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Prostaglandin G/H synthase 2 (EC 1.14.99.1) (Cyclooxygenase-2) (COX-2) (PHS II) (Prostaglandin H2 synthase 2) (PGH synthase 2) (PGHS-2) (Prostaglandin-endoperoxide synthase 2)

 PGH2_HUMAN              Reviewed;         604 AA.
P35354; A8K802; Q16876;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 2.
22-NOV-2017, entry version 192.
RecName: Full=Prostaglandin G/H synthase 2;
EC=1.14.99.1;
AltName: Full=Cyclooxygenase-2;
Short=COX-2;
AltName: Full=PHS II;
AltName: Full=Prostaglandin H2 synthase 2;
Short=PGH synthase 2;
Short=PGHS-2;
AltName: Full=Prostaglandin-endoperoxide synthase 2;
Flags: Precursor;
Name=PTGS2; Synonyms=COX2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Endothelial cell;
PubMed=8473346;
Jones D.A., Carlton D.P., McIntyre T.M., Zimmerman G.A.,
Prescott S.M.;
"Molecular cloning of human prostaglandin endoperoxide synthase type
II and demonstration of expression in response to cytokines.";
J. Biol. Chem. 268:9049-9054(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Endothelial cell;
PubMed=1380156; DOI=10.1073/pnas.89.16.7384;
Hla T., Neilson K.;
"Human cyclooxygenase-2 cDNA.";
Proc. Natl. Acad. Sci. U.S.A. 89:7384-7388(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Peripheral blood;
PubMed=8181472; DOI=10.1111/j.1432-1033.1994.tb18804.x;
Kosaka T., Miyata A., Ihara H., Hara S., Sugimoto T., Takeda O.,
Takahashi E., Tanabe T.;
"Characterization of the human gene (PTGS2) encoding prostaglandin-
endoperoxide synthase 2.";
Eur. J. Biochem. 221:889-897(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=7945196; DOI=10.1042/bj3020723;
Appleby S.B., Ristimaki A., Neilson K., Narko K., Hla T.;
"Structure of the human cyclo-oxygenase-2 gene.";
Biochem. J. 302:723-727(1994).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
Sharma S.V., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-228; ALA-428;
ALA-511 AND ARG-587.
NIEHS SNPs program;
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Synovium;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
CHARACTERIZATION.
PubMed=7947975; DOI=10.1016/0167-4838(94)90148-1;
Barnett J., Chow J., Ives D., Chiou M., Mackenzie R., Osen E.,
Nguyen B., Tsing S., Bach C., Freire J.;
"Purification, characterization and selective inhibition of human
prostaglandin G/H synthase 1 and 2 expressed in the baculovirus
system.";
Biochim. Biophys. Acta 1209:130-139(1994).
[13]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
S-NITROSYLATION AT CYS-526, AND MUTAGENESIS OF CYS-526; CYS-555 AND
CYS-561.
PubMed=16373578; DOI=10.1126/science.1119407;
Kim S.F., Huri D.A., Snyder S.H.;
"Inducible nitric oxide synthase binds, S-nitrosylates, and activates
cyclooxygenase-2.";
Science 310:1966-1970(2005).
[14]
GLYCOSYLATION AT ASN-580.
PubMed=17113084; DOI=10.1016/j.febslet.2006.10.073;
Sevigny M.B., Li C.F., Alas M., Hughes-Fulford M.;
"Glycosylation regulates turnover of cyclooxygenase-2.";
FEBS Lett. 580:6533-6536(2006).
[15]
VARIANT ALA-511.
PubMed=15308583; DOI=10.1093/carcin/bgh260;
Goodman J.E., Bowman E.D., Chanock S.J., Alberg A.J., Harris C.C.;
"Arachidonate lipoxygenase (ALOX) and cyclooxygenase (COX)
polymorphisms and colon cancer risk.";
Carcinogenesis 25:2467-2472(2004).
[16]
REVIEW ON FUNCTION; TISSUE SPECIFICITY AND INHIBITION BY NSAIDS.
PubMed=10966456; DOI=10.1146/annurev.biochem.69.1.145;
Smith W.L., DeWitt D.L., Garavito R.M.;
"Cyclooxygenases: structural, cellular, and molecular biology.";
Annu. Rev. Biochem. 69:145-182(2000).
[17]
REVIEW ON FUNCTION; INHIBITION BY ASPIRIN AND INVOLVEMENT IN
COLORECTAL CANCER.
PubMed=24605250; DOI=10.4292/wjgpt.v5.i1.40;
Sostres C., Gargallo C.J., Lanas A.;
"Aspirin, cyclooxygenase inhibition and colorectal cancer.";
World J. Gastrointest. Pharmacol. Ther. 5:40-49(2014).
-!- FUNCTION: 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. {ECO:0000269|PubMed:16373578}.
-!- CATALYTIC ACTIVITY: Arachidonate + AH(2) + 2 O(2) = prostaglandin
H(2) + A + H(2)O. {ECO:0000269|PubMed:16373578}.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
subunit. {ECO:0000250};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=16.2 uM for arachidonate (in absence of sodium nitroprusside
NO donor) {ECO:0000269|PubMed:16373578};
KM=17.0 uM for arachidonate (in presence of sodium nitroprusside
NO donor) {ECO:0000269|PubMed:16373578};
Vmax=81.3 nmol/min/mg enzyme (in absence of sodium nitroprusside
NO donor) {ECO:0000269|PubMed:16373578};
Vmax=132 nmol/min/mg enzyme (in absence of sodium nitroprusside
NO donor) {ECO:0000269|PubMed:16373578};
-!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane
protein. Endoplasmic reticulum membrane; Peripheral membrane
protein.
-!- INDUCTION: By cytokines and mitogens.
-!- PTM: S-nitrosylation by NOS2 (iNOS) activates enzyme activity. S-
nitrosylation may take place on different Cys residues in addition
to Cys-526. {ECO:0000269|PubMed:16373578}.
-!- 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.
-!- MISCELLANEOUS: 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.
-!- MISCELLANEOUS: 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.
-!- SIMILARITY: Belongs to the prostaglandin G/H synthase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PTGS2ID509ch1q31.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ptgs2/";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/ptgs2/";
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EMBL; L15326; AAA35803.1; -; mRNA.
EMBL; M90100; AAA58433.1; -; mRNA.
EMBL; D28235; BAA05698.1; -; Genomic_DNA.
EMBL; U04636; AAA57317.1; -; Genomic_DNA.
EMBL; AY462100; AAR23927.1; -; mRNA.
EMBL; AY229989; AAO38056.1; -; Genomic_DNA.
EMBL; AY382629; AAQ75702.1; -; Genomic_DNA.
EMBL; AK292167; BAF84856.1; -; mRNA.
EMBL; AL033533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471067; EAW91216.1; -; Genomic_DNA.
EMBL; BC013734; AAH13734.1; -; mRNA.
CCDS; CCDS1371.1; -.
PIR; A46150; A46150.
RefSeq; NP_000954.1; NM_000963.3.
UniGene; Hs.196384; -.
PDB; 1V0X; Model; -; A=1-604.
PDB; 5F19; X-ray; 2.04 A; A/B=19-569.
PDB; 5F1A; X-ray; 2.38 A; A/B=19-570.
PDB; 5IKQ; X-ray; 2.41 A; A/B=19-569.
PDB; 5IKR; X-ray; 2.34 A; A/B=19-569.
PDB; 5IKT; X-ray; 2.45 A; A/B=19-569.
PDB; 5IKV; X-ray; 2.51 A; A/B=19-569.
PDB; 5KIR; X-ray; 2.70 A; A/B=19-569.
PDBsum; 1V0X; -.
PDBsum; 5F19; -.
PDBsum; 5F1A; -.
PDBsum; 5IKQ; -.
PDBsum; 5IKR; -.
PDBsum; 5IKT; -.
PDBsum; 5IKV; -.
PDBsum; 5KIR; -.
ProteinModelPortal; P35354; -.
SMR; P35354; -.
BioGrid; 111715; 36.
CORUM; P35354; -.
DIP; DIP-28131N; -.
IntAct; P35354; 2.
MINT; MINT-203337; -.
STRING; 9606.ENSP00000356438; -.
BindingDB; P35354; -.
ChEMBL; CHEMBL230; -.
DrugBank; DB03477; 1-Phenylsulfonamide-3-Trifluoromethyl-5-Parabromophenylpyrazole.
DrugBank; DB00316; Acetaminophen.
DrugBank; DB00945; Acetylsalicylic acid.
DrugBank; DB00041; Aldesleukin.
DrugBank; DB00233; Aminosalicylic Acid.
DrugBank; DB01435; Antipyrine.
DrugBank; DB01419; Antrafenine.
DrugBank; DB01014; Balsalazide.
DrugBank; DB00963; Bromfenac.
DrugBank; DB00887; Bumetanide.
DrugBank; DB06774; Capsaicin.
DrugBank; DB00821; Carprofen.
DrugBank; DB00482; Celecoxib.
DrugBank; DB00856; Chlorphenesin.
DrugBank; DB05095; Cimicoxib.
DrugBank; DB00515; Cisplatin.
DrugBank; DB00720; Clodronate.
DrugBank; DB00250; Dapsone.
DrugBank; DB05804; dehydroepiandrosterone sulfate.
DrugBank; DB00035; Desmopressin.
DrugBank; DB00586; Diclofenac.
DrugBank; DB00861; Diflunisal.
DrugBank; DB00154; Dihomo-gamma-linolenic acid.
DrugBank; DB01395; Drospirenone.
DrugBank; DB00005; Etanercept.
DrugBank; DB00749; Etodolac.
DrugBank; DB00773; Etoposide.
DrugBank; DB01628; Etoricoxib.
DrugBank; DB00573; Fenoprofen.
DrugBank; DB09217; Firocoxib.
DrugBank; DB02266; Flufenamic Acid.
DrugBank; DB00712; Flurbiprofen.
DrugBank; DB01404; Ginseng.
DrugBank; DB01050; Ibuprofen.
DrugBank; DB00159; Icosapent.
DrugBank; DB00328; Indomethacin.
DrugBank; DB01009; Ketoprofen.
DrugBank; DB00465; Ketorolac.
DrugBank; DB00480; Lenalidomide.
DrugBank; DB04725; Licofelone.
DrugBank; DB06725; Lornoxicam.
DrugBank; DB01283; Lumiracoxib.
DrugBank; DB01397; Magnesium salicylate.
DrugBank; DB00939; Meclofenamic acid.
DrugBank; DB00784; Mefenamic acid.
DrugBank; DB00814; Meloxicam.
DrugBank; DB00244; Mesalazine.
DrugBank; DB00461; Nabumetone.
DrugBank; DB00788; Naproxen.
DrugBank; DB06802; Nepafenac.
DrugBank; DB04552; Niflumic Acid.
DrugBank; DB04743; Nimesulide.
DrugBank; DB06804; Nonoxynol-9.
DrugBank; DB00991; Oxaprozin.
DrugBank; DB08439; Parecoxib.
DrugBank; DB00812; Phenylbutazone.
DrugBank; DB00554; Piroxicam.
DrugBank; DB08910; Pomalidomide.
DrugBank; DB03866; Prostaglandin G2.
DrugBank; DB02709; Resveratrol.
DrugBank; DB00884; Risedronate.
DrugBank; DB00533; Rofecoxib.
DrugBank; DB00936; Salicylic acid.
DrugBank; DB01399; Salsalate.
DrugBank; DB00360; Sapropterin.
DrugBank; DB05875; substance P.
DrugBank; DB00795; Sulfasalazine.
DrugBank; DB00605; Sulindac.
DrugBank; DB00870; Suprofen.
DrugBank; DB08819; Tafluprost.
DrugBank; DB00469; Tenoxicam.
DrugBank; DB01041; Thalidomide.
DrugBank; DB01600; Tiaprofenic acid.
DrugBank; DB00500; Tolmetin.
DrugBank; DB00620; Triamcinolone.
DrugBank; DB01401; Trisalicylate-choline.
DrugBank; DB00580; Valdecoxib.
GuidetoPHARMACOLOGY; 1376; -.
SwissLipids; SLP:000000830; -.
PeroxiBase; 3321; HsPGHS02.
iPTMnet; P35354; -.
PhosphoSitePlus; P35354; -.
BioMuta; PTGS2; -.
DMDM; 3915797; -.
EPD; P35354; -.
MaxQB; P35354; -.
PaxDb; P35354; -.
PeptideAtlas; P35354; -.
PRIDE; P35354; -.
DNASU; 5743; -.
Ensembl; ENST00000367468; ENSP00000356438; ENSG00000073756.
GeneID; 5743; -.
KEGG; hsa:5743; -.
UCSC; uc001gsb.4; human.
CTD; 5743; -.
DisGeNET; 5743; -.
EuPathDB; HostDB:ENSG00000073756.11; -.
GeneCards; PTGS2; -.
HGNC; HGNC:9605; PTGS2.
HPA; CAB000113; -.
HPA; HPA001335; -.
MIM; 600262; gene.
neXtProt; NX_P35354; -.
OpenTargets; ENSG00000073756; -.
PharmGKB; PA293; -.
eggNOG; KOG2408; Eukaryota.
eggNOG; ENOG410XPZ3; LUCA.
GeneTree; ENSGT00390000010743; -.
HOGENOM; HOG000013149; -.
HOVERGEN; HBG000366; -.
InParanoid; P35354; -.
KO; K11987; -.
OMA; CNNVKGC; -.
OrthoDB; EOG091G03CD; -.
PhylomeDB; P35354; -.
TreeFam; TF329675; -.
BioCyc; MetaCyc:HS01115-MONOMER; -.
BRENDA; 1.14.99.1; 2681.
Reactome; R-HSA-197264; Nicotinamide salvaging.
Reactome; R-HSA-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
SABIO-RK; P35354; -.
SIGNOR; P35354; -.
UniPathway; UPA00662; -.
GeneWiki; Prostaglandin-endoperoxide_synthase_2; -.
GeneWiki; PTGS2; -.
GenomeRNAi; 5743; -.
PRO; PR:P35354; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000073756; -.
CleanEx; HS_PTGS2; -.
ExpressionAtlas; P35354; baseline and differential.
Genevisible; P35354; HS.
GO; GO:0005901; C:caveola; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:ParkinsonsUK-UCL.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0043005; C:neuron projection; IDA:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0050473; F:arachidonate 15-lipoxygenase activity; TAS:Reactome.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0020037; F:heme binding; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004601; F:peroxidase activity; TAS:Reactome.
GO; GO:0004666; F:prostaglandin-endoperoxide synthase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
GO; GO:0071318; P:cellular response to ATP; IEA:Ensembl.
GO; GO:0071498; P:cellular response to fluid shear stress; IEA:Ensembl.
GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEP:UniProtKB.
GO; GO:0071284; P:cellular response to lead ion; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0071471; P:cellular response to non-ionic osmotic stress; IEA:Ensembl.
GO; GO:0034644; P:cellular response to UV; IEA:Ensembl.
GO; GO:0019371; P:cyclooxygenase pathway; IDA:BHF-UCL.
GO; GO:0046697; P:decidualization; IEA:Ensembl.
GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
GO; GO:0042633; P:hair cycle; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:0007612; P:learning; IEA:Ensembl.
GO; GO:0019372; P:lipoxygenase pathway; TAS:Reactome.
GO; GO:0035633; P:maintenance of permeability of blood-brain barrier; IEA:Ensembl.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:0006928; P:movement of cell or subcellular component; TAS:ProtInc.
GO; GO:0034356; P:NAD biosynthesis via nicotinamide riboside salvage pathway; TAS:Reactome.
GO; GO:0097756; P:negative regulation of blood vessel diameter; IEA:Ensembl.
GO; GO:0051926; P:negative regulation of calcium ion transport; IEA:Ensembl.
GO; GO:0045786; P:negative regulation of cell cycle; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
GO; GO:1902219; P:negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress; IEA:Ensembl.
GO; GO:0045986; P:negative regulation of smooth muscle contraction; IEA:Ensembl.
GO; GO:0032227; P:negative regulation of synaptic transmission, dopaminergic; IEA:Ensembl.
GO; GO:0030728; P:ovulation; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0090336; P:positive regulation of brown fat cell differentiation; ISS:BHF-UCL.
GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISS:BHF-UCL.
GO; GO:0031622; P:positive regulation of fever generation; ISS:BHF-UCL.
GO; GO:0090271; P:positive regulation of fibroblast growth factor production; ISS:BHF-UCL.
GO; GO:0042346; P:positive regulation of NF-kappaB import into nucleus; IEA:Ensembl.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:BHF-UCL.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0090362; P:positive regulation of platelet-derived growth factor production; ISS:BHF-UCL.
GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; NAS:BHF-UCL.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0045987; P:positive regulation of smooth muscle contraction; IEA:Ensembl.
GO; GO:0031915; P:positive regulation of synaptic plasticity; IEA:Ensembl.
GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
GO; GO:0071636; P:positive regulation of transforming growth factor beta production; ISS:BHF-UCL.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISS:BHF-UCL.
GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
GO; GO:0001516; P:prostaglandin biosynthetic process; ISS:UniProtKB.
GO; GO:0006693; P:prostaglandin metabolic process; TAS:ProtInc.
GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
GO; GO:0050727; P:regulation of inflammatory response; NAS:UniProtKB.
GO; GO:1990776; P:response to angiotensin; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0070542; P:response to fatty acid; IEA:Ensembl.
GO; GO:0009750; P:response to fructose; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0010226; P:response to lithium ion; IEA:Ensembl.
GO; GO:0010042; P:response to manganese ion; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
GO; GO:0034612; P:response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0033280; P:response to vitamin D; IEA:Ensembl.
GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
Gene3D; 1.10.640.10; -; 1.
InterPro; IPR029576; COX-2.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR010255; Haem_peroxidase.
InterPro; IPR019791; Haem_peroxidase_animal.
InterPro; IPR037120; Haem_peroxidase_sf.
PANTHER; PTHR11903:SF8; PTHR11903:SF8; 1.
Pfam; PF03098; An_peroxidase; 1.
Pfam; PF00008; EGF; 1.
PRINTS; PR00457; ANPEROXIDASE.
SUPFAM; SSF48113; SSF48113; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS50292; PEROXIDASE_3; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Dioxygenase; Disulfide bond;
Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
Glycoprotein; Heme; Iron; Lipid biosynthesis; Lipid metabolism;
Membrane; Metal-binding; Microsome; Oxidoreductase; Peroxidase;
Polymorphism; Prostaglandin biosynthesis; Prostaglandin metabolism;
Reference proteome; S-nitrosylation; Signal.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 604 Prostaglandin G/H synthase 2.
/FTId=PRO_0000023875.
DOMAIN 18 55 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
ACT_SITE 193 193 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00298}.
ACT_SITE 371 371 For cyclooxygenase activity.
{ECO:0000250}.
METAL 374 374 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00298}.
BINDING 106 106 Substrate. {ECO:0000250}.
BINDING 341 341 Substrate. {ECO:0000250}.
BINDING 371 371 Substrate. {ECO:0000250}.
SITE 516 516 Aspirin-acetylated serine. {ECO:0000250}.
MOD_RES 526 526 S-nitrosocysteine.
{ECO:0000305|PubMed:16373578}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 130 130 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 396 396 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 580 580 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17113084}.
DISULFID 21 32 {ECO:0000250}.
DISULFID 22 145 {ECO:0000250}.
DISULFID 26 42 {ECO:0000250}.
DISULFID 44 54 {ECO:0000250}.
DISULFID 555 561 {ECO:0000250}.
VARIANT 228 228 R -> H (in dbSNP:rs3218622).
{ECO:0000269|Ref.6}.
/FTId=VAR_016262.
VARIANT 428 428 P -> A (in dbSNP:rs4648279).
{ECO:0000269|Ref.6}.
/FTId=VAR_016263.
VARIANT 488 488 E -> G (in dbSNP:rs5272).
/FTId=VAR_011980.
VARIANT 511 511 V -> A (in dbSNP:rs5273).
{ECO:0000269|PubMed:15308583,
ECO:0000269|Ref.6}.
/FTId=VAR_011981.
VARIANT 587 587 G -> R (in dbSNP:rs3218625).
{ECO:0000269|Ref.6}.
/FTId=VAR_016264.
MUTAGEN 526 526 C->S: Prevents activation by nitric oxid
(NO). {ECO:0000269|PubMed:16373578}.
MUTAGEN 555 555 C->S: Abolishes enzyme activity.
{ECO:0000269|PubMed:16373578}.
MUTAGEN 561 561 C->S: Does not affect activation by
nitric oxid (NO).
{ECO:0000269|PubMed:16373578}.
CONFLICT 165 165 E -> G (in Ref. 2; AAA58433).
{ECO:0000305}.
CONFLICT 438 438 I -> T (in Ref. 1; AAA35803).
{ECO:0000305}.
TURN 20 23 {ECO:0000244|PDB:5F19}.
STRAND 31 35 {ECO:0000244|PDB:5F19}.
TURN 36 38 {ECO:0000244|PDB:5F19}.
STRAND 39 43 {ECO:0000244|PDB:5F19}.
STRAND 47 50 {ECO:0000244|PDB:5F19}.
TURN 51 54 {ECO:0000244|PDB:5F19}.
HELIX 59 66 {ECO:0000244|PDB:5F19}.
HELIX 71 78 {ECO:0000244|PDB:5F19}.
HELIX 82 89 {ECO:0000244|PDB:5F19}.
HELIX 92 107 {ECO:0000244|PDB:5F19}.
STRAND 120 122 {ECO:0000244|PDB:5F19}.
HELIX 125 129 {ECO:0000244|PDB:5F19}.
STRAND 135 138 {ECO:0000244|PDB:5F19}.
STRAND 150 153 {ECO:0000244|PDB:5F19}.
HELIX 160 167 {ECO:0000244|PDB:5F19}.
HELIX 182 192 {ECO:0000244|PDB:5F19}.
TURN 193 195 {ECO:0000244|PDB:5F19}.
TURN 200 202 {ECO:0000244|PDB:5F19}.
STRAND 206 208 {ECO:0000244|PDB:5F19}.
HELIX 217 220 {ECO:0000244|PDB:5F19}.
HELIX 224 230 {ECO:0000244|PDB:5F19}.
STRAND 241 243 {ECO:0000244|PDB:5F19}.
STRAND 246 248 {ECO:0000244|PDB:5F19}.
HELIX 252 255 {ECO:0000244|PDB:5F19}.
HELIX 267 269 {ECO:0000244|PDB:5F19}.
TURN 276 279 {ECO:0000244|PDB:5F19}.
HELIX 282 305 {ECO:0000244|PDB:5F19}.
HELIX 311 332 {ECO:0000244|PDB:5F19}.
HELIX 334 339 {ECO:0000244|PDB:5F19}.
HELIX 349 352 {ECO:0000244|PDB:5F19}.
HELIX 365 370 {ECO:0000244|PDB:5F19}.
HELIX 374 376 {ECO:0000244|PDB:5F19}.
STRAND 379 383 {ECO:0000244|PDB:5F19}.
STRAND 386 388 {ECO:0000244|PDB:5F19}.
HELIX 390 393 {ECO:0000244|PDB:5F19}.
HELIX 398 414 {ECO:0000244|PDB:5F19}.
STRAND 420 424 {ECO:0000244|PDB:5F19}.
HELIX 428 430 {ECO:0000244|PDB:5F19}.
HELIX 431 443 {ECO:0000244|PDB:5F19}.
HELIX 449 455 {ECO:0000244|PDB:5F19}.
HELIX 464 468 {ECO:0000244|PDB:5F19}.
STRAND 469 471 {ECO:0000244|PDB:5F19}.
HELIX 472 481 {ECO:0000244|PDB:5F19}.
HELIX 484 486 {ECO:0000244|PDB:5F19}.
HELIX 489 495 {ECO:0000244|PDB:5F19}.
STRAND 503 505 {ECO:0000244|PDB:5F19}.
HELIX 506 521 {ECO:0000244|PDB:5F19}.
HELIX 524 526 {ECO:0000244|PDB:5F19}.
TURN 528 530 {ECO:0000244|PDB:5F19}.
HELIX 533 536 {ECO:0000244|PDB:5F19}.
HELIX 539 546 {ECO:0000244|PDB:5F19}.
HELIX 550 557 {ECO:0000244|PDB:5F19}.
SEQUENCE 604 AA; 68996 MW; 72FBD699F6128519 CRC64;
MLARALLLCA VLALSHTANP CCSHPCQNRG VCMSVGFDQY KCDCTRTGFY GENCSTPEFL
TRIKLFLKPT PNTVHYILTH FKGFWNVVNN IPFLRNAIMS YVLTSRSHLI DSPPTYNADY
GYKSWEAFSN LSYYTRALPP VPDDCPTPLG VKGKKQLPDS NEIVEKLLLR RKFIPDPQGS
NMMFAFFAQH FTHQFFKTDH KRGPAFTNGL GHGVDLNHIY GETLARQRKL RLFKDGKMKY
QIIDGEMYPP TVKDTQAEMI YPPQVPEHLR FAVGQEVFGL VPGLMMYATI WLREHNRVCD
VLKQEHPEWG DEQLFQTSRL ILIGETIKIV IEDYVQHLSG YHFKLKFDPE LLFNKQFQYQ
NRIAAEFNTL YHWHPLLPDT FQIHDQKYNY QQFIYNNSIL LEHGITQFVE SFTRQIAGRV
AGGRNVPPAV QKVSQASIDQ SRQMKYQSFN EYRKRFMLKP YESFEELTGE KEMSAELEAL
YGDIDAVELY PALLVEKPRP DAIFGETMVE VGAPFSLKGL MGNVICSPAY WKPSTFGGEV
GFQIINTASI QSLICNNVKG CPFTSFSVPD PELIKTVTIN ASSSRSGLDD INPTVLLKER
STEL


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