PTGES3 prostaglandin E synthase 3 [Homo sapiens (human)] - Gene

Summary

Official Symbol: PTGES3provided by HGNC
Official Full Name: prostaglandin E synthase 3provided by HGNC
Primary source: HGNC:HGNC:16049
See related: Ensembl:ENSG00000110958 MIM:607061; AllianceGenome:HGNC:16049
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: P23; TEBP; cPGES
Summary: This gene encodes an enzyme that converts prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2). This protein functions as a co-chaperone with heat shock protein 90 (HSP90), localizing to response elements in DNA and disrupting transcriptional activation complexes. Alternative splicing results in multiple transcript variants. There are multiple pseudogenes of this gene on several different chromosomes. [provided by RefSeq, Feb 2016]
Expression: Ubiquitous expression in ovary (RPKM 50.6), endometrium (RPKM 43.3) and 25 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 12q13.3; 12

Exon count:: 9

Annotation release	Status	Assembly	Chr	Location
RS_2023_10	current	GRCh38.p14 (GCF_000001405.40)	12	NC_000012.12 (56663349..56688284, complement)
RS_2023_10	current	T2T-CHM13v2.0 (GCF_009914755.1)	12	NC_060936.1 (56631338..56658334, complement)
105.20220307	previous assembly	GRCh37.p13 (GCF_000001405.25)	12	NC_000012.11 (57057133..57082068, complement)

Chromosome 12 - NC_000012.12 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: HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The integration of multidisciplinary approaches revealed PTGES3 as a novel drug target for breast cancer treatment.
Title: The integration of multidisciplinary approaches revealed PTGES3 as a novel drug target for breast cancer treatment.
Effect of PTGES3 on the Prognosis and Immune Regulation in Lung Adenocarcinoma.
Title: Effect of PTGES3 on the Prognosis and Immune Regulation in Lung Adenocarcinoma.
p23 and Aha1: Distinct Functions Promote Client Maturation.
Title: p23 and Aha1: Distinct Functions Promote Client Maturation.
Structure of Hsp90-p23-GR reveals the Hsp90 client-remodelling mechanism.
Title: Structure of Hsp90-p23-GR reveals the Hsp90 client-remodelling mechanism.
PTGES3 is a Putative Prognostic Marker in Breast Cancer.
Title: PTGES3 is a Putative Prognostic Marker in Breast Cancer.
A cytosolic heat shock protein 90 and co-chaperone p23 complex activates RIPK3/MLKL during necroptosis of endothelial cells in acute respiratory distress syndrome.
Title: A cytosolic heat shock protein 90 and co-chaperone p23 complex activates RIPK3/MLKL during necroptosis of endothelial cells in acute respiratory distress syndrome.
Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle.
Title: Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle.
Selective Autophagy Maintains the Aryl Hydrocarbon Receptor Levels in HeLa Cells: A Mechanism That Is Dependent on the p23 Co-Chaperone.
Title: Selective Autophagy Maintains the Aryl Hydrocarbon Receptor Levels in HeLa Cells: A Mechanism That Is Dependent on the p23 Co-Chaperone.
Computational aided mechanistic understanding of Camellia sinensis bioactive compounds against co-chaperone p23 as potential anticancer agent.
Title: Computational aided mechanistic understanding of Camellia sinensis bioactive compounds against co-chaperone p23 as potential anticancer agent.
This study evaluated the mechanism by which p23 triggers degradation of AHR, and the role of HSP90 in this process.
Title: p23 protects the human aryl hydrocarbon receptor from degradation via a heat shock protein 90-independent mechanism.

Submit: New GeneRIF Correction See all GeneRIFs (37)

Phenotypes

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Review eQTL and phenotype association data in this region using PheGenI

EBI GWAS Catalog

Description
New gene functions in megakaryopoiesis and platelet formation. EBI GWAS Catalog EBI GWAS CatalogPubMed

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

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Replication interactions

Interaction	Pubs
Knockdown of prostaglandin E synthase 3 (PTGES3) by siRNA inhibits the early stages of HIV-1 replication in 293T cells infected with VSV-G pseudotyped HIV-1	PubMed

Protein interactions

Protein	Gene	Interaction	Pubs
Rev	rev	HIV-1 Rev interacting protein, prostaglandin E synthase 3 (PTGES3), is identified by the in-vitro binding experiments involving cytosolic or nuclear extracts from HeLa cells	PubMed
Vpu	vpu	HIV-1 Vpu is identified to have a physical interaction with prostaglandin E synthase 3 (PTGES3; TEBP) in human HEK293 and/or Jurkat cell lines by using affinity tagging and purification mass spectrometry analyses	PubMed

Go to the HIV-1, Human Interaction Database

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

G29926 (e-PCR)
- UniSTS:81491

D15S1477 (e-PCR)
- UniSTS:474482

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

RH92953 (e-PCR)
- UniSTS:87258

SHGC-23727 (e-PCR)
- UniSTS:33498

PTGES3 (e-PCR)
- UniSTS:504032

SHGC-75126 (e-PCR)
- UniSTS:29165

RH45308 (e-PCR)
- UniSTS:38905

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables DNA polymerase binding	IPI Inferred from Physical Interaction more info	PubMed
enables Hsp90 protein binding	IBA Inferred from Biological aspect of Ancestor more info
enables Hsp90 protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables prostaglandin-E synthase activity	IBA Inferred from Biological aspect of Ancestor more info
enables prostaglandin-E synthase activity	IDA Inferred from Direct Assay more info	PubMed
enables prostaglandin-E synthase activity	TAS Traceable Author Statement more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein-folding chaperone binding	IBA Inferred from Biological aspect of Ancestor more info
enables telomerase activity	IDA Inferred from Direct Assay more info	PubMed
enables unfolded protein binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in chaperone cofactor-dependent protein refolding	IDA Inferred from Direct Assay more info	PubMed
involved_in chaperone-mediated protein complex assembly	IBA Inferred from Biological aspect of Ancestor more info
involved_in chaperone-mediated protein complex assembly	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in cyclooxygenase pathway	TAS Traceable Author Statement more info
involved_in fibroblast proliferation	IEA Inferred from Electronic Annotation more info
involved_in glucocorticoid receptor signaling pathway	IEA Inferred from Electronic Annotation more info
involved_in glycogen biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in lung saccule development	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of phosphorylation	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of telomerase activity	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of telomerase activity	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in prostaglandin biosynthetic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in prostaglandin biosynthetic process	IDA Inferred from Direct Assay more info	PubMed
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein stabilization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in signal transduction	TAS Traceable Author Statement more info	PubMed
involved_in skin development	IEA Inferred from Electronic Annotation more info
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 telomere maintenance	TAS Traceable Author Statement more info	PubMed
involved_in telomere maintenance via telomerase	IBA Inferred from Biological aspect of Ancestor more info
involved_in telomere maintenance via telomerase	IDA Inferred from Direct Assay more info	PubMed
involved_in telomere maintenance via telomerase	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in chromosome, telomeric region	IC Inferred by Curator more info	PubMed
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	TAS Traceable Author Statement more info
located_in nucleoplasm	TAS Traceable Author Statement more info
located_in nucleus	HDA more info	PubMed
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
part_of protein folding chaperone complex	IDA Inferred from Direct Assay more info	PubMed
part_of protein-containing complex	IMP Inferred from Mutant Phenotype more info	PubMed
part_of telomerase holoenzyme complex	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: prostaglandin E synthase 3

Names: Hsp90 co-chaperone; cytosolic prostaglandin E synthase; cytosolic prostaglandin E2 synthase; progesterone receptor complex p23; prostaglandin E synthase 3 (cytosolic); telomerase-binding protein p23; unactive progesterone receptor, 23 kD

NP_001269530.1

EC 5.3.99.3

NP_001269531.1

EC 5.3.99.3

NP_001269532.1

EC 5.3.99.3

NP_001269533.1

EC 5.3.99.3

NP_001269534.1

EC 5.3.99.3

NP_006592.3

EC 5.3.99.3

XP_005268633.1

EC 5.3.99.3

XP_006719262.1

EC 5.3.99.3

XP_011536075.1

EC 5.3.99.3

XP_011536076.1

EC 5.3.99.3

XP_016874205.1

EC 5.3.99.3

XP_054226794.1

EC 5.3.99.3

XP_054226795.1

EC 5.3.99.3

XP_054226796.1

EC 5.3.99.3

XP_054226797.1

EC 5.3.99.3

XP_054226798.1

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_001282601.2 → NP_001269530.1 prostaglandin E synthase 3 isoform b

See identical proteins and their annotated locations for NP_001269530.1

Status: REVIEWED

Description

Transcript Variant: This variant (2) lacks an alternate in-frame exon in the 3' coding region, compared to variant 1, resulting in an isoform (b) that is shorter than isoform a.

Source sequence(s)

AK298147, BC003005, BG927063, BP194632

Consensus CDS

CCDS61160.1

UniProtKB/Swiss-Prot

Q15185

Related

ENSP00000414892.2, ENST00000448157.6

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.
NM_001282602.2 → NP_001269531.1 prostaglandin E synthase 3 isoform c

See identical proteins and their annotated locations for NP_001269531.1

Status: REVIEWED

Description

Transcript Variant: This variant (3) lacks an in-frame exon in the central coding region, compared to variant 1, resulting in an isoform (c) that is shorter than isoform a.

Source sequence(s)

AK298160, BC003005, BG927063, BP194632

Consensus CDS

CCDS61159.1

UniProtKB/Swiss-Prot

Q15185

Related

ENSP00000405299.3, ENST00000414274.7

Conserved Domains (1) summary

cl00175
Location:3 → 95

alpha-crystallin-Hsps_p23-like; alpha-crystallin domain (ACD) found in alpha-crystallin-type small heat shock proteins, and a similar domain found in p23 (a cochaperone for Hsp90) and in other p23-like proteins.
NM_001282603.2 → NP_001269532.1 prostaglandin E synthase 3 isoform d

See identical proteins and their annotated locations for NP_001269532.1

Status: REVIEWED

Description

Transcript Variant: This variant (4) lacks an in-frame exon in the central coding region, compared to variant 1, resulting in an isoform (d) that is shorter than isoform a.

Source sequence(s)

AK295208, BC003005, BG927063, BP194632

Consensus CDS

CCDS61158.1

UniProtKB/Swiss-Prot

Q15185

Related

ENSP00000402385.2, ENST00000436399.6

Conserved Domains (1) summary

cl00175
Location:3 → 76

alpha-crystallin-Hsps_p23-like; alpha-crystallin domain (ACD) found in alpha-crystallin-type small heat shock proteins, and a similar domain found in p23 (a cochaperone for Hsp90) and in other p23-like proteins.
NM_001282604.2 → NP_001269533.1 prostaglandin E synthase 3 isoform e

See identical proteins and their annotated locations for NP_001269533.1

Status: REVIEWED

Description

Transcript Variant: This variant (5) contains an alternate exon in the 5' region, and initiates translation at an alternate start codon, compared to variant 1. The encoded isoform (e) has a distinct and longer N-terminus, compared to isoform a.

Source sequence(s)

BC003005, BG927063, BM541503, BP194632

Consensus CDS

CCDS73485.1

UniProtKB/TrEMBL

A0A087WYT3

Related

ENSP00000482075.1, ENST00000614328.4

Conserved Domains (1) summary

cd00237
Location:7 → 113

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.
NM_001282605.2 → NP_001269534.1 prostaglandin E synthase 3 isoform f

See identical proteins and their annotated locations for NP_001269534.1

Status: REVIEWED

Description

Transcript Variant: This variant (6) lacks two alternate in-frame exons, compared to variant 1. The encoded isoform (f) is shorter than isoform a.

Source sequence(s)

BC003005, BG927063, BP194632, BU167210

UniProtKB/Swiss-Prot

Q15185

Conserved Domains (1) summary

cl00175
Location:3 → 95

alpha-crystallin-Hsps_p23-like; alpha-crystallin domain (ACD) found in alpha-crystallin-type small heat shock proteins, and a similar domain found in p23 (a cochaperone for Hsp90) and in other p23-like proteins.
NM_006601.7 → NP_006592.3 prostaglandin E synthase 3 isoform a

See identical proteins and their annotated locations for NP_006592.3

Status: REVIEWED

Description

Transcript Variant: This variant (1) encodes isoform a.

Source sequence(s)

BC003005, BG927063, BP194632

Consensus CDS

CCDS31836.1

UniProtKB/Swiss-Prot

A8K7D0, B4DHP2, B4DP11, B4DP21, Q15185, Q8WU70

Related

ENSP00000262033.6, ENST00000262033.11

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.

RNA

NR_104219.2 RNA Sequence

Status: REVIEWED

Description

Transcript Variant: This variant (7) differs in the 5' terminal exon and uses an alternate splice site in the 3' region, compared to variant 1. This variant is represented as non-coding because uses of the 5' most expected translational start codon would render the transcript a candidate for nonsense-mediated mRNA decay (NMD).

Source sequence(s)

AC117378, AK098214, BC003005, BG927063, CA773263, DA556848

Related

ENST00000537473.2

RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2023_10

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p14 Primary Assembly

Genomic

NC_000012.12 Reference GRCh38.p14 Primary Assembly

Range

56663349..56688284 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_006719199.3 → XP_006719262.1 prostaglandin E synthase 3 isoform X5

Conserved Domains (1) summary

cl00175
Location:7 → 99

alpha-crystallin-Hsps_p23-like; alpha-crystallin domain (ACD) found in alpha-crystallin-type small heat shock proteins, and a similar domain found in p23 (a cochaperone for Hsp90) and in other p23-like proteins.
XM_011537774.3 → XP_011536076.1 prostaglandin E synthase 3 isoform X4

Conserved Domains (1) summary

cd00237
Location:7 → 113

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.
XM_005268576.6 → XP_005268633.1 prostaglandin E synthase 3 isoform X2

See identical proteins and their annotated locations for XP_005268633.1

Conserved Domains (1) summary

cd00237
Location:7 → 113

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.
XM_011537773.3 → XP_011536075.1 prostaglandin E synthase 3 isoform X3

See identical proteins and their annotated locations for XP_011536075.1

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.
XM_017018716.2 → XP_016874205.1 prostaglandin E synthase 3 isoform X1

UniProtKB/TrEMBL

B3KUY2

Conserved Domains (1) summary

cd00237
Location:7 → 113

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.

Alternate T2T-CHM13v2.0

Genomic

NC_060936.1 Alternate T2T-CHM13v2.0

Range

56631338..56658334 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_054370823.1 → XP_054226798.1 prostaglandin E synthase 3 isoform X5
XM_054370822.1 → XP_054226797.1 prostaglandin E synthase 3 isoform X4
XM_054370820.1 → XP_054226795.1 prostaglandin E synthase 3 isoform X2
XM_054370819.1 → XP_054226794.1 prostaglandin E synthase 3 isoform X1

UniProtKB/TrEMBL

B3KUY2
XM_054370821.1 → XP_054226796.1 prostaglandin E synthase 3 isoform X3