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

Gene ID: 10728, updated on 27-Nov-2024

Summary

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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
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Genomic context

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See PTGES3 in Genome Data Viewer
Location:
12q13.3; 12
Exon count:
9
Annotation release Status Assembly Chr Location
RS_2024_08 current GRCh38.p14 (GCF_000001405.40) 12 NC_000012.12 (56663349..56688284, complement)
RS_2024_08 current T2T-CHM13v2.0 (GCF_009914755.1) 12 NC_060936.1 (56631338..56658334, complement)
RS_2024_09 previous assembly GRCh37.p13 (GCF_000001405.25) 12 NC_000012.11 (57057133..57082068, complement)

Chromosome 12 - NC_000012.12Genomic Context describing neighboring genes Neighboring gene NANOG-H3K27ac-H3K4me1 hESC enhancer GRCh37_chr12:57038866-57039576 Neighboring gene OCT4-NANOG-H3K27ac-H3K4me1 hESC enhancer GRCh37_chr12:57039577-57040285 Neighboring gene ATP synthase F1 subunit beta Neighboring gene small nucleolar RNA, C/D box 59B Neighboring gene small nucleolar RNA, C/D box 59A Neighboring gene ATAC-STARR-seq lymphoblastoid active region 6511 Neighboring gene MPRA-validated peak1743 silencer Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 4563 Neighboring gene RNA, 7SL, cytoplasmic 809, pseudogene Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr12:57074705-57075584 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 6512 Neighboring gene ATAC-STARR-seq lymphoblastoid silent region 4564 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 6513 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 6514 Neighboring gene NANOG-H3K27ac-H3K4me1 hESC enhancer GRCh37_chr12:57081953-57082478 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 6515 Neighboring gene H3K27ac-H3K4me1 hESC enhancer GRCh37_chr12:57083531-57084056 Neighboring gene ReSE screen-validated silencer GRCh37_chr12:57094539-57094693 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 6516 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 6517 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 6518 Neighboring gene nascent polypeptide associated complex subunit alpha Neighboring gene ATAC-STARR-seq lymphoblastoid active region 6519 Neighboring gene DNA primase subunit 1 Neighboring gene Sharpr-MPRA regulatory region 96

Genomic regions, transcripts, and products

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Go to nucleotide: Graphics FASTA GenBank

Expression

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  • 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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Related articles in PubMed

  1. The integration of multidisciplinary approaches revealed PTGES3 as a novel drug target for breast cancer treatment. Yin Q, et al. J Transl Med, 2024 Jan 20. PMID 38245717, Free PMC Article
  2. Computational aided mechanistic understanding of Camellia sinensis bioactive compounds against co-chaperone p23 as potential anticancer agent. Bharadwaj S, et al. J Cell Biochem, 2019 Nov. PMID 31257629
  3. A cytosolic heat shock protein 90 and co-chaperone p23 complex activates RIPK3/MLKL during necroptosis of endothelial cells in acute respiratory distress syndrome. Yu X, et al. J Mol Med (Berl), 2020 Apr. PMID 32072232
  4. The co-chaperone p23 promotes prostate cancer motility and metastasis. Cano LQ, et al. Mol Oncol, 2015 Jan. PMID 25241147, Free PMC Article
  5. Dysregulation of glucocorticoid receptor co-factors FKBP5, BAG1 and PTGES3 in prefrontal cortex in psychotic illness. Sinclair D, et al. Sci Rep, 2013 Dec 18. PMID 24345775, Free PMC Article

See all (216) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. 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.
  2. 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.
  3. p23 and Aha1: Distinct Functions Promote Client Maturation.
    Title: p23 and Aha1: Distinct Functions Promote Client Maturation.
  4. Structure of Hsp90-p23-GR reveals the Hsp90 client-remodelling mechanism.
    Title: Structure of Hsp90-p23-GR reveals the Hsp90 client-remodelling mechanism.
  5. PTGES3 is a Putative Prognostic Marker in Breast Cancer.
    Title: PTGES3 is a Putative Prognostic Marker in Breast Cancer.
  6. 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.
  7. 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.
  8. 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.
  9. 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.
  10. 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

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

Pathways from PubChem

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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Markers

Homology

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 glycogen biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in lung saccule development IEA
Inferred from Electronic Annotation
more info
  
involved_in nuclear receptor-mediated glucocorticoid signaling pathway IEA
Inferred from Electronic Annotation
more info
  
involved_in positive regulation of telomere maintenance via telomerase IDA
Inferred from Direct Assay
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
  
acts_upstream_of_positive_effect telomere maintenance via telomerase IDA
Inferred from Direct Assay
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 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
NP_001269531.1
NP_001269532.1
NP_001269533.1
NP_001269534.1
NP_006592.3
XP_005268633.1
XP_006719262.1
XP_011536075.1
XP_011536076.1
XP_016874205.1
XP_054226794.1
XP_054226795.1
XP_054226796.1
XP_054226797.1
XP_054226798.1

NCBI Reference Sequences (RefSeq)

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NEW Try the new Transcript table

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)

  1. 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.

  2. 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.

  3. 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.

  4. 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.

  5. 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.

  6. 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

  1. 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_2024_08

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

Reference GRCh38.p14 Primary Assembly

Genomic

  1. NC_000012.12 Reference GRCh38.p14 Primary Assembly

    Range
    56663349..56688284 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. 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.

  2. 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.

  3. 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.

  4. 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.

  5. 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

  1. NC_060936.1 Alternate T2T-CHM13v2.0

    Range
    56631338..56658334 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_054370823.1 → XP_054226798.1  prostaglandin E synthase 3 isoform X5

  2. XM_054370822.1 → XP_054226797.1  prostaglandin E synthase 3 isoform X4

  3. XM_054370820.1 → XP_054226795.1  prostaglandin E synthase 3 isoform X2

  4. XM_054370819.1 → XP_054226794.1  prostaglandin E synthase 3 isoform X1

    UniProtKB/TrEMBL
    B3KUY2

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

Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
Q15185.1 GenPept UniProtKB/Swiss-Prot:Q15185

Gene LinkOut

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