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Protein

Prostaglandin E synthase 2

Gene

Ptges2

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

Functioni

Isomerase that catalyzes the conversion of PGH2 into the more stable prostaglandin E2 (PGE2) (By similarity). May also have transactivation activity toward IFN-gamma (IFNG), possibly via an interaction with CEBPB; however, the relevance of transcription activation activity remains unclear.1 PublicationBy 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.By similarity

Enzyme regulationi

Isomerase activity is increased by sulfhydril compounds. Dithiothreitol (DTT) is most effective, followed by glutathione (GSH) and 2-mercaptoethanol.By similarity

Pathwayi: prostaglandin biosynthesis

This protein is involved in the pathway prostaglandin biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway prostaglandin biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei147 – 1471Glutathione; via amide nitrogen and carbonyl oxygenBy similarity

GO - Molecular functioni

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • positive regulation of transcription, DNA-templated Source: MGI
  • prostaglandin biosynthetic process Source: UniProtKB-UniPathway
  • secretion Source: MGI
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

UniPathwayiUPA00662.

Names & Taxonomyi

Protein namesi
Recommended name:
Prostaglandin E synthase 2 (EC:5.3.99.3By similarity)
Alternative name(s):
GATE-binding factor 11 Publication
Short name:
GBF-11 Publication
Microsomal prostaglandin E synthase 2
Short name:
mPGES-2
Cleaved into the following chain:
Gene namesi
Name:Ptges2
Synonyms:Gbf1, Pges2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1917592. Ptges2.

Subcellular locationi

Prostaglandin E synthase 2 truncated form :
  • Cytoplasm By similarity

  • Note: Synthesized as a Golgi membrane-bound protein, which is further cleaved into the predominant soluble truncated form.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5656LumenalSequence analysisAdd
BLAST
Transmembranei57 – 7317HelicalSequence analysisAdd
BLAST
Topological domaini74 – 384311CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytosol Source: MGI
  • Golgi membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • mitochondrion Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 384384Prostaglandin E synthase 2PRO_0000013131Add
BLAST
Chaini87 – 384298Prostaglandin E synthase 2 truncated formBy similarityPRO_0000013132Add
BLAST

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei86 – 872CleavageBy similarity

Proteomic databases

EPDiQ8BWM0.
MaxQBiQ8BWM0.
PaxDbiQ8BWM0.
PeptideAtlasiQ8BWM0.
PRIDEiQ8BWM0.

PTM databases

iPTMnetiQ8BWM0.
PhosphoSiteiQ8BWM0.
SwissPalmiQ8BWM0.

Expressioni

Tissue specificityi

Widely expressed. Expressed in brain, heart, liver, colon and lung.2 Publications

Inductioni

Constitutively expressed. Not induced during tissue inflammation. Down-regulated in the absence of Ptges.2 Publications

Gene expression databases

BgeeiQ8BWM0.
CleanExiMM_PTGES2.
ExpressionAtlasiQ8BWM0. baseline and differential.
GenevisibleiQ8BWM0. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with EXOSC10 (By similarity). May interact with CEBPB.By similarity1 Publication

Protein-protein interaction databases

IntActiQ8BWM0. 1 interaction.
MINTiMINT-4113056.
STRINGi10090.ENSMUSP00000028162.

Structurei

3D structure databases

ProteinModelPortaliQ8BWM0.
SMRiQ8BWM0. Positions 99-372.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini89 – 192104GlutaredoxinPROSITE-ProRule annotationAdd
BLAST
Domaini262 – 376115GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni163 – 1642Glutathione bindingBy similarity

Sequence similaritiesi

Belongs to the GST superfamily.Curated
Contains 1 glutaredoxin domain.PROSITE-ProRule annotation
Contains 1 GST C-terminal domain.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3029. Eukaryota.
ENOG410XS2X. LUCA.
GeneTreeiENSGT00390000000224.
HOGENOMiHOG000231901.
HOVERGENiHBG069136.
InParanoidiQ8BWM0.
KOiK05309.
OMAiPMVLIRQ.
OrthoDBiEOG7060R5.
TreeFamiTF314304.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR002109. Glutaredoxin.
IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8BWM0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQAARLSWV LVSSRCALTE GLLTRPWQPL SAQSRAGFTR VAAGSRGAAV
60 70 80 90 100
RKGSPRLLGA AALALGGALG LYHTVRWHQR SQDLRAERSA AQLPLSNSLQ
110 120 130 140 150
LTLYQYKTCP FCSKVRAFLD FHSLPYQVVE VNPVRRTEIK FSSYRKVPIL
160 170 180 190 200
VAQEGDSLQQ LNDSSVIISA LKTYLVSGQP LEEVITYYPP MKAMNDQGKE
210 220 230 240 250
VTEFCNKYWL MLDEKEAQQM YGGKEARTEE MKWRQWADDW LVHLISPNVY
260 270 280 290 300
RTPAEALASF DYIVREGKFG AVEAAMAKYV GAAAMYLISK RLKSRHHLQD
310 320 330 340 350
DVRVDLYEAA NKWVTAVGKD RPFMGGQKPN LADLAVYGVL RVMEGLEAFD
360 370 380
DLMRHSHIQP WYLRMERAIE EAPSVHHVNP SCKD
Length:384
Mass (Da):43,324
Last modified:July 27, 2011 - v3
Checksum:i5A737A01466582CA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti210 – 2101L → P in AAH04846 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK050616 mRNA. Translation: BAC34345.1.
AL928669 Genomic DNA. Translation: CAM22503.1.
CH466542 Genomic DNA. Translation: EDL08547.1.
BC004846 mRNA. Translation: AAH04846.1.
CCDSiCCDS15914.1.
RefSeqiNP_598544.2. NM_133783.2.
UniGeneiMm.28048.

Genome annotation databases

EnsembliENSMUST00000028162; ENSMUSP00000028162; ENSMUSG00000026820.
GeneIDi96979.
KEGGimmu:96979.
UCSCiuc008jfm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK050616 mRNA. Translation: BAC34345.1.
AL928669 Genomic DNA. Translation: CAM22503.1.
CH466542 Genomic DNA. Translation: EDL08547.1.
BC004846 mRNA. Translation: AAH04846.1.
CCDSiCCDS15914.1.
RefSeqiNP_598544.2. NM_133783.2.
UniGeneiMm.28048.

3D structure databases

ProteinModelPortaliQ8BWM0.
SMRiQ8BWM0. Positions 99-372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BWM0. 1 interaction.
MINTiMINT-4113056.
STRINGi10090.ENSMUSP00000028162.

PTM databases

iPTMnetiQ8BWM0.
PhosphoSiteiQ8BWM0.
SwissPalmiQ8BWM0.

Proteomic databases

EPDiQ8BWM0.
MaxQBiQ8BWM0.
PaxDbiQ8BWM0.
PeptideAtlasiQ8BWM0.
PRIDEiQ8BWM0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028162; ENSMUSP00000028162; ENSMUSG00000026820.
GeneIDi96979.
KEGGimmu:96979.
UCSCiuc008jfm.2. mouse.

Organism-specific databases

CTDi80142.
MGIiMGI:1917592. Ptges2.

Phylogenomic databases

eggNOGiKOG3029. Eukaryota.
ENOG410XS2X. LUCA.
GeneTreeiENSGT00390000000224.
HOGENOMiHOG000231901.
HOVERGENiHBG069136.
InParanoidiQ8BWM0.
KOiK05309.
OMAiPMVLIRQ.
OrthoDBiEOG7060R5.
TreeFamiTF314304.

Enzyme and pathway databases

UniPathwayiUPA00662.

Miscellaneous databases

PROiQ8BWM0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BWM0.
CleanExiMM_PTGES2.
ExpressionAtlasiQ8BWM0. baseline and differential.
GenevisibleiQ8BWM0. MM.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR002109. Glutaredoxin.
IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel transactivating factor that regulates interferon-gamma-dependent gene expression."
    Hu J., Meng Q., Roy S.K., Raha A., Hu J., Zhang J., Hashimoto K., Kalvakolanu D.V.
    J. Biol. Chem. 277:30253-30263(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], POSSIBLE FUNCTION, POSSIBLE SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Kidney.
  2. "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.
    Tissue: Thymus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Strain: 129.
    Tissue: Mammary tumor.
  6. "Cellular prostaglandin E2 production by membrane-bound prostaglandin E synthase-2 via both cyclooxygenases-1 and -2."
    Murakami M., Nakashima K., Kamei D., Masuda S., Ishikawa Y., Ishii T., Ohmiya Y., Watanabe K., Kudo I.
    J. Biol. Chem. 278:37937-37947(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION.
  7. "Prostaglandin E2 and microsomal prostaglandin E synthase-2 expression are decreased in the cyclooxygenase-2-deficient mouse brain despite compensatory induction of cyclooxygenase-1 and Ca2+-dependent phospholipase A2."
    Bosetti F., Langenbach R., Weerasinghe G.R.
    J. Neurochem. 91:1389-1397(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  8. "IFN-gamma-stimulated transcriptional activation by IFN-gamma-activated transcriptional element-binding factor 1 occurs via an inducible interaction with CAAAT/enhancer-binding protein-beta."
    Meng Q., Raha A., Roy S., Hu J., Kalvakolanu D.V.
    J. Immunol. 174:6203-6211(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CEBPB.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiPGES2_MOUSE
AccessioniPrimary (citable) accession number: Q8BWM0
Secondary accession number(s): A2ASQ2, Q99J30
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 116 of the entry and version 3 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.