PLCG1_BOVIN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PLCG1_BOVIN
• UniProt AC: P08487
• Protein Name: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
• Gene Name: PLCG1
• Organism: Bos taurus (Bovine).
• Sequence Length: 1291
• Subcellular Localization: Cell projection, lamellipodium. Cell projection, ruffle. Rapidly redistributed to ruffles and lamellipodia structures in response to epidermal growth factor (EGF) treatment..
• Protein Description: Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand-mediated activation of receptor-type tyrosine kinases, such as PDGFRA, PDGFRB, FGFR1, FGFR2, FGFR3 and FGFR4. Plays a role in actin reorganization and cell migration (By similarity)..
• Protein Sequence: MAGAASPCANGCGPSAPSDAEVVHLCRSLEVGTVMTLFYSKKSQRPERKTFQVKLETRQITWSRGADKIEGAIDIREIKEIRPGKTSRDFDRYQEDPAFRPDQSHCFVILYGMEFRLKTLSLQATSEDEVNMWIRGLTWLMEDTLQAATPLQIERWLRKQFYSVDRNREDRISAKDLKNMLSQVNYRVPNMRFLRERLTDLEQRTSDITYGQFAQLYRSLMYSAQKTMDLPFLEASALRAGERPELCRVSLPEFQQFLLEYQGELWAVDRLQVQEFMLSFLRDPLREIEEPYFFLDEFVTFLFSKENSIWNSQLDEVCPDTMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDGPDGMPVIYHGHTLTTKIKFSDVLHTIKEHAFVASEYPVILSIEDHCSIAQQRNMAQYFKKVLGDTLLTKPVDIAADGLPSPNQLKRKILIKHKKLAEGSAYEEVPTSVMYSENDISNSIKNGILYLEDPVNHEWYPHYFVLTSSKIYYSEETSSDQGNEDEEEPKEASGSTELHSNEKWFHGKLGAGRDGRHIAERLLTEYCIETGAPDGSFLVRESETFVGDYTLSFWRNGKVQHCRIHSRQDAGTPKFFLTDNLVFDSLYDLITHYQQVPLRCNEFEMRLSEPVPQTNAHESKEWYHASLTRAQAEHMLMRVPRDGAFLVRKRNEPNSYAISFRAEGKIKHCRVQQEGQTVMLGNSEFDSLVDLISYYEKHPLYRKMKLRYPINEEALEKIGTAEPDYGALYEGRNPGFYVEANPMPTFKCAVKALFDYKAQREDELTFTKSAIIQNVEKQEGGWWRGDYGGKKQLWFPSNYVEEMVSPAALEPEREHLDENSPLGDLLRGVLDVPACQIAVRPEGKNNRLFVFSISMASVAHWSLDVAADSQEELQDWVKKIREVAQTADARLTEGKMMERRKKIALELSELVVYCRPVPFDEEKIGTERACYRDMSSFPETKAEKYVNKAKGKKFLQYNRLQLSRIYPKGQRLDSSNYDPLPMWICGSQLVALNFQTPDKPMQMNQALFLAGGHCGYVLQPSVMRDEAFDPFDKSSLRGLEPCAICIEVLGARHLPKNGRGIVCPFVEIEVAGAEYDSIKQKTEFVVDNGLNPVWPAKPFHFQISNPEFAFLRFVVYEEDMFSDQNFLAQATFPVKGLKTGYRAVPLKNNYSEGLELASLLVKIDVFPAKQENGDLSPFGGASLRERSCDASGPLFHGRAREGSFEARYQQPFEDFRISQEHLADHFDGRDRRTPRRTRVNGDNRL

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
2	Acetylation	------MAGAASPCA ------CCCCCCCCC	27.86	-
389	Ubiquitination	HTLTTKIKFSDVLHT CEEEEEEEHHHHHHH	40.13	-
472	Phosphorylation	KLAEGSAYEEVPTSV HHCCCCCCCCCCCCE	17.83	1708307
506	Phosphorylation	DPVNHEWYPHYFVLT CCCCCCCCCEEEEEE	4.16	-
509	Phosphorylation	NHEWYPHYFVLTSSK CCCCCCEEEEEECCE	7.29	-
771	Phosphorylation	IGTAEPDYGALYEGR HCCCCCCCCCCCCCC	18.27	1689310
775	Phosphorylation	EPDYGALYEGRNPGF CCCCCCCCCCCCCCC	18.79	-
783	Phosphorylation	EGRNPGFYVEANPMP CCCCCCCEEECCCCC	11.86	1689310
941	Ubiquitination	DARLTEGKMMERRKK HHHCCCCHHHHHHHH	28.92	-
977	Phosphorylation	IGTERACYRDMSSFP HCCCCHHCCCHHHCC	14.52	-
1222	Phosphorylation	KQENGDLSPFGGASL CCCCCCCCCCCCCCH	23.95	-
1228	Phosphorylation	LSPFGGASLRERSCD CCCCCCCCHHHCCCC	31.10	-
1249	Phosphorylation	HGRAREGSFEARYQQ CCCCCCCCCEEECCC	18.37	-
1254	Phosphorylation	EGSFEARYQQPFEDF CCCCEEECCCCHHHC	20.67	1689310
1264	Phosphorylation	PFEDFRISQEHLADH CHHHCCCCHHHHHHH	25.84	-

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
472	Y	Phosphorylation	Kinase	EGFR	P00533	PSP
472	Y	Phosphorylation	Kinase	EGFR	-	PhosphoELM
771	Y	Phosphorylation	Kinase	EGFR	P00533	PSP
771	Y	Phosphorylation	Kinase	SYK	Q32PK0	GPS
771	Y	Phosphorylation	Kinase	SYK	-	Uniprot
771	Y	Phosphorylation	Kinase	EGFR	-	PhosphoELM
783	Y	Phosphorylation	Kinase	EGFR	P00533	PSP
783	Y	Phosphorylation	Kinase	ITK	-	Uniprot
783	Y	Phosphorylation	Kinase	SYK	-	Uniprot
783	Y	Phosphorylation	Kinase	TXK	-	Uniprot
783	Y	Phosphorylation	Kinase	EGFR	-	PhosphoELM
1254	Y	Phosphorylation	Kinase	EGFR	P00533	PSP
1254	Y	Phosphorylation	Kinase	EGFR	-	PhosphoELM

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PLCG1_BOVIN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PLCG1_BOVIN !!

Protein-Protein Interaction

Oops, there are no PPI records of PLCG1_BOVIN !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"PDGF stimulation of inositol phospholipid hydrolysis requires PLC-gamma 1 phosphorylation on tyrosine residues 783 and 1254.";
Kim H.K., Kim J.W., Zilberstein A., Margolis B., Kim J.G.,Schlessinger J., Rhee S.G.;
Cell 65:435-441(1991).
Cited for: PHOSPHORYLATION AT TYR-783 AND TYR-1254.
PubMed: 1708307

"Identification of two epidermal growth factor-sensitive tyrosinephosphorylation sites of phospholipase C-gamma in intact HSC-1cells.";
Whal M.I., Nishibe S., Kim J.W., Kim H.K., Rhee S.G., Carpenter G.;
J. Biol. Chem. 265:3944-3948(1990).
Cited for: PHOSPHORYLATION AT TYR-771; TYR-783 AND TYR-1254.
PubMed: 1689311

"Tyrosine residues in bovine phospholipase C-gamma phosphorylated bythe epidermal growth factor receptor in vitro.";
Kim J.W., Sim S.S., Kim U.H., Nishibe S., Whal M.I., Carpenter G.,Rhee S.G.;
J. Biol. Chem. 265:3940-3943(1990).
Cited for: PHOSPHORYLATION AT TYR-771; TYR-783 AND TYR-1254.
PubMed: 1689310