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P23219 (PGH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 167. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prostaglandin G/H synthase 1

EC=1.14.99.1
Alternative name(s):
Cyclooxygenase-1
Short name=COX-1
Prostaglandin H2 synthase 1
Short name=PGH synthase 1
Short name=PGHS-1
Short name=PHS 1
Prostaglandin-endoperoxide synthase 1
Gene names
Name:PTGS1
Synonyms:COX1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length599 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 + AH2 + 2 O2 = prostaglandin H2 + A + H2O.

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity.

Pathway

Lipid metabolism; prostaglandin biosynthesis.

Subunit structure

Homodimer.

Subcellular location

Microsome membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein.

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.

Sequence similarities

Belongs to the prostaglandin G/H synthase family.

Contains 1 EGF-like domain.

Sequence caution

The sequence CAI14716.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
Prostaglandin biosynthesis
Prostaglandin metabolism
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainEGF-like domain
Signal
   LigandHeme
Iron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
Peroxidase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processarachidonic acid metabolic process

Traceable author statement. Source: Reactome

cyclooxygenase pathway

Inferred from direct assay PubMed 1380156. Source: BHF-UCL

lipid metabolic process

Non-traceable author statement Ref.2. Source: ProtInc

prostaglandin biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of blood pressure

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from electronic annotation. Source: InterPro

small molecule metabolic process

Traceable author statement. Source: Reactome

xenobiotic metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

intracellular membrane-bounded organelle

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

photoreceptor outer segment

Inferred from electronic annotation. Source: Ensembl

   Molecular_functiondioxygenase activity

Inferred from electronic annotation. Source: UniProtKB-KW

heme binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

peroxidase activity

Traceable author statement. Source: Reactome

prostaglandin-endoperoxide synthase activity

Inferred from direct assay PubMed 1380156. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P23219-1)

Also known as: Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P23219-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     396-432: Missing.
Isoform 3 (identifier: P23219-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: MSRSLLLWFLLFLLLLPPLPVLLADPGAPTPV → MRKPRLM
     396-432: Missing.
Isoform 4 (identifier: P23219-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-109: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: P23219-5)

Also known as: 1b3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MSR → MSRECDPGARWGIFLASGGALNARLSPSSLSSAG
Isoform 6 (identifier: P23219-6)

Also known as: 1b2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MSR → MSRECDPGARWGIFLASWWSLECQLSPSSLSSAG

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323
Chain24 – 599576Prostaglandin G/H synthase 1
PRO_0000023868

Regions

Domain31 – 6939EGF-like

Sites

Active site2061Proton acceptor By similarity
Active site3841For cyclooxygenase activity By similarity
Metal binding3871Iron (heme axial ligand) By similarity
Site5291Aspirin-acetylated serine

Amino acid modifications

Glycosylation671N-linked (GlcNAc...) Potential
Glycosylation1031N-linked (GlcNAc...) Potential
Glycosylation1431N-linked (GlcNAc...) Potential
Disulfide bond35 ↔ 46 By similarity
Disulfide bond36 ↔ 158 By similarity
Disulfide bond40 ↔ 56 By similarity
Disulfide bond58 ↔ 68 By similarity
Disulfide bond568 ↔ 574 By similarity

Natural variations

Alternative sequence1 – 109109Missing in isoform 4.
VSP_046932
Alternative sequence1 – 3232MSRSL…APTPV → MRKPRLM in isoform 3.
VSP_053936
Alternative sequence1 – 33MSR → MSRECDPGARWGIFLASGGA LNARLSPSSLSSAG in isoform 5.
VSP_054862
Alternative sequence1 – 33MSR → MSRECDPGARWGIFLASWWS LECQLSPSSLSSAG in isoform 6.
VSP_054863
Alternative sequence396 – 43237Missing in isoform 2 and isoform 3.
VSP_004673
Natural variant81W → R. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11
Corresponds to variant rs1236913 [ dbSNP | Ensembl ].
VAR_013451
Natural variant171P → L. Ref.6 Ref.8
Corresponds to variant rs3842787 [ dbSNP | Ensembl ].
VAR_013452
Natural variant531R → H. Ref.8
Corresponds to variant rs3842789 [ dbSNP | Ensembl ].
VAR_019161
Natural variant1491R → L. Ref.8
Corresponds to variant rs10306140 [ dbSNP | Ensembl ].
VAR_019162
Natural variant1851K → T.
Corresponds to variant rs3842792 [ dbSNP | Ensembl ].
VAR_056663
Natural variant2371L → M. Ref.8 Ref.14
Corresponds to variant rs5789 [ dbSNP | Ensembl ].
VAR_019163
Natural variant3411K → R.
Corresponds to variant rs3842799 [ dbSNP | Ensembl ].
VAR_056664
Natural variant3591K → R.
Corresponds to variant rs5791 [ dbSNP | Ensembl ].
VAR_013453
Natural variant4431I → V.
Corresponds to variant rs5792 [ dbSNP | Ensembl ].
VAR_013454
Natural variant4811V → I. Ref.14
Corresponds to variant rs5794 [ dbSNP | Ensembl ].
VAR_028017

Experimental info

Mutagenesis5291S → N: Abolishes cyclooxygenase activity. Ref.2
Sequence conflict121F → L in AAA36439. Ref.1
Sequence conflict1131R → L in AAA36439. Ref.1
Sequence conflict3781M → T in AAA36439. Ref.1
Sequence conflict4231D → G in BAG65237. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: 1F4F734BCD00346D

FASTA59968,686
        10         20         30         40         50         60 
MSRSLLLWFL LFLLLLPPLP VLLADPGAPT PVNPCCYYPC QHQGICVRFG LDRYQCDCTR 

        70         80         90        100        110        120 
TGYSGPNCTI PGLWTWLRNS LRPSPSFTHF LLTHGRWFWE FVNATFIREM LMRLVLTVRS 

       130        140        150        160        170        180 
NLIPSPPTYN SAHDYISWES FSNVSYYTRI LPSVPKDCPT PMGTKGKKQL PDAQLLARRF 

       190        200        210        220        230        240 
LLRRKFIPDP QGTNLMFAFF AQHFTHQFFK TSGKMGPGFT KALGHGVDLG HIYGDNLERQ 

       250        260        270        280        290        300 
YQLRLFKDGK LKYQVLDGEM YPPSVEEAPV LMHYPRGIPP QSQMAVGQEV FGLLPGLMLY 

       310        320        330        340        350        360 
ATLWLREHNR VCDLLKAEHP TWGDEQLFQT TRLILIGETI KIVIEEYVQQ LSGYFLQLKF 

       370        380        390        400        410        420 
DPELLFGVQF QYRNRIAMEF NHLYHWHPLM PDSFKVGSQE YSYEQFLFNT SMLVDYGVEA 

       430        440        450        460        470        480 
LVDAFSRQIA GRIGGGRNMD HHILHVAVDV IRESREMRLQ PFNEYRKRFG MKPYTSFQEL 

       490        500        510        520        530        540 
VGEKEMAAEL EELYGDIDAL EFYPGLLLEK CHPNSIFGES MIEIGAPFSL KGLLGNPICS 

       550        560        570        580        590 
PEYWKPSTFG GEVGFNIVKT ATLKKLVCLN TKTCPYVSFR VPDASQDDGP AVERPSTEL 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: 7AB78D6FD94F5FF1
Show »

FASTA56264,513
Isoform 3 [UniParc].

Checksum: 9AD6A32F6FE7CF05
Show »

FASTA53761,930
Isoform 4 [UniParc].

Checksum: 8C340B40B682E98C
Show »

FASTA49056,085
Isoform 5 (1b3) [UniParc].

Checksum: B70763422AC0C249
Show »

FASTA63071,717
Isoform 6 (1b2) [UniParc].

Checksum: 7A7080D69D5583C1
Show »

FASTA63072,010

References

« Hide 'large scale' references
[1]"Cloning of human gene encoding prostaglandin endoperoxide synthase and primary structure of the enzyme."
Yokoyama C., Tanabe T.
Biochem. Biophys. Res. Commun. 165:888-894(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT ARG-8.
[2]"Human platelet/erythroleukemia cell prostaglandin G/H synthase: cDNA cloning, expression, and gene chromosomal assignment."
Funk C.D., Funk L.B., Kennedy M.E., Pong A.S., Fitzgerald G.A.
FASEB J. 5:2304-2312(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF SER-529, VARIANT ARG-8.
[3]"Immunoaffinity purification and cDNA cloning of human platelet prostaglandin endoperoxide synthase (cyclooxygenase)."
Takahashi Y., Ueda N., Yoshimoto T., Yamamoto S., Yokoyama C., Miyata A., Tanabe T., Fuse I., Hattori A., Shibata A.
Biochem. Biophys. Res. Commun. 182:433-438(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-8.
Tissue: Platelet.
[4]"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."
Diaz A., Reginato A.M., Jimenez S.A.
J. Biol. Chem. 267:10816-10822(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT ARG-8.
Tissue: Lung fibroblast.
[5]"Cloning, expression, and functional characterization of human cyclooxygenase-1 splicing variants: evidence for intron 1 retention."
Qin N., Zhang S.P., Reitz T.L., Mei J.M., Flores C.M.
J. Pharmacol. Exp. Ther. 315:1298-1305(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6).
[6]"Characterization of the human prostaglandin H synthase 1 gene (PTGS1): exclusion by genetic linkage analysis as a second modifier gene in familial thrombosis."
Scott B.T., Hasstedt S.J., Bovill E.G., Callas P.W., Valliere J.E., Wang L.-H., Wu K.K., Long G.L.
Blood Coagul. Fibrinolysis 13:519-531(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS ARG-8 AND LEU-17.
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), VARIANT ARG-8.
Tissue: Caudate nucleus, Hippocampus and Trachea.
[8]SeattleSNPs variation discovery resource
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS ARG-8; LEU-17; HIS-53; LEU-149 AND MET-237.
[9]"DNA sequence and analysis of human chromosome 9."
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. expand/collapse author list , 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.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-8.
[11]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-8.
Tissue: Brain.
[12]"Cyclooxygenases: structural, cellular, and molecular biology."
Smith W.L., DeWitt D.L., Garavito R.M.
Annu. Rev. Biochem. 69:145-182(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION; TISSUE SPECIFICITY AND INHIBITION BY NSAIDS.
[13]"Aspirin, cyclooxygenase inhibition and colorectal cancer."
Sostres C., Gargallo C.J., Lanas A.
World J. Gastrointest. Pharmacol. Ther. 5:40-49(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION; INHIBITION BY ASPIRIN AND INVOLVEMENT IN COLORECTAL CANCER.
[14]"Arachidonate lipoxygenase (ALOX) and cyclooxygenase (COX) polymorphisms and colon cancer risk."
Goodman J.E., Bowman E.D., Chanock S.J., Alberg A.J., Harris C.C.
Carcinogenesis 25:2467-2472(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MET-237 AND ILE-481.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31822 expand/collapse EMBL AC list , M31812, M31813, M31814, M31815, M31816, M31817, M31818, M31819, M31820, M31821 Genomic DNA. Translation: AAA36439.1.
M59979 mRNA. Translation: AAA03630.1.
S78220 mRNA. Translation: AAB21215.1.
S36219 mRNA. Translation: AAB22216.1.
S36271 mRNA. Translation: AAB22217.1.
DQ180741 mRNA. Translation: ABA60098.1.
DQ180742 mRNA. Translation: ABA60099.1.
AF440204 Genomic DNA. Translation: AAL33601.1.
AK290022 mRNA. Translation: BAF82711.1.
AK295221 mRNA. Translation: BAG58214.1.
AK304403 mRNA. Translation: BAG65237.1.
AY449688 Genomic DNA. Translation: AAR08907.1.
AL162424, AL359636 Genomic DNA. Translation: CAI14714.1.
AL162424, AL359636 Genomic DNA. Translation: CAI14715.1.
AL162424 Genomic DNA. Translation: CAI14716.1. Sequence problems.
AL359636, AL162424 Genomic DNA. Translation: CAM45740.1.
AL359636, AL162424 Genomic DNA. Translation: CAM45741.1.
CH471090 Genomic DNA. Translation: EAW87530.1.
BC029840 mRNA. Translation: AAH29840.1.
CCDSCCDS59520.1. [P23219-3]
CCDS6842.1. [P23219-1]
CCDS6843.1. [P23219-2]
PIRJH0259.
RefSeqNP_000953.2. NM_000962.3. [P23219-1]
NP_001258094.1. NM_001271165.1. [P23219-4]
NP_001258095.1. NM_001271166.1.
NP_001258297.1. NM_001271368.1. [P23219-3]
NP_542158.1. NM_080591.2. [P23219-2]
XP_006717255.1. XM_006717192.1. [P23219-3]
UniGeneHs.201978.

3D structure databases

ProteinModelPortalP23219.
SMRP23219. Positions 31-583.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111714. 7 interactions.
IntActP23219. 1 interaction.
MINTMINT-4530066.
STRING9606.ENSP00000354612.

Chemistry

BindingDBP23219.
ChEMBLCHEMBL221.
DrugBankDB00316. Acetaminophen.
DB00945. Aspirin.
DB01014. Balsalazide.
DB00963. Bromfenac.
DB01188. Ciclopirox.
DB00586. Diclofenac.
DB00861. Diflunisal.
DB04817. Dipyrone.
DB00749. Etodolac.
DB00573. Fenoprofen.
DB00712. Flurbiprofen.
DB00154. gamma-Homolinolenic acid.
DB01050. Ibuprofen.
DB00159. Icosapent.
DB00328. Indomethacin.
DB01009. Ketoprofen.
DB00465. Ketorolac.
DB01283. Lumiracoxib.
DB00939. Meclofenamic acid.
DB00784. Mefenamic acid.
DB00244. Mesalazine.
DB00350. Minoxidil.
DB00461. Nabumetone.
DB00788. Naproxen.
DB03783. Phenacetin.
DB00554. Piroxicam.
DB00533. Rofecoxib.
DB00936. Salicyclic acid.
DB01399. Salsalate.
DB00605. Sulindac.
DB00870. Suprofen.
DB00469. Tenoxicam.
DB00500. Tolmetin.
GuidetoPHARMACOLOGY1375.

Protein family/group databases

PeroxiBase3320. HsPGHS01.

PTM databases

PhosphoSiteP23219.

Polymorphism databases

DMDM317373262.

Proteomic databases

MaxQBP23219.
PaxDbP23219.
PRIDEP23219.

Protocols and materials databases

DNASU5742.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000223423; ENSP00000223423; ENSG00000095303. [P23219-2]
ENST00000362012; ENSP00000354612; ENSG00000095303. [P23219-1]
ENST00000540753; ENSP00000437709; ENSG00000095303. [P23219-3]
GeneID5742.
KEGGhsa:5742.
UCSCuc004bmf.2. human. [P23219-2]
uc004bmg.2. human. [P23219-1]

Organism-specific databases

CTD5742.
GeneCardsGC09P125133.
HGNCHGNC:9604. PTGS1.
HPACAB020315.
HPA002834.
MIM176805. gene.
neXtProtNX_P23219.
PharmGKBPA24346.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39991.
HOGENOMHOG000013149.
HOVERGENHBG000366.
InParanoidP23219.
KOK00509.
OMAFKTSGKM.
OrthoDBEOG7RFTHC.
PhylomeDBP23219.
TreeFamTF329675.

Enzyme and pathway databases

BioCycMetaCyc:HS01815-MONOMER.
BRENDA1.14.99.1. 2681.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00662.

Gene expression databases

ArrayExpressP23219.
BgeeP23219.
CleanExHS_PTGS1.
GenevestigatorP23219.

Family and domain databases

Gene3D1.10.640.10. 1 hit.
InterProIPR000742. EG-like_dom.
IPR010255. Haem_peroxidase.
IPR002007. Haem_peroxidase_animal.
IPR019791. Haem_peroxidase_animal_subgr.
[Graphical view]
PfamPF03098. An_peroxidase. 1 hit.
[Graphical view]
PRINTSPR00457. ANPEROXIDASE.
SMARTSM00181. EGF. 1 hit.
[Graphical view]
SUPFAMSSF48113. SSF48113. 1 hit.
PROSITEPS50026. EGF_3. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTGS1. human.
GeneWikiPTGS1.
GenomeRNAi5742.
NextBio22352.
PROP23219.
SOURCESearch...

Entry information

Entry namePGH1_HUMAN
AccessionPrimary (citable) accession number: P23219
Secondary accession number(s): A8K1V7 expand/collapse secondary AC list , B4DHQ2, B4E2S5, Q15122, Q3HY28, Q3HY29, Q5T7T6, Q5T7T7, Q5T7T8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 167 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM