dbPTM

TEBP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TEBP_HUMAN
UniProt AC	Q15185
Protein Name	Prostaglandin E synthase 3
Gene Name	PTGES3
Organism	Homo sapiens (Human).
Sequence Length	160
Subcellular Localization	Cytoplasm .
Protein Description	Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2). [PubMed: 10922363 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]
Protein Sequence	MQPASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFHCIDPNDSKHKRTDRSILCCLRKGESGQSWPRLTKERAKLNWLSVDFNNWKDWEDDSDEDMSNFDRFSEMMNNMGGDEDVDLPEVDGADDDSQDSDDEKMPDLE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MQPASAKW -------CCCCCCCC	10.99	-
7	Acetylation	-MQPASAKWYDRRDY -CCCCCCCCCCCCCE	43.73	23954790
7	Ubiquitination	-MQPASAKWYDRRDY -CCCCCCCCCCCCCE	43.73	21890473
7	Ubiquitination	-MQPASAKWYDRRDY -CCCCCCCCCCCCCE	43.73	21890473
7	Ubiquitination	-MQPASAKWYDRRDY -CCCCCCCCCCCCCE	43.73	21890473
7	Ubiquitination	-MQPASAKWYDRRDY -CCCCCCCCCCCCCE	43.73	21890473
14	Phosphorylation	KWYDRRDYVFIEFCV CCCCCCCEEEEEEEE	8.75	22817900
24	Phosphorylation	IEFCVEDSKDVNVNF EEEEEECCCCCEEEE	19.76	29759185
33	Malonylation	DVNVNFEKSKLTFSC CCEEEEEECCEEEEE	49.07	26320211
33	Ubiquitination	DVNVNFEKSKLTFSC CCEEEEEECCEEEEE	49.07	21890473
33	Sumoylation	DVNVNFEKSKLTFSC CCEEEEEECCEEEEE	49.07	19608861
33	Ubiquitination	DVNVNFEKSKLTFSC CCEEEEEECCEEEEE	49.07	21890473
33	Ubiquitination	DVNVNFEKSKLTFSC CCEEEEEECCEEEEE	49.07	21890473
33	Methylation	DVNVNFEKSKLTFSC CCEEEEEECCEEEEE	49.07	19608861
33	Acetylation	DVNVNFEKSKLTFSC CCEEEEEECCEEEEE	49.07	19608861
33	Sumoylation	DVNVNFEKSKLTFSC CCEEEEEECCEEEEE	49.07	-
33	Ubiquitination	DVNVNFEKSKLTFSC CCEEEEEECCEEEEE	49.07	21906983
34	Phosphorylation	VNVNFEKSKLTFSCL CEEEEEECCEEEEEC	26.21	28450419
35	Sumoylation	NVNFEKSKLTFSCLG EEEEEECCEEEEECC	63.72	-
35	Ubiquitination	NVNFEKSKLTFSCLG EEEEEECCEEEEECC	63.72	21890473
35	Ubiquitination	NVNFEKSKLTFSCLG EEEEEECCEEEEECC	63.72	21890473
35	Sumoylation	NVNFEKSKLTFSCLG EEEEEECCEEEEECC	63.72	28112733
35	Acetylation	NVNFEKSKLTFSCLG EEEEEECCEEEEECC	63.72	23749302
35	Ubiquitination	NVNFEKSKLTFSCLG EEEEEECCEEEEECC	63.72	21890473
35	Ubiquitination	NVNFEKSKLTFSCLG EEEEEECCEEEEECC	63.72	21890473
35	Acetylation	NVNFEKSKLTFSCLG EEEEEECCEEEEECC	63.72	-
37	Phosphorylation	NFEKSKLTFSCLGGS EEEECCEEEEECCCC	19.76	28450419
39	Phosphorylation	EKSKLTFSCLGGSDN EECCEEEEECCCCCC	11.82	29255136
40	S-nitrosocysteine	KSKLTFSCLGGSDNF ECCEEEEECCCCCCC	3.41	-
40	S-nitrosylation	KSKLTFSCLGGSDNF ECCEEEEECCCCCCC	3.41	19483679
40	Glutathionylation	KSKLTFSCLGGSDNF ECCEEEEECCCCCCC	3.41	22555962
44	Phosphorylation	TFSCLGGSDNFKHLN EEEECCCCCCCCCCC	27.81	29255136
48	Acetylation	LGGSDNFKHLNEIDL CCCCCCCCCCCCEEE	54.13	-
48	Ubiquitination	LGGSDNFKHLNEIDL CCCCCCCCCCCCEEE	54.13	21890473
48	Ubiquitination	LGGSDNFKHLNEIDL CCCCCCCCCCCCEEE	54.13	21890473
48	Methylation	LGGSDNFKHLNEIDL CCCCCCCCCCCCEEE	54.13	71275
48	Acetylation	LGGSDNFKHLNEIDL CCCCCCCCCCCCEEE	54.13	23749302
48	Ubiquitination	LGGSDNFKHLNEIDL CCCCCCCCCCCCEEE	54.13	21906983
58	Glutathionylation	NEIDLFHCIDPNDSK CCEEEEEEECCCCCC	2.71	22555962
64	Phosphorylation	HCIDPNDSKHKRTDR EEECCCCCCCCCCCC	43.21	28450419
65	Ubiquitination	CIDPNDSKHKRTDRS EECCCCCCCCCCCCE	56.88	21890473
65	Ubiquitination	CIDPNDSKHKRTDRS EECCCCCCCCCCCCE	56.88	21890473
65	2-Hydroxyisobutyrylation	CIDPNDSKHKRTDRS EECCCCCCCCCCCCE	56.88	-
65	Sumoylation	CIDPNDSKHKRTDRS EECCCCCCCCCCCCE	56.88	-
65	Ubiquitination	CIDPNDSKHKRTDRS EECCCCCCCCCCCCE	56.88	21906983
65	Sumoylation	CIDPNDSKHKRTDRS EECCCCCCCCCCCCE	56.88	28112733
65	Acetylation	CIDPNDSKHKRTDRS EECCCCCCCCCCCCE	56.88	25953088
67	Ubiquitination	DPNDSKHKRTDRSIL CCCCCCCCCCCCEEE	61.81	-
67	Ubiquitination	DPNDSKHKRTDRSIL CCCCCCCCCCCCEEE	61.81	-
69	Phosphorylation	NDSKHKRTDRSILCC CCCCCCCCCCEEEEE	40.34	23312004
72	Phosphorylation	KHKRTDRSILCCLRK CCCCCCCEEEEEEEC	23.79	20873877
75	S-nitrosocysteine	RTDRSILCCLRKGES CCCCEEEEEEECCCC	1.64	-
75	S-palmitoylation	RTDRSILCCLRKGES CCCCEEEEEEECCCC	1.64	29575903
75	S-nitrosylation	RTDRSILCCLRKGES CCCCEEEEEEECCCC	1.64	19483679
76	S-nitrosylation	TDRSILCCLRKGESG CCCEEEEEEECCCCC	3.55	19483679
76	S-palmitoylation	TDRSILCCLRKGESG CCCEEEEEEECCCCC	3.55	29575903
76	S-nitrosocysteine	TDRSILCCLRKGESG CCCEEEEEEECCCCC	3.55	-
79	Ubiquitination	SILCCLRKGESGQSW EEEEEEECCCCCCCC	54.82	21890473
79	Ubiquitination	SILCCLRKGESGQSW EEEEEEECCCCCCCC	54.82	21890473
79	Acetylation	SILCCLRKGESGQSW EEEEEEECCCCCCCC	54.82	26051181
79	Sumoylation	SILCCLRKGESGQSW EEEEEEECCCCCCCC	54.82	-
79	Sumoylation	SILCCLRKGESGQSW EEEEEEECCCCCCCC	54.82	-
79	Ubiquitination	SILCCLRKGESGQSW EEEEEEECCCCCCCC	54.82	21890473
82	Phosphorylation	CCLRKGESGQSWPRL EEEECCCCCCCCCCC	51.29	23927012
85	Phosphorylation	RKGESGQSWPRLTKE ECCCCCCCCCCCCHH	42.44	23401153
90	Phosphorylation	GQSWPRLTKERAKLN CCCCCCCCHHHHHCC	31.94	29514088
91	Ubiquitination	QSWPRLTKERAKLNW CCCCCCCHHHHHCCE	50.20	-
91	Acetylation	QSWPRLTKERAKLNW CCCCCCCHHHHHCCE	50.20	11921337
95	Sumoylation	RLTKERAKLNWLSVD CCCHHHHHCCEEEEC	48.88	-
95	Ubiquitination	RLTKERAKLNWLSVD CCCHHHHHCCEEEEC	48.88	21890473
95	Sumoylation	RLTKERAKLNWLSVD CCCHHHHHCCEEEEC	48.88	-
95	Ubiquitination	RLTKERAKLNWLSVD CCCHHHHHCCEEEEC	48.88	21890473
100	Phosphorylation	RAKLNWLSVDFNNWK HHHCCEEEECCCCCC	15.97	22617229
113 (in isoform 4)	Phosphorylation	-	56.04	25849741
113	Phosphorylation	WKDWEDDSDEDMSNF CCCCCCCCCCCCCHH	56.04	19664994
118 (in isoform 3)	Phosphorylation	-	46.82	22210691
118	Phosphorylation	DDSDEDMSNFDRFSE CCCCCCCCHHHHHHH	46.82	22167270
118 (in isoform 4)	Phosphorylation	-	46.82	25849741
121 (in isoform 3)	Phosphorylation	-	55.77	22210691
124 (in isoform 4)	Phosphorylation	-	26.02	23663014
124	Phosphorylation	MSNFDRFSEMMNNMG CCHHHHHHHHHHHCC	26.02	23927012
127 (in isoform 4)	Phosphorylation	-	2.62	26055452
130 (in isoform 4)	Phosphorylation	-	5.58	25159151
148	Phosphorylation	VDGADDDSQDSDDEK CCCCCCCCCCCCCCC	42.77	23927012
151	Phosphorylation	ADDDSQDSDDEKMPD CCCCCCCCCCCCCCC	39.05	23927012

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
113	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
118	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS

Functions of PTM Sites

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

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MCR_HUMAN	NR3C2	physical	10691735
GCR_HUMAN	NR3C1	physical	10691735
TERT_HUMAN	TERT	physical	10197982
HS90A_HUMAN	HSP90AA1	physical	14761955
CHIP_HUMAN	STUB1	physical	20661446
FKBP5_HUMAN	FKBP5	physical	20661446
FKBP2_HUMAN	FKBP2	physical	20661446
PPP5_HUMAN	PPP5C	physical	20661446
AIP_HUMAN	AIP	physical	20661446
DNJC7_HUMAN	DNAJC7	physical	20661446
WAP53_HUMAN	WRAP53	physical	22939629
URM1_HUMAN	URM1	physical	22939629
KAT2A_HUMAN	KAT2A	physical	23022381
HS90A_HUMAN	HSP90AA1	physical	23022381
SURF1_HUMAN	SURF1	physical	21988832
ANDR_HUMAN	AR	physical	22899854
TEBP_HUMAN	PTGES3	physical	10811660
DNM3A_HUMAN	DNMT3A	physical	8772199
DNM3A_MOUSE	Dnmt3a	physical	8772199
THA_HUMAN	THRA	physical	10691735
HS90A_HUMAN	HSP90AA1	physical	11447118
E2AK2_HUMAN	EIF2AK2	physical	11447118
TEBP_HUMAN	PTGES3	physical	10543959
HS90B_HUMAN	HSP90AB1	physical	10543959
HS90A_HUMAN	HSP90AA1	physical	22806877
HS90B_HUMAN	HSP90AB1	physical	17010336
HS90A_HUMAN	HSP90AA1	physical	18172314
HS90A_HUMAN	HSP90AA1	physical	10642522
CALR_HUMAN	CALR	physical	26344197
CALU_HUMAN	CALU	physical	26344197
NACA2_HUMAN	NACA2	physical	26344197
PACN2_HUMAN	PACSIN2	physical	26344197
RBP2_HUMAN	RANBP2	physical	26344197
STIP1_HUMAN	STIP1	physical	26344197
TKT_HUMAN	TKT	physical	26344197
AIP_HUMAN	AIP	physical	11013261
AHR_HUMAN	AHR	physical	11013261
HS90A_HUMAN	HSP90AA1	physical	19740745
EGLN1_HUMAN	EGLN1	physical	23413029
AHSA1_HUMAN	AHSA1	physical	22504172
HS90A_HUMAN	HSP90AA1	physical	18285346
HS90B_HUMAN	HSP90AB1	physical	18285346
HS90A_HUMAN	HSP90AA1	physical	14987994
HS90A_CHICK	HSP90AA1	physical	12324468
HS90A_HUMAN	HSP90AA1	physical	11413142
FKBP4_HUMAN	FKBP4	physical	11413142
PPID_HUMAN	PPID	physical	11413142
HS90A_HUMAN	HSP90AA1	physical	16403413
HS90A_HUMAN	HSP90AA1	physical	22504172
CDC37_HUMAN	CDC37	physical	22504172
HS90A_HUMAN	HSP90AA1	physical	26151834
EGLN1_HUMAN	EGLN1	physical	24711448

Drug and Disease Associations

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

Regulatory Network of TEBP_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-7 AND LYS-33, ANDMASS SPECTROMETRY.	19608861 [Abstract]
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33, AND MASS SPECTROMETRY.	16916647 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-148 ANDSER-151, AND MASS SPECTROMETRY.	19369195 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-148 ANDSER-151, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASSSPECTROMETRY.	18318008 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-148 ANDSER-151, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-148 ANDSER-151, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASSSPECTROMETRY.	19367720 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-151, ANDMASS SPECTROMETRY.	17287340 [Abstract]
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline."; Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; Electrophoresis 28:2027-2034(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASSSPECTROMETRY.	17487921 [Abstract]
"Phosphoproteomic analysis of the human pituitary."; Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.; Pituitary 9:109-120(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASSSPECTROMETRY.	16807684 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-118; SER-148AND SER-151, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry."; Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.; Nat. Methods 2:591-598(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASSSPECTROMETRY.	16094384 [Abstract]