Ptges3 prostaglandin E synthase 3 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Ptges3provided by MGI
Official Full Name: prostaglandin E synthase 3provided by MGI
Primary source: MGI:MGI:1929282
See related: Ensembl:ENSMUSG00000071072 AllianceGenome:MGI:1929282
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: p23; Tebp; Ptges; cPGES; sid3177; 5730442A20Rik
Summary: Enables DNA polymerase binding activity. Involved in telomerase holoenzyme complex assembly. Acts upstream of with a positive effect on telomere maintenance via telomerase. Acts upstream of or within several processes, including glycogen biosynthetic process; nuclear receptor-mediated glucocorticoid signaling pathway; and prostaglandin biosynthetic process. Predicted to be located in actin filament; neuronal cell body; and perinuclear region of cytoplasm. Predicted to be part of protein folding chaperone complex and telomerase holoenzyme complex. Predicted to be active in cytosol and nucleus. Is expressed in several structures, including liver and skin. Orthologous to human PTGES3 (prostaglandin E synthase 3). [provided by Alliance of Genome Resources, Nov 2024]
Expression: Ubiquitous expression in CNS E11.5 (RPKM 32.9), adrenal adult (RPKM 31.2) and 28 other tissues See more
Orthologs: human all
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Genomic context

Location:: 10 D3; 10 76.39 cM

Exon count:: 8

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	10	NC_000076.7 (127894851..127913123)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	10	NC_000076.6 (128058982..128077254)

Chromosome 10 - NC_000076.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Mouse ENCODE transcriptome data Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Skin differentiation is impaired, and both apoptosis and cell proliferation are augmented in the absence of p23; the consequences are a severe thinning of the stratum corneum and reduced numbers of hair follicles. Since the phenotype of p23-null embryos is strikingly similar to that of embryos lacking the glucocorticoid receptor, a paradigmatic Hsp90-p23 client protein, we investigated glucocorticoid signaling.
Title: Defective glucocorticoid receptor signaling and keratinocyte-autonomous defects contribute to skin phenotype of mouse embryos lacking the Hsp90 co-chaperone p23.
Results identified two proteins P23 and HCLS1, which were not known as RNA-binding proteins, exhibiting RNA-binding activity.
Title: Identification of RNA-binding Proteins in Macrophages by Interactome Capture.
we report the generation of transgenic mouse lines that overexpress wild-type p23 or uncleavable p23
Title: The small co-chaperone p23 overexpressing transgenic mouse.
Data support a model in which p23 and GCN5 regulate diverse multistep pathways by controlling the longevity of protein-DNA complexes.
Title: The p23 molecular chaperone and GCN5 acetylase jointly modulate protein-DNA dynamics and open chromatin status.
p23 co-chaperone protects the aryl hydrocarbon receptor from degradation
Title: p23 co-chaperone protects the aryl hydrocarbon receptor from degradation in mouse and human cell lines.
Cleavage product p19 was not seen in brain samples from a mouse model of Alzheimer disease, but p23 and p19 were seen in hypoxic cultured cells experienceing endoplasmic reticulum stress.
Title: The small chaperone protein p23 and its cleaved product p19 in cellular stress.
In cytosol only one protein called p23 hsp90 binds to Bax but the binding protein does not affect the subcellular localization and pro-apoptotic activity of Bax.
Title: Cytosolic Bax: does it require binding proteins to keep its pro-apoptotic activity in check?
The p23 cochaperone of Hsp90, which plays a major role in glucocorticoid receptor folding and function, associates with influenza virus polymerase.
Title: Influenza virus infection induces the nuclear relocalization of the Hsp90 co-chaperone p23 and inhibits the glucocorticoid receptor response.
Overexpression of p23 contributes to the development of hydronephrosis through the upregulation of the aryl hydrocarbon receptor pathway in vivo.
Title: Transgenic overexpression of p23 induces spontaneous hydronephrosis in mice.
prostaglandin E synthase (cPGES/p23) acts as a regulatory factor for expression of a PGE2-inactivating enzyme, 15-PGDH
Title: Involvement of the constitutive prostaglandin E synthase cPGES/p23 in expression of an initial prostaglandin E2 inactivating enzyme, 15-PGDH.

Submit: New GeneRIF Correction See all GeneRIFs (12)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (1) 1 citation
Gene trapped (2) 1 citation
Targeted (1) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

UniSTS:234880 (e-PCR)
- UniSTS:234880

NoName (e-PCR)
- UniSTS:236483

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables DNA polymerase binding	IPI Inferred from Physical Interaction more info	PubMed
enables DNA polymerase binding	ISO Inferred from Sequence Orthology more info
enables Hsp90 protein binding	IBA Inferred from Biological aspect of Ancestor more info
enables Hsp90 protein binding	IEA Inferred from Electronic Annotation more info
enables Hsp90 protein binding	ISO Inferred from Sequence Orthology more info
enables enzyme binding	ISO Inferred from Sequence Orthology more info
enables p53 binding	ISO Inferred from Sequence Orthology more info
enables prostaglandin-E synthase activity	IBA Inferred from Biological aspect of Ancestor more info
enables prostaglandin-E synthase activity	ISO Inferred from Sequence Orthology more info
enables prostaglandin-E synthase activity	ISS Inferred from Sequence or Structural Similarity more info
enables protein-folding chaperone binding	IBA Inferred from Biological aspect of Ancestor more info
enables telomerase activity	IEA Inferred from Electronic Annotation more info
enables telomerase activity	ISO Inferred from Sequence Orthology more info
enables unfolded protein binding	ISO Inferred from Sequence Orthology more info
enables unfolded protein binding	ISS Inferred from Sequence or Structural Similarity more info

Process	Evidence Code	Pubs
involved_in chaperone cofactor-dependent protein refolding	IEA Inferred from Electronic Annotation more info
involved_in chaperone cofactor-dependent protein refolding	ISO Inferred from Sequence Orthology more info
involved_in chaperone-mediated protein complex assembly	IBA Inferred from Biological aspect of Ancestor more info
involved_in chaperone-mediated protein complex assembly	IEA Inferred from Electronic Annotation more info
involved_in chaperone-mediated protein complex assembly	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within fibroblast proliferation	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within glycogen biosynthetic process	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within lung saccule development	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in neuron apoptotic process	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within nuclear receptor-mediated glucocorticoid signaling pathway	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of gene expression	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of phosphorylation	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of telomere maintenance via telomerase	IEA Inferred from Electronic Annotation more info
involved_in prostaglandin biosynthetic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in prostaglandin biosynthetic process	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within prostaglandin biosynthetic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in prostaglandin biosynthetic process	ISO Inferred from Sequence Orthology more info
involved_in prostaglandin biosynthetic process	ISS Inferred from Sequence or Structural Similarity more info
involved_in prostaglandin metabolic process	ISO Inferred from Sequence Orthology more info
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein stabilization	IEA Inferred from Electronic Annotation more info
involved_in protein stabilization	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within skin development	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in telomerase holoenzyme complex assembly	IBA Inferred from Biological aspect of Ancestor more info
involved_in telomerase holoenzyme complex assembly	IDA Inferred from Direct Assay more info	PubMed
involved_in telomerase holoenzyme complex assembly	ISO Inferred from Sequence Orthology more info
involved_in telomere maintenance via telomerase	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_positive_effect telomere maintenance via telomerase	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_positive_effect telomere maintenance via telomerase	ISO Inferred from Sequence Orthology more info
involved_in telomere maintenance via telomerase	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
located_in actin filament	ISO Inferred from Sequence Orthology more info
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in neuronal cell body	ISO Inferred from Sequence Orthology more info
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
located_in perinuclear region of cytoplasm	ISO Inferred from Sequence Orthology more info
part_of protein folding chaperone complex	IEA Inferred from Electronic Annotation more info
part_of protein folding chaperone complex	ISO Inferred from Sequence Orthology more info
part_of protein-containing complex	ISO Inferred from Sequence Orthology more info
part_of telomerase holoenzyme complex	IEA Inferred from Electronic Annotation more info
part_of telomerase holoenzyme complex	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: prostaglandin E synthase 3

Names: cytosolic prostaglandin E2 synthase; hsp90 co-chaperone; p23 cochaperone; progesterone receptor complex p23; prostaglandin E synthase 3 (cytosolic); sid 3177; telomerase binding protein, p23

NP_062740.1

EC 5.3.99.3

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_019766.4 → NP_062740.1 prostaglandin E synthase 3

See identical proteins and their annotated locations for NP_062740.1

Status: PROVISIONAL

Source sequence(s)

AC131120

Consensus CDS

CCDS36087.1

UniProtKB/Swiss-Prot

Q542V4, Q9D7V0, Q9R0Q7, Q9WV83

UniProtKB/TrEMBL

Q3TJG6

Related

ENSMUSP00000050292.8, ENSMUST00000052798.14

Conserved Domains (1) summary

cd00237
Location:3 → 109

p23; p23 binds heat shock protein (Hsp)90 and participates in the folding of a number of Hsp90 clients, including the progesterone receptor. p23 also has a passive chaperoning activity and in addition may participate in prostaglandin synthesis.