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Q9H7Z7 (PGES2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prostaglandin E synthase 2

EC=4.1.2.-
EC=5.3.99.3
Alternative name(s):
Microsomal prostaglandin E synthase 2
Short name=mPGES-2

Cleaved into the following chain:

  1. Prostaglandin E synthase 2 truncated form
Gene names
Name:PTGES2
Synonyms:C9orf15, PGES2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Dual function enzyme which exhibits both isomerase and lyase activities. Its catalytic activity is altered by the presence or absence of the cofactors glutathione (GSH) and heme. The GSH-heme complex-bound enzyme (mPGES-2h) acts as a lyase and catalyzes the degradation of prostaglandin E2 H2 (PGH2) to 12(S)-hydroxy-5(Z),8(E),10(E)-heptadecatrienoic acid (HHT) and malondialdehyde (MDA) while the GSH-heme complex-free enzyme (mPGES-2) acts as an isomerase and catalyzes the isomerization of PGH2 into the more stable prostaglandin E2 (PGE2) form By similarity.

Catalytic activity

(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.

(5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = malonaldehyde + (5Z,8E,10E)-(12S)-hydroxyheptadeca-5,8,10-trienoate.

Cofactor

Dihydrolipoic acid; required for isomerase activity. Ref.6

Glutathione (GSH). Required for lyase activity By similarity. Ref.6

Heme. Required for lyase activity By similarity. Ref.6

Pathway

Lipid metabolism; prostaglandin biosynthesis.

Subunit structure

Homodimer. May interact with CEBPB By similarity. Interacts with EXOSC10. Ref.8

Subcellular location

Golgi apparatus membrane; Single-pass membrane protein Ref.7.

Prostaglandin E synthase 2 truncated form: Cytoplasmperinuclear region. 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. Ref.7

Tissue specificity

Widely expressed. Expressed in the heart, including apex, inter-ventricular septum, both atria and ventricles, but not in the aorta. Also expressed in fetal heart. Detected in various regions of the brain: cerebellum; occipital, frontal and parietal lobes. Also expressed in the lymph nodes, skeletal muscle, kidney and trachea, but not in the thymus or lung. Overexpressed in colorectal cancer. Ref.5

Sequence similarities

Belongs to the GST superfamily.

Contains 1 glutaredoxin domain.

Contains 1 GST C-terminal domain.

Sequence caution

The sequence CAI13822.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
Prostaglandin biosynthesis
Prostaglandin metabolism
   Cellular componentCytoplasm
Golgi apparatus
Membrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   Molecular functionIsomerase
Lyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

prostaglandin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

secretion

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrion

Inferred from direct assay. Source: LIFEdb

nucleus

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: Ensembl

electron carrier activity

Inferred from electronic annotation. Source: InterPro

glutathione binding

Inferred from sequence or structural similarity. Source: UniProtKB

heme binding

Inferred from sequence or structural similarity. Source: UniProtKB

lyase activity

Inferred from sequence or structural similarity. Source: UniProtKB

prostaglandin-E synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein disulfide oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 377377Prostaglandin E synthase 2
PRO_0000013127
Chain88 – 377290Prostaglandin E synthase 2 truncated form By similarity
PRO_0000013128

Regions

Topological domain1 – 5757Lumenal Potential
Transmembrane58 – 7417Helical; Potential
Topological domain75 – 377303Cytoplasmic Potential
Domain90 – 193104Glutaredoxin
Domain263 – 377115GST C-terminal
Region164 – 1652Glutathione binding By similarity

Sites

Binding site1481Glutathione; via amide nitrogen and carbonyl oxygen By similarity
Site87 – 882Cleavage By similarity

Natural variations

Natural variant2981R → H.
Corresponds to variant rs13283456 [ dbSNP | Ensembl ].
VAR_049494

Experimental info

Mutagenesis1101C → S: Loss of function. Ref.6
Mutagenesis1131C → S: Does not strongly affect enzyme activity. Ref.6
Sequence conflict3191G → S in BAD97240. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9H7Z7 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 82F2DF867BB8337C

FASTA37741,943
        10         20         30         40         50         60 
MDPAARVVRA LWPGGCALAW RLGGRPQPLL PTQSRAGFAG AAGGPSPVAA ARKGSPRLLG 

        70         80         90        100        110        120 
AAALALGGAL GLYHTARWHL RAQDLHAERS AAQLSLSSRL QLTLYQYKTC PFCSKVRAFL 

       130        140        150        160        170        180 
DFHALPYQVV EVNPVRRAEI KFSSYRKVPI LVAQEGESSQ QLNDSSVIIS ALKTYLVSGQ 

       190        200        210        220        230        240 
PLEEIITYYP AMKAVNEQGK EVTEFGNKYW LMLNEKEAQQ VYGGKEARTE EMKWRQWADD 

       250        260        270        280        290        300 
WLVHLISPNV YRTPTEALAS FDYIVREGKF GAVEGAVAKY MGAAAMYLIS KRLKSRHRLQ 

       310        320        330        340        350        360 
DNVREDLYEA ADKWVAAVGK DRPFMGGQKP NLADLAVYGV LRVMEGLDAF DDLMQHTHIQ 

       370 
PWYLRVERAI TEASPAH 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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: Embryo.
[2]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"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. expand/collapse author list , 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].
[4]"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: Brain and Lung.
[5]"Identification and characterization of a novel type of membrane-associated prostaglandin E synthase."
Tanikawa N., Ohmiya Y., Ohkubo H., Hashimoto K., Kangawa K., Kojima M., Ito S., Watanabe K.
Biochem. Biophys. Res. Commun. 291:884-889(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"Essential 110Cys in active site of membrane-associated prostaglandin E synthase-2."
Watanabe K., Ohkubo H., Niwa H., Tanikawa N., Koda N., Ito S., Ohmiya Y.
Biochem. Biophys. Res. Commun. 306:577-581(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR, MUTAGENESIS OF CYS-110 AND CYS-113.
[7]"Cellular prostaglandin E2 production by membrane-bound prostaglandin E synthase-2 via both cyclooxygenases-1 and -2."
Murakami M., Nakashima K., Kamei D., Masuda S., Ishikawa Y., Ishii T., Ohmiya Y., Watanabe K., Kudo I.
J. Biol. Chem. 278:37937-37947(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE, SUBCELLULAR LOCATION.
[8]"A protein interaction framework for human mRNA degradation."
Lehner B., Sanderson C.M.
Genome Res. 14:1315-1323(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EXOSC10.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK024100 mRNA. Translation: BAB14826.1.
AK223520 mRNA. Translation: BAD97240.1.
AL590708 Genomic DNA. Translation: CAI13821.1.
AL590708 Genomic DNA. Translation: CAI13822.1. Sequence problems.
BC009397 mRNA. Translation: AAH09397.2.
BC009456 mRNA. Translation: AAH09456.1.
BC011613 mRNA. Translation: AAH11613.1.
RefSeqNP_001243264.1. NM_001256335.1.
NP_079348.1. NM_025072.6.
NP_945176.1. NM_198938.2.
UniGeneHs.495219.

3D structure databases

ProteinModelPortalQ9H7Z7.
SMRQ9H7Z7. Positions 100-373.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123135. 7 interactions.
IntActQ9H7Z7. 6 interactions.
STRING9606.ENSP00000345341.

Chemistry

BindingDBQ9H7Z7.
ChEMBLCHEMBL4411.

PTM databases

PhosphoSiteQ9H7Z7.

Polymorphism databases

DMDM73921741.

Proteomic databases

PaxDbQ9H7Z7.
PRIDEQ9H7Z7.

Protocols and materials databases

DNASU80142.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338961; ENSP00000345341; ENSG00000148334.
GeneID80142.
KEGGhsa:80142.
UCSCuc004bti.4. human.

Organism-specific databases

CTD80142.
GeneCardsGC09M130882.
HGNCHGNC:17822. PTGES2.
HPAHPA020631.
MIM608152. gene.
neXtProtNX_Q9H7Z7.
PharmGKBPA33949.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG316980.
HOGENOMHOG000231901.
HOVERGENHBG069136.
InParanoidQ9H7Z7.
KOK05309.
OMAAMYFISK.
OrthoDBEOG7060R5.
PhylomeDBQ9H7Z7.
TreeFamTF314304.

Enzyme and pathway databases

BioCycMetaCyc:HS07514-MONOMER.
BRENDA5.3.99.3. 2681.
UniPathwayUPA00662.

Gene expression databases

ArrayExpressQ9H7Z7.
BgeeQ9H7Z7.
CleanExHS_PTGES2.
GenevestigatorQ9H7Z7.

Family and domain databases

Gene3D1.20.1050.10. 2 hits.
3.40.30.10. 1 hit.
InterProIPR002109. Glutaredoxin.
IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
PS50405. GST_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTGES2. human.
GeneWikiPTGES2.
GenomeRNAi80142.
NextBio70401.
PROQ9H7Z7.
SOURCESearch...

Entry information

Entry namePGES2_HUMAN
AccessionPrimary (citable) accession number: Q9H7Z7
Secondary accession number(s): Q53EW9 expand/collapse secondary AC list , Q5SYV6, Q96GI0, Q96GL2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM