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O14684

- PTGES_HUMAN

UniProt

O14684 - PTGES_HUMAN

Protein

Prostaglandin E synthase

Gene

PTGES

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    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 1 Publication; Multi-pass membrane protein 1 Publication

    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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO14684.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1212LumenalAdd
    BLAST
    Topological domaini42 – 6019CytoplasmicAdd
    BLAST
    Topological domaini91 – 955Lumenal
    Topological domaini120 – 1234Cytoplasmic

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei13 – 4129HelicalAdd
    BLAST
    Transmembranei61 – 9030HelicalAdd
    BLAST
    Transmembranei96 – 11924HelicalAdd
    BLAST
    Transmembranei124 – 15229HelicalAdd
    BLAST

    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.
    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

    Experimental Info

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

    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

    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: October 1, 2014
    This is version 116 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