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Prostaglandin G/H synthase 1 (EC 1.14.99.1) (Cyclooxygenase-1) (COX-1) (Prostaglandin H2 synthase 1) (PGH synthase 1) (PGHS-1) (PHS 1) (Prostaglandin-endoperoxide synthase 1)

 PGH1_HUMAN              Reviewed;         599 AA.
P23219; A8K1V7; B4DHQ2; B4E2S5; Q15122; Q3HY28; Q3HY29; Q5T7T6;
Q5T7T7; Q5T7T8;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
25-OCT-2017, entry version 194.
RecName: Full=Prostaglandin G/H synthase 1;
EC=1.14.99.1;
AltName: Full=Cyclooxygenase-1;
Short=COX-1;
AltName: Full=Prostaglandin H2 synthase 1;
Short=PGH synthase 1;
Short=PGHS-1;
Short=PHS 1;
AltName: Full=Prostaglandin-endoperoxide synthase 1;
Flags: Precursor;
Name=PTGS1; Synonyms=COX1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT ARG-8.
PubMed=2512924; DOI=10.1016/S0006-291X(89)80049-X;
Yokoyama C., Tanabe T.;
"Cloning of human gene encoding prostaglandin endoperoxide synthase
and primary structure of the enzyme.";
Biochem. Biophys. Res. Commun. 165:888-894(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF SER-529, AND
VARIANT ARG-8.
PubMed=1907252;
Funk C.D., Funk L.B., Kennedy M.E., Pong A.S., Fitzgerald G.A.;
"Human platelet/erythroleukemia cell prostaglandin G/H synthase: cDNA
cloning, expression, and gene chromosomal assignment.";
FASEB J. 5:2304-2312(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-8.
TISSUE=Platelet;
PubMed=1734857; DOI=10.1016/0006-291X(92)91750-K;
Takahashi Y., Ueda N., Yoshimoto T., Yamamoto S., Yokoyama C.,
Miyata A., Tanabe T., Fuse I., Hattori A., Shibata A.;
"Immunoaffinity purification and cDNA cloning of human platelet
prostaglandin endoperoxide synthase (cyclooxygenase).";
Biochem. Biophys. Res. Commun. 182:433-438(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT ARG-8.
TISSUE=Lung fibroblast;
PubMed=1587858;
Diaz A., Reginato A.M., Jimenez S.A.;
"Alternative splicing of human prostaglandin G/H synthase mRNA and
evidence of differential regulation of the resulting transcripts by
transforming growth factor beta 1, interleukin 1 beta, and tumor
necrosis factor alpha.";
J. Biol. Chem. 267:10816-10822(1992).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6).
PubMed=16141368; DOI=10.1124/jpet.105.090944;
Qin N., Zhang S.P., Reitz T.L., Mei J.M., Flores C.M.;
"Cloning, expression, and functional characterization of human
cyclooxygenase-1 splicing variants: evidence for intron 1 retention.";
J. Pharmacol. Exp. Ther. 315:1298-1305(2005).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS ARG-8 AND
LEU-17.
PubMed=12192304; DOI=10.1097/00001721-200209000-00007;
Scott B.T., Hasstedt S.J., Bovill E.G., Callas P.W., Valliere J.E.,
Wang L.-H., Wu K.K., Long G.L.;
"Characterization of the human prostaglandin H synthase 1 gene
(PTGS1): exclusion by genetic linkage analysis as a second modifier
gene in familial thrombosis.";
Blood Coagul. Fibrinolysis 13:519-531(2002).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), AND
VARIANT ARG-8.
TISSUE=Caudate nucleus, Hippocampus, and Trachea;
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).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS ARG-8;
LEU-17; HIS-53; LEU-149 AND MET-237.
SeattleSNPs variation discovery resource;
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-8.
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] (ISOFORM 1), AND VARIANT ARG-8.
TISSUE=Brain;
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]
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).
[13]
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).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[15]
VARIANTS MET-237 AND ILE-481.
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).
-!- FUNCTION: Converts arachidonate to prostaglandin H2 (PGH2), a
committed step in prostanoid synthesis. Involved in the
constitutive production of prostanoids in particular in the
stomach and platelets. In gastric epithelial cells, it is a key
step in the generation of prostaglandins, such as prostaglandin E2
(PGE2), which plays an important role in cytoprotection. In
platelets, it is involved in the generation of thromboxane A2
(TXA2), which promotes platelet activation and aggregation,
vasoconstriction and proliferation of vascular smooth muscle
cells.
-!- CATALYTIC ACTIVITY: Arachidonate + AH(2) + 2 O(2) = prostaglandin
H(2) + A + H(2)O.
-!- 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};
-!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
-!- SUBUNIT: Homodimer.
-!- SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane
protein. Endoplasmic reticulum membrane; Peripheral membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=Long;
IsoId=P23219-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=P23219-2; Sequence=VSP_004673;
Name=3;
IsoId=P23219-3; Sequence=VSP_053936, VSP_004673;
Name=4;
IsoId=P23219-4; Sequence=VSP_046932;
Note=No experimental confirmation available.;
Name=5; Synonyms=1b3;
IsoId=P23219-5; Sequence=VSP_054862;
Name=6; Synonyms=1b2;
IsoId=P23219-6; Sequence=VSP_054863;
-!- 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}.
-!- SEQUENCE CAUTION:
Sequence=CAI14716.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/ptgs1/";
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EMBL; M31822; AAA36439.1; -; Genomic_DNA.
EMBL; M31812; AAA36439.1; JOINED; Genomic_DNA.
EMBL; M31813; AAA36439.1; JOINED; Genomic_DNA.
EMBL; M31814; AAA36439.1; JOINED; Genomic_DNA.
EMBL; M31815; AAA36439.1; JOINED; Genomic_DNA.
EMBL; M31816; AAA36439.1; JOINED; Genomic_DNA.
EMBL; M31817; AAA36439.1; JOINED; Genomic_DNA.
EMBL; M31818; AAA36439.1; JOINED; Genomic_DNA.
EMBL; M31819; AAA36439.1; JOINED; Genomic_DNA.
EMBL; M31820; AAA36439.1; JOINED; Genomic_DNA.
EMBL; M31821; AAA36439.1; JOINED; Genomic_DNA.
EMBL; M59979; AAA03630.1; -; mRNA.
EMBL; S78220; AAB21215.1; -; mRNA.
EMBL; S36219; AAB22216.1; -; mRNA.
EMBL; S36271; AAB22217.1; -; mRNA.
EMBL; DQ180741; ABA60098.1; -; mRNA.
EMBL; DQ180742; ABA60099.1; -; mRNA.
EMBL; AF440204; AAL33601.1; -; Genomic_DNA.
EMBL; AK290022; BAF82711.1; -; mRNA.
EMBL; AK295221; BAG58214.1; -; mRNA.
EMBL; AK304403; BAG65237.1; -; mRNA.
EMBL; AY449688; AAR08907.1; -; Genomic_DNA.
EMBL; AL162424; CAI14714.1; -; Genomic_DNA.
EMBL; AL359636; CAI14714.1; JOINED; Genomic_DNA.
EMBL; AL162424; CAI14715.1; -; Genomic_DNA.
EMBL; AL359636; CAI14715.1; JOINED; Genomic_DNA.
EMBL; AL162424; CAI14716.1; ALT_SEQ; Genomic_DNA.
EMBL; AL359636; CAM45740.1; -; Genomic_DNA.
EMBL; AL162424; CAM45740.1; JOINED; Genomic_DNA.
EMBL; AL359636; CAM45741.1; -; Genomic_DNA.
EMBL; AL162424; CAM45741.1; JOINED; Genomic_DNA.
EMBL; CH471090; EAW87530.1; -; Genomic_DNA.
EMBL; BC029840; AAH29840.1; -; mRNA.
CCDS; CCDS59520.1; -. [P23219-3]
CCDS; CCDS59521.1; -. [P23219-4]
CCDS; CCDS6842.1; -. [P23219-1]
CCDS; CCDS6843.1; -. [P23219-2]
PIR; JH0259; JH0259.
RefSeq; NP_000953.2; NM_000962.3. [P23219-1]
RefSeq; NP_001258094.1; NM_001271165.1. [P23219-4]
RefSeq; NP_001258095.1; NM_001271166.1.
RefSeq; NP_001258297.1; NM_001271368.1. [P23219-3]
RefSeq; NP_542158.1; NM_080591.2. [P23219-2]
RefSeq; XP_011517178.1; XM_011518876.2. [P23219-4]
UniGene; Hs.201978; -.
ProteinModelPortal; P23219; -.
SMR; P23219; -.
BioGrid; 111714; 6.
CORUM; P23219; -.
IntAct; P23219; 2.
MINT; MINT-4530066; -.
STRING; 9606.ENSP00000354612; -.
BindingDB; P23219; -.
ChEMBL; CHEMBL221; -.
DrugBank; DB02773; (3-Chloro-4-Propoxy-Phenyl)-Acetic Acid.
DrugBank; DB07983; 1-(4-IODOBENZOYL)-5-METHOXY-2-METHYL INDOLE-3-ACETIC ACID.
DrugBank; DB07981; 2-[1-(4-CHLOROBENZOYL)-5-METHOXY-2-METHYL-1H-INDOL-3-YL]-N-[(1R)-1-(HYDROXYMETHYL)PROPYL]ACETAMIDE.
DrugBank; DB07984; 2-[1-(4-CHLOROBENZOYL)-5-METHOXY-2-METHYL-1H-INDOL-3-YL]-N-[(1S)-1-(HYDROXYMETHYL)PROPYL]ACETAMIDE.
DrugBank; DB02198; 2-Bromoacetyl Group.
DrugBank; DB06736; Aceclofenac.
DrugBank; DB00316; Acetaminophen.
DrugBank; DB03667; Acetic Acid Salicyloyl-Amino-Ester.
DrugBank; DB00945; Acetylsalicylic acid.
DrugBank; DB01435; Antipyrine.
DrugBank; DB01419; Antrafenine.
DrugBank; DB04557; Arachidonic Acid.
DrugBank; DB01014; Balsalazide.
DrugBank; DB02379; Beta-D-Glucose.
DrugBank; DB00963; Bromfenac.
DrugBank; DB00796; Candesartan.
DrugBank; DB00821; Carprofen.
DrugBank; DB01136; Carvedilol.
DrugBank; DB00672; Chlorpropamide.
DrugBank; DB00250; Dapsone.
DrugBank; DB00035; Desmopressin.
DrugBank; DB00829; Diazepam.
DrugBank; DB00586; Diclofenac.
DrugBank; DB00711; Diethylcarbamazine.
DrugBank; DB00861; Diflunisal.
DrugBank; DB00154; Dihomo-gamma-linolenic acid.
DrugBank; DB01075; Diphenhydramine.
DrugBank; DB00470; Dronabinol.
DrugBank; DB00216; Eletriptan.
DrugBank; DB00402; Eszopiclone.
DrugBank; DB00749; Etodolac.
DrugBank; DB00773; Etoposide.
DrugBank; DB00573; Fenoprofen.
DrugBank; DB02266; Flufenamic Acid.
DrugBank; DB00712; Flurbiprofen.
DrugBank; DB03753; Flurbiprofen Methyl Ester.
DrugBank; DB01355; Hexobarbital.
DrugBank; DB00327; Hydromorphone.
DrugBank; DB01892; Hyperforin.
DrugBank; DB01050; Ibuprofen.
DrugBank; DB00159; Icosapent.
DrugBank; DB01181; Ifosfamide.
DrugBank; DB00619; Imatinib.
DrugBank; DB00328; Indomethacin.
DrugBank; DB01029; Irbesartan.
DrugBank; DB01221; Ketamine.
DrugBank; DB06738; Ketobemidone.
DrugBank; DB01009; Ketoprofen.
DrugBank; DB00465; Ketorolac.
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; DB04817; Metamizole.
DrugBank; DB00350; Minoxidil.
DrugBank; DB00471; Montelukast.
DrugBank; DB00461; Nabumetone.
DrugBank; DB00788; Naproxen.
DrugBank; DB00731; Nateglinide.
DrugBank; DB05822; NCX 4016.
DrugBank; DB06802; Nepafenac.
DrugBank; DB04552; Niflumic Acid.
DrugBank; DB00540; Nortriptyline.
DrugBank; DB01837; O-acetyl-L-serine.
DrugBank; DB00991; Oxaprozin.
DrugBank; DB03752; P-(2'-Iodo-5'-Thenoyl)Hydrotropic Acid.
DrugBank; DB03783; Phenacetin.
DrugBank; DB00812; Phenylbutazone.
DrugBank; DB01132; Pioglitazone.
DrugBank; DB00554; Piroxicam.
DrugBank; DB02110; Protoporphyrin Ix Containing Co.
DrugBank; DB02709; Resveratrol.
DrugBank; DB00533; Rofecoxib.
DrugBank; DB00412; Rosiglitazone.
DrugBank; DB00936; Salicylic acid.
DrugBank; DB01399; Salsalate.
DrugBank; DB01015; Sulfamethoxazole.
DrugBank; DB00795; Sulfasalazine.
DrugBank; DB00605; Sulindac.
DrugBank; DB00870; Suprofen.
DrugBank; DB00469; Tenoxicam.
DrugBank; DB00857; Terbinafine.
DrugBank; DB01041; Thalidomide.
DrugBank; DB01600; Tiaprofenic acid.
DrugBank; DB00500; Tolmetin.
DrugBank; DB00214; Torasemide.
DrugBank; DB05109; Trabectedin.
DrugBank; DB08814; Triflusal.
DrugBank; DB01401; Trisalicylate-choline.
DrugBank; DB00313; Valproic Acid.
DrugBank; DB00582; Voriconazole.
DrugBank; DB00549; Zafirlukast.
DrugBank; DB06737; Zaltoprofen.
DrugBank; DB00744; Zileuton.
DrugBank; DB00425; Zolpidem.
DrugBank; DB01198; Zopiclone.
GuidetoPHARMACOLOGY; 1375; -.
SwissLipids; SLP:000001103; -.
PeroxiBase; 3320; HsPGHS01.
iPTMnet; P23219; -.
PhosphoSitePlus; P23219; -.
DMDM; 317373262; -.
EPD; P23219; -.
MaxQB; P23219; -.
PaxDb; P23219; -.
PeptideAtlas; P23219; -.
PRIDE; P23219; -.
DNASU; 5742; -.
Ensembl; ENST00000223423; ENSP00000223423; ENSG00000095303. [P23219-2]
Ensembl; ENST00000362012; ENSP00000354612; ENSG00000095303. [P23219-1]
Ensembl; ENST00000373698; ENSP00000362802; ENSG00000095303. [P23219-4]
Ensembl; ENST00000540753; ENSP00000437709; ENSG00000095303. [P23219-3]
Ensembl; ENST00000619306; ENSP00000483540; ENSG00000095303. [P23219-6]
GeneID; 5742; -.
KEGG; hsa:5742; -.
UCSC; uc004bmf.3; human. [P23219-1]
CTD; 5742; -.
DisGeNET; 5742; -.
EuPathDB; HostDB:ENSG00000095303.14; -.
GeneCards; PTGS1; -.
HGNC; HGNC:9604; PTGS1.
HPA; CAB020315; -.
HPA; HPA002834; -.
MIM; 176805; gene.
neXtProt; NX_P23219; -.
OpenTargets; ENSG00000095303; -.
PharmGKB; PA24346; -.
eggNOG; KOG2408; Eukaryota.
eggNOG; ENOG410XPZ3; LUCA.
GeneTree; ENSGT00390000010743; -.
HOGENOM; HOG000013149; -.
HOVERGEN; HBG000366; -.
InParanoid; P23219; -.
KO; K00509; -.
OMA; FKTSGKM; -.
OrthoDB; EOG091G03CD; -.
PhylomeDB; P23219; -.
TreeFam; TF329675; -.
BioCyc; MetaCyc:HS01815-MONOMER; -.
BRENDA; 1.14.99.1; 2681.
Reactome; R-HSA-140180; COX reactions.
Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
SIGNOR; P23219; -.
UniPathway; UPA00662; -.
ChiTaRS; PTGS1; human.
GeneWiki; PTGS1; -.
GenomeRNAi; 5742; -.
PRO; PR:P23219; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000095303; -.
CleanEx; HS_PTGS1; -.
ExpressionAtlas; P23219; baseline and differential.
Genevisible; P23219; HS.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl.
GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
GO; GO:0020037; F:heme binding; IEA:InterPro.
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:BHF-UCL.
GO; GO:0019371; P:cyclooxygenase pathway; IDA:BHF-UCL.
GO; GO:0006954; P:inflammatory response; IEA:InterPro.
GO; GO:0006629; P:lipid metabolic process; NAS:ProtInc.
GO; GO:0001516; P:prostaglandin biosynthetic process; ISS:UniProtKB.
GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
InterPro; IPR029580; COX-1.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR010255; Haem_peroxidase.
InterPro; IPR019791; Haem_peroxidase_animal.
PANTHER; PTHR11903:SF6; PTHR11903:SF6; 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;
Alternative splicing; Complete proteome; Dioxygenase; Disulfide bond;
EGF-like domain; 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; Signal.
SIGNAL 1 23
CHAIN 24 599 Prostaglandin G/H synthase 1.
/FTId=PRO_0000023868.
DOMAIN 31 69 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
ACT_SITE 206 206 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00298}.
ACT_SITE 384 384 For cyclooxygenase activity.
{ECO:0000250}.
METAL 387 387 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00298}.
SITE 529 529 Aspirin-acetylated serine.
CARBOHYD 67 67 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 103 103 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 143 143 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 35 46 {ECO:0000250}.
DISULFID 36 158 {ECO:0000250}.
DISULFID 40 56 {ECO:0000250}.
DISULFID 58 68 {ECO:0000250}.
DISULFID 568 574 {ECO:0000250}.
VAR_SEQ 1 109 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046932.
VAR_SEQ 1 32 MSRSLLLWFLLFLLLLPPLPVLLADPGAPTPV -> MRKPR
LM (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_053936.
VAR_SEQ 1 3 MSR -> MSRECDPGARWGIFLASGGALNARLSPSSLSSAG
(in isoform 5).
{ECO:0000303|PubMed:16141368}.
/FTId=VSP_054862.
VAR_SEQ 1 3 MSR -> MSRECDPGARWGIFLASWWSLECQLSPSSLSSAG
(in isoform 6).
{ECO:0000303|PubMed:16141368}.
/FTId=VSP_054863.
VAR_SEQ 396 432 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:1587858}.
/FTId=VSP_004673.
VARIANT 8 8 W -> R (in dbSNP:rs1236913).
{ECO:0000269|PubMed:12192304,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1587858,
ECO:0000269|PubMed:1734857,
ECO:0000269|PubMed:1907252,
ECO:0000269|PubMed:2512924,
ECO:0000269|Ref.10, ECO:0000269|Ref.8}.
/FTId=VAR_013451.
VARIANT 17 17 P -> L (in dbSNP:rs3842787).
{ECO:0000269|PubMed:12192304,
ECO:0000269|Ref.8}.
/FTId=VAR_013452.
VARIANT 53 53 R -> H (in dbSNP:rs3842789).
{ECO:0000269|Ref.8}.
/FTId=VAR_019161.
VARIANT 149 149 R -> L (in dbSNP:rs10306140).
{ECO:0000269|Ref.8}.
/FTId=VAR_019162.
VARIANT 185 185 K -> T (in dbSNP:rs3842792).
/FTId=VAR_056663.
VARIANT 237 237 L -> M (in dbSNP:rs5789).
{ECO:0000269|PubMed:15308583,
ECO:0000269|Ref.8}.
/FTId=VAR_019163.
VARIANT 341 341 K -> R (in dbSNP:rs3842799).
/FTId=VAR_056664.
VARIANT 359 359 K -> R (in dbSNP:rs5791).
/FTId=VAR_013453.
VARIANT 443 443 I -> V (in dbSNP:rs5792).
/FTId=VAR_013454.
VARIANT 481 481 V -> I (in dbSNP:rs5794).
{ECO:0000269|PubMed:15308583}.
/FTId=VAR_028017.
MUTAGEN 529 529 S->N: Abolishes cyclooxygenase activity.
{ECO:0000269|PubMed:1907252}.
CONFLICT 12 12 F -> L (in Ref. 1; AAA36439).
{ECO:0000305}.
CONFLICT 113 113 R -> L (in Ref. 1; AAA36439).
{ECO:0000305}.
CONFLICT 378 378 M -> T (in Ref. 1; AAA36439).
{ECO:0000305}.
CONFLICT 423 423 D -> G (in Ref. 7; BAG65237).
{ECO:0000305}.
SEQUENCE 599 AA; 68686 MW; 1F4F734BCD00346D CRC64;
MSRSLLLWFL LFLLLLPPLP VLLADPGAPT PVNPCCYYPC QHQGICVRFG LDRYQCDCTR
TGYSGPNCTI PGLWTWLRNS LRPSPSFTHF LLTHGRWFWE FVNATFIREM LMRLVLTVRS
NLIPSPPTYN SAHDYISWES FSNVSYYTRI LPSVPKDCPT PMGTKGKKQL PDAQLLARRF
LLRRKFIPDP QGTNLMFAFF AQHFTHQFFK TSGKMGPGFT KALGHGVDLG HIYGDNLERQ
YQLRLFKDGK LKYQVLDGEM YPPSVEEAPV LMHYPRGIPP QSQMAVGQEV FGLLPGLMLY
ATLWLREHNR VCDLLKAEHP TWGDEQLFQT TRLILIGETI KIVIEEYVQQ LSGYFLQLKF
DPELLFGVQF QYRNRIAMEF NHLYHWHPLM PDSFKVGSQE YSYEQFLFNT SMLVDYGVEA
LVDAFSRQIA GRIGGGRNMD HHILHVAVDV IRESREMRLQ PFNEYRKRFG MKPYTSFQEL
VGEKEMAAEL EELYGDIDAL EFYPGLLLEK CHPNSIFGES MIEIGAPFSL KGLLGNPICS
PEYWKPSTFG GEVGFNIVKT ATLKKLVCLN TKTCPYVSFR VPDASQDDGP AVERPSTEL


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