortali Q05769.
SMRi Q05769. Positions 18-569.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202463. 5 interactions.
DIPi DIP-31082N.
IntActi Q05769. 1 interaction.

Chemistry

BindingDBi Q05769.
ChEMBLi CHEMBL4321.

Protein family/group databases

PeroxiBasei 3360. MmPGHS02.

PTM databases

PhosphoSitei Q05769.
UniCarbKBi Q05769.

Proteomic databases

PaxDbi Q05769.
PRIDEi Q05769.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000035065 ; ENSMUSP00000035065 ; ENSMUSG00000032487 .
GeneIDi 19225.
KEGGi mmu:19225.
UCSCi uc007cxv.1. mouse.

Organism-specific databases

CTDi 5743.
MGIi MGI:97798. Ptgs2.

Phylogenomic databases

eggNOGi NOG39991.
GeneTreei ENSGT00390000010743.
HOGENOMi HOG000013149.
HOVERGENi HBG000366.
InParanoidi Q05769.
KOi K11987.
OMAi ICNNVKG.
OrthoDBi EOG7RFTHC.
PhylomeDBi Q05769.
TreeFami TF329675.

Enzyme and pathway databases

UniPathwayi UPA00662 .
Reactomei REACT_188623. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
REACT_196559. Synthesis of 15-eicosatetraenoic acid derivatives.

Miscellaneous databases

EvolutionaryTracei Q05769.
NextBioi 296012.
PROi Q05769.
SOURCEi Search...

Gene expression databases

Bgeei Q05769.
CleanExi MM_PTGS2.
Genevestigatori Q05769.

Family and domain databases

Gene3Di 1.10.640.10. 1 hit.
InterProi IPR029576. COX-2.
IPR000742. EG-like_dom.
IPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
[Graphical view ]
PANTHERi PTHR11903:SF8. PTHR11903:SF8. 1 hit.
Pfami PF03098. An_peroxidase. 2 hits.
[Graphical view ]
PRINTSi PR00457. ANPEROXIDASE.
SMARTi SM00181. EGF. 1 hit.
[Graphical view ]
SUPFAMi SSF48113. SSF48113. 1 hit.
PROSITEi PS50026. EGF_3. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "TIS10, a phorbol ester tumor promoter-inducible mRNA from Swiss 3T3 cells, encodes a novel prostaglandin synthase/cyclooxygenase homologue."
    Kujubu D.A., Fletcher B.S., Varnum B.C., Lim R.W., Herschman H.R.
    J. Biol. Chem. 266:12866-12872(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Swiss.
  2. "Structure of the mitogen-inducible TIS10 gene and demonstration that the TIS10-encoded protein is a functional prostaglandin G/H synthase."
    Fletcher B.S., Kujubu D.A., Perrin D.M., Herschman H.R.
    J. Biol. Chem. 267:4338-4344(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Identification of an immediate early gene, pghs-B, whose protein product has prostaglandin synthase/cyclooxygenase activity."
    Ryseck R.-P., Raynoschek C., Macdonald-Bravo H., Dorfman K., Mattei M.-G., Bravo R.
    Cell Growth Differ. 3:443-450(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "cDNA cloning and functional activity of a glucocorticoid-regulated inflammatory cyclooxygenase."
    O'Banion M.K., Winn V.D., Young D.A.
    Proc. Natl. Acad. Sci. U.S.A. 89:4888-4892(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Hippocampus, Mammary gland and Spleen.
  6. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "A serum- and glucocorticoid-regulated 4-kilobase mRNA encodes a cyclooxygenase-related protein."
    O'Banion M.K., Sadowski H.B., Winn V., Young D.A.
    J. Biol. Chem. 266:23261-23267(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 281-360.
  8. "The mouse macrophage activation-associated marker protein, p71/73, is an inducible prostaglandin endoperoxide synthase (cyclooxygenase)."
    Phillips T.A., Kujubu D.A., Mackay R.J., Herschman H.R., Russell S.W., Pace J.L.
    J. Leukoc. Biol. 53:411-419(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
  9. "N-glycosylation of prostaglandin endoperoxide synthases-1 and -2 and their orientations in the endoplasmic reticulum."
    Otto J.C., Dewitt D.L., Smith W.L.
    J. Biol. Chem. 268:18234-18242(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-53; ASN-130; ASN-396 AND ASN-580, ABSENCE OF GLYCOSYLATION AT ASN-592.
  10. "Igf2bp1 is required for full induction of Ptgs2 mRNA in colonic mesenchymal stem cells in mice."
    Manieri N.A., Drylewicz M.R., Miyoshi H., Stappenbeck T.S.
    Gastroenterology 143:110-121(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INTESTINAL WOUND REPAIR, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
  11. "Cyclooxygenases: structural, cellular, and molecular biology."
    Smith W.L., DeWitt D.L., Garavito R.M.
    Annu. Rev. Biochem. 69:145-182(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION; TISSUE SPECIFICITY AND INHIBITION BY NSAIDS.
  12. "Aspirin, cyclooxygenase inhibition and colorectal cancer."
    Sostres C., Gargallo C.J., Lanas A.
    World J. Gastrointest. Pharmacol. Ther. 5:40-49(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION; INHIBITION BY ASPIRIN AND INVOLVEMENT IN COLORECTAL CANCER.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH (S)-FLURBIPROFEN; INDOMETHACIN; HEME AND 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE, COFACTOR, GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 18-569 IN COMPLEX WITH ARACHIDONIC ACID, GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396.
  15. "A novel mechanism of cyclooxygenase-2 inhibition involving interactions with Ser-530 and Tyr-385."
    Rowlinson S.W., Kiefer J.R., Prusakiewicz J.J., Pawlitz J.L., Kozak K.R., Kalgutkar A.S., Stallings W.C., Kurumbail R.G., Marnett L.J.
    J. Biol. Chem. 278:45763-45769(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH HEME AND DICLOFENAC, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, DISULFIDE BONDS, ENZYME REGULATION, GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396.
  16. "Structural basis of fatty acid substrate binding to cyclooxygenase-2."
    Vecchio A.J., Simmons D.M., Malkowski M.G.
    J. Biol. Chem. 285:22152-22163(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 20-604 IN COMPLEX WITH HEME; ACRYLIC ACID; ARACHIDONIC ACID AND DOCOSAHEXAENOIC ACID, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, COFACTOR, FUNCTION, DISULFIDE BONDS, MUTAGENESIS OF LEU-517 AND ASN-580, GLYCOSYLATION AT ASN-53; ASN-130; ASN-396 AND ASN-580.
  17. "Molecular basis for cyclooxygenase inhibition by the non-steroidal anti-inflammatory drug naproxen."
    Duggan K.C., Walters M.J., Musee J., Harp J.M., Kiefer J.R., Oates J.A., Marnett L.J.
    J. Biol. Chem. 285:34950-34959(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 18-604 IN COMPLEXES WITH HEME AND NAPROXEN ANALOGS, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, DISULFIDE BONDS, GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396.
  18. "The structural basis of endocannabinoid oxygenation by cyclooxygenase-2."
    Vecchio A.J., Malkowski M.G.
    J. Biol. Chem. 286:20736-20745(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 20-599 IN COMPLEX WITH HEME; ACRYLIC ACID AND ARACHIDONIC ACID, FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396.

Entry informationi

Entry nameiPGH2_MOUSE
AccessioniPrimary (citable) accession number: Q05769
Secondary accession number(s): Q543K3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: September 3, 2014
This is version 159 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The conversion of arachidonate to prostaglandin H2 is a 2 step reaction: a cyclooxygenase (COX) reaction which converts arachidonate to prostaglandin G2 (PGG2) and a peroxidase reaction in which PGG2 is reduced to prostaglandin H2 (PGH2). The cyclooxygenase reaction occurs in a hydrophobic channel in the core of the enzyme. The peroxidase reaction occurs at a heme-containing active site located near the protein surface. The nonsteroidal anti-inflammatory drugs (NSAIDs) binding site corresponds to the cyclooxygenase active site.
Conversion of arachidonate to prostaglandin H2 is mediated by 2 different isozymes: the constitutive PTGS1 and the inducible PTGS2. PGHS1 is expressed constitutively and generally produces prostanoids acutely in response to hormonal stimuli to fine-tune physiological processes requiring instantaneous, continuous regulation (e.g. hemostasis). PGHS2 is inducible and typically produces prostanoids that mediate responses to physiological stresses such as infection and inflammation.
PTGS1 and PTGS2 are the targets of nonsteroidal anti-inflammatory drugs (NSAIDs) including aspirin and ibuprofen. Aspirin is able to produce an irreversible inactivation of the enzyme through a serine acetylation. Inhibition of the PGHSs with NSAIDs acutely reduces inflammation, pain, and fever, and long-term use of these drugs reduces fatal thrombotic events, as well as the development of colon cancer and Alzheimer's disease. PTGS2 is the principal isozyme responsible for production of inflammatory prostaglandins. New generation PTGSs inhibitors strive to be selective for PTGS2, to avoid side effects such as gastrointestinal complications and ulceration.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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

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