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P02686

- MBP_HUMAN

UniProt

P02686 - MBP_HUMAN

Protein

Myelin basic protein

Gene

MBP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 173 (01 Oct 2014)
      Sequence version 3 (18 Oct 2001)
      Previous versions | rss
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    Functioni

    The classic group of MBP isoforms (isoform 4-isoform 14) are with PLP the most abundant protein components of the myelin membrane in the CNS. They have a role in both its formation and stabilization. The smaller isoforms might have an important role in remyelination of denuded axons in multiple sclerosis. The non-classic group of MBP isoforms (isoform 1-isoform 3/Golli-MBPs) may preferentially have a role in the early developing brain long before myelination, maybe as components of transcriptional complexes, and may also be involved in signaling pathways in T-cells and neural cells. Differential splicing events combined with optional post-translational modifications give a wide spectrum of isomers, with each of them potentially having a specialized function. Induces T-cell proliferation.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. structural constituent of myelin sheath Source: Ensembl

    GO - Biological processi

    1. axon ensheathment Source: ProtInc
    2. central nervous system development Source: ProtInc
    3. immune response Source: ProtInc
    4. membrane organization Source: Ensembl
    5. myelination Source: Ensembl
    6. negative regulation of axonogenesis Source: Ensembl
    7. response to toxic substance Source: Ensembl
    8. substantia nigra development Source: UniProt
    9. synaptic transmission Source: ProtInc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myelin basic protein
    Short name:
    MBP
    Alternative name(s):
    Myelin A1 protein
    Myelin membrane encephalitogenic protein
    Gene namesi
    Name:MBP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:6925. MBP.

    Subcellular locationi

    Isoform 3 : Nucleus 1 Publication
    Note: Targeted to nucleus in oligodendrocytes.

    GO - Cellular componenti

    1. compact myelin Source: Ensembl
    2. internode region of axon Source: Ensembl
    3. neuronal cell body Source: Ensembl
    4. nucleus Source: UniProtKB-SubCell
    5. plasma membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell membrane, Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    The reduction in the surface charge of citrullinated and/or methylated MBP could result in a weakened attachment to the myelin membrane. This mechanism could be operative in demyelinating diseases such as chronical multiple sclerosis (MS), and fulminating MS (Marburg disease).

    Keywords - Diseasei

    Autoimmune encephalomyelitis

    Organism-specific databases

    PharmGKBiPA30667.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 304304Myelin basic proteinPRO_0000158990Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei141 – 1411PhosphoserineBy similarity
    Modified residuei159 – 1591Citrulline; in form C81 Publication
    Modified residuei165 – 1651Citrulline; in form C81 Publication
    Modified residuei167 – 1671Citrulline1 Publication
    Modified residuei169 – 1691PhosphothreonineBy similarity
    Modified residuei174 – 1741PhosphoserineBy similarity
    Modified residuei190 – 1901PhosphoserineBy similarity
    Modified residuei199 – 1991Citrulline1 Publication
    Modified residuei203 – 2031PhosphotyrosineBy similarity
    Modified residuei229 – 2291PhosphothreonineBy similarity
    Modified residuei231 – 2311Citrulline1 Publication
    Modified residuei232 – 2321PhosphothreonineBy similarity
    Modified residuei237 – 2371Deamidated glutamineBy similarity
    Modified residuei241 – 2411Omega-N-methylarginine; alternate1 Publication
    Modified residuei241 – 2411Symmetric dimethylarginine; alternate1 Publication
    Modified residuei249 – 2491PhosphoserineBy similarity
    Modified residuei256 – 2561Citrulline; in form C81 Publication
    Modified residuei264 – 2641Citrulline; in form C82 Publications
    Modified residuei281 – 2811Deamidated glutamineBy similarity
    Modified residuei293 – 2931Citrulline; in form C81 Publication
    Modified residuei295 – 2951PhosphoserineBy similarity
    Modified residuei296 – 2961Citrulline1 Publication
    Modified residuei299 – 2991Phosphoserine; by UHMK11 Publication
    Modified residuei303 – 3031Citrulline1 Publication
    Modified residuei304 – 3041Citrulline; in form C81 Publication

    Post-translational modificationi

    Several charge isomers of MBP; C1 (the most cationic, least modified, and most abundant form), C2, C3, C4, C5, C6, C7, C8-A and C8-B (the least cationic form); are produced as a result of optional PTM, such as phosphorylation, deamidation of glutamine or asparagine, arginine citrullination and methylation. C8-A and C8-B contain each two mass isoforms termed C8-A(H), C8-A(L), C8-B(H) and C8-B(L), (H) standing for higher and (L) for lower molecular weight. C3, C4 and C5 are phosphorylated. The ratio of methylated arginine residues decreases during aging, making the protein more cationic.3 Publications
    The N-terminal alanine is acetylated (isoform 3, isoform 4, isoform 5 and isoform 6).
    Arg-241 was found to be 6% monomethylated and 60% symmetrically dimethylated.
    Phosphorylated by TAOK2, VRK2, MAPK11, MAPK12, MAPK14 and MINK1.

    Keywords - PTMi

    Acetylation, Citrullination, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP02686.
    PaxDbiP02686.
    PRIDEiP02686.

    PTM databases

    PhosphoSiteiP02686.

    Miscellaneous databases

    PMAP-CutDBA8MYL4.

    Expressioni

    Tissue specificityi

    MBP isoforms are found in both the central and the peripheral nervous system, whereas Golli-MBP isoforms are expressed in fetal thymus, spleen and spinal cord, as well as in cell lines derived from the immune system.1 Publication

    Developmental stagei

    Expression begins abruptly in 14-16 week old fetuses. Even smaller isoforms seem to be produced during embryogenesis; some of these persisting in the adult. Isoform 4 expression is more evident at 16 weeks and its relative proportion declines thereafter.

    Gene expression databases

    ArrayExpressiP02686.
    BgeeiP02686.
    CleanExiHS_MBP.
    GenevestigatoriP02686.

    Organism-specific databases

    HPAiCAB002300.
    HPA049222.

    Interactioni

    Subunit structurei

    Homodimer. Isoform 3 exists as a homodimer.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    nek-3Q8I6292EBI-7056012,EBI-7056031From a different organism.
    Plk4Q647022EBI-7056012,EBI-2552433From a different organism.

    Protein-protein interaction databases

    BioGridi110325. 74 interactions.
    DIPiDIP-36624N.
    IntActiP02686. 13 interactions.
    MINTiMINT-5005920.

    Structurei

    Secondary structure

    1
    304
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi146 – 1549
    Beta strandi160 – 1623
    Beta strandi173 – 1797
    Beta strandi241 – 2488
    Beta strandi284 – 2896

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BX2X-ray2.60C/F217-231[»]
    1FV1X-ray1.90C/F218-237[»]
    1HQRX-ray3.20C221-233[»]
    1K2DX-ray2.20P135-144[»]
    1QCLmodel-A135-304[»]
    1YMMX-ray3.50C217-240[»]
    1ZGLX-ray2.80C/F/I/L221-233[»]
    DisProtiDP00236.
    ProteinModelPortaliP02686.
    SMRiP02686. Positions 211-244.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02686.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni179 – 22244Induces experimental autoimmune encephalomyelitis (EAE) 1Add
    BLAST
    Regioni246 – 25611Induces experimental autoimmune encephalomyelitis (EAE) 2Add
    BLAST

    Sequence similaritiesi

    Belongs to the myelin basic protein family.Curated

    Phylogenomic databases

    eggNOGiNOG75180.
    HOVERGENiHBG008347.
    InParanoidiP02686.
    KOiK17269.
    OMAiFALEASY.
    OrthoDBiEOG7M0NRZ.
    PhylomeDBiP02686.
    TreeFamiTF333391.

    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]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: P02686-1) [UniParc]FASTAAdd to Basket

    Also known as: Golli-MBP1, HOG7

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGNHAGKREL NAEKASTNSE TNRGESEKKR NLGELSRTTS EDNEVFGEAD    50
    ANQNNGTSSQ DTAVTDSKRT ADPKNAWQDA HPADPGSRPH LIRLFSRDAP 100
    GREDNTFKDR PSESDELQTI QEDSAATSES LDVMASQKRP SQRHGSKYLA 150
    TASTMDHARH GFLPRHRDTG ILDSIGRFFG GDRGAPKRGS GKDSHHPART 200
    AHYGSLPQKS HGRTQDENPV VHFFKNIVTP RTPPPSQGKG RGLSLSRFSW 250
    GAEGQRPGFG YGGRASDYKS AHKGFKGVDA QGTLSKIFKL GGRDSRSGSP 300
    MARR 304
    Length:304
    Mass (Da):33,117
    Last modified:October 18, 2001 - v3
    Checksum:i4AD7305C1D5434C4
    GO
    Isoform 2 (identifier: P02686-2) [UniParc]FASTAAdd to Basket

    Also known as: Golli-MBP2, HOG5

    The sequence of this isoform differs from the canonical sequence as follows:
         193-304: DSHHPARTAH...SRSGSPMARR → VSSEE

    Show »
    Length:197
    Mass (Da):21,522
    Checksum:i0B2F47BA214706F2
    GO
    Isoform 3 (identifier: P02686-3) [UniParc]FASTAAdd to Basket

    Also known as: MBP1, 21.5 kDa

    The sequence of this isoform differs from the canonical sequence as follows:
         1-133: Missing.
         192-192: K → KVPWLKPGRSPLPSHARSQPGLCNMYK

    Note: Initiator Met-1 is removed. Contains a N-acetylalanine at position 2. Contains a non-traditional PY nuclear localization signal. Mutagenesis of Cys-81 to Ser prevents dimerization.

    Show »
    Length:197
    Mass (Da):21,493
    Checksum:i230FD99ECEC75FC5
    GO
    Isoform 4 (identifier: P02686-4) [UniParc]FASTAAdd to Basket

    Also known as: MBP2, 20.2 kDa

    The sequence of this isoform differs from the canonical sequence as follows:
         1-133: Missing.
         192-192: K → KVPWLKPGRSPLPSHARSQPGLCNMYK
         240-250: Missing.

    Note: Initiator Met-1 is removed. Contains a N-acetylalanine at position 2.

    Show »
    Length:186
    Mass (Da):20,246
    Checksum:i6CCF96DD90FE1CEB
    GO
    Isoform 5 (identifier: P02686-5) [UniParc]FASTAAdd to Basket

    Also known as: MBP3, 18.5 kDa

    The sequence of this isoform differs from the canonical sequence as follows:
         1-133: Missing.

    Note: Initiator Met-1 is removed. Contains a N-acetylalanine at position 2.

    Show »
    Length:171
    Mass (Da):18,591
    Checksum:i8E73B56787611054
    GO
    Isoform 6 (identifier: P02686-6) [UniParc]FASTAAdd to Basket

    Also known as: MBP4, 17.2 kDa

    The sequence of this isoform differs from the canonical sequence as follows:
         1-133: Missing.
         240-250: Missing.

    Note: Initiator Met-1 is removed. Contains a N-acetylalanine at position 2.

    Show »
    Length:160
    Mass (Da):17,343
    Checksum:i0107AAD603FCD876
    GO

    Sequence cautioni

    The sequence AAC41944.1 differs from that shown. Reason: Contaminating sequence. The C-terminus contains a Histidine tag.
    The sequence CAH10359.1 differs from that shown. Reason: wrong intron-exon boundaries.
    The sequence BAD92223.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti300 – 3001P → T in CAG38771. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 133133Missing in isoform 3, isoform 4, isoform 5 and isoform 6. 7 PublicationsVSP_003308Add
    BLAST
    Alternative sequencei192 – 1921K → KVPWLKPGRSPLPSHARSQP GLCNMYK in isoform 3 and isoform 4. 2 PublicationsVSP_003309
    Alternative sequencei193 – 304112DSHHP…PMARR → VSSEE in isoform 2. 2 PublicationsVSP_003311Add
    BLAST
    Alternative sequencei240 – 25011Missing in isoform 4 and isoform 6. 4 PublicationsVSP_003310Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M30047 mRNA. Translation: AAA59559.1.
    M20009 mRNA. Translation: AAA59561.1.
    M13577 mRNA. Translation: AAA59562.1.
    M30516 mRNA. Translation: AAA59563.1.
    M30515 mRNA. Translation: AAA59564.1.
    X17286
    , X17287, X17290, X17288, X17369, X17289 Genomic DNA. Translation: CAA35179.1.
    L18862 Genomic DNA. Translation: AAA72008.1.
    L18864 Genomic DNA. Translation: AAA72009.1.
    L18865 Genomic DNA. Translation: AAA72010.1.
    L18866 Genomic DNA. Translation: AAA72011.1.
    L41657 Genomic DNA. Translation: AAC41944.1. Sequence problems.
    CR536534 mRNA. Translation: CAG38771.1.
    CR541919 mRNA. Translation: CAG46717.1.
    CR627018 mRNA. Translation: CAH10359.1. Sequence problems.
    AK128770 mRNA. Translation: BAG54728.1.
    AK128788 mRNA. Translation: BAG54734.1.
    AB208986 mRNA. Translation: BAD92223.1. Different initiation.
    AC018529 Genomic DNA. No translation available.
    AC093330 Genomic DNA. No translation available.
    BC008749 mRNA. Translation: AAH08749.3.
    BC065248 mRNA. Translation: AAH65248.1.
    BC080654 mRNA. Translation: AAH80654.1.
    BC101771 mRNA. Translation: AAI01772.1.
    BC101773 mRNA. Translation: AAI01774.1.
    BC143348 mRNA. Translation: AAI43349.1.
    BC143350 mRNA. Translation: AAI43351.1.
    M63599 Genomic DNA. Translation: AAA59560.1.
    CCDSiCCDS12011.1. [P02686-4]
    CCDS32847.1. [P02686-3]
    CCDS42448.1. [P02686-6]
    CCDS42449.1. [P02686-5]
    CCDS42450.1. [P02686-2]
    PIRiA49635.
    S10482. MBHUB.
    RefSeqiNP_001020252.1. NM_001025081.1. [P02686-3]
    NP_001020261.1. NM_001025090.1. [P02686-5]
    NP_001020263.1. NM_001025092.1. [P02686-6]
    NP_001020271.1. NM_001025100.1. [P02686-2]
    NP_001020272.1. NM_001025101.1. [P02686-1]
    NP_002376.1. NM_002385.2. [P02686-4]
    UniGeneiHs.551713.

    Genome annotation databases

    EnsembliENST00000355994; ENSP00000348273; ENSG00000197971. [P02686-1]
    ENST00000359645; ENSP00000352667; ENSG00000197971. [P02686-4]
    ENST00000382582; ENSP00000372025; ENSG00000197971. [P02686-3]
    ENST00000397860; ENSP00000380958; ENSG00000197971. [P02686-2]
    ENST00000397863; ENSP00000380961; ENSG00000197971. [P02686-2]
    ENST00000397865; ENSP00000380963; ENSG00000197971. [P02686-6]
    ENST00000397866; ENSP00000380964; ENSG00000197971. [P02686-5]
    ENST00000580402; ENSP00000462223; ENSG00000197971. [P02686-1]
    GeneIDi4155.
    KEGGihsa:4155.
    UCSCiuc002lml.3. human. [P02686-3]
    uc002lmn.3. human. [P02686-4]
    uc002lmp.3. human. [P02686-6]
    uc002lmr.3. human. [P02686-2]
    uc010xfd.2. human. [P02686-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Myelin basic protein entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M30047 mRNA. Translation: AAA59559.1 .
    M20009 mRNA. Translation: AAA59561.1 .
    M13577 mRNA. Translation: AAA59562.1 .
    M30516 mRNA. Translation: AAA59563.1 .
    M30515 mRNA. Translation: AAA59564.1 .
    X17286
    , X17287 , X17290 , X17288 , X17369 , X17289 Genomic DNA. Translation: CAA35179.1 .
    L18862 Genomic DNA. Translation: AAA72008.1 .
    L18864 Genomic DNA. Translation: AAA72009.1 .
    L18865 Genomic DNA. Translation: AAA72010.1 .
    L18866 Genomic DNA. Translation: AAA72011.1 .
    L41657 Genomic DNA. Translation: AAC41944.1 . Sequence problems.
    CR536534 mRNA. Translation: CAG38771.1 .
    CR541919 mRNA. Translation: CAG46717.1 .
    CR627018 mRNA. Translation: CAH10359.1 . Sequence problems.
    AK128770 mRNA. Translation: BAG54728.1 .
    AK128788 mRNA. Translation: BAG54734.1 .
    AB208986 mRNA. Translation: BAD92223.1 . Different initiation.
    AC018529 Genomic DNA. No translation available.
    AC093330 Genomic DNA. No translation available.
    BC008749 mRNA. Translation: AAH08749.3 .
    BC065248 mRNA. Translation: AAH65248.1 .
    BC080654 mRNA. Translation: AAH80654.1 .
    BC101771 mRNA. Translation: AAI01772.1 .
    BC101773 mRNA. Translation: AAI01774.1 .
    BC143348 mRNA. Translation: AAI43349.1 .
    BC143350 mRNA. Translation: AAI43351.1 .
    M63599 Genomic DNA. Translation: AAA59560.1 .
    CCDSi CCDS12011.1. [P02686-4 ]
    CCDS32847.1. [P02686-3 ]
    CCDS42448.1. [P02686-6 ]
    CCDS42449.1. [P02686-5 ]
    CCDS42450.1. [P02686-2 ]
    PIRi A49635.
    S10482. MBHUB.
    RefSeqi NP_001020252.1. NM_001025081.1. [P02686-3 ]
    NP_001020261.1. NM_001025090.1. [P02686-5 ]
    NP_001020263.1. NM_001025092.1. [P02686-6 ]
    NP_001020271.1. NM_001025100.1. [P02686-2 ]
    NP_001020272.1. NM_001025101.1. [P02686-1 ]
    NP_002376.1. NM_002385.2. [P02686-4 ]
    UniGenei Hs.551713.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BX2 X-ray 2.60 C/F 217-231 [» ]
    1FV1 X-ray 1.90 C/F 218-237 [» ]
    1HQR X-ray 3.20 C 221-233 [» ]
    1K2D X-ray 2.20 P 135-144 [» ]
    1QCL model - A 135-304 [» ]
    1YMM X-ray 3.50 C 217-240 [» ]
    1ZGL X-ray 2.80 C/F/I/L 221-233 [» ]
    DisProti DP00236.
    ProteinModelPortali P02686.
    SMRi P02686. Positions 211-244.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110325. 74 interactions.
    DIPi DIP-36624N.
    IntActi P02686. 13 interactions.
    MINTi MINT-5005920.

    PTM databases

    PhosphoSitei P02686.

    Proteomic databases

    MaxQBi P02686.
    PaxDbi P02686.
    PRIDEi P02686.

    Protocols and materials databases

    DNASUi 4155.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355994 ; ENSP00000348273 ; ENSG00000197971 . [P02686-1 ]
    ENST00000359645 ; ENSP00000352667 ; ENSG00000197971 . [P02686-4 ]
    ENST00000382582 ; ENSP00000372025 ; ENSG00000197971 . [P02686-3 ]
    ENST00000397860 ; ENSP00000380958 ; ENSG00000197971 . [P02686-2 ]
    ENST00000397863 ; ENSP00000380961 ; ENSG00000197971 . [P02686-2 ]
    ENST00000397865 ; ENSP00000380963 ; ENSG00000197971 . [P02686-6 ]
    ENST00000397866 ; ENSP00000380964 ; ENSG00000197971 . [P02686-5 ]
    ENST00000580402 ; ENSP00000462223 ; ENSG00000197971 . [P02686-1 ]
    GeneIDi 4155.
    KEGGi hsa:4155.
    UCSCi uc002lml.3. human. [P02686-3 ]
    uc002lmn.3. human. [P02686-4 ]
    uc002lmp.3. human. [P02686-6 ]
    uc002lmr.3. human. [P02686-2 ]
    uc010xfd.2. human. [P02686-1 ]

    Organism-specific databases

    CTDi 4155.
    GeneCardsi GC18M074690.
    HGNCi HGNC:6925. MBP.
    HPAi CAB002300.
    HPA049222.
    MIMi 159430. gene.
    neXtProti NX_P02686.
    PharmGKBi PA30667.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG75180.
    HOVERGENi HBG008347.
    InParanoidi P02686.
    KOi K17269.
    OMAi FALEASY.
    OrthoDBi EOG7M0NRZ.
    PhylomeDBi P02686.
    TreeFami TF333391.

    Miscellaneous databases

    ChiTaRSi MBP. human.
    EvolutionaryTracei P02686.
    GeneWikii Myelin_basic_protein.
    GenomeRNAii 4155.
    NextBioi 16362.
    PMAP-CutDB A8MYL4.
    PROi P02686.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02686.
    Bgeei P02686.
    CleanExi HS_MBP.
    Genevestigatori P02686.

    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. "Amino acid sequence of the encephalitogenic basic protein from human myelin."
      Carnegie P.R.
      Biochem. J. 123:57-67(1971) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE (ISOFORM 5).
    2. "Isolation and characterization of a cDNA coding for a novel human 17.3K myelin basic protein (MBP) variant."
      Roth H.J., Kronquist K.E., Pretorius P.J., Crandall B.F., Campagnoni A.T.
      J. Neurosci. Res. 16:227-238(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
      Tissue: Embryonic spinal cord.
    3. "Identification of three forms of human myelin basic protein by cDNA cloning."
      Kamholz J., de Ferra F., Puckett C., Lazzarini R.A.
      Proc. Natl. Acad. Sci. U.S.A. 83:4962-4966(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 5).
    4. "Evidence for the expression of four myelin basic protein variants in the developing human spinal cord through cDNA cloning."
      Roth H.J., Kronquist K.E., de Rosbo N., Crandall B.F., Campagnoni A.T.
      J. Neurosci. Res. 17:321-328(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5 AND 6).
      Tissue: Embryonic spinal cord.
    5. "The organization of the human myelin basic protein gene. Comparison with the mouse gene."
      Streicher R., Stoffel W.
      Biol. Chem. Hoppe-Seyler 370:503-510(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 3; 4; 5 AND 6).
    6. "The human myelin basic protein gene is included within a 179-kilobase transcription unit: expression in the immune and central nervous systems."
      Pribyl T.M., Campagnoni C.W., Kampf K., Kashima T., Handley V.W., McMahon J., Campagnoni A.T.
      Proc. Natl. Acad. Sci. U.S.A. 90:10695-10699(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
      Tissue: Brain.
    7. "Purification of immunologically active recombinant 21.5 kDa isoform of human myelin basic protein."
      Nye S.H., Pelfrey C.M., Burkwit J.J., Voskuhl R.R., Lenardo M.J., Mueller J.P.
      Mol. Immunol. 32:1131-1141(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3), FUNCTION, DIMERIZATION, MUTAGENESIS.
    8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Amygdala.
    10. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
      Tissue: Hippocampus and Subthalamic nucleus.
    11. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    13. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 5 AND 6).
      Tissue: Brain, Lung and Skin.
    14. "Repetitive DNA (TGGA)n 5' to the human myelin basic protein gene: a new form of oligonucleotide repetitive sequence showing length polymorphism."
      Boylan K.B., Ayres T.M., Popko B., Takahashi N., Hood L.E., Prusiner S.B.
      Genomics 6:16-22(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 135-192.
    15. "Analysis of the primary sequence of human myelin basic protein peptides 1-44 and 90-170 by fast atom bombardment mass spectrometry."
      Scoble H.A., Whitaker J.N., Biemann K.
      J. Neurochem. 47:614-616(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 135-178 AND 224-304 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY.
    16. "The isolation, characterization, and lipid-aggregating properties of a citrulline containing myelin basic protein."
      Wood D.D., Moscarello M.A.
      J. Biol. Chem. 264:5121-5127(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 148-304 (ISOFORM 5), CITRULLINATION AT ARG-159; ARG-165; ARG-256; ARG-264; ARG-293 AND ARG-304.
      Tissue: Brain.
    17. "The isolation and characterization of four myelin basic proteins from the unbound fraction during CM52 chromatography."
      Boulias C., Pang H., Mastronardi F., Moscarello M.A.
      Arch. Biochem. Biophys. 322:174-182(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 156-172 AND 302-304, CHARACTERIZATION OF C8.
      Tissue: Brain.
    18. "Amino acid sequence of human myelin basic protein peptide 45-89 as determined by mass spectrometry."
      Gibson B.W., Gilliom R.D., Whitaker J.N., Biemann K.
      J. Biol. Chem. 259:5028-5031(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 179-223 (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY.
    19. "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., Kibler R.F.
      J. Biol. Chem. 246:4630-4640(1971)
      Cited for: PROTEIN SEQUENCE OF 179-222 (ISOFORM 5), SEQUENCE REVISION.
    20. "Immunologic properties of the main encephalitogenic peptide from the basic protein of human myelin."
      Lennon V.A., Wilks A.V., Carnegie P.R.
      J. Immunol. 105:1223-1230(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 246-269 (ISOFORM 3), ENCEPHALITOGENIC PEPTIDE.
    21. "Leukocyte gelatinase B cleavage releases encephalitogens from human myelin basic protein."
      Proost P., Van Damme J., Opdenakker G.
      Biochem. Biophys. Res. Commun. 192:1175-1181(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
      Tissue: Brain.
    22. "Isolation and partial characterization of methylated arginines from the encephalitogenic basic protein of myelin."
      Baldwin G.S., Carnegie P.R.
      Biochem. J. 123:69-74(1971) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT ARG-241.
    23. "Selective activation of p38 mitogen-activated protein (MAP) kinase isoforms by the MAP kinase kinases MKK3 and MKK6."
      Enslen H., Raingeaud J., Davis R.J.
      J. Biol. Chem. 273:1741-1748(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY MAPK11; MAPK12 AND MAPK14.
    24. "Specific Ser-Pro phosphorylation by the RNA-recognition motif containing kinase KIS."
      Maucuer A., Le Caer J.P., Manceau V., Sobel A.
      Eur. J. Biochem. 267:4456-4464(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-299 BY UMHK1.
    25. "PSK, a novel STE20-like kinase derived from prostatic carcinoma that activates the JNK MAPK pathway and regulates actin cytoskeletal organisation."
      Moore T.M., Garg R., Johnson C., Coptcoat M.J., Ridley A.J., Morris J.D.H.
      J. Biol. Chem. 275:4311-4322(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY TAOK2.
    26. "Involvement of MINK, a Ste20 family kinase, in Ras oncogene-induced growth arrest in human ovarian surface epithelial cells."
      Nicke B., Bastien J., Khanna S.J., Warne P.H., Cowling V., Cook S.J., Peters G., Delpuech O., Schulze A., Berns K., Mullenders J., Beijersbergen R.L., Bernards R., Ganesan T.S., Downward J., Hancock D.C.
      Mol. Cell 20:673-685(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY MINK1.
    27. "The subcellular localization of vaccinia-related kinase-2 (VRK2) isoforms determines their different effect on p53 stability in tumour cell lines."
      Blanco S., Klimcakova L., Vega F.M., Lazo P.A.
      FEBS J. 273:2487-2504(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY VRK2.
    28. "Prostate-derived sterile 20-like kinase 1-alpha induces apoptosis. JNK-and caspase-dependent nuclear localization is a requirement for membrane blebbing."
      Zihni C., Mitsopoulos C., Tavares I.A., Baum B., Ridley A.J., Morris J.D.
      J. Biol. Chem. 282:6484-6493(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY TAOK2.
    29. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    30. "The 21.5-kDa isoform of myelin basic protein has a non-traditional PY-nuclear-localization signal."
      Smith G.S., Seymour L.V., Boggs J.M., Harauz G.
      Biochem. Biophys. Res. Commun. 422:670-675(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION (ISOFORM 3).
    31. "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-167; ARG-199; ARG-231; ARG-264; ARG-296 AND ARG-303.
    32. "Conformation of a tetradecapeptide epitope of myelin basic protein."
      Mendz G.L., Barden J.A., Martenson R.E.
      Eur. J. Biochem. 231:659-666(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 135-148, CLEAVAGE OF INITIATOR METHIONINE (ISOFORMS 3; 4; 5 AND 6), ACETYLATION AT ALA-2 (ISOFORMS 3; 4; 5 AND 6).
    33. "Three-dimensional structure of myelin basic protein. II. Molecular modeling and considerations of predicted structures in multiple sclerosis."
      Ridsdale R.A., Beniac D.R., Tompkins T.A., Moscarello M.A., Harauz G.
      J. Biol. Chem. 272:4269-4275(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF 135-279 (ISOFORM 5).
    34. "Structural basis for the binding of an immunodominant peptide from myelin basic protein in different registers by two HLA-DR2 proteins."
      Li Y., Li H., Martin R., Mariuzza R.A.
      J. Mol. Biol. 304:177-188(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 218-237 IN COMPLEX WITH HLA-DRA/HLA-DRB5 HETERODIMER.
    35. "Crystal structure of a superantigen bound to the high-affinity, zinc-dependent site on MHC class II."
      Li Y., Li H., Dimasi N., McCormick J.K., Martin R., Schuck P., Schlievert P.M., Mariuzza R.A.
      Immunity 14:93-104(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 221-233 IN COMPLEX WITH HLA-DRA/HLA-DRB5 HETERODIMER AND STREPTOCOCCUS PYOGENES SPEC PEPTIDE.
    36. "Structure of a human autoimmune TCR bound to a myelin basic protein self-peptide and a multiple sclerosis-associated MHC class II molecule."
      Li Y., Huang Y., Lue J., Quandt J.A., Martin R., Mariuzza R.A.
      EMBO J. 24:2968-2979(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 221-233 IN COMPLEX WITH HLA-DRA/HLA-DRB5 HETERODIMER AND TRAC.

    Entry informationi

    Entry nameiMBP_HUMAN
    AccessioniPrimary (citable) accession number: P02686
    Secondary accession number(s): A4FU54
    , A6NI84, A8MY86, A8MYL4, B3KY66, B7ZKS2, B7ZKS4, Q15337, Q15338, Q15339, Q15340, Q59GX3, Q65ZS4, Q6AI64, Q6FH37, Q6FI04, Q6PK23
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: October 18, 2001
    Last modified: October 1, 2014
    This is version 173 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3