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Protein

Myelin basic protein

Gene

MBP

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Myelin basic protein
Short name:
MBP
Alternative name(s):
20 kDa microtubule-stabilizing protein
Myelin A1 protein
Gene namesi
Name:MBP
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Keywords - Diseasei

Autoimmune encephalomyelitis

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 169169Myelin basic proteinPRO_0000158987Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylalanine1 Publication
Modified residuei7 – 71Phosphoserine; in C5 and C61 Publication
Modified residuei23 – 231Citrulline; in form C8b1 Publication
Modified residuei29 – 291CitrullineBy similarity
Modified residuei33 – 331PhosphothreonineBy similarity
Modified residuei38 – 381PhosphoserineBy similarity
Modified residuei41 – 411Citrulline1 Publication
Modified residuei47 – 471Citrulline; in form C8b1 Publication
Modified residuei54 – 541Phosphoserine; in C4, C5 and C61 Publication
Modified residuei63 – 631Citrulline1 Publication
Modified residuei67 – 671PhosphotyrosineBy similarity
Modified residuei94 – 941PhosphothreonineBy similarity
Modified residuei96 – 961Citrulline; in form C2, C3, C8a and C8b2 Publications
Modified residuei97 – 971Phosphothreonine; by MAPK; in C3, C4, C5 and C63 Publications
Modified residuei102 – 1021Deamidated glutamine; in form C51 Publication
Modified residuei106 – 1061Citrulline; alternate1 Publication
Modified residuei106 – 1061Omega-N-methylarginine; alternate3 Publications
Modified residuei106 – 1061Symmetric dimethylarginine; alternate3 Publications
Modified residuei112 – 1121Citrulline1 Publication
Modified residuei114 – 1141PhosphoserineBy similarity
Modified residuei120 – 1201Deamidated glutamine; in form C31 Publication
Modified residuei121 – 1211N6-acetyllysine1 Publication
Modified residuei129 – 1291Citrulline1 Publication
Modified residuei146 – 1461Deamidated glutamine; in form C21 Publication
Modified residuei158 – 1581CitrullineBy similarity
Modified residuei160 – 1601Phosphoserine; in C4 and C61 Publication
Modified residuei161 – 1611Citrulline; in form C32 Publications
Modified residuei164 – 1641Phosphoserine; in form C3, C5 and C61 Publication
Modified residuei168 – 1681Citrulline1 Publication
Modified residuei169 – 1691Citrulline1 Publication

Post-translational modificationi

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.4 Publications
Phosphorylated by TAOK2, VRK2, MAPK11, MAPK12, MAPK14 and MINK1.By similarity

Keywords - PTMi

Acetylation, Citrullination, Methylation, Phosphoprotein

Proteomic databases

PRIDEiP02687.

Miscellaneous databases

PMAP-CutDBP02687.

Expressioni

Tissue specificityi

Found in both the central and the peripheral nervous system.

Interactioni

Subunit structurei

Homodimer; self-associates in the presence of lysolipid.

Binary interactionsi

WithEntry#Exp.IntActNotes
dclk2A2A1214EBI-908215,EBI-9006039From a different organism.
LRRK2Q5S0073EBI-908215,EBI-5323863From a different organism.
MAPK1P284822EBI-908215,EBI-959949From a different organism.

Protein-protein interaction databases

DIPiDIP-29967N.
IntActiP02687. 35 interactions.
STRINGi9913.ENSBTAP00000002984.

Structurei

3D structure databases

DisProtiDP00047.
ProteinModelPortaliP02687.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni43 – 8745Induces experimental autoimmune encephalomyelitis (EAE) 1Add
BLAST
Regioni114 – 1229Induces experimental autoimmune encephalomyelitis (EAE) 2

Sequence similaritiesi

Belongs to the myelin basic protein family.Curated

Phylogenomic databases

eggNOGiNOG75180.
HOGENOMiHOG000293395.
HOVERGENiHBG008347.
InParanoidiP02687.

Family and domain databases

InterProiIPR000548. Myelin_BP.
[Graphical view]
PANTHERiPTHR11429. PTHR11429. 1 hit.
PfamiPF01669. Myelin_MBP. 1 hit.
[Graphical view]
PRINTSiPR00212. MYELINMBP.
PROSITEiPS00569. MYELIN_MBP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P02687-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
AAQKRPSQRS KYLASASTMD HARHGFLPRH RDTGILDSLG RFFGSDRGAP
60 70 80 90 100
KRGSGKDGHH AARTTHYGSL PQKAQGHRPQ DENPVVHFFK NIVTPRTPPP
110 120 130 140 150
SQGKGRGLSL SRFSWGAEGQ KPGFGYGGRA SDYKSAHKGL KGHDAQGTLS
160
KIFKLGGRDS RSGSPMARR
Length:169
Mass (Da):18,323
Last modified:July 21, 1986 - v1
Checksum:i8E1157B7A1978484
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF226693 mRNA. Translation: AAK00645.1.
PIRiA92089. MBBOB.
UniGeneiBt.64741.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF226693 mRNA. Translation: AAK00645.1.
PIRiA92089. MBBOB.
UniGeneiBt.64741.

3D structure databases

DisProtiDP00047.
ProteinModelPortaliP02687.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29967N.
IntActiP02687. 35 interactions.
STRINGi9913.ENSBTAP00000002984.

Proteomic databases

PRIDEiP02687.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiNOG75180.
HOGENOMiHOG000293395.
HOVERGENiHBG008347.
InParanoidiP02687.

Miscellaneous databases

PMAP-CutDBP02687.

Family and domain databases

InterProiIPR000548. Myelin_BP.
[Graphical view]
PANTHERiPTHR11429. PTHR11429. 1 hit.
PfamiPF01669. Myelin_MBP. 1 hit.
[Graphical view]
PRINTSiPR00212. MYELINMBP.
PROSITEiPS00569. MYELIN_MBP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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: DEAMIDATION AT GLN-146, PHOSPHORYLATION AT SER-54; THR-97; SER-160 AND SER-164.
  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.

Entry informationi

Entry nameiMBP_BOVIN
AccessioniPrimary (citable) accession number: P02687
Secondary accession number(s): Q9BGM8, Q9TS63, Q9TSA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 24, 2015
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.