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Protein

Prostaglandin E synthase 3

Gene

Ptges3

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

Functioni

Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2). Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes. Facilitates HIF alpha proteins hydroxylation via interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway.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.By similarity

Pathwayi: prostaglandin biosynthesis

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

GO - Molecular functioni

GO - Biological processi

  • cell proliferation Source: MGI
  • chaperone cofactor-dependent protein refolding Source: MGI
  • glucocorticoid receptor signaling pathway Source: MGI
  • glycogen biosynthetic process Source: MGI
  • lung saccule development Source: MGI
  • prostaglandin biosynthetic process Source: UniProtKB
  • RNA-dependent DNA replication Source: MGI
  • skin development 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

ReactomeiR-MMU-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
R-MMU-3371511. HSF1 activation.
R-MMU-3371568. Attenuation phase.
UniPathwayiUPA00662.

Names & Taxonomyi

Protein namesi
Recommended name:
Prostaglandin E synthase 3 (EC:5.3.99.3By similarity)
Alternative name(s):
Cytosolic prostaglandin E2 synthase
Short name:
cPGES
Hsp90 co-chaperone
Progesterone receptor complex p23
Sid 3177
Telomerase-binding protein p23
Gene namesi
Name:Ptges3
Synonyms:Sid3177, Tebp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1929282. Ptges3.

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 160160Prostaglandin E synthase 3PRO_0000218953Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei33 – 331N6-acetyllysineCombined sources
Modified residuei44 – 441PhosphoserineCombined sources
Modified residuei85 – 851PhosphoserineBy similarity
Modified residuei100 – 1001PhosphoserineCombined sources
Modified residuei113 – 1131PhosphoserineCombined sources1 Publication
Modified residuei118 – 1181PhosphoserineCombined sources
Modified residuei148 – 1481PhosphoserineCombined sources
Modified residuei151 – 1511PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9R0Q7.
MaxQBiQ9R0Q7.
PaxDbiQ9R0Q7.
PRIDEiQ9R0Q7.

PTM databases

iPTMnetiQ9R0Q7.
PhosphoSiteiQ9R0Q7.

Expressioni

Tissue specificityi

Expressed in testis, kidney, bladder and ovary.1 Publication

Gene expression databases

BgeeiQ9R0Q7.
CleanExiMM_PTGES3.
ExpressionAtlasiQ9R0Q7. baseline and differential.
GenevisibleiQ9R0Q7. MM.

Interactioni

Subunit structurei

Binds to the progesterone receptor. Interacts with TERT; the interaction, together with HSP90AA1, is required for correct assembly and stabilization of the telomerase holoenzyme complex. Interacts (via PXLE motif) with EGLN1/PHD2, recruiting EGLN1/PHD2 to the HSP90 pathway to facilitate HIF alpha proteins hydroxylation.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi207917. 10 interactions.
IntActiQ9R0Q7. 3 interactions.
MINTiMINT-3289867.
STRINGi10090.ENSMUSP00000050292.

Structurei

3D structure databases

ProteinModelPortaliQ9R0Q7.
SMRiQ9R0Q7. Positions 1-110.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9090CSPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi157 – 1604PXLE motifBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi108 – 16053Asp/Glu-richAdd
BLAST

Sequence similaritiesi

Belongs to the p23/wos2 family.Curated
Contains 1 CS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3158. Eukaryota.
ENOG41121RT. LUCA.
GeneTreeiENSGT00510000046493.
HOGENOMiHOG000177563.
HOVERGENiHBG002143.
InParanoidiQ9R0Q7.
KOiK15730.
OMAiENESKHK.
OrthoDBiEOG77HDGK.
PhylomeDBiQ9R0Q7.
TreeFamiTF315077.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PfamiPF04969. CS. 1 hit.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS51203. CS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9R0Q7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQPASAKWYD RRDYVFIEFC VEDSKDVNVN FEKSKLTFSC LGGSDNFKHL
60 70 80 90 100
NEIDLFHCID PNDSKHKRTD RSILCCLRKG ESGQSWPRLT KERAKLNWLS
110 120 130 140 150
VDFNNWKDWE DDSDEDMSNF DRFSEMMDHM GGDEDVDLPE VDGADDDSQD
160
SDDEKMPDLE
Length:160
Mass (Da):18,721
Last modified:May 1, 2000 - v1
Checksum:i7702CB59D7AFD739
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 882PR → LG in AAD39543 (Ref. 3) Curated
Sequence conflicti108 – 1081D → N in AAP34198 (PubMed:14563409).Curated
Sequence conflicti108 – 1081D → N in BAB25906 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY281130 mRNA. Translation: AAP34198.1.
AB024935 mRNA. Translation: BAA84684.1.
AF153479 mRNA. Translation: AAD39543.1.
AK008805 mRNA. Translation: BAB25906.1.
AK075932 mRNA. Translation: BAC36062.1.
AK075987 mRNA. Translation: BAC36099.1.
AK077538 mRNA. Translation: BAC36854.1.
AK168073 mRNA. Translation: BAE40047.1.
AK168210 mRNA. Translation: BAE40169.1.
AK168721 mRNA. Translation: BAE40563.1.
BC003708 mRNA. Translation: AAH03708.1.
BC085264 mRNA. Translation: AAH85264.1.
CCDSiCCDS36087.1.
RefSeqiNP_062740.1. NM_019766.4.
XP_006544122.1. XM_006544059.2.
UniGeneiMm.305816.

Genome annotation databases

EnsembliENSMUST00000052798; ENSMUSP00000050292; ENSMUSG00000071072.
GeneIDi102641464.
56351.
KEGGimmu:102641464.
mmu:56351.
UCSCiuc007hld.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY281130 mRNA. Translation: AAP34198.1.
AB024935 mRNA. Translation: BAA84684.1.
AF153479 mRNA. Translation: AAD39543.1.
AK008805 mRNA. Translation: BAB25906.1.
AK075932 mRNA. Translation: BAC36062.1.
AK075987 mRNA. Translation: BAC36099.1.
AK077538 mRNA. Translation: BAC36854.1.
AK168073 mRNA. Translation: BAE40047.1.
AK168210 mRNA. Translation: BAE40169.1.
AK168721 mRNA. Translation: BAE40563.1.
BC003708 mRNA. Translation: AAH03708.1.
BC085264 mRNA. Translation: AAH85264.1.
CCDSiCCDS36087.1.
RefSeqiNP_062740.1. NM_019766.4.
XP_006544122.1. XM_006544059.2.
UniGeneiMm.305816.

3D structure databases

ProteinModelPortaliQ9R0Q7.
SMRiQ9R0Q7. Positions 1-110.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207917. 10 interactions.
IntActiQ9R0Q7. 3 interactions.
MINTiMINT-3289867.
STRINGi10090.ENSMUSP00000050292.

PTM databases

iPTMnetiQ9R0Q7.
PhosphoSiteiQ9R0Q7.

Proteomic databases

EPDiQ9R0Q7.
MaxQBiQ9R0Q7.
PaxDbiQ9R0Q7.
PRIDEiQ9R0Q7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000052798; ENSMUSP00000050292; ENSMUSG00000071072.
GeneIDi102641464.
56351.
KEGGimmu:102641464.
mmu:56351.
UCSCiuc007hld.1. mouse.

Organism-specific databases

CTDi10728.
MGIiMGI:1929282. Ptges3.

Phylogenomic databases

eggNOGiKOG3158. Eukaryota.
ENOG41121RT. LUCA.
GeneTreeiENSGT00510000046493.
HOGENOMiHOG000177563.
HOVERGENiHBG002143.
InParanoidiQ9R0Q7.
KOiK15730.
OMAiENESKHK.
OrthoDBiEOG77HDGK.
PhylomeDBiQ9R0Q7.
TreeFamiTF315077.

Enzyme and pathway databases

UniPathwayiUPA00662.
ReactomeiR-MMU-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
R-MMU-3371511. HSF1 activation.
R-MMU-3371568. Attenuation phase.

Miscellaneous databases

ChiTaRSiPtges3. mouse.
NextBioi312354.
PROiQ9R0Q7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9R0Q7.
CleanExiMM_PTGES3.
ExpressionAtlasiQ9R0Q7. baseline and differential.
GenevisibleiQ9R0Q7. MM.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PfamiPF04969. CS. 1 hit.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS51203. CS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic structure and genitourinary expression of mouse cytosolic prostaglandin E(2) synthase gene."
    Zhang Y., Schneider A., Rao R., Lu W.J., Fan X., Davis L., Breyer R.M., Breyer M.D., Guan Y.
    Biochim. Biophys. Acta 1634:15-23(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: C57BL/6J.
    Tissue: Kidney.
  2. "Mouse p23 uniactive progesterone receptor complexes."
    Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. Cheong C., Lee H.-W.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  4. "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 DBA/2.
    Tissue: Liver and Stomach.
  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: C57BL/6J.
    Tissue: Mammary gland and Olfactory epithelium.
  6. Lubec G., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 36-48.
    Tissue: Brain.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  8. "Phosphoproteome analysis of mouse liver using immobilized metal affinity purification and linear ion trap mass spectrometry."
    Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.
    Rapid Commun. Mass Spectrom. 18:2169-2176(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-113.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-100; SER-113; SER-118; SER-148 AND SER-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  13. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiTEBP_MOUSE
AccessioniPrimary (citable) accession number: Q9R0Q7
Secondary accession number(s): Q542V4, Q9D7V0, Q9WV83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: March 16, 2016
This is version 146 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, Direct protein sequencing, 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.