PTGES2
entrez
80142
canonical
uniprot
Q9H7Z7
canonical
ensembl
ENSG00000148334
resolver
ensp
ENSP00000277462
resolver
ensp
ENSP00000345341
resolver
ensp
ENSP00000482913
resolver
ensp
ENSP00000503821
resolver
ensp
ENSP00000504746
resolver
enst
ENST00000277462
resolver
enst
ENST00000338961
resolver
enst
ENST00000617202
resolver
enst
ENST00000677691
resolver
enst
ENST00000678916
resolver
genesymbol
PTGES2
resolver
genesymbol_syn
C9orf15
resolver
genesymbol_syn
PGES2
resolver
hgnc
HGNC:17822
resolver
uniprot
A0A024R8C3
resolver
uniprot
A0A7I2V5X6
resolver
uniprot
A6NHH0
resolver
uniprot
B3KPZ2
resolver
uniprot
B4DWP1
resolver
uniprot
Q53EW9
resolver
uniprot
Q5SYV6
resolver
uniprot
Q96GI0
resolver
uniprot
Q96GL2
resolver
uniprot_entry
A0A7I2V5X6_HUMAN
resolver
uniprot_entry
A6NHH0_HUMAN
resolver
uniprot_entry
B3KPZ2_HUMAN
resolver
uniprot_entry
B4DWP1_HUMAN
resolver
uniprot_entry
PGES2_HUMAN
resolver
uniprot_sec
A0A024R8C3
resolver
uniprot_sec
Q53EW9
resolver
uniprot_sec
Q5SYV6
resolver
uniprot_sec
Q96GI0
resolver
uniprot_sec
Q96GL2
resolver
activity_regulation
ACTIVITY REGULATION: Isomerase activity is increased by sulfhydril compounds. Dithiothreitol (DTT) is most effective, followed by dihydrolipoic acid, glutathione (GSH) and 2-mercaptoethanol. {ECO:0000269|PubMed:12804604}.
uniprot
proteins
amino_acid_sequence
MDPAARVVRALWPGGCALAWRLGGRPQPLLPTQSRAGFAGAAGGPSPVAAARKGSPRLLGAAALALGGALGLYHTARWHLRAQDLHAERSAAQLSLSSRLQLTLYQYKTCPFCSKVRAFLDFHALPYQVVEVNPVRRAEIKFSSYRKVPILVAQEGESSQQLNDSSVIISALKTYLVSGQPLEEIITYYPAMKAVNEQGKEVTEFGNKYWLMLNEKEAQQVYGGKEARTEEMKWRQWADDWLVHLISPNVYRTPTEALASFDYIVREGKFGAVEGAVAKYMGAAAMYLISKRLKSRHRLQDNVREDLYEAADKWVAAVGKDRPFMGGQKPNLADLAVYGVLRVMEGLDAFDDLMQHTHIQPWYLRVERAITEASPAH
uniprot
proteins
ec_number
5.3.99.3
uniprot
proteins
function
FUNCTION: Isomerase that catalyzes the conversion of PGH2 into the more stable prostaglandin E2 (PGE2) (in vitro) (PubMed:12804604, PubMed:17585783, PubMed:18198127). The biological function and the GSH-dependent property of PTGES2 is still under debate (PubMed:17585783, PubMed:18198127). In vivo, PTGES2 could form a complex with GSH and heme and would not participate in PGE2 synthesis but would catalyze the degradation of prostaglandin E2 H2 (PGH2) to 12(S)-hydroxy-5(Z),8(E),10(E)-heptadecatrienoic acid (HHT) and malondialdehyde (MDA) (By similarity) (PubMed:17585783). {ECO:0000250|UniProtKB:Q9N0A4, ECO:0000269|PubMed:12804604, ECO:0000269|PubMed:17585783, ECO:0000269|PubMed:18198127}.
uniprot
proteins
mass_dalton
41943
uniprot
proteins
mutagenesis
MUTAGEN 110; /note="C->S: Loss of prostaglandin-E synthase activity. Can bind glutathione-heme and exhibits PGH2 degradation activity."; /evidence="ECO:0000269|PubMed:12804604, ECO:0000269|PubMed:17585783"; MUTAGEN 113; /note="C->S: Slightly decreased prostaglandin-E synthase activity."; /evidence="ECO:0000269|PubMed:12804604
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
uniprot
proteins
post_translational_modification
PTM: Synthesized as a Golgi membrane-associated protein, and the proteolytic removal of the N-terminal hydrophobic domain leads to the formation of a mature cytosolic enzyme. {ECO:0000269|PubMed:12835322}.
uniprot
proteins
protein_family
GST superfamily
uniprot
proteins
pubmed
11866447
uniprot
proteins
pubmed
12804604
uniprot
proteins
pubmed
12835322
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15231747
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17585783
uniprot
proteins
pubmed
18198127
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
sequence_length
377
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:12835322}; Single-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Prostaglandin E synthase 2 truncated form]: Cytoplasm, perinuclear region {ECO:0000269|PubMed:12835322}. Note=Synthesized as a Golgi membrane-bound protein, which is further cleaved into the predominant soluble truncated form. The truncated form is cytoplasmic and is enriched in the perinuclear region. {ECO:0000269|PubMed:12835322}.
uniprot
proteins
transmembrane_region
TRANSMEM 58..74; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins