MAGI3_HUMAN - dbPTM
MAGI3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MAGI3_HUMAN
UniProt AC Q5TCQ9
Protein Name Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3
Gene Name MAGI3
Organism Homo sapiens (Human).
Sequence Length 1481
Subcellular Localization Cell membrane
Peripheral membrane protein. Cell junction, tight junction. Nucleus. Concentrates in specific sites at the plasma membrane and in the nucleus. In epithelial cells, it localizes at tight junctions (By similarity)..
Protein Description Acts as a scaffolding protein at cell-cell junctions, thereby regulating various cellular and signaling processes. Cooperates with PTEN to modulate the kinase activity of AKT1. Its interaction with PTPRB and tyrosine phosphorylated proteins suggests that it may link receptor tyrosine phosphatase with its substrates at the plasma membrane. In polarized epithelial cells, involved in efficient trafficking of TGFA to the cell surface. Regulates the ability of LPAR2 to activate ERK and RhoA pathways. Regulates the JNK signaling cascade via its interaction with FZD4 and VANGL2..
Protein Sequence MSKTLKKKKHWLSKVQECAVSWAGPPGDFGAEIRGGAERGEFPYLGRLREEPGGGTCCVVSGKAPSPGDVLLEVNGTPVSGLTNRDTLAVIRHFREPIRLKTVKPGKVINKDLRHYLSLQFQKGSIDHKLQQVIRDNLYLRTIPCTTRAPRDGEVPGVDYNFISVEQFKALEESGALLESGTYDGNFYGTPKPPAEPSPFQPDPVDQVLFDNEFDAESQRKRTTSVSKMERMDSSLPEEEEDEDKEAINGSGNAENRERHSESSDWMKTVPSYNQTNSSMDFRNYMMRDETLEPLPKNWEMAYTDTGMIYFIDHNTKTTTWLDPRLCKKAKAPEDCEDGELPYGWEKIEDPQYGTYYVDHLNQKTQFENPVEEAKRKKQLGQVEIGSSKPDMEKSHFTRDPSQLKGVLVRASLKKSTMGFGFTIIGGDRPDEFLQVKNVLKDGPAAQDGKIAPGDVIVDINGNCVLGHTHADVVQMFQLVPVNQYVNLTLCRGYPLPDDSEDPVVDIVAATPVINGQSLTKGETCMNPQDFKPGAMVLEQNGKSGHTLTGDGLNGPSDASEQRVSMASSGSSQPELVTIPLIKGPKGFGFAIADSPTGQKVKMILDSQWCQGLQKGDIIKEIYHQNVQNLTHLQVVEVLKQFPVGADVPLLILRGGPPSPTKTAKMKTDKKENAGSLEAINEPIPQPMPFPPSIIRSGSPKLDPSEVYLKSKTLYEDKPPNTKDLDVFLRKQESGFGFRVLGGDGPDQSIYIGAIIPLGAAEKDGRLRAADELMCIDGIPVKGKSHKQVLDLMTTAARNGHVLLTVRRKIFYGEKQPEDDSSQAFISTQNGSPRLNRAEVPARPAPQEPYDVVLQRKENEGFGFVILTSKNKPPPGVIPHKIGRVIEGSPADRCGKLKVGDHISAVNGQSIVELSHDNIVQLIKDAGVTVTLTVIAEEEHHGPPSGTNSARQSPALQHRPMGQSQANHIPGDRSALEGEIGKDVSTSYRHSWSDHKHLAQPDTAVISVVGSRHNQNLGCYPVELERGPRGFGFSLRGGKEYNMGLFILRLAEDGPAIKDGRIHVGDQIVEINGEPTQGITHTRAIELIQAGGNKVLLLLRPGTGLIPDHGDWDINNPSSSNVIYDEQSPLPPSSHFASIFEESHVPVIEESLRVQICEKAEELKDIVPEKKSTLNENQPEIKHQSLLQKNVSKRDPPSSHGHSNKKNLLKVENGVTRRGRSVSPKKPASQHSEEHLDKIPSPLKNNPKRRPRDQSLSPSKGENKSCQVSTRAGSGQDQCRKSRGRSASPKKQQKIEGSKAPSNAEAKLLEGKSRRIAGYTGSNAEQIPDGKEKSDVIRKDAKQNQLEKSRTRSPEKKIKRMVEKSLPSKMTNKTTSKEVSENEKGKKVTTGETSSSNDKIGENVQLSEKRLKQEPEEKVVSNKTEDHKGKELEAADKNKETGRFKPESSSPVKKTLITPGPWKVPSGNKVTGTIGMAEKRQ
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
102PhosphorylationREPIRLKTVKPGKVI
CCCEECCCCCCCCCC		38.05-
116PhosphorylationINKDLRHYLSLQFQK
CCHHHHHHHHHEECC		7.4919835603
118PhosphorylationKDLRHYLSLQFQKGS
HHHHHHHHHEECCCC		16.9819835603
147PhosphorylationLRTIPCTTRAPRDGE
EEEECCCCCCCCCCC		31.39-
223PhosphorylationAESQRKRTTSVSKME
HHHHHHHCCCHHHHH		26.8526434776
224PhosphorylationESQRKRTTSVSKMER
HHHHHHCCCHHHHHH		31.0326434776
225PhosphorylationSQRKRTTSVSKMERM
HHHHHCCCHHHHHHH		24.6326434776
234PhosphorylationSKMERMDSSLPEEEE
HHHHHHHCCCCCCCC		25.1625884760
234 (in isoform 4)Phosphorylation-25.1627251275
235PhosphorylationKMERMDSSLPEEEED
HHHHHHCCCCCCCCH		43.6129978859
251PhosphorylationDKEAINGSGNAENRE
CHHHHCCCCCHHHHH		25.1223401153
251 (in isoform 4)Phosphorylation-25.1224719451
261PhosphorylationAENRERHSESSDWMK
HHHHHHCCCCCCHHH		45.4528348404
261 (in isoform 4)Phosphorylation-45.4527251275
263PhosphorylationNRERHSESSDWMKTV
HHHHCCCCCCHHHCC		36.2928348404
269PhosphorylationESSDWMKTVPSYNQT
CCCCHHHCCCCCCCC		22.8821955146
272PhosphorylationDWMKTVPSYNQTNSS
CHHHCCCCCCCCCCC		32.1723663014
272 (in isoform 4)Phosphorylation-32.1727251275
273PhosphorylationWMKTVPSYNQTNSSM
HHHCCCCCCCCCCCH		12.7623663014
276PhosphorylationTVPSYNQTNSSMDFR
CCCCCCCCCCCHHHH		33.1721955146
278PhosphorylationPSYNQTNSSMDFRNY
CCCCCCCCCHHHHHH		30.3521955146
279PhosphorylationSYNQTNSSMDFRNYM
CCCCCCCCHHHHHHH		25.1721955146
285PhosphorylationSSMDFRNYMMRDETL
CCHHHHHHHHCCCCC		6.5027642862
353 (in isoform 3)Phosphorylation-19.4728152594
353 (in isoform 4)Phosphorylation-19.4728152594
355 (in isoform 3)Phosphorylation-13.5228152594
355 (in isoform 4)Phosphorylation-13.5228152594
356 (in isoform 3)Phosphorylation-9.3428152594
356 (in isoform 4)Phosphorylation-9.3428152594
357 (in isoform 3)Phosphorylation-8.0628152594
357 (in isoform 4)Phosphorylation-8.0628152594
403AcetylationHFTRDPSQLKGVLVR
CCCCCHHHHHHEEHH		55.58-
412PhosphorylationKGVLVRASLKKSTMG
HHEEHHHHCCCCCCC		40.6329853039
413PhosphorylationGVLVRASLKKSTMGF
HEEHHHHCCCCCCCC		42.8929853039
419AcetylationSLKKSTMGFGFTIIG
HCCCCCCCCCEEEEC		42.46-
572 (in isoform 4)Phosphorylation-29.5527251275
595PhosphorylationFGFAIADSPTGQKVK
CCEEEECCCCCCEEE		28.9023186163
595 (in isoform 4)Phosphorylation-28.9024719451
596PhosphorylationGFAIADSPTGQKVKM
CEEEECCCCCCEEEE		27.9628857561
597PhosphorylationFAIADSPTGQKVKMI
EEEECCCCCCEEEEE		53.9628857561
603PhosphorylationPTGQKVKMILDSQWC
CCCCEEEEEECCHHH		29.5128857561
620PhosphorylationLQKGDIIKEIYHQNV
CCCCCHHHHHHHHCC		18.4930266825
622PhosphorylationKGDIIKEIYHQNVQN
CCCHHHHHHHHCCCC		57.0830266825
659 (in isoform 4)Phosphorylation-29.6124719451
676 (in isoform 4)Phosphorylation-2.5824719451
684PhosphorylationLEAINEPIPQPMPFP
CCCCCCCCCCCCCCC		48.6230266825
686PhosphorylationAINEPIPQPMPFPPS
CCCCCCCCCCCCCHH		45.4230266825
688PhosphorylationNEPIPQPMPFPPSII
CCCCCCCCCCCHHHH		33.7126074081
688 (in isoform 1)O-linked_Glycosylation-33.7130379171
699PhosphorylationPSIIRSGSPKLDPSE
HHHHCCCCCCCCHHH		15.2832645325
699 (in isoform 4)Phosphorylation-15.2824719451
701PhosphorylationIIRSGSPKLDPSEVY
HHCCCCCCCCHHHEE		22.1826657352
718PhosphorylationSKTLYEDKPPNTKDL
ECCCCCCCCCCCCCC		30.7726074081
722PhosphorylationYEDKPPNTKDLDVFL
CCCCCCCCCCCCEEE		32.9623927012
724PhosphorylationDKPPNTKDLDVFLRK
CCCCCCCCCCEEEEC		21.8028355574
730PhosphorylationKDLDVFLRKQESGFG
CCCCEEEECCCCCCC		39.0823403867
733PhosphorylationDVFLRKQESGFGFRV
CEEEECCCCCCCEEE		12.3623403867
747PhosphorylationVLGGDGPDQSIYIGA
ECCCCCCCCEEEEEE		31.5423917254
820PhosphorylationGEKQPEDDSSQAFIS
CCCCCCCCCCCCEEE		12.3523532336
832PhosphorylationFISTQNGSPRLNRAE
EEECCCCCCCCCCCC		29.0123186163
832 (in isoform 4)Phosphorylation-29.0124719451
837PhosphorylationNGSPRLNRAEVPARP
CCCCCCCCCCCCCCC		28.0427542207
846PhosphorylationEVPARPAPQEPYDVV
CCCCCCCCCCCCEEE		36.3523403867
847PhosphorylationVPARPAPQEPYDVVL
CCCCCCCCCCCEEEE		32.3023403867
852PhosphorylationAPQEPYDVVLQRKEN
CCCCCCEEEEEEECC		19.9330266825
853PhosphorylationPQEPYDVVLQRKENE
CCCCCEEEEEEECCC		22.6530266825
857PhosphorylationYDVVLQRKENEGFGF
CEEEEEEECCCCCEE		17.8830266825
875PhosphorylationTSKNKPPPGVIPHKI
ECCCCCCCCCCCCCC		22.18-
915PhosphorylationGQSIVELSHDNIVQL
CCEEEEECCCCHHHH		49.38-
933 (in isoform 4)Phosphorylation-18.9327251275
940PhosphorylationTVIAEEEHHGPPSGT
EEEECHHHCCCCCCC		18.45-
953 (in isoform 4)Phosphorylation-4.1124719451
956PhosphorylationSARQSPALQHRPMGQ
CCCCCCCCCCCCCCH		13.8227732954
958PhosphorylationRQSPALQHRPMGQSQ
CCCCCCCCCCCCHHH		10.6627732954
970PhosphorylationQSQANHIPGDRSALE
HHHCCCCCCCHHHHC		62.4727732954
972PhosphorylationQANHIPGDRSALEGE
HCCCCCCCHHHHCCC		30.2727732954
974PhosphorylationNHIPGDRSALEGEIG
CCCCCCHHHHCCCCC		25.3527732954
978PhosphorylationGDRSALEGEIGKDVS
CCHHHHCCCCCCCCC		13.4426657352
987 (in isoform 4)Phosphorylation-27.0324719451
991 (in isoform 4)Phosphorylation-18.1527251275
999PhosphorylationWSDHKHLAQPDTAVI
CCCCCCCCCCCCEEE		41.7823312004
1010PhosphorylationTAVISVVGSRHNQNL
CEEEEEECCCCCCCC		23.0523312004
1011PhosphorylationAVISVVGSRHNQNLG
EEEEEECCCCCCCCC		29.6223312004
1012PhosphorylationVISVVGSRHNQNLGC
EEEEECCCCCCCCCE		16.8024719451
1013PhosphorylationISVVGSRHNQNLGCY
EEEECCCCCCCCCEE		16.6623312004
1016PhosphorylationVGSRHNQNLGCYPVE
ECCCCCCCCCEEEEE		21.1927732954
1018PhosphorylationSRHNQNLGCYPVELE
CCCCCCCCEEEEEEC		32.6227732954
1032PhosphorylationERGPRGFGFSLRGGK
CCCCCCCCEECCCCC		12.2623684312
1034 (in isoform 4)Phosphorylation-4.6224719451
1036PhosphorylationRGFGFSLRGGKEYNM
CCCCEECCCCCEEEE		20.8223684312
1039UbiquitinationGFSLRGGKEYNMGLF
CEECCCCCEEEEEEE		31.1833845483
1059PhosphorylationEDGPAIKDGRIHVGD
CCCCCEECCCEEECC		19.9630266825
1221 (in isoform 4)Phosphorylation-34.4027251275
1223 (in isoform 4)Phosphorylation-40.1127251275
1232 (in isoform 4)Phosphorylation-52.8227251275
1241PhosphorylationEHLDKIPSPLKNNPK
HHHHCCCCCCCCCCC		18.9523312004
1246PhosphorylationIPSPLKNNPKRRPRD
CCCCCCCCCCCCCCC		29.7628176443
1248PhosphorylationSPLKNNPKRRPRDQS
CCCCCCCCCCCCCCC		32.0428176443
1248 (in isoform 1)O-linked_Glycosylation-32.0430379171
1251UbiquitinationKNNPKRRPRDQSLSP
CCCCCCCCCCCCCCC		49.5621853274
1254PhosphorylationPKRRPRDQSLSPSKG
CCCCCCCCCCCCCCC		36.6325002506
1255PhosphorylationKRRPRDQSLSPSKGE
CCCCCCCCCCCCCCC		46.3533259812
1255 (in isoform 4)Phosphorylation-46.3524719451
1257PhosphorylationRPRDQSLSPSKGENK
CCCCCCCCCCCCCCC		36.7225849741
1257 (in isoform 4)Phosphorylation-36.7224719451
1266PhosphorylationSKGENKSCQVSTRAG
CCCCCCCCCEECCCC		46.4625022875
1280PhosphorylationGSGQDQCRKSRGRSA
CCCHHHHHHHCCCCC		34.7929255136
1280 (in isoform 1)O-linked_Glycosylation-34.7930379171
1282PhosphorylationGQDQCRKSRGRSASP
CHHHHHHHCCCCCCH		32.1629255136
1284PhosphorylationDQCRKSRGRSASPKK
HHHHHHCCCCCCHHH		50.3329255136
1307PhosphorylationAPSNAEAKLLEGKSR
CCCHHHHHHHCCCCC		22.1825849741
1327PhosphorylationTGSNAEQIPDGKEKS
CCCCHHHCCCCCCCH		54.2329083192
1327 (in isoform 1)O-linked_Glycosylation-54.2330379171
1345PhosphorylationRKDAKQNQLEKSRTR
HHHHHHHHHHHHCCC		32.9628348404
1347PhosphorylationDAKQNQLEKSRTRSP
HHHHHHHHHHCCCCH		25.6828348404
1374PhosphorylationPSKMTNKTTSKEVSE
CCCCCCCCCCCCHHH		29.5226074081
1376PhosphorylationKMTNKTTSKEVSENE
CCCCCCCCCCHHHCC		42.4626074081
1378PhosphorylationTNKTTSKEVSENEKG
CCCCCCCCHHHCCCC		36.4826074081
1389"N6,N6-dimethyllysine"NEKGKKVTTGETSSS
CCCCCCCCCCCCCCC		45.97-
1389MethylationNEKGKKVTTGETSSS
CCCCCCCCCCCCCCC		45.97-
1393PhosphorylationKKVTTGETSSSNDKI
CCCCCCCCCCCCCCC		40.1124719451
1407 (in isoform 4)Phosphorylation-49.0927251275
1412"N6,N6-dimethyllysine"QLSEKRLKQEPEEKV
CCCHHHHHCCCHHHH		54.18-
1412MethylationQLSEKRLKQEPEEKV
CCCHHHHHCCCHHHH		54.18-
1414PhosphorylationSEKRLKQEPEEKVVS
CHHHHHCCCHHHHCC		37.6522468782
1415PhosphorylationEKRLKQEPEEKVVSN
HHHHHCCCHHHHCCC		35.6922468782
1419PhosphorylationKQEPEEKVVSNKTED
HCCCHHHHCCCCCCC		27.7122468782
1432PhosphorylationEDHKGKELEAADKNK
CCCCCCCCCHHHHCC		24.7928348404
1450 (in isoform 4)Phosphorylation-60.7824719451
1462AcetylationTLITPGPWKVPSGNK
EEECCCCCCCCCCCE		66.25-
1473PhosphorylationSGNKVTGTIGMAEKR
CCCEEECCEEECCCC		44.6429116813
1474PhosphorylationGNKVTGTIGMAEKRQ
CCEEECCEEECCCCC		36.6825849741
1475PhosphorylationNKVTGTIGMAEKRQ-
CEEECCEEECCCCC-		42.8825159151
1479UbiquitinationGTIGMAEKRQ-----
CCEEECCCCC-----		49.1221853274
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 MAGI3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MAGI3_HUMAN !!
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 MAGI3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AGRB1_HUMANBAI1physical
10748157
PTEN_HUMANPTENphysical
10748157
ACK1_HUMANTNK2physical
19144635
PCBP2_HUMANPCBP2physical
26344197
RPE_HUMANRPEphysical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MAGI3_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-620, AND MASSSPECTROMETRY.

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