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P02687

- MBP_BOVIN

UniProt

P02687 - MBP_BOVIN

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Protein

Myelin basic protein

Gene

MBP

Organism
Bos taurus (Bovine)
Status
Reviewed - 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

  1. structural constituent of myelin sheath Source: InterPro
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: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB-KW
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 C6
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 C6
Modified residuei63 – 631Citrulline1 Publication
Modified residuei67 – 671PhosphotyrosineBy similarity
Modified residuei94 – 941PhosphothreonineBy similarity
Modified residuei96 – 961Citrulline2 Publications
Modified residuei96 – 961Citrulline; in form C2, C3, C8a and C8b2 Publications
Modified residuei97 – 971Phosphothreonine; by MAPK; in C3, C4, C5 and C62 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 C2
Modified residuei158 – 1581CitrullineBy similarity
Modified residuei160 – 1601Phosphoserine; in C4 and C6
Modified residuei161 – 1611Citrulline2 Publications
Modified residuei161 – 1611Citrulline; in form C32 Publications
Modified residuei164 – 1641Phosphoserine; by UHMK1
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.

Structurei

3D structure databases

DisProtiDP00047.
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 .
PIRi A92089. MBBOB.
UniGenei Bt.64741.

3D structure databases

DisProti DP00047.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29967N.
IntActi P02687. 35 interactions.

Proteomic databases

PRIDEi P02687.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG75180.
HOGENOMi HOG000293395.
HOVERGENi HBG008347.
InParanoidi P02687.

Miscellaneous databases

PMAP-CutDB P02687.

Family and domain databases

InterProi IPR000548. Myelin_BP.
[Graphical view ]
PANTHERi PTHR11429. PTHR11429. 1 hit.
Pfami PF01669. Myelin_MBP. 1 hit.
[Graphical view ]
PRINTSi PR00212. MYELINMBP.
PROSITEi PS00569. MYELIN_MBP. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: 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.

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: October 29, 2014
This is version 118 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