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Q05769 (PGH2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prostaglandin G/H synthase 2

EC=1.14.99.1
Alternative name(s):
Cyclooxygenase-2
Short name=COX-2
Glucocorticoid-regulated inflammatory cyclooxygenase
Gripghs
Macrophage activation-associated marker protein P71/73
PES-2
PHS II
Prostaglandin H2 synthase 2
Short name=PGH synthase 2
Short name=PGHS-2
Prostaglandin-endoperoxide synthase 2
TIS10 protein
Gene names
Name:Ptgs2
Synonyms:Cox-2, Cox2, Pghs-b, Tis10
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length604 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates the formation of prostaglandins from arachidonate. May have a role as a major mediator of inflammation and/or a role for prostanoid signaling in activity-dependent plasticity. Critical component of colonic mucosal wound repair. Ref.10 Ref.14 Ref.15 Ref.16 Ref.17

Catalytic activity

Arachidonate + AH2 + 2 O2 = prostaglandin H2 + A + H2O. Ref.14 Ref.15 Ref.16 Ref.17

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group per subunit. Ref.11 Ref.14 Ref.15

Enzyme regulation

Inhibited by the nonsteroidal anti-inflammatory drugs aspirin, naproxen, diclofenac, meclofenamic acid, indomethacin and their analogs. Ref.14 Ref.16

Pathway

Lipid metabolism; prostaglandin biosynthesis.

Subunit structure

Homodimer. Ref.15

Subcellular location

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

Tissue specificity

Following colon injury, expressed in the wound bed mesenchyme during the first phase of repair, probably by colonic mesenchymal stem cells (at protein level). Ref.10

Developmental stage

During colonic wound repair, highly up-regulated (more than 1600-fold) in the mesenchyme of the wound bed 2 days after injury as compared to uninjured mucosa. Further increase in expression is observed at day 4 following injury (close to 2200-fold). Down-regulated at day 6 (only 93-fold increase as compared to uninjured mucosa). Ref.10

Induction

By cytokines and mitogens. Ref.14 Ref.16

Post-translational modification

S-nitrosylation by NOS2 (iNOS) activates enzyme activity. S-nitrosylation may take place on different Cys residues in addition to Cys-526 By similarity.

Disruption phenotype

Mutant mice exhibit defects in colonic mucosal wound repair. Ref.10

Miscellaneous

Acts both as a dioxygenase and as a peroxidase.

Target of nonsteroidal anti-inflammatory drugs, such as aspirin.

Sequence similarities

Belongs to the prostaglandin G/H synthase family.

Contains 1 EGF-like domain.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
Prostaglandin biosynthesis
Prostaglandin metabolism
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   DomainSignal
   LigandHeme
Iron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
Peroxidase
   PTMDisulfide bond
Glycoprotein
S-nitrosylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processanagen

Inferred from mutant phenotype PubMed 15713628. Source: MGI

angiogenesis

Inferred from electronic annotation. Source: Ensembl

bone mineralization

Inferred from sequence orthology PubMed 18519738. Source: MGI

brown fat cell differentiation

Inferred from mutant phenotype PubMed 20448152. Source: BHF-UCL

cellular response to ATP

Inferred from electronic annotation. Source: Ensembl

cellular response to UV

Inferred from electronic annotation. Source: Ensembl

cellular response to hypoxia

Inferred from electronic annotation. Source: Ensembl

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

cyclooxygenase pathway

Inferred from direct assay Ref.14. Source: UniProtKB

decidualization

Inferred from electronic annotation. Source: Ensembl

embryo implantation

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Inferred from electronic annotation. Source: Ensembl

keratinocyte differentiation

Non-traceable author statement PubMed 12067981. Source: UniProtKB

learning

Inferred from electronic annotation. Source: Ensembl

maintenance of blood-brain barrier

Inferred from electronic annotation. Source: Ensembl

memory

Inferred from electronic annotation. Source: Ensembl

negative regulation of calcium ion transport

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell cycle

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle contraction

Inferred from electronic annotation. Source: Ensembl

negative regulation of synaptic transmission, dopaminergic

Inferred from electronic annotation. Source: Ensembl

ovulation

Inferred from electronic annotation. Source: Ensembl

positive regulation of NF-kappaB import into nucleus

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of brown fat cell differentiation

Inferred from mutant phenotype PubMed 20448152. Source: BHF-UCL

positive regulation of cell migration involved in sprouting angiogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of fever generation

Inferred from direct assay PubMed 19940926. Source: BHF-UCL

positive regulation of fibroblast growth factor production

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric oxide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of platelet-derived growth factor production

Inferred from electronic annotation. Source: Ensembl

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of smooth muscle contraction

Inferred from electronic annotation. Source: Ensembl

positive regulation of synaptic plasticity

Inferred from electronic annotation. Source: Ensembl

positive regulation of synaptic transmission, glutamatergic

Inferred from electronic annotation. Source: Ensembl

positive regulation of transforming growth factor beta production

Inferred from electronic annotation. Source: Ensembl

positive regulation of vasoconstriction

Inferred from electronic annotation. Source: Ensembl

positive regulation vascular endothelial growth factor production

Inferred from electronic annotation. Source: Ensembl

prostaglandin biosynthetic process

Inferred from direct assay Ref.14. Source: UniProtKB

regulation of blood pressure

Inferred from mutant phenotype PubMed 12093889. Source: MGI

regulation of cell proliferation

Inferred from genetic interaction PubMed 10783317PubMed 10987272PubMed 11245490PubMed 11809702PubMed 8945508. Source: MGI

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to fatty acid

Inferred from electronic annotation. Source: Ensembl

response to fructose

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to lithium ion

Inferred from electronic annotation. Source: Ensembl

response to manganese ion

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from electronic annotation. Source: InterPro

response to tumor necrosis factor

Inferred from electronic annotation. Source: Ensembl

response to vitamin D

Inferred from electronic annotation. Source: Ensembl

sensory perception of pain

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 12021206. Source: MGI

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuron projection

Inferred from direct assay PubMed 12355421. Source: MGI

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionheme binding

Inferred from direct assay Ref.14. Source: UniProtKB

lipid binding

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen

Inferred from electronic annotation. Source: Ensembl

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

prostaglandin-endoperoxide synthase activity

Inferred from direct assay Ref.14. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.14. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717
Chain18 – 604587Prostaglandin G/H synthase 2
PRO_0000023876

Regions

Domain18 – 5538EGF-like

Sites

Active site1931Proton acceptor Ref.15
Active site3711For cyclooxygenase activity Ref.15
Metal binding3741Iron (heme axial ligand)
Binding site1061Substrate
Binding site3411Substrate
Binding site3711Substrate
Site5161Aspirin-acetylated serine
Site5921Not glycosylated

Amino acid modifications

Modified residue5261S-nitrosocysteine By similarity
Glycosylation531N-linked (GlcNAc...) Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17
CAR_000222
Glycosylation1301N-linked (GlcNAc...) Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17
CAR_000223
Glycosylation3961N-linked (GlcNAc...) Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17
CAR_000224
Glycosylation5801N-linked (GlcNAc...) Ref.9 Ref.15
CAR_000225
Disulfide bond21 ↔ 32 Ref.14 Ref.15 Ref.16
Disulfide bond22 ↔ 145 Ref.14 Ref.15 Ref.16
Disulfide bond26 ↔ 42 Ref.14 Ref.15 Ref.16
Disulfide bond44 ↔ 54 Ref.14 Ref.15 Ref.16
Disulfide bond555 ↔ 561 Ref.14 Ref.15 Ref.16

Experimental info

Mutagenesis5171L → A, F, P or T: Slightly reduced activity. Ref.15
Mutagenesis5801N → A: Loss of glycosylation site. Ref.15
Sequence conflict981I → T in AAA39924. Ref.1
Sequence conflict1421A → R in AAA39918. Ref.3
Sequence conflict3011I → L no nucleotide entry Ref.7
Sequence conflict5851H → R in AAA39918. Ref.3

Secondary structure

............................................................................................................. 604
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q05769 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: DFE1658295C92064

FASTA60469,013
        10         20         30         40         50         60 
MLFRAVLLCA ALGLSQAANP CCSNPCQNRG ECMSTGFDQY KCDCTRTGFY GENCTTPEFL 

        70         80         90        100        110        120 
TRIKLLLKPT PNTVHYILTH FKGVWNIVNN IPFLRSLIMK YVLTSRSYLI DSPPTYNVHY 

       130        140        150        160        170        180 
GYKSWEAFSN LSYYTRALPP VADDCPTPMG VKGNKELPDS KEVLEKVLLR REFIPDPQGS 

       190        200        210        220        230        240 
NMMFAFFAQH FTHQFFKTDH KRGPGFTRGL GHGVDLNHIY GETLDRQHKL RLFKDGKLKY 

       250        260        270        280        290        300 
QVIGGEVYPP TVKDTQVEMI YPPHIPENLQ FAVGQEVFGL VPGLMMYATI WLREHNRVCD 

       310        320        330        340        350        360 
ILKQEHPEWG DEQLFQTSRL ILIGETIKIV IEDYVQHLSG YHFKLKFDPE LLFNQQFQYQ 

       370        380        390        400        410        420 
NRIASEFNTL YHWHPLLPDT FNIEDQEYSF KQFLYNNSIL LEHGLTQFVE SFTRQIAGRV 

       430        440        450        460        470        480 
AGGRNVPIAV QAVAKASIDQ SREMKYQSLN EYRKRFSLKP YTSFEELTGE KEMAAELKAL 

       490        500        510        520        530        540 
YSDIDVMELY PALLVEKPRP DAIFGETMVE LGAPFSLKGL MGNPICSPQY WKPSTFGGEV 

       550        560        570        580        590        600 
GFKIINTASI QSLICNNVKG CPFTSFNVQD PQPTKTATIN ASASHSRLDD INPTVLIKRR 


STEL 

« Hide

References

« Hide 'large scale' references
[1]"TIS10, a phorbol ester tumor promoter-inducible mRNA from Swiss 3T3 cells, encodes a novel prostaglandin synthase/cyclooxygenase homologue."
Kujubu D.A., Fletcher B.S., Varnum B.C., Lim R.W., Herschman H.R.
J. Biol. Chem. 266:12866-12872(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Swiss.
[2]"Structure of the mitogen-inducible TIS10 gene and demonstration that the TIS10-encoded protein is a functional prostaglandin G/H synthase."
Fletcher B.S., Kujubu D.A., Perrin D.M., Herschman H.R.
J. Biol. Chem. 267:4338-4344(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Identification of an immediate early gene, pghs-B, whose protein product has prostaglandin synthase/cyclooxygenase activity."
Ryseck R.-P., Raynoschek C., Macdonald-Bravo H., Dorfman K., Mattei M.-G., Bravo R.
Cell Growth Differ. 3:443-450(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"cDNA cloning and functional activity of a glucocorticoid-regulated inflammatory cyclooxygenase."
O'Banion M.K., Winn V.D., Young D.A.
Proc. Natl. Acad. Sci. U.S.A. 89:4888-4892(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Hippocampus, Mammary gland and Spleen.
[6]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"A serum- and glucocorticoid-regulated 4-kilobase mRNA encodes a cyclooxygenase-related protein."
O'Banion M.K., Sadowski H.B., Winn V., Young D.A.
J. Biol. Chem. 266:23261-23267(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 281-360.
[8]"The mouse macrophage activation-associated marker protein, p71/73, is an inducible prostaglandin endoperoxide synthase (cyclooxygenase)."
Phillips T.A., Kujubu D.A., Mackay R.J., Herschman H.R., Russell S.W., Pace J.L.
J. Leukoc. Biol. 53:411-419(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[9]"N-glycosylation of prostaglandin endoperoxide synthases-1 and -2 and their orientations in the endoplasmic reticulum."
Otto J.C., Dewitt D.L., Smith W.L.
J. Biol. Chem. 268:18234-18242(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-53; ASN-130; ASN-396 AND ASN-580, ABSENCE OF GLYCOSYLATION AT ASN-592.
[10]"Igf2bp1 is required for full induction of Ptgs2 mRNA in colonic mesenchymal stem cells in mice."
Manieri N.A., Drylewicz M.R., Miyoshi H., Stappenbeck T.S.
Gastroenterology 143:110-121(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN INTESTINAL WOUND REPAIR, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[11]"Structural basis for selective inhibition of cyclooxygenase-2 by anti-inflammatory agents."
Kurumbail R.G., Stevens A.M., Gierse J.K., McDonald J.J., Stegeman R.A., Pay J.Y., Gildehaus D., Miyashiro J.M., Penning T.D., Seibert K., Isakson P.C., Stallings W.C.
Nature 384:644-648(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH (S)-FLURBIPROFEN; INDOMETHACIN; HEME AND 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE, COFACTOR, GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396.
[12]Erratum
Kurumbail R.G., Stevens A.M., Gierse J.K., McDonald J.J., Stegeman R.A., Pay J.Y., Gildehaus D., Miyashiro J.M., Penning T.D., Seibert K., Isakson P.C., Stallings W.C.
Nature 385:555-555(1997)
[13]"Structural insights into the stereochemistry of the cyclooxygenase reaction."
Kiefer J.R., Pawlitz J.L., Moreland K.T., Stegeman R.A., Hood W.F., Gierse J.K., Stevens A.M., Goodwin D.C., Rowlinson S.W., Marnett L.J., Stallings W.C., Kurumbail R.G.
Nature 405:97-101(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 18-569 IN COMPLEX WITH ARACHIDONIC ACID, GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396.
[14]"A novel mechanism of cyclooxygenase-2 inhibition involving interactions with Ser-530 and Tyr-385."
Rowlinson S.W., Kiefer J.R., Prusakiewicz J.J., Pawlitz J.L., Kozak K.R., Kalgutkar A.S., Stallings W.C., Kurumbail R.G., Marnett L.J.
J. Biol. Chem. 278:45763-45769(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH HEME AND DICLOFENAC, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, DISULFIDE BONDS, ENZYME REGULATION, GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396.
[15]"Structural basis of fatty acid substrate binding to cyclooxygenase-2."
Vecchio A.J., Simmons D.M., Malkowski M.G.
J. Biol. Chem. 285:22152-22163(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 20-604 IN COMPLEX WITH HEME; ACRYLIC ACID; ARACHIDONIC ACID AND DOCOSAHEXAENOIC ACID, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, COFACTOR, FUNCTION, DISULFIDE BONDS, MUTAGENESIS OF LEU-517 AND ASN-580, GLYCOSYLATION AT ASN-53; ASN-130; ASN-396 AND ASN-580.
[16]"Molecular basis for cyclooxygenase inhibition by the non-steroidal anti-inflammatory drug naproxen."
Duggan K.C., Walters M.J., Musee J., Harp J.M., Kiefer J.R., Oates J.A., Marnett L.J.
J. Biol. Chem. 285:34950-34959(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 18-604 IN COMPLEXES WITH HEME AND NAPROXEN ANALOGS, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, DISULFIDE BONDS, GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396.
[17]"The structural basis of endocannabinoid oxygenation by cyclooxygenase-2."
Vecchio A.J., Malkowski M.G.
J. Biol. Chem. 286:20736-20745(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 20-599 IN COMPLEX WITH HEME; ACRYLIC ACID AND ARACHIDONIC ACID, FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64291 mRNA. Translation: AAA39924.1.
M94967 mRNA. Translation: AAA39918.1.
M82866 expand/collapse EMBL AC list , M82862, M82863, M82864, M82865 Genomic DNA. Translation: AAA40448.1.
M88242 mRNA. Translation: AAA37740.1.
AK049923 mRNA. Translation: BAC33986.1.
AK144956 mRNA. Translation: BAE26154.1.
AK166221 mRNA. Translation: BAE38639.1.
AK172161 mRNA. Translation: BAE42855.1.
CH466520 Genomic DNA. Translation: EDL39487.1.
PIRA49010.
RefSeqNP_035328.2. NM_011198.3.
UniGeneMm.292547.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CVUX-ray2.40A/B18-569[»]
1CX2X-ray3.00A/B/C/D18-604[»]
1DCXmodel-A/B18-569[»]
1DD0model-A/B18-569[»]
1DDXX-ray3.00A/B/C/D18-569[»]
1PXXX-ray2.90A/B/C/D1-604[»]
3HS5X-ray2.10A/B20-604[»]
3HS6X-ray2.40A/B20-604[»]
3HS7X-ray2.65A/B20-604[»]
3KRKX-ray2.40A/B20-604[»]
3LN0X-ray2.20A/B/C/D18-604[»]
3LN1X-ray2.40A/B/C/D18-604[»]
3MDLX-ray2.20A/B20-599[»]
3MQEX-ray2.80A/B/C/D18-604[»]
3NT1X-ray1.73A/B18-604[»]
3NTBX-ray2.27A/B/C/D18-604[»]
3NTGX-ray2.19A/B/C/D18-569[»]
3OLTX-ray2.45A/B20-604[»]
3OLUX-ray2.35A/B20-604[»]
3PGHX-ray2.50A/B/C/D18-604[»]
3Q7DX-ray2.40A/B18-604[»]
3QH0X-ray2.10A/B1-604[»]
3QMOX-ray3.00A/B1-604[»]
3RR3X-ray2.84A/B/C/D18-577[»]
3TZIX-ray2.15A/B20-604[»]
4COXX-ray2.90A/B/C/D18-604[»]
4E1GX-ray2.10A/B1-604[»]
4FM5X-ray2.81A/B/C/D1-604[»]
4M10X-ray2.01A/B/C/D18-604[»]
4M11X-ray2.45A/B/C/D18-569[»]
4OTYX-ray2.35A/B18-604[»]
5COXX-ray3.00A/B/C/D18-604[»]
6COXX-ray2.80A/B18-604[»]
ProteinModelPortalQ05769.
SMRQ05769. Positions 18-569.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202463. 5 interactions.
DIPDIP-31082N.
IntActQ05769. 1 interaction.

Chemistry

BindingDBQ05769.
ChEMBLCHEMBL4321.

Protein family/group databases

PeroxiBase3360. MmPGHS02.

PTM databases

PhosphoSiteQ05769.
UniCarbKBQ05769.

Proteomic databases

PaxDbQ05769.
PRIDEQ05769.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035065; ENSMUSP00000035065; ENSMUSG00000032487.
GeneID19225.
KEGGmmu:19225.
UCSCuc007cxv.1. mouse.

Organism-specific databases

CTD5743.
MGIMGI:97798. Ptgs2.

Phylogenomic databases

eggNOGNOG39991.
GeneTreeENSGT00390000010743.
HOGENOMHOG000013149.
HOVERGENHBG000366.
InParanoidQ05769.
KOK11987.
OMAICNNVKG.
OrthoDBEOG7RFTHC.
PhylomeDBQ05769.
TreeFamTF329675.

Enzyme and pathway databases

UniPathwayUPA00662.

Gene expression databases

BgeeQ05769.
CleanExMM_PTGS2.
GenevestigatorQ05769.

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. 2 hits.
[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

EvolutionaryTraceQ05769.
NextBio296012.
PROQ05769.
SOURCESearch...

Entry information

Entry namePGH2_MOUSE
AccessionPrimary (citable) accession number: Q05769
Secondary accession number(s): Q543K3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot