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P35354 (PGH2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·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
PHS II
Prostaglandin H2 synthase 2
Short name=PGH synthase 2
Short name=PGHS-2
Prostaglandin-endoperoxide synthase 2
Gene names
Name:PTGS2
Synonyms:COX2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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

Critical component of colonic mucosal wound repair By similarity. 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.13

Catalytic activity

Arachidonate + AH2 + 2 O2 = prostaglandin H2 + A + H2O. Ref.13

Cofactor

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

Pathway

Lipid metabolism; prostaglandin biosynthesis.

Subunit structure

Homodimer By similarity.

Subcellular location

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

Induction

By cytokines and mitogens.

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.

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.

Biophysicochemical properties

Kinetic parameters:

KM=16.2 µM for arachidonate (in absence of sodium nitroprusside NO donor) Ref.13

KM=17.0 µM for arachidonate (in presence of sodium nitroprusside NO donor)

Vmax=81.3 nmol/min/mg enzyme (in absence of sodium nitroprusside NO donor)

Vmax=132 nmol/min/mg enzyme (in absence of sodium nitroprusside NO donor)

Ontologies

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

Inferred from electronic annotation. Source: Ensembl

angiogenesis

Inferred from electronic annotation. Source: Ensembl

arachidonic acid metabolic process

Traceable author statement. Source: Reactome

bone mineralization

Inferred from electronic annotation. Source: Ensembl

brown fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

cellular component movement

Traceable author statement PubMed 9630216. Source: ProtInc

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 expression pattern PubMed 21296955. Source: UniProtKB

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

cyclooxygenase pathway

Inferred from direct assay Ref.2. Source: BHF-UCL

decidualization

Inferred from electronic annotation. Source: Ensembl

embryo implantation

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Inferred from electronic annotation. Source: Ensembl

learning

Inferred from electronic annotation. Source: Ensembl

lipoxygenase pathway

Traceable author statement. Source: Reactome

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 sequence or structural similarity PubMed 20448152. Source: BHF-UCL

positive regulation of cell migration involved in sprouting angiogenesis

Inferred from sequence or structural similarity PubMed 9630216. Source: BHF-UCL

positive regulation of fever generation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of fibroblast growth factor production

Inferred from sequence or structural similarity PubMed 9630216. Source: BHF-UCL

positive regulation of nitric oxide biosynthetic process

Inferred from sequence or structural similarity PubMed 9630216. Source: BHF-UCL

positive regulation of platelet-derived growth factor production

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of prostaglandin biosynthetic process

Non-traceable author statement PubMed 20448152. Source: BHF-UCL

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 sequence or structural similarity PubMed 9630216. Source: BHF-UCL

positive regulation of vasoconstriction

Inferred from electronic annotation. Source: Ensembl

positive regulation vascular endothelial growth factor production

Inferred from sequence or structural similarity PubMed 9630216. Source: BHF-UCL

prostaglandin biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

prostaglandin metabolic process

Traceable author statement PubMed 9630216. Source: ProtInc

regulation of blood pressure

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of inflammatory response

Non-traceable author statement PubMed 14511332. Source: UniProtKB

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

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 14511332. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

neuron projection

Inferred from direct assay PubMed 12355421. Source: MGI

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionarachidonate 15-lipoxygenase activity

Traceable author statement. Source: Reactome

enzyme binding

Inferred from physical interaction Ref.13. Source: UniProtKB

heme binding

Inferred from sequence or structural similarity. Source: UniProtKB

lipid binding

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

peroxidase activity

Non-traceable author statement PubMed 14511332. Source: UniProtKB

prostaglandin-endoperoxide synthase activity

Inferred from direct assay Ref.13. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 604587Prostaglandin G/H synthase 2
PRO_0000023875

Regions

Domain18 – 5538EGF-like

Sites

Active site1931Proton acceptor By similarity
Active site3711For cyclooxygenase activity By similarity
Metal binding3741Iron (heme axial ligand) By similarity
Binding site1061Substrate By similarity
Binding site3411Substrate By similarity
Binding site3711Substrate By similarity
Site5161Aspirin-acetylated serine By similarity

Amino acid modifications

Modified residue5261S-nitrosocysteine Probable
Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation1301N-linked (GlcNAc...) Potential
Glycosylation3961N-linked (GlcNAc...) Potential
Glycosylation5801N-linked (GlcNAc...) Ref.14
Disulfide bond21 ↔ 32 By similarity
Disulfide bond22 ↔ 145 By similarity
Disulfide bond26 ↔ 42 By similarity
Disulfide bond44 ↔ 54 By similarity
Disulfide bond555 ↔ 561 By similarity

Natural variations

Natural variant2281R → H. Ref.6
Corresponds to variant rs3218622 [ dbSNP | Ensembl ].
VAR_016262
Natural variant4281P → A. Ref.6
Corresponds to variant rs4648279 [ dbSNP | Ensembl ].
VAR_016263
Natural variant4881E → G.
Corresponds to variant rs5272 [ dbSNP | Ensembl ].
VAR_011980
Natural variant5111V → A. Ref.6 Ref.15
Corresponds to variant rs5273 [ dbSNP | Ensembl ].
VAR_011981
Natural variant5871G → R. Ref.6
Corresponds to variant rs3218625 [ dbSNP | Ensembl ].
VAR_016264

Experimental info

Mutagenesis5261C → S: Prevents activation by nitric oxid (NO). Ref.13
Mutagenesis5551C → S: Abolishes enzyme activity. Ref.13
Mutagenesis5611C → S: Does not affect activation by nitric oxid (NO). Ref.13
Sequence conflict1651E → G in AAA58433. Ref.2
Sequence conflict4381I → T in AAA35803. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P35354 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: 72FBD699F6128519

FASTA60468,996
        10         20         30         40         50         60 
MLARALLLCA VLALSHTANP CCSHPCQNRG VCMSVGFDQY KCDCTRTGFY GENCSTPEFL 

        70         80         90        100        110        120 
TRIKLFLKPT PNTVHYILTH FKGFWNVVNN IPFLRNAIMS YVLTSRSHLI DSPPTYNADY 

       130        140        150        160        170        180 
GYKSWEAFSN LSYYTRALPP VPDDCPTPLG VKGKKQLPDS NEIVEKLLLR RKFIPDPQGS 

       190        200        210        220        230        240 
NMMFAFFAQH FTHQFFKTDH KRGPAFTNGL GHGVDLNHIY GETLARQRKL RLFKDGKMKY 

       250        260        270        280        290        300 
QIIDGEMYPP TVKDTQAEMI YPPQVPEHLR FAVGQEVFGL VPGLMMYATI WLREHNRVCD 

       310        320        330        340        350        360 
VLKQEHPEWG DEQLFQTSRL ILIGETIKIV IEDYVQHLSG YHFKLKFDPE LLFNKQFQYQ 

       370        380        390        400        410        420 
NRIAAEFNTL YHWHPLLPDT FQIHDQKYNY QQFIYNNSIL LEHGITQFVE SFTRQIAGRV 

       430        440        450        460        470        480 
AGGRNVPPAV QKVSQASIDQ SRQMKYQSFN EYRKRFMLKP YESFEELTGE KEMSAELEAL 

       490        500        510        520        530        540 
YGDIDAVELY PALLVEKPRP DAIFGETMVE VGAPFSLKGL MGNVICSPAY WKPSTFGGEV 

       550        560        570        580        590        600 
GFQIINTASI QSLICNNVKG CPFTSFSVPD PELIKTVTIN ASSSRSGLDD INPTVLLKER 


STEL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of human prostaglandin endoperoxide synthase type II and demonstration of expression in response to cytokines."
Jones D.A., Carlton D.P., McIntyre T.M., Zimmerman G.A., Prescott S.M.
J. Biol. Chem. 268:9049-9054(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Endothelial cell.
[2]"Human cyclooxygenase-2 cDNA."
Hla T., Neilson K.
Proc. Natl. Acad. Sci. U.S.A. 89:7384-7388(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Endothelial cell.
[3]"Characterization of the human gene (PTGS2) encoding prostaglandin-endoperoxide synthase 2."
Kosaka T., Miyata A., Ihara H., Hara S., Sugimoto T., Takeda O., Takahashi E., Tanabe T.
Eur. J. Biochem. 221:889-897(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Peripheral blood.
[4]"Structure of the human cyclo-oxygenase-2 gene."
Appleby S.B., Ristimaki A., Neilson K., Narko K., Hla T.
Biochem. J. 302:723-727(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Placenta.
[5]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Sharma S.V., Aronstam R.S.
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[6]NIEHS SNPs program
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-228; ALA-428; ALA-511 AND ARG-587.
[7]SeattleSNPs variation discovery resource
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"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].
Tissue: Synovium.
[9]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [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].
[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].
Tissue: Lung.
[12]"Purification, characterization and selective inhibition of human prostaglandin G/H synthase 1 and 2 expressed in the baculovirus system."
Barnett J., Chow J., Ives D., Chiou M., Mackenzie R., Osen E., Nguyen B., Tsing S., Bach C., Freire J.
Biochim. Biophys. Acta 1209:130-139(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[13]"Inducible nitric oxide synthase binds, S-nitrosylates, and activates cyclooxygenase-2."
Kim S.F., Huri D.A., Snyder S.H.
Science 310:1966-1970(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, S-NITROSYLATION AT CYS-526, MUTAGENESIS OF CYS-526; CYS-555 AND CYS-561.
[14]"Glycosylation regulates turnover of cyclooxygenase-2."
Sevigny M.B., Li C.F., Alas M., Hughes-Fulford M.
FEBS Lett. 580:6533-6536(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-580.
[15]"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: VARIANT ALA-511.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L15326 mRNA. Translation: AAA35803.1.
M90100 mRNA. Translation: AAA58433.1.
D28235 Genomic DNA. Translation: BAA05698.1.
U04636 Genomic DNA. Translation: AAA57317.1.
AY462100 mRNA. Translation: AAR23927.1.
AY229989 Genomic DNA. Translation: AAO38056.1.
AY382629 Genomic DNA. Translation: AAQ75702.1.
AK292167 mRNA. Translation: BAF84856.1.
AL033533 Genomic DNA. Translation: CAB41240.1.
CH471067 Genomic DNA. Translation: EAW91216.1.
BC013734 mRNA. Translation: AAH13734.1.
PIRA46150.
RefSeqNP_000954.1. NM_000963.3.
UniGeneHs.196384.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1V0Xmodel-A1-604[»]
ProteinModelPortalP35354.
SMRP35354. Positions 18-568.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111715. 27 interactions.
DIPDIP-28131N.
IntActP35354. 1 interaction.
MINTMINT-203337.
STRING9606.ENSP00000356438.

Chemistry

BindingDBP35354.
ChEMBLCHEMBL230.
DrugBankDB00316. Acetaminophen.
DB00945. Aspirin.
DB01014. Balsalazide.
DB00963. Bromfenac.
DB00821. Carprofen.
DB00482. Celecoxib.
DB01188. Ciclopirox.
DB00586. Diclofenac.
DB00861. Diflunisal.
DB01240. Epoprostenol.
DB00749. Etodolac.
DB01628. Etoricoxib.
DB00573. Fenoprofen.
DB00712. Flurbiprofen.
DB00154. gamma-Homolinolenic acid.
DB01404. Ginseng.
DB01050. Ibuprofen.
DB00159. Icosapent.
DB00328. Indomethacin.
DB01009. Ketoprofen.
DB00465. Ketorolac.
DB00480. Lenalidomide.
DB01283. Lumiracoxib.
DB00939. Meclofenamic acid.
DB00784. Mefenamic acid.
DB00814. Meloxicam.
DB00244. Mesalazine.
DB00461. Nabumetone.
DB00788. Naproxen.
DB00991. Oxaprozin.
DB00812. Phenylbutazone.
DB00533. Rofecoxib.
DB00936. Salicyclic acid.
DB01399. Salsalate.
DB00605. Sulindac.
DB00870. Suprofen.
DB00469. Tenoxicam.
DB01041. Thalidomide.
DB01600. Tiaprofenic acid.
DB00500. Tolmetin.
DB00580. Valdecoxib.
GuidetoPHARMACOLOGY1376.

Protein family/group databases

PeroxiBase3321. HsPGHS02.

PTM databases

PhosphoSiteP35354.

Polymorphism databases

DMDM3915797.

Proteomic databases

PaxDbP35354.
PRIDEP35354.

Protocols and materials databases

DNASU5743.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367468; ENSP00000356438; ENSG00000073756.
GeneID5743.
KEGGhsa:5743.
UCSCuc001gsb.3. human.

Organism-specific databases

CTD5743.
GeneCardsGC01M186640.
HGNCHGNC:9605. PTGS2.
HPACAB000113.
HPA001335.
MIM600262. gene.
neXtProtNX_P35354.
PharmGKBPA293.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39991.
HOGENOMHOG000013149.
HOVERGENHBG000366.
InParanoidP35354.
KOK11987.
OMAICNNVKG.
OrthoDBEOG7RFTHC.
PhylomeDBP35354.
TreeFamTF329675.

Enzyme and pathway databases

BioCycMetaCyc:HS01115-MONOMER.
BRENDA1.14.99.1. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKP35354.
UniPathwayUPA00662.

Gene expression databases

ArrayExpressP35354.
BgeeP35354.
CleanExHS_PTGS2.
GenevestigatorP35354.

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

GeneWikiProstaglandin-endoperoxide_synthase_2.
PTGS2.
GenomeRNAi5743.
NextBio22358.
PROP35354.
SOURCESearch...

Entry information

Entry namePGH2_HUMAN
AccessionPrimary (citable) accession number: P35354
Secondary accession number(s): A8K802, Q16876
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 15, 1998
Last modified: April 16, 2014
This is version 156 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 1

Human chromosome 1: entries, gene names and cross-references to MIM