UniProtKB - Q9R0Q7 (TEBP_MOUSE)
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Protein
Prostaglandin E synthase 3
Gene
Ptges3
Organism
Mus musculus (Mouse)
Status
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
: prostaglandin biosynthesis Pathwayi
This protein is involved in the pathway prostaglandin biosynthesis, which is part of Lipid metabolism.By similarityView all proteins of this organism that are known to be involved in the pathway prostaglandin biosynthesis and in Lipid metabolism.
GO - Molecular functioni
- DNA polymerase binding Source: BHF-UCL
- Hsp90 protein binding Source: MGI
- p53 binding Source: Ensembl
- prostaglandin-E synthase activity Source: UniProtKB
- telomerase activity Source: MGI
- unfolded protein binding Source: UniProtKB
GO - Biological processi
- cell proliferation Source: MGI
- chaperone cofactor-dependent protein refolding Source: MGI
- chaperone-mediated protein complex assembly Source: MGI
- glucocorticoid receptor signaling pathway Source: MGI
- glycogen biosynthetic process Source: MGI
- lung saccule development Source: MGI
- negative regulation of cell death Source: Ensembl
- positive regulation of gene expression Source: Ensembl
- positive regulation of phosphorylation Source: MGI
- positive regulation of telomerase activity Source: BHF-UCL
- prostaglandin biosynthetic process Source: MGI
- protein stabilization Source: MGI
- sensory perception of pain Source: Ensembl
- skin development Source: MGI
- telomerase holoenzyme complex assembly Source: BHF-UCL
- telomere maintenance via telomerase Source: BHF-UCL
Keywordsi
Molecular function | Isomerase |
Biological process | Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism |
Enzyme and pathway databases
Reactomei | R-MMU-2162123. Synthesis of Prostaglandins (PG) and Thromboxanes (TX). R-MMU-3371497. HSP90 chaperone cycle for steroid hormone receptors (SHR). R-MMU-3371511. HSF1 activation. R-MMU-3371568. Attenuation phase. R-MMU-8937144. Aryl hydrocarbon receptor signalling. |
UniPathwayi | UPA00662. |
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 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:1929282. Ptges3. |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000218953 | 1 – 160 | Prostaglandin E synthase 3Add BLAST | 160 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 33 | N6-acetyllysineCombined sources | 1 | |
Cross-linki | 35 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 44 | PhosphoserineCombined sources | 1 | |
Cross-linki | 65 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 85 | PhosphoserineBy similarity | 1 | |
Modified residuei | 100 | PhosphoserineCombined sources | 1 | |
Modified residuei | 113 | PhosphoserineCombined sources1 Publication | 1 | |
Modified residuei | 118 | PhosphoserineCombined sources | 1 | |
Modified residuei | 148 | PhosphoserineCombined sources | 1 | |
Modified residuei | 151 | PhosphoserineCombined sources | 1 |
Keywords - PTMi
Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
EPDi | Q9R0Q7. |
MaxQBi | Q9R0Q7. |
PaxDbi | Q9R0Q7. |
PRIDEi | Q9R0Q7. |
PTM databases
iPTMneti | Q9R0Q7. |
PhosphoSitePlusi | Q9R0Q7. |
Expressioni
Tissue specificityi
Expressed in testis, kidney, bladder and ovary.1 Publication
Gene expression databases
Bgeei | ENSMUSG00000071072. |
CleanExi | MM_PTGES3. |
ExpressionAtlasi | Q9R0Q7. baseline and differential. |
Genevisiblei | Q9R0Q7. 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. Interacts with HSP90AA1, FLCN, FNIP1 and FNIP2.By similarity
GO - Molecular functioni
- DNA polymerase binding Source: BHF-UCL
- Hsp90 protein binding Source: MGI
- p53 binding Source: Ensembl
- unfolded protein binding Source: UniProtKB
Protein-protein interaction databases
BioGridi | 207917. 12 interactors. |
IntActi | Q9R0Q7. 3 interactors. |
MINTi | Q9R0Q7. |
STRINGi | 10090.ENSMUSP00000050292. |
Structurei
3D structure databases
ProteinModelPortali | Q9R0Q7. |
SMRi | Q9R0Q7. |
ModBasei | Search... |
MobiDBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1 – 90 | CSPROSITE-ProRule annotationAdd BLAST | 90 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 157 – 160 | PXLE motifBy similarity | 4 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 108 – 160 | Asp/Glu-richAdd BLAST | 53 |
Sequence similaritiesi
Belongs to the p23/wos2 family.Curated
Phylogenomic databases
eggNOGi | KOG3158. Eukaryota. ENOG41121RT. LUCA. |
GeneTreei | ENSGT00510000046493. |
HOGENOMi | HOG000177563. |
HOVERGENi | HBG002143. |
InParanoidi | Q9R0Q7. |
KOi | K15730. |
OMAi | KAAGPYW. |
OrthoDBi | EOG091G0XLQ. |
PhylomeDBi | Q9R0Q7. |
TreeFami | TF315077. |
Family and domain databases
Gene3Di | 2.60.40.790. 1 hit. |
InterProi | View protein in InterPro IPR007052. CS_dom. IPR008978. HSP20-like_chaperone. |
Pfami | View protein in Pfam PF04969. CS. 1 hit. |
SUPFAMi | SSF49764. SSF49764. 1 hit. |
PROSITEi | View protein in PROSITE PS51203. CS. 1 hit. |
i Sequence
Sequence statusi: Complete.
Q9R0Q7-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 87 – 88 | PR → LG in AAD39543 (Ref. 3) Curated | 2 | |
Sequence conflicti | 108 | D → N in AAP34198 (PubMed:14563409).Curated | 1 | |
Sequence conflicti | 108 | D → N in BAB25906 (PubMed:16141072).Curated | 1 |
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. |
CCDSi | CCDS36087.1. |
RefSeqi | NP_062740.1. NM_019766.4. |
UniGenei | Mm.305816. |
Genome annotation databases
Ensembli | ENSMUST00000052798; ENSMUSP00000050292; ENSMUSG00000071072. |
GeneIDi | 56351. |
KEGGi | mmu:56351. |
UCSCi | uc007hld.1. mouse. |
Similar proteinsi
Entry informationi
Entry namei | TEBP_MOUSE | |
Accessioni | Q9R0Q7Primary (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: | February 28, 2018 | |
This is version 162 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |