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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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  3. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed:17081983 ]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed:17974005 ]
  5. Nusbaum C, Zody MC, Borowsky ML, Kamal M, Kodira CD, Taylor TD, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Abouelleil A, Allen NR, Anderson S, Bloom T, Bugalter B, Butler J, Cook A, DeCaprio D, Engels R, Garber M, Gnirke A, Hafez N, Hall JL, Norman CH, Itoh T, Jaffe DB, Kuroki Y, Lehoczky J, Lui A, Macdonald P, Mauceli E, Mikkelsen TS, Naylor JW, Nicol R, Nguyen C, Noguchi H, O'Leary SB, O'Neill K, Piqani B, Smith CL, Talamas JA, Topham K, Totoki Y, Toyoda A, Wain HM, Young SK, Zeng Q, Zimmer AR, Fujiyama A, Hattori M, Birren BW, Sakaki Y, Lander ES: DNA sequence and analysis of human chromosome 18. Nature. 2005 Sep 22;437(7058):551-5. [PubMed:16177791 ]
  6. Carnegie PR: Amino acid sequence of the encephalitogenic basic protein from human myelin. Biochem J. 1971 Jun;123(1):57-67. [PubMed:4108501 ]
  7. Roth HJ, Kronquist K, Pretorius PJ, Crandall BF, Campagnoni AT: Isolation and characterization of a cDNA coding for a novel human 17.3K myelin basic protein (MBP) variant. J Neurosci Res. 1986;16(1):227-38. [PubMed:2427738 ]
  8. Kamholz J, de Ferra F, Puckett C, Lazzarini R: Identification of three forms of human myelin basic protein by cDNA cloning. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4962-6. [PubMed:2425357 ]
  9. Roth HJ, Kronquist KE, Kerlero de Rosbo N, Crandall BF, Campagnoni AT: Evidence for the expression of four myelin basic protein variants in the developing human spinal cord through cDNA cloning. J Neurosci Res. 1987;17(4):321-8. [PubMed:2442403 ]
  10. Streicher R, Stoffel W: The organization of the human myelin basic protein gene. Comparison with the mouse gene. Biol Chem Hoppe Seyler. 1989 May;370(5):503-10. [PubMed:2472816 ]
  11. Pribyl TM, Campagnoni CW, Kampf K, Kashima T, Handley VW, McMahon J, Campagnoni AT: The human myelin basic protein gene is included within a 179-kilobase transcription unit: expression in the immune and central nervous systems. Proc Natl Acad Sci U S A. 1993 Nov 15;90(22):10695-9. [PubMed:7504278 ]
  12. Nye SH, Pelfrey CM, Burkwit JJ, Voskuhl RR, Lenardo MJ, Mueller JP: Purification of immunologically active recombinant 21.5 kDa isoform of human myelin basic protein. Mol Immunol. 1995 Oct;32(14-15):1131-41. [PubMed:8544862 ]
  13. Boylan KB, Ayres TM, Popko B, Takahashi N, Hood LE, Prusiner SB: Repetitive DNA (TGGA)n 5' to the human myelin basic protein gene: a new form of oligonucleotide repetitive sequence showing length polymorphism. Genomics. 1990 Jan;6(1):16-22. [PubMed:1689270 ]
  14. Scoble HA, Whitaker JN, Biemann K: Analysis of the primary sequence of human myelin basic protein peptides 1-44 and 90-170 by fast atom bombardment mass spectrometry. J Neurochem. 1986 Aug;47(2):614-6. [PubMed:2426402 ]
  15. Wood DD, Moscarello MA: The isolation, characterization, and lipid-aggregating properties of a citrulline containing myelin basic protein. J Biol Chem. 1989 Mar 25;264(9):5121-7. [PubMed:2466844 ]
  16. Boulias C, Pang H, Mastronardi F, Moscarello MA: The isolation and characterization of four myelin basic proteins from the unbound fraction during CM52 chromatography. Arch Biochem Biophys. 1995 Sep 10;322(1):174-82. [PubMed:7574672 ]
  17. Gibson BW, Gilliom RD, Whitaker JN, Biemann K: Amino acid sequence of human myelin basic protein peptide 45-89 as determined by mass spectrometry. J Biol Chem. 1984 Apr 25;259(8):5028-31. [PubMed:6201481 ]
  18. Lennon VA, Wilks AV, Carnegie PR: Immunologic properties of the main encephalitogenic peptide from the basic protein of human myelin. J Immunol. 1970 Nov;105(5):1223-30. [PubMed:4099924 ]
  19. Proost P, Van Damme J, Opdenakker G: Leukocyte gelatinase B cleavage releases encephalitogens from human myelin basic protein. Biochem Biophys Res Commun. 1993 May 14;192(3):1175-81. [PubMed:7685161 ]
  20. Baldwin GS, Carnegie PR: Isolation and partial characterization of methylated arginines from the encephalitogenic basic protein of myelin. Biochem J. 1971 Jun;123(1):69-74. [PubMed:5128665 ]
  21. Mendz GL, Barden JA, Martenson RE: Conformation of a tetradecapeptide epitope of myelin basic protein. Eur J Biochem. 1995 Aug 1;231(3):659-66. [PubMed:7544282 ]
  22. Ridsdale RA, Beniac DR, Tompkins TA, Moscarello MA, Harauz G: Three-dimensional structure of myelin basic protein. II. Molecular modeling and considerations of predicted structures in multiple sclerosis. J Biol Chem. 1997 Feb 14;272(7):4269-75. [PubMed:9020143 ]
  23. Li Y, Li H, Martin R, Mariuzza RA: Structural basis for the binding of an immunodominant peptide from myelin basic protein in different registers by two HLA-DR2 proteins. J Mol Biol. 2000 Nov 24;304(2):177-88. [PubMed:11080454 ]
  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 ]