CPLM-021489

Genbank Nucleotide ID

Prostaglandin E synthase 2

Protein Synonyms/Alias

Microsomal prostaglandin E synthase 2; mPGES-2; Prostaglandin E synthase 2 truncated form

Homo sapiens (Human)

Position	Peptide	Type	References
141	PVRRAEIKFSSYRKV	ubiquitination	[1, 2, 3, 4, 5, 6]
193	ITYYPAMKAVNEQGK	ubiquitination	[2, 4, 7]
216	YWLMLNEKEAQQVYG	ubiquitination	[4, 7]
225	AQQVYGGKEARTEEM	ubiquitination	[3]
269	DYIVREGKFGAVEGA	ubiquitination	[3]

[1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[2] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[7] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]

Functional Description

Isomerase that catalyzes the conversion of unstable intermediate of prostaglandin E2 H2 (PGH2) into the more stable prostaglandin E2 (PGE2) form. May also have transactivation activity toward IFN-gamma (IFNG), possibly via an interaction with CEBPB; however, the relevance of transcription activation activity remains unclear.

DOMAIN 90 193 Glutaredoxin.
DOMAIN 263 377 GST C-terminal.
REGION 164 165 Glutathione binding (By similarity).
BINDING 148 148 Glutathione; via amide nitrogen and

Complete proteome; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism; Golgi apparatus; Isomerase; Lipid biosynthesis; Lipid metabolism; Membrane; Polymorphism; Prostaglandin biosynthesis; Prostaglandin metabolism; Reference proteome; Transmembrane; Transmembrane helix.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; IEA:Compara.
GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
GO:0005739; C:mitochondrion; IDA:LIFEdb.
GO:0005634; C:nucleus; IEA:Compara.
GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO:0003677; F:DNA binding; IEA:Compara.
GO:0009055; F:electron carrier activity; IEA:InterPro.
GO:0050220; F:prostaglandin-E synthase activity; IEA:EC.
GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO:0045893; P:positive regulation of transcription, DNA-dependent; IEA:Compara.
GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-UniPathway.
GO:0046903; P:secretion; IEA:Compara.

IPR002109; Glutaredoxin.
IPR010987; Glutathione-S-Trfase_C-like.
IPR017933; Glutathione_S_Trfase/Cl_chnl_C.
IPR004046; GST_C.
IPR012336; Thioredoxin-like_fold.

PS00195; GLUTAREDOXIN_1
PS51354; GLUTAREDOXIN_2
PS50405; GST_CTER