PLAK_MOUSE - dbPTM
PLAK_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLAK_MOUSE
UniProt AC Q02257
Protein Name Junction plakoglobin
Gene Name Jup
Organism Mus musculus (Mouse).
Sequence Length 745
Subcellular Localization Cell junction, adherens junction. Cell junction, desmosome. Cytoplasm, cytoskeleton. Membrane
Peripheral membrane protein. Cytoplasmic in a soluble and membrane-associated form.
Protein Description Common junctional plaque protein. The membrane-associated plaques are architectural elements in an important strategic position to influence the arrangement and function of both the cytoskeleton and the cells within the tissue. The presence of plakoglobin in both the desmosomes and in the intermediate junctions suggests that it plays a central role in the structure and function of submembranous plaques. Acts as a substrate for VE-PTP and is required by it to stimulate VE-cadherin function in endothelial cells. Can replace beta-catenin in E-cadherin/catenin adhesion complexes which are proposed to couple cadherins to the actin cytoskeleton..
Protein Sequence MEVMNLIEQPIKVTEWQQTYTYDSGIHSGVNTCVPSVSSKGIMDEDDACGRQYTLKKTTTYTQGVPQNQGDLEYQMSTTARAKRVREAMCPGVSGEDSSLLLATQVEGQTTNLQRLAEPSQLLKSAIVHLINYQDDAELATRALPELTKLLNDEDPVVVTKAAMIVNQLSKKEASRRALMGSPQLVAAVVRTMQNTSDLDTARCTTSILHNLSHHREGLLAIFKSGGIPALVRMLSSPVESVLFYAITTLHNLLLYQEGAKMAVRLADGLQKMVPLLNKNNPKFLAITTDCLQLLAYGNQESKLIILANGGPQGLVQIMRNYSYEKLLWTTSRVLKVLSVCPSNKPAIVEAGGMQALGKHLTSNSPRLVQNCLWTLRNLSDVATKQEGLESVLKILVNQLSVDDVNVLTCATGTLSNLTCNNSKNKTLVTQNSGVEALIHAILRAGDKDDITEPAVCALRHLTSRHPEAEMAQNSVRLNYGIPAIVKLLNQPNQWPLVKATIGLIRNLALCPANHAPLQEAAVIPRLVQLLVKAHQDAQRHVAAGTQQPYTDGVRMEEIVEGCTGALHILARDPMNRMEIFRLNTIPLFVQLLYSSVENIQRVAAGVLCELAQDKEAADAIDAEGASAPLMELLHSRNEGTATYAAAVLFRISEDKNPDYRKRVSVELTNSLFKHDPAAWEAAQSMIPINEPYADDMDATYRPMYSSDVPLDPLDMHMDLDGDYPMDTYSDGLRPPYPTADHMLA
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
1Acetylation-------MEVMNLIE
-------CCCCCHHC		8.70-
14O-linked_GlycosylationIEQPIKVTEWQQTYT
HCCCEEEEEEEEEEE		26.89-
38PhosphorylationNTCVPSVSSKGIMDE
CCCCCCCCCCCCCCC		30.5823140645
39PhosphorylationTCVPSVSSKGIMDED
CCCCCCCCCCCCCCC		32.5223140645
53PhosphorylationDDACGRQYTLKKTTT
CCCCCCEEEEEEEEE		16.8129899451
54PhosphorylationDACGRQYTLKKTTTY
CCCCCEEEEEEEEEE		24.6222817900
56AcetylationCGRQYTLKKTTTYTQ
CCCEEEEEEEEEEEC		40.037623953
57UbiquitinationGRQYTLKKTTTYTQG
CCEEEEEEEEEEECC		54.97-
74PhosphorylationQNQGDLEYQMSTTAR
CCCCCCHHHHHHHHH		19.4729899451
77PhosphorylationGDLEYQMSTTARAKR
CCCHHHHHHHHHHHH		13.6923140645
78PhosphorylationDLEYQMSTTARAKRV
CCHHHHHHHHHHHHH		21.0925521595
79PhosphorylationLEYQMSTTARAKRVR
CHHHHHHHHHHHHHH		13.5725521595
94PhosphorylationEAMCPGVSGEDSSLL
HHHCCCCCCCCCHHE		42.2428973931
99PhosphorylationGVSGEDSSLLLATQV
CCCCCCCHHEEEEEE		35.04-
120PhosphorylationLQRLAEPSQLLKSAI
HHHHHCHHHHHHHHH		25.60-
124UbiquitinationAEPSQLLKSAIVHLI
HCHHHHHHHHHHHHH		46.57-
125PhosphorylationEPSQLLKSAIVHLIN
CHHHHHHHHHHHHHC		24.17-
171UbiquitinationMIVNQLSKKEASRRA
HHHHHHCHHHHHHHH		64.32-
182PhosphorylationSRRALMGSPQLVAAV
HHHHHCCCHHHHHHH		8.7725521595
201PhosphorylationQNTSDLDTARCTTSI
CCCCCCHHHHHHHHH		24.2528576409
205PhosphorylationDLDTARCTTSILHNL
CCHHHHHHHHHHHHH		20.30-
224UbiquitinationEGLLAIFKSGGIPAL
CCHHHHHHCCCHHHH		41.92-
372S-nitrosylationSPRLVQNCLWTLRNL
CHHHHHHHHHHHHHH		1.5521278135
372S-nitrosocysteineSPRLVQNCLWTLRNL
CHHHHHHHHHHHHHH		1.55-
448UbiquitinationAILRAGDKDDITEPA
HHHHCCCCCCCCHHH		57.28-
457S-nitrosylationDITEPAVCALRHLTS
CCCHHHHHHHHHHHH		2.9921278135
457S-palmitoylationDITEPAVCALRHLTS
CCCHHHHHHHHHHHH		2.9928526873
457S-nitrosocysteineDITEPAVCALRHLTS
CCCHHHHHHHHHHHH		2.99-
464PhosphorylationCALRHLTSRHPEAEM
HHHHHHHHCCCHHHH		34.6529514104
475PhosphorylationEAEMAQNSVRLNYGI
HHHHHHHHHHHHCCH		9.1322871156
480PhosphorylationQNSVRLNYGIPAIVK
HHHHHHHCCHHHHHH		22.4825177544
550PhosphorylationAAGTQQPYTDGVRME
HCCCCCCCCCCCCHH		17.0822817900
660PhosphorylationSEDKNPDYRKRVSVE
HCCCCCCHHHHHHHH		21.2029514104
665PhosphorylationPDYRKRVSVELTNSL
CCHHHHHHHHHHHHH		17.5725521595
669PhosphorylationKRVSVELTNSLFKHD
HHHHHHHHHHHHHCC		14.8427742792
671PhosphorylationVSVELTNSLFKHDPA
HHHHHHHHHHHCCHH		29.9224899341
730PhosphorylationDYPMDTYSDGLRPPY
CCCCCCCCCCCCCCC		27.56-
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 PLAK_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLAK_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 PLAK_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTNA1_MOUSECtnna1physical
14647292
P85A_MOUSEPik3r1physical
24567360
INSR_MOUSEInsrphysical
24567360
APC_HUMANAPCphysical
26496610
VATA_HUMANATP6V1Aphysical
26496610
KCC2G_HUMANCAMK2Gphysical
26496610
CTNA1_HUMANCTNNA1physical
26496610
DHC24_HUMANDHCR24physical
26496610
DSC2_HUMANDSC2physical
26496610
DSG2_HUMANDSG2physical
26496610
EVPL_HUMANEVPLphysical
26496610
PPIB_HUMANPPIBphysical
26496610
TRY1_HUMANPRSS1physical
26496610
TPD52_HUMANTPD52physical
26496610
THIO_HUMANTXNphysical
26496610
UBP7_HUMANUSP7physical
26496610
U5S1_HUMANEFTUD2physical
26496610
PDCD6_HUMANPDCD6physical
26496610
SCAM3_HUMANSCAMP3physical
26496610
PRP8_HUMANPRPF8physical
26496610
CGRF1_HUMANCGRRF1physical
26496610
DHX30_HUMANDHX30physical
26496610
CHM2B_HUMANCHMP2Bphysical
26496610
HIG1A_HUMANHIGD1Aphysical
26496610
RT17_HUMANMRPS17physical
26496610
RAB14_HUMANRAB14physical
26496610
SRRT_HUMANSRRTphysical
26496610
GAR1_HUMANGAR1physical
26496610
SMU1_HUMANSMU1physical
26496610
PR40A_HUMANPRPF40Aphysical
26496610
FGD6_HUMANFGD6physical
26496610
BDP1_HUMANBDP1physical
26496610
DMAP1_HUMANDMAP1physical
26496610
SYF1_HUMANXAB2physical
26496610
AK1BA_HUMANAKR1B10physical
26496610
WDR35_HUMANWDR35physical
26496610
TBL1R_HUMANTBL1XR1physical
26496610
ZC3HE_HUMANZC3H14physical
26496610
TRUA_HUMANPUS1physical
26496610
ARI5B_HUMANARID5Bphysical
26496610
PR14L_HUMANPRR14Lphysical
26496610
CCD84_HUMANCCDC84physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLAK_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665, AND MASSSPECTROMETRY.

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