DLGP2_MOUSE - dbPTM
DLGP2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DLGP2_MOUSE
UniProt AC Q8BJ42
Protein Name Disks large-associated protein 2 {ECO:0000250|UniProtKB:Q9P1A6}
Gene Name Dlgap2 {ECO:0000312|MGI:MGI:2443181}
Organism Mus musculus (Mouse).
Sequence Length 1059
Subcellular Localization Cell membrane
Peripheral membrane protein. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Cell junction, synapse. Postsynaptic density of neuronal cells..
Protein Description May play a role in the molecular organization of synapses and neuronal cell signaling. Could be an adapter protein linking ion channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-95/SAP90 at the plasma membrane..
Protein Sequence MGTAQVLPGILQKHCCILPDRNTESQCTLCGEPEEEEGGDLAQPGLSFPGPAEEDIDQQYSWSPTQHFNEERYSPAPRNMKGLTGSRNQPQLCAGHTCGLSPPDDCEHPHDHMHHGSDVRQPYLLSPAESCPMDHHRCSPRSSVHSECMMMPVMLGDHVSSSTFPRMHYSSHYDTRDDCAMSHTSTKVNRIPANLLDQFEKQLPLHRDGFHTLQYQRASAATEQRNESPGRIRHLVHSVQKLFTKSHSLEGSSKSNINGTKSDSRVDDHHQSHLSKHSKRSKSKERKPESKHKSGMSSWWSSDDNLDSDSTYRTPSVAHRHHMDHIPHCYPEALQSPFGDLSLKTSKSNNDVKCSACEGLALTPDTRYMKRSSWSTLTVSQAKEAYRKSSLNLDKPLVHPEIKPSLRPCHYLQVPQDDWGAYPTGGKEEEIPCRRMRSGSYIKAMGDEESGESDSSPKTSPTVAIRPEPLLKPIIQRPLGDHQTQSYLQAATEVPVGHSLNPSINYNSPKFRSRNQSYMRAVSTLSQASCVSQMSEAEVNGQFESVCESVFSEVESQAMDALDLPGCFRTRSHSYLRAIQAGYSQDDECIPVMTSSNMTSTIRSTAAVSYTNYKKTPPPVPPRTTSKPLISVTAQSSTESTQDAYQDSRAQRMSPWPQDSRGGLYNSMDSLDSNKAMNLALETAAAQRHAADTQSSSTRSIDKAVLASKAEELLKSRCSSIGVQDSEFPDHQPYPRSDVETATDSDTESRGLREYHSVGVQVEDEKRHGRFKRSNSVTAAVQADLELEGFPGHVSMEDKGLQFGSSFQRHSEPSTPTQYGALRTVRTQGLFSYREDYRTQVDTSTLPPPDPWLEPSLDTVETGRMSPCRRDGSWFLKLLHTETKRMEGWCKEMEREAEENDLLEDILGKIRSAVGSAQLLMSQKFQQFYWLCQQNMDPSAMPRPTSQDLAGYWDMLQLSVEDVSMKFDELHQLKLNDWKIIESPERKEERKIPPPIPKKPPKGKFPITREKSLDLPDRQRQEARRRLMAAKRAASFRQNSATERADSIEIYIPEAQTRL
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
15S-palmitoylationPGILQKHCCILPDRN
CHHHHHCEEECCCCC		1.6728680068
117PhosphorylationHDHMHHGSDVRQPYL
CCCCCCCCCCCCCEE		28.68-
130PhosphorylationYLLSPAESCPMDHHR
EECCHHHHCCCCCCC		26.1529899451
139PhosphorylationPMDHHRCSPRSSVHS
CCCCCCCCCCHHHHH		24.2529899451
142PhosphorylationHHRCSPRSSVHSECM
CCCCCCCHHHHHHHH		39.8419060867
173PhosphorylationRMHYSSHYDTRDDCA
CCCCCCCCCCCCCCH		22.43-
184PhosphorylationDDCAMSHTSTKVNRI
CCCHHCCCCHHCCCC		30.6829899451
212PhosphorylationLHRDGFHTLQYQRAS
CCCCCHHHHHHHHHH		17.1929899451
215PhosphorylationDGFHTLQYQRASAAT
CCHHHHHHHHHHHHH		11.7729899451
222PhosphorylationYQRASAATEQRNESP
HHHHHHHHHHHCCCC		32.1629899451
228PhosphorylationATEQRNESPGRIRHL
HHHHHCCCCHHHHHH		35.8822324799
246PhosphorylationVQKLFTKSHSLEGSS
HHHHHHCCCCCCCCC		18.4320415495
248PhosphorylationKLFTKSHSLEGSSKS
HHHHCCCCCCCCCCC		34.9020415495
275PhosphorylationDHHQSHLSKHSKRSK
HHHHHHHHHHHHHHH		23.9327841257
291AcetylationKERKPESKHKSGMSS
CCCCCCCCCCCCCCC		54.087627919
293AcetylationRKPESKHKSGMSSWW
CCCCCCCCCCCCCCC		53.067627931
302PhosphorylationGMSSWWSSDDNLDSD
CCCCCCCCCCCCCCC		34.9519060867
308PhosphorylationSSDDNLDSDSTYRTP
CCCCCCCCCCCCCCC		36.3129899451
312PhosphorylationNLDSDSTYRTPSVAH
CCCCCCCCCCCCHHH		19.2118034455
336PhosphorylationCYPEALQSPFGDLSL
CCHHHHCCCCCCCCC		24.0529899451
342PhosphorylationQSPFGDLSLKTSKSN
CCCCCCCCCCCCCCC		32.3429899451
355O-linked_GlycosylationSNNDVKCSACEGLAL
CCCCCCCCHHCCEEC		30.1868733859
368PhosphorylationALTPDTRYMKRSSWS
ECCCCCCCCCCCCCC		14.7420047950
372PhosphorylationDTRYMKRSSWSTLTV
CCCCCCCCCCCCEEH		30.5520047950
373PhosphorylationTRYMKRSSWSTLTVS
CCCCCCCCCCCEEHH		29.1320047950
375PhosphorylationYMKRSSWSTLTVSQA
CCCCCCCCCEEHHHH		18.5820047950
376PhosphorylationMKRSSWSTLTVSQAK
CCCCCCCCEEHHHHH		21.8620047950
390PhosphorylationKEAYRKSSLNLDKPL
HHHHHHHCCCCCCCC		25.0627841257
438PhosphorylationIPCRRMRSGSYIKAM
CCCCHHCCCCCEEEC		23.8123737553
440PhosphorylationCRRMRSGSYIKAMGD
CCHHCCCCCEEECCC		25.5729899451
441PhosphorylationRRMRSGSYIKAMGDE
CHHCCCCCEEECCCC		15.2329899451
450PhosphorylationKAMGDEESGESDSSP
EECCCCCCCCCCCCC		45.9025521595
453PhosphorylationGDEESGESDSSPKTS
CCCCCCCCCCCCCCC		46.4425521595
455PhosphorylationEESGESDSSPKTSPT
CCCCCCCCCCCCCCC		58.7925521595
456PhosphorylationESGESDSSPKTSPTV
CCCCCCCCCCCCCCE		35.0925521595
508PhosphorylationNPSINYNSPKFRSRN
CCCCCCCCHHHHHCC		21.07-
572PhosphorylationPGCFRTRSHSYLRAI
CCCCCCCCHHHHHHH		19.0322324799
574PhosphorylationCFRTRSHSYLRAIQA
CCCCCCHHHHHHHHC		27.4022324799
583PhosphorylationLRAIQAGYSQDDECI
HHHHHCCCCCCCCCE		13.2329899451
584PhosphorylationRAIQAGYSQDDECIP
HHHHCCCCCCCCCEE		26.6429899451
604PhosphorylationNMTSTIRSTAAVSYT
CCCCCCCCCEEEEEC		20.67-
605PhosphorylationMTSTIRSTAAVSYTN
CCCCCCCCEEEEECC		14.59-
613PhosphorylationAAVSYTNYKKTPPPV
EEEEECCCCCCCCCC		13.18-
616PhosphorylationSYTNYKKTPPPVPPR
EECCCCCCCCCCCCC		36.5521183079
624PhosphorylationPPPVPPRTTSKPLIS
CCCCCCCCCCCCEEE		40.9923375375
626PhosphorylationPVPPRTTSKPLISVT
CCCCCCCCCCEEEEE		31.5023375375
631PhosphorylationTTSKPLISVTAQSST
CCCCCEEEEEECCCC		22.5421183079
633PhosphorylationSKPLISVTAQSSTES
CCCEEEEEECCCCCC		16.5222807455
633O-linked_GlycosylationSKPLISVTAQSSTES
CCCEEEEEECCCCCC		16.5222645316
636PhosphorylationLISVTAQSSTESTQD
EEEEEECCCCCCHHH		36.4419060867
637PhosphorylationISVTAQSSTESTQDA
EEEEECCCCCCHHHH		24.9019060867
638PhosphorylationSVTAQSSTESTQDAY
EEEECCCCCCHHHHH		38.9219060867
640PhosphorylationTAQSSTESTQDAYQD
EECCCCCCHHHHHHH		31.3019060867
641PhosphorylationAQSSTESTQDAYQDS
ECCCCCCHHHHHHHH		25.0021183079
645PhosphorylationTESTQDAYQDSRAQR
CCCHHHHHHHHHHHH		22.5729899451
665PhosphorylationQDSRGGLYNSMDSLD
CCCCCCCCCCHHHCC		14.4121183079
667PhosphorylationSRGGLYNSMDSLDSN
CCCCCCCCHHHCCHH		15.4825521595
670PhosphorylationGLYNSMDSLDSNKAM
CCCCCHHHCCHHHHH		25.9925521595
673PhosphorylationNSMDSLDSNKAMNLA
CCHHHCCHHHHHHHH		45.5925521595
698PhosphorylationADTQSSSTRSIDKAV
HCCCCCCHHHHHHHH		30.3129899451
700PhosphorylationTQSSSTRSIDKAVLA
CCCCCHHHHHHHHHH		34.9221183079
709UbiquitinationDKAVLASKAEELLKS
HHHHHHHHHHHHHHH		54.96-
716PhosphorylationKAEELLKSRCSSIGV
HHHHHHHHHHHHCCC		38.1925619855
719PhosphorylationELLKSRCSSIGVQDS
HHHHHHHHHCCCCCC		24.7129899451
720PhosphorylationLLKSRCSSIGVQDSE
HHHHHHHHCCCCCCC		27.3019060867
733 (in isoform 2)Phosphorylation-37.3629899451
741PhosphorylationYPRSDVETATDSDTE
CCHHHCCCCCCCCCH		34.4022324799
743PhosphorylationRSDVETATDSDTESR
HHHCCCCCCCCCHHC		43.3825521595
745PhosphorylationDVETATDSDTESRGL
HCCCCCCCCCHHCCC		41.9225521595
747PhosphorylationETATDSDTESRGLRE
CCCCCCCCHHCCCHH		39.5525521595
749PhosphorylationATDSDTESRGLREYH
CCCCCCHHCCCHHHH		33.4725521595
755PhosphorylationESRGLREYHSVGVQV
HHCCCHHHHCCEEEE		7.9229899451
774PhosphorylationRHGRFKRSNSVTAAV
CCCCCCCCCCCCCEE		33.7629899451
776PhosphorylationGRFKRSNSVTAAVQA
CCCCCCCCCCCEEEC		23.3019060867
778PhosphorylationFKRSNSVTAAVQADL
CCCCCCCCCEEECCE		14.5529899451
795PhosphorylationEGFPGHVSMEDKGLQ
CCCCCCEEHHHCCCC		15.6929899451
805PhosphorylationDKGLQFGSSFQRHSE
HCCCCCCCCHHCCCC		29.3029899451
806PhosphorylationKGLQFGSSFQRHSEP
CCCCCCCCHHCCCCC		26.2729899451
811O-linked_GlycosylationGSSFQRHSEPSTPTQ
CCCHHCCCCCCCCCH		54.084048811
811PhosphorylationGSSFQRHSEPSTPTQ
CCCHHCCCCCCCCCH		54.0821930439
814PhosphorylationFQRHSEPSTPTQYGA
HHCCCCCCCCCHHCC		42.8620415495
815PhosphorylationQRHSEPSTPTQYGAL
HCCCCCCCCCHHCCC		40.8619060867
817PhosphorylationHSEPSTPTQYGALRT
CCCCCCCCHHCCCHH		34.2120415495
873PhosphorylationSPCRRDGSWFLKLLH
CCCCCCCCHHHHHHH		20.9521183079
983PhosphorylationNDWKIIESPERKEER
CCCEECCCCCHHHHC		22.9625177544
1012PhosphorylationFPITREKSLDLPDRQ
CCCCCCCCCCCCHHH		23.5125521595
1035PhosphorylationMAAKRAASFRQNSAT
HHHHHHHHHHHCCHH		21.7022324799
1040PhosphorylationAASFRQNSATERADS
HHHHHHCCHHCCCCE		28.3822324799
1042PhosphorylationSFRQNSATERADSIE
HHHHCCHHCCCCEEE		26.3122324799
1047PhosphorylationSATERADSIEIYIPE
CHHCCCCEEEEECCH		22.5725521595
1051PhosphorylationRADSIEIYIPEAQTR
CCCEEEEECCHHHHC		9.5320415495
1057PhosphorylationIYIPEAQTRL-----
EECCHHHHCC-----		40.7729899451
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 DLGP2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DLGP2_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 DLGP2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of DLGP2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DLGP2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-745 AND SER-1047, ANDMASS SPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228; SER-440; SER-574;SER-1012; SER-1040 AND SER-1047, AND MASS SPECTROMETRY.
"Proteomic analysis of in vivo phosphorylated synaptic proteins.";
Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,Blackstock W.P., Choudhary J.S., Grant S.G.;
J. Biol. Chem. 280:5972-5982(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440; SER-450 ANDSER-453, AND MASS 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-312, AND MASSSPECTROMETRY.

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