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Protein

Prostaglandin E synthase 3

Gene

PTGES3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) (PubMed:10922363). Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes (PubMed:11274138, PubMed:12077419). Facilitates HIF alpha proteins hydroxylation via interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway (PubMed:24711448).4 Publications

Caution

Catalytic activityi

(5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate.1 Publication

Kineticsi

  1. KM=14 µM for PGH21 Publication
  1. Vmax=190 nmol/min/mg enzyme toward PGH21 Publication

Pathwayi: prostaglandin biosynthesis

This protein is involved in the pathway prostaglandin biosynthesis, which is part of Lipid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway prostaglandin biosynthesis and in Lipid metabolism.

GO - Molecular functioni

  • DNA polymerase binding Source: BHF-UCL
  • Hsp90 protein binding Source: CAFA
  • prostaglandin-E synthase activity Source: UniProtKB
  • telomerase activity Source: UniProtKB
  • unfolded protein binding Source: UniProtKB

GO - Biological processi

  • chaperone cofactor-dependent protein refolding Source: UniProtKB
  • chaperone-mediated protein complex assembly Source: CAFA
  • cyclooxygenase pathway Source: Reactome
  • positive regulation of phosphorylation Source: BHF-UCL
  • positive regulation of telomerase activity Source: BHF-UCL
  • prostaglandin biosynthetic process Source: UniProtKB
  • protein stabilization Source: CAFA
  • regulation of cellular response to heat Source: Reactome
  • signal transduction Source: ProtInc
  • telomerase holoenzyme complex assembly Source: BHF-UCL
  • telomere maintenance Source: UniProtKB
  • telomere maintenance via telomerase Source: BHF-UCL
  • xenobiotic metabolic process Source: Reactome

Keywordsi

Molecular functionChaperone, Isomerase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism

Enzyme and pathway databases

BioCyciMetaCyc:HS03359-MONOMER
ReactomeiR-HSA-2162123 Synthesis of Prostaglandins (PG) and Thromboxanes (TX)
R-HSA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-HSA-3371511 HSF1 activation
R-HSA-3371568 Attenuation phase
R-HSA-8937144 Aryl hydrocarbon receptor signalling
SABIO-RKiQ15185
SIGNORiQ15185
UniPathwayiUPA00662

Chemistry databases

SwissLipidsiSLP:000000831

Names & Taxonomyi

Protein namesi
Recommended name:
Prostaglandin E synthase 3 (EC:5.3.99.31 Publication)
Alternative name(s):
Cytosolic prostaglandin E2 synthase
Short name:
cPGES
Hsp90 co-chaperone
Progesterone receptor complex p23
Telomerase-binding protein p23
Gene namesi
Name:PTGES3
Synonyms:P23, TEBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000110958.15
HGNCiHGNC:16049 PTGES3
MIMi607061 gene
neXtProtiNX_Q15185

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi10728
OpenTargetsiENSG00000110958
PharmGKBiPA142671118

Chemistry databases

ChEMBLiCHEMBL3341580
DrugBankiDB05036 Grn163l

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002189521 – 160Prostaglandin E synthase 3Add BLAST160

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei33N6-acetyllysineCombined sources1
Cross-linki35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei44PhosphoserineCombined sources1
Cross-linki65Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei85PhosphoserineCombined sources1
Modified residuei100PhosphoserineBy similarity1
Modified residuei113PhosphoserineCombined sources1 Publication1
Modified residuei118PhosphoserineCombined sources1
Modified residuei148PhosphoserineCombined sources1
Modified residuei151PhosphoserineCombined sources1
Isoform 4 (identifier: Q15185-4)
Modified residuei130PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ15185
MaxQBiQ15185
PaxDbiQ15185
PeptideAtlasiQ15185
PRIDEiQ15185
TopDownProteomicsiQ15185-1 [Q15185-1]

PTM databases

iPTMnetiQ15185
PhosphoSitePlusiQ15185
SwissPalmiQ15185

Expressioni

Gene expression databases

BgeeiENSG00000110958
CleanExiHS_PTGES3
ExpressionAtlasiQ15185 baseline and differential
GenevisibleiQ15185 HS

Organism-specific databases

HPAiCAB034319
HPA038672
HPA038673

Interactioni

Subunit structurei

Probably forms a complex composed of chaperones HSP90 and HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and client protein TSC2 (PubMed:29127155). Binds to the progesterone receptor (PubMed:8114727). Interacts with TERT; the interaction, together with HSP90AA1, is required for correct assembly and stabilization of the telomerase holoenzyme complex (PubMed:11274138). Interacts (via PXLE motif) with EGLN1/PHD2, recruiting EGLN1/PHD2 to the HSP90 pathway to facilitate HIF alpha proteins hydroxylation (PubMed:24711448). Interacts with HSP90AA1, FLCN, FNIP1 and FNIP2 (PubMed:27353360).4 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • DNA polymerase binding Source: BHF-UCL
  • Hsp90 protein binding Source: CAFA
  • unfolded protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115952106 interactors.
CORUMiQ15185
DIPiDIP-279N
ELMiQ15185
IntActiQ15185 58 interactors.
STRINGi9606.ENSP00000262033

Structurei

Secondary structure

1160
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 10Combined sources5
Beta strandi12 – 19Combined sources8
Beta strandi24 – 32Combined sources9
Beta strandi35 – 42Combined sources8
Turni43 – 46Combined sources4
Beta strandi47 – 57Combined sources11
Beta strandi59 – 68Combined sources10
Beta strandi73 – 81Combined sources9
Beta strandi87 – 92Combined sources6
Beta strandi99 – 101Combined sources3
Turni103 – 105Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EJFX-ray2.49A/B1-125[»]
1LG0model-A1-110[»]
DisProtiDP00358
ProteinModelPortaliQ15185
SMRiQ15185
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15185

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 90CSPROSITE-ProRule annotationAdd BLAST90

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi157 – 160PXLE motif1 Publication4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi108 – 160Asp/Glu-richAdd BLAST53

Domaini

The PXLE motif mediates interaction with EGLN1/PHD2.1 Publication

Sequence similaritiesi

Belongs to the p23/wos2 family.Curated

Phylogenomic databases

eggNOGiKOG3158 Eukaryota
ENOG41121RT LUCA
GeneTreeiENSGT00510000046493
HOGENOMiHOG000177563
HOVERGENiHBG002143
InParanoidiQ15185
KOiK15730
PhylomeDBiQ15185
TreeFamiTF315077

Family and domain databases

Gene3Di2.60.40.7901 hit
InterProiView protein in InterPro
IPR007052 CS_dom
IPR008978 HSP20-like_chaperone
PfamiView protein in Pfam
PF04969 CS, 1 hit
SUPFAMiSSF49764 SSF49764, 1 hit
PROSITEiView protein in PROSITE
PS51203 CS, 1 hit

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15185-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MQPASAKWYD RRDYVFIEFC VEDSKDVNVN FEKSKLTFSC LGGSDNFKHL
60 70 80 90 100
NEIDLFHCID PNDSKHKRTD RSILCCLRKG ESGQSWPRLT KERAKLNWLS
110 120 130 140 150
VDFNNWKDWE DDSDEDMSNF DRFSEMMNNM GGDEDVDLPE VDGADDDSQD
160
SDDEKMPDLE
Length:160
Mass (Da):18,697
Last modified:November 1, 1996 - v1
Checksum:i23538BB9D7AFD73F
GO
Isoform 2 (identifier: Q15185-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     63-95: Missing.

Note: No experimental confirmation available.
Show »
Length:127
Mass (Da):14,844
Checksum:i6C189780960CB97D
GO
Isoform 3 (identifier: Q15185-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     96-125: Missing.

Note: No experimental confirmation available.
Show »
Length:130
Mass (Da):14,959
Checksum:iDAA51580AD82CA72
GO
Isoform 4 (identifier: Q15185-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     126-146: Missing.

Note: No experimental confirmation available.Combined sources
Show »
Length:139
Mass (Da):16,476
Checksum:i9582520CFE2A0C5A
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_05536363 – 95Missing in isoform 2. 1 PublicationAdd BLAST33
Alternative sequenceiVSP_05536496 – 125Missing in isoform 3. 1 PublicationAdd BLAST30
Alternative sequenceiVSP_055365126 – 146Missing in isoform 4. 1 PublicationAdd BLAST21

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L24804 mRNA Translation: AAA18537.1
AK291945 mRNA Translation: BAF84634.1
AK295208 mRNA Translation: BAG58204.1
AK298147 mRNA Translation: BAG60423.1
AK298160 mRNA Translation: BAG60433.1
AC117378 Genomic DNA No translation available.
CH471054 Genomic DNA Translation: EAW96953.1
CH471054 Genomic DNA Translation: EAW96958.1
BC003005 mRNA Translation: AAH03005.1
BC021167 mRNA Translation: AAH21167.1
CCDSiCCDS31836.1 [Q15185-1]
CCDS61158.1 [Q15185-2]
CCDS61159.1 [Q15185-3]
CCDS61160.1 [Q15185-4]
PIRiA56211
RefSeqiNP_001269530.1, NM_001282601.1 [Q15185-4]
NP_001269531.1, NM_001282602.1 [Q15185-3]
NP_001269532.1, NM_001282603.1 [Q15185-2]
NP_001269533.1, NM_001282604.1
NP_001269534.1, NM_001282605.1
NP_006592.3, NM_006601.6 [Q15185-1]
UniGeneiHs.50425

Genome annotation databases

EnsembliENST00000262033; ENSP00000262033; ENSG00000110958 [Q15185-1]
ENST00000414274; ENSP00000405299; ENSG00000110958 [Q15185-3]
ENST00000436399; ENSP00000402385; ENSG00000110958 [Q15185-2]
ENST00000448157; ENSP00000414892; ENSG00000110958 [Q15185-4]
GeneIDi10728
KEGGihsa:10728
UCSCiuc001slu.6 human [Q15185-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiTEBP_HUMAN
AccessioniPrimary (citable) accession number: Q15185
Secondary accession number(s): A8K7D0
, B4DHP2, B4DP11, B4DP21, Q8WU70
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: April 25, 2018
This is version 179 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome