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Prostaglandin G/H synthase 2 (EC 1.14.99.1) (Cyclooxygenase-2) (COX-2) (PHS II) (Prostaglandin H2 synthase 2) (PGH synthase 2) (PGHS-2) (Prostaglandin-endoperoxide synthase 2)

 PGH2_HUMAN              Reviewed;         604 AA.
P35354; A8K802; Q16876;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 2.
03-JUL-2019, entry version 205.
RecName: Full=Prostaglandin G/H synthase 2;
EC=1.14.99.1 {ECO:0000269|PubMed:16373578, ECO:0000269|PubMed:26859324, ECO:0000269|PubMed:27226593};
AltName: Full=Cyclooxygenase-2;
Short=COX-2;
AltName: Full=PHS II;
AltName: Full=Prostaglandin H2 synthase 2;
Short=PGH synthase 2;
Short=PGHS-2;
AltName: Full=Prostaglandin-endoperoxide synthase 2;
Flags: Precursor;
Name=PTGS2; Synonyms=COX2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Endothelial cell;
PubMed=8473346;
Jones D.A., Carlton D.P., McIntyre T.M., Zimmerman G.A.,
Prescott S.M.;
"Molecular cloning of human prostaglandin endoperoxide synthase type
II and demonstration of expression in response to cytokines.";
J. Biol. Chem. 268:9049-9054(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Endothelial cell;
PubMed=1380156; DOI=10.1073/pnas.89.16.7384;
Hla T., Neilson K.;
"Human cyclooxygenase-2 cDNA.";
Proc. Natl. Acad. Sci. U.S.A. 89:7384-7388(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Peripheral blood;
PubMed=8181472; DOI=10.1111/j.1432-1033.1994.tb18804.x;
Kosaka T., Miyata A., Ihara H., Hara S., Sugimoto T., Takeda O.,
Takahashi E., Tanabe T.;
"Characterization of the human gene (PTGS2) encoding prostaglandin-
endoperoxide synthase 2.";
Eur. J. Biochem. 221:889-897(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=7945196; DOI=10.1042/bj3020723;
Appleby S.B., Ristimaki A., Neilson K., Narko K., Hla T.;
"Structure of the human cyclo-oxygenase-2 gene.";
Biochem. J. 302:723-727(1994).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
Sharma S.V., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-228; ALA-428;
ALA-511 AND ARG-587.
NIEHS SNPs program;
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Synovium;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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., 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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
CHARACTERIZATION.
PubMed=7947975; DOI=10.1016/0167-4838(94)90148-1;
Barnett J., Chow J., Ives D., Chiou M., Mackenzie R., Osen E.,
Nguyen B., Tsing S., Bach C., Freire J.;
"Purification, characterization and selective inhibition of human
prostaglandin G/H synthase 1 and 2 expressed in the baculovirus
system.";
Biochim. Biophys. Acta 1209:130-139(1994).
[13]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
S-NITROSYLATION AT CYS-526, AND MUTAGENESIS OF CYS-526; CYS-555 AND
CYS-561.
PubMed=16373578; DOI=10.1126/science.1119407;
Kim S.F., Huri D.A., Snyder S.H.;
"Inducible nitric oxide synthase binds, S-nitrosylates, and activates
cyclooxygenase-2.";
Science 310:1966-1970(2005).
[14]
GLYCOSYLATION AT ASN-580.
PubMed=17113084; DOI=10.1016/j.febslet.2006.10.073;
Sevigny M.B., Li C.F., Alas M., Hughes-Fulford M.;
"Glycosylation regulates turnover of cyclooxygenase-2.";
FEBS Lett. 580:6533-6536(2006).
[15]
REVIEW ON FUNCTION; TISSUE SPECIFICITY AND INHIBITION BY NSAIDS.
PubMed=10966456; DOI=10.1146/annurev.biochem.69.1.145;
Smith W.L., DeWitt D.L., Garavito R.M.;
"Cyclooxygenases: structural, cellular, and molecular biology.";
Annu. Rev. Biochem. 69:145-182(2000).
[16]
REVIEW ON FUNCTION; INHIBITION BY ASPIRIN AND INVOLVEMENT IN
COLORECTAL CANCER.
PubMed=24605250; DOI=10.4292/wjgpt.v5.i1.40;
Sostres C., Gargallo C.J., Lanas A.;
"Aspirin, cyclooxygenase inhibition and colorectal cancer.";
World J. Gastrointest. Pharmacol. Ther. 5:40-49(2014).
[17] {ECO:0000244|PDB:5KIR}
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 19-569 IN COMPLEX WITH
PROTOPORPHYRIN IX AND ROFECOXIB, COFACTOR, GLYCOSYLATION AT ASN-130
AND ASN-396, AND DISULFIDE BONDS.
PubMed=27710942; DOI=10.1107/S2053230X16014230;
Orlando B.J., Malkowski M.G.;
"Crystal structure of rofecoxib bound to human cyclooxygenase-2.";
Acta Crystallogr. F 72:772-776(2016).
[18] {ECO:0000244|PDB:5F19, ECO:0000244|PDB:5F1A}
X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 19-569 IN COMPLEX WITH
PROTOPORPHYRIN IX AND SALICYLIC ACID, FUNCTION, CATALYTIC ACTIVITY,
COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF
SER-516 AND GLY-519, ACTIVITY REGULATION, GLYCOSYLATION AT ASN-53;
ASN-130 AND ASN-396, AND DISULFIDE BONDS.
PubMed=26859324; DOI=10.1021/acs.biochem.5b01378;
Lucido M.J., Orlando B.J., Vecchio A.J., Malkowski M.G.;
"Crystal Structure of Aspirin-Acetylated Human Cyclooxygenase-2:
Insight into the Formation of Products with Reversed
Stereochemistry.";
Biochemistry 55:1226-1238(2016).
[19] {ECO:0000244|PDB:5IKQ, ECO:0000244|PDB:5IKR, ECO:0000244|PDB:5IKT, ECO:0000244|PDB:5IKV}
X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS) OF 19-569 IN COMPLEX WITH
PROTOPORPHYRIN IX AND FLUFENAMIC ACID, FUNCTION, CATALYTIC ACTIVITY,
ACTIVITY REGULATION, COFACTOR, SUBUNIT, GLYCOSYLATION AT ASN-53;
ASN-130 AND ASN-396, DISULFIDE BONDS, AND MUTAGENESIS OF TYR-371 AND
SER-516.
PubMed=27226593; DOI=10.1074/jbc.M116.725713;
Orlando B.J., Malkowski M.G.;
"Substrate-selective Inhibition of Cyclooxygeanse-2 by Fenamic Acid
Derivatives Is Dependent on Peroxide Tone.";
J. Biol. Chem. 291:15069-15081(2016).
[20]
VARIANT ALA-511.
PubMed=15308583; DOI=10.1093/carcin/bgh260;
Goodman J.E., Bowman E.D., Chanock S.J., Alberg A.J., Harris C.C.;
"Arachidonate lipoxygenase (ALOX) and cyclooxygenase (COX)
polymorphisms and colon cancer risk.";
Carcinogenesis 25:2467-2472(2004).
-!- FUNCTION: Converts arachidonate to prostaglandin H2 (PGH2), a
committed step in prostanoid synthesis (PubMed:26859324,
PubMed:27226593). Constitutively expressed in some tissues in
physiological conditions, such as the endothelium, kidney and
brain, and in pathological conditions, such as in cancer. PTGS2 is
responsible for production of inflammatory prostaglandins. Up-
regulation of PTGS2 is also associated with increased cell
adhesion, phenotypic changes, resistance to apoptosis and tumor
angiogenesis. In cancer cells, PTGS2 is a key step in the
production of prostaglandin E2 (PGE2), which plays important roles
in modulating motility, proliferation and resistance to apoptosis.
During neuroinflammation, plays a role in neuronal secretion of
specialized preresolving mediators (SPMs), especially 15-R-lipoxin
A4, that regulates phagocytic microglia (By similarity).
{ECO:0000250|UniProtKB:Q05769, ECO:0000269|PubMed:16373578,
ECO:0000269|PubMed:26859324, ECO:0000269|PubMed:27226593}.
-!- CATALYTIC ACTIVITY:
Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + 2 O2 = A + H2O
+ prostaglandin H2; Xref=Rhea:RHEA:23728, ChEBI:CHEBI:13193,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
ChEBI:CHEBI:32395, ChEBI:CHEBI:57405; EC=1.14.99.1;
Evidence={ECO:0000269|PubMed:16373578,
ECO:0000269|PubMed:26859324, ECO:0000269|PubMed:27226593};
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000269|PubMed:26859324,
ECO:0000269|PubMed:27226593, ECO:0000269|PubMed:27710942};
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
subunit. {ECO:0000269|PubMed:26859324,
ECO:0000269|PubMed:27226593, ECO:0000269|PubMed:27710942};
-!- ACTIVITY REGULATION: Inhibited by nonsteroidal anti-inflammatory
drugs (NSAIDs) including aspirin, ibuprofen, flurbiprofen and
celecoxib (PubMed:26859324). Inhibited by flufenamic acid,
mefenamic acid and tolfenamic acid (PubMed:27226593).
{ECO:0000269|PubMed:26859324, ECO:0000269|PubMed:27226593}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=16.2 uM for arachidonate (in absence of sodium nitroprusside
NO donor) {ECO:0000269|PubMed:16373578};
KM=12 uM for arachidonic acid {ECO:0000269|PubMed:26859324};
KM=17.0 uM for arachidonate (in presence of sodium nitroprusside
NO donor) {ECO:0000269|PubMed:16373578};
Vmax=81.3 nmol/min/mg enzyme (in absence of sodium nitroprusside
NO donor) {ECO:0000269|PubMed:16373578};
Vmax=132 nmol/min/mg enzyme (in absence of sodium nitroprusside
NO donor) {ECO:0000269|PubMed:16373578};
-!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
{ECO:0000269|PubMed:26859324, ECO:0000269|PubMed:27226593}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:26859324,
ECO:0000269|PubMed:27226593}.
-!- SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane
protein. Endoplasmic reticulum membrane; Peripheral membrane
protein.
-!- INDUCTION: By cytokines and mitogens.
-!- PTM: S-nitrosylation by NOS2 (iNOS) activates enzyme activity. S-
nitrosylation may take place on different Cys residues in addition
to Cys-526. {ECO:0000269|PubMed:16373578}.
-!- PTM: Acetylated at Ser-565 by SPHK1. During neuroinflammation,
acetylation by SPHK1 promotes neuronal secretion of specialized
preresolving mediators (SPMs), especially 15-R-lipoxin A4, which
results in an increase of phagocytic microglia.
{ECO:0000250|UniProtKB:Q05769}.
-!- 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.
-!- MISCELLANEOUS: 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.
-!- MISCELLANEOUS: PTGS1 and PTGS2 are the targets of nonsteroidal
anti-inflammatory drugs (NSAIDs) including aspirin and ibuprofen
(PubMed:27710942, PubMed:26859324, PubMed:27226593). Aspirin is
able to produce an irreversible inactivation of the enzyme through
a serine acetylation (PubMed:26859324). 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.
{ECO:0000269|PubMed:26859324, ECO:0000269|PubMed:27226593,
ECO:0000269|PubMed:27710942}.
-!- SIMILARITY: Belongs to the prostaglandin G/H synthase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PTGS2ID509ch1q31.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ptgs2/";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/ptgs2/";
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EMBL; L15326; AAA35803.1; -; mRNA.
EMBL; M90100; AAA58433.1; -; mRNA.
EMBL; D28235; BAA05698.1; -; Genomic_DNA.
EMBL; U04636; AAA57317.1; -; Genomic_DNA.
EMBL; AY462100; AAR23927.1; -; mRNA.
EMBL; AY229989; AAO38056.1; -; Genomic_DNA.
EMBL; AY382629; AAQ75702.1; -; Genomic_DNA.
EMBL; AK292167; BAF84856.1; -; mRNA.
EMBL; AL033533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471067; EAW91216.1; -; Genomic_DNA.
EMBL; BC013734; AAH13734.1; -; mRNA.
CCDS; CCDS1371.1; -.
PIR; A46150; A46150.
RefSeq; NP_000954.1; NM_000963.3.
PDB; 1V0X; Model; -; A=1-604.
PDB; 5F19; X-ray; 2.04 A; A/B=19-569.
PDB; 5F1A; X-ray; 2.38 A; A/B=19-570.
PDB; 5IKQ; X-ray; 2.41 A; A/B=19-569.
PDB; 5IKR; X-ray; 2.34 A; A/B=19-569.
PDB; 5IKT; X-ray; 2.45 A; A/B=19-569.
PDB; 5IKV; X-ray; 2.51 A; A/B=19-569.
PDB; 5KIR; X-ray; 2.70 A; A/B=19-569.
PDBsum; 1V0X; -.
PDBsum; 5F19; -.
PDBsum; 5F1A; -.
PDBsum; 5IKQ; -.
PDBsum; 5IKR; -.
PDBsum; 5IKT; -.
PDBsum; 5IKV; -.
PDBsum; 5KIR; -.
SMR; P35354; -.
BioGrid; 111715; 36.
CORUM; P35354; -.
DIP; DIP-28131N; -.
IntAct; P35354; 4.
STRING; 9606.ENSP00000356438; -.
BindingDB; P35354; -.
ChEMBL; CHEMBL230; -.
DrugBank; DB03477; 1-Phenylsulfonamide-3-Trifluoromethyl-5-Parabromophenylpyrazole.
DrugBank; DB00316; Acetaminophen.
DrugBank; DB00945; Acetylsalicylic acid.
DrugBank; DB00041; Aldesleukin.
DrugBank; DB00233; Aminosalicylic Acid.
DrugBank; DB01435; Antipyrine.
DrugBank; DB01419; Antrafenine.
DrugBank; DB01014; Balsalazide.
DrugBank; DB00963; Bromfenac.
DrugBank; DB00887; Bumetanide.
DrugBank; DB06774; Capsaicin.
DrugBank; DB00821; Carprofen.
DrugBank; DB00482; Celecoxib.
DrugBank; DB00856; Chlorphenesin.
DrugBank; DB05095; Cimicoxib.
DrugBank; DB00515; Cisplatin.
DrugBank; DB00720; Clodronate.
DrugBank; DB00250; Dapsone.
DrugBank; DB05804; dehydroepiandrosterone sulfate.
DrugBank; DB00035; Desmopressin.
DrugBank; DB00586; Diclofenac.
DrugBank; DB00861; Diflunisal.
DrugBank; DB00154; Dihomo-gamma-linolenic acid.
DrugBank; DB01395; Drospirenone.
DrugBank; DB00005; Etanercept.
DrugBank; DB00749; Etodolac.
DrugBank; DB00773; Etoposide.
DrugBank; DB01628; Etoricoxib.
DrugBank; DB00573; Fenoprofen.
DrugBank; DB09217; Firocoxib.
DrugBank; DB02266; Flufenamic Acid.
DrugBank; DB00712; Flurbiprofen.
DrugBank; DB01404; Ginseng.
DrugBank; DB01050; Ibuprofen.
DrugBank; DB00159; Icosapent.
DrugBank; DB00328; Indomethacin.
DrugBank; DB01009; Ketoprofen.
DrugBank; DB00465; Ketorolac.
DrugBank; DB00480; Lenalidomide.
DrugBank; DB04725; Licofelone.
DrugBank; DB06725; Lornoxicam.
DrugBank; DB01283; Lumiracoxib.
DrugBank; DB01397; Magnesium salicylate.
DrugBank; DB00939; Meclofenamic acid.
DrugBank; DB00784; Mefenamic acid.
DrugBank; DB00814; Meloxicam.
DrugBank; DB00244; Mesalazine.
DrugBank; DB00461; Nabumetone.
DrugBank; DB00788; Naproxen.
DrugBank; DB06802; Nepafenac.
DrugBank; DB04552; Niflumic Acid.
DrugBank; DB04743; Nimesulide.
DrugBank; DB06804; Nonoxynol-9.
DrugBank; DB00991; Oxaprozin.
DrugBank; DB08439; Parecoxib.
DrugBank; DB00812; Phenylbutazone.
DrugBank; DB00554; Piroxicam.
DrugBank; DB08910; Pomalidomide.
DrugBank; DB03866; Prostaglandin G2.
DrugBank; DB02709; Resveratrol.
DrugBank; DB00884; Risedronate.
DrugBank; DB00533; Rofecoxib.
DrugBank; DB00936; Salicylic acid.
DrugBank; DB01399; Salsalate.
DrugBank; DB00360; Sapropterin.
DrugBank; DB05875; substance P.
DrugBank; DB00795; Sulfasalazine.
DrugBank; DB00605; Sulindac.
DrugBank; DB00870; Suprofen.
DrugBank; DB08819; Tafluprost.
DrugBank; DB00469; Tenoxicam.
DrugBank; DB01041; Thalidomide.
DrugBank; DB01600; Tiaprofenic acid.
DrugBank; DB00500; Tolmetin.
DrugBank; DB00620; Triamcinolone.
DrugBank; DB01401; Trisalicylate-choline.
DrugBank; DB00580; Valdecoxib.
GuidetoPHARMACOLOGY; 1376; -.
SwissLipids; SLP:000000830; -.
PeroxiBase; 3321; HsPGHS02.
GlyConnect; 1649; -.
iPTMnet; P35354; -.
PhosphoSitePlus; P35354; -.
BioMuta; PTGS2; -.
DMDM; 3915797; -.
EPD; P35354; -.
jPOST; P35354; -.
MaxQB; P35354; -.
PaxDb; P35354; -.
PeptideAtlas; P35354; -.
PRIDE; P35354; -.
ProteomicsDB; 55035; -.
DNASU; 5743; -.
Ensembl; ENST00000367468; ENSP00000356438; ENSG00000073756.
GeneID; 5743; -.
KEGG; hsa:5743; -.
UCSC; uc001gsb.4; human.
CTD; 5743; -.
DisGeNET; 5743; -.
GeneCards; PTGS2; -.
HGNC; HGNC:9605; PTGS2.
HPA; CAB000113; -.
HPA; HPA001335; -.
MIM; 600262; gene.
neXtProt; NX_P35354; -.
OpenTargets; ENSG00000073756; -.
PharmGKB; PA293; -.
eggNOG; KOG2408; Eukaryota.
eggNOG; ENOG410XPZ3; LUCA.
GeneTree; ENSGT00390000010743; -.
HOGENOM; HOG000013149; -.
InParanoid; P35354; -.
KO; K11987; -.
OMA; KGCPFTA; -.
OrthoDB; 559299at2759; -.
PhylomeDB; P35354; -.
TreeFam; TF329675; -.
BioCyc; MetaCyc:HS01115-MONOMER; -.
BRENDA; 1.14.99.1; 2681.
Reactome; R-HSA-197264; Nicotinamide salvaging.
Reactome; R-HSA-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
Reactome; R-HSA-9018677; Biosynthesis of DHA-derived SPMs.
Reactome; R-HSA-9018679; Biosynthesis of EPA-derived SPMs.
Reactome; R-HSA-9025094; Biosynthesis of DPAn-3 SPMs.
Reactome; R-HSA-9027604; Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives.
SABIO-RK; P35354; -.
SIGNOR; P35354; -.
UniPathway; UPA00662; -.
GeneWiki; Prostaglandin-endoperoxide_synthase_2; -.
GeneWiki; PTGS2; -.
GenomeRNAi; 5743; -.
PRO; PR:P35354; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000073756; Expressed in 186 organ(s), highest expression level in seminal vesicle.
ExpressionAtlas; P35354; baseline and differential.
Genevisible; P35354; HS.
GO; GO:0005901; C:caveola; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:ParkinsonsUK-UCL.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0043005; C:neuron projection; IDA:MGI.
GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0020037; F:heme binding; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:Ensembl.
GO; GO:0004601; F:peroxidase activity; NAS:UniProtKB.
GO; GO:0004666; F:prostaglandin-endoperoxide synthase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
GO; GO:0071318; P:cellular response to ATP; IEA:Ensembl.
GO; GO:0071498; P:cellular response to fluid shear stress; IEA:Ensembl.
GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEP:UniProtKB.
GO; GO:0071284; P:cellular response to lead ion; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0071471; P:cellular response to non-ionic osmotic stress; IEA:Ensembl.
GO; GO:0034644; P:cellular response to UV; IEA:Ensembl.
GO; GO:0019371; P:cyclooxygenase pathway; IDA:BHF-UCL.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0046697; P:decidualization; IEA:Ensembl.
GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
GO; GO:0042633; P:hair cycle; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:0007612; P:learning; IEA:Ensembl.
GO; GO:0019372; P:lipoxygenase pathway; TAS:Reactome.
GO; GO:0042759; P:long-chain fatty acid biosynthetic process; TAS:Reactome.
GO; GO:0035633; P:maintenance of permeability of blood-brain barrier; IEA:Ensembl.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:0034356; P:NAD biosynthesis via nicotinamide riboside salvage pathway; TAS:Reactome.
GO; GO:0097756; P:negative regulation of blood vessel diameter; IEA:Ensembl.
GO; GO:0051926; P:negative regulation of calcium ion transport; IEA:Ensembl.
GO; GO:0045786; P:negative regulation of cell cycle; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
GO; GO:1902219; P:negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress; IEA:Ensembl.
GO; GO:0045986; P:negative regulation of smooth muscle contraction; IEA:Ensembl.
GO; GO:0032227; P:negative regulation of synaptic transmission, dopaminergic; IEA:Ensembl.
GO; GO:0030728; P:ovulation; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0090336; P:positive regulation of brown fat cell differentiation; ISS:BHF-UCL.
GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISS:BHF-UCL.
GO; GO:0031622; P:positive regulation of fever generation; ISS:BHF-UCL.
GO; GO:0090271; P:positive regulation of fibroblast growth factor production; ISS:BHF-UCL.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:BHF-UCL.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0090362; P:positive regulation of platelet-derived growth factor production; ISS:BHF-UCL.
GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; NAS:BHF-UCL.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0045987; P:positive regulation of smooth muscle contraction; IEA:Ensembl.
GO; GO:0031915; P:positive regulation of synaptic plasticity; IEA:Ensembl.
GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
GO; GO:0071636; P:positive regulation of transforming growth factor beta production; ISS:BHF-UCL.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISS:BHF-UCL.
GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
GO; GO:0001516; P:prostaglandin biosynthetic process; ISS:UniProtKB.
GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
GO; GO:0050727; P:regulation of inflammatory response; NAS:UniProtKB.
GO; GO:0150077; P:regulation of neuroinflammatory response; ISS:UniProtKB.
GO; GO:1990776; P:response to angiotensin; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0070542; P:response to fatty acid; IEA:Ensembl.
GO; GO:0009750; P:response to fructose; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0010226; P:response to lithium ion; IEA:Ensembl.
GO; GO:0010042; P:response to manganese ion; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
GO; GO:0034612; P:response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0033280; P:response to vitamin D; IEA:Ensembl.
GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
Gene3D; 1.10.640.10; -; 1.
InterPro; IPR029576; COX-2.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR019791; Haem_peroxidase_animal.
InterPro; IPR010255; Haem_peroxidase_sf.
InterPro; IPR037120; Haem_peroxidase_sf_animal.
PANTHER; PTHR11903:SF8; PTHR11903:SF8; 1.
Pfam; PF03098; An_peroxidase; 1.
Pfam; PF00008; EGF; 1.
PRINTS; PR00457; ANPEROXIDASE.
SUPFAM; SSF48113; SSF48113; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS50292; PEROXIDASE_3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Dioxygenase;
Disulfide bond; Endoplasmic reticulum; Fatty acid biosynthesis;
Fatty acid metabolism; Glycoprotein; Heme; Iron; Lipid biosynthesis;
Lipid metabolism; Membrane; Metal-binding; Microsome; Oxidoreductase;
Peroxidase; Polymorphism; Prostaglandin biosynthesis;
Prostaglandin metabolism; Reference proteome; S-nitrosylation; Signal;
Transferase.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 604 Prostaglandin G/H synthase 2.
/FTId=PRO_0000023875.
DOMAIN 18 55 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
ACT_SITE 193 193 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00298}.
ACT_SITE 371 371 For cyclooxygenase activity.
{ECO:0000250|UniProtKB:Q05769}.
METAL 374 374 Iron (heme axial ligand).
{ECO:0000255|PROSITE-ProRule:PRU00298}.
BINDING 106 106 Substrate.
{ECO:0000250|UniProtKB:Q05769}.
BINDING 341 341 Substrate.
{ECO:0000250|UniProtKB:Q05769}.
SITE 516 516 Aspirin-acetylated serine.
{ECO:0000269|PubMed:26859324}.
MOD_RES 526 526 S-nitrosocysteine.
{ECO:0000305|PubMed:16373578}.
MOD_RES 565 565 O-acetylserine.
{ECO:0000250|UniProtKB:Q05769}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5F19,
ECO:0000244|PDB:5F1A,
ECO:0000244|PDB:5IKQ,
ECO:0000244|PDB:5IKT,
ECO:0000269|PubMed:26859324,
ECO:0000269|PubMed:27226593}.
CARBOHYD 130 130 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5F19,
ECO:0000244|PDB:5F1A,
ECO:0000244|PDB:5IKQ,
ECO:0000244|PDB:5IKR,
ECO:0000244|PDB:5IKT,
ECO:0000244|PDB:5IKV,
ECO:0000244|PDB:5KIR,
ECO:0000269|PubMed:26859324,
ECO:0000269|PubMed:27226593,
ECO:0000269|PubMed:27710942}.
CARBOHYD 396 396 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5F19,
ECO:0000244|PDB:5F1A,
ECO:0000244|PDB:5IKQ,
ECO:0000244|PDB:5IKR,
ECO:0000244|PDB:5IKT,
ECO:0000244|PDB:5IKV,
ECO:0000244|PDB:5KIR,
ECO:0000269|PubMed:26859324,
ECO:0000269|PubMed:27226593,
ECO:0000269|PubMed:27710942}.
CARBOHYD 580 580 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17113084}.
DISULFID 21 32 {ECO:0000244|PDB:5F19,
ECO:0000244|PDB:5F1A,
ECO:0000244|PDB:5IKQ,
ECO:0000244|PDB:5IKR,
ECO:0000244|PDB:5IKT,
ECO:0000244|PDB:5IKV,
ECO:0000244|PDB:5KIR,
ECO:0000269|PubMed:26859324,
ECO:0000269|PubMed:27226593,
ECO:0000269|PubMed:27710942}.
DISULFID 22 145 {ECO:0000244|PDB:5F19,
ECO:0000244|PDB:5F1A,
ECO:0000244|PDB:5IKQ,
ECO:0000244|PDB:5IKR,
ECO:0000244|PDB:5IKT,
ECO:0000244|PDB:5IKV,
ECO:0000244|PDB:5KIR,
ECO:0000269|PubMed:26859324,
ECO:0000269|PubMed:27226593,
ECO:0000269|PubMed:27710942}.
DISULFID 26 42 {ECO:0000244|PDB:5F19,
ECO:0000244|PDB:5F1A,
ECO:0000244|PDB:5IKQ,
ECO:0000244|PDB:5IKR,
ECO:0000244|PDB:5IKT,
ECO:0000244|PDB:5IKV,
ECO:0000244|PDB:5KIR,
ECO:0000269|PubMed:26859324,
ECO:0000269|PubMed:27226593,
ECO:0000269|PubMed:27710942}.
DISULFID 44 54 {ECO:0000244|PDB:5F19,
ECO:0000244|PDB:5F1A,
ECO:0000244|PDB:5IKQ,
ECO:0000244|PDB:5IKR,
ECO:0000244|PDB:5IKT,
ECO:0000244|PDB:5IKV,
ECO:0000244|PDB:5KIR,
ECO:0000269|PubMed:26859324,
ECO:0000269|PubMed:27226593,
ECO:0000269|PubMed:27710942}.
DISULFID 555 561 {ECO:0000244|PDB:5F19,
ECO:0000244|PDB:5F1A,
ECO:0000244|PDB:5IKQ,
ECO:0000244|PDB:5IKR,
ECO:0000244|PDB:5IKT,
ECO:0000244|PDB:5IKV,
ECO:0000244|PDB:5KIR,
ECO:0000269|PubMed:26859324,
ECO:0000269|PubMed:27226593,
ECO:0000269|PubMed:27710942}.
VARIANT 228 228 R -> H (in dbSNP:rs3218622).
{ECO:0000269|Ref.6}.
/FTId=VAR_016262.
VARIANT 428 428 P -> A (in dbSNP:rs4648279).
{ECO:0000269|Ref.6}.
/FTId=VAR_016263.
VARIANT 488 488 E -> G (in dbSNP:rs5272).
/FTId=VAR_011980.
VARIANT 511 511 V -> A (in dbSNP:rs5273).
{ECO:0000269|PubMed:15308583,
ECO:0000269|Ref.6}.
/FTId=VAR_011981.
VARIANT 587 587 G -> R (in dbSNP:rs3218625).
{ECO:0000269|Ref.6}.
/FTId=VAR_016264.
MUTAGEN 371 371 Y->A: Decreased protein stability.
Increased decrease of protein stability;
when associated with A-516.
{ECO:0000269|PubMed:27226593}.
MUTAGEN 516 516 S->A: No effect on protein stability.
Increased decrease of protein stability;
when associated with A-371.
{ECO:0000269|PubMed:27226593}.
MUTAGEN 516 516 S->T: Decreased enzyme activity with
arachidonic acid. Loss of cyclooxygenase
activity; when associated with V-519.
{ECO:0000269|PubMed:26859324}.
MUTAGEN 519 519 G->V: Loss of cyclooxygenase activity.
Loss of cyclooxygenase activity; when
associated with T-516.
{ECO:0000269|PubMed:26859324}.
MUTAGEN 526 526 C->S: Prevents activation by nitric oxid
(NO). {ECO:0000269|PubMed:16373578}.
MUTAGEN 555 555 C->S: Abolishes enzyme activity.
{ECO:0000269|PubMed:16373578}.
MUTAGEN 561 561 C->S: Does not affect activation by
nitric oxid (NO).
{ECO:0000269|PubMed:16373578}.
CONFLICT 165 165 E -> G (in Ref. 2; AAA58433).
{ECO:0000305}.
CONFLICT 438 438 I -> T (in Ref. 1; AAA35803).
{ECO:0000305}.
TURN 20 23 {ECO:0000244|PDB:5F19}.
STRAND 31 35 {ECO:0000244|PDB:5F19}.
TURN 36 38 {ECO:0000244|PDB:5F19}.
STRAND 39 43 {ECO:0000244|PDB:5F19}.
STRAND 47 50 {ECO:0000244|PDB:5F19}.
TURN 51 54 {ECO:0000244|PDB:5F19}.
HELIX 59 66 {ECO:0000244|PDB:5F19}.
HELIX 71 78 {ECO:0000244|PDB:5F19}.
HELIX 82 89 {ECO:0000244|PDB:5F19}.
HELIX 92 107 {ECO:0000244|PDB:5F19}.
STRAND 120 122 {ECO:0000244|PDB:5F19}.
HELIX 125 129 {ECO:0000244|PDB:5F19}.
STRAND 135 138 {ECO:0000244|PDB:5F19}.
STRAND 150 153 {ECO:0000244|PDB:5F19}.
HELIX 160 167 {ECO:0000244|PDB:5F19}.
HELIX 182 192 {ECO:0000244|PDB:5F19}.
TURN 193 195 {ECO:0000244|PDB:5F19}.
TURN 200 202 {ECO:0000244|PDB:5F19}.
STRAND 206 208 {ECO:0000244|PDB:5F19}.
HELIX 217 220 {ECO:0000244|PDB:5F19}.
HELIX 224 230 {ECO:0000244|PDB:5F19}.
STRAND 241 243 {ECO:0000244|PDB:5F19}.
STRAND 246 248 {ECO:0000244|PDB:5F19}.
HELIX 252 255 {ECO:0000244|PDB:5F19}.
HELIX 267 269 {ECO:0000244|PDB:5F19}.
TURN 276 279 {ECO:0000244|PDB:5F19}.
HELIX 282 305 {ECO:0000244|PDB:5F19}.
HELIX 311 332 {ECO:0000244|PDB:5F19}.
HELIX 334 339 {ECO:0000244|PDB:5F19}.
HELIX 349 352 {ECO:0000244|PDB:5F19}.
HELIX 365 370 {ECO:0000244|PDB:5F19}.
HELIX 374 376 {ECO:0000244|PDB:5F19}.
STRAND 379 383 {ECO:0000244|PDB:5F19}.
STRAND 386 388 {ECO:0000244|PDB:5F19}.
HELIX 390 393 {ECO:0000244|PDB:5F19}.
HELIX 398 414 {ECO:0000244|PDB:5F19}.
STRAND 420 424 {ECO:0000244|PDB:5F19}.
HELIX 428 430 {ECO:0000244|PDB:5F19}.
HELIX 431 443 {ECO:0000244|PDB:5F19}.
HELIX 449 455 {ECO:0000244|PDB:5F19}.
HELIX 464 468 {ECO:0000244|PDB:5F19}.
STRAND 469 471 {ECO:0000244|PDB:5F19}.
HELIX 472 481 {ECO:0000244|PDB:5F19}.
HELIX 484 486 {ECO:0000244|PDB:5F19}.
HELIX 489 495 {ECO:0000244|PDB:5F19}.
STRAND 503 505 {ECO:0000244|PDB:5F19}.
HELIX 506 521 {ECO:0000244|PDB:5F19}.
HELIX 524 526 {ECO:0000244|PDB:5F19}.
TURN 528 530 {ECO:0000244|PDB:5F19}.
HELIX 533 536 {ECO:0000244|PDB:5F19}.
HELIX 539 546 {ECO:0000244|PDB:5F19}.
HELIX 550 557 {ECO:0000244|PDB:5F19}.
SEQUENCE 604 AA; 68996 MW; 72FBD699F6128519 CRC64;
MLARALLLCA VLALSHTANP CCSHPCQNRG VCMSVGFDQY KCDCTRTGFY GENCSTPEFL
TRIKLFLKPT PNTVHYILTH FKGFWNVVNN IPFLRNAIMS YVLTSRSHLI DSPPTYNADY
GYKSWEAFSN LSYYTRALPP VPDDCPTPLG VKGKKQLPDS NEIVEKLLLR RKFIPDPQGS
NMMFAFFAQH FTHQFFKTDH KRGPAFTNGL GHGVDLNHIY GETLARQRKL RLFKDGKMKY
QIIDGEMYPP TVKDTQAEMI YPPQVPEHLR FAVGQEVFGL VPGLMMYATI WLREHNRVCD
VLKQEHPEWG DEQLFQTSRL ILIGETIKIV IEDYVQHLSG YHFKLKFDPE LLFNKQFQYQ
NRIAAEFNTL YHWHPLLPDT FQIHDQKYNY QQFIYNNSIL LEHGITQFVE SFTRQIAGRV
AGGRNVPPAV QKVSQASIDQ SRQMKYQSFN EYRKRFMLKP YESFEELTGE KEMSAELEAL
YGDIDAVELY PALLVEKPRP DAIFGETMVE VGAPFSLKGL MGNVICSPAY WKPSTFGGEV
GFQIINTASI QSLICNNVKG CPFTSFSVPD PELIKTVTIN ASSSRSGLDD INPTVLLKER
STEL


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E0122h ELISA kit COX1,COX-1,Cyclooxygenase-1,Homo sapiens,Human,PGH synthase 1,PGHS-1,PHS 1,Prostaglandin G_H synthase 1,Prostaglandin H2 synthase 1,Prostaglandin-endoperoxide synthase 1,PTGS1 96T
U0699Rb CLIA COX2,COX-2,COX-2,Cyclooxygenase-2,Oryctolagus cuniculus,PGH synthase 2,PGHS-2,PHS II,Prostaglandin G_H synthase 2,Prostaglandin H2 synthase 2,Prostaglandin-endoperoxide synthase 2,PTGS2,Rabbit 96T
E0699h ELISA COX2,COX-2,Cyclooxygenase-2,Homo sapiens,Human,PGH synthase 2,PGHS-2,PHS II,Prostaglandin G_H synthase 2,Prostaglandin H2 synthase 2,Prostaglandin-endoperoxide synthase 2,PTGS2 96T
U0699h CLIA COX2,COX-2,Cyclooxygenase-2,Homo sapiens,Human,PGH synthase 2,PGHS-2,PHS II,Prostaglandin G_H synthase 2,Prostaglandin H2 synthase 2,Prostaglandin-endoperoxide synthase 2,PTGS2 96T
E0122h ELISA COX1,COX-1,Cyclooxygenase-1,Homo sapiens,Human,PGH synthase 1,PGHS-1,PHS 1,Prostaglandin G_H synthase 1,Prostaglandin H2 synthase 1,Prostaglandin-endoperoxide synthase 1,PTGS1 96T
E0699h ELISA kit COX2,COX-2,Cyclooxygenase-2,Homo sapiens,Human,PGH synthase 2,PGHS-2,PHS II,Prostaglandin G_H synthase 2,Prostaglandin H2 synthase 2,Prostaglandin-endoperoxide synthase 2,PTGS2 96T
E0122Rb ELISA kit COX1,COX-1,Cyclooxygenase-1,Oryctolagus cuniculus,PGH synthase 1,PGHS-1,PHS 1,Prostaglandin G_H synthase 1,Prostaglandin H2 synthase 1,Prostaglandin-endoperoxide synthase 1,PTGS1,Rabbit 96T
U0122m CLIA Cox1,COX-1,Cox-1,Cyclooxygenase-1,Mouse,Mus musculus,PGH synthase 1,PGHS-1,PHS 1,Prostaglandin G_H synthase 1,Prostaglandin H2 synthase 1,Prostaglandin-endoperoxide synthase 1,Ptgs1 96T
U0699b CLIA Bos taurus,Bovine,COX2,COX-2,Cyclooxygenase-2,PGH synthase 2,PGHS-2,PHS II,Prostaglandin G_H synthase 2,Prostaglandin H2 synthase 2,Prostaglandin-endoperoxide synthase 2,PTGS2 96T
E0122r ELISA Cox1,COX-1,Cox-1,Cyclooxygenase-1,PGH synthase 1,PGHS-1,PHS 1,Prostaglandin G_H synthase 1,Prostaglandin H2 synthase 1,Prostaglandin-endoperoxide synthase 1,Ptgs1,Rat,Rattus norvegicus 96T
E0122b ELISA Bos taurus,Bovine,COX1,COX-1,COX-1,Cyclooxygenase-1,PGH synthase 1,PGHS-1,PHS 1,Prostaglandin G_H synthase 1,Prostaglandin H2 synthase 1,Prostaglandin-endoperoxide synthase 1,PTGS1 96T
E0699b ELISA Bos taurus,Bovine,COX2,COX-2,Cyclooxygenase-2,PGH synthase 2,PGHS-2,PHS II,Prostaglandin G_H synthase 2,Prostaglandin H2 synthase 2,Prostaglandin-endoperoxide synthase 2,PTGS2 96T
U0699r CLIA Cox2,COX-2,Cox-2,Cyclooxygenase-2,PGH synthase 2,PGHS-2,PHS II,Prostaglandin G_H synthase 2,Prostaglandin H2 synthase 2,Prostaglandin-endoperoxide synthase 2,Ptgs2,Rat,Rattus norvegicus 96T
E0122b ELISA kit Bos taurus,Bovine,COX1,COX-1,COX-1,Cyclooxygenase-1,PGH synthase 1,PGHS-1,PHS 1,Prostaglandin G_H synthase 1,Prostaglandin H2 synthase 1,Prostaglandin-endoperoxide synthase 1,PTGS1 96T
E0122m ELISA kit Cox1,COX-1,Cox-1,Cyclooxygenase-1,Mouse,Mus musculus,PGH synthase 1,PGHS-1,PHS 1,Prostaglandin G_H synthase 1,Prostaglandin H2 synthase 1,Prostaglandin-endoperoxide synthase 1,Ptgs1 96T
U0122b CLIA Bos taurus,Bovine,COX1,COX-1,COX-1,Cyclooxygenase-1,PGH synthase 1,PGHS-1,PHS 1,Prostaglandin G_H synthase 1,Prostaglandin H2 synthase 1,Prostaglandin-endoperoxide synthase 1,PTGS1 96T
E0122m ELISA Cox1,COX-1,Cox-1,Cyclooxygenase-1,Mouse,Mus musculus,PGH synthase 1,PGHS-1,PHS 1,Prostaglandin G_H synthase 1,Prostaglandin H2 synthase 1,Prostaglandin-endoperoxide synthase 1,Ptgs1 96T
E0699b ELISA kit Bos taurus,Bovine,COX2,COX-2,Cyclooxygenase-2,PGH synthase 2,PGHS-2,PHS II,Prostaglandin G_H synthase 2,Prostaglandin H2 synthase 2,Prostaglandin-endoperoxide synthase 2,PTGS2 96T
U0122r CLIA Cox1,COX-1,Cox-1,Cyclooxygenase-1,PGH synthase 1,PGHS-1,PHS 1,Prostaglandin G_H synthase 1,Prostaglandin H2 synthase 1,Prostaglandin-endoperoxide synthase 1,Ptgs1,Rat,Rattus norvegicus 96T
E0699r ELISA Cox2,COX-2,Cox-2,Cyclooxygenase-2,PGH synthase 2,PGHS-2,PHS II,Prostaglandin G_H synthase 2,Prostaglandin H2 synthase 2,Prostaglandin-endoperoxide synthase 2,Ptgs2,Rat,Rattus norvegicus 96T
E0699r ELISA kit Cox2,COX-2,Cox-2,Cyclooxygenase-2,PGH synthase 2,PGHS-2,PHS II,Prostaglandin G_H synthase 2,Prostaglandin H2 synthase 2,Prostaglandin-endoperoxide synthase 2,Ptgs2,Rat,Rattus norvegicus 96T
Pathways :
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP1403: AMPK signaling
WP668: Octadecanoid Pathway
WP1424: Globo Sphingolipid Metabolism
WP1621: Arginine and proline metabolism
WP2208: Cardiolipin Biosynthesis
WP2248: anthocyanin biosynthesis
WP296: TCA Cycle - biocyc
WP626: Abscisic Acid Biosynthesis
WP1423: Ganglio Sphingolipid Metabolism
WP1461: Photosynthetic Carbon Reduction
WP2199: Seed Development
WP2211: Geranylgeranyldiphosphate biosynthesis II (plastidic)
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP1422: Sphingolipid Metabolism
WP677: Momilactone biosynthesis
WP1708: Terpenoid backbone biosynthesis
WP2210: Oryzalexin S biosynthesis
WP303: Prostaglandin Synthesis and Regulation
WP877: Prostaglandin Synthesis and Regulation
WP1111: Prostaglandin Synthesis and Regulation
WP767: Prostaglandin Synthesis and Regulation
WP995: Prostaglandin Synthesis and Regulation
WP374: Prostaglandin Synthesis and Regulation
WP1439: Prostaglandin pathway

Related Genes :
[HPGDS GSTS PGDS PTGDS2] Hematopoietic prostaglandin D synthase (H-PGDS) (EC 5.3.99.2) (GST class-sigma) (Glutathione S-transferase) (EC 2.5.1.18) (Glutathione-dependent PGD synthase) (Glutathione-requiring prostaglandin D synthase) (Prostaglandin-H2 D-isomerase)
[PTGES2 C9orf15 PGES2] Prostaglandin E synthase 2 (Membrane-associated prostaglandin E synthase-2) (mPGE synthase-2) (Microsomal prostaglandin E synthase 2) (mPGES-2) (Prostaglandin-H(2) E-isomerase) (EC 5.3.99.3) [Cleaved into: Prostaglandin E synthase 2 truncated form]
[PTGDS PDS] Prostaglandin-H2 D-isomerase (EC 5.3.99.2) (Beta-trace protein) (Cerebrin-28) (Glutathione-independent PGD synthase) (Lipocalin-type prostaglandin-D synthase) (Prostaglandin-D2 synthase) (PGD2 synthase) (PGDS) (PGDS2)
[] 9,11-endoperoxide prostaglandin H2 reductase (EC 1.1.1.-) (Prostaglandin F2-alpha synthase)
[Hpgds Gsts Pgds Ptgds2] Hematopoietic prostaglandin D synthase (H-PGDS) (EC 5.3.99.2) (GST class-sigma) (Glutathione S-transferase) (EC 2.5.1.18) (Glutathione-dependent PGD synthase) (Glutathione-requiring prostaglandin D synthase) (Prostaglandin-H2 D-isomerase)
[HPGDS GSTS PGDS PTGDS2] Hematopoietic prostaglandin D synthase (H-PGDS) (EC 5.3.99.2) (GST class-sigma) (Glutathione S-transferase) (EC 2.5.1.18) (Glutathione-dependent PGD synthase) (Glutathione-requiring prostaglandin D synthase) (Prostaglandin-H2 D-isomerase)
[P100/11E] 9,11-endoperoxide prostaglandin H2 reductase (EC 1.1.1.-) (Prostaglandin F2-alpha synthase)
[PTGES2 PGES2 QccE-11222] Prostaglandin E synthase 2 (EC 5.3.99.3) (Microsomal prostaglandin E synthase 2) (mPGES-2) [Cleaved into: Prostaglandin E synthase 2 truncated form]
[AKR1C3 DDH1 HSD17B5 KIAA0119 PGFS] Aldo-keto reductase family 1 member C3 (EC 1.-.-.-) (17-beta-hydroxysteroid dehydrogenase type 5) (17-beta-HSD 5) (3-alpha-HSD type II, brain) (3-alpha-hydroxysteroid dehydrogenase type 2) (3-alpha-HSD type 2) (EC 1.1.1.357) (Chlordecone reductase homolog HAKRb) (Dihydrodiol dehydrogenase 3) (DD-3) (DD3) (Dihydrodiol dehydrogenase type I) (HA1753) (Indanol dehydrogenase) (EC 1.1.1.112) (Prostaglandin F synthase) (PGFS) (EC 1.1.1.188) (Testosterone 17-beta-dehydrogenase 5) (EC 1.1.1.239) (EC 1.1.1.64) (Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase) (EC 1.3.1.20)
[PTGIS CYP8 CYP8A1] Prostacyclin synthase (EC 5.3.99.4) (Prostaglandin I2 synthase)
[Nos2 Inosl] Nitric oxide synthase, inducible (EC 1.14.13.39) (Inducible NO synthase) (Inducible NOS) (iNOS) (Macrophage NOS) (MAC-NOS) (NOS type II) (Peptidyl-cysteine S-nitrosylase NOS2)
[AKR1C3] Aldo-keto reductase family 1 member C3 homolog (EC 1.-.-.-) (17-beta-hydroxysteroid dehydrogenase type 5) (17-beta-HSD 5) (3-alpha-hydroxysteroid dehydrogenase type 2) (3-alpha-HSD type 2) (EC 1.1.1.357) (Indanol dehydrogenase) (EC 1.1.1.112) (Prostaglandin F synthase) (PGFS) (EC 1.1.1.188) (Testosterone 17-beta-dehydrogenase 5) (EC 1.1.1.239) (EC 1.1.1.64) (Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase) (EC 1.3.1.20)
[Ptgis Cyp8] Prostacyclin synthase (EC 5.3.99.4) (Prostaglandin I2 synthase)
[Prxl2b Fam213b] Prostamide/prostaglandin F synthase (Prostamide/PG F synthase) (Prostamide/PGF synthase) (EC 1.11.1.20) (Peroxiredoxin-like 2B)
[Ptgis Cyp8] Prostacyclin synthase (EC 5.3.99.4) (Prostaglandin I2 synthase)
[CYP2S1 UNQ891/PRO1906] Cytochrome P450 2S1 (EC 1.14.14.-) (CYPIIS1) (Hydroperoxy icosatetraenoate dehydratase) (EC 4.2.1.152) (Thromboxane-A synthase) (EC 5.3.99.5)
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[ptgis ptgisl] Prostacyclin synthase (EC 5.3.99.4) (Prostaglandin I2 synthase) (PGIS)
[Cyp2s1] Cytochrome P450 2S1 (EC 1.14.14.-) (CYPIIS1) (Hydroperoxy icosatetraenoate dehydratase) (EC 4.2.1.152) (Thromboxane-A synthase) (EC 5.3.99.5)
[PTGIS CYP8] Prostacyclin synthase (EC 5.3.99.4) (Prostaglandin I2 synthase)
[TK UL23] Thymidine kinase (EC 2.7.1.21)
[] Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (VPX); Capsid protein VP1 (P1D) (Virion protein 1); Assembly signal 2A (pX); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]
[tgs1 Rv3130c MTCY03A2.28 MTCY164.41c] Probable diacyglycerol O-acyltransferase tgs1 (TGS1) (EC 2.3.1.20) (Probable triacylglycerol synthase tgs1)
[CBR1 CBR CRN SDR21C1] Carbonyl reductase [NADPH] 1 (EC 1.1.1.184) (15-hydroxyprostaglandin dehydrogenase [NADP(+)]) (EC 1.1.1.197) (NADPH-dependent carbonyl reductase 1) (Prostaglandin 9-ketoreductase) (Prostaglandin-E(2) 9-reductase) (EC 1.1.1.189) (Short chain dehydrogenase/reductase family 21C member 1)
[PRXL2B C1orf93 FAM213B] Prostamide/prostaglandin F synthase (Prostamide/PG F synthase) (Prostamide/PGF synthase) (EC 1.11.1.20) (Peroxiredoxin-like 2B) (Protein FAM213B)
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BMT53_00170 BUE81_10670 BvCms12BK_01457 BvCms28BK_04168 BvCmsHHP001_02632 BvCmsKKP061_00566 BvCmsKSP008_02510 BvCmsKSP015_01352 BvCmsKSP036_04668 BvCmsKSP045_04450 BvCmsKSP058_03204 BvCmsKSP067_02879 BvCmsKSP083_03900 BvCmsNSNP027_04914 BvCmsNSP006_03750 BvCmsNSP007_03329 BvCmsNSP039_03266 BvCmsNSP047_03567 BvCmsNSP078_03451 BvCmsSINP011_04162 BvCmsSIP006_05510 BvCmsSIP082_02402 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 CDL37_00765 CIJ94_05515 COD46_23180 CQP61_17160 CRD98_26150 CY655_12940 D5618_21870 D9D20_21030 D9D43_06110 D9H68_20750 D9H70_25730 D9I87_15275 DL800_09215 DNQ41_14245 DQE83_22775 DTL43_21780 DTM25_06080 DU321_04440 E2855_02503 E2863_02392 EC95NR1_00961 ED648_25045 EFB45_10990 EPS97_16570 EPT01_11070 EQ825_23250 ERS085379_01273 ERS085386_05041 EVY21_22520 ExPECSC038_01920 EXX32_14605 EXX71_02385 EXX78_21815 EYD11_09165 HmCmsJML079_02678 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PU06_24500 SAMEA3472043_00447 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[cyp158a2 SCO1207] Biflaviolin synthase CYP158A2 (EC 1.14.19.69) (Cytochrome P450 158A2) (CYP158A2)
[pyrG A6592_02570 A8M42_16405 A9R57_06965 AC067_22330 AC789_1c31020 ACN002_2797 ACN77_07080 ACN81_20385 ACU57_24415 ACU90_23015 AJ318_22735 AKG99_03555 AM270_00945 AM446_06950 AM464_05605 AM465_10605 AML07_12460 AML35_05300 APT94_17890 APU18_18535 APZ14_09290 ARC77_10140 AU473_08010 AUQ13_17535 AUS26_15660 AW059_10675 AW106_00665 AWE53_025360 AWF59_014510 AWG78_018325 AWP75_20610 AZZ83_003241 B1K96_20050 B7C53_10055 B9M99_21725 B9N33_09475 B9T59_19685 BANRA_01301 BANRA_01853 BANRA_03509 BANRA_03630 BANRA_04184 BANRA_04324 BB545_13920 BE963_03670 BEN53_16995 BET08_07180 BFD68_17190 BHF46_05050 BHS81_16640 BHS87_15735 BIQ87_15835 BIU72_09520 BIZ41_16885 BJJ90_05265 BK248_12970 BK292_23205 BK334_11935 BK373_15870 BK375_10085 BK383_11680 BK400_05820 BMT49_17330 BMT53_21250 BMT91_11105 BN17_26661 BTQ04_11510 BTQ06_23845 BUE81_06975 BvCms12BK_05148 BvCms2454_02052 BvCms35BK_01272 BvCmsA75A_01806 BvCmsC61A_01055 BvCmsF63A_03709 BvCmsH15A_01164 BvCmsHHP001_01156 BvCmsHHP019_01127 BvCmsHHP056_01979 BvCmsJ76A_03658 BvCmsKKNP011_03618 BvCmsKKP021_00792 BvCmsKKP036_03980 BvCmsKKP061_04391 BvCmsKSNP019_00375 BvCmsKSNP073_04203 BvCmsKSNP081_03790 BvCmsKSNP120_03969 BvCmsKSP011_02434 BvCmsKSP015_01987 BvCmsKSP018_02104 BvCmsKSP024_03358 BvCmsKSP026_00102 BvCmsKSP036_04364 BvCmsKSP039_02057 BvCmsKSP040_03316 BvCmsKSP045_02208 BvCmsKSP054_03892 BvCmsKSP058_00862 BvCmsKSP061_02833 BvCmsKSP067_03640 BvCmsKSP076_05173 BvCmsKSP081_02474 BvCmsKSP083_02177 BvCmsNSNP006_02217 BvCmsNSNP023_04008 BvCmsNSNP027_02902 BvCmsNSNP036_03047 BvCmsNSP007_01096 BvCmsNSP039_01404 BvCmsNSP045_00318 BvCmsNSP047_01557 BvCmsNSP052_01369 BvCmsNSP072_00181 BvCmsOUP014_01917 BvCmsSINP011_00512 BvCmsSINP012_00021 BvCmsSINP022_00781 BvCmsSINP036_01056 BvCmsSIP010_03098 BvCmsSIP019_01766 BvCmsSIP044_01614 BvCmsSIP082_01367 BVL39_12970 BW690_04975 BWP17_05185 BXT93_24405 BZL31_00820 BZL69_02125 C1I57_04860 C2M16_17770 C2U48_20025 C3449_06035 C4J69_11655 C4K41_05275 C4M78_00835 C5715_23540 C5N07_06155 C5P01_05005 C5P43_15935 C5P44_09340 C6669_14670 C6986_17750 C6B13_03370 C7235_05745 C7B02_19400 C7B06_11630 C7B07_14530 C7B08_01430 C9E25_03325 C9E67_05815 CA593_12975 CCZ14_04445 CCZ17_10850 CDL37_13440 CG692_07005 CIJ94_12220 COD30_01795 COD46_07095 CPA47_05400 CQP61_06810 CR538_05495 CR539_18815 CRE06_03485 CRM83_26360 CRT43_16405 CRT46_16440 CSB64_15850 CT143_09630 CT146_00680 CV83915_03339 CVH05_06295 CWM24_00790 CWS33_03125 CY655_17835 D0X26_06660 D1900_12730 D2183_19100 D2184_01135 D2185_02785 D2F89_14380 D3821_11140 D3O91_13425 D3Y67_06430 D4M06_10805 D7K63_03745 D7K66_09735 D7Y10_03025 D9D20_04450 D9D33_19300 D9D43_17525 D9E35_20180 D9F17_11720 D9G11_10545 D9G42_05640 D9G48_11875 D9H53_12755 D9H68_17340 D9H70_12195 D9H94_16855 D9I11_16725 D9I18_10690 D9I20_00375 D9I87_07250 D9I88_14405 D9I97_09750 D9J03_22055 D9J11_17735 D9J44_16360 D9J46_14445 D9J60_10045 D9K48_23835 D9K54_13555 D9L89_10810 D9L99_02095 D9N32_10755 D9X97_06540 DB357_11665 DB359_08835 DC440_05995 DD762_13665 DIV22_29760 DL455_11645 DL545_05995 DL800_20505 DM102_10625 DM129_10705 DMI04_14240 DNB37_12630 DNQ41_18960 DNR41_08670 DNX30_08935 DOY56_02000 DP258_16075 DP277_11440 DQE83_04685 DQO13_13250 DS732_20695 DS966_06010 DTL43_09355 DTL90_02675 DTM10_03745 DTM25_22630 DTM45_13530 DU321_06150 DU333_12515 DW236_13020 DWB25_05920 E0E06_12020 E2855_03617 E2863_03463 E4Z89_05020 E5M00_06220 EAI42_07155 EAI44_18400 EAI46_14335 EAI52_12500 EB509_19080 EB510_16355 EB515_03490 EC1094V2_904 EC3234A_48c00890 EC3426_03921 EC382_15705 EC95NR1_02021 Eco118UI_16400 ECONIH1_15890 ECs3640 ECTO124_01152 ECTO6_01068 ED225_00710 ED600_14885 ED607_09825 ED611_00710 ED648_01520 ED903_09700 ED944_03505 EEA45_12675 EEP23_14050 EF173_03685 EFB45_09310 EFV06_07140 EFV07_19330 EFV08_05820 EGT48_09620 EGY17_03100 EIA08_07275 EIA21_04795 EJC48_07220 EJC75_12775 EJH97_05405 EKI52_20580 EL75_0914 EL79_0915 EL80_0918 EO240_11330 EO241_20205 EPS71_16810 EPS86_06805 EPS91_16285 EPS94_11415 EPS97_09215 EPT01_17055 EQ820_17285 EQ823_14605 EQ825_07980 EQ830_01100 ERL57_14345 ERS085365_02427 ERS085366_03042 ERS085374_03279 ERS085386_03410 ERS085416_02898 ERS139211_02072 ERS150873_02003 ERS150876_01467 EVY14_17325 EVY21_09330 EWK56_05345 EWK57_07880 ExPECSC007_02175 ExPECSC022_03623 ExPECSC036_01290 ExPECSC038_01963 ExPECSC065_01289 EXX06_06960 EXX09_09010 EXX13_05855 EXX23_03700 EXX24_19085 EXX29_07810 EXX30_11455 EXX32_11595 EXX39_16105 EXX40_00470 EXX53_03685 EXX55_06445 EXX69_04660 EXX71_16235 EXX73_09105 EXX77_13495 EXX78_11575 EXX87_15385 EYD11_05205 EYY78_11015 FORC28_1110 FORC82_1067 GJ11_18025 HmCms184_04776 HmCmsJML072_03065 HmCmsJML074_04422 HmCmsJML079_03779 HmCmsJML122_00699 HmCmsJML146_01816 HmCmsJML204_00525 HMPREF3040_01161 HW43_18180 JD73_16335 MJ49_17095 MS6198_30910 MS8345_02965 NCTC10082_03473 NCTC10090_04050 NCTC10418_01701 NCTC10764_00296 NCTC10766_00690 NCTC10767_02309 NCTC11022_02860 NCTC11112_00121 NCTC11181_03277 NCTC12950_01251 NCTC13127_01436 NCTC13462_04807 NCTC13846_01212 NCTC7927_01209 NCTC8500_01090 NCTC8960_03783 NCTC9007_03892 NCTC9036_01135 NCTC9037_01243 NCTC9044_00576 NCTC9045_01221 NCTC9050_04166 NCTC9058_00847 NCTC9062_02131 NCTC9075_01630 NCTC9077_01409 NCTC9081_05851 NCTC9117_01609 NCTC9119_01271 NCTC9434_01004 NCTC9702_01298 NCTC9706_03296 NCTC9775_04845 NCTC9777_02704 NCTC9969_01292 PU06_02080 RG28_07675 RK56_023165 SAMEA3472033_01264 SAMEA3472043_01265 SAMEA3472044_02272 SAMEA3472047_00339 SAMEA3472056_05455 SAMEA3472070_01673 SAMEA3472080_03155 SAMEA3472090_00131 SAMEA3472108_00527 SAMEA3472110_03462 SAMEA3472112_03722 SAMEA3472114_02432 SAMEA3472147_03296 SAMEA3484427_03298 SAMEA3484429_03415 SAMEA3484434_01581 SAMEA3485101_02257 SAMEA3485113_02257 SAMEA3752372_03639 SAMEA3752553_01510 SAMEA3752557_03040 SAMEA3752559_02995 SAMEA3752620_01282 SAMEA3753064_02287 SAMEA3753097_02219 SAMEA3753164_01192 SAMEA3753290_02847 SAMEA3753300_01107 SK85_03024 SY51_15605 U12A_02895 U14A_02898 UC41_20365 UN91_03645 WQ89_10170 WR15_06090 YDC107_1339] CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase)
[prpC STM0369] 2-methylcitrate synthase (2-MCS) (mcs) (EC 2.3.3.5) (Citrate synthase) (EC 2.3.3.16)
[cyc2 SCO6073 SC9B1.20] Germacradienol/geosmin synthase [Includes: Germacradienol/germacrene D synthase (EC 4.2.3.22) (EC 4.2.3.75) (Sesquiterpene cyclase) (Sesquiterpene synthase); Geosmin synthase (EC 4.1.99.16)]

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