dbPTM

TEBP_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TEBP_MOUSE
UniProt AC	Q9R0Q7
Protein Name	Prostaglandin E synthase 3
Gene Name	Ptges3
Organism	Mus musculus (Mouse).
Sequence Length	160
Subcellular Localization	Cytoplasm .
Protein Description	Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2). 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. Facilitates HIF alpha proteins hydroxylation via interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway..
Protein Sequence	MQPASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFHCIDPNDSKHKRTDRSILCCLRKGESGQSWPRLTKERAKLNWLSVDFNNWKDWEDDSDEDMSNFDRFSEMMDHMGGDEDVDLPEVDGADDDSQDSDDEKMPDLE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Succinylation	-MQPASAKWYDRRDY -CCCCCCCCCCCCCE	43.73	23806337
7	Acetylation	-MQPASAKWYDRRDY -CCCCCCCCCCCCCE	43.73	23806337
20	Glutathionylation	DYVFIEFCVEDSKDV CEEEEEEEEECCCCC	1.81	24333276
33	Ubiquitination	DVNVNFEKSKLTFSC CCEEEEEECCEEEEE	49.07	-
33	Acetylation	DVNVNFEKSKLTFSC CCEEEEEECCEEEEE	49.07	23806337
33	Malonylation	DVNVNFEKSKLTFSC CCEEEEEECCEEEEE	49.07	26320211
35	Ubiquitination	NVNFEKSKLTFSCLG EEEEEECCEEEEECC	63.72	-
35	Acetylation	NVNFEKSKLTFSCLG EEEEEECCEEEEECC	63.72	22826441
37	Phosphorylation	NFEKSKLTFSCLGGS EEEECCEEEEECCCC	19.76	29899451
39	Phosphorylation	EKSKLTFSCLGGSDN EECCEEEEECCCCCC	11.82	28066266
40	S-palmitoylation	KSKLTFSCLGGSDNF ECCEEEEECCCCCCC	3.41	28526873
40	S-nitrosylation	KSKLTFSCLGGSDNF ECCEEEEECCCCCCC	3.41	20925432
40	Glutathionylation	KSKLTFSCLGGSDNF ECCEEEEECCCCCCC	3.41	24333276
40	S-nitrosocysteine	KSKLTFSCLGGSDNF ECCEEEEECCCCCCC	3.41	-
44	Phosphorylation	TFSCLGGSDNFKHLN EEEECCCCCCCCCCC	27.81	26824392
48	Acetylation	LGGSDNFKHLNEIDL CCCCCCCCCCCCEEE	54.13	71277
48	Ubiquitination	LGGSDNFKHLNEIDL CCCCCCCCCCCCEEE	54.13	-
58	S-nitrosocysteine	NEIDLFHCIDPNDSK CCEEEEEEECCCCCC	2.71	-
58	S-palmitoylation	NEIDLFHCIDPNDSK CCEEEEEEECCCCCC	2.71	28526873
58	S-nitrosylation	NEIDLFHCIDPNDSK CCEEEEEEECCCCCC	2.71	20925432
58	Glutathionylation	NEIDLFHCIDPNDSK CCEEEEEEECCCCCC	2.71	24333276
75	Glutathionylation	RTDRSILCCLRKGES CCCCEEEEEEECCCC	1.64	24333276
76	Glutathionylation	TDRSILCCLRKGESG CCCEEEEEEECCCCC	3.55	24333276
82	Phosphorylation	CCLRKGESGQSWPRL EEEECCCCCCCCCCC	51.29	25266776
85	Phosphorylation	RKGESGQSWPRLTKE ECCCCCCCCCCCCHH	42.44	23684622
95	Ubiquitination	RLTKERAKLNWLSVD CCCHHHHHCCEEEEC	48.88	-
95	Acetylation	RLTKERAKLNWLSVD CCCHHHHHCCEEEEC	48.88	22826441
100	Phosphorylation	RAKLNWLSVDFNNWK HHHCCEEEECCCCCC	15.97	21082442
113	Phosphorylation	WKDWEDDSDEDMSNF CCCCCCCCCHHCCCH	56.04	24925903
118	Phosphorylation	DDSDEDMSNFDRFSE CCCCHHCCCHHHHHH	46.82	25521595
124	Phosphorylation	MSNFDRFSEMMDHMG CCCHHHHHHHHHHCC	26.02	24925903
148	Phosphorylation	VDGADDDSQDSDDEK CCCCCCCCCCCCCCC	42.77	24925903
151	Phosphorylation	ADDDSQDSDDEKMPD CCCCCCCCCCCCCCC	39.05	25521595

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of TEBP_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TEBP_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of TEBP_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HS90B_MOUSE	Hsp90ab1	physical	22123826
DNM3A_MOUSE	Dnmt3a	physical	8772199
KAT2A_MOUSE	Kat2a	physical	23022381

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TEBP_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASSSPECTROMETRY.	19144319 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-148 ANDSER-151, AND MASS SPECTROMETRY.	19367708 [Abstract]
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis."; Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; J. Proteome Res. 7:3957-3967(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASSSPECTROMETRY.	18630941 [Abstract]
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASSSPECTROMETRY.	17114649 [Abstract]
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASSSPECTROMETRY.	17203969 [Abstract]
"Phosphoproteome analysis of mouse liver using immobilized metalaffinity purification and linear ion trap mass spectrometry."; Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.; Rapid Commun. Mass Spectrom. 18:2169-2176(2004). Cited for: PHOSPHORYLATION AT SER-113.	15378723 [Abstract]
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASSSPECTROMETRY.	15345747 [Abstract]