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UniProtKB/Swiss-Prot entry P04370


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MBP_MOUSE
Primary accession number P04370
Secondary accession numbers Q01585 Q03139 Q03176 Q61836 Q61837 Q99KE4 Q9QWP1
Integrated into Swiss-Prot on March 20, 1987
Sequence was last modified on October 18, 2001 (Sequence version 2)
Annotations were last modified on    June 10, 2008 (Entry version 98)
Name and origin of the protein
Protein name Myelin basic protein
Synonyms MBP
Myelin A1 protein
Gene name
Name: Mbp
Synonyms: Shi
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/S0092-8674(85)80109-4; PubMed=2410136 [NCBI, ExPASy, EBI, Israel, Japan]
Takahashi N., Roach A., Teplow D.B., Prusiner S.B., Hood L.E.;
"Cloning and characterization of the myelin basic protein gene from mouse: one gene can encode both 14 kd and 18.5 kd MBPs by alternate use of exons.";
Cell 42:139-148(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0092-8674(85)90245-4; PubMed=2416470 [NCBI, ExPASy, EBI, Israel, Japan]
de Ferra F., Engh H., Hudson L., Kamholz J., Puckett C., Molineaux S., Lazzarini R.A.;
"Alternative splicing accounts for the four forms of myelin basic protein.";
Cell 43:721-727(1985).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 7), AND NUCLEOTIDE SEQUENCE [MRNA] OF 9-194.
STRAIN=C57BL/6J;
TISSUE=Brain;
PubMed=2433693 [NCBI, ExPASy, EBI, Israel, Japan]
Newman S., Kitamura K., Campagnoni A.T.;
"Identification of a cDNA coding for a fifth form of myelin basic protein in mouse.";
Proc. Natl. Acad. Sci. U.S.A. 84:886-890(1987).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8).
PubMed=1692584 [NCBI, ExPASy, EBI, Israel, Japan]
Kitamura K., Newman S.L., Campagnoni C.W., Verdi J.M., Mohandas T., Handley V.W., Campagnoni A.T.;
"Expression of a novel transcript of the myelin basic protein gene.";
J. Neurochem. 54:2032-2041(1990).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=C57BL/6;
TISSUE=Bone marrow;
PubMed=1279125 [NCBI, ExPASy, EBI, Israel, Japan]
Grima B., Zelenika D., Pessac B.;
"A novel transcript overlapping the myelin basic protein gene.";
J. Neurochem. 59:2318-2323(1992).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3).
STRAIN=C57BL/6;
TISSUE=Brain;
PubMed=7680345 [NCBI, ExPASy, EBI, Israel, Japan]
Campagnoni A.T., Pribyl T.M., Campagnoni C.W., Kampf K., Amur-Umarjee S., Landry C.F., Handley V.W., Newman S., Garbay B., Kitamura K.;
"Structure and developmental regulation of Golli-mbp, a 105-kilobase gene that encompasses the myelin basic protein gene and is expressed in cells in the oligodendrocyte lineage in the brain.";
J. Biol. Chem. 268:4930-4938(1993).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
STRAIN=C57BL/6J;
TISSUE=Cerebellum;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
TISSUE=Mammary tumor;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 135-157.
DOI=10.1016/0378-1119(89)90380-6; PubMed=2470651 [NCBI, ExPASy, EBI, Israel, Japan]
Miura M., Tamura T.A., Aoyama A., Mikoshiba K.;
"The promoter elements of the mouse myelin basic protein gene function efficiently in NG108-15 neuronal/glial cells.";
Gene 75:31-38(1989).
[10]
PROTEIN SEQUENCE OF 146-157; 164-175; 196-205 AND 211-222, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-224.
PubMed=2452084 [NCBI, ExPASy, EBI, Israel, Japan]
Okano H., Tamura T., Miura M., Aoyama A., Ikenaka K., Oshimura M., Mikoshiba K.;
"Gene organization and transcription of duplicated MBP genes of myelin deficient (shi(mld)) mutant mouse.";
EMBO J. 7:77-83(1988).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 193-222.
PubMed=6198644 [NCBI, ExPASy, EBI, Israel, Japan]
Zeller N.K., Hunkeler M.J., Campagnoni A.T., Sprague J., Lazzarini R.A.;
"Characterization of mouse myelin basic protein messenger RNAs with a myelin basic protein cDNA clone.";
Proc. Natl. Acad. Sci. U.S.A. 81:18-22(1984).
[13]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 6 AND 9).
PubMed=2425357 [NCBI, ExPASy, EBI, Israel, Japan]
Kamholz J., de Ferra F., Puckett C., Lazzarini R.A.;
"Identification of three forms of human myelin basic protein by cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 83:4962-4966(1986).
[14]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 10 AND 11).
TISSUE=Spinal cord;
PubMed=1705957 [NCBI, ExPASy, EBI, Israel, Japan]
Aruga J., Okano H., Mikoshiba K.;
"Identification of the new isoforms of mouse myelin basic protein: the existence of exon 5a.";
J. Neurochem. 56:1222-1226(1991).
[15]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 12 AND 13).
TISSUE=Embryonic brain;
PubMed=7681106 [NCBI, ExPASy, EBI, Israel, Japan]
Nakajima K., Ikenaka K., Kagawa T., Aruga J., Nakao J., Nakahira K., Shiota C., Kim S.U., Mikoshiba K.;
"Novel isoforms of mouse myelin basic protein predominantly expressed in embryonic stage.";
J. Neurochem. 60:1554-1563(1993).
[16]
DEVELOPMENTAL STAGE.
PubMed=9736652 [NCBI, ExPASy, EBI, Israel, Japan]
Landry C.F., Pribyl T.M., Ellison J.A., Givogri M.I., Kampf K., Campagnoni C.W., Campagnoni A.T.;
"Embryonic expression of the myelin basic protein gene: identification of a promoter region that targets transgene expression to pioneer neurons.";
J. Neurosci. 18:7315-7327(1998).
[17]
FUNCTION.
PubMed=11145205 [NCBI, ExPASy, EBI, Israel, Japan]
Campagnoni A.T., Skoff R.P.;
"The pathobiology of myelin mutants reveal novel biological functions of the MBP and PLP genes.";
Brain Pathol. 11:74-91(2001).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144; SER-201 AND THR-229, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1074/jbc.M411220200; PubMed=15572359 [NCBI, ExPASy, EBI, Israel, Japan]
Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., Blackstock W.P., Choudhary J.S., Grant S.G.;
"Proteomic analysis of in vivo phosphorylated synaptic proteins.";
J. Biol. Chem. 280:5972-5982(2005).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172 AND SER-178, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1002/pmic.200401066; PubMed=15648052 [NCBI, ExPASy, EBI, Israel, Japan]
Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L., Hart G.W., Burlingame A.L.;
"Quantitative analysis of both protein expression and serine / threonine post-translational modifications through stable isotope labeling with dithiothreitol.";
Proteomics 5:388-398(2005).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1074/mcp.T500041-MCP200; PubMed=16452087 [NCBI, ExPASy, EBI, Israel, Japan]
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-199, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1021/pr0701254; PubMed=18034455 [NCBI, ExPASy, EBI, Israel, Japan]
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-167, AND MASS SPECTROMETRY.
TISSUE=Brain;
Lubec G., Kang S.;
Submitted (APR-2007) to UniProtKB.
Comments
  • FUNCTION: The classic group of MBP isoforms (isoform 4-isoform 13) are with PLP the most abundant protein components of the myelin membrane in the CNS, AND MASS SPECTROMETRY. They have a role in both its formation and stabilization. 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 to optional post-translational modifications give a wide spectrum of isomers, with each of them potentially having a specialized function.
  • SUBUNIT: Homodimer (By similarity).
  • SUBCELLULAR LOCATION: Isoform 13: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.
  • SUBCELLULAR LOCATION: Isoform 12: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.
  • SUBCELLULAR LOCATION: Isoform 11: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.
  • SUBCELLULAR LOCATION: Isoform 10: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.
  • SUBCELLULAR LOCATION: Isoform 9: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.
  • SUBCELLULAR LOCATION: Isoform 8: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.
  • SUBCELLULAR LOCATION: Isoform 7: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.
  • SUBCELLULAR LOCATION: Isoform 6: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.
  • SUBCELLULAR LOCATION: Isoform 5: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.
  • SUBCELLULAR LOCATION: Isoform 4: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.
  • SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Nucleus.
  • SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus.
  • SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus.
  • ALTERNATIVE PRODUCTS: 13 named isoforms [FASTA] produced by alternative splicing. Additional isoforms seem to exist.
    Name1
    SynonymsGolli-MBP1, J37
    Isoform IDP04370-1
    This is the isoform sequence displayed in this entry.
    Name2
    SynonymsGolli-MBP2, BG21, HMBPR
    Isoform IDP04370-2
    Features which should be applied to build the isoform sequence: VSP_003314.
    Name3
    SynonymsGolli-MBP3, TP8
    Isoform IDP04370-3
    Features which should be applied to build the isoform sequence: VSP_003313.
    Name4
    Synonyms21.5-kDa
    Isoform IDP04370-4
    Features which should be applied to build the isoform sequence: VSP_003312, VSP_003315, VSP_003319.
    Name5
    Synonyms18.5-kDa
    Isoform IDP04370-5
    Features which should be applied to build the isoform sequence: VSP_003312, VSP_003319.
    Name6
    Synonyms17-kDa-a
    Isoform IDP04370-6
    Features which should be applied to build the isoform sequence: VSP_003312, VSP_003315, VSP_003318.
    Name7
    Synonyms17-kDa-b
    Isoform IDP04370-7
    Features which should be applied to build the isoform sequence: VSP_003312, VSP_003320.
    Name8
    Synonyms14-kDa
    Isoform IDP04370-8
    Features which should be applied to build the isoform sequence: VSP_003312, VSP_003318.
    Name9
    Isoform IDP04370-9
    Features which should be applied to build the isoform sequence: VSP_003312, VSP_003315, VSP_003320.
    Name10
    Synonyms21-kDa
    Isoform IDP04370-10
    Features which should be applied to build the isoform sequence: VSP_003312, VSP_003317.
    Name11
    Synonyms19.7-kDa
    Isoform IDP04370-11
    Features which should be applied to build the isoform sequence: VSP_003312, VSP_003315, VSP_003316.
    Name12
    Synonyms15.6-kDa
    Isoform IDP04370-13
    Features which should be applied to build the isoform sequence: VSP_003312, VSP_003315.
    Name13
    Synonyms13-kDa
    Isoform IDP04370-14
    Features which should be applied to build the isoform sequence: VSP_003312.
  • TISSUE SPECIFICITY: In the embryo, isoform 1-isoform 3 are found in neurons within the central nervous system (primarily in pioneer neurons important in the formation of the cortex) and the peripheral nervous system. They are also expressed in the thymus, gut, lung and kidney. In the adult, isoform 1-isoform 3 are highly expressed in the brain (mainly in brain regions rich in oligodendrocytes) and spleen. Lower levels are seen in the heart, kidney and lung. Isoform 2 is also found in cells of the immune system. The isoforms missing the 134 first amino acids (isoform 4-isoform 13) are almost exclusively produced in the myelin-forming cells, the mature oligodendrocytes.
  • DEVELOPMENTAL STAGE: The differential expression of MBP isoforms is developmentally regulated. Isoform 2 and isoform 3 are first expressed during embryonic stages (as early as at embryonic day 11.5), expression of isoform 1 is turned on shortly after birth. Expression of the isoforms missing the 134 first amino acids occurs later, presumably as the oligodendrocytes approach their terminally differentiated state.
  • PTM: As in other animals, several charge isomers may be 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.
  • PTM: Methylated on arginine residues; decreases with the age of the animal, making MBP more cationic.
  • DISEASE: Defects in Mbp are a cause of dysmyelinating diseases such as the shiverer (SHI) and myelin deficient (MLD) diseases characterized by decreased myelination in the CNS, tremors, and convulsions of progressively increasing severity leading to early death. The shiverer mice only express isoform 2, the MLD mice have a reduced amount of Mbp.
  • SIMILARITY: Belongs to the myelin basic protein family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M11533; AAA39496.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11291; AAA39496.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11529; AAA39496.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11530; AAA39496.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11531; AAA39496.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11532; AAA39496.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11533; AAA39497.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11291; AAA39497.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11529; AAA39497.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11530; AAA39497.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11531; AAA39497.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00404; AAA39499.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00398; AAA39499.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00400; AAA39499.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00401; AAA39499.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00402; AAA39499.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00404; AAA39500.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00398; AAA39500.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00399; AAA39500.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00400; AAA39500.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00401; AAA39500.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00402; AAA39500.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00404; AAA39501.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00398; AAA39501.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00400; AAA39501.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00401; AAA39501.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00402; AAA39501.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00403; AAA39501.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00404; AAA39502.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00398; AAA39502.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00399; AAA39502.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00400; AAA39502.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00401; AAA39502.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00402; AAA39502.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L00403; AAA39502.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M15060; AAB59711.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M15062; AAB59712.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X67319; CAA47733.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L07507; AAA37720.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L07508; AAA37721.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L07509; AAA37722.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L07505; AAA37719.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L07504; AAA37719.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK005129; BAB23830.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004704; AAH04704.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M24410; AAA39498.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M36275; AAA39504.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K00989; AAA39495.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M20010; AAA39503.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A45421; MBMSB.
RefSeq NP_001020425.1; -.
NP_001020429.1; -.
NP_001020430.1; -.
NP_034907.1; -.
UniGene Mm.252063
3D structure databases
HSSP P02686; 1QCL. [HSSP ENTRY / PDB]
DisProt DP00237; -.
ModBase P04370.
PTM databases
PhosphoSite P04370; -.
Organism-specific databases
MGI MGI:96925; Mbp.
GeneLynx Mbp; Mus musculus.
Gene expression databases
ArrayExpress P04370; -.
CleanEx MM_MBP; -.
GermOnline ENSMUSG00000041607; Mus musculus.
Ontologies
GO
GO:0043025; Cellular component: cell soma (inferred from direct assay from MGI).
GO:0033269; Cellular component: internode region of axon (inferred from direct assay from MGI).
GO:0043209; Cellular component: myelin sheath (inferred from direct assay from MGI).
GO:0042552; Biological process: myelination (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR000548; Myelin_BP.
Graphical view of domain structure.
PANTHER PTHR11429; Myelin_BP; 1.
Pfam PF01669; Myelin_MBP; 1.
Pfam graphical view of domain structure.
PRINTS PR00212; MYELINMBP.
ProDom PD004542; Myelin_BP; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00569; MYELIN_MBP; 1.
BLOCKS P04370.
Genome annotation databases
Ensembl ENSMUSG00000041607; Mus musculus. [Contig view]
GeneID 17196; -.
Phylogenomic databases
HOVERGEN P04370; -.
Other
SOURCE Mbp; Mus musculus.
ProtoNet P04370.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Alternative splicing; Autoimmune encephalomyelitis; Citrullination; Cytoplasm; Direct protein sequencing; Membrane; Methylation; Nucleus; Phosphoprotein; Structural protein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   250  250     Myelin basic protein. PRO_0000158991
MOD_RES   96    96        Phosphoserine (By similarity). 
MOD_RES   135   135        N-acetylalanine; in isoform 4, isoform 5, isoform 6, isoform 7, isoform 8 and isoform 9 (By similarity). 
MOD_RES   141   141        Phosphoserine (By similarity). 
MOD_RES   144   144        Phosphoserine. 
MOD_RES   157   157        Citrulline (By similarity). 
MOD_RES   163   163        Citrulline (By similarity). 
MOD_RES   167   167        Phosphothreonine. 
MOD_RES   172   172        Phosphoserine. 
MOD_RES   178   178        Phosphoserine. 
MOD_RES   188   188        Phosphoserine (By similarity). 
MOD_RES   199   199        Phosphotyrosine. 
MOD_RES   201   201        Phosphoserine. 
MOD_RES   226   226        Phosphothreonine (By similarity). 
MOD_RES   229   229        Phosphothreonine. 
MOD_RES   234   234        Deamidated glutamine (By similarity). 
MOD_RES   239   239        Citrulline (By similarity). 
MOD_RES   241   241        Phosphoserine (By similarity). 
MOD_RES   245   245        Phosphoserine. 
MOD_RES   250   250        Citrulline (By similarity). 
VAR_SEQ   1   133        Missing (in isoform 4, isoform 5, isoform 6, isoform 7, isoform 8, isoform 9, isoform 10, isoform 11, isoform 12 and isoform 13). VSP_003312
VAR_SEQ   48   250        EADAIQNNGTSAEDTAVTDSKHTADPKNNWQGAHPADPGN RPHLIRLFSRDAPGREDNTFKDRPSESDELQTIQEDPTAA SGGLDVMASQKRPSQRSKYLATASTMDHARHGFLPRHRDT GILDSIGRFFSGDRGAPKRGSGKDSHTRTTHYGSLPQKSQ HGRTQDENPVVHFFKNIVTPRTPPPSQGKGGRDSRSGS PMARR -> LTHENYPLWLPAPEVAARPDPR (in isoform 3). VSP_003313
VAR_SEQ   190   190        K -> KVPWLKQSRSPLPSHARSRPGLCHMYK (in