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O14684

- PTGES_HUMAN

UniProt

O14684 - PTGES_HUMAN

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Protein

Prostaglandin E synthase

Gene
PTGES, MGST1L1, MPGES1, PGES, PIG12
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Glutathione.1 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: Chromosome 9

Organism-specific databases

HGNCiHGNC:9599. PTGES.

Subcellular locationi

Membrane; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212Lumenal2 PublicationsAdd
BLAST
Transmembranei13 – 4129HelicalAdd
BLAST
Topological domaini42 – 6019Cytoplasmic2 PublicationsAdd
BLAST
Transmembranei61 – 9030HelicalAdd
BLAST
Topological domaini91 – 955Lumenal2 Publications
Transmembranei96 – 11924HelicalAdd
BLAST
Topological domaini120 – 1234Cytoplasmic2 Publications
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.
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 – 4129
Beta strandi44 – 463
Helixi47 – 526
Helixi56 – 583
Helixi63 – 9028
Helixi96 – 11823
Helixi125 – 15026

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DWWelectron microscopy3.50A/B/C1-152[»]
4AL0X-ray1.16A1-152[»]
4AL1X-ray1.95A1-152[»]
4BPMX-ray2.08A10-152[»]
ProteinModelPortaliO14684.
SMRiO14684. Positions 7-152.

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.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG67817.
HOGENOMiHOG000231759.
HOVERGENiHBG052470.
InParanoidiO14684.
KOiK15729.
OMAiGLQYCRS.
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

MPAHSLVMSS PALPAFLLCS TLLVIKMYVV AIITGQVRLR KKAFANPEDA    50
LRHGGPQYCR SDPDVERCLR AHRNDMETIY PFLFLGFVYS FLGPNPFVAW 100
MHFLVFLVGR VAHTVAYLGK LRAPIRSVTY TLAQLPCASM ALQILWEAAR 150
HL 152
Length:152
Mass (Da):17,102
Last modified:May 30, 2000 - v2
Checksum:iBF9B9ED81CA67A3D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551G → GG in AAC39534. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS6927.1.
RefSeqi NP_004869.1. NM_004878.4.
UniGenei Hs.146688.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3DWW electron microscopy 3.50 A/B/C 1-152 [» ]
4AL0 X-ray 1.16 A 1-152 [» ]
4AL1 X-ray 1.95 A 1-152 [» ]
4BPM X-ray 2.08 A 10-152 [» ]
ProteinModelPortali O14684.
SMRi O14684. Positions 7-152.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114912. 2 interactions.
STRINGi 9606.ENSP00000342385.

Chemistry

BindingDBi O14684.
ChEMBLi CHEMBL5658.

Proteomic databases

MaxQBi O14684.
PaxDbi O14684.
PeptideAtlasi O14684.
PRIDEi O14684.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000340607 ; ENSP00000342385 ; ENSG00000148344 .
GeneIDi 9536.
KEGGi hsa:9536.
UCSCi uc004byi.3. human.

Organism-specific databases

CTDi 9536.
GeneCardsi GC09M132500.
HGNCi HGNC:9599. PTGES.
HPAi HPA045064.
MIMi 605172. gene.
neXtProti NX_O14684.
PharmGKBi PA33948.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG67817.
HOGENOMi HOG000231759.
HOVERGENi HBG052470.
InParanoidi O14684.
KOi K15729.
OMAi GLQYCRS.
OrthoDBi EOG7288T0.
PhylomeDBi O14684.
TreeFami TF105327.

Enzyme and pathway databases

BioCyci MetaCyc:HS07518-MONOMER.
BRENDAi 5.3.99.3. 2681.
Reactomei REACT_150149. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).

Miscellaneous databases

ChiTaRSi PTGES. human.
EvolutionaryTracei O14684.
GeneWikii PTGES.
GenomeRNAii 9536.
NextBioi 35754.
PROi O14684.
SOURCEi Search...

Gene expression databases

Bgeei O14684.
CleanExi HS_PTGES.
Genevestigatori O14684.

Family and domain databases

Gene3Di 1.20.120.550. 1 hit.
InterProi IPR023352. MAPEG-like_dom.
IPR001129. Membr-assoc_MAPEG.
[Graphical view ]
Pfami PF01124. MAPEG. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1999) [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(2000) [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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary gland.
  5. SeattleSNPs variation discovery resource
    Submitted (APR-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(2004) [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(2004) [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(2002) [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(2003) [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(2013) [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: September 3, 2014
This is version 115 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

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