MPP6_HUMAN - dbPTM
MPP6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MPP6_HUMAN
UniProt AC Q9NZW5
Protein Name MAGUK p55 subfamily member 6
Gene Name MPP6
Organism Homo sapiens (Human).
Sequence Length 540
Subcellular Localization Membrane
Peripheral membrane protein.
Protein Description
Protein Sequence MQQVLENLTELPSSTGAEEIDLIFLKGIMENPIVKSLAKAHERLEDSKLEAVSDNNLELVNEILEDITPLINVDENVAELVGILKEPHFQSLLEAHDIVASKCYDSPPSSPEMNNSSINNQLLPVDAIRILGIHKRAGEPLGVTFRVENNDLVIARILHGGMIDRQGLLHVGDIIKEVNGHEVGNNPKELQELLKNISGSVTLKILPSYRDTITPQQVFVKCHFDYNPYNDNLIPCKEAGLKFSKGEILQIVNREDPNWWQASHVKEGGSAGLIPSQFLEEKRKAFVRRDWDNSGPFCGTISSKKKKKMMYLTTRNAEFDRHEIQIYEEVAKMPPFQRKTLVLIGAQGVGRRSLKNRFIVLNPTRFGTTVPFTSRKPREDEKDGQAYKFVSRSEMEADIKAGKYLEHGEYEGNLYGTKIDSILEVVQTGRTCILDVNPQALKVLRTSEFMPYVVFIAAPELETLRAMHKAVVDAGITTKLLTDSDLKKTVDESARIQRAYNHYFDLIIINDNLDKAFEKLQTAIEKLRMEPQWVPISWVY
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
104PhosphorylationDIVASKCYDSPPSSP
HHHHHHCCCCCCCCC
24.1629255136
106PhosphorylationVASKCYDSPPSSPEM
HHHHCCCCCCCCCCC
16.5529255136
109PhosphorylationKCYDSPPSSPEMNNS
HCCCCCCCCCCCCCC
63.0129255136
110PhosphorylationCYDSPPSSPEMNNSS
CCCCCCCCCCCCCCC
30.5629255136
116PhosphorylationSSPEMNNSSINNQLL
CCCCCCCCCCCCCCC
27.8229255136
117PhosphorylationSPEMNNSSINNQLLP
CCCCCCCCCCCCCCC
31.3029255136
136MethylationRILGIHKRAGEPLGV
HHEEEHHCCCCCEEC
33.3954429701
162SulfoxidationARILHGGMIDRQGLL
EEEECCCCCCCCCCC
3.2221406390
195UbiquitinationKELQELLKNISGSVT
HHHHHHHHHCCCCEE
65.9321890473
195UbiquitinationKELQELLKNISGSVT
HHHHHHHHHCCCCEE
65.9321890473
198PhosphorylationQELLKNISGSVTLKI
HHHHHHCCCCEEEEE
34.12-
202PhosphorylationKNISGSVTLKILPSY
HHCCCCEEEEECCCC
24.8322210691
208PhosphorylationVTLKILPSYRDTITP
EEEEECCCCCCCCCH
29.3824719451
209PhosphorylationTLKILPSYRDTITPQ
EEEECCCCCCCCCHH
15.5722210691
214PhosphorylationPSYRDTITPQQVFVK
CCCCCCCCHHHEEEE
19.6923312004
237UbiquitinationNDNLIPCKEAGLKFS
CCCEEEHHHHCCCCC
45.29-
242UbiquitinationPCKEAGLKFSKGEIL
EHHHHCCCCCCCCEE
46.83-
245UbiquitinationEAGLKFSKGEILQIV
HHCCCCCCCCEEEEE
64.79-
266UbiquitinationWWQASHVKEGGSAGL
CEECCCCCCCCCCCC
45.26-
282UbiquitinationPSQFLEEKRKAFVRR
CHHHHHHHHHHHHHC
50.23-
300PhosphorylationNSGPFCGTISSKKKK
CCCCCCCEECCCCCC
20.9027080861
302PhosphorylationGPFCGTISSKKKKKM
CCCCCEECCCCCCEE
35.6225159151
303PhosphorylationPFCGTISSKKKKKMM
CCCCEECCCCCCEEE
44.6421815630
311PhosphorylationKKKKKMMYLTTRNAE
CCCCEEEEEEECCCC
9.4427642862
313PhosphorylationKKKMMYLTTRNAEFD
CCEEEEEEECCCCCC
13.2628857561
314PhosphorylationKKMMYLTTRNAEFDR
CEEEEEEECCCCCCH
21.2328857561
321MethylationTRNAEFDRHEIQIYE
ECCCCCCHHHHHHHH
34.3624391053
327PhosphorylationDRHEIQIYEEVAKMP
CHHHHHHHHHHHCCC
6.9420007894
340PhosphorylationMPPFQRKTLVLIGAQ
CCCCCCCEEEEECCC
25.0421406692
353PhosphorylationAQGVGRRSLKNRFIV
CCCCCHHHCCCCEEE
42.19-
368PhosphorylationLNPTRFGTTVPFTSR
ECCCCCCCCCCCCCC
23.1621406692
369PhosphorylationNPTRFGTTVPFTSRK
CCCCCCCCCCCCCCC
26.9321406692
373PhosphorylationFGTTVPFTSRKPRED
CCCCCCCCCCCCCCC
22.8821406692
374PhosphorylationGTTVPFTSRKPREDE
CCCCCCCCCCCCCCC
38.3921406692
387PhosphorylationDEKDGQAYKFVSRSE
CCCCCCEEEEECHHH
9.32-
391PhosphorylationGQAYKFVSRSEMEAD
CCEEEEECHHHHHHH
32.9725159151
393PhosphorylationAYKFVSRSEMEADIK
EEEEECHHHHHHHHH
33.5125159151
403UbiquitinationEADIKAGKYLEHGEY
HHHHHHCCCCCCCEE
52.0721890473
403UbiquitinationEADIKAGKYLEHGEY
HHHHHHCCCCCCCEE
52.0721890473
404PhosphorylationADIKAGKYLEHGEYE
HHHHHCCCCCCCEEC
19.1921406692
410PhosphorylationKYLEHGEYEGNLYGT
CCCCCCEECCCEECC
33.4621406692
415PhosphorylationGEYEGNLYGTKIDSI
CEECCCEECCCHHHH
27.0921406692
417PhosphorylationYEGNLYGTKIDSILE
ECCCEECCCHHHHHH
15.9821406692
442UbiquitinationDVNPQALKVLRTSEF
ECCHHHHHHHHHCCC
42.09-
446PhosphorylationQALKVLRTSEFMPYV
HHHHHHHHCCCCCEE
28.57-
482PhosphorylationGITTKLLTDSDLKKT
CCCCEECCHHHHHHH
43.84-
493PhosphorylationLKKTVDESARIQRAY
HHHHHCHHHHHHHHH
20.55-
500PhosphorylationSARIQRAYNHYFDLI
HHHHHHHHHHHCCEE
12.5019060867
503PhosphorylationIQRAYNHYFDLIIIN
HHHHHHHHCCEEEEC
8.6427811184
515UbiquitinationIINDNLDKAFEKLQT
EECCCHHHHHHHHHH
59.1321890473
515UbiquitinationIINDNLDKAFEKLQT
EECCCHHHHHHHHHH
59.1321890473
519UbiquitinationNLDKAFEKLQTAIEK
CHHHHHHHHHHHHHH
39.1721890473
519UbiquitinationNLDKAFEKLQTAIEK
CHHHHHHHHHHHHHH
39.1721890473

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 MPP6_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MPP6_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 MPP6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FRIL_HUMANFTLphysical
15231747
THOP1_HUMANTHOP1physical
15231747
EIF3G_HUMANEIF3Gphysical
15231747
RHG18_HUMANARHGAP18physical
15231747
SKAP_HUMANKNSTRNphysical
15231747
EXOSX_HUMANEXOSC10physical
15231747
SNX9_HUMANSNX9physical
15231747
SK2L2_HUMANSKIV2L2physical
15231747
AATF_HUMANAATFphysical
15231747
LIN7A_HUMANLIN7Aphysical
11311936
DLRB1_HUMANDYNLRB1physical
15231747
RS20_HUMANRPS20physical
15231747
SMCA4_HUMANSMARCA4physical
15231747
DYN2_HUMANDNM2physical
15231747
PARN_HUMANPARNphysical
15231747

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 MPP6_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-500, AND MASSSPECTROMETRY.

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