Q05769 (PGH2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	604 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. 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.
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-561 By similarity.
Miscellaneous	This enzyme acts both as a dioxygenase and as a peroxidase. This enzyme is the 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 process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism Prostaglandin biosynthesis Prostaglandin metabolism
Cellular component	Endoplasmic reticulum Membrane Microsome
Domain	Signal
Ligand	Heme Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase Peroxidase
PTM	Disulfide bond Glycoprotein Phosphoprotein S-nitrosylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	anagen Inferred from mutant phenotype PubMed 15713628. Source: MGI angiogenesis Inferred from electronic annotation. Source: Compara 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: Compara cellular response to UV Inferred from electronic annotation. Source: Compara cellular response to hypoxia Inferred from electronic annotation. Source: Compara cellular response to mechanical stimulus Inferred from electronic annotation. Source: Compara cyclooxygenase pathway Inferred from direct assay Ref.14. Source: UniProtKB decidualization Inferred from electronic annotation. Source: Compara embryo implantation Inferred from electronic annotation. Source: Compara inflammatory response Inferred from electronic annotation. Source: Compara keratinocyte differentiation Non-traceable author statement PubMed 12067981. Source: UniProtKB learning Inferred from electronic annotation. Source: Compara maintenance of blood-brain barrier Inferred from electronic annotation. Source: Compara memory Inferred from electronic annotation. Source: Compara negative regulation of calcium ion transport Inferred from electronic annotation. Source: Compara negative regulation of cell cycle Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of smooth muscle contraction Inferred from electronic annotation. Source: Compara negative regulation of synaptic transmission, dopaminergic Inferred from electronic annotation. Source: Compara ovulation Inferred from electronic annotation. Source: Compara positive regulation of NF-kappaB import into nucleus Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara 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: Compara 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: Compara positive regulation of nitric oxide biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of platelet-derived growth factor production Inferred from electronic annotation. Source: Compara positive regulation of smooth muscle cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of smooth muscle contraction Inferred from electronic annotation. Source: Compara positive regulation of synaptic plasticity Inferred from electronic annotation. Source: Compara positive regulation of synaptic transmission, glutamatergic Inferred from electronic annotation. Source: Compara positive regulation of transforming growth factor beta production Inferred from electronic annotation. Source: Compara positive regulation of vasoconstriction Inferred from electronic annotation. Source: Compara positive regulation vascular endothelial growth factor production Inferred from electronic annotation. Source: Compara 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: Compara response to estradiol stimulus Inferred from electronic annotation. Source: Compara response to fatty acid Inferred from electronic annotation. Source: Compara response to fructose stimulus Inferred from electronic annotation. Source: Compara response to glucocorticoid stimulus Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara response to lithium ion Inferred from electronic annotation. Source: Compara response to manganese ion Inferred from electronic annotation. Source: Compara response to oxidative stress Inferred from electronic annotation. Source: InterPro response to tumor necrosis factor Inferred from electronic annotation. Source: Compara response to vitamin D Inferred from electronic annotation. Source: Compara sensory perception of pain Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm 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: Compara
Molecular_function	heme binding Inferred from direct assay Ref.14. Source: UniProtKB lipid binding Inferred from electronic annotation. Source: Compara 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: UniProtKB-KW peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW prostaglandin-endoperoxide synthase activity Inferred from direct assay Ref.14. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Chain

18 – 604

587

Prostaglandin G/H synthase 2

PRO_0000023876

Regions

Domain

18 – 55

38

EGF-like

Sites

Active site

193

1

Proton acceptor Ref.15

Active site

371

1

For cyclooxygenase activity Ref.15

Metal binding

374

1

Iron (heme axial ligand)

Binding site

106

1

Substrate

Binding site

341

1

Substrate

Binding site

371

1

Substrate

Site

516

1

Aspirin-acetylated serine

Site

592

1

Not glycosylated

Amino acid modifications

Modified residue

437

1

Phosphoserine Ref.10

Modified residue

446

1

Phosphotyrosine Ref.10

Modified residue

561

1

S-nitrosocysteine By similarity

Glycosylation

53

1

N-linked (GlcNAc...) Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17

CAR_000222

Glycosylation

130

1

N-linked (GlcNAc...) Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17

CAR_000223

Glycosylation

396

1

N-linked (GlcNAc...) Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17

CAR_000224

Glycosylation

580

1

N-linked (GlcNAc...) Ref.9 Ref.15

CAR_000225

Disulfide bond

21 ↔ 32

Ref.14 Ref.15 Ref.16

Disulfide bond

22 ↔ 145

Ref.14 Ref.15 Ref.16

Disulfide bond

26 ↔ 42

Ref.14 Ref.15 Ref.16

Disulfide bond

44 ↔ 54

Ref.14 Ref.15 Ref.16

Disulfide bond

555 ↔ 561

Ref.14 Ref.15 Ref.16

Experimental info

Mutagenesis

517

1

L → A, F, P or T: Slightly reduced activity. Ref.15

Mutagenesis

580

1

N → A: Loss of glycosylation site. Ref.15

Sequence conflict

98

1

I → T in AAA39924. Ref.1

Sequence conflict

142

1

A → R in AAA39918. Ref.3

Sequence conflict

301

1

I → L no nucleotide entry Ref.7

Sequence conflict

585

1

H → R in AAA39918. Ref.3

Secondary structure

1

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604

Helix Strand Turn

Details...

Turn

20 – 23

4

Helix

27 – 29

3

Beta strand

31 – 36

6

Beta strand

39 – 43

5

Beta strand

47 – 50

4

Turn

51 – 54

4

Helix

59 – 67

9

Helix

71 – 78

8

Helix

82 – 89

8

Helix

92 – 107

16

Beta strand

117 – 119

3

Beta strand

120 – 122

3

Helix

125 – 129

5

Beta strand

131 – 133

3

Beta strand

135 – 138

4

Beta strand

145 – 147

3

Beta strand

150 – 153

4

Helix

160 – 167

8

Helix

182 – 192

11

Turn

193 – 195

3

Turn

200 – 202

3

Beta strand

206 – 208

3

Beta strand

213 – 215

3

Helix

217 – 220

4

Helix

224 – 230

7

Beta strand

241 – 243

3

Beta strand

246 – 248

3

Helix

252 – 255

4

Beta strand

263 – 265

3

Helix

267 – 269

3

Turn

276 – 279

4

Helix

282 – 305

24

Helix

311 – 332

22

Helix

334 – 339

6

Helix

349 – 352

4

Helix

365 – 370

6

Helix

374 – 376

3

Beta strand

379 – 383

5

Beta strand

386 – 388

3

Helix

390 – 393

4

Helix

398 – 414

17

Beta strand

420 – 424

5

Helix

428 – 430

3

Helix

431 – 443

13

Helix

449 – 455

7

Helix

464 – 468

5

Beta strand

469 – 471

3

Helix

472 – 481

10

Helix

484 – 486

3

Helix

489 – 495

7

Beta strand

503 – 505

3

Helix

506 – 521

16

Helix

524 – 526

3

Turn

528 – 530

3

Helix

533 – 536

4

Helix

539 – 546

8

Helix

550 – 557

8

Beta strand

558 – 560

3

Sequences

	Sequence		Length	Mass (Da)
	Q05769 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: DFE1658295C92064	FASTA	604	69,013
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND TYR-446, MASS SPECTROMETRY. Tissue: Liver.
[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 , 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.

IPI

IPI00308785.

PIR

A49010.

RefSeq

NP_035328.2. NM_011198.3.

UniGene

Mm.292547.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CVU	X-ray	2.40	A/B	18-569	[»]
1CX2	X-ray	3.00	A/B/C/D	18-604	[»]
1DCX	model	-	A/B	18-569	[»]
1DD0	model	-	A/B	18-569	[»]
1DDX	X-ray	3.00	A/B/C/D	18-569	[»]
1PXX	X-ray	2.90	A/B/C/D	1-604	[»]
3HS5	X-ray	2.10	A/B	20-604	[»]
3HS6	X-ray	2.40	A/B	20-604	[»]
3HS7	X-ray	2.65	A/B	20-604	[»]
3KRK	X-ray	2.40	A/B	20-604	[»]
3LN0	X-ray	2.20	A/B/C/D	18-604	[»]
3LN1	X-ray	2.40	A/B/C/D	18-604	[»]
3MDL	X-ray	2.20	A/B	20-599	[»]
3MQE	X-ray	2.80	A/B/C/D	18-604	[»]
3NT1	X-ray	1.73	A/B	18-604	[»]
3NTB	X-ray	2.27	A/B/C/D	18-604	[»]
3NTG	X-ray	2.19	A/B/C/D	18-569	[»]
3OLT	X-ray	2.45	A/B	20-604	[»]
3OLU	X-ray	2.35	A/B	20-604	[»]
3PGH	X-ray	2.50	A/B/C/D	18-604	[»]
3Q7D	X-ray	2.40	A/B	18-604	[»]
3QH0	X-ray	2.10	A/B	1-604	[»]
3QMO	X-ray	3.00	A/B	1-604	[»]
3RR3	X-ray	2.84	A/B/C/D	18-577	[»]
3TZI	X-ray	2.15	A/B	20-604	[»]
4COX	X-ray	2.90	A/B/C/D	18-604	[»]
4E1G	X-ray	2.10	A/B	1-604	[»]
4FM5	X-ray	2.81	A/B/C/D	1-604	[»]
5COX	X-ray	3.00	A/B/C/D	18-604	[»]
6COX	X-ray	2.80	A/B	18-604	[»]

ProteinModelPortal

Q05769.

SMR

Q05769. Positions 18-569.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31082N.

IntAct

Q05769. 1 interaction.

Protein family/group databases

PeroxiBase

3360. MmPGHS02.

PTM databases

GlycoSuiteDB

Q05769.

PhosphoSite

Q05769.

Proteomic databases

PaxDb

Q05769.

PRIDE

Q05769.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000035065; ENSMUSP00000035065; ENSMUSG00000032487.

GeneID

19225.

KEGG

mmu:19225.

Organism-specific databases

CTD

5743.

MGI

MGI:97798. Ptgs2.

Phylogenomic databases

eggNOG

NOG39991.

GeneTree

ENSGT00390000010743.

HOGENOM

HOG000013149.

HOVERGEN

HBG000366.

InParanoid

Q05769.

KO

K11987.

OMA

THFKGVW.

OrthoDB

EOG4H19VF.

Enzyme and pathway databases

UniPathway

UPA00662.

Gene expression databases

Bgee

Q05769.

CleanEx

MM_PTGS2.

Genevestigator

Q05769.

GermOnline

ENSMUSG00000032487. Mus musculus.

Family and domain databases

Gene3D

1.10.640.10. 1 hit.

InterPro

IPR000742. EG-like_dom.
IPR010255. Haem_peroxidase.
IPR002007. Haem_peroxidase_animal.
IPR019791. Haem_peroxidase_animal_subgr.
[Graphical view]

Pfam

PF03098. An_peroxidase. 2 hits.
[Graphical view]

PRINTS

PR00457. ANPEROXIDASE.

SMART

SM00181. EGF. 1 hit.
[Graphical view]

SUPFAM

SSF48113. Peroxidase_super. 1 hit.

PROSITE

PS00022. EGF_1. False negative.
PS01186. EGF_2. False negative.
PS50026. EGF_3. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q05769.

ChEMBL

CHEMBL4321.

EvolutionaryTrace

Q05769.

NextBio

296012.

SOURCE

Search...

Entry information

Entry name

PGH2_MOUSE

Accession

Primary (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 3, 2013
This is version 147 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program