PLCG1_MOUSE - dbPTM
PLCG1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLCG1_MOUSE
UniProt AC Q62077
Protein Name 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
Gene Name Plcg1
Organism Mus musculus (Mouse).
Sequence Length 1302
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..
Protein Sequence MAGVATPCANGCGPGAPSEAEVLHLCRSLEVGTVMTLFYSKKSQRPERKTFQVKLETRQITWSRGADKIEGSIDIREIKEIRPGKTSRDFDRYQEDPAFRPDQSHCFVILYGMEFRLKTLSLQATSEDEVNMWIKGLTWLMEDTLQAATPLQIERWLRKQFYSVDRNREDRISAKDLKNMLSQVNYRVPNMRFLRERLTDLEQRSGDITYGQFAQLYRSLMYSAQKTMDLPFLETNALRTGERPEHCQVSLSEFQQFLLEYQGELWAVDRLQVQEFMLSFLRDPLREIEEPYFFLDELVTFLFSKENSVWNSQLDAVCPDTMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDGPDGMPVIYHGHTLTTKIKFSDVLHTIKEHAFVASEYPVILSIEDHCSIAQQRNMAQHFRKVLGDTLLTKPVDIAADGLPSPNQLRRKILIKHKKLAEGSAYEEVPTSVMYSENDISNSIKNGILYLEDPVNHEWYPHYFVLTSSKIYYSEETSSDQGNEDEEEPKEASSSTELHSSEKWFHGKLGAGRDGRHIAERLLTEYCIETGAPDGSFLVRESETFVGDYTLSFWRNGKVQHCRIHSRQDAGTPKFFLTDNLVFDSLYDLITHYQQVPLRCNEFEMRLSEPVPQTNAHESKEWYHASLTRAQAEHMLMRVPRDGAFLVRKRNEPNSYAISFRAEGKIKHCRVQQEGQTVMLGNSEFDSLVDLISYYEKHPLYRKMKLRYPINEEALEKIGTAEPDYGALYEGRNPGFYVEANPMPTFKCAVKALFDYKAQREDELTFTKSAIIQNVEKQDGGWWRGDYGGKKQLWFPSNYVEEMINPAVLEPEREHLDENSPLGDLLRGVLDVPACQIAIRPEGKNNRLFVFSISMPSVAQWSLDVAADSQEELQDWVKKIREVAQTADARLTEGKMMERRKKIALELSELVVYCRPVPFDEEKIGTERACYRDMSSFPETKAEKYVNKAKGKKFLQYNRLQLSRIYPKGQRLDSSNYDPLPMWICGSQLVALNFQTPDKPMQMNQALFMAGGHCGYVLQPSTMRDEAFDPFDKSSLRGLEPCVICIEVLGARHLPKNGRGIVCPFVEIEVAGAEYDSTKQKTEFVVDNGLNPVWPAKPFHFQISNPEFAFLRFVVYEEDMFSDQNFLAQATFPVKGLKTGYRAVPLKNNYSEDLELASLLIKIDIFPAKENGDLSPFSGISLRERASDASSQLFHVRAREGSFEARYQQPFEDFRISQEHLADHFDSRERSTSDGPSSATNLIEDPLHDKLWKCSL
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
2Acetylation------MAGVATPCA
------CCCCCCCCC		32.26-
6Phosphorylation--MAGVATPCANGCG
--CCCCCCCCCCCCC		19.2529514104
178UbiquitinationRISAKDLKNMLSQVN
CCCHHHHHHHHHHCC		50.90-
186PhosphorylationNMLSQVNYRVPNMRF
HHHHHCCCCCCCHHH		17.7128066266
210PhosphorylationQRSGDITYGQFAQLY
HHHCCCCHHHHHHHH		14.84-
217PhosphorylationYGQFAQLYRSLMYSA
HHHHHHHHHHHHHHH		6.00-
222PhosphorylationQLYRSLMYSAQKTMD
HHHHHHHHHHHHHCC		13.22-
223PhosphorylationLYRSLMYSAQKTMDL
HHHHHHHHHHHHCCC		15.40-
226UbiquitinationSLMYSAQKTMDLPFL
HHHHHHHHHCCCCCH		45.60-
227PhosphorylationLMYSAQKTMDLPFLE
HHHHHHHHCCCCCHH		12.1129550500
235PhosphorylationMDLPFLETNALRTGE
CCCCCHHCCCCCCCC		28.1229550500
379PhosphorylationPDGMPVIYHGHTLTT
CCCCEEEEECCEEEE		11.2822817900
383PhosphorylationPVIYHGHTLTTKIKF
EEEEECCEEEEEEEH		30.3222817900
385PhosphorylationIYHGHTLTTKIKFSD
EEECCEEEEEEEHHH		27.4822817900
386PhosphorylationYHGHTLTTKIKFSDV
EECCEEEEEEEHHHH		33.6122817900
389AcetylationHTLTTKIKFSDVLHT
CEEEEEEEHHHHHHH		40.1322826441
431UbiquitinationNMAQHFRKVLGDTLL
HHHHHHHHHHCCHHC		40.65-
440UbiquitinationLGDTLLTKPVDIAAD
HCCHHCCCCCCCCCC		42.91-
470PhosphorylationHKKLAEGSAYEEVPT
HHHHCCCCCCCCCCC		21.1225338131
472PhosphorylationKLAEGSAYEEVPTSV
HHCCCCCCCCCCCCE		17.8329514104
481PhosphorylationEVPTSVMYSENDISN
CCCCCEECCCCCCCH		15.6322817900
496PhosphorylationSIKNGILYLEDPVNH
HHHCCEEEEECCCCC		13.21-
506PhosphorylationDPVNHEWYPHYFVLT
CCCCCCCCCEEEEEE		4.1622817900
509PhosphorylationNHEWYPHYFVLTSSK
CCCCCCEEEEEECCE		7.29-
518PhosphorylationVLTSSKIYYSEETSS
EEECCEEEEECCCCC		12.5025195567
519PhosphorylationLTSSKIYYSEETSSD
EECCEEEEECCCCCC		17.0623737553
520PhosphorylationTSSKIYYSEETSSDQ
ECCEEEEECCCCCCC		16.4021149613
523PhosphorylationKIYYSEETSSDQGNE
EEEEECCCCCCCCCC		29.4921149613
524PhosphorylationIYYSEETSSDQGNED
EEEECCCCCCCCCCC		34.8925521595
525PhosphorylationYYSEETSSDQGNEDE
EEECCCCCCCCCCCC		41.1825521595
542PhosphorylationPKEASSSTELHSSEK
CCCCCCCCCCCCCCC		44.5129899451
582PhosphorylationETGAPDGSFLVRESE
HHCCCCCCEEEEECC		23.8429176673
618PhosphorylationHSRQDAGTPKFFLTD
ECCCCCCCCCEEECC		25.6525367039
624PhosphorylationGTPKFFLTDNLVFDS
CCCCEEECCCHHHHH		20.0625367039
631PhosphorylationTDNLVFDSLYDLITH
CCCHHHHHHHHHHHH		19.8425367039
633PhosphorylationNLVFDSLYDLITHYQ
CHHHHHHHHHHHHHH		16.8025367039
637PhosphorylationDSLYDLITHYQQVPL
HHHHHHHHHHHHCCC		23.1025367039
639PhosphorylationLYDLITHYQQVPLRC
HHHHHHHHHHCCCCC		7.6225367039
766PhosphorylationEALEKIGTAEPDYGA
HHHHHHCCCCCCCCC		31.1829514104
771PhosphorylationIGTAEPDYGALYEGR
HCCCCCCCCCCCCCC		18.2716512673
775PhosphorylationEPDYGALYEGRNPGF
CCCCCCCCCCCCCCC		18.7922817900
783PhosphorylationEGRNPGFYVEANPMP
CCCCCCCEEECCCCC		11.8619217431
815PhosphorylationDELTFTKSAIIQNVE
CCCEEEHHHEEECEE		22.9525338131
823AcetylationAIIQNVEKQDGGWWR
HEEECEEECCCCEEC		49.7822826441
833PhosphorylationGGWWRGDYGGKKQLW
CCEECCCCCCCEEEE		30.5129514104
941UbiquitinationDARLTEGKMMERRKK
HHHCCCCHHHHHHHH		28.92-
977PhosphorylationIGTERACYRDMSSFP
HCCCCHHCCCHHHCC		14.5222499769
1003PhosphorylationKGKKFLQYNRLQLSR
HCCHHHHHCCEEHHC		12.3729514104
1215UbiquitinationKIDIFPAKENGDLSP
HEEEEECCCCCCCCC		52.53-
1221PhosphorylationAKENGDLSPFSGISL
CCCCCCCCCCCCCCH		28.7426824392
1224PhosphorylationNGDLSPFSGISLRER
CCCCCCCCCCCHHHH		38.3026745281
1227PhosphorylationLSPFSGISLRERASD
CCCCCCCCHHHHHCC		25.5422817900
1233PhosphorylationISLRERASDASSQLF
CCHHHHHCCCCCCCE		39.6725521595
1236PhosphorylationRERASDASSQLFHVR
HHHHCCCCCCCEEEE		24.4928833060
1237PhosphorylationERASDASSQLFHVRA
HHHCCCCCCCEEEEE		32.4028833060
1248PhosphorylationHVRAREGSFEARYQQ
EEEECCCCCEEECCC		18.3726824392
1253PhosphorylationEGSFEARYQQPFEDF
CCCCEEECCCCHHHC		20.6715657076
1263PhosphorylationPFEDFRISQEHLADH
CHHHCCCCHHHHHHH		25.8426824392
1273PhosphorylationHLADHFDSRERSTSD
HHHHHCCCCCCCCCC		34.7925777480
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
771YPhosphorylationKinaseFGFR2P21803
PSP
771YPhosphorylationKinaseSYKP48025
Uniprot
783YPhosphorylationKinaseITKQ08881
PSP
783YPhosphorylationKinaseITKQ03526
Uniprot
783YPhosphorylationKinaseSYKP48025
Uniprot
783YPhosphorylationKinaseSRCP05480
PSP
783YPhosphorylationKinaseTXKP42682
Uniprot
783YPhosphorylationKinaseFLT1P35969
GPS
-KUbiquitinationE3 ubiquitin ligaseCblbQ3TTA7
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLCG1_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 PLCG1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VGFR1_MOUSEFlt1physical
17962812
PGFRB_MOUSEPdgfrbphysical
17620338
CBL_MOUSECblphysical
7517397
NTRK1_MOUSENtrk1physical
21574998
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLCG1_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-1248 AND SER-1263, ANDMASS SPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-379; TYR-481; TYR-506AND TYR-977, AND MASS SPECTROMETRY.
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-771 AND TYR-775, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory