MAGI2_MOUSE - dbPTM
MAGI2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MAGI2_MOUSE
UniProt AC Q9WVQ1
Protein Name Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2
Gene Name Magi2
Organism Mus musculus (Mouse).
Sequence Length 1275
Subcellular Localization Cytoplasm. Late endosome. Cell junction, synapse, synaptosome. Cell membrane
Peripheral membrane protein. Localized diffusely in the cytoplasm before nerve growth factor (NGF) stimulation. Recruted to late endosomes after NGF stimulation. Membrane-a
Protein Description Seems to act as scaffold molecule at synaptic junctions by assembling neurotransmitter receptors and cell adhesion proteins. Plays a role in nerve growth factor (NGF)-induced recruitment of RAPGEF2 to late endosomes and neurite outgrowth. May play a role in regulating activin-mediated signaling in neuronal cells. Enhances the ability of PTEN to suppress AKT1 activation (By similarity)..
Protein Sequence MSKSLKKKSHWTSKVHESVIGRNPEGQLGFELKGGAENGQFPYLGEVKPGKVAYESGSKLVSEELLLEVNETPVAGLTIRDVLAVIKHCKDPLRLKCVKQGGIVDKDLRHYLNLRFQKGSVDHELQQIIRDNLYLRTVPCTTRPHKEGEVPGVDYIFITVEEFMELEKSGALLESGTYEDNYYGTPKPPAEPAPLLNVTDQILPGATPSAEGKRKRNKSVTNMEKASIEPPEEEEEERPVVNGNGVVITPESSEHEDKSAGASGETPSQPYPAPVYSQPEELKDQMDDTKPTKPEENEDSDPLPDNWEMAYTEKGEVYFIDHNTKTTSWLDPRLAKKAKPPEECKENELPYGWEKIDDPIYGTYYVDHINRRTQFENPVLEAKRKLQQHNMPHTELGAKPLQAPGFREKPLFTRDASQLKGTFLSTTLKKSNMGFGFTIIGGDEPDEFLQVKSVIPDGPAAQDGKMETGDVIVYINEVCVLGHTHADVVKLFQSVPIGQSVNLVLCRGYPLPFDPEDPANSMVPPLAIMERPPPVMVNGRHNYETYLEYISRTSQSVPDITDRPPHSLHSMPADGQLDGTYPPPVHDDNVSMASSGATQAELMTLTIVKGAQGFGFTIADSPTGQRVKQILDIQGCPGLCEGDLIVEINQQNVQNLSHTEVVDILKDCPVGSETSLIIHRGGFFSPWKTPKPMMDRWENQGSPQTSLSAPAVPQNLPFPPALHRSSFPDSTEAFDPRKPDPYELYEKSRAIYESRQQVPPRTSFRMDSSGPDYKELDVHLRRMESGFGFRILGGDEPGQPILIGAVIAMGSADRDGRLHPGDELVYVDGIPVAGKTHRYVIDLMHHAARNGQVNLTVRRKVLCGGEPCPENGRSPGSVSTHHSSPRSDYATYSNSNHAAPSSNASPPEGFASHSLQTSDVVIHRKENEGFGFVIISSLNRPESGATITVPHKIGRIIDGSPADRCAKLKVGDRILAVNGQSIINMPHADIVKLIKDAGLSVTLRIIPQEELNSPTSAPSSEKQSPMAQQHSPLAQQSPLAQPSPATPNSPVAQPAPPQPLQLQGHENSYRSEVKARQDVKPDIRQPPFTDYRQPPLDYRQPPGGDYSQPPPLDYRQHSPDTRQYPLSDYRQPQDFDYFTVDMEKGAKGFGFSIRGGREYKMDLYVLRLAEDGPAIRNGRMRVGDQIIEINGESTRDMTHARAIELIKSGGRRVRLLLKRGTGQVPEYGMVPSSLSMCMKSDKHGSPYFYLLGHPKDTTNPTPGVLPLPPPQACRK
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
219PhosphorylationGKRKRNKSVTNMEKA
CCCCCCCCCCCHHHC		37.4122324799
221PhosphorylationRKRNKSVTNMEKASI
CCCCCCCCCHHHCCC		35.6222324799
266PhosphorylationSAGASGETPSQPYPA
CCCCCCCCCCCCCCC		31.5925521595
361PhosphorylationEKIDDPIYGTYYVDH
EECCCCCCCEEECCC		14.5925177544
365PhosphorylationDPIYGTYYVDHINRR
CCCCCEEECCCCCCC		10.1522817900
621PhosphorylationFGFTIADSPTGQRVK
CCEEEECCCCCHHHH		18.4925521595
623PhosphorylationFTIADSPTGQRVKQI
EEEECCCCCHHHHHH		50.3122324799
685PhosphorylationIHRGGFFSPWKTPKP
EECCCCCCCCCCCCC		27.8224925903
689PhosphorylationGFFSPWKTPKPMMDR
CCCCCCCCCCCCHHH		32.4515064633
702PhosphorylationDRWENQGSPQTSLSA
HHHCCCCCCCCCCCC		12.2231437775
705PhosphorylationENQGSPQTSLSAPAV
CCCCCCCCCCCCCCC		34.7120415495
706PhosphorylationNQGSPQTSLSAPAVP
CCCCCCCCCCCCCCC		18.3221183079
708PhosphorylationGSPQTSLSAPAVPQN
CCCCCCCCCCCCCCC		31.7919060867
725PhosphorylationFPPALHRSSFPDSTE
CCCHHCCCCCCCCCC		26.1125521595
726PhosphorylationPPALHRSSFPDSTEA
CCHHCCCCCCCCCCC		40.5325521595
730PhosphorylationHRSSFPDSTEAFDPR
CCCCCCCCCCCCCCC		28.5221183079
731PhosphorylationRSSFPDSTEAFDPRK
CCCCCCCCCCCCCCC		38.4221183079
768PhosphorylationRTSFRMDSSGPDYKE
CCCEECCCCCCCHHH		28.0525521595
769PhosphorylationTSFRMDSSGPDYKEL
CCEECCCCCCCHHHH		50.5151458971
773PhosphorylationMDSSGPDYKELDVHL
CCCCCCCHHHHHHHH		14.9751458979
826PhosphorylationHPGDELVYVDGIPVA
CCCCEEEEECCEECC		12.8722817900
874PhosphorylationPCPENGRSPGSVSTH
CCCCCCCCCCCCCCC		34.7055441643
883PhosphorylationGSVSTHHSSPRSDYA
CCCCCCCCCCCHHCC		34.1429899451
884PhosphorylationSVSTHHSSPRSDYAT
CCCCCCCCCCHHCCC		21.7055445925
937PhosphorylationFGFVIISSLNRPESG
EEEEEEECCCCCCCC		21.1829899451
943PhosphorylationSSLNRPESGATITVP
ECCCCCCCCCEEEEC		36.0929899451
1013PhosphorylationIPQEELNSPTSAPSS
CCHHHHCCCCCCCCC		42.0325521595
1015PhosphorylationQEELNSPTSAPSSEK
HHHHCCCCCCCCCCC		37.0225521595
1016PhosphorylationEELNSPTSAPSSEKQ
HHHCCCCCCCCCCCC		41.3824925903
1019PhosphorylationNSPTSAPSSEKQSPM
CCCCCCCCCCCCCCC		51.3429899451
1020PhosphorylationSPTSAPSSEKQSPMA
CCCCCCCCCCCCCCH		47.9924925903
1129PhosphorylationRQYPLSDYRQPQDFD
CCCCCHHCCCCCCCC		14.0522807455
1152PhosphorylationGAKGFGFSIRGGREY
CCCCCCEEEECCCEE		16.2619060867
1198PhosphorylationGESTRDMTHARAIEL
CCCCCCCCHHHHHHH		19.3729899451
1245PhosphorylationMKSDKHGSPYFYLLG
HCCCCCCCCEEEECC		19.0225521595
1247PhosphorylationSDKHGSPYFYLLGHP
CCCCCCCEEEECCCC		13.4229899451
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 MAGI2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MAGI2_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 MAGI2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AVR2A_MOUSEAcvr2aphysical
10681527
SMAD3_MOUSESmad3physical
10681527
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MAGI2_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-1013, AND MASSSPECTROMETRY.
"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-361; TYR-365 ANDTYR-826, AND MASS SPECTROMETRY.

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