Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P02687

- MBP_BOVIN

UniProt

P02687 - MBP_BOVIN

Protein

Myelin basic protein

Gene

MBP

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. 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. protein binding Source: IntAct
    2. structural constituent of myelin sheath Source: InterPro

    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. myelin sheath Source: UniProtKB-SubCell
    2. plasma membrane Source: UniProtKB-KW

    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

    AAQKRPSQRS KYLASASTMD HARHGFLPRH RDTGILDSLG RFFGSDRGAP    50
    KRGSGKDGHH AARTTHYGSL PQKAQGHRPQ DENPVVHFFK NIVTPRTPPP 100
    SQGKGRGLSL SRFSWGAEGQ KPGFGYGGRA SDYKSAHKGL KGHDAQGTLS 150
    KIFKLGGRDS RSGSPMARR 169
    Length:169
    Mass (Da):18,323
    Last modified:July 21, 1986 - v1
    Checksum:i8E1157B7A1978484
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF226693 mRNA. Translation: AAK00645.1.
    PIRiA92089. MBBOB.
    UniGeneiBt.64741.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 1, 2014
    This is version 117 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