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

Gene ID: 10728, updated on 3-May-2020

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
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

Genomic context

See PTGES3 in Genome Data Viewer
Location:
12q13.3; 12
Exon count:
9
Annotation release Status Assembly Chr Location
109.20200228 current GRCh38.p13 (GCF_000001405.39) 12 NC_000012.12 (56663341..56689575, complement)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 12 NC_000012.11 (57057125..57082138, complement)

Chromosome 12 - NC_000012.12Genomic Context describing neighboring genes 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 RNA, 7SL, cytoplasmic 809, pseudogene Neighboring gene nascent polypeptide associated complex subunit alpha Neighboring gene DNA primase subunit 1

Genomic regions, transcripts, and products

Expression

  • 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

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Phenotypes

NHGRI GWAS Catalog

Description
New gene functions in megakaryopoiesis and platelet formation.
NHGRI GWA Catalog

HIV-1 interactions

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
Vpr vpr Interaction of HIV-1 Vpr with human p23 is presumed based on homology to yeast cell cycle regulator p21 protein Wos2 which suppresses HIV-1 Vpr-induced G2 arrest in vitro, most likely through the inhibition of Wee1 or interaction with Cdc2 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

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Markers

Homology

Gene Ontology Provided by GOA

Function Evidence Code Pubs
DNA polymerase binding IPI
Inferred from Physical Interaction
more info
PubMed 
Hsp90 protein binding IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
Hsp90 protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
chaperone binding IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
prostaglandin-E synthase activity IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
prostaglandin-E synthase activity IDA
Inferred from Direct Assay
more info
PubMed 
protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
telomerase activity IDA
Inferred from Direct Assay
more info
PubMed 
unfolded protein binding IDA
Inferred from Direct Assay
more info
PubMed 
Process Evidence Code Pubs
chaperone cofactor-dependent protein refolding IDA
Inferred from Direct Assay
more info
PubMed 
chaperone-mediated protein complex assembly IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
chaperone-mediated protein complex assembly IMP
Inferred from Mutant Phenotype
more info
PubMed 
cyclooxygenase pathway TAS
Traceable Author Statement
more info
 
positive regulation of phosphorylation IDA
Inferred from Direct Assay
more info
PubMed 
positive regulation of telomerase activity IDA
Inferred from Direct Assay
more info
PubMed 
positive regulation of telomerase activity IMP
Inferred from Mutant Phenotype
more info
PubMed 
prostaglandin biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
prostaglandin biosynthetic process IDA
Inferred from Direct Assay
more info
PubMed 
protein folding IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
protein stabilization IMP
Inferred from Mutant Phenotype
more info
PubMed 
regulation of cellular response to heat TAS
Traceable Author Statement
more info
 
signal transduction TAS
Traceable Author Statement
more info
PubMed 
telomerase holoenzyme complex assembly IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
telomerase holoenzyme complex assembly IDA
Inferred from Direct Assay
more info
PubMed 
telomere maintenance TAS
Traceable Author Statement
more info
PubMed 
telomere maintenance via telomerase IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
telomere maintenance via telomerase IDA
Inferred from Direct Assay
more info
PubMed 
telomere maintenance via telomerase IMP
Inferred from Mutant Phenotype
more info
PubMed 
xenobiotic metabolic process TAS
Traceable Author Statement
more info
 
Component Evidence Code Pubs
chaperone complex IDA
Inferred from Direct Assay
more info
PubMed 
chromosome, telomeric region IC
Inferred by Curator
more info
PubMed 
cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
cytosol IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
cytosol TAS
Traceable Author Statement
more info
 
nucleoplasm TAS
Traceable Author Statement
more info
 
nucleus HDA PubMed 
nucleus IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
protein-containing complex IMP
Inferred from Mutant Phenotype
more info
PubMed 
telomerase holoenzyme complex IDA
Inferred from Direct Assay
more info
PubMed 

General protein information

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

NCBI Reference Sequences (RefSeq)

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_001282601.2NP_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:3109
    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_001282602.2NP_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:395
    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_001282603.2NP_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:376
    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_001282604.1NP_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/Swiss-Prot
    Q15185
    UniProtKB/TrEMBL
    A0A087WYT3
    Related
    ENSP00000482075.1, ENST00000614328.4
    Conserved Domains (1) summary
    cd00237
    Location:7113
    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_001282605.2NP_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:395
    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_006601.7NP_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
    Q15185
    UniProtKB/TrEMBL
    A0A024RB32
    Related
    ENSP00000262033.6, ENST00000262033.11
    Conserved Domains (1) summary
    cd00237
    Location:3109
    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: Homo sapiens Updated Annotation Release 109.

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

Reference GRCh38.p13 Primary Assembly

Genomic

  1. NC_000012.12 Reference GRCh38.p13 Primary Assembly

    Range
    56663341..56689575 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_005268576.5XP_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:7113
    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. XM_006719199.2XP_006719262.1  prostaglandin E synthase 3 isoform X5

    Conserved Domains (1) summary
    cl00175
    Location:799
    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. XM_011537774.2XP_011536076.1  prostaglandin E synthase 3 isoform X4

    Conserved Domains (1) summary
    cd00237
    Location:7113
    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_011537773.2XP_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:3109
    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_017018716.1XP_016874205.1  prostaglandin E synthase 3 isoform X1

    UniProtKB/TrEMBL
    B3KUY2
    Conserved Domains (1) summary
    cd00237
    Location:7113
    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.
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