PGES2_HUMAN - dbPTM
PGES2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PGES2_HUMAN
UniProt AC Q9H7Z7
Protein Name Prostaglandin E synthase 2
Gene Name PTGES2
Organism Homo sapiens (Human).
Sequence Length 377
Subcellular Localization Golgi apparatus membrane
Single-pass membrane protein .
Prostaglandin E synthase 2 truncated form: Cytoplasm, perinuclear region . Synthesized as a Golgi membrane-bound protein, which is further cleaved into the predominant soluble truncated form.
Protein Description Isomerase that catalyzes the conversion of PGH2 into the more stable prostaglandin E2 (PGE2)..
Protein Sequence MDPAARVVRALWPGGCALAWRLGGRPQPLLPTQSRAGFAGAAGGPSPVAAARKGSPRLLGAAALALGGALGLYHTARWHLRAQDLHAERSAAQLSLSSRLQLTLYQYKTCPFCSKVRAFLDFHALPYQVVEVNPVRRAEIKFSSYRKVPILVAQEGESSQQLNDSSVIISALKTYLVSGQPLEEIITYYPAMKAVNEQGKEVTEFGNKYWLMLNEKEAQQVYGGKEARTEEMKWRQWADDWLVHLISPNVYRTPTEALASFDYIVREGKFGAVEGAVAKYMGAAAMYLISKRLKSRHRLQDNVREDLYEAADKWVAAVGKDRPFMGGQKPNLADLAVYGVLRVMEGLDAFDDLMQHTHIQPWYLRVERAITEASPAH
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
46PhosphorylationAGAAGGPSPVAAARK
CCCCCCCCHHHHHHC		34.9723312004
53AcetylationSPVAAARKGSPRLLG
CHHHHHHCCCHHHHH		60.0411790047
75PhosphorylationGALGLYHTARWHLRA
HHHHHHHHHHHHHHH		12.3622210691
90PhosphorylationQDLHAERSAAQLSLS
HHHHHHHHHHHHCHH		21.3322167270
95PhosphorylationERSAAQLSLSSRLQL
HHHHHHHCHHHCCEE		17.7122167270
97PhosphorylationSAAQLSLSSRLQLTL
HHHHHCHHHCCEEEE		15.2722167270
98PhosphorylationAAQLSLSSRLQLTLY
HHHHCHHHCCEEEEE		42.1622167270
103PhosphorylationLSSRLQLTLYQYKTC
HHHCCEEEEEECCCC		15.5128152594
105PhosphorylationSRLQLTLYQYKTCPF
HCCEEEEEECCCCCC		12.4528152594
107PhosphorylationLQLTLYQYKTCPFCS
CEEEEEECCCCCCHH		8.4928152594
109PhosphorylationLTLYQYKTCPFCSKV
EEEEECCCCCCHHHC		22.07-
115UbiquitinationKTCPFCSKVRAFLDF
CCCCCHHHCHHHHCC		36.60-
127PhosphorylationLDFHALPYQVVEVNP
HCCCCCCEEEEEECC		18.13-
141UbiquitinationPVRRAEIKFSSYRKV
CCCCEEEECCCCCCC		30.6021890473
141AcetylationPVRRAEIKFSSYRKV
CCCCEEEECCCCCCC		30.6027452117
147UbiquitinationIKFSSYRKVPILVAQ
EECCCCCCCCEEEEE		44.10-
188PhosphorylationPLEEIITYYPAMKAV
CHHHHHHHHHHHHHH		9.31-
192SulfoxidationIITYYPAMKAVNEQG
HHHHHHHHHHHHHHC		2.1831801345
193UbiquitinationITYYPAMKAVNEQGK
HHHHHHHHHHHHHCC		51.8221890473
200UbiquitinationKAVNEQGKEVTEFGN
HHHHHHCCEEHHHCC		49.02-
203PhosphorylationNEQGKEVTEFGNKYW
HHHCCEEHHHCCEEE		27.0424719451
208UbiquitinationEVTEFGNKYWLMLNE
EEHHHCCEEEEEECH		37.88-
208AcetylationEVTEFGNKYWLMLNE
EEHHHCCEEEEEECH		37.8826051181
209PhosphorylationVTEFGNKYWLMLNEK
EHHHCCEEEEEECHH		14.0522817900
216UbiquitinationYWLMLNEKEAQQVYG
EEEEECHHHHHHHHC		58.2221890473
222PhosphorylationEKEAQQVYGGKEART
HHHHHHHHCCCCCCC		18.8022817900
225UbiquitinationAQQVYGGKEARTEEM
HHHHHCCCCCCCHHH		43.78-
2252-HydroxyisobutyrylationAQQVYGGKEARTEEM
HHHHHCCCCCCCHHH		43.78-
233UbiquitinationEARTEEMKWRQWADD
CCCCHHHHHHHHHHH		42.37-
253PhosphorylationISPNVYRTPTEALAS
HCCCCCCCCHHHHHC		19.5120068231
255PhosphorylationPNVYRTPTEALASFD
CCCCCCCHHHHHCCC		33.0220068231
260PhosphorylationTPTEALASFDYIVRE
CCHHHHHCCCEEEEC		21.35-
263PhosphorylationEALASFDYIVREGKF
HHHHCCCEEEECCCC		10.17-
269UbiquitinationDYIVREGKFGAVEGA
CEEEECCCCCCHHHH		35.55-
2692-HydroxyisobutyrylationDYIVREGKFGAVEGA
CEEEECCCCCCHHHH		35.55-
269AcetylationDYIVREGKFGAVEGA
CEEEECCCCCCHHHH		35.5527452117
280PhosphorylationVEGAVAKYMGAAAMY
HHHHHHHHHHHHHHH		7.34-
287PhosphorylationYMGAAAMYLISKRLK
HHHHHHHHHHHHHHH		8.9929449344
290PhosphorylationAAAMYLISKRLKSRH
HHHHHHHHHHHHHCH		14.7722817900
308PhosphorylationDNVREDLYEAADKWV
HHHHHHHHHHHHHHH		18.82-
313UbiquitinationDLYEAADKWVAAVGK
HHHHHHHHHHHHHCC		38.55-
371PhosphorylationLRVERAITEASPAH-
HHHHHHHHHCCCCC-		25.2320068231
374PhosphorylationERAITEASPAH----
HHHHHHCCCCC----		19.1824719451
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 PGES2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PGES2_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 PGES2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
QCR10_HUMANUQCR11physical
22939629
PGES2_HUMANPTGES2physical
17585783
CA189_HUMANC1orf189physical
25416956
Drug and Disease Associations
Kegg Disease
H00025 Penile cancer
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 PGES2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-290, AND MASSSPECTROMETRY.

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