GenomeNet

Database: UniProt/SWISS-PROT
Entry: PGH1_HUMAN
LinkDB: PGH1_HUMAN
Original site: PGH1_HUMAN 
ID   PGH1_HUMAN              Reviewed;         599 AA.
AC   P23219; A8K1V7; B4DHQ2; B4E2S5; Q15122; Q3HY28; Q3HY29; Q5T7T6;
AC   Q5T7T7; Q5T7T8;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   25-APR-2018, entry version 197.
DE   RecName: Full=Prostaglandin G/H synthase 1;
DE            EC=1.14.99.1;
DE   AltName: Full=Cyclooxygenase-1;
DE            Short=COX-1;
DE   AltName: Full=Prostaglandin H2 synthase 1;
DE            Short=PGH synthase 1;
DE            Short=PGHS-1;
DE            Short=PHS 1;
DE   AltName: Full=Prostaglandin-endoperoxide synthase 1;
DE   Flags: Precursor;
GN   Name=PTGS1; Synonyms=COX1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT ARG-8.
RX   PubMed=2512924; DOI=10.1016/S0006-291X(89)80049-X;
RA   Yokoyama C., Tanabe T.;
RT   "Cloning of human gene encoding prostaglandin endoperoxide synthase
RT   and primary structure of the enzyme.";
RL   Biochem. Biophys. Res. Commun. 165:888-894(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF SER-529, AND
RP   VARIANT ARG-8.
RX   PubMed=1907252;
RA   Funk C.D., Funk L.B., Kennedy M.E., Pong A.S., Fitzgerald G.A.;
RT   "Human platelet/erythroleukemia cell prostaglandin G/H synthase: cDNA
RT   cloning, expression, and gene chromosomal assignment.";
RL   FASEB J. 5:2304-2312(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-8.
RC   TISSUE=Platelet;
RX   PubMed=1734857; DOI=10.1016/0006-291X(92)91750-K;
RA   Takahashi Y., Ueda N., Yoshimoto T., Yamamoto S., Yokoyama C.,
RA   Miyata A., Tanabe T., Fuse I., Hattori A., Shibata A.;
RT   "Immunoaffinity purification and cDNA cloning of human platelet
RT   prostaglandin endoperoxide synthase (cyclooxygenase).";
RL   Biochem. Biophys. Res. Commun. 182:433-438(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT ARG-8.
RC   TISSUE=Lung fibroblast;
RX   PubMed=1587858;
RA   Diaz A., Reginato A.M., Jimenez S.A.;
RT   "Alternative splicing of human prostaglandin G/H synthase mRNA and
RT   evidence of differential regulation of the resulting transcripts by
RT   transforming growth factor beta 1, interleukin 1 beta, and tumor
RT   necrosis factor alpha.";
RL   J. Biol. Chem. 267:10816-10822(1992).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6).
RX   PubMed=16141368; DOI=10.1124/jpet.105.090944;
RA   Qin N., Zhang S.P., Reitz T.L., Mei J.M., Flores C.M.;
RT   "Cloning, expression, and functional characterization of human
RT   cyclooxygenase-1 splicing variants: evidence for intron 1 retention.";
RL   J. Pharmacol. Exp. Ther. 315:1298-1305(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS ARG-8 AND
RP   LEU-17.
RX   PubMed=12192304; DOI=10.1097/00001721-200209000-00007;
RA   Scott B.T., Hasstedt S.J., Bovill E.G., Callas P.W., Valliere J.E.,
RA   Wang L.-H., Wu K.K., Long G.L.;
RT   "Characterization of the human prostaglandin H synthase 1 gene
RT   (PTGS1): exclusion by genetic linkage analysis as a second modifier
RT   gene in familial thrombosis.";
RL   Blood Coagul. Fibrinolysis 13:519-531(2002).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), AND
RP   VARIANT ARG-8.
RC   TISSUE=Caudate nucleus, Hippocampus, and Trachea;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS ARG-8;
RP   LEU-17; HIS-53; LEU-149 AND MET-237.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA   Rogers J., Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-8.
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-8.
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [12]
RP   REVIEW ON FUNCTION; TISSUE SPECIFICITY AND INHIBITION BY NSAIDS.
RX   PubMed=10966456; DOI=10.1146/annurev.biochem.69.1.145;
RA   Smith W.L., DeWitt D.L., Garavito R.M.;
RT   "Cyclooxygenases: structural, cellular, and molecular biology.";
RL   Annu. Rev. Biochem. 69:145-182(2000).
RN   [13]
RP   REVIEW ON FUNCTION; INHIBITION BY ASPIRIN AND INVOLVEMENT IN
RP   COLORECTAL CANCER.
RX   PubMed=24605250; DOI=10.4292/wjgpt.v5.i1.40;
RA   Sostres C., Gargallo C.J., Lanas A.;
RT   "Aspirin, cyclooxygenase inhibition and colorectal cancer.";
RL   World J. Gastrointest. Pharmacol. Ther. 5:40-49(2014).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [15]
RP   VARIANTS MET-237 AND ILE-481.
RX   PubMed=15308583; DOI=10.1093/carcin/bgh260;
RA   Goodman J.E., Bowman E.D., Chanock S.J., Alberg A.J., Harris C.C.;
RT   "Arachidonate lipoxygenase (ALOX) and cyclooxygenase (COX)
RT   polymorphisms and colon cancer risk.";
RL   Carcinogenesis 25:2467-2472(2004).
CC   -!- FUNCTION: Converts arachidonate to prostaglandin H2 (PGH2), a
CC       committed step in prostanoid synthesis. Involved in the
CC       constitutive production of prostanoids in particular in the
CC       stomach and platelets. In gastric epithelial cells, it is a key
CC       step in the generation of prostaglandins, such as prostaglandin E2
CC       (PGE2), which plays an important role in cytoprotection. In
CC       platelets, it is involved in the generation of thromboxane A2
CC       (TXA2), which promotes platelet activation and aggregation,
CC       vasoconstriction and proliferation of vascular smooth muscle
CC       cells.
CC   -!- CATALYTIC ACTIVITY: Arachidonate + AH(2) + 2 O(2) = prostaglandin
CC       H(2) + A + H(2)O.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
CC       subunit. {ECO:0000250};
CC   -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane
CC       protein. Endoplasmic reticulum membrane; Peripheral membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1; Synonyms=Long;
CC         IsoId=P23219-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short;
CC         IsoId=P23219-2; Sequence=VSP_004673;
CC       Name=3;
CC         IsoId=P23219-3; Sequence=VSP_053936, VSP_004673;
CC       Name=4;
CC         IsoId=P23219-4; Sequence=VSP_046932;
CC         Note=No experimental confirmation available.;
CC       Name=5; Synonyms=1b3;
CC         IsoId=P23219-5; Sequence=VSP_054862;
CC       Name=6; Synonyms=1b2;
CC         IsoId=P23219-6; Sequence=VSP_054863;
CC   -!- MISCELLANEOUS: The conversion of arachidonate to prostaglandin H2
CC       is a 2 step reaction: a cyclooxygenase (COX) reaction which
CC       converts arachidonate to prostaglandin G2 (PGG2) and a peroxidase
CC       reaction in which PGG2 is reduced to prostaglandin H2 (PGH2). The
CC       cyclooxygenase reaction occurs in a hydrophobic channel in the
CC       core of the enzyme. The peroxidase reaction occurs at a heme-
CC       containing active site located near the protein surface. The
CC       nonsteroidal anti-inflammatory drugs (NSAIDs) binding site
CC       corresponds to the cyclooxygenase active site.
CC   -!- MISCELLANEOUS: Conversion of arachidonate to prostaglandin H2 is
CC       mediated by 2 different isozymes: the constitutive PTGS1 and the
CC       inducible PTGS2. PGHS1 is expressed constitutively and generally
CC       produces prostanoids acutely in response to hormonal stimuli to
CC       fine-tune physiological processes requiring instantaneous,
CC       continuous regulation (e.g. hemostasis). PGHS2 is inducible and
CC       typically produces prostanoids that mediate responses to
CC       physiological stresses such as infection and inflammation.
CC   -!- MISCELLANEOUS: PTGS1 and PTGS2 are the targets of nonsteroidal
CC       anti-inflammatory drugs (NSAIDs) including aspirin and ibuprofen.
CC       Aspirin is able to produce an irreversible inactivation of the
CC       enzyme through a serine acetylation. Inhibition of the PGHSs with
CC       NSAIDs acutely reduces inflammation, pain, and fever, and long-
CC       term use of these drugs reduces fatal thrombotic events, as well
CC       as the development of colon cancer and Alzheimer's disease. PTGS2
CC       is the principal isozyme responsible for production of
CC       inflammatory prostaglandins. New generation PTGSs inhibitors
CC       strive to be selective for PTGS2, to avoid side effects such as
CC       gastrointestinal complications and ulceration.
CC   -!- SIMILARITY: Belongs to the prostaglandin G/H synthase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI14716.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/ptgs1/";
DR   EMBL; M31822; AAA36439.1; -; Genomic_DNA.
DR   EMBL; M31812; AAA36439.1; JOINED; Genomic_DNA.
DR   EMBL; M31813; AAA36439.1; JOINED; Genomic_DNA.
DR   EMBL; M31814; AAA36439.1; JOINED; Genomic_DNA.
DR   EMBL; M31815; AAA36439.1; JOINED; Genomic_DNA.
DR   EMBL; M31816; AAA36439.1; JOINED; Genomic_DNA.
DR   EMBL; M31817; AAA36439.1; JOINED; Genomic_DNA.
DR   EMBL; M31818; AAA36439.1; JOINED; Genomic_DNA.
DR   EMBL; M31819; AAA36439.1; JOINED; Genomic_DNA.
DR   EMBL; M31820; AAA36439.1; JOINED; Genomic_DNA.
DR   EMBL; M31821; AAA36439.1; JOINED; Genomic_DNA.
DR   EMBL; M59979; AAA03630.1; -; mRNA.
DR   EMBL; S78220; AAB21215.1; -; mRNA.
DR   EMBL; S36219; AAB22216.1; -; mRNA.
DR   EMBL; S36271; AAB22217.1; -; mRNA.
DR   EMBL; DQ180741; ABA60098.1; -; mRNA.
DR   EMBL; DQ180742; ABA60099.1; -; mRNA.
DR   EMBL; AF440204; AAL33601.1; -; Genomic_DNA.
DR   EMBL; AK290022; BAF82711.1; -; mRNA.
DR   EMBL; AK295221; BAG58214.1; -; mRNA.
DR   EMBL; AK304403; BAG65237.1; -; mRNA.
DR   EMBL; AY449688; AAR08907.1; -; Genomic_DNA.
DR   EMBL; AL162424; CAI14714.1; -; Genomic_DNA.
DR   EMBL; AL359636; CAI14714.1; JOINED; Genomic_DNA.
DR   EMBL; AL162424; CAI14715.1; -; Genomic_DNA.
DR   EMBL; AL359636; CAI14715.1; JOINED; Genomic_DNA.
DR   EMBL; AL162424; CAI14716.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL359636; CAM45740.1; -; Genomic_DNA.
DR   EMBL; AL162424; CAM45740.1; JOINED; Genomic_DNA.
DR   EMBL; AL359636; CAM45741.1; -; Genomic_DNA.
DR   EMBL; AL162424; CAM45741.1; JOINED; Genomic_DNA.
DR   EMBL; CH471090; EAW87530.1; -; Genomic_DNA.
DR   EMBL; BC029840; AAH29840.1; -; mRNA.
DR   CCDS; CCDS59520.1; -. [P23219-3]
DR   CCDS; CCDS59521.1; -. [P23219-4]
DR   CCDS; CCDS6842.1; -. [P23219-1]
DR   CCDS; CCDS6843.1; -. [P23219-2]
DR   PIR; JH0259; JH0259.
DR   RefSeq; NP_000953.2; NM_000962.3. [P23219-1]
DR   RefSeq; NP_001258094.1; NM_001271165.1. [P23219-4]
DR   RefSeq; NP_001258095.1; NM_001271166.1.
DR   RefSeq; NP_001258297.1; NM_001271368.1. [P23219-3]
DR   RefSeq; NP_542158.1; NM_080591.2. [P23219-2]
DR   RefSeq; XP_011517178.1; XM_011518876.2. [P23219-4]
DR   UniGene; Hs.201978; -.
DR   ProteinModelPortal; P23219; -.
DR   SMR; P23219; -.
DR   BioGrid; 111714; 6.
DR   CORUM; P23219; -.
DR   IntAct; P23219; 2.
DR   MINT; P23219; -.
DR   STRING; 9606.ENSP00000354612; -.
DR   BindingDB; P23219; -.
DR   ChEMBL; CHEMBL221; -.
DR   DrugBank; DB02773; (3-Chloro-4-Propoxy-Phenyl)-Acetic Acid.
DR   DrugBank; DB07983; 1-(4-IODOBENZOYL)-5-METHOXY-2-METHYL INDOLE-3-ACETIC ACID.
DR   DrugBank; DB07981; 2-[1-(4-CHLOROBENZOYL)-5-METHOXY-2-METHYL-1H-INDOL-3-YL]-N-[(1R)-1-(HYDROXYMETHYL)PROPYL]ACETAMIDE.
DR   DrugBank; DB07984; 2-[1-(4-CHLOROBENZOYL)-5-METHOXY-2-METHYL-1H-INDOL-3-YL]-N-[(1S)-1-(HYDROXYMETHYL)PROPYL]ACETAMIDE.
DR   DrugBank; DB02198; 2-Bromoacetyl Group.
DR   DrugBank; DB06736; Aceclofenac.
DR   DrugBank; DB00316; Acetaminophen.
DR   DrugBank; DB03667; Acetic Acid Salicyloyl-Amino-Ester.
DR   DrugBank; DB00945; Acetylsalicylic acid.
DR   DrugBank; DB01435; Antipyrine.
DR   DrugBank; DB01419; Antrafenine.
DR   DrugBank; DB04557; Arachidonic Acid.
DR   DrugBank; DB01014; Balsalazide.
DR   DrugBank; DB02379; Beta-D-Glucose.
DR   DrugBank; DB00963; Bromfenac.
DR   DrugBank; DB00796; Candesartan.
DR   DrugBank; DB00821; Carprofen.
DR   DrugBank; DB01136; Carvedilol.
DR   DrugBank; DB00672; Chlorpropamide.
DR   DrugBank; DB00250; Dapsone.
DR   DrugBank; DB00035; Desmopressin.
DR   DrugBank; DB00829; Diazepam.
DR   DrugBank; DB00586; Diclofenac.
DR   DrugBank; DB00711; Diethylcarbamazine.
DR   DrugBank; DB00861; Diflunisal.
DR   DrugBank; DB00154; Dihomo-gamma-linolenic acid.
DR   DrugBank; DB01075; Diphenhydramine.
DR   DrugBank; DB00470; Dronabinol.
DR   DrugBank; DB00216; Eletriptan.
DR   DrugBank; DB00402; Eszopiclone.
DR   DrugBank; DB00749; Etodolac.
DR   DrugBank; DB00773; Etoposide.
DR   DrugBank; DB00573; Fenoprofen.
DR   DrugBank; DB02266; Flufenamic Acid.
DR   DrugBank; DB00712; Flurbiprofen.
DR   DrugBank; DB03753; Flurbiprofen Methyl Ester.
DR   DrugBank; DB01355; Hexobarbital.
DR   DrugBank; DB00327; Hydromorphone.
DR   DrugBank; DB01892; Hyperforin.
DR   DrugBank; DB01050; Ibuprofen.
DR   DrugBank; DB00159; Icosapent.
DR   DrugBank; DB01181; Ifosfamide.
DR   DrugBank; DB00619; Imatinib.
DR   DrugBank; DB00328; Indomethacin.
DR   DrugBank; DB01029; Irbesartan.
DR   DrugBank; DB01221; Ketamine.
DR   DrugBank; DB06738; Ketobemidone.
DR   DrugBank; DB01009; Ketoprofen.
DR   DrugBank; DB00465; Ketorolac.
DR   DrugBank; DB06725; Lornoxicam.
DR   DrugBank; DB01283; Lumiracoxib.
DR   DrugBank; DB01397; Magnesium salicylate.
DR   DrugBank; DB00939; Meclofenamic acid.
DR   DrugBank; DB00784; Mefenamic acid.
DR   DrugBank; DB00814; Meloxicam.
DR   DrugBank; DB00244; Mesalazine.
DR   DrugBank; DB04817; Metamizole.
DR   DrugBank; DB00350; Minoxidil.
DR   DrugBank; DB00471; Montelukast.
DR   DrugBank; DB00461; Nabumetone.
DR   DrugBank; DB00788; Naproxen.
DR   DrugBank; DB00731; Nateglinide.
DR   DrugBank; DB05822; NCX 4016.
DR   DrugBank; DB06802; Nepafenac.
DR   DrugBank; DB04552; Niflumic Acid.
DR   DrugBank; DB00540; Nortriptyline.
DR   DrugBank; DB01837; O-acetyl-L-serine.
DR   DrugBank; DB00991; Oxaprozin.
DR   DrugBank; DB03752; P-(2'-Iodo-5'-Thenoyl)Hydrotropic Acid.
DR   DrugBank; DB03783; Phenacetin.
DR   DrugBank; DB00812; Phenylbutazone.
DR   DrugBank; DB01132; Pioglitazone.
DR   DrugBank; DB00554; Piroxicam.
DR   DrugBank; DB02110; Protoporphyrin Ix Containing Co.
DR   DrugBank; DB02709; Resveratrol.
DR   DrugBank; DB00533; Rofecoxib.
DR   DrugBank; DB00412; Rosiglitazone.
DR   DrugBank; DB00936; Salicylic acid.
DR   DrugBank; DB01399; Salsalate.
DR   DrugBank; DB01015; Sulfamethoxazole.
DR   DrugBank; DB00795; Sulfasalazine.
DR   DrugBank; DB00605; Sulindac.
DR   DrugBank; DB00870; Suprofen.
DR   DrugBank; DB00469; Tenoxicam.
DR   DrugBank; DB00857; Terbinafine.
DR   DrugBank; DB01041; Thalidomide.
DR   DrugBank; DB01600; Tiaprofenic acid.
DR   DrugBank; DB00500; Tolmetin.
DR   DrugBank; DB00214; Torasemide.
DR   DrugBank; DB05109; Trabectedin.
DR   DrugBank; DB08814; Triflusal.
DR   DrugBank; DB01401; Trisalicylate-choline.
DR   DrugBank; DB00313; Valproic Acid.
DR   DrugBank; DB00582; Voriconazole.
DR   DrugBank; DB00549; Zafirlukast.
DR   DrugBank; DB06737; Zaltoprofen.
DR   DrugBank; DB00744; Zileuton.
DR   DrugBank; DB00425; Zolpidem.
DR   DrugBank; DB01198; Zopiclone.
DR   GuidetoPHARMACOLOGY; 1375; -.
DR   SwissLipids; SLP:000001103; -.
DR   PeroxiBase; 3320; HsPGHS01.
DR   iPTMnet; P23219; -.
DR   PhosphoSitePlus; P23219; -.
DR   DMDM; 317373262; -.
DR   EPD; P23219; -.
DR   MaxQB; P23219; -.
DR   PaxDb; P23219; -.
DR   PeptideAtlas; P23219; -.
DR   PRIDE; P23219; -.
DR   DNASU; 5742; -.
DR   Ensembl; ENST00000223423; ENSP00000223423; ENSG00000095303. [P23219-2]
DR   Ensembl; ENST00000362012; ENSP00000354612; ENSG00000095303. [P23219-1]
DR   Ensembl; ENST00000373698; ENSP00000362802; ENSG00000095303. [P23219-4]
DR   Ensembl; ENST00000540753; ENSP00000437709; ENSG00000095303. [P23219-3]
DR   Ensembl; ENST00000619306; ENSP00000483540; ENSG00000095303. [P23219-6]
DR   GeneID; 5742; -.
DR   KEGG; hsa:5742; -.
DR   UCSC; uc004bmf.3; human. [P23219-1]
DR   CTD; 5742; -.
DR   DisGeNET; 5742; -.
DR   EuPathDB; HostDB:ENSG00000095303.14; -.
DR   GeneCards; PTGS1; -.
DR   HGNC; HGNC:9604; PTGS1.
DR   HPA; CAB020315; -.
DR   HPA; HPA002834; -.
DR   MIM; 176805; gene.
DR   neXtProt; NX_P23219; -.
DR   OpenTargets; ENSG00000095303; -.
DR   PharmGKB; PA24346; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   eggNOG; ENOG410XPZ3; LUCA.
DR   GeneTree; ENSGT00390000010743; -.
DR   HOGENOM; HOG000013149; -.
DR   HOVERGEN; HBG000366; -.
DR   InParanoid; P23219; -.
DR   KO; K00509; -.
DR   OMA; FKTSGKM; -.
DR   OrthoDB; EOG091G03CD; -.
DR   PhylomeDB; P23219; -.
DR   TreeFam; TF329675; -.
DR   BioCyc; MetaCyc:HS01815-MONOMER; -.
DR   BRENDA; 1.14.99.1; 2681.
DR   Reactome; R-HSA-140180; COX reactions.
DR   Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR   SIGNOR; P23219; -.
DR   UniPathway; UPA00662; -.
DR   ChiTaRS; PTGS1; human.
DR   GeneWiki; PTGS1; -.
DR   GenomeRNAi; 5742; -.
DR   PRO; PR:P23219; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   Bgee; ENSG00000095303; -.
DR   CleanEx; HS_PTGS1; -.
DR   ExpressionAtlas; P23219; baseline and differential.
DR   Genevisible; P23219; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; TAS:Reactome.
DR   GO; GO:0004666; F:prostaglandin-endoperoxide synthase activity; IDA:BHF-UCL.
DR   GO; GO:0019371; P:cyclooxygenase pathway; IDA:BHF-UCL.
DR   GO; GO:0006954; P:inflammatory response; IEA:InterPro.
DR   GO; GO:0001516; P:prostaglandin biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR   Gene3D; 1.10.640.10; -; 1.
DR   InterPro; IPR029580; COX-1.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR010255; Haem_peroxidase.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR037120; Haem_peroxidase_sf.
DR   PANTHER; PTHR11903:SF6; PTHR11903:SF6; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   Pfam; PF00008; EGF; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SUPFAM; SSF48113; SSF48113; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Dioxygenase; Disulfide bond;
KW   EGF-like domain; Endoplasmic reticulum; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Glycoprotein; Heme; Iron; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Metal-binding; Microsome; Oxidoreductase;
KW   Peroxidase; Polymorphism; Prostaglandin biosynthesis;
KW   Prostaglandin metabolism; Reference proteome; Signal.
FT   SIGNAL        1     23
FT   CHAIN        24    599       Prostaglandin G/H synthase 1.
FT                                /FTId=PRO_0000023868.
FT   DOMAIN       31     69       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   ACT_SITE    206    206       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00298}.
FT   ACT_SITE    384    384       For cyclooxygenase activity.
FT                                {ECO:0000250}.
FT   METAL       387    387       Iron (heme axial ligand).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00298}.
FT   SITE        529    529       Aspirin-acetylated serine.
FT   CARBOHYD     67     67       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    103    103       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    143    143       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     35     46       {ECO:0000250}.
FT   DISULFID     36    158       {ECO:0000250}.
FT   DISULFID     40     56       {ECO:0000250}.
FT   DISULFID     58     68       {ECO:0000250}.
FT   DISULFID    568    574       {ECO:0000250}.
FT   VAR_SEQ       1    109       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_046932.
FT   VAR_SEQ       1     32       MSRSLLLWFLLFLLLLPPLPVLLADPGAPTPV -> MRKPR
FT                                LM (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_053936.
FT   VAR_SEQ       1      3       MSR -> MSRECDPGARWGIFLASGGALNARLSPSSLSSAG
FT                                (in isoform 5).
FT                                {ECO:0000303|PubMed:16141368}.
FT                                /FTId=VSP_054862.
FT   VAR_SEQ       1      3       MSR -> MSRECDPGARWGIFLASWWSLECQLSPSSLSSAG
FT                                (in isoform 6).
FT                                {ECO:0000303|PubMed:16141368}.
FT                                /FTId=VSP_054863.
FT   VAR_SEQ     396    432       Missing (in isoform 2 and isoform 3).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:1587858}.
FT                                /FTId=VSP_004673.
FT   VARIANT       8      8       W -> R (in dbSNP:rs1236913).
FT                                {ECO:0000269|PubMed:12192304,
FT                                ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:1587858,
FT                                ECO:0000269|PubMed:1734857,
FT                                ECO:0000269|PubMed:1907252,
FT                                ECO:0000269|PubMed:2512924,
FT                                ECO:0000269|Ref.10, ECO:0000269|Ref.8}.
FT                                /FTId=VAR_013451.
FT   VARIANT      17     17       P -> L (in dbSNP:rs3842787).
FT                                {ECO:0000269|PubMed:12192304,
FT                                ECO:0000269|Ref.8}.
FT                                /FTId=VAR_013452.
FT   VARIANT      53     53       R -> H (in dbSNP:rs3842789).
FT                                {ECO:0000269|Ref.8}.
FT                                /FTId=VAR_019161.
FT   VARIANT     149    149       R -> L (in dbSNP:rs10306140).
FT                                {ECO:0000269|Ref.8}.
FT                                /FTId=VAR_019162.
FT   VARIANT     185    185       K -> T (in dbSNP:rs3842792).
FT                                /FTId=VAR_056663.
FT   VARIANT     237    237       L -> M (in dbSNP:rs5789).
FT                                {ECO:0000269|PubMed:15308583,
FT                                ECO:0000269|Ref.8}.
FT                                /FTId=VAR_019163.
FT   VARIANT     341    341       K -> R (in dbSNP:rs3842799).
FT                                /FTId=VAR_056664.
FT   VARIANT     359    359       K -> R (in dbSNP:rs5791).
FT                                /FTId=VAR_013453.
FT   VARIANT     443    443       I -> V (in dbSNP:rs5792).
FT                                /FTId=VAR_013454.
FT   VARIANT     481    481       V -> I (in dbSNP:rs5794).
FT                                {ECO:0000269|PubMed:15308583}.
FT                                /FTId=VAR_028017.
FT   MUTAGEN     529    529       S->N: Abolishes cyclooxygenase activity.
FT                                {ECO:0000269|PubMed:1907252}.
FT   CONFLICT     12     12       F -> L (in Ref. 1; AAA36439).
FT                                {ECO:0000305}.
FT   CONFLICT    113    113       R -> L (in Ref. 1; AAA36439).
FT                                {ECO:0000305}.
FT   CONFLICT    378    378       M -> T (in Ref. 1; AAA36439).
FT                                {ECO:0000305}.
FT   CONFLICT    423    423       D -> G (in Ref. 7; BAG65237).
FT                                {ECO:0000305}.
SQ   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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