DP00236: Myelin basic proteinFASTA viewXML view

General information
DisProt:DP00236
Name:Myelin basic protein
Synonym(s):MBP_HUMAN
MBP
Myelin A1 protein
Myelin membrane encephalitogenic protein
First appeared in release:Release 2.2 (04/14/2005)
UniProt:P02686
UniGene:Hs.551713
SwissProt: MBP_HUMAN
TrEMBL:  
NCBI (GI): 17378805
Source organism:Homo sapiens (Human)
Sequence length:304
Percent disordered:56%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MGNHAGKREL NAEKASTNSE TNRGESEKKR NLGELSRTTS EDNEVFGEAD ANQNNGTSSQ - 60
DTAVTDSKRT ADPKNAWQDA HPADPGSRPH LIRLFSRDAP GREDNTFKDR PSESDELQTI - 120
QEDSAATSES LDVMASQKRP SQRHGSKYLA TASTMDHARH GFLPRHRDTG ILDSIGRFFG - 180
GDRGAPKRGS GKDSHHPART AHYGSLPQKS HGRTQDENPV VHFFKNIVTP RTPPPSQGKG - 240
RGLSLSRFSW GAEGQRPGFG YGGRASDYKS AHKGFKGVDA QGTLSKIFKL GGRDSRSGSP - 300
MARR



Functional narrative    

Myelin basic protein (MBP) has a role in formation and stabilization of bilayers in the central and peripheral nervous system. MBP self associates as a homodimer on the cytoplasmic side of myelin. According to the CD spectra, lipid-free protein is mainly disordered with small amounts of alpha-helix and beta-sheet. The addition of lipid induces stabilization with secondary structure formation. There is an increase in alpha-helix and beta-sheet upon transition from a polar to an apolar environment.

Region 1: 134-304

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name: 
Location:134 - 304
Length:171
Region sequence:

MASQKRPSQRHGSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFGGDRGAPKRGSGKD
SHHPARTAHYGSLPQKSHGRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAE
GQRPGFGYGGRASDYKSAHKGFKGVDAQGTLSKIFKLGGRDSRSGSPMARR

Modification type: Isoform
Mutant
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Molecular assembly
Functional subclasses: Protein-protein binding
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (294 K; pH: 7.2; Tris (buffer) 0.3 mM)
References:
  1. Deibler GE, Burlin TV, Stone AL. "Three isoforms of human myelin basic protein: purification and structure." J Neurosci Res. 1995; 41(6): 819-27. PubMed: 7500383
Comments:
The experimental sequence was the 18.5 kDa isoform and therefore did not include residues 1 - 133 of the sequence listed in SwissProt.

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