PKP3_HUMAN - dbPTM
PKP3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PKP3_HUMAN
UniProt AC Q9Y446
Protein Name Plakophilin-3
Gene Name PKP3
Organism Homo sapiens (Human).
Sequence Length 797
Subcellular Localization Nucleus. Cell junction, desmosome. Nuclear and associated with desmosomes.
Protein Description May play a role in junctional plaques..
Protein Sequence MQDGNFLLSALQPEAGVCSLALPSDLQLDRRGAEGPEAERLRAARVQEQVRARLLQLGQQPRHNGAAEPEPEAETARGTSRGQYHTLQAGFSSRSQGLSGDKTSGFRPIAKPAYSPASWSSRSAVDLSCSRRLSSAHNGGSAFGAAGYGGAQPTPPMPTRPVSFHERGGVGSRADYDTLSLRSLRLGPGGLDDRYSLVSEQLEPAATSTYRAFAYERQASSSSSRAGGLDWPEATEVSPSRTIRAPAVRTLQRFQSSHRSRGVGGAVPGAVLEPVARAPSVRSLSLSLADSGHLPDVHGFNSYGSHRTLQRLSSGFDDIDLPSAVKYLMASDPNLQVLGAAYIQHKCYSDAAAKKQARSLQAVPRLVKLFNHANQEVQRHATGAMRNLIYDNADNKLALVEENGIFELLRTLREQDDELRKNVTGILWNLSSSDHLKDRLARDTLEQLTDLVLSPLSGAGGPPLIQQNASEAEIFYNATGFLRNLSSASQATRQKMRECHGLVDALVTSINHALDAGKCEDKSVENAVCVLRNLSYRLYDEMPPSALQRLEGRGRRDLAGAPPGEVVGCFTPQSRRLRELPLAADALTFAEVSKDPKGLEWLWSPQIVGLYNRLLQRCELNRHTTEAAAGALQNITAGDRRWAGVLSRLALEQERILNPLLDRVRTADHHQLRSLTGLIRNLSRNARNKDEMSTKVVSHLIEKLPGSVGEKSPPAEVLVNIIAVLNNLVVASPIAARDLLYFDGLRKLIFIKKKRDSPDSEKSSRAASSLLANLWQYNKLHRDFRAKGYRKEDFLGP
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
9PhosphorylationQDGNFLLSALQPEAG
CCCCCHHHHCCCCCC
29.1328348404
19PhosphorylationQPEAGVCSLALPSDL
CCCCCCCCEECCCCC
17.8027470641
24PhosphorylationVCSLALPSDLQLDRR
CCCEECCCCCCCCCC
52.3728348404
75PhosphorylationEPEPEAETARGTSRG
CCCCHHHHCCCCCCC
28.8027470641
79PhosphorylationEAETARGTSRGQYHT
HHHHCCCCCCCHHEE
15.0827470641
80PhosphorylationAETARGTSRGQYHTL
HHHCCCCCCCHHEEE
36.9225394399
81MethylationETARGTSRGQYHTLQ
HHCCCCCCCHHEEEC
35.7524129315
84PhosphorylationRGTSRGQYHTLQAGF
CCCCCCHHEEECCCC
10.2921945579
86PhosphorylationTSRGQYHTLQAGFSS
CCCCHHEEECCCCCC
18.6821945579
92PhosphorylationHTLQAGFSSRSQGLS
EEECCCCCCCCCCCC
24.7521945579
93PhosphorylationTLQAGFSSRSQGLSG
EECCCCCCCCCCCCC
33.4221945579
95PhosphorylationQAGFSSRSQGLSGDK
CCCCCCCCCCCCCCC
30.4622617229
99PhosphorylationSSRSQGLSGDKTSGF
CCCCCCCCCCCCCCC
52.3420068231
102UbiquitinationSQGLSGDKTSGFRPI
CCCCCCCCCCCCCCC
48.3829967540
103PhosphorylationQGLSGDKTSGFRPIA
CCCCCCCCCCCCCCC
38.5321945579
104PhosphorylationGLSGDKTSGFRPIAK
CCCCCCCCCCCCCCC
41.4921945579
111AcetylationSGFRPIAKPAYSPAS
CCCCCCCCCCCCCCC
30.7926051181
114PhosphorylationRPIAKPAYSPASWSS
CCCCCCCCCCCCCCC
24.5821945579
115PhosphorylationPIAKPAYSPASWSSR
CCCCCCCCCCCCCCC
18.9821945579
117UbiquitinationAKPAYSPASWSSRSA
CCCCCCCCCCCCCCC
20.0729967540
118PhosphorylationKPAYSPASWSSRSAV
CCCCCCCCCCCCCCH
30.7621945579
120PhosphorylationAYSPASWSSRSAVDL
CCCCCCCCCCCCHHH
17.2421945579
121PhosphorylationYSPASWSSRSAVDLS
CCCCCCCCCCCHHHH
24.8121945579
123PhosphorylationPASWSSRSAVDLSCS
CCCCCCCCCHHHHHH
34.2928355574
128PhosphorylationSRSAVDLSCSRRLSS
CCCCHHHHHHCCHHH
12.9423927012
130PhosphorylationSAVDLSCSRRLSSAH
CCHHHHHHCCHHHCC
19.6323927012
134PhosphorylationLSCSRRLSSAHNGGS
HHHHCCHHHCCCCCC
24.5426657352
135PhosphorylationSCSRRLSSAHNGGSA
HHHCCHHHCCCCCCC
37.8328188228
141PhosphorylationSSAHNGGSAFGAAGY
HHCCCCCCCCCCCCC
23.0928152594
148PhosphorylationSAFGAAGYGGAQPTP
CCCCCCCCCCCCCCC
13.9923927012
154PhosphorylationGYGGAQPTPPMPTRP
CCCCCCCCCCCCCCC
28.1328152594
159PhosphorylationQPTPPMPTRPVSFHE
CCCCCCCCCCCCCCC
41.1628152594
163PhosphorylationPMPTRPVSFHERGGV
CCCCCCCCCCCCCCC
24.4628152594
172PhosphorylationHERGGVGSRADYDTL
CCCCCCCCCCCCCCC
23.1421945579
176PhosphorylationGVGSRADYDTLSLRS
CCCCCCCCCCCCCCC
15.1625159151
178PhosphorylationGSRADYDTLSLRSLR
CCCCCCCCCCCCCEE
16.4221945579
180PhosphorylationRADYDTLSLRSLRLG
CCCCCCCCCCCEECC
24.6723927012
183PhosphorylationYDTLSLRSLRLGPGG
CCCCCCCCEECCCCC
24.1228355574
195PhosphorylationPGGLDDRYSLVSEQL
CCCCHHHHHHHHHCC
17.2221945579
196PhosphorylationGGLDDRYSLVSEQLE
CCCHHHHHHHHHCCC
24.1621945579
199PhosphorylationDDRYSLVSEQLEPAA
HHHHHHHHHCCCCCC
25.5621945579
207PhosphorylationEQLEPAATSTYRAFA
HCCCCCCCHHHHHHH
24.5721945579
208PhosphorylationQLEPAATSTYRAFAY
CCCCCCCHHHHHHHH
20.7921945579
209PhosphorylationLEPAATSTYRAFAYE
CCCCCCHHHHHHHHH
16.8121945579
210PhosphorylationEPAATSTYRAFAYER
CCCCCHHHHHHHHHH
10.3421945579
215PhosphorylationSTYRAFAYERQASSS
HHHHHHHHHHHCCCC
12.7525106551
220PhosphorylationFAYERQASSSSSRAG
HHHHHHCCCCCCCCC
23.5521406692
221PhosphorylationAYERQASSSSSRAGG
HHHHHCCCCCCCCCC
36.9421406692
222PhosphorylationYERQASSSSSRAGGL
HHHHCCCCCCCCCCC
29.8221406692
223PhosphorylationERQASSSSSRAGGLD
HHHCCCCCCCCCCCC
26.2821406692
224PhosphorylationRQASSSSSRAGGLDW
HHCCCCCCCCCCCCC
28.2633259812
235PhosphorylationGLDWPEATEVSPSRT
CCCCCCCCCCCCCCC
34.9530266825
238PhosphorylationWPEATEVSPSRTIRA
CCCCCCCCCCCCCCC
15.7819664994
239PhosphorylationPEATEVSPSRTIRAP
CCCCCCCCCCCCCCC
32.7633259812
240PhosphorylationEATEVSPSRTIRAPA
CCCCCCCCCCCCCCH
34.2530266825
242PhosphorylationTEVSPSRTIRAPAVR
CCCCCCCCCCCCHHH
21.1028857561
250PhosphorylationIRAPAVRTLQRFQSS
CCCCHHHHHHHHHHH
22.2028857561
256PhosphorylationRTLQRFQSSHRSRGV
HHHHHHHHHHHHCCC
25.9624719451
257PhosphorylationTLQRFQSSHRSRGVG
HHHHHHHHHHHCCCC
16.4927282143
260PhosphorylationRFQSSHRSRGVGGAV
HHHHHHHHCCCCCCC
28.1423312004
261MethylationFQSSHRSRGVGGAVP
HHHHHHHCCCCCCCC
43.7124129315
280PhosphorylationEPVARAPSVRSLSLS
HCCCCCCCCCEEEEE
29.2227273156
283PhosphorylationARAPSVRSLSLSLAD
CCCCCCCEEEEEHHH
21.8327273156
285PhosphorylationAPSVRSLSLSLADSG
CCCCCEEEEEHHHCC
19.7027273156
287PhosphorylationSVRSLSLSLADSGHL
CCCEEEEEHHHCCCC
20.3823927012
291PhosphorylationLSLSLADSGHLPDVH
EEEEHHHCCCCCCCC
23.6223927012
302PhosphorylationPDVHGFNSYGSHRTL
CCCCCCCCCCCHHHH
28.7223927012
303PhosphorylationDVHGFNSYGSHRTLQ
CCCCCCCCCCHHHHH
24.6123927012
305PhosphorylationHGFNSYGSHRTLQRL
CCCCCCCCHHHHHHH
11.1023927012
308PhosphorylationNSYGSHRTLQRLSSG
CCCCCHHHHHHHHCC
23.0930266825
313PhosphorylationHRTLQRLSSGFDDID
HHHHHHHHCCCCCCC
30.5120201521
314PhosphorylationRTLQRLSSGFDDIDL
HHHHHHHCCCCCCCH
48.3320201521
323PhosphorylationFDDIDLPSAVKYLMA
CCCCCHHHHHHHHHH
53.6523927012
327PhosphorylationDLPSAVKYLMASDPN
CHHHHHHHHHHCCCC
8.6326657352
331PhosphorylationAVKYLMASDPNLQVL
HHHHHHHCCCCCEEE
39.3730278072
342PhosphorylationLQVLGAAYIQHKCYS
CEEECHHHHHHHHCC
10.6920068231
349PhosphorylationYIQHKCYSDAAAKKQ
HHHHHHCCHHHHHHH
30.1827251275
359PhosphorylationAAKKQARSLQAVPRL
HHHHHHHHHHHHHHH
28.0520873877
390PhosphorylationGAMRNLIYDNADNKL
HHHHHHHHCCCCCEE
13.3021082442
396UbiquitinationIYDNADNKLALVEEN
HHCCCCCEEEEEHHC
35.3729967540
411UbiquitinationGIFELLRTLREQDDE
CHHHHHHHHHHCCHH
30.0929967540
424PhosphorylationDELRKNVTGILWNLS
HHHHHHHHHHHHCCC
28.0920068231
431PhosphorylationTGILWNLSSSDHLKD
HHHHHCCCCCHHHHH
25.2820068231
432PhosphorylationGILWNLSSSDHLKDR
HHHHCCCCCHHHHHH
42.8420068231
433PhosphorylationILWNLSSSDHLKDRL
HHHCCCCCHHHHHHH
26.1820068231
4372-HydroxyisobutyrylationLSSSDHLKDRLARDT
CCCCHHHHHHHHHHH
37.06-
518UbiquitinationNHALDAGKCEDKSVE
HHHHHCCCCCCCCHH
35.8529967540
533UbiquitinationNAVCVLRNLSYRLYD
HHHHHHHHCHHHCCC
29.2229967540
539PhosphorylationRNLSYRLYDEMPPSA
HHCHHHCCCCCCHHH
10.8121253578
545PhosphorylationLYDEMPPSALQRLEG
CCCCCCHHHHHHHCC
35.4224043423
569S-palmitoylationPPGEVVGCFTPQSRR
CCCCEEEEECCCCHH
2.0125002405
571PhosphorylationGEVVGCFTPQSRRLR
CCEEEEECCCCHHHH
25.2121712546
574PhosphorylationVGCFTPQSRRLRELP
EEEECCCCHHHHHCC
22.1430183078
594UbiquitinationLTFAEVSKDPKGLEW
HHHHHHCCCCCCCHH
81.0829967540
609UbiquitinationLWSPQIVGLYNRLLQ
HCCHHHHHHHHHHHH
24.8729967540
647PhosphorylationRRWAGVLSRLALEQE
HHHHHHHHHHHHHHH
23.8924719451
666PhosphorylationPLLDRVRTADHHQLR
HHHHHHHHCCHHHHH
33.3125599653
674PhosphorylationADHHQLRSLTGLIRN
CCHHHHHHHHHHHHH
38.5820873877
676PhosphorylationHHQLRSLTGLIRNLS
HHHHHHHHHHHHHHH
31.0520873877
695UbiquitinationNKDEMSTKVVSHLIE
CHHHHHHHHHHHHHH
33.0829967540
703UbiquitinationVVSHLIEKLPGSVGE
HHHHHHHHCCCCCCC
53.6529967540
710UbiquitinationKLPGSVGEKSPPAEV
HCCCCCCCCCCCHHH
48.4829967540
718UbiquitinationKSPPAEVLVNIIAVL
CCCCHHHHHHHHHHH
1.5129967540
741PhosphorylationIAARDLLYFDGLRKL
HHHHHHHHHCCHHHE
13.6128152594
752AcetylationLRKLIFIKKKRDSPD
HHHEEEEEECCCCCC
41.30130667
757PhosphorylationFIKKKRDSPDSEKSS
EEEECCCCCCCHHHH
34.3429514088
760PhosphorylationKKRDSPDSEKSSRAA
ECCCCCCCHHHHHHH
50.7629514088
768PhosphorylationEKSSRAASSLLANLW
HHHHHHHHHHHHHHH
22.1228348404
769PhosphorylationKSSRAASSLLANLWQ
HHHHHHHHHHHHHHH
23.7528348404
791UbiquitinationFRAKGYRKEDFLGP-
HHHCCCCHHHCCCC-
53.8329967540
806Ubiquitination----------------
----------------
29967540

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
195YPhosphorylationKinaseSRCP12931
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PKP3_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 PKP3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DSG1_HUMANDSG1physical
12707304
DSG2_HUMANDSG2physical
12707304
DSG3_HUMANDSG3physical
12707304
DSC1_HUMANDSC1physical
12707304
DSC2_HUMANDSC2physical
12707304
DSC3_HUMANDSC3physical
12707304
PLAK_HUMANJUPphysical
12707304
K1C18_HUMANKRT18physical
12707304
DESP_HUMANDSPphysical
12707304

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 PKP3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND MASSSPECTROMETRY.
"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-180; SER-238; SER-240;SER-313 AND SER-314, AND MASS SPECTROMETRY.
"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-238, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND MASSSPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-84; TYR-176; TYR-195 ANDTYR-390, AND MASS SPECTROMETRY.
"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-84; TYR-176; TYR-195 ANDTYR-390, AND MASS SPECTROMETRY.
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules.";
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.;
Mol. Cell. Proteomics 4:1240-1250(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-84 AND TYR-195, AND MASSSPECTROMETRY.

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