[1]
|
PROTEIN SEQUENCE.
PubMed=5096093 [NCBI, ExPASy, EBI, Israel, Japan]
Eylar E.H.,
Brostoff S.W.,
Hashim G.,
Caccam J.,
Burnett P.;
"Basic A1 protein of the myelin membrane. The complete amino acid sequence.";
J. Biol. Chem. 246:5770-5784(1971).
|
[2]
|
SEQUENCE REVISION.
PubMed=4129204 [NCBI, ExPASy, EBI, Israel, Japan]
Brostoff S.W.,
Reuter W.,
Hichens M.,
Eylar E.H.;
"Specific cleavage of the A1 protein from myelin with cathepsin D.";
J. Biol. Chem. 249:559-567(1974).
|
[3]
|
NUCLEOTIDE SEQUENCE [MRNA] OF 4-56.
Pietrowski D.,
Medugorac I.,
Foerster M.;
"A new MBP allele in Bos taurus is characterized by BseNI PCR-RFLP.";
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
|
[4]
|
PROTEIN SEQUENCE OF 43-87.
Shapira R.,
McKneally S.S.,
Chou F.C.-H.,
Kibler R.F.;
"Encephalitogenic fragment of myelin basic protein. Amino acid sequence of bovine, rabbit, guinea pig, monkey, and human fragments.";
J. Biol. Chem. 246:4630-4640(1971).
|
[5]
|
PROTEIN SEQUENCE OF 38-58 AND 119-141.
TISSUE=Brain;
DOI=10.1021/bi00152a022; PubMed=1382581 [NCBI, ExPASy, EBI, Israel, Japan]
Pirollet F.,
Derancourt J.,
Haiech J.,
Job D.,
Margolis R.L.;
"Ca(2+)-calmodulin regulated effectors of microtubule stability in bovine brain.";
Biochemistry 31:8849-8855(1992).
|
[6]
|
PROTEIN SEQUENCE OF 30-42; 74-89 AND 114-129.
DOI=10.1074/jbc.270.51.30551; PubMed=8530487 [NCBI, ExPASy, EBI, Israel, Japan]
Prasad K.,
Barouch W.,
Martin B.M.,
Greene L.E.,
Eisenberg E.;
"Purification of a new clathrin assembly protein from bovine brain coated vesicles and its identification as myelin basic protein.";
J. Biol. Chem. 270:30551-30556(1995).
|
[7]
|
SYNTHESIS OF ALLERGIC ENCEPHALOMYELITIS INDUCING REGION.
PubMed=5442707 [NCBI, ExPASy, EBI, Israel, Japan]
Eylar E.H.,
Caccam J.,
Jackson J.J.,
Westall F.C.,
Robinson A.B.;
"Experimental allergic encephalomyelitis: synthesis of disease-inducing site of the basic protein.";
Science 168:1220-1223(1970).
|
[8]
|
METHYLATION AT ARG-106.
PubMed=4994464 [NCBI, ExPASy, EBI, Israel, Japan]
Brostoff S.W.,
Eylar E.H.;
"Localization of methylated arginine in the A1 protein from myelin.";
Proc. Natl. Acad. Sci. U.S.A. 68:765-769(1971).
|
[9]
|
POST-TRANSLATIONAL MODIFICATIONS.
PubMed=57115 [NCBI, ExPASy, EBI, Israel, Japan]
Chou F.C.-H.,
Chou C.-H.J.,
Shapira R.,
Kibler R.F.;
"Basis of microheterogeneity of myelin basic protein.";
J. Biol. Chem. 251:2671-2679(1976).
|
[10]
|
PROTEIN SEQUENCE OF 97-104, AND PHOSPHORYLATION AT THR-97.
PubMed=1700979 [NCBI, ExPASy, EBI, Israel, Japan]
Erickson A.K.,
Payne D.M.,
Martino P.A.,
Rossomando A.J.,
Shabanowitz J.,
Weber M.J.,
Hunt D.F.,
Sturgill T.W.;
"Identification by mass spectrometry of threonine 97 in bovine myelin basic protein as a specific phosphorylation site for mitogen-activated protein kinase.";
J. Biol. Chem. 265:19728-19735(1990).
|
[11]
|
POST-TRANSLATIONAL MODIFICATIONS.
DOI=10.1021/bi972347t; PubMed=9485392 [NCBI, ExPASy, EBI, Israel, Japan]
Zand R.,
Li M.X.,
Jin X.,
Lubman D.;
"Determination of the sites of posttranslational modifications in the charge isomers of bovine myelin basic protein by capillary electrophoresis-mass spectroscopy.";
Biochemistry 37:2441-2449(1998).
|
[12]
|
DIMERIZATION.
DOI=10.1021/bi00550a015; PubMed=6155143 [NCBI, ExPASy, EBI, Israel, Japan]
Smith R.;
"Sedimentation analysis of the self-association of bovine myelin basic protein.";
Biochemistry 19:1826-1831(1980).
|
|
- FUNCTION: 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).
- SUBUNIT: Homodimer; self-associates in the presence of lysolipid.
- INTERACTION:
O64682:At2g34650 (xeno); NbExp=1; IntAct=EBI-908215, EBI-1393382;
P28482:MAPK1 (xeno); NbExp=1; IntAct=EBI-908215, EBI-959949;
- SUBCELLULAR LOCATION: Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic side of myelin.
- TISSUE SPECIFICITY: Found in both the central and the peripheral nervous system.
- PTM: At least 6 charge isomers; C1 (the most cationic and least modified form), C2, C3, C4, C5 and C6 (the least cationic form); are produced as a result of optional post-translatonial modifications, such as phosphorylation of serine or threonine residues, deamidation of glutamine or asparagine residues, citrullination and methylation of arginine residues.
- SIMILARITY: Belongs to the myelin basic protein family.
|
ExPASy Home page
SIB Switzerland
