Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods
Falcon deep research synthesis for PTGES3
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PTGES3 is bifunctional: a cytosolic glutathione-dependent prostaglandin E synthase and the p23 HSP90 co-chaperone that stabilizes ATP-bound HSP90 closed states.
"PTGES3/cPGES is annotated to catalyze the isomerization/conversion of prostaglandin H2 (PGH2) to prostaglandin E2 (PGE2), and PTGES3 is explicitly identified as the co-chaperone p23 in authoritative HSP90 machinery literature."
Functional requirement of p23 and Hsp90 in telomerase complexes.
An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function.
Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone.
Molecular identification of cytosolic prostaglandin E2 synthase that is functionally coupled with cyclooxygenase-1 in immediate prostaglandin E2 biosynthesis.
Disassembly of transcriptional regulatory complexes by molecular chaperones.
Differential regulation of telomerase activity by six telomerase subunits.
Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system.
Large-scale mapping of human protein-protein interactions by mass spectrometry.
A truncated form of p23 down-regulates telomerase activity via disruption of Hsp90 function.
Curcumin inhibits nuclear localization of telomerase by dissociating the Hsp90 co-chaperone p23 from hTERT.
A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting protein.
N-terminal domain of human Hsp90 triggers binding to the cochaperone p23.
Proteomic characterization of the human sperm nucleus.
Toward an understanding of the protein interaction network of the human liver.
Hsp90 cochaperones p23 and FKBP4 physically interact with hAgo2 and activate RNA interference-mediated silencing in mammalian cells.
Human-chromatin-related protein interactions identify a demethylase complex required for chromosome segregation.
A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways.
The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding.
Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
OpenCell: Endogenous tagging for the cartography of human cellular organization.
Chr21 protein-protein interactions: enrichment in proteins involved in intellectual disability, autism, and late-onset Alzheimer's disease.
Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes.
In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis.
Synthesis of Prostaglandins (PG) and Thromboxanes (TX)
Prostaglandin E synthase isomerizes PGH2 to PGE2
Dissociation of cytosolic HSF1:HSP90 complex
Dissociation of HSF1:HSP90 complex in the nucleus
HSP90:FKBP4:PTGES3 binds HSF1 trimer
Dissociation of cytosolic HSF1:HSP90:HDAC6:PTGES3 upon sensing protein aggregates
FKBP4 replaces FKBP5 within HSP90:ATP:FKBP5:unfolded protein
HSP90:ATP:p23:FKBP52:SHR:SH translocates to the nucleus
p23 (PTGES3) binds HSP90:ATP:FKBP5:nascent protein
NR3C2 ligands bind NR3C2 (in the HSP90 chaperone complex)
p23 (PTGES3) binds HSP90:ATP:FKBP4:nascent protein
AHR:2xHSP90:AIP:PTGES3 binds TCDD
AHR:TCDD:2xHSP90AB1:AIP:PTGES3 translocates from cytosol to nucleoplasm
AHR:TCDD:2xHSP90AB1:AIP:PTGES3 dissociates
HSP90-dependent ATP hydrolysis promotes release of ESR:ESTG from chaperone complex
ESTG binds ESR1:chaperone complex
Estrogen-independent phosphorylation of ESR1 S118 by MAPK1 and MAPK3
Progesterone stimulation promotes PGR:P4 binding to ESR1:ESTG
NR3C1 binds NR3C1 agonists
NR3C1 ligands bind NR3C1 (in the HSP90 chaperone complex)
Androgens binds AR (in the HSP90 chaperone complex)
ESTG binds ESR2:chaperone complex
ESR1 binds ESR1 antagonists
NR3C2 binds NR3C2 antagonists
P4 bind PGR (in the HSP90 chaperone complex)
NR3C2 binds fludrocortisone
PGR binds PGR antagonists
The HSP90 chaperone machinery.
The p23 co-chaperone is a succinate-activated COX-2 transcription factor in lung adenocarcinoma tumorigenesis.
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Nuclear p23/PTGES3 functions as an HSP90-independent transcription factor for COX-2 (PTGS2), driven by succinate-dependent lysine succinylation at K7, K33, and K79 that promotes nuclear translocation
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Nuclear p23 expression was detected in >90% of lung adenocarcinoma tumor tissues versus ~5% of adjacent normal tissues
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Small-molecule inhibitor M16 inhibits p23 succinylation and nuclear translocation, suppressing tumor growth in a p23-dependent manner
HSP90 multi-functionality in cancer.