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P02687 (MBP_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myelin basic protein

Short name=MBP
Alternative name(s):
20 kDa microtubule-stabilizing protein
Myelin A1 protein
Gene names
Name:MBP
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length169 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 structure

Homodimer; self-associates in the presence of lysolipid. Ref.12

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.

Post-translational modification

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.

Phosphorylated by TAOK2, VRK2, MAPK11, MAPK12, MAPK14 and MINK1 By similarity. Ref.10 Ref.13

Sequence similarities

Belongs to the myelin basic protein family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

dclk2A2A1214EBI-908215,EBI-9006039From a different organism.
LRRK2Q5S0073EBI-908215,EBI-5323863From a different organism.
MAPK1P284822EBI-908215,EBI-959949From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 169169Myelin basic protein
PRO_0000158987

Regions

Region43 – 8745Induces experimental autoimmune encephalomyelitis (EAE) 1
Region114 – 1229Induces experimental autoimmune encephalomyelitis (EAE) 2

Amino acid modifications

Modified residue11N-acetylalanine Ref.13
Modified residue71Phosphoserine; in C5 and C6
Modified residue231Citrulline; in form C8b
Modified residue291Citrulline By similarity
Modified residue331Phosphothreonine By similarity
Modified residue381Phosphoserine By similarity
Modified residue411Citrulline
Modified residue471Citrulline; in form C8b
Modified residue541Phosphoserine; in C4, C5 and C6
Modified residue631Citrulline
Modified residue671Phosphotyrosine By similarity
Modified residue941Phosphothreonine By similarity
Modified residue961Citrulline
Modified residue961Citrulline; in form C2, C3, C8a and C8b
Modified residue971Phosphothreonine; by MAPK; in C3, C4, C5 and C6 Ref.10 Ref.13
Modified residue1021Deamidated glutamine; in form C5 Ref.13
Modified residue1061Citrulline; alternate
Modified residue1061Omega-N-methylarginine; alternate Ref.8 Ref.13 Ref.14
Modified residue1061Symmetric dimethylarginine; alternate Ref.8 Ref.13 Ref.14
Modified residue1121Citrulline
Modified residue1141Phosphoserine By similarity
Modified residue1201Deamidated glutamine; in form C3 Ref.13
Modified residue1211N6-acetyllysine Ref.13
Modified residue1291Citrulline
Modified residue1461Deamidated glutamine; in form C2
Modified residue1581Citrulline By similarity
Modified residue1601Phosphoserine; in C4 and C6
Modified residue1611Citrulline
Modified residue1611Citrulline; in form C3
Modified residue1641Phosphoserine; by UHMK1
Modified residue1681Citrulline
Modified residue1691Citrulline

Sequences

Sequence LengthMass (Da)Tools
P02687 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 8E1157B7A1978484

FASTA16918,323
        10         20         30         40         50         60 
AAQKRPSQRS KYLASASTMD HARHGFLPRH RDTGILDSLG RFFGSDRGAP KRGSGKDGHH 

        70         80         90        100        110        120 
AARTTHYGSL PQKAQGHRPQ DENPVVHFFK NIVTPRTPPP SQGKGRGLSL SRFSWGAEGQ 

       130        140        150        160 
KPGFGYGGRA SDYKSAHKGL KGHDAQGTLS KIFKLGGRDS RSGSPMARR 

« Hide

References

[1]"Basic A1 protein of the myelin membrane. The complete amino acid sequence."
Eylar E.H., Brostoff S.W., Hashim G., Caccam J., Burnett P.
J. Biol. Chem. 246:5770-5784(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[2]"Specific cleavage of the A1 protein from myelin with cathepsin D."
Brostoff S.W., Reuter W., Hichens M., Eylar E.H.
J. Biol. Chem. 249:559-567(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[3]"A new MBP allele in Bos taurus is characterized by BseNI PCR-RFLP."
Pietrowski D., Medugorac I., Foerster M.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-56.
[4]"Encephalitogenic fragment of myelin basic protein. Amino acid sequence of bovine, rabbit, guinea pig, monkey, and human fragments."
Shapira R., McKneally S.S., Chou F.C.-H., Kibler R.F.
J. Biol. Chem. 246:4630-4640(1971)
Cited for: PROTEIN SEQUENCE OF 43-87.
[5]"Ca(2+)-calmodulin regulated effectors of microtubule stability in bovine brain."
Pirollet F., Derancourt J., Haiech J., Job D., Margolis R.L.
Biochemistry 31:8849-8855(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 38-58 AND 119-141.
Tissue: Brain.
[6]"Purification of a new clathrin assembly protein from bovine brain coated vesicles and its identification as myelin basic protein."
Prasad K., Barouch W., Martin B.M., Greene L.E., Eisenberg E.
J. Biol. Chem. 270:30551-30556(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 30-42; 74-89 AND 114-129.
[7]"Experimental allergic encephalomyelitis: synthesis of disease-inducing site of the basic protein."
Eylar E.H., Caccam J., Jackson J.J., Westall F.C., Robinson A.B.
Science 168:1220-1223(1970) [PubMed] [Europe PMC] [Abstract]
Cited for: SYNTHESIS OF ALLERGIC ENCEPHALOMYELITIS INDUCING REGION.
[8]"Localization of methylated arginine in the A1 protein from myelin."
Brostoff S.W., Eylar E.H.
Proc. Natl. Acad. Sci. U.S.A. 68:765-769(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT ARG-106.
[9]"Basis of microheterogeneity of myelin basic protein."
Chou F.C.-H., Chou C.-H.J., Shapira R., Kibler R.F.
J. Biol. Chem. 251:2671-2679(1976) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[10]"Identification by mass spectrometry of threonine 97 in bovine myelin basic protein as a specific phosphorylation site for mitogen-activated protein kinase."
Erickson A.K., Payne D.M., Martino P.A., Rossomando A.J., Shabanowitz J., Weber M.J., Hunt D.F., Sturgill T.W.
J. Biol. Chem. 265:19728-19735(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 97-104, PHOSPHORYLATION AT THR-97.
[11]"Determination of the sites of posttranslational modifications in the charge isomers of bovine myelin basic protein by capillary electrophoresis-mass spectroscopy."
Zand R., Li M.X., Jin X., Lubman D.
Biochemistry 37:2441-2449(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: POST-TRANSLATIONAL MODIFICATIONS.
[12]"Sedimentation analysis of the self-association of bovine myelin basic protein."
Smith R.
Biochemistry 19:1826-1831(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: DIMERIZATION.
[13]"Myelin basic protein undergoes a broader range of modifications in mammals than in lower vertebrates."
Zhang C., Walker A.K., Zand R., Moscarello M.A., Yan J.M., Andrews P.C.
J. Proteome Res. 11:4791-4802(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT ALA-1 AND LYS-121, METHYLATION AT ARG-106, DEAMIDATION AT GLN-102 AND GLN-120, CITRULLINATION AT ARG-23; ARG-47; ARG-96 AND ARG-161, PHOSPHORYLATION AT THR-97.
[14]"Identification and Characterization of citrulline-modified brain proteins by combining HCD and CID fragmentation."
Jin Z., Fu Z., Yang J., Troncosco J., Everett A.D., Van Eyk J.E.
Proteomics 13:2682-2691(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: CITRULLINATION AT ARG-41; ARG-63; ARG-96; ARG-106; ARG-112; ARG-129; ARG-158; ARG-161; ARG-168 AND ARG-169, METHYLATION AT ARG-106.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF226693 mRNA. Translation: AAK00645.1.
PIRMBBOB. A92089.
UniGeneBt.64741.

3D structure databases

DisProtDP00047.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29967N.
IntActP02687. 35 interactions.

Proteomic databases

PRIDEP02687.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG75180.
HOGENOMHOG000293395.
HOVERGENHBG008347.
InParanoidP02687.

Family and domain databases

InterProIPR000548. Myelin_BP.
[Graphical view]
PANTHERPTHR11429. PTHR11429. 1 hit.
PfamPF01669. Myelin_MBP. 1 hit.
[Graphical view]
PRINTSPR00212. MYELINMBP.
PROSITEPS00569. MYELIN_MBP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PMAP-CutDBP02687.

Entry information

Entry nameMBP_BOVIN
AccessionPrimary (citable) accession number: P02687
Secondary accession number(s): Q9BGM8, Q9TS63, Q9TSA6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families