PEPL_MOUSE - dbPTM
PEPL_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PEPL_MOUSE
UniProt AC Q9R269
Protein Name Periplakin
Gene Name Ppl
Organism Mus musculus (Mouse).
Sequence Length 1755
Subcellular Localization Cell junction, desmosome. Cytoplasm, cytoskeleton. Cell membrane. Nucleus. Mitochondrion. Associated with desmosomes and intermediate filaments.
Protein Description Component of the cornified envelope of keratinocytes. May link the cornified envelope to desmosomes and intermediate filaments. May act as a localization signal in PKB/AKT-mediated signaling..
Protein Sequence MHSLFRKRNKGKYSPTVQTRSISNKELSDLIEQLQKNADQVERNIVDTEAKMQSDLARMQEGQLPEHRDAALQNVSDSEKLLYVLEADSAIAKHMKHPQGDMIAEDIRQLKERVTNLRGKHKQMYSLAVKEADPRVNWDTLVDEKLDKLSSQSFGTDLPLVDSQVEQHNIFHNEVKAIGPHLAKDKEQNSELQAKYQKLLTASQARQQHLSSLQDYMQRCTNELYWLDQQAKGRMQYDWSDRNLDYPSRRRQYENFINRNLEAKEERINKLHTEGDQLLTAEHPGRNSIEAHMEAVHAEWKEYLNLLICEESHLKYMEDYHQFHKDMKDAQELLRKVDSDLNQKYSPDFKDRYQIELLLRELDDQEKALDKYEDVVRGLQRRGQQVVPLKYRRETPLKPIPVEALCDFESDQGLISRGYSYTLQKNNGESWELTDSTGKKLAAPAVCFIIPPTDPEALALADSLGSQYRSVRQKATGSKHALQQRHEVLRTENPGDASDLQGRQLLAGLDKVASDLDRQEKAITGILRPPLEQGRAIEDSAERAKGLKNITNELLQIEPEKTQCTAECEAFVQALPASGTAPLLKTRVEDTNQKYERLVWLLEAAQEKVDVANRLENSLQRGRELLASYENRLIQDDTMPESGHVLDRKRQELEAMASELQAHKSLLGEVGKNLQVAKQCSSSLASRFQEHCPDLERQEAEVHKLNQRFNNLSQQVERRAQSLQSARAAYDEYCSGYNRVLQFLAKTPSYEPQETDSLGQMETKLKNQKNLLDELASREQEVQKVYADSQQYQQAVKDYELEAEKLRSLLDLENGRNSHVNKRARLQSPAAKVKEEEAALAAKFTEVNAINRQRLQNLEFALNLLRQQPEAGVTHETLQGGKLSSGMEETWKIKKELEEEIERRQQLENEVKSAQEEIQTLKDQGPQESLVRKEVLKKVPDPALEESFQQLQQTLAEEQHKNQLLQEELGALQLRLQALEQETRDGGQEYVVKEVLRIEPDRAQEDEVLQLREELEALRRQKGAREAEVLLLQQRVAALAAEKSRVQEKVTEREVVKLQNDPQLEAEYRRLQEEHQREGTLREKQEEELSFLQAKLRRLEKERAMAEGKITVKEVLKVEKDAAVEREVNDLTRQYEDEAAKARSGQREKTELLRKIWALEEENAKVVVQEKVREIVRPDPKAESEVANLRLELVEQERKFRGAEEQLKSYQSELEALRNRGPQVEVKEVTKEVIKYTTDPETEQELQRLREEIMDKTRLIERCDLEIYQLKQEIQALKDTKPQVQTREVVQEILQFQEDPQTKKEVESLRIQLSEEQKKQVDLEGERASQEEKIKRKEEELAQQRKERVVRQEVVQYEDEPDLRAEVTAFTNSIDAELRQIDKLHVELRRLQHRRAELERQLEELERERQARRAAELEVQRLQQRLAALEQEEAKTGEKVTHTQKVVLQQDPQQTREHALLRAQLEEERHRRQLLEGELEPLRRKLAALEKAEIKEKVVFSESVQVEKGDTEQEIQRLKKSLEEESQSKRELDSEVTRLEAKLSELEFYNSKSSKELDFLREENHKLQLERQNLQLETRRLQSEIEMAATETRDLKNITTIDSGTHLNSRLWSLEKELDDLKKMSKDKDLEIDELQRRLGSVAVKREQRENHLRRSIVVIDPDTGRELSPEEAHRAGLIDWKMFVKLRSQECDWEEISVKGPNGESSVIHDRKSGKKFSIEDALQSGRLTAAQYDRYVNKDMSIQELAVLVSGQK
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
13PhosphorylationRKRNKGKYSPTVQTR
CCCCCCCCCCCCCCC
28.6620139300
14PhosphorylationKRNKGKYSPTVQTRS
CCCCCCCCCCCCCCC
19.9920139300
16PhosphorylationNKGKYSPTVQTRSIS
CCCCCCCCCCCCCCC
21.2126643407
19PhosphorylationKYSPTVQTRSISNKE
CCCCCCCCCCCCHHH
23.2723375375
21PhosphorylationSPTVQTRSISNKELS
CCCCCCCCCCHHHHH
33.4823375375
23PhosphorylationTVQTRSISNKELSDL
CCCCCCCCHHHHHHH
42.9919854140
36UbiquitinationDLIEQLQKNADQVER
HHHHHHHHCHHHHHH
63.8022790023
76PhosphorylationDAALQNVSDSEKLLY
HHHHHCCCCHHHHHH
42.8628973931
78PhosphorylationALQNVSDSEKLLYVL
HHHCCCCHHHHHHHH
29.1728973931
312PhosphorylationNLLICEESHLKYMED
HHHHHCHHHHHHHHH
16.3025293948
463PhosphorylationEALALADSLGSQYRS
HHHHHHHHHHHHHHH
29.08-
747PhosphorylationVLQFLAKTPSYEPQE
HHHHHHCCCCCCCCC
16.3220469934
749PhosphorylationQFLAKTPSYEPQETD
HHHHCCCCCCCCCCC
47.5720469934
750PhosphorylationFLAKTPSYEPQETDS
HHHCCCCCCCCCCCC
32.6020469934
755PhosphorylationPSYEPQETDSLGQME
CCCCCCCCCCHHHHH
26.1620469934
757PhosphorylationYEPQETDSLGQMETK
CCCCCCCCHHHHHHH
41.6520469934
763PhosphorylationDSLGQMETKLKNQKN
CCHHHHHHHHHHHHH
36.0120469934
777PhosphorylationNLLDELASREQEVQK
HHHHHHHHHHHHHHH
49.3125367039
884PhosphorylationTLQGGKLSSGMEETW
CCCCCCCCCCHHHHH
28.4728973931
885PhosphorylationLQGGKLSSGMEETWK
CCCCCCCCCHHHHHH
53.23-
895UbiquitinationEETWKIKKELEEEIE
HHHHHHHHHHHHHHH
71.63-
947PhosphorylationPDPALEESFQQLQQT
CCHHHHHHHHHHHHH
20.98-
1308PhosphorylationQTKKEVESLRIQLSE
CCHHHHHHHHHHCCH
28.2927742792
1314PhosphorylationESLRIQLSEEQKKQV
HHHHHHCCHHHHHHC
23.7827742792
1329PhosphorylationDLEGERASQEEKIKR
CCCCCHHCHHHHHHH
44.3328973931
1348MethylationLAQQRKERVVRQEVV
HHHHHHHHHHHHHHH
34.9515230859
1373PhosphorylationEVTAFTNSIDAELRQ
HHHHHHHCHHHHHHH
20.8428973931
1583PhosphorylationLETRRLQSEIEMAAT
HHHHHHHHHHHHHHH
45.17-
1599PhosphorylationTRDLKNITTIDSGTH
CCCCCCCEEECCCCC
27.3929472430
1600PhosphorylationRDLKNITTIDSGTHL
CCCCCCEEECCCCCH
20.9929472430
1603PhosphorylationKNITTIDSGTHLNSR
CCCEEECCCCCHHHH
41.5630352176
1605PhosphorylationITTIDSGTHLNSRLW
CEEECCCCCHHHHHH
27.4330352176
1609PhosphorylationDSGTHLNSRLWSLEK
CCCCCHHHHHHHHHH
34.8029472430
1656PhosphorylationRENHLRRSIVVIDPD
HHHCCCCEEEEECCC
17.1927742792
1719PhosphorylationRKSGKKFSIEDALQS
CCCCCCEEHHHHHHH
33.6726239621

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 PEPL_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PEPL_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 PEPL_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BFSP2_MOUSEBfsp2physical
19029034
BFSP1_MOUSEBfsp1physical
19029034
VIME_MOUSEVimphysical
19029034

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PEPL_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-14 AND SER-1656, ANDMASS SPECTROMETRY.

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