UniProt Accession

 TEBP_HUMAN; Q15185; A8K7D0; Q8WU70 

Genbank Protein ID

 L24804; AK291945; CH471054; BC003005; BC021167 

Genbank Nucleotide ID

 AAA18537.1; BAF84634.1; EAW96953.1; AAH03005.1; AAH21167.1 

Protein Name

 Prostaglandin E synthase 3 

Protein Synonyms/Alias

 Cytosolic prostaglandin E2 synthase; cPGES; Hsp90 co-chaperone; Progesterone receptor complex p23; Telomerase-binding protein p23 

Gene Name

 PTGES3 

Gene Synonyms/Alias

 P23; TEBP 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
7	*MQPASAKWYDRRDY	acetylation	[1]
7	*MQPASAKWYDRRDY	ubiquitination	[2, 3, 4, 5]
33	DVNVNFEKSKLTFSC	acetylation	[1, 6]
33	DVNVNFEKSKLTFSC	ubiquitination	[7, 8]
35	NVNFEKSKLTFSCLG	ubiquitination	[3, 4, 7]
48	LGGSDNFKHLNEIDL	ubiquitination	[4, 7]
65	CIDPNDSKHKRTDRS	ubiquitination	[4, 7]
67	DPNDSKHKRTDRSIL	ubiquitination	[4]
79	SILCCLRKGESGQSW	ubiquitination	[4, 7, 8]
95	RLTKERAKLNWLSVD	ubiquitination	[2, 3, 4, 5, 7]

Reference

 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] 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]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] 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]
 [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] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [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]
 [8] 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] 

Functional Description

 Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor- mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes. 

Sequence Annotation

 DOMAIN 1 90 CS.
 MOD_RES 33 33 N6-acetyllysine.
 MOD_RES 113 113 Phosphoserine.
 MOD_RES 118 118 Phosphoserine.
 MOD_RES 148 148 Phosphoserine.
 MOD_RES 151 151 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Fatty acid biosynthesis; Fatty acid metabolism; Isomerase; Lipid biosynthesis; Lipid metabolism; Phosphoprotein; Prostaglandin biosynthesis; Prostaglandin metabolism; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 160 AA 

Protein Sequence

Gene Ontology

 GO:0000781; C:chromosome, telomeric region; IC:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005697; C:telomerase holoenzyme complex; IDA:UniProtKB.
 GO:0050220; F:prostaglandin-E synthase activity; IDA:UniProtKB.
 GO:0003720; F:telomerase activity; IDA:UniProtKB.
 GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
 GO:0070389; P:chaperone cofactor-dependent protein refolding; IDA:UniProtKB.
 GO:0019371; P:cyclooxygenase pathway; TAS:Reactome.
 GO:0007165; P:signal transduction; TAS:ProtInc.
 GO:0000723; P:telomere maintenance; TAS:UniProtKB. 

Interpro

 IPR007052; CS-like_domain.
 IPR017447; CS_domain.
 IPR008978; HSP20-like_chaperone. 

Pfam

 PF04969; CS 

SMART

  

PROSITE

 PS51203; CS 

PRINTS