CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016628
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Prostaglandin E synthase 2 
Protein Synonyms/Alias
 GATE-binding factor 1; GBF-1; Microsomal prostaglandin E synthase 2; mPGES-2; Prostaglandin E synthase 2 truncated form 
Gene Name
 Ptges2 
Gene Synonyms/Alias
 Gbf1; Pges2 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
140PVRRTEIKFSSYRKVubiquitination[1]
232EARTEEMKWRQWADDacetylation[2]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123
Functional Description
 Isomerase that catalyzes the conversion of unstable intermediate of prostaglandin E2 H2 (PGH2) into the more stable prostaglandin E2 (PGE2) form (By similarity). May also have transactivation activity toward IFN-gamma (IFNG), possibly via an interaction with CEBPB; however, the relevance of transcription activation activity remains unclear. 
Sequence Annotation
 DOMAIN 89 192 Glutaredoxin.
 DOMAIN 262 376 GST C-terminal.
 REGION 163 164 Glutathione binding (By similarity).
 BINDING 147 147 Glutathione; via amide nitrogen and  
Keyword
 Complete proteome; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism; Golgi apparatus; Isomerase; Lipid biosynthesis; Lipid metabolism; Membrane; Nucleus; Prostaglandin biosynthesis; Prostaglandin metabolism; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 384 AA 
Protein Sequence
MAQAARLSWV LVSSRCALTE GLLTRPWQPL SAQSRAGFTR VAAGSRGAAV RKGSPRLLGA 60
AALALGGALG LYHTVRWHQR SQDLRAERSA AQLPLSNSLQ LTLYQYKTCP FCSKVRAFLD 120
FHSLPYQVVE VNPVRRTEIK FSSYRKVPIL VAQEGDSLQQ LNDSSVIISA LKTYLVSGQP 180
LEEVITYYPP MKAMNDQGKE VTEFCNKYWL MLDEKEAQQM YGGKEARTEE MKWRQWADDW 240
LVHLISPNVY RTPAEALASF DYIVREGKFG AVEAAMAKYV GAAAMYLISK RLKSRHHLQD 300
DVRVDLYEAA NKWVTAVGKD RPFMGGQKPN LADLAVYGVL RVMEGLEAFD DLMRHSHIQP 360
WYLRMERAIE EAPSVHHVNP SCKD 384 
Gene Ontology
 GO:0005829; C:cytosol; IDA:MGI.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005634; C:nucleus; IDA:MGI.
 GO:0003677; F:DNA binding; IDA:MGI.
 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; IDA:MGI.
 GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0046903; P:secretion; IDA:MGI. 
Interpro
 IPR002109; Glutaredoxin.
 IPR010987; Glutathione-S-Trfase_C-like.
 IPR012336; Thioredoxin-like_fold. 
Pfam
  
SMART
  
PROSITE
 PS00195; GLUTAREDOXIN_1
 PS51354; GLUTAREDOXIN_2
 PS50405; GST_CTER 
PRINTS