MPP2_HUMAN - dbPTM
MPP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MPP2_HUMAN
UniProt AC Q14168
Protein Name MAGUK p55 subfamily member 2
Gene Name MPP2 {ECO:0000312|HGNC:HGNC:7220}
Organism Homo sapiens (Human).
Sequence Length 576
Subcellular Localization Cytoplasm, cytoskeleton . Membrane . Cell projection, dendrite . Cell projection, dendritic spine membrane . Prominently expressed in the post-synaptic densities of dendritic spines, is also detected in dendritic shafts.
Protein Description Postsynaptic MAGUK scaffold protein that links CADM1 cell adhesion molecules to core components of the postsynaptic density (By similarity). In CA1 pyramidal neurons, required for synaptic KCNN2-containing channel function and long-term potentiation expression (By similarity). Seems to negatively regulate SRC function in epithelial cells. [PubMed: 19665017]
Protein Sequence MPVAATNSETAMQQVLDNLGSLPSATGAAELDLIFLRGIMESPIVRSLAKVIMVLWFMQQNVFVPMKYMLKYFGAHERLEETKLEAVRDNNLELVQEILRDLAHVAEQSSTAAELAHILQEPHFQSLLETHDSVASKTYETPPPSPGLDPTFSNQPVPPDAVRMVGIRKTAGEHLGVTFRVEGGELVIARILHGGMVAQQGLLHVGDIIKEVNGQPVGSDPRALQELLRNASGSVILKILPSYQEPHLPRQVFVKCHFDYDPARDSLIPCKEAGLRFNAGDLLQIVNQDDANWWQACHVEGGSAGLIPSQLLEEKRKAFVKRDLELTPNSGTLCGSLSGKKKKRMMYLTTKNAEFDRHELLIYEEVARMPPFRRKTLVLIGAQGVGRRSLKNKLIMWDPDRYGTTVPYTSRRPKDSEREGQGYSFVSRGEMEADVRAGRYLEHGEYEGNLYGTRIDSIRGVVAAGKVCVLDVNPQAVKVLRTAEFVPYVVFIEAPDFETLRAMNRAALESGISTKQLTEADLRRTVEESSRIQRGYGHYFDLCLVNSNLERTFRELQTAMEKLRTEPQWVPVSWVY
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
2 (in isoform 4)Phosphorylation-25.1829116813
4 (in isoform 3)Phosphorylation-11.6030631047
7 (in isoform 3)Phosphorylation-32.8730631047
10 (in isoform 3)Phosphorylation-27.5320363803
15 (in isoform 3)Phosphorylation-4.0020363803
18 (in isoform 3)Phosphorylation-41.9820363803
19 (in isoform 3)Phosphorylation-5.0020363803
42PhosphorylationFLRGIMESPIVRSLA
HHHHHHCCHHHHHHH		11.5330266825
83UbiquitinationHERLEETKLEAVRDN
HHHHHHHHHHHHHCC		47.84-
87PhosphorylationEETKLEAVRDNNLEL
HHHHHHHHHCCCHHH		6.0427251275
138PhosphorylationHDSVASKTYETPPPS
CHHHHHCCCCCCCCC		24.8930266825
139PhosphorylationDSVASKTYETPPPSP
HHHHHCCCCCCCCCC		22.8819413330
141PhosphorylationVASKTYETPPPSPGL
HHHCCCCCCCCCCCC		30.5930266825
145PhosphorylationTYETPPPSPGLDPTF
CCCCCCCCCCCCCCC		37.0630266825
151PhosphorylationPSPGLDPTFSNQPVP
CCCCCCCCCCCCCCC		39.0919413330
153PhosphorylationPGLDPTFSNQPVPPD
CCCCCCCCCCCCCCC		36.7128450419
159PhosphorylationFSNQPVPPDAVRMVG
CCCCCCCCCCEEEEE		42.2919413330
160PhosphorylationSNQPVPPDAVRMVGI
CCCCCCCCCEEEEEE		52.1819413330
162PhosphorylationQPVPPDAVRMVGIRK
CCCCCCCEEEEEEEE		5.4519413330
166PhosphorylationPDAVRMVGIRKTAGE
CCCEEEEEEEECCCC		12.4919413330
172PhosphorylationVGIRKTAGEHLGVTF
EEEEECCCCCCEEEE		28.2619413330
234PhosphorylationLLRNASGSVILKILP
HHHCCCCCCEEEECC		11.95-
255MethylationLPRQVFVKCHFDYDP
CCCEEEEEEECCCCC		15.55-
255PhosphorylationLPRQVFVKCHFDYDP
CCCEEEEEEECCCCC		15.55-
276MethylationPCKEAGLRFNAGDLL
CHHHHCCCCCCHHHE		23.12-
292UbiquitinationIVNQDDANWWQACHV
EECCCCCCCCCCCCC		47.73-
327PhosphorylationVKRDLELTPNSGTLC
HHCCCEECCCCCCCC		15.8525159151
336PhosphorylationNSGTLCGSLSGKKKK
CCCCCCCCCCCCCCC		20.5425159151
336UbiquitinationNSGTLCGSLSGKKKK
CCCCCCCCCCCCCCC		20.54-
338PhosphorylationGTLCGSLSGKKKKRM
CCCCCCCCCCCCCCE		50.7125159151
340AcetylationLCGSLSGKKKKRMMY
CCCCCCCCCCCCEEE		59.0325953088
348PhosphorylationKKKRMMYLTTKNAEF
CCCCEEEEEECCCCC		2.39-
357PhosphorylationTKNAEFDRHELLIYE
ECCCCCCHHHHHHHH		30.42-
359PhosphorylationNAEFDRHELLIYEEV
CCCCCHHHHHHHHHH		46.28-
363PhosphorylationDRHELLIYEEVARMP
CHHHHHHHHHHHCCC		13.1520007894
376PhosphorylationMPPFRRKTLVLIGAQ
CCCCCCCEEEEECCC		21.9321406692
384PhosphorylationLVLIGAQGVGRRSLK
EEEECCCCCCHHHHC		24.26-
389PhosphorylationAQGVGRRSLKNKLIM
CCCCCHHHHCCCEEE		42.19-
397PhosphorylationLKNKLIMWDPDRYGT
HCCCEEEECCCCCCC		13.64-
402PhosphorylationIMWDPDRYGTTVPYT
EEECCCCCCCCCCCC		26.6323401153
404PhosphorylationWDPDRYGTTVPYTSR
ECCCCCCCCCCCCCC		18.7123401153
405PhosphorylationDPDRYGTTVPYTSRR
CCCCCCCCCCCCCCC		18.3423401153
408PhosphorylationRYGTTVPYTSRRPKD
CCCCCCCCCCCCCCC		17.0123401153
409PhosphorylationYGTTVPYTSRRPKDS
CCCCCCCCCCCCCCC		15.0823401153
410PhosphorylationGTTVPYTSRRPKDSE
CCCCCCCCCCCCCCC		22.0523401153
423PhosphorylationSEREGQGYSFVSRGE
CCCCCCCCCEEECCC		7.3425884760
424PhosphorylationEREGQGYSFVSRGEM
CCCCCCCCEEECCCC		26.4628796482
427PhosphorylationGQGYSFVSRGEMEAD
CCCCCEEECCCCEEE		32.3425002506
429PhosphorylationGYSFVSRGEMEADVR
CCCEEECCCCEEEEE		30.9718767875
430PhosphorylationYSFVSRGEMEADVRA
CCEEECCCCEEEEEC		32.5118767875
431PhosphorylationSFVSRGEMEADVRAG
CEEECCCCEEEEECC		5.9918767875
444PhosphorylationAGRYLEHGEYEGNLY
CCCCCCCCEEECCEE		29.79-
446PhosphorylationRYLEHGEYEGNLYGT
CCCCCCEEECCEECC		33.4620007894
467PhosphorylationGVVAAGKVCVLDVNP
CEEECCCEEEEECCH		2.39-
499UbiquitinationIEAPDFETLRAMNRA
EECCCHHHHHHHHHH		22.87-
499UbiquitinationIEAPDFETLRAMNRA
EECCCHHHHHHHHHH		22.87-
514PhosphorylationALESGISTKQLTEAD
HHHCCCCHHHCCHHH		22.38-
529PhosphorylationLRRTVEESSRIQRGY
HHHHHHHHHHHHCCC		16.0621815630
530PhosphorylationRRTVEESSRIQRGYG
HHHHHHHHHHHCCCC		36.3621815630
552PhosphorylationVNSNLERTFRELQTA
ECCCHHHHHHHHHHH		20.05-
576PhosphorylationWVPVSWVY-------
CEECCCCC-------		13.4325690035
583UbiquitinationY--------------
C--------------		-
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 MPP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MPP2_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 MPP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LIN7A_HUMANLIN7Aphysical
25416956
LIN7C_HUMANLIN7Cphysical
28514442
DLG1_HUMANDLG1physical
28514442
LIN7B_HUMANLIN7Bphysical
28514442
LIN7A_HUMANLIN7Aphysical
28514442
MPP6_HUMANMPP6physical
28514442
GID4_HUMANGID4physical
28514442
ARMC8_HUMANARMC8physical
28514442
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 MPP2_HUMAN

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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 THR-138; TYR-139; THR-141;SER-145 AND THR-151, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141, AND MASSSPECTROMETRY.

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