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Protein

Prostaglandin E synthase

Gene

PTGES

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2).1 Publication

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

Cofactori

glutathione1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei117 – 1171Glutathione
Binding sitei126 – 1261Glutathione
Binding sitei130 – 1301Glutathione
Binding sitei134 – 1341Glutathione

GO - Molecular functioni

  1. glutathione binding Source: UniProtKB
  2. prostaglandin-E synthase activity Source: UniProtKB

GO - Biological processi

  1. acute inflammatory response Source: Ensembl
  2. arachidonic acid metabolic process Source: Reactome
  3. chronic inflammatory response Source: Ensembl
  4. cyclooxygenase pathway Source: Reactome
  5. negative regulation of cell proliferation Source: Ensembl
  6. prostaglandin biosynthetic process Source: UniProtKB
  7. prostaglandin metabolic process Source: ProtInc
  8. response to calcium ion Source: Ensembl
  9. response to cytokine Source: Ensembl
  10. response to lipopolysaccharide Source: Ensembl
  11. response to organic cyclic compound Source: Ensembl
  12. response to retinoic acid Source: Ensembl
  13. signal transduction Source: ProtInc
  14. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism

Enzyme and pathway databases

BioCyciMetaCyc:HS07518-MONOMER.
BRENDAi5.3.99.3. 2681.
ReactomeiREACT_150149. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).

Names & Taxonomyi

Protein namesi
Recommended name:
Prostaglandin E synthase (EC:5.3.99.3)
Alternative name(s):
Microsomal glutathione S-transferase 1-like 1
Short name:
MGST1-L1
Microsomal prostaglandin E synthase 1
Short name:
MPGES-1
p53-induced gene 12 protein
Gene namesi
Name:PTGES
Synonyms:MGST1L1, MPGES1, PGES, PIG12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:9599. PTGES.

Subcellular locationi

Membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212LumenalAdd
BLAST
Transmembranei13 – 4129HelicalAdd
BLAST
Topological domaini42 – 6019CytoplasmicAdd
BLAST
Transmembranei61 – 9030HelicalAdd
BLAST
Topological domaini91 – 955Lumenal
Transmembranei96 – 11924HelicalAdd
BLAST
Topological domaini120 – 1234Cytoplasmic
Transmembranei124 – 15229HelicalAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: Reactome
  2. integral component of membrane Source: UniProtKB
  3. membrane Source: ProtInc
  4. nuclear envelope lumen Source: Ensembl
  5. perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi66 – 661E → A: Reduces enzyme activity by 50%. 1 Publication
Mutagenesisi67 – 671R → A: Loss of enzyme activity. 1 Publication
Mutagenesisi70 – 701R → A: Slightly reduced enzyme activity. 1 Publication
Mutagenesisi72 – 721H → A: Reduces enzyme activity by 70%. 1 Publication
Mutagenesisi110 – 1101R → A or S: Loss of enzyme activity. 1 Publication
Mutagenesisi117 – 1171Y → A: Loss of enzyme activity. 1 Publication
Mutagenesisi117 – 1171Y → F: No effect on enzyme activity. 1 Publication

Organism-specific databases

PharmGKBiPA33948.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 152152Prostaglandin E synthasePRO_0000217745Add
BLAST

Proteomic databases

MaxQBiO14684.
PaxDbiO14684.
PeptideAtlasiO14684.
PRIDEiO14684.

Expressioni

Inductioni

By p53/TP53.1 Publication

Gene expression databases

BgeeiO14684.
CleanExiHS_PTGES.
ExpressionAtlasiO14684. baseline and differential.
GenevestigatoriO14684.

Organism-specific databases

HPAiHPA045064.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

BioGridi114912. 2 interactions.
STRINGi9606.ENSP00000342385.

Structurei

Secondary structure

1
152
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 4129Combined sources
Beta strandi44 – 463Combined sources
Helixi47 – 526Combined sources
Helixi56 – 583Combined sources
Helixi63 – 9028Combined sources
Helixi96 – 11823Combined sources
Helixi125 – 15026Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DWWelectron microscopy3.50A/B/C1-152[»]
4AL0X-ray1.16A1-152[»]
4AL1X-ray1.95A1-152[»]
4BPMX-ray2.08A10-152[»]
4WABX-ray2.70A10-151[»]
ProteinModelPortaliO14684.
SMRiO14684. Positions 7-152.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO14684.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni28 – 3811Glutathione bindingAdd
BLAST
Regioni70 – 778Glutathione binding
Regioni110 – 1134Glutathione binding

Sequence similaritiesi

Belongs to the MAPEG family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG67817.
GeneTreeiENSGT00390000011980.
HOGENOMiHOG000231759.
HOVERGENiHBG052470.
InParanoidiO14684.
KOiK15729.
OMAiKMYVVAV.
OrthoDBiEOG7288T0.
PhylomeDBiO14684.
TreeFamiTF105327.

Family and domain databases

Gene3Di1.20.120.550. 1 hit.
InterProiIPR023352. MAPEG-like_dom.
IPR001129. Membr-assoc_MAPEG.
[Graphical view]
PfamiPF01124. MAPEG. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O14684-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAHSLVMSS PALPAFLLCS TLLVIKMYVV AIITGQVRLR KKAFANPEDA
60 70 80 90 100
LRHGGPQYCR SDPDVERCLR AHRNDMETIY PFLFLGFVYS FLGPNPFVAW
110 120 130 140 150
MHFLVFLVGR VAHTVAYLGK LRAPIRSVTY TLAQLPCASM ALQILWEAAR

HL
Length:152
Mass (Da):17,102
Last modified:May 30, 2000 - v2
Checksum:iBF9B9ED81CA67A3D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551G → GG in AAC39534 (PubMed:9305847).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF010316 mRNA. Translation: AAC39534.1.
AF027740 mRNA. Translation: AAB82299.1.
AJ271802, AJ271803, AJ271804 Genomic DNA. Translation: CAB72099.1.
AK311947 mRNA. Translation: BAG34888.1.
EF543149 Genomic DNA. Translation: ABQ01233.1.
AL590369, AL592219 Genomic DNA. Translation: CAI14506.1.
AL592219, AL590369 Genomic DNA. Translation: CAI16116.1.
BC008280 mRNA. Translation: AAH08280.1.
CCDSiCCDS6927.1.
RefSeqiNP_004869.1. NM_004878.4.
UniGeneiHs.146688.

Genome annotation databases

EnsembliENST00000340607; ENSP00000342385; ENSG00000148344.
GeneIDi9536.
KEGGihsa:9536.
UCSCiuc004byi.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF010316 mRNA. Translation: AAC39534.1.
AF027740 mRNA. Translation: AAB82299.1.
AJ271802, AJ271803, AJ271804 Genomic DNA. Translation: CAB72099.1.
AK311947 mRNA. Translation: BAG34888.1.
EF543149 Genomic DNA. Translation: ABQ01233.1.
AL590369, AL592219 Genomic DNA. Translation: CAI14506.1.
AL592219, AL590369 Genomic DNA. Translation: CAI16116.1.
BC008280 mRNA. Translation: AAH08280.1.
CCDSiCCDS6927.1.
RefSeqiNP_004869.1. NM_004878.4.
UniGeneiHs.146688.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DWWelectron microscopy3.50A/B/C1-152[»]
4AL0X-ray1.16A1-152[»]
4AL1X-ray1.95A1-152[»]
4BPMX-ray2.08A10-152[»]
4WABX-ray2.70A10-151[»]
ProteinModelPortaliO14684.
SMRiO14684. Positions 7-152.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114912. 2 interactions.
STRINGi9606.ENSP00000342385.

Chemistry

BindingDBiO14684.
ChEMBLiCHEMBL5658.

Proteomic databases

MaxQBiO14684.
PaxDbiO14684.
PeptideAtlasiO14684.
PRIDEiO14684.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000340607; ENSP00000342385; ENSG00000148344.
GeneIDi9536.
KEGGihsa:9536.
UCSCiuc004byi.3. human.

Organism-specific databases

CTDi9536.
GeneCardsiGC09M132500.
HGNCiHGNC:9599. PTGES.
HPAiHPA045064.
MIMi605172. gene.
neXtProtiNX_O14684.
PharmGKBiPA33948.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG67817.
GeneTreeiENSGT00390000011980.
HOGENOMiHOG000231759.
HOVERGENiHBG052470.
InParanoidiO14684.
KOiK15729.
OMAiKMYVVAV.
OrthoDBiEOG7288T0.
PhylomeDBiO14684.
TreeFamiTF105327.

Enzyme and pathway databases

BioCyciMetaCyc:HS07518-MONOMER.
BRENDAi5.3.99.3. 2681.
ReactomeiREACT_150149. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).

Miscellaneous databases

ChiTaRSiPTGES. human.
EvolutionaryTraceiO14684.
GeneWikiiPTGES.
GenomeRNAii9536.
NextBioi35754.
PROiO14684.
SOURCEiSearch...

Gene expression databases

BgeeiO14684.
CleanExiHS_PTGES.
ExpressionAtlasiO14684. baseline and differential.
GenevestigatoriO14684.

Family and domain databases

Gene3Di1.20.120.550. 1 hit.
InterProiIPR023352. MAPEG-like_dom.
IPR001129. Membr-assoc_MAPEG.
[Graphical view]
PfamiPF01124. MAPEG. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION BY TP53.
    Tissue: Colon cancer.
  2. "Identification of human prostaglandin E synthase: a microsomal, glutathione-dependent, inducible enzyme, constituting a potential novel drug target."
    Jakobsson P.-J., Thoren S., Morgenstern R., Samuelsson B.
    Proc. Natl. Acad. Sci. U.S.A. 96:7220-7225(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Human glutathione dependent prostaglandin E synthase: gene structure and regulation."
    Forsberg L., Leeb L., Thoren S., Morgenstern R., Jakobsson P.J.
    FEBS Lett. 471:78-82(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary gland.
  5. SeattleSNPs variation discovery resource
    Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pancreas.
  8. "Purification and characterization of recombinant microsomal prostaglandin E synthase-1."
    Ouellet M., Falgueyret J.-P., Ear P.H., Pen A., Mancini J.A., Riendeau D., Percival M.D.
    Protein Expr. Purif. 26:489-495(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME KINETICS.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Human microsomal prostaglandin E synthase-1: purification, functional characterization, and projection structure determination."
    Thoren S., Weinander R., Saha S., Jegerschold C., Pettersson P.L., Samuelsson B., Hebert H., Hamberg M., Morgenstern R., Jakobsson P.-J.
    J. Biol. Chem. 278:22199-22209(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON CRYOMICROSCOPY.
  11. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.5 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, TRANSMEMBRANE TOPOLOGY, MUTAGENESIS OF GLU-66; ARG-67; ARG-70; HIS-72; ARG-110 AND TYR-117.
  12. "Crystal structure of microsomal prostaglandin E2 synthase provides insight into diversity in the MAPEG superfamily."
    Sjogren T., Nord J., Ek M., Johansson P., Liu G., Geschwindner S.
    Proc. Natl. Acad. Sci. U.S.A. 110:3806-3811(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS) IN COMPLEXES WITH GLUTATIONE, SUBUNIT, PROBABLE TOPOLOGY.

Entry informationi

Entry nameiPTGES_HUMAN
AccessioniPrimary (citable) accession number: O14684
Secondary accession number(s): O14900, Q5SZC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: March 4, 2015
This is version 120 of the entry and version 2 of the sequence. [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, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.