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Protein

Prostaglandin E synthase

Gene

Ptges

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2).By similarity

Catalytic activityi

(5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate.

Cofactori

glutathioneBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei118 – 1181GlutathioneBy similarity
Binding sitei127 – 1271GlutathioneBy similarity
Binding sitei131 – 1311GlutathioneBy similarity
Binding sitei135 – 1351GlutathioneBy similarity

GO - Molecular functioni

  • glutathione binding Source: UniProtKB
  • prostaglandin-D synthase activity Source: MGI
  • prostaglandin-E synthase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism

Enzyme and pathway databases

BRENDAi5.3.99.3. 3474.
ReactomeiR-MMU-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).

Names & Taxonomyi

Protein namesi
Recommended name:
Prostaglandin E synthase (EC:5.3.99.3)
Short name:
mPGES-1
Alternative name(s):
Microsomal prostaglandin E synthase 1
Gene namesi
Name:Ptges
Synonyms:Pges
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1927593. Ptges.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1313LumenalBy similarityAdd
BLAST
Transmembranei14 – 4229HelicalBy similarityAdd
BLAST
Topological domaini43 – 6119CytoplasmicBy similarityAdd
BLAST
Transmembranei62 – 9130HelicalBy similarityAdd
BLAST
Topological domaini92 – 965LumenalBy similarity
Transmembranei97 – 12024HelicalBy similarityAdd
BLAST
Topological domaini121 – 1244CytoplasmicBy similarity
Transmembranei125 – 15329HelicalBy similarityAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: MGI
  • integral component of membrane Source: UniProtKB
  • nuclear envelope lumen Source: MGI
  • perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2046261.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 153153Prostaglandin E synthasePRO_0000217747Add
BLAST

Proteomic databases

MaxQBiQ9JM51.
PaxDbiQ9JM51.
PRIDEiQ9JM51.

Expressioni

Gene expression databases

BgeeiQ9JM51.
CleanExiMM_PTGES.
GenevisibleiQ9JM51. MM.

Interactioni

Subunit structurei

Homotrimer.By similarity

Protein-protein interaction databases

BioGridi211054. 1 interaction.
STRINGi10090.ENSMUSP00000099916.

Structurei

3D structure databases

ProteinModelPortaliQ9JM51.
SMRiQ9JM51. Positions 14-153.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni29 – 3911Glutathione bindingBy similarityAdd
BLAST
Regioni71 – 788Glutathione bindingBy similarity
Regioni111 – 1144Glutathione bindingBy similarity

Sequence similaritiesi

Belongs to the MAPEG family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IY81. Eukaryota.
ENOG4111VJG. LUCA.
GeneTreeiENSGT00390000011980.
HOGENOMiHOG000231759.
HOVERGENiHBG052470.
InParanoidiQ9JM51.
KOiK15729.
OMAiCFSMALQ.
OrthoDBiEOG7288T0.
PhylomeDBiQ9JM51.
TreeFamiTF105327.

Family and domain databases

Gene3Di1.20.120.550. 1 hit.
InterProiIPR023352. MAPEG-like_dom.
IPR001129. Membr-assoc_MAPEG.
[Graphical view]
PfamiPF01124. MAPEG. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JM51-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSPGLVMES GQVLPAFLLC STLLVIKMYA VAVITGQMRL RKKAFANPED
60 70 80 90 100
ALKRGGLQYY RSDPDVERCL RAHRNDMETI YPFLFLGFVY SFLGPNPLIA
110 120 130 140 150
WIHFLVVLTG RVVHTVAYLG KLNPRLRSGA YVLAQFSCFS MALQILWEVA

HHL
Length:153
Mass (Da):17,286
Last modified:October 1, 2000 - v1
Checksum:i08A1AF2D288D53F2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB041997 mRNA. Translation: BAA96083.1.
AB035323 mRNA. Translation: BAB71813.1.
AK010757 mRNA. Translation: BAB27163.1.
AK033752 mRNA. Translation: BAC28463.1.
AK172621 mRNA. Translation: BAE43099.1.
BC024960 mRNA. Translation: AAH24960.1.
CCDSiCCDS15889.1.
RefSeqiNP_071860.1. NM_022415.3.
UniGeneiMm.28768.

Genome annotation databases

EnsembliENSMUST00000102852; ENSMUSP00000099916; ENSMUSG00000050737.
GeneIDi64292.
KEGGimmu:64292.
UCSCiuc008jcz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB041997 mRNA. Translation: BAA96083.1.
AB035323 mRNA. Translation: BAB71813.1.
AK010757 mRNA. Translation: BAB27163.1.
AK033752 mRNA. Translation: BAC28463.1.
AK172621 mRNA. Translation: BAE43099.1.
BC024960 mRNA. Translation: AAH24960.1.
CCDSiCCDS15889.1.
RefSeqiNP_071860.1. NM_022415.3.
UniGeneiMm.28768.

3D structure databases

ProteinModelPortaliQ9JM51.
SMRiQ9JM51. Positions 14-153.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211054. 1 interaction.
STRINGi10090.ENSMUSP00000099916.

Chemistry

ChEMBLiCHEMBL2046261.

Proteomic databases

MaxQBiQ9JM51.
PaxDbiQ9JM51.
PRIDEiQ9JM51.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102852; ENSMUSP00000099916; ENSMUSG00000050737.
GeneIDi64292.
KEGGimmu:64292.
UCSCiuc008jcz.1. mouse.

Organism-specific databases

CTDi9536.
MGIiMGI:1927593. Ptges.

Phylogenomic databases

eggNOGiENOG410IY81. Eukaryota.
ENOG4111VJG. LUCA.
GeneTreeiENSGT00390000011980.
HOGENOMiHOG000231759.
HOVERGENiHBG052470.
InParanoidiQ9JM51.
KOiK15729.
OMAiCFSMALQ.
OrthoDBiEOG7288T0.
PhylomeDBiQ9JM51.
TreeFamiTF105327.

Enzyme and pathway databases

BRENDAi5.3.99.3. 3474.
ReactomeiR-MMU-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).

Miscellaneous databases

NextBioi320001.
PROiQ9JM51.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JM51.
CleanExiMM_PTGES.
GenevisibleiQ9JM51. MM.

Family and domain databases

Gene3Di1.20.120.550. 1 hit.
InterProiIPR023352. MAPEG-like_dom.
IPR001129. Membr-assoc_MAPEG.
[Graphical view]
PfamiPF01124. MAPEG. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Regulation of prostaglandin E2 biosynthesis by inducible membrane-associated prostaglandin E2 synthase that acts in concert with cyclooxygenase-2."
    Murakami M., Naraba H., Tanioka T., Semmyo N., Nakatani Y., Kojima F., Ikeda T., Fueki M., Ueno A., Oh S., Kudo I.
    J. Biol. Chem. 275:32783-32792(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
  2. "Biochemical characterization of mouse microsomal prostaglandin E synthase-1 and its colocalization with cyclooxygenase-2 in peritoneal macrophages."
    Lazarus M., Kubata B.K., Eguchi N., Fujitani Y., Urade Y., Hayaishi O.
    Arch. Biochem. Biophys. 397:336-341(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Tissue: Spleen.
  3. "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: Embryonic stem cell, Epididymis and Spleen.
  4. "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].
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Lung.

Entry informationi

Entry nameiPTGES_MOUSE
AccessioniPrimary (citable) accession number: Q9JM51
Secondary accession number(s): Q3T9C5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: October 1, 2000
Last modified: November 11, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.