Hmdb loader
Identification
HMDB Protein ID HMDBP01768
Secondary Accession Numbers
  • 7121
Name Myelin basic protein
Synonyms
  1. MBP
  2. Myelin A1 protein
  3. Myelin membrane encephalitogenic protein
Gene Name MBP
Protein Type Enzyme
Biological Properties
General Function Involved in structural constituent of myelin sheath
Specific 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
Pathways Not Available
Reactions Not Available
GO Classification
Function
structural molecule activity
structural constituent of myelin sheath
Cellular Location
  1. Peripheral membrane protein
  2. Cytoplasmic side
  3. Myelin membrane
Gene Properties
Chromosome Location Chromosome:1
Locus 18q23
SNPs MBP
Gene Sequence
>915 bp
ATGGGAAACCACGCAGGCAAACGAGAATTAAATGCCGAGAAGGCCAGTACGAATAGTGAA
ACTAACAGAGGAGAATCTGAAAAAAAGAGAAACCTGGGTGAACTTTCACGGACAACCTCA
GAGGACAACGAAGTGTTCGGAGAGGCAGATGCGAACCAGAACAATGGGACCTCCTCTCAG
GACACAGCGGTGACTGACTCCAAGCGCACAGCGGACCCGAAGAATGCCTGGCAGGATGCC
CACCCAGCTGACCCAGGGAGCCGCCCCCACTTGATCCGCCTCTTTTCCCGAGATGCCCCG
GGGAGGGAGGACAACACCTTCAAAGACAGGCCCTCTGAGTCCGACGAGCTCCAGACCATC
CAAGAAGACAGTGCAGCCACCTCCGAGAGCCTGGATGTGATGGCGTCACAGAAGAGACCC
TCCCAGAGGCACGGATCCAAGTACCTGGCCACAGCAAGTACCATGGACCATGCCAGGCAT
GGCTTCCTCCCAAGGCACAGAGACACGGGCATCCTTGACTCCATCGGGCGCTTCTTTGGC
GGTGACAGGGGTGCGCCCAAGCGGGGCTCTGGCAAGGACTCACACCACCCGGCAAGAACT
GCTCACTACGGCTCCCTGCCCCAGAAGTCACACGGCCGGACCCAAGATGAAAACCCCGTA
GTCCACTTCTTCAAGAACATTGTGACGCCTCGCACACCACCCCCGTCGCAGGGAAAGGGG
AGAGGACTGTCCCTGAGCAGATTTAGCTGGGGGGCCGAAGGCCAGAGACCAGGATTTGGC
TACGGAGGCAGAGCGTCCGACTATAAATCGGCTCACAAGGGATTCAAGGGAGTCGATGCC
CAGGGCACGCTTTCCAAAATTTTTAAGCTGGGAGGAAGAGATAGTCGCTCTGGATCACCC
ATGGCTAGACGCTGA
Protein Properties
Number of Residues 304
Molecular Weight 33116.9
Theoretical pI 10.46
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Myelin basic protein
MGNHAGKRELNAEKASTNSETNRGESEKKRNLGELSRTTSEDNEVFGEADANQNNGTSSQ
DTAVTDSKRTADPKNAWQDAHPADPGSRPHLIRLFSRDAPGREDNTFKDRPSESDELQTI
QEDSAATSESLDVMASQKRPSQRHGSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFG
GDRGAPKRGSGKDSHHPARTAHYGSLPQKSHGRTQDENPVVHFFKNIVTPRTPPPSQGKG
RGLSLSRFSWGAEGQRPGFGYGGRASDYKSAHKGFKGVDAQGTLSKIFKLGGRDSRSGSP
MARR
GenBank ID Protein 68509940
UniProtKB/Swiss-Prot ID P02686
UniProtKB/Swiss-Prot Entry Name MBP_HUMAN
PDB IDs
GenBank Gene ID NM_001025101.1
GeneCard ID MBP
GenAtlas ID MBP
HGNC ID HGNC:6925
References
General References
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  24. Li Y, Li H, Dimasi N, McCormick JK, Martin R, Schuck P, Schlievert PM, Mariuzza RA: Crystal structure of a superantigen bound to the high-affinity, zinc-dependent site on MHC class II. Immunity. 2001 Jan;14(1):93-104. [PubMed:11163233 ]
  25. Li Y, Huang Y, Lue J, Quandt JA, Martin R, Mariuzza RA: Structure of a human autoimmune TCR bound to a myelin basic protein self-peptide and a multiple sclerosis-associated MHC class II molecule. EMBO J. 2005 Sep 7;24(17):2968-79. Epub 2005 Aug 4. [PubMed:16079912 ]