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Protein

Prostaglandin G/H synthase 2

Gene

PTGS2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.1 Publication

Catalytic activityi

Arachidonate + AH2 + 2 O2 = prostaglandin H2 + A + H2O.1 Publication

Cofactori

heme bBy similarityNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.By similarity

Kineticsi

  1. KM=16.2 µM for arachidonate (in absence of sodium nitroprusside NO donor)1 Publication
  2. KM=17.0 µM for arachidonate (in presence of sodium nitroprusside NO donor)1 Publication
  1. Vmax=81.3 nmol/min/mg enzyme (in absence of sodium nitroprusside NO donor)1 Publication
  2. Vmax=132 nmol/min/mg enzyme (in absence of sodium nitroprusside NO donor)1 Publication

Pathwayi: prostaglandin biosynthesis

This protein is involved in the pathway prostaglandin biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway prostaglandin biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei106 – 1061SubstrateBy similarity
Active sitei193 – 1931Proton acceptorPROSITE-ProRule annotation
Binding sitei341 – 3411SubstrateBy similarity
Active sitei371 – 3711For cyclooxygenase activityBy similarity
Binding sitei371 – 3711SubstrateBy similarity
Metal bindingi374 – 3741Iron (heme axial ligand)PROSITE-ProRule annotation
Sitei516 – 5161Aspirin-acetylated serineBy similarity

GO - Molecular functioni

  • arachidonate 15-lipoxygenase activity Source: Reactome
  • enzyme binding Source: UniProtKB
  • heme binding Source: UniProtKB
  • lipid binding Source: Ensembl
  • metal ion binding Source: UniProtKB-KW
  • peroxidase activity Source: UniProtKB
  • prostaglandin-endoperoxide synthase activity Source: UniProtKB

GO - Biological processi

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

BioCyciMetaCyc:HS01115-MONOMER.
BRENDAi1.14.99.1. 2681.
ReactomeiR-HSA-197264. Nicotinamide salvaging.
R-HSA-2142770. Synthesis of 15-eicosatetraenoic acid derivatives.
R-HSA-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
SABIO-RKP35354.
SIGNORiP35354.
UniPathwayiUPA00662.

Protein family/group databases

PeroxiBasei3321. HsPGHS02.

Chemistry

SwissLipidsiSLP:000000830.

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
PHS II
Prostaglandin H2 synthase 2
Short name:
PGH synthase 2
Short name:
PGHS-2
Prostaglandin-endoperoxide synthase 2
Gene namesi
Name:PTGS2
Synonyms:COX2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9605. PTGS2.

Subcellular locationi

GO - Cellular componenti

  • caveola Source: Ensembl
  • cytoplasm Source: UniProtKB
  • endoplasmic reticulum Source: ParkinsonsUK-UCL
  • endoplasmic reticulum lumen Source: ParkinsonsUK-UCL
  • endoplasmic reticulum membrane Source: Reactome
  • neuron projection Source: MGI
  • nucleus Source: UniProtKB
  • protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi526 – 5261C → S: Prevents activation by nitric oxid (NO). 1 Publication
Mutagenesisi555 – 5551C → S: Abolishes enzyme activity. 1 Publication
Mutagenesisi561 – 5611C → S: Does not affect activation by nitric oxid (NO). 1 Publication

Organism-specific databases

PharmGKBiPA293.

Chemistry

ChEMBLiCHEMBL2094253.
DrugBankiDB00316. Acetaminophen.
DB00945. Acetylsalicylic acid.
DB00041. Aldesleukin.
DB00233. Aminosalicylic Acid.
DB01435. Antipyrine.
DB01419. Antrafenine.
DB01014. Balsalazide.
DB00963. Bromfenac.
DB00887. Bumetanide.
DB06774. Capsaicin.
DB00821. Carprofen.
DB00482. Celecoxib.
DB00856. Chlorphenesin.
DB00515. Cisplatin.
DB00720. Clodronate.
DB00250. Dapsone.
DB00035. Desmopressin.
DB00586. Diclofenac.
DB00861. Diflunisal.
DB00154. Dihomo-gamma-linolenic acid.
DB01395. Drospirenone.
DB00005. Etanercept.
DB00749. Etodolac.
DB00773. Etoposide.
DB01628. Etoricoxib.
DB00573. Fenoprofen.
DB00712. Flurbiprofen.
DB01404. Ginseng.
DB01050. Ibuprofen.
DB00159. Icosapent.
DB00328. Indomethacin.
DB01009. Ketoprofen.
DB00465. Ketorolac.
DB00480. Lenalidomide.
DB06725. Lornoxicam.
DB01283. Lumiracoxib.
DB01397. Magnesium salicylate.
DB00939. Meclofenamic acid.
DB00784. Mefenamic acid.
DB00814. Meloxicam.
DB00244. Mesalazine.
DB00461. Nabumetone.
DB00788. Naproxen.
DB06802. Nepafenac.
DB04552. Niflumic Acid.
DB04743. Nimesulide.
DB06804. Nonoxynol-9.
DB00991. Oxaprozin.
DB08439. Parecoxib.
DB00812. Phenylbutazone.
DB00554. Piroxicam.
DB08910. Pomalidomide.
DB00884. Risedronate.
DB00936. Salicylic acid.
DB01399. Salsalate.
DB00795. Sulfasalazine.
DB00605. Sulindac.
DB00870. Suprofen.
DB08819. Tafluprost.
DB00469. Tenoxicam.
DB00360. Tetrahydrobiopterin.
DB01041. Thalidomide.
DB01600. Tiaprofenic acid.
DB00500. Tolmetin.
DB00620. Triamcinolone.
DB01401. Trisalicylate-choline.
GuidetoPHARMACOLOGYi1376.

Polymorphism and mutation databases

BioMutaiPTGS2.
DMDMi3915797.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Chaini18 – 604587Prostaglandin G/H synthase 2PRO_0000023875Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi21 ↔ 32By similarity
Disulfide bondi22 ↔ 145By similarity
Disulfide bondi26 ↔ 42By similarity
Disulfide bondi44 ↔ 54By similarity
Glycosylationi53 – 531N-linked (GlcNAc...)Sequence analysis
Glycosylationi130 – 1301N-linked (GlcNAc...)Sequence analysis
Glycosylationi396 – 3961N-linked (GlcNAc...)Sequence analysis
Modified residuei526 – 5261S-nitrosocysteine1 Publication
Disulfide bondi555 ↔ 561By similarity
Glycosylationi580 – 5801N-linked (GlcNAc...)1 Publication

Post-translational modificationi

S-nitrosylation by NOS2 (iNOS) activates enzyme activity. S-nitrosylation may take place on different Cys residues in addition to Cys-526.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, S-nitrosylation

Proteomic databases

EPDiP35354.
MaxQBiP35354.
PaxDbiP35354.
PeptideAtlasiP35354.
PRIDEiP35354.

PTM databases

iPTMnetiP35354.
PhosphoSiteiP35354.

Expressioni

Inductioni

By cytokines and mitogens.

Gene expression databases

BgeeiENSG00000073756.
CleanExiHS_PTGS2.
ExpressionAtlasiP35354. baseline and differential.
GenevisibleiP35354. HS.

Organism-specific databases

HPAiCAB000113.
HPA001335.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

  • enzyme binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111715. 32 interactions.
DIPiDIP-28131N.
IntActiP35354. 2 interactions.
MINTiMINT-203337.
STRINGi9606.ENSP00000356438.

Chemistry

BindingDBiP35354.

Structurei

Secondary structure

1
604
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni20 – 234Combined sources
Beta strandi31 – 355Combined sources
Turni36 – 383Combined sources
Beta strandi39 – 435Combined sources
Beta strandi47 – 504Combined sources
Turni51 – 544Combined sources
Helixi59 – 668Combined sources
Helixi71 – 788Combined sources
Helixi82 – 898Combined sources
Helixi92 – 10716Combined sources
Beta strandi120 – 1223Combined sources
Helixi125 – 1295Combined sources
Beta strandi135 – 1384Combined sources
Beta strandi150 – 1534Combined sources
Helixi160 – 1678Combined sources
Helixi182 – 19211Combined sources
Turni193 – 1953Combined sources
Turni200 – 2023Combined sources
Beta strandi206 – 2083Combined sources
Helixi217 – 2204Combined sources
Helixi224 – 2307Combined sources
Beta strandi241 – 2433Combined sources
Beta strandi246 – 2483Combined sources
Helixi252 – 2554Combined sources
Helixi267 – 2693Combined sources
Turni276 – 2794Combined sources
Helixi282 – 30524Combined sources
Helixi311 – 33222Combined sources
Helixi334 – 3396Combined sources
Helixi349 – 3524Combined sources
Helixi365 – 3706Combined sources
Helixi374 – 3763Combined sources
Beta strandi379 – 3835Combined sources
Beta strandi386 – 3883Combined sources
Helixi390 – 3934Combined sources
Helixi398 – 41417Combined sources
Beta strandi420 – 4245Combined sources
Helixi428 – 4303Combined sources
Helixi431 – 44313Combined sources
Helixi449 – 4557Combined sources
Helixi464 – 4685Combined sources
Beta strandi469 – 4713Combined sources
Helixi472 – 48110Combined sources
Helixi484 – 4863Combined sources
Helixi489 – 4957Combined sources
Beta strandi503 – 5053Combined sources
Helixi506 – 52116Combined sources
Helixi524 – 5263Combined sources
Turni528 – 5303Combined sources
Helixi533 – 5364Combined sources
Helixi539 – 5468Combined sources
Helixi550 – 5578Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V0Xmodel-A1-604[»]
5F19X-ray2.04A/B19-569[»]
5F1AX-ray2.38A/B19-570[»]
5IKQX-ray2.41A/B19-569[»]
5IKRX-ray2.34A/B19-569[»]
5IKTX-ray2.45A/B19-569[»]
5IKVX-ray2.51A/B19-569[»]
ProteinModelPortaliP35354.
SMRiP35354. Positions 18-568.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 5538EGF-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the prostaglandin G/H synthase family.Curated
Contains 1 EGF-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2408. Eukaryota.
ENOG410XPZ3. LUCA.
GeneTreeiENSGT00390000010743.
HOGENOMiHOG000013149.
HOVERGENiHBG000366.
InParanoidiP35354.
KOiK11987.
OMAiCNNVKGC.
OrthoDBiEOG091G03CD.
PhylomeDBiP35354.
TreeFamiTF329675.

Family and domain databases

Gene3Di1.10.640.10. 1 hit.
InterProiIPR029576. COX-2.
IPR000742. EGF-like_dom.
IPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
[Graphical view]
PANTHERiPTHR11903:SF8. PTHR11903:SF8. 1 hit.
PfamiPF03098. An_peroxidase. 1 hit.
PF00008. EGF. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
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.

P35354-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLARALLLCA VLALSHTANP CCSHPCQNRG VCMSVGFDQY KCDCTRTGFY
60 70 80 90 100
GENCSTPEFL TRIKLFLKPT PNTVHYILTH FKGFWNVVNN IPFLRNAIMS
110 120 130 140 150
YVLTSRSHLI DSPPTYNADY GYKSWEAFSN LSYYTRALPP VPDDCPTPLG
160 170 180 190 200
VKGKKQLPDS NEIVEKLLLR RKFIPDPQGS NMMFAFFAQH FTHQFFKTDH
210 220 230 240 250
KRGPAFTNGL GHGVDLNHIY GETLARQRKL RLFKDGKMKY QIIDGEMYPP
260 270 280 290 300
TVKDTQAEMI YPPQVPEHLR FAVGQEVFGL VPGLMMYATI WLREHNRVCD
310 320 330 340 350
VLKQEHPEWG DEQLFQTSRL ILIGETIKIV IEDYVQHLSG YHFKLKFDPE
360 370 380 390 400
LLFNKQFQYQ NRIAAEFNTL YHWHPLLPDT FQIHDQKYNY QQFIYNNSIL
410 420 430 440 450
LEHGITQFVE SFTRQIAGRV AGGRNVPPAV QKVSQASIDQ SRQMKYQSFN
460 470 480 490 500
EYRKRFMLKP YESFEELTGE KEMSAELEAL YGDIDAVELY PALLVEKPRP
510 520 530 540 550
DAIFGETMVE VGAPFSLKGL MGNVICSPAY WKPSTFGGEV GFQIINTASI
560 570 580 590 600
QSLICNNVKG CPFTSFSVPD PELIKTVTIN ASSSRSGLDD INPTVLLKER

STEL
Length:604
Mass (Da):68,996
Last modified:December 15, 1998 - v2
Checksum:i72FBD699F6128519
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti165 – 1651E → G in AAA58433 (PubMed:1380156).Curated
Sequence conflicti438 – 4381I → T in AAA35803 (PubMed:8473346).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti228 – 2281R → H.1 Publication
Corresponds to variant rs3218622 [ dbSNP | Ensembl ].
VAR_016262
Natural varianti428 – 4281P → A.1 Publication
Corresponds to variant rs4648279 [ dbSNP | Ensembl ].
VAR_016263
Natural varianti488 – 4881E → G.
Corresponds to variant rs5272 [ dbSNP | Ensembl ].
VAR_011980
Natural varianti511 – 5111V → A.2 Publications
Corresponds to variant rs5273 [ dbSNP | Ensembl ].
VAR_011981
Natural varianti587 – 5871G → R.1 Publication
Corresponds to variant rs3218625 [ dbSNP | Ensembl ].
VAR_016264

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L15326 mRNA. Translation: AAA35803.1.
M90100 mRNA. Translation: AAA58433.1.
D28235 Genomic DNA. Translation: BAA05698.1.
U04636 Genomic DNA. Translation: AAA57317.1.
AY462100 mRNA. Translation: AAR23927.1.
AY229989 Genomic DNA. Translation: AAO38056.1.
AY382629 Genomic DNA. Translation: AAQ75702.1.
AK292167 mRNA. Translation: BAF84856.1.
AL033533 Genomic DNA. Translation: CAB41240.1.
CH471067 Genomic DNA. Translation: EAW91216.1.
BC013734 mRNA. Translation: AAH13734.1.
CCDSiCCDS1371.1.
PIRiA46150.
RefSeqiNP_000954.1. NM_000963.3.
UniGeneiHs.196384.

Genome annotation databases

EnsembliENST00000367468; ENSP00000356438; ENSG00000073756.
GeneIDi5743.
KEGGihsa:5743.
UCSCiuc001gsb.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs
SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L15326 mRNA. Translation: AAA35803.1.
M90100 mRNA. Translation: AAA58433.1.
D28235 Genomic DNA. Translation: BAA05698.1.
U04636 Genomic DNA. Translation: AAA57317.1.
AY462100 mRNA. Translation: AAR23927.1.
AY229989 Genomic DNA. Translation: AAO38056.1.
AY382629 Genomic DNA. Translation: AAQ75702.1.
AK292167 mRNA. Translation: BAF84856.1.
AL033533 Genomic DNA. Translation: CAB41240.1.
CH471067 Genomic DNA. Translation: EAW91216.1.
BC013734 mRNA. Translation: AAH13734.1.
CCDSiCCDS1371.1.
PIRiA46150.
RefSeqiNP_000954.1. NM_000963.3.
UniGeneiHs.196384.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V0Xmodel-A1-604[»]
5F19X-ray2.04A/B19-569[»]
5F1AX-ray2.38A/B19-570[»]
5IKQX-ray2.41A/B19-569[»]
5IKRX-ray2.34A/B19-569[»]
5IKTX-ray2.45A/B19-569[»]
5IKVX-ray2.51A/B19-569[»]
ProteinModelPortaliP35354.
SMRiP35354. Positions 18-568.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111715. 32 interactions.
DIPiDIP-28131N.
IntActiP35354. 2 interactions.
MINTiMINT-203337.
STRINGi9606.ENSP00000356438.

Chemistry

BindingDBiP35354.
ChEMBLiCHEMBL2094253.
DrugBankiDB00316. Acetaminophen.
DB00945. Acetylsalicylic acid.
DB00041. Aldesleukin.
DB00233. Aminosalicylic Acid.
DB01435. Antipyrine.
DB01419. Antrafenine.
DB01014. Balsalazide.
DB00963. Bromfenac.
DB00887. Bumetanide.
DB06774. Capsaicin.
DB00821. Carprofen.
DB00482. Celecoxib.
DB00856. Chlorphenesin.
DB00515. Cisplatin.
DB00720. Clodronate.
DB00250. Dapsone.
DB00035. Desmopressin.
DB00586. Diclofenac.
DB00861. Diflunisal.
DB00154. Dihomo-gamma-linolenic acid.
DB01395. Drospirenone.
DB00005. Etanercept.
DB00749. Etodolac.
DB00773. Etoposide.
DB01628. Etoricoxib.
DB00573. Fenoprofen.
DB00712. Flurbiprofen.
DB01404. Ginseng.
DB01050. Ibuprofen.
DB00159. Icosapent.
DB00328. Indomethacin.
DB01009. Ketoprofen.
DB00465. Ketorolac.
DB00480. Lenalidomide.
DB06725. Lornoxicam.
DB01283. Lumiracoxib.
DB01397. Magnesium salicylate.
DB00939. Meclofenamic acid.
DB00784. Mefenamic acid.
DB00814. Meloxicam.
DB00244. Mesalazine.
DB00461. Nabumetone.
DB00788. Naproxen.
DB06802. Nepafenac.
DB04552. Niflumic Acid.
DB04743. Nimesulide.
DB06804. Nonoxynol-9.
DB00991. Oxaprozin.
DB08439. Parecoxib.
DB00812. Phenylbutazone.
DB00554. Piroxicam.
DB08910. Pomalidomide.
DB00884. Risedronate.
DB00936. Salicylic acid.
DB01399. Salsalate.
DB00795. Sulfasalazine.
DB00605. Sulindac.
DB00870. Suprofen.
DB08819. Tafluprost.
DB00469. Tenoxicam.
DB00360. Tetrahydrobiopterin.
DB01041. Thalidomide.
DB01600. Tiaprofenic acid.
DB00500. Tolmetin.
DB00620. Triamcinolone.
DB01401. Trisalicylate-choline.
GuidetoPHARMACOLOGYi1376.
SwissLipidsiSLP:000000830.

Protein family/group databases

PeroxiBasei3321. HsPGHS02.

PTM databases

iPTMnetiP35354.
PhosphoSiteiP35354.

Polymorphism and mutation databases

BioMutaiPTGS2.
DMDMi3915797.

Proteomic databases

EPDiP35354.
MaxQBiP35354.
PaxDbiP35354.
PeptideAtlasiP35354.
PRIDEiP35354.

Protocols and materials databases

DNASUi5743.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367468; ENSP00000356438; ENSG00000073756.
GeneIDi5743.
KEGGihsa:5743.
UCSCiuc001gsb.4. human.

Organism-specific databases

CTDi5743.
GeneCardsiPTGS2.
HGNCiHGNC:9605. PTGS2.
HPAiCAB000113.
HPA001335.
MIMi600262. gene.
neXtProtiNX_P35354.
PharmGKBiPA293.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2408. Eukaryota.
ENOG410XPZ3. LUCA.
GeneTreeiENSGT00390000010743.
HOGENOMiHOG000013149.
HOVERGENiHBG000366.
InParanoidiP35354.
KOiK11987.
OMAiCNNVKGC.
OrthoDBiEOG091G03CD.
PhylomeDBiP35354.
TreeFamiTF329675.

Enzyme and pathway databases

UniPathwayiUPA00662.
BioCyciMetaCyc:HS01115-MONOMER.
BRENDAi1.14.99.1. 2681.
ReactomeiR-HSA-197264. Nicotinamide salvaging.
R-HSA-2142770. Synthesis of 15-eicosatetraenoic acid derivatives.
R-HSA-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
SABIO-RKP35354.
SIGNORiP35354.

Miscellaneous databases

GeneWikiiProstaglandin-endoperoxide_synthase_2.
PTGS2.
GenomeRNAii5743.
PROiP35354.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000073756.
CleanExiHS_PTGS2.
ExpressionAtlasiP35354. baseline and differential.
GenevisibleiP35354. HS.

Family and domain databases

Gene3Di1.10.640.10. 1 hit.
InterProiIPR029576. COX-2.
IPR000742. EGF-like_dom.
IPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
[Graphical view]
PANTHERiPTHR11903:SF8. PTHR11903:SF8. 1 hit.
PfamiPF03098. An_peroxidase. 1 hit.
PF00008. EGF. 1 hit.
[Graphical view]
PRINTSiPR00457. ANPEROXIDASE.
SUPFAMiSSF48113. SSF48113. 1 hit.
PROSITEiPS50026. EGF_3. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPGH2_HUMAN
AccessioniPrimary (citable) accession number: P35354
Secondary accession number(s): A8K802, Q16876
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 15, 1998
Last modified: September 7, 2016
This is version 180 of the entry and version 2 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

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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

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 one 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.