MBP_RAT - dbPTM
MBP_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MBP_RAT
UniProt AC P02688
Protein Name Myelin basic protein
Gene Name Mbp
Organism Rattus norvegicus (Rat).
Sequence Length 195
Subcellular Localization Myelin membrane
Peripheral membrane protein
Cytoplasmic side. Cytoplasmic side of myelin.
Protein Description Is, with PLP, the most abundant protein component of the myelin membrane in the CNS. Has a role in both the formation and stabilization of this compact multilayer arrangement of bilayers. Each splice variant and charge isomer may have a specialized function in the assembly of an optimized, biochemically functional myelin membrane (By similarity)..
Protein Sequence MASQKRPSQRHGSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFSGDRGAPKRGSGKVPWLKQSRSPLPSHARSRPGLCHMYKDSHTRTTHYGSLPQKSQRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTLSKIFKLGGRDSRSGSPMARR
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
2Acetylation------MASQKRPSQ
------CCCCCCCCC
22.224141893
3Phosphorylation-----MASQKRPSQR
-----CCCCCCCCCC
34.6327097102
8PhosphorylationMASQKRPSQRHGSKY
CCCCCCCCCCCCCCE
43.8327097102
13PhosphorylationRPSQRHGSKYLATAS
CCCCCCCCCEEEEHH
16.4125575281
14AcetylationPSQRHGSKYLATAST
CCCCCCCCEEEEHHH
49.2025786129
15PhosphorylationSQRHGSKYLATASTM
CCCCCCCEEEEHHHH
11.8525403869
18PhosphorylationHGSKYLATASTMDHA
CCCCEEEEHHHHHHH
20.6725403869
20PhosphorylationSKYLATASTMDHARH
CCEEEEHHHHHHHHH
21.6525403869
21PhosphorylationKYLATASTMDHARHG
CEEEEHHHHHHHHHC
24.9325403869
26CitrullinationASTMDHARHGFLPRH
HHHHHHHHHCCCCCC
27.35-
26CitrullinationASTMDHARHGFLPRH
HHHHHHHHHCCCCCC
27.35-
32CitrullinationARHGFLPRHRDTGIL
HHHCCCCCCCCCCCH
39.35-
32CitrullinationARHGFLPRHRDTGIL
HHHCCCCCCCCCCCH
39.35-
36PhosphorylationFLPRHRDTGILDSIG
CCCCCCCCCCHHHHH
26.5330411139
41PhosphorylationRDTGILDSIGRFFSG
CCCCCHHHHHHHCCC
24.4027097102
44MethylationGILDSIGRFFSGDRG
CCHHHHHHHCCCCCC
27.97-
47PhosphorylationDSIGRFFSGDRGAPK
HHHHHHCCCCCCCCC
36.7522673903
50MethylationGRFFSGDRGAPKRGS
HHHCCCCCCCCCCCC
46.85-
57 (in isoform 5)Phosphorylation-39.2025403869
57 (in isoform 4)Phosphorylation-39.2025403869
57 (in isoform 2)Phosphorylation-39.2025403869
57PhosphorylationRGAPKRGSGKVPWLK
CCCCCCCCCCCCCHH
39.2022817900
59 (in isoform 2)Ubiquitination-46.98-
64AcetylationSGKVPWLKQSRSPLP
CCCCCCHHCCCCCCC
42.2122902405
66PhosphorylationKVPWLKQSRSPLPSH
CCCCHHCCCCCCCCH
32.8930411139
68PhosphorylationPWLKQSRSPLPSHAR
CCHHCCCCCCCCHHC
35.7230411139
74 (in isoform 2)Ubiquitination-18.58-
84PhosphorylationRPGLCHMYKDSHTRT
CCCCCEECCCCCCCC
6.49-
85AcetylationPGLCHMYKDSHTRTT
CCCCEECCCCCCCCC
45.2222902405
92PhosphorylationKDSHTRTTHYGSLPQ
CCCCCCCCCCCCCCC
15.15-
94PhosphorylationSHTRTTHYGSLPQKS
CCCCCCCCCCCCCHH
13.30-
96PhosphorylationTRTTHYGSLPQKSQR
CCCCCCCCCCCHHCC
29.7030411139
100AcetylationHYGSLPQKSQRTQDE
CCCCCCCHHCCCCCC
46.7622902405
100UbiquitinationHYGSLPQKSQRTQDE
CCCCCCCHHCCCCCC
46.76-
101PhosphorylationYGSLPQKSQRTQDEN
CCCCCCHHCCCCCCC
21.4625403869
104PhosphorylationLPQKSQRTQDENPVV
CCCHHCCCCCCCCCC
32.5125403869
115UbiquitinationNPVVHFFKNIVTPRT
CCCCEEECCCCCCCC
44.83-
115AcetylationNPVVHFFKNIVTPRT
CCCCEEECCCCCCCC
44.8322902405
119PhosphorylationHFFKNIVTPRTPPPS
EEECCCCCCCCCCCC
11.8525403869
119 (in isoform 4)Phosphorylation-11.8527115346
120 (in isoform 2)Ubiquitination-27.53-
122PhosphorylationKNIVTPRTPPPSQGK
CCCCCCCCCCCCCCC
41.1530411139
127DeamidationPRTPPPSQGKGRGLS
CCCCCCCCCCCCCCC
64.49-
127Deamidated glutaminePRTPPPSQGKGRGLS
CCCCCCCCCCCCCCC
64.49-
129MethylationTPPPSQGKGRGLSLS
CCCCCCCCCCCCCCC
37.49-
131Symmetric dimethylargininePPSQGKGRGLSLSRF
CCCCCCCCCCCCCCE
46.49-
131MethylationPPSQGKGRGLSLSRF
CCCCCCCCCCCCCCE
46.494141893
134PhosphorylationQGKGRGLSLSRFSWG
CCCCCCCCCCCEECC
27.4230411139
139PhosphorylationGLSLSRFSWGAEGQK
CCCCCCEECCCCCCC
24.4030411139
145 (in isoform 3)Phosphorylation-40.0327115346
146AcetylationSWGAEGQKPGFGYGG
ECCCCCCCCCCCCCC
58.9522902405
146UbiquitinationSWGAEGQKPGFGYGG
ECCCCCCCCCCCCCC
58.95-
151PhosphorylationGQKPGFGYGGRASDY
CCCCCCCCCCCHHHH
17.72-
154CitrullinationPGFGYGGRASDYKSA
CCCCCCCCHHHHHHH
26.93-
154CitrullinationPGFGYGGRASDYKSA
CCCCCCCCHHHHHHH
26.93-
166AcetylationKSAHKGFKGAYDAQG
HHHCCCCCCCCCCCC
51.8322902405
169PhosphorylationHKGFKGAYDAQGTLS
CCCCCCCCCCCCHHH
22.08-
172DeamidationFKGAYDAQGTLSKIF
CCCCCCCCCHHHHHH
42.37-
172Deamidated glutamineFKGAYDAQGTLSKIF
CCCCCCCCCHHHHHH
42.37-
174PhosphorylationGAYDAQGTLSKIFKL
CCCCCCCHHHHHHHC
18.7730411139
176PhosphorylationYDAQGTLSKIFKLGG
CCCCCHHHHHHHCCC
24.4427097102
177AcetylationDAQGTLSKIFKLGGR
CCCCHHHHHHHCCCC
56.1022902405
180AcetylationGTLSKIFKLGGRDSR
CHHHHHHHCCCCCCC
50.0922902405
184CitrullinationKIFKLGGRDSRSGSP
HHHHCCCCCCCCCCC
36.61-
184CitrullinationKIFKLGGRDSRSGSP
HHHHCCCCCCCCCCC
36.61-
186PhosphorylationFKLGGRDSRSGSPMA
HHCCCCCCCCCCCCC
27.3022673903
188PhosphorylationLGGRDSRSGSPMARR
CCCCCCCCCCCCCCC
47.8028551015
190PhosphorylationGRDSRSGSPMARR--
CCCCCCCCCCCCC--
16.8525403869
195CitrullinationSGSPMARR-------
CCCCCCCC-------
41.16-
195CitrullinationSGSPMARR-------
CCCCCCCC-------
41.16-

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
190SPhosphorylationKinaseUHMK1Q63285
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
131RMethylation

-

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 MBP_RAT !!

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

Oops, there are no PPI records of MBP_RAT !!

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

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Related Literatures of Post-Translational Modification

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