dbPTM

PGH2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PGH2_MOUSE
UniProt AC	Q05769
Protein Name	Prostaglandin G/H synthase 2
Gene Name	Ptgs2
Organism	Mus musculus (Mouse).
Sequence Length	604
Subcellular Localization	Microsome membrane Peripheral membrane protein. Endoplasmic reticulum membrane Peripheral membrane protein.
Protein Description	Converts arachidonate to prostaglandin H2 (PGH2), a committed step in prostanoid synthesis. Constitutively expressed in some tissues in physiological conditions, such as the endothelium, kidney and brain, and in pathological conditions, such as in cancer. PTGS2 is responsible for production of inflammatory prostaglandins. Up-regulation of PTGS2 is also associated with increased cell adhesion, phenotypic changes, resistance to apoptosis and tumor angiogenesis. In cancer cells, PTGS2 is a key step in the production of prostaglandin E2 (PGE2), which plays important roles in modulating motility, proliferation and resistance to apoptosis..
Protein Sequence	MLFRAVLLCAALGLSQAANPCCSNPCQNRGECMSTGFDQYKCDCTRTGFYGENCTTPEFLTRIKLLLKPTPNTVHYILTHFKGVWNIVNNIPFLRSLIMKYVLTSRSYLIDSPPTYNVHYGYKSWEAFSNLSYYTRALPPVADDCPTPMGVKGNKELPDSKEVLEKVLLRREFIPDPQGSNMMFAFFAQHFTHQFFKTDHKRGPGFTRGLGHGVDLNHIYGETLDRQHKLRLFKDGKLKYQVIGGEVYPPTVKDTQVEMIYPPHIPENLQFAVGQEVFGLVPGLMMYATIWLREHNRVCDILKQEHPEWGDEQLFQTSRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIASEFNTLYHWHPLLPDTFNIEDQEYSFKQFLYNNSILLEHGLTQFVESFTRQIAGRVAGGRNVPIAVQAVAKASIDQSREMKYQSLNEYRKRFSLKPYTSFEELTGEKEMAAELKALYSDIDVMELYPALLVEKPRPDAIFGETMVELGAPFSLKGLMGNPICSPQYWKPSTFGGEVGFKIINTASIQSLICNNVKGCPFTSFNVQDPQPTKTATINASASHSRLDDINPTVLIKRRSTEL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
53	N-linked_Glycosylation	RTGFYGENCTTPEFL CCCCCCCCCCCHHHH	24.87	20463020
130	N-linked_Glycosylation	KSWEAFSNLSYYTRA CCHHHHHCCCHHHCC	26.93	20463020
359	Phosphorylation	LFNQQFQYQNRIASE HHCCHHHHHHHHHHH	14.72	30635358
396	N-linked_Glycosylation	SFKQFLYNNSILLEH CHHHHHHCCHHHHHC	37.61	20463020
437	Phosphorylation	VQAVAKASIDQSREM HHHHHHHCCCCCHHH	26.45	17203969
444	Oxidation	SIDQSREMKYQSLNE CCCCCHHHHHHHHHH	4.81	17203969
446	Phosphorylation	DQSREMKYQSLNEYR CCCHHHHHHHHHHHH	11.30	17203969
448	Phosphorylation	SREMKYQSLNEYRKR CHHHHHHHHHHHHHH	30.03	17203969
457	Phosphorylation	NEYRKRFSLKPYTSF HHHHHHCCCCCCCCH	39.24	22817900
526	S-nitrosylation	GLMGNPICSPQYWKP CCCCCCCCCCCCCCC	5.25	-
565	Acetylation	VKGCPFTSFNVQDPQ CCCCCCCCEECCCCC	18.40	29662056
580	N-linked_Glycosylation	PTKTATINASASHSR CCCEEEEEEECCCCC	24.40	20463020
582	Phosphorylation	KTATINASASHSRLD CEEEEEEECCCCCCC	26.30	30635358
584	Phosphorylation	ATINASASHSRLDDI EEEEEECCCCCCCCC	21.35	30635358
586	Phosphorylation	INASASHSRLDDINP EEEECCCCCCCCCCC	31.85	30635358

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 PGH2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
526	C	S-nitrosylation	-
S-nitrosylation may take place on different Cys residues in addition to Cys-526.
565	S	Acetylation	29662056
Acetylated at Ser-565 by SPHK1.

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 PGH2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NOS2_MOUSE	Nos2	physical	16373578
NUCB1_MOUSE	Nucb1	physical	8643612
PGH2_MOUSE	Ptgs2	physical	21467029
NOS1_MOUSE	Nos1	physical	18650379

Drug and Disease Associations

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

Regulatory Network of PGH2_MOUSE

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"The structural basis of endocannabinoid oxygenation bycyclooxygenase-2."; Vecchio A.J., Malkowski M.G.; J. Biol. Chem. 286:20736-20745(2011). Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 20-599 IN COMPLEX WITH HEME;ACRYLIC ACID AND ARACHIDONIC ACID, FUNCTION, CATALYTIC ACTIVITY, ANDGLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396.	21489986 [Abstract]
"Molecular basis for cyclooxygenase inhibition by the non-steroidalanti-inflammatory drug naproxen."; Duggan K.C., Walters M.J., Musee J., Harp J.M., Kiefer J.R.,Oates J.A., Marnett L.J.; J. Biol. Chem. 285:34950-34959(2010). Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 18-604 IN COMPLEXES WITHHEME AND NAPROXEN ANALOGS, FUNCTION, CATALYTIC ACTIVITY, ENZYMEREGULATION, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-53; ASN-130 ANDASN-396.	20810665 [Abstract]
"Structural basis of fatty acid substrate binding to cyclooxygenase-2."; Vecchio A.J., Simmons D.M., Malkowski M.G.; J. Biol. Chem. 285:22152-22163(2010). Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 20-604 IN COMPLEX WITH HEME;ACRYLIC ACID; ARACHIDONIC ACID AND DOCOSAHEXAENOIC ACID, CATALYTICACTIVITY, ACTIVE SITE, SUBUNIT, COFACTOR, FUNCTION, DISULFIDE BONDS,MUTAGENESIS OF LEU-517 AND ASN-580, AND GLYCOSYLATION AT ASN-53;ASN-130; ASN-396 AND ASN-580.	20463020 [Abstract]
"A novel mechanism of cyclooxygenase-2 inhibition involvinginteractions with Ser-530 and Tyr-385."; Rowlinson S.W., Kiefer J.R., Prusakiewicz J.J., Pawlitz J.L.,Kozak K.R., Kalgutkar A.S., Stallings W.C., Kurumbail R.G.,Marnett L.J.; J. Biol. Chem. 278:45763-45769(2003). Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH HEME ANDDICLOFENAC, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, DISULFIDE BONDS,ENZYME REGULATION, AND GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396.	12925531 [Abstract]
"Structural insights into the stereochemistry of the cyclooxygenasereaction."; Kiefer J.R., Pawlitz J.L., Moreland K.T., Stegeman R.A., Hood W.F.,Gierse J.K., Stevens A.M., Goodwin D.C., Rowlinson S.W., Marnett L.J.,Stallings W.C., Kurumbail R.G.; Nature 405:97-101(2000). Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 18-569 IN COMPLEX WITHARACHIDONIC ACID, AND GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396.	10811226 [Abstract]
"Structural basis for selective inhibition of cyclooxygenase-2 byanti-inflammatory agents."; Kurumbail R.G., Stevens A.M., Gierse J.K., McDonald J.J.,Stegeman R.A., Pay J.Y., Gildehaus D., Miyashiro J.M., Penning T.D.,Seibert K., Isakson P.C., Stallings W.C.; Nature 384:644-648(1996). Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH(S)-FLURBIPROFEN; INDOMETHACIN; HEME AND1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE,COFACTOR, AND GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396.	8967954 [Abstract]
"N-glycosylation of prostaglandin endoperoxide synthases-1 and -2 andtheir orientations in the endoplasmic reticulum."; Otto J.C., Dewitt D.L., Smith W.L.; J. Biol. Chem. 268:18234-18242(1993). Cited for: GLYCOSYLATION AT ASN-53; ASN-130; ASN-396 AND ASN-580, AND ABSENCE OFGLYCOSYLATION AT ASN-592.	8349699 [Abstract]
Phosphorylation
Reference	PubMed
"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-437 AND TYR-446, ANDMASS SPECTROMETRY.	17203969 [Abstract]

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