ID:MBP_HUMAN DESCRIPTION: RecName: Full=Myelin basic protein; Short=MBP; AltName: Full=Myelin A1 protein; AltName: Full=Myelin membrane encephalitogenic protein; FUNCTION: The classic group of MBP isoforms (isoform 4-isoform 14) are with PLP the most abundant protein components of the myelin membrane in the CNS. They have a role in both its formation and stabilization. The smaller isoforms might have an important role in remyelination of denuded axons in multiple sclerosis. The non- classic group of MBP isoforms (isoform 1-isoform 3/Golli-MBPs) may preferentially have a role in the early developing brain long before myelination, maybe as components of transcriptional complexes, and may also be involved in signaling pathways in T- cells and neural cells. Differential splicing events combined with optional post-translational modifications give a wide spectrum of isomers, with each of them potentially having a specialized function. Induces T-cell proliferation. SUBUNIT: Homodimer. Isoform 3 exists as a homodimer. SUBCELLULAR LOCATION: Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic side of myelin. TISSUE SPECIFICITY: MBP isoforms are found in both the central and the peripheral nervous system, whereas Golli-MBP isoforms are expressed in fetal thymus, spleen and spinal cord, as well as in cell lines derived from the immune system. DEVELOPMENTAL STAGE: Expression begins abruptly in 14-16 week old fetuses. Even smaller isoforms seem to be produced during embryogenesis; some of these persisting in the adult. Isoform 4 expression is more evident at 16 weeks and its relative proportion declines thereafter. PTM: Several charge isomers of MBP; C1 (the most cationic, least modified, and most abundant form), C2, C3, C4, C5, C6, C7, C8-A and C8-B (the least cationic form); are produced as a result of optional PTM, such as phosphorylation, deamidation of glutamine or asparagine, arginine citrullination and methylation. C8-A and C8-B contain each two mass isoforms termed C8-A(H), C8-A(L), C8-B(H) and C8-B(L), (H) standing for higher and (L) for lower molecular weight. C3, C4 and C5 are phosphorylated. The ratio of methylated arginine residues decreases during aging, making the protein more cationic. PTM: The N-terminal alanine is acetylated (isoform 3, isoform 4, isoform 5 and isoform 6). PTM: Arg-241 was found to be 6% monomethylated and 60% symmetrically dimethylated. PTM: Phosphorylated by TAOK2, VRK2, MAPK11, MAPK12, MAPK14 and MINK1. DISEASE: Note=The reduction in the surface charge of citrullinated and/or methylated MBP could result in a weakened attachment to the myelin membrane. This mechanism could be operative in demyelinating diseases such as chronical multiple sclerosis (MS), and fulminating MS (Marburg disease). SIMILARITY: Belongs to the myelin basic protein family. SEQUENCE CAUTION: Sequence=AAC41944.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. The C-terminus contains a Histidine tag; Sequence=BAD92223.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; Sequence=CAH10359.1; Type=Miscellaneous discrepancy; Note=wrong intron-exon boundaries; WEB RESOURCE: Name=Wikipedia; Note=Myelin basic protein entry; URL="http://en.wikipedia.org/wiki/Myelin_basic_protein";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P02686
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
US Server
Sequence and Links to Tools and Databases 
Common Gene Haplotype Alleles 
