PKP1_MOUSE - dbPTM
PKP1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PKP1_MOUSE
UniProt AC P97350
Protein Name Plakophilin-1
Gene Name Pkp1
Organism Mus musculus (Mouse).
Sequence Length 728
Subcellular Localization Nucleus. Cell junction, desmosome. Nuclear and associated with desmosomes..
Protein Description Seems to play a role in junctional plaques..
Protein Sequence MNHSPLKTALAYECFQDQDNSTLALPSDQKMKTGTSGRQRVQEQVMMTVKRQKSKSSQSSTLSHSNRGSMYDGLADNYNNYGTTSRSSYFSKFQAGNGSWGYPIYNGTLKREPDNRRFSSYSQMENWSRHYPRGSCATPGAGSDICFMQKIKASRSEPDLYCDPRGTLRKGTLGSKGHKTTQNRCSFYSTCSGQKAVKKCPVRPPSCTSKQDPVYVPPISCNKDLSFGHSRASSKICSEDIECSGLTIPKAVQYLCSQDEKYQAIGAYYIQHTCFQDESAKQQVYQLGGICKLVDLLRSPNQNVQQAAAGALRNLVFRSTPNKLETRRQNGIREAVSLLRRSGSTEIQKQLTGLLWNLSSTDELKEELVADALPVLTDRVIIPFSGWCDGNSNMSREVVDPEVFFNATGCLRNLSSADAGRQTMRNYSGLIDSLMAYVQNCVAASRCDDKSVENCMCILHNLSYRLDAEVPTRYRQLEYNTRNAYTEKSSTGCFSNRGDKMMNNNYDCPLPEEETNPKGSSWLYHSDAIRTYLNLMGKSKKDATLEACAGALQNLTASKGLMSNGMSQLIGIKEKGLPQIARLLQSGNSDVVRSGASLLSNMSRHPVLHRVMGNQVFPEVTRLLTSHTGNTSNSEDILSSACYTVRNLMTSQPQMAKQYFSNSMLNNVFNLCRNTASSPKAAEAARLLLSDMWASKELQSVLRQQGFDRNMMGNIAGANNLRNFTSRF
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
4Phosphorylation----MNHSPLKTALA
----CCCCHHHHHHH		27.2419367708
56PhosphorylationVKRQKSKSSQSSTLS
HHHHHCCCCCCCCCC		40.4728507225
59PhosphorylationQKSKSSQSSTLSHSN
HHCCCCCCCCCCCCC		27.52-
60PhosphorylationKSKSSQSSTLSHSNR
HCCCCCCCCCCCCCC		26.2328507225
61PhosphorylationSKSSQSSTLSHSNRG
CCCCCCCCCCCCCCC		37.2128059163
63PhosphorylationSSQSSTLSHSNRGSM
CCCCCCCCCCCCCCC		25.5919367708
65PhosphorylationQSSTLSHSNRGSMYD
CCCCCCCCCCCCCCC		25.5022817900
69PhosphorylationLSHSNRGSMYDGLAD
CCCCCCCCCCCCCCC		15.7828507225
81PhosphorylationLADNYNNYGTTSRSS
CCCCCCCCCCCCCHH		16.5328507225
99PhosphorylationKFQAGNGSWGYPIYN
CCCCCCCCCCCCCCC		22.71-
111MethylationIYNGTLKREPDNRRF
CCCCCCCCCCCCCCC		64.8930988901
119PhosphorylationEPDNRRFSSYSQMEN
CCCCCCCCCHHHHCC		26.9322817900
120PhosphorylationPDNRRFSSYSQMENW
CCCCCCCCHHHHCCC		26.5428507225
122PhosphorylationNRRFSSYSQMENWSR
CCCCCCHHHHCCCHH		25.6222817900
128PhosphorylationYSQMENWSRHYPRGS
HHHHCCCHHHCCCCC		22.2922817900
138PhosphorylationYPRGSCATPGAGSDI
CCCCCCCCCCCCCCC		26.9519060867
143PhosphorylationCATPGAGSDICFMQK
CCCCCCCCCCCHHHH		24.2222817900
154PhosphorylationFMQKIKASRSEPDLY
HHHHHHHCCCCCCCE		31.1921183079
156PhosphorylationQKIKASRSEPDLYCD
HHHHHCCCCCCCEEC		51.4922817900
172PhosphorylationRGTLRKGTLGSKGHK
CCCCCCCCCCCCCCC		30.86-
181PhosphorylationGSKGHKTTQNRCSFY
CCCCCCCCCCCCCEE		28.7523375375
186PhosphorylationKTTQNRCSFYSTCSG
CCCCCCCCEEECCCC		24.7923375375
188PhosphorylationTQNRCSFYSTCSGQK
CCCCCCEEECCCCCC		6.18-
189PhosphorylationQNRCSFYSTCSGQKA
CCCCCEEECCCCCCC		22.4123375375
190PhosphorylationNRCSFYSTCSGQKAV
CCCCEEECCCCCCCH		10.1823375375
192PhosphorylationCSFYSTCSGQKAVKK
CCEEECCCCCCCHHC		44.3323375375
206PhosphorylationKCPVRPPSCTSKQDP
CCCCCCCCCCCCCCC		32.4822817900
208PhosphorylationPVRPPSCTSKQDPVY
CCCCCCCCCCCCCCC		43.2123375375
209PhosphorylationVRPPSCTSKQDPVYV
CCCCCCCCCCCCCCC		32.4223375375
215PhosphorylationTSKQDPVYVPPISCN
CCCCCCCCCCCCCCC		16.7823375375
220PhosphorylationPVYVPPISCNKDLSF
CCCCCCCCCCCCCCC		19.8823375375
226PhosphorylationISCNKDLSFGHSRAS
CCCCCCCCCCCCCCC		39.0422817900
230PhosphorylationKDLSFGHSRASSKIC
CCCCCCCCCCCCCCC		29.8922817900
233PhosphorylationSFGHSRASSKICSED
CCCCCCCCCCCCCCC		30.9319367708
234PhosphorylationFGHSRASSKICSEDI
CCCCCCCCCCCCCCC		25.6719367708
238PhosphorylationRASSKICSEDIECSG
CCCCCCCCCCCCCCC		41.6022817900
415PhosphorylationTGCLRNLSSADAGRQ
HHHHHCCCHHHHHHH		27.3326643407
416PhosphorylationGCLRNLSSADAGRQT
HHHHCCCHHHHHHHH		33.0826643407
423PhosphorylationSADAGRQTMRNYSGL
HHHHHHHHHHHHHHH		19.4126643407
427PhosphorylationGRQTMRNYSGLIDSL
HHHHHHHHHHHHHHH		8.1826643407
428PhosphorylationRQTMRNYSGLIDSLM
HHHHHHHHHHHHHHH		30.5826643407
433PhosphorylationNYSGLIDSLMAYVQN
HHHHHHHHHHHHHHH		17.0426643407
437PhosphorylationLIDSLMAYVQNCVAA
HHHHHHHHHHHHHHH		6.6526643407
445PhosphorylationVQNCVAASRCDDKSV
HHHHHHHCCCCCCCH		24.5726643407
451PhosphorylationASRCDDKSVENCMCI
HCCCCCCCHHHHHHH		41.48-
474PhosphorylationDAEVPTRYRQLEYNT
CCCCCHHHHHCCCCC		12.7522817900
489PhosphorylationRNAYTEKSSTGCFSN
CCCCCCCCCCCCCCC		27.2223375375
490PhosphorylationNAYTEKSSTGCFSNR
CCCCCCCCCCCCCCH		39.6323375375
526PhosphorylationGSSWLYHSDAIRTYL
CCCCHHHHHHHHHHH		18.3829895711
531PhosphorylationYHSDAIRTYLNLMGK
HHHHHHHHHHHHCCC		26.6729895711
532PhosphorylationHSDAIRTYLNLMGKS
HHHHHHHHHHHCCCC		5.4629895711
539PhosphorylationYLNLMGKSKKDATLE
HHHHCCCCHHHHHHH		38.9329895711
563PhosphorylationTASKGLMSNGMSQLI
HHCCCHHHCHHHHHH		34.9625777480
567PhosphorylationGLMSNGMSQLIGIKE
CHHHCHHHHHHCCHH		24.1925777480
628PhosphorylationTRLLTSHTGNTSNSE
HHHHHCCCCCCCCHH		31.7124759943
639PhosphorylationSNSEDILSSACYTVR
CCHHHHHHHHHHHHH		19.0724759943
640PhosphorylationNSEDILSSACYTVRN
CHHHHHHHHHHHHHH		20.9324759943
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 PKP1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PKP1_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 PKP1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PKP1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PKP1_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-65; SER-156; SER-206;SER-226 AND SER-230, AND MASS SPECTROMETRY.

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