MYPR_MOUSE - dbPTM
MYPR_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYPR_MOUSE
UniProt AC P60202
Protein Name Myelin proteolipid protein
Gene Name Plp1
Organism Mus musculus (Mouse).
Sequence Length 277
Subcellular Localization Cell membrane
Multi-pass membrane protein . Myelin membrane . Colocalizes with SIRT2 in internodal regions, at paranodal axoglial junction and Schmidt-Lanterman incisures of myelin sheat.
Protein Description This is the major myelin protein from the central nervous system. It plays an important role in the formation or maintenance of the multilamellar structure of myelin..
Protein Sequence MGLLECCARCLVGAPFASLVATGLCFFGVALFCGCGHEALTGTEKLIETYFSKNYQDYEYLINVIHAFQYVIYGTASFFFLYGALLLAEGFYTTGAVRQIFGDYKTTICGKGLSATVTGGQKGRGSRGQHQAHSLERVCHCLGKWLGHPDKFVGITYALTVVWLLVFACSAVPVYIYFNTWTTCQSIAFPSKTSASIGSLCADARMYGVLPWNAFPGKVCGSNLLSICKTAEFQMTFHLFIAAFVGAAATLVSLLTFMIAATYNFAVLKLMGRGTKF
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
6S-palmitoylation--MGLLECCARCLVG
--CCHHHHHHHHHCC
1.9128680068
7S-palmitoylation-MGLLECCARCLVGA
-CCHHHHHHHHHCCC
1.6328680068
10S-palmitoylationLLECCARCLVGAPFA
HHHHHHHHHCCCHHH
1.6015923654
104PhosphorylationVRQIFGDYKTTICGK
HHHHHCCCCEEEECC
15.6025521595
105AcetylationRQIFGDYKTTICGKG
HHHHCCCCEEEECCC
43.887969393
105UbiquitinationRQIFGDYKTTICGKG
HHHHCCCCEEEECCC
43.8822790023
107PhosphorylationIFGDYKTTICGKGLS
HHCCCCEEEECCCEE
15.32-
109S-palmitoylationGDYKTTICGKGLSAT
CCCCEEEECCCEEEE
4.2928680068
109S-nitrosylationGDYKTTICGKGLSAT
CCCCEEEECCCEEEE
4.2924895380
111UbiquitinationYKTTICGKGLSATVT
CCEEEECCCEEEEEC
52.8722790023
114PhosphorylationTICGKGLSATVTGGQ
EEECCCEEEEECCCC
30.4825521595
114O-linked_GlycosylationTICGKGLSATVTGGQ
EEECCCEEEEECCCC
30.484042003
116PhosphorylationCGKGLSATVTGGQKG
ECCCEEEEECCCCCC
18.4125521595
118PhosphorylationKGLSATVTGGQKGRG
CCEEEEECCCCCCCC
31.1025521595
118O-linked_GlycosylationKGLSATVTGGQKGRG
CCEEEEECCCCCCCC
31.1029155983
122UbiquitinationATVTGGQKGRGSRGQ
EEECCCCCCCCCCCH
54.5822790023
122AcetylationATVTGGQKGRGSRGQ
EEECCCCCCCCCCCH
54.58155455
126PhosphorylationGGQKGRGSRGQHQAH
CCCCCCCCCCHHHHH
31.7029899451
134PhosphorylationRGQHQAHSLERVCHC
CCHHHHHHHHHHHHH
34.6322324799
139S-palmitoylationAHSLERVCHCLGKWL
HHHHHHHHHHHHHHC
2.0528680068
141S-palmitoylationSLERVCHCLGKWLGH
HHHHHHHHHHHHCCC
4.5428680068
193PhosphorylationSIAFPSKTSASIGSL
HHCCCCCCCCCHHHH
33.5919060867
194PhosphorylationIAFPSKTSASIGSLC
HCCCCCCCCCHHHHH
24.6120415495
196PhosphorylationFPSKTSASIGSLCAD
CCCCCCCCHHHHHHH
27.5225521595
199O-palmitoylationKTSASIGSLCADARM
CCCCCHHHHHHHHHH
20.71-
201S-nitrosylationSASIGSLCADARMYG
CCCHHHHHHHHHHHC
3.2724895380
207NitrationLCADARMYGVLPWNA
HHHHHHHHCCCCCCC
9.87-
218UbiquitinationPWNAFPGKVCGSNLL
CCCCCCCCCCCCHHH
34.29-
228S-nitrosylationGSNLLSICKTAEFQM
CCHHHHHHCCCHHHH
2.6224895380

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 MYPR_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MYPR_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 MYPR_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of MYPR_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MYPR_MOUSE

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Related Literatures of Post-Translational Modification

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