Details for: PTGES3

Gene ID: 10728

Symbol: PTGES3

Ensembl ID: ENSG00000110958

Description: prostaglandin E synthase 3

Associated with

Other Information

Genular Protein ID: 928917070

Symbol: TEBP_HUMAN

Name: Prostaglandin E synthase 3

UniProtKB Accession Codes:

Q15185 A8K7D0 B4DHP2 B4DP11 B4DP21 Q8WU70

Database IDs:

AGR 1 AlphaFoldDB 1 Antibodypedia 1 BMRB 1 Bgee 1 BioCyc 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 4 CDD 1 CORUM 1 CTD 1 ChEBI 2 ChEMBL 1 ChiTaRS 1 DIP 1 DNASU 1 DisGeNET 1 DisProt 1 DrugBank 3 EC 1 ELM 1 EMBL 10 EMDB 5 EPD 1 Ensembl 4 EvolutionaryTrace 1 ExpressionAtlas 1 GO 30 Gene3D 1 GeneCards 1 GeneTree 1 GeneWiki 1 Genevisible 1 GenomeRNAi 1 GlyGen 1 HGNC 1 HPA 1 InParanoid 1 IntAct 1 InterPro 3 KEGG 1 MANE-Select 1 MIM 1 MINT 1 MassIVE 1 MaxQB 1 NCBI Taxonomy 1 OpenTargets 1 OrthoDB 1 PANTHER 2 PDB 6 PDBsum 4 PIR 1 PRIDE 1 PRO 1 PROSITE 1 PROSITE-ProRule 1 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 1 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 4 Pumba 1 RNAct 1 Reactome 8 RefSeq 6 Rhea 1 SABIO-RK 1 SAM 1 SASBDB 1 SIGNOR 1 SMR 1 STRING 1 SUPFAM 1 SignaLink 1 SwissLipids 1 SwissPalm 1 TopDownProteomics 1 TreeFam 1 UCSC 1 UniPathway 1 UniProtKB 2 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 8114727

Title: Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes.

PubMed ID: 8114727

DOI: 10.1128/mcb.14.3.1956-1963.1994

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 16541075

Title: The finished DNA sequence of human chromosome 12.

PubMed ID: 16541075

DOI: 10.1038/nature04569

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 11274138

Title: Stable association of hsp90 and p23, but Not hsp70, with active human telomerase.

PubMed ID: 11274138

DOI: 10.1074/jbc.c100055200

PubMed ID: 12077419

Title: Disassembly of transcriptional regulatory complexes by molecular chaperones.

PubMed ID: 12077419

DOI: 10.1126/science.1073051

PubMed ID: 10922363

Title: Molecular identification of cytosolic prostaglandin E2 synthase that is functionally coupled with cyclooxygenase-1 in immediate prostaglandin E2 biosynthesis.

PubMed ID: 10922363

DOI: 10.1074/jbc.m003504200

PubMed ID: 14654843

Title: Proteomic characterization of the human centrosome by protein correlation profiling.

PubMed ID: 14654843

DOI: 10.1038/nature02166

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16807684

Title: Phosphoproteomic analysis of the human pituitary.

PubMed ID: 16807684

DOI: 10.1007/s11102-006-8916-x

PubMed ID: 17487921

Title: Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line.

PubMed ID: 17487921

DOI: 10.1002/elps.200600782

PubMed ID: 19367720

Title: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.

PubMed ID: 19367720

DOI: 10.1021/pr800500r

PubMed ID: 18088087

Title: Phosphoproteome of resting human platelets.

PubMed ID: 18088087

DOI: 10.1021/pr0704130

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 18318008

Title: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.

PubMed ID: 18318008

DOI: 10.1002/pmic.200700884

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19369195

Title: Large-scale proteomics analysis of the human kinome.

PubMed ID: 19369195

DOI: 10.1074/mcp.m800588-mcp200

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22451931

Title: Caspase-7 uses an exosite to promote poly(ADP ribose) polymerase 1 proteolysis.

PubMed ID: 22451931

DOI: 10.1073/pnas.1200934109

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24711448

Title: Defective Tibetan PHD2 binding to p23 links high altitude adaption to altered oxygen sensing.

PubMed ID: 24711448

DOI: 10.1074/jbc.m113.541227

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 27353360

Title: The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding.

PubMed ID: 27353360

DOI: 10.1038/ncomms12037

PubMed ID: 28863261

Title: Characterization of Hsp90 co-chaperone p23 cleavage by caspase-7 uncovers a peptidase-substrate interaction involving intrinsically disordered regions.

PubMed ID: 28863261

DOI: 10.1021/acs.biochem.7b00298

PubMed ID: 29127155

Title: Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients.

PubMed ID: 29127155

DOI: 10.15252/embj.201796700

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 10811660

Title: Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone.

PubMed ID: 10811660

DOI: 10.1074/jbc.m003410200

Sequence Information:

  • Length: 160
  • Mass: 18697
  • Checksum: 23538BB9D7AFD73F
  • Sequence:
    • MQPASAKWYD RRDYVFIEFC VEDSKDVNVN FEKSKLTFSC LGGSDNFKHL NEIDLFHCID 
PNDSKHKRTD RSILCCLRKG ESGQSWPRLT KERAKLNWLS VDFNNWKDWE DDSDEDMSNF 
DRFSEMMNNM GGDEDVDLPE VDGADDDSQD SDDEKMPDLE

Genular Protein ID: 1645611720

Symbol: A0A087WYT3_HUMAN

Name: N/A

UniProtKB Accession Codes:

A0A087WYT3

Database IDs:

ARBA 14 AlphaFoldDB 1 Antibodypedia 1 Bgee 1 BioGRID-ORCS 1 CDD 1 CTD 1 ChEBI 2 ChiTaRS 1 DNASU 1 EC 1 EMBL 1 EPD 1 Ensembl 2 ExpressionAtlas 1 GO 5 Gene3D 1 GeneTree 1 GenomeRNAi 1 HGNC 1 IntAct 1 InterPro 3 MassIVE 1 MaxQB 1 NCBI Taxonomy 1 OMA 1 OrthoDB 1 PANTHER 2 PROSITE 2 PeptideAtlas 1 Pfam 1 Proteomes 2 RefSeq 1 Rhea 1 RuleBase 1 SAM 1 SMR 1 SUPFAM 1 UCSC 1 UniPathway 1 VEuPathDB 1

Citations:

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16541075

Title: The finished DNA sequence of human chromosome 12.

PubMed ID: 16541075

DOI: 10.1038/nature04569

PubMed ID: 16807684

Title: Phosphoproteomic analysis of the human pituitary.

PubMed ID: 16807684

DOI: 10.1007/s11102-006-8916-x

PubMed ID: 17487921

Title: Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line.

PubMed ID: 17487921

DOI: 10.1002/elps.200600782

PubMed ID: 18088087

Title: Phosphoproteome of resting human platelets.

PubMed ID: 18088087

DOI: 10.1021/pr0704130

PubMed ID: 19367720

Title: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.

PubMed ID: 19367720

DOI: 10.1021/pr800500r

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 18318008

Title: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.

PubMed ID: 18318008

DOI: 10.1002/pmic.200700884

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19369195

Title: Large-scale proteomics analysis of the human kinome.

PubMed ID: 19369195

DOI: 10.1074/mcp.M800588-MCP200

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

Sequence Information:

  • Length: 164
  • Mass: 19155
  • Checksum: 6CBD3E481BE9E81A
  • Sequence:
    • MSLEKQPASA KWYDRRDYVF IEFCVEDSKD VNVNFEKSKL TFSCLGGSDN FKHLNEIDLF 
HCIDPNDSKH KRTDRSILCC LRKGESGQSW PRLTKERAKL NWLSVDFNNW KDWEDDSDED 
MSNFDRFSEM MNNMGGDEDV DLPEVDGADD DSQDSDDEKM PDLE

Genular Protein ID: 1980650312

Symbol: B3KUY2_HUMAN

Name: N/A

UniProtKB Accession Codes:

B3KUY2

Database IDs:

ARBA 14 AlphaFoldDB 1 BioGRID-ORCS 1 CDD 1 CTD 1 ChEBI 2 ChiTaRS 1 DNASU 1 EC 1 EMBL 4 GO 5 Gene3D 1 GenomeRNAi 1 IntAct 1 InterPro 3 MaxQB 1 NCBI Taxonomy 1 OrthoDB 1 PANTHER 2 PROSITE 2 PeptideAtlas 1 Pfam 1 RefSeq 1 Rhea 1 RuleBase 1 SUPFAM 1 UniPathway 1

Citations:

PubMed ID: 11181995

Title: The sequence of the human genome.

PubMed ID: 11181995

DOI: 10.1126/science.1058040

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

Sequence Information:

  • Length: 165
  • Mass: 19449
  • Checksum: 054C08D184610439
  • Sequence:
    • MFYLRQPASA KWYDRRDYVF IEFCVEDSKD VNVNFEKSKL TFSCLGGSDN FKHLNEIDLF 
HCIDPNDSKH KRTDRSILCC LRKGESGQSW PRLTKERAKL NWLSVDFNNW KDWEDDSDED 
MSNFDRFSEM MNNMGGDEDV DLPEVDGADD VSLKILFSVY FHTIK

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.