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PTGES3 prostaglandin E synthase 3 [ Canis lupus familiaris (dog) ]

Gene ID: 612760, updated on 5-Mar-2024

Summary

Official Symbol
PTGES3provided by VGNC
Official Full Name
prostaglandin E synthase 3provided by VGNC
Primary source
VGNC:VGNC:54535
See related
Ensembl:ENSCAFG00845008893
Gene type
protein coding
RefSeq status
MODEL
Organism
Canis lupus familiaris (sub-species: familiaris)
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis
Orthologs
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Genomic context

Location:
chromosome: 10
Exon count:
8
Annotation release Status Assembly Chr Location
106 current ROS_Cfam_1.0 (GCF_014441545.1) 10 NC_051814.1 (895074..912966, complement)
106 current Dog10K_Boxer_Tasha (GCF_000002285.5) 10 NC_006592.4 (948938..967016, complement)
106 current UU_Cfam_GSD_1.0 (GCF_011100685.1) 10 NC_049231.1 (1238847..1256742, complement)
106 current UMICH_Zoey_3.1 (GCF_005444595.1) 10 NC_049270.1 (871924..889991, complement)
106 current UNSW_CanFamBas_1.0 (GCF_013276365.1) 10 NC_049751.1 (1115085..1132100, complement)

Chromosome 10 - NC_051814.1Genomic Context describing neighboring genes Neighboring gene small nucleolar RNA SNORD59 Neighboring gene small nucleolar RNA SNORD59 Neighboring gene ATP synthase F1 subunit beta Neighboring gene nascent polypeptide associated complex subunit alpha Neighboring gene hydroxysteroid 17-beta dehydrogenase 6 Neighboring gene DNA primase subunit 1

Genomic regions, transcripts, and products

General gene information

Markers

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables Hsp90 protein binding IEA
Inferred from Electronic Annotation
more info
PubMed 
enables prostaglandin-E synthase activity IEA
Inferred from Electronic Annotation
more info
PubMed 
enables protein-folding chaperone binding IEA
Inferred from Electronic Annotation
more info
PubMed 
Process Evidence Code Pubs
involved_in chaperone-mediated protein complex assembly IEA
Inferred from Electronic Annotation
more info
PubMed 
involved_in prostaglandin biosynthetic process IEA
Inferred from Electronic Annotation
more info
PubMed 
involved_in protein folding IEA
Inferred from Electronic Annotation
more info
PubMed 
involved_in telomerase holoenzyme complex assembly IEA
Inferred from Electronic Annotation
more info
PubMed 
involved_in telomere maintenance via telomerase IEA
Inferred from Electronic Annotation
more info
PubMed 
Component Evidence Code Pubs
located_in cytosol IEA
Inferred from Electronic Annotation
more info
PubMed 
located_in nucleus IEA
Inferred from Electronic Annotation
more info
PubMed 

General protein information

Preferred Names
prostaglandin E synthase 3
XP_005625578.1
XP_038343760.1
XP_038405651.1
XP_038469614.1
XP_038534974.1

NCBI Reference Sequences (RefSeq)

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RefSeqs of Annotated Genomes: Canis lupus familiaris Annotation Release 106 details...Open this link in a new tab

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

Reference ROS_Cfam_1.0

Genomic

  1. NC_051814.1 Reference ROS_Cfam_1.0

    Range
    895074..912966 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_038679046.1XP_038534974.1  prostaglandin E synthase 3

    UniProtKB/TrEMBL
    A0A8C0S2E1, A0A8I3RUZ5
    Related
    ENSCAFP00845012419.1, ENSCAFT00845015963.1
    Conserved Domains (1) summary
    cd00237
    Location:22128
    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 UMICH_Zoey_3.1

Genomic

  1. NC_049270.1 Alternate UMICH_Zoey_3.1

    Range
    871924..889991 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_038487832.1XP_038343760.1  prostaglandin E synthase 3

    Conserved Domains (1) summary
    cd00237
    Location:22128
    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 UNSW_CanFamBas_1.0

Genomic

  1. NC_049751.1 Alternate UNSW_CanFamBas_1.0

    Range
    1115085..1132100 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_038613686.1XP_038469614.1  prostaglandin E synthase 3

    Conserved Domains (1) summary
    cd00237
    Location:22128
    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 UU_Cfam_GSD_1.0

Genomic

  1. NC_049231.1 Alternate UU_Cfam_GSD_1.0

    Range
    1238847..1256742 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_038549723.1XP_038405651.1  prostaglandin E synthase 3

    UniProtKB/TrEMBL
    A0A8C0S2E1, A0A8I3RUZ5
    Conserved Domains (1) summary
    cd00237
    Location:22128
    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 Dog10K_Boxer_Tasha Primary Assembly

Genomic

  1. NC_006592.4 Alternate Dog10K_Boxer_Tasha Primary Assembly

    Range
    948938..967016 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_005625521.3XP_005625578.1  prostaglandin E synthase 3

    UniProtKB/TrEMBL
    A0A8C0S2E1, A0A8I3RUZ5
    Conserved Domains (1) summary
    cd00237
    Location:22128
    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.