MPP5_HUMAN - dbPTM
MPP5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MPP5_HUMAN
UniProt AC Q8N3R9
Protein Name MAGUK p55 subfamily member 5
Gene Name MPP5
Organism Homo sapiens (Human).
Sequence Length 675
Subcellular Localization Cell membrane
Peripheral membrane protein. Endomembrane system
Peripheral membrane protein. Cell junction, tight junction. Localized to the tight junctions of epithelial cells and a subset of intracellular vesicles. In the retina, detected at the o
Protein Description May play a role in tight junctions biogenesis and in the establishment of cell polarity in epithelial cells. May modulate SC6A1/GAT1-mediated GABA uptake by stabilizing the transporter. Required for localization of EZR to the apical membrane of parietal cells and may play a role in the dynamic remodeling of the apical cytoskeleton (By similarity)..
Protein Sequence MTTSHMNGHVTEESDSEVKNVDLASPEEHQKHREMAVDCPGDLGTRMMPIRRSAQLERIRQQQEDMRRRREEEGKKQELDLNSSMRLKKLAQIPPKTGIDNPMFDTEEGIVLESPHYAVKILEIEDLFSSLKHIQHTLVDSQSQEDISLLLQLVQNKDFQNAFKIHNAITVHMNKASPPFPLISNAQDLAQEVQTVLKPVHHKEGQELTALLNTPHIQALLLAHDKVAEQEMQLEPITDERVYESIGQYGGETVKIVRIEKARDIPLGATVRNEMDSVIISRIVKGGAAEKSGLLHEGDEVLEINGIEIRGKDVNEVFDLLSDMHGTLTFVLIPSQQIKPPPAKETVIHVKAHFDYDPSDDPYVPCRELGLSFQKGDILHVISQEDPNWWQAYREGDEDNQPLAGLVPGKSFQQQREAMKQTIEEDKEPEKSGKLWCAKKNKKKRKKVLYNANKNDDYDNEEILTYEEMSLYHQPANRKRPIILIGPQNCGQNELRQRLMNKEKDRFASAVPHTTRSRRDQEVAGRDYHFVSRQAFEADIAAGKFIEHGEFEKNLYGTSIDSVRQVINSGKICLLSLRTQSLKTLRNSDLKPYIIFIAPPSQERLRALLAKEGKNPKPEELREIIEKTREMEQNNGHYFDTAIVNSDLDKAYQELLRLINKLDTEPQWVPSTWLR
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
2Acetylation------MTTSHMNGH
------CCCCCCCCC		36.6919413330
2Phosphorylation------MTTSHMNGH
------CCCCCCCCC		36.6920068231
3Phosphorylation-----MTTSHMNGHV
-----CCCCCCCCCC		18.4823090842
4Phosphorylation----MTTSHMNGHVT
----CCCCCCCCCCC		16.1523090842
11PhosphorylationSHMNGHVTEESDSEV
CCCCCCCCCCCCCCC		28.4928450419
14PhosphorylationNGHVTEESDSEVKNV
CCCCCCCCCCCCCCC		39.9628355574
16PhosphorylationHVTEESDSEVKNVDL
CCCCCCCCCCCCCCC		54.2728450419
25PhosphorylationVKNVDLASPEEHQKH
CCCCCCCCHHHHHHH		39.8925159151
45PhosphorylationDCPGDLGTRMMPIRR
CCCCCHHHCCCCCHH		23.7629083192
53PhosphorylationRMMPIRRSAQLERIR
CCCCCHHHHHHHHHH		15.5424706070
83PhosphorylationKQELDLNSSMRLKKL
HHHCCCCHHHHHHHH		32.5829255136
84PhosphorylationQELDLNSSMRLKKLA
HHCCCCHHHHHHHHH		13.5729255136
106PhosphorylationIDNPMFDTEEGIVLE
CCCCCCCCCCCEEEE		25.3528348404
114PhosphorylationEEGIVLESPHYAVKI
CCCEEEECCCEEEEE		16.9029978859
117PhosphorylationIVLESPHYAVKILEI
EEEECCCEEEEEEEH		19.2427642862
129PhosphorylationLEIEDLFSSLKHIQH
EEHHHHHHHHHHHHH		41.9028348404
130PhosphorylationEIEDLFSSLKHIQHT
EHHHHHHHHHHHHHH		33.8228348404
214PhosphorylationELTALLNTPHIQALL
HHHHHHCCHHHHHHH		19.06-
238PhosphorylationEMQLEPITDERVYES
HHCCCCCCCHHHHHH		42.3921945579
243PhosphorylationPITDERVYESIGQYG
CCCCHHHHHHHHHCC		15.3521945579
245PhosphorylationTDERVYESIGQYGGE
CCHHHHHHHHHCCCE		17.8421945579
249PhosphorylationVYESIGQYGGETVKI
HHHHHHHCCCEEEEE		23.1421945579
253PhosphorylationIGQYGGETVKIVRIE
HHHCCCEEEEEEEEE		30.3019664994
270PhosphorylationRDIPLGATVRNEMDS
CCCCCCCCCCCCCCH		20.42-
277PhosphorylationTVRNEMDSVIISRIV
CCCCCCCHHHHHHHH		17.57-
281PhosphorylationEMDSVIISRIVKGGA
CCCHHHHHHHHHCCH		12.58-
356PhosphorylationHVKAHFDYDPSDDPY
EEEEECCCCCCCCCC		28.8927642862
363PhosphorylationYDPSDDPYVPCRELG
CCCCCCCCCCHHHHC		24.8228674419
372PhosphorylationPCRELGLSFQKGDIL
CHHHHCCEECCCCEE		24.6730266825
383PhosphorylationGDILHVISQEDPNWW
CCEEEEEECCCCCHH		26.82-
410UbiquitinationLAGLVPGKSFQQQRE
CCCCCCCHHHHHHHH		41.86-
447UbiquitinationKNKKKRKKVLYNANK
CCCCHHHHHEEECCC		41.32-
528PhosphorylationQEVAGRDYHFVSRQA
HHHCCCCCEECCHHH		8.8720007894
532PhosphorylationGRDYHFVSRQAFEAD
CCCCEECCHHHHHHH		20.1025348954
553UbiquitinationIEHGEFEKNLYGTSI
CCCCCCCCCCCCCCH		58.53-
556PhosphorylationGEFEKNLYGTSIDSV
CCCCCCCCCCCHHHH		27.9628152594
558PhosphorylationFEKNLYGTSIDSVRQ
CCCCCCCCCHHHHHH		14.6728152594
559PhosphorylationEKNLYGTSIDSVRQV
CCCCCCCCHHHHHHH		21.7528152594
576PhosphorylationSGKICLLSLRTQSLK
HCCEEEEECCCCCHH		11.6729514088
579O-linked_GlycosylationICLLSLRTQSLKTLR
EEEEECCCCCHHHHH		28.0130379171
579PhosphorylationICLLSLRTQSLKTLR
EEEEECCCCCHHHHH		28.0129514088
581PhosphorylationLLSLRTQSLKTLRNS
EEECCCCCHHHHHCC		31.0829514088
588PhosphorylationSLKTLRNSDLKPYII
CHHHHHCCCCCCEEE		37.5828152594
593PhosphorylationRNSDLKPYIIFIAPP
HCCCCCCEEEEECCC		12.6928152594
611UbiquitinationRLRALLAKEGKNPKP
HHHHHHHHCCCCCCH		67.95-
617UbiquitinationAKEGKNPKPEELREI
HHCCCCCCHHHHHHH		74.57-
638PhosphorylationMEQNNGHYFDTAIVN
HHHHCCCCCCHHHCC		12.4427259358
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 MPP5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MPP5_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 MPP5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
INADL_HUMANINADLphysical
11927608
LIN7A_HUMANLIN7Aphysical
23718855
ZN451_HUMANZNF451physical
23718855
AMOL1_HUMANAMOTL1physical
24366813
AMOT_HUMANAMOTphysical
24366813
INADL_HUMANINADLphysical
24366813
LIN7A_HUMANLIN7Aphysical
24366813
LIN7C_HUMANLIN7Cphysical
24366813
MPDZ_HUMANMPDZphysical
24366813
LIN7C_HUMANLIN7Cphysical
28514442
MPDZ_HUMANMPDZphysical
28514442
INADL_HUMANINADLphysical
28514442
AMOL2_HUMANAMOTL2physical
28514442
RP3A_HUMANRPH3Aphysical
28514442
LIN7B_HUMANLIN7Bphysical
28514442
AMOL1_HUMANAMOTL1physical
28514442
LIN7A_HUMANLIN7Aphysical
28514442
SH3K1_HUMANSH3KBP1physical
28514442
AMOT_HUMANAMOTphysical
28514442
YAP1_HUMANYAP1physical
28514442
GAK_HUMANGAKphysical
28514442
STXB4_HUMANSTXBP4physical
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 MPP5_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-243, AND MASSSPECTROMETRY.

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