MBP_MOUSE
ID MBP_MOUSE Reviewed; 250 AA.
AC P04370; Q01585; Q03139; Q03176; Q61836; Q61837; Q99KE4; Q9QWP1;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Myelin basic protein;
DE Short=MBP;
DE AltName: Full=Myelin A1 protein;
GN Name=Mbp; Synonyms=Shi;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2410136; DOI=10.1016/s0092-8674(85)80109-4;
RA Takahashi N., Roach A., Teplow D.B., Prusiner S.B., Hood L.E.;
RT "Cloning and characterization of the myelin basic protein gene from mouse:
RT one gene can encode both 14 kd and 18.5 kd MBPs by alternate use of
RT exons.";
RL Cell 42:139-148(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2416470; DOI=10.1016/0092-8674(85)90245-4;
RA de Ferra F., Engh H., Hudson L., Kamholz J., Puckett C., Molineaux S.,
RA Lazzarini R.A.;
RT "Alternative splicing accounts for the four forms of myelin basic
RT protein.";
RL Cell 43:721-727(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 7), AND NUCLEOTIDE SEQUENCE
RP [MRNA] OF 9-194.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=2433693; DOI=10.1073/pnas.84.3.886;
RA Newman S., Kitamura K., Campagnoni A.T.;
RT "Identification of a cDNA coding for a fifth form of myelin basic protein
RT in mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:886-890(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8).
RX PubMed=1692584; DOI=10.1111/j.1471-4159.1990.tb04908.x;
RA Kitamura K., Newman S.L., Campagnoni C.W., Verdi J.M., Mohandas T.,
RA Handley V.W., Campagnoni A.T.;
RT "Expression of a novel transcript of the myelin basic protein gene.";
RL J. Neurochem. 54:2032-2041(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=1279125; DOI=10.1111/j.1471-4159.1992.tb10126.x;
RA Grima B., Zelenika D., Pessac B.;
RT "A novel transcript overlapping the myelin basic protein gene.";
RL J. Neurochem. 59:2318-2323(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=7680345; DOI=10.1016/s0021-9258(18)53485-2;
RA Campagnoni A.T., Pribyl T.M., Campagnoni C.W., Kampf K., Amur-Umarjee S.,
RA Landry C.F., Handley V.W., Newman S., Garbay B., Kitamura K.;
RT "Structure and developmental regulation of Golli-mbp, a 105-kilobase gene
RT that encompasses the myelin basic protein gene and is expressed in cells in
RT the oligodendrocyte lineage in the brain.";
RL J. Biol. Chem. 268:4930-4938(1993).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 135-157.
RX PubMed=2470651; DOI=10.1016/0378-1119(89)90380-6;
RA Miura M., Tamura T.A., Aoyama A., Mikoshiba K.;
RT "The promoter elements of the mouse myelin basic protein gene function
RT efficiently in NG108-15 neuronal/glial cells.";
RL Gene 75:31-38(1989).
RN [10]
RP PROTEIN SEQUENCE OF 146-157; 164-175; 196-205 AND 211-222, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-224.
RX PubMed=2452084; DOI=10.1002/j.1460-2075.1988.tb02785.x;
RA Okano H., Tamura T., Miura M., Aoyama A., Ikenaka K., Oshimura M.,
RA Mikoshiba K.;
RT "Gene organization and transcription of duplicated MBP genes of myelin
RT deficient (shi(mld)) mutant mouse.";
RL EMBO J. 7:77-83(1988).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 193-222.
RX PubMed=6198644; DOI=10.1073/pnas.81.1.18;
RA Zeller N.K., Hunkeler M.J., Campagnoni A.T., Sprague J., Lazzarini R.A.;
RT "Characterization of mouse myelin basic protein messenger RNAs with a
RT myelin basic protein cDNA clone.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:18-22(1984).
RN [13]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 6 AND 9).
RX PubMed=2425357; DOI=10.1073/pnas.83.13.4962;
RA Kamholz J., de Ferra F., Puckett C., Lazzarini R.A.;
RT "Identification of three forms of human myelin basic protein by cDNA
RT cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:4962-4966(1986).
RN [14]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 10 AND 11).
RC TISSUE=Spinal cord;
RX PubMed=1705957; DOI=10.1111/j.1471-4159.1991.tb11414.x;
RA Aruga J., Okano H., Mikoshiba K.;
RT "Identification of the new isoforms of mouse myelin basic protein: the
RT existence of exon 5a.";
RL J. Neurochem. 56:1222-1226(1991).
RN [15]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 12 AND 13).
RC TISSUE=Embryonic brain;
RX PubMed=7681106; DOI=10.1111/j.1471-4159.1993.tb03321.x;
RA Nakajima K., Ikenaka K., Kagawa T., Aruga J., Nakao J., Nakahira K.,
RA Shiota C., Kim S.U., Mikoshiba K.;
RT "Novel isoforms of mouse myelin basic protein predominantly expressed in
RT embryonic stage.";
RL J. Neurochem. 60:1554-1563(1993).
RN [16]
RP DEVELOPMENTAL STAGE.
RX PubMed=9736652; DOI=10.1523/jneurosci.18-18-07315.1998;
RA Landry C.F., Pribyl T.M., Ellison J.A., Givogri M.I., Kampf K.,
RA Campagnoni C.W., Campagnoni A.T.;
RT "Embryonic expression of the myelin basic protein gene: identification of a
RT promoter region that targets transgene expression to pioneer neurons.";
RL J. Neurosci. 18:7315-7327(1998).
RN [17]
RP FUNCTION.
RX PubMed=11145205; DOI=10.1111/j.1750-3639.2001.tb00383.x;
RA Campagnoni A.T., Skoff R.P.;
RT "The pathobiology of myelin mutants reveal novel biological functions of
RT the MBP and PLP genes.";
RL Brain Pathol. 11:74-91(2001).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15648052; DOI=10.1002/pmic.200401066;
RA Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
RA Hart G.W., Burlingame A.L.;
RT "Quantitative analysis of both protein expression and serine / threonine
RT post-translational modifications through stable isotope labeling with
RT dithiothreitol.";
RL Proteomics 5:388-398(2005).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-167 AND THR-229,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 (ISOFORM 10),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 (ISOFORM 4),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122 (ISOFORMS 4 AND 6),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 (ISOFORM 5),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-96 (ISOFORMS 5 AND 8), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-199, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT TYR-147 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT TYR-151 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP TYR-125 (ISOFORM 5), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-40; SER-144; SER-151;
RP THR-167; SER-172; THR-197; SER-206; THR-211 AND THR-229, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [23]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-175 AND ARG-181, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: The classic group of MBP isoforms (isoform 4-isoform 13) are
CC with PLP the most abundant protein components of the myelin membrane in
CC the CNS. They have a role in both its formation and stabilization. The
CC non-classic group of MBP isoforms (isoform 1-isoform 3/Golli-MBPs) may
CC preferentially have a role in the early developing brain long before
CC myelination, maybe as components of transcriptional complexes, and may
CC also be involved in signaling pathways in T-cells and neural cells.
CC Differential splicing events combined to optional post-translational
CC modifications give a wide spectrum of isomers, with each of them
CC potentially having a specialized function.
CC {ECO:0000269|PubMed:11145205}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 13]: Myelin membrane; Peripheral
CC membrane protein; Cytoplasmic side.
CC -!- SUBCELLULAR LOCATION: [Isoform 12]: Myelin membrane; Peripheral
CC membrane protein; Cytoplasmic side.
CC -!- SUBCELLULAR LOCATION: [Isoform 11]: Myelin membrane; Peripheral
CC membrane protein; Cytoplasmic side.
CC -!- SUBCELLULAR LOCATION: [Isoform 10]: Myelin membrane; Peripheral
CC membrane protein; Cytoplasmic side.
CC -!- SUBCELLULAR LOCATION: [Isoform 9]: Myelin membrane; Peripheral membrane
CC protein; Cytoplasmic side.
CC -!- SUBCELLULAR LOCATION: [Isoform 8]: Myelin membrane; Peripheral membrane
CC protein; Cytoplasmic side.
CC -!- SUBCELLULAR LOCATION: [Isoform 7]: Myelin membrane; Peripheral membrane
CC protein; Cytoplasmic side.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Myelin membrane; Peripheral membrane
CC protein; Cytoplasmic side.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Myelin membrane; Peripheral membrane
CC protein; Cytoplasmic side.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Myelin membrane; Peripheral membrane
CC protein; Cytoplasmic side.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=13;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Golli-MBP1, J37;
CC IsoId=P04370-1; Sequence=Displayed;
CC Name=2; Synonyms=Golli-MBP2, BG21, HMBPR;
CC IsoId=P04370-2; Sequence=VSP_003314;
CC Name=3; Synonyms=Golli-MBP3, TP8;
CC IsoId=P04370-3; Sequence=VSP_003313;
CC Name=4; Synonyms=21.5-kDa;
CC IsoId=P04370-4; Sequence=VSP_003312, VSP_003315, VSP_003319;
CC Name=5; Synonyms=18.5-kDa;
CC IsoId=P04370-5; Sequence=VSP_003312, VSP_003319;
CC Name=6; Synonyms=17-kDa-a;
CC IsoId=P04370-6; Sequence=VSP_003312, VSP_003315, VSP_003318;
CC Name=7; Synonyms=17-kDa-b;
CC IsoId=P04370-7; Sequence=VSP_003312, VSP_003320;
CC Name=8; Synonyms=14-kDa;
CC IsoId=P04370-8; Sequence=VSP_003312, VSP_003318;
CC Name=9;
CC IsoId=P04370-9; Sequence=VSP_003312, VSP_003315, VSP_003320;
CC Name=10; Synonyms=21-kDa;
CC IsoId=P04370-10; Sequence=VSP_003312, VSP_003317;
CC Name=11; Synonyms=19.7-kDa;
CC IsoId=P04370-11; Sequence=VSP_003312, VSP_003315, VSP_003316;
CC Name=12; Synonyms=15.6-kDa;
CC IsoId=P04370-13; Sequence=VSP_003312, VSP_003315;
CC Name=13; Synonyms=13-kDa;
CC IsoId=P04370-14; Sequence=VSP_003312;
CC -!- TISSUE SPECIFICITY: In the embryo, isoform 1-isoform 3 are found in
CC neurons within the central nervous system (primarily in pioneer neurons
CC important in the formation of the cortex) and the peripheral nervous
CC system. They are also expressed in the thymus, gut, lung and kidney. In
CC the adult, isoform 1-isoform 3 are highly expressed in the brain
CC (mainly in brain regions rich in oligodendrocytes) and spleen. Lower
CC levels are seen in the heart, kidney and lung. Isoform 2 is also found
CC in cells of the immune system. The isoforms missing the 134 first amino
CC acids (isoform 4-isoform 13) are almost exclusively produced in the
CC myelin-forming cells, the mature oligodendrocytes.
CC -!- DEVELOPMENTAL STAGE: The differential expression of MBP isoforms is
CC developmentally regulated. Isoform 2 and isoform 3 are first expressed
CC during embryonic stages (as early as at embryonic day 11.5), expression
CC of isoform 1 is turned on shortly after birth. Expression of the
CC isoforms missing the 134 first amino acids occurs later, presumably as
CC the oligodendrocytes approach their terminally differentiated state.
CC {ECO:0000269|PubMed:9736652}.
CC -!- PTM: As in other animals, several charge isomers may be produced as a
CC result of optional post-translational modifications, such as
CC phosphorylation of serine or threonine residues, deamidation of
CC glutamine or asparagine residues, citrullination and methylation of
CC arginine residues.
CC -!- PTM: Methylated on arginine residues; decreases with the age of the
CC animal, making MBP more cationic.
CC -!- PTM: Phosphorylated by TAOK2, VRK2, MAPK11, MAPK12, MAPK14 and MINK1.
CC {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved in B cell lysosomes by cathepsin CTSG
CC which degrades the major immunogenic MBP epitope and prevents the
CC activation of MBP-specific autoreactive T cells.
CC {ECO:0000250|UniProtKB:P02686}.
CC -!- DISEASE: Note=Defects in Mbp are a cause of dysmyelinating diseases
CC such as the shiverer (SHI) and myelin deficient (MLD) diseases
CC characterized by decreased myelination in the CNS, tremors, and
CC convulsions of progressively increasing severity leading to early
CC death. The shiverer mice only express isoform 2, the MLD mice have a
CC reduced amount of Mbp.
CC -!- SIMILARITY: Belongs to the myelin basic protein family. {ECO:0000305}.
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DR EMBL; M11533; AAA39496.1; -; Genomic_DNA.
DR EMBL; M11291; AAA39496.1; JOINED; Genomic_DNA.
DR EMBL; M11529; AAA39496.1; JOINED; Genomic_DNA.
DR EMBL; M11530; AAA39496.1; JOINED; Genomic_DNA.
DR EMBL; M11531; AAA39496.1; JOINED; Genomic_DNA.
DR EMBL; M11532; AAA39496.1; JOINED; Genomic_DNA.
DR EMBL; M11533; AAA39497.1; -; Genomic_DNA.
DR EMBL; M11291; AAA39497.1; JOINED; Genomic_DNA.
DR EMBL; M11529; AAA39497.1; JOINED; Genomic_DNA.
DR EMBL; M11530; AAA39497.1; JOINED; Genomic_DNA.
DR EMBL; M11531; AAA39497.1; JOINED; Genomic_DNA.
DR EMBL; L00404; AAA39499.1; -; Genomic_DNA.
DR EMBL; L00398; AAA39499.1; JOINED; Genomic_DNA.
DR EMBL; L00400; AAA39499.1; JOINED; Genomic_DNA.
DR EMBL; L00401; AAA39499.1; JOINED; Genomic_DNA.
DR EMBL; L00402; AAA39499.1; JOINED; Genomic_DNA.
DR EMBL; L00404; AAA39500.1; -; Genomic_DNA.
DR EMBL; L00398; AAA39500.1; JOINED; Genomic_DNA.
DR EMBL; L00399; AAA39500.1; JOINED; Genomic_DNA.
DR EMBL; L00400; AAA39500.1; JOINED; Genomic_DNA.
DR EMBL; L00401; AAA39500.1; JOINED; Genomic_DNA.
DR EMBL; L00402; AAA39500.1; JOINED; Genomic_DNA.
DR EMBL; L00404; AAA39501.1; -; Genomic_DNA.
DR EMBL; L00398; AAA39501.1; JOINED; Genomic_DNA.
DR EMBL; L00400; AAA39501.1; JOINED; Genomic_DNA.
DR EMBL; L00401; AAA39501.1; JOINED; Genomic_DNA.
DR EMBL; L00402; AAA39501.1; JOINED; Genomic_DNA.
DR EMBL; L00403; AAA39501.1; JOINED; Genomic_DNA.
DR EMBL; L00404; AAA39502.1; -; Genomic_DNA.
DR EMBL; L00398; AAA39502.1; JOINED; Genomic_DNA.
DR EMBL; L00399; AAA39502.1; JOINED; Genomic_DNA.
DR EMBL; L00400; AAA39502.1; JOINED; Genomic_DNA.
DR EMBL; L00401; AAA39502.1; JOINED; Genomic_DNA.
DR EMBL; L00402; AAA39502.1; JOINED; Genomic_DNA.
DR EMBL; L00403; AAA39502.1; JOINED; Genomic_DNA.
DR EMBL; M15060; AAB59711.1; -; mRNA.
DR EMBL; M15062; AAB59712.1; -; mRNA.
DR EMBL; X67319; CAA47733.1; -; mRNA.
DR EMBL; L07507; AAA37720.1; -; mRNA.
DR EMBL; L07508; AAA37721.1; -; mRNA.
DR EMBL; L07509; AAA37722.1; -; mRNA.
DR EMBL; L07505; AAA37719.1; -; Genomic_DNA.
DR EMBL; L07504; AAA37719.1; JOINED; Genomic_DNA.
DR EMBL; AK005129; BAB23830.1; -; mRNA.
DR EMBL; BC004704; AAH04704.1; -; mRNA.
DR EMBL; M24410; AAA39498.1; -; Genomic_DNA.
DR EMBL; M36275; AAA39504.1; -; Genomic_DNA.
DR EMBL; K00989; AAA39495.1; -; mRNA.
DR EMBL; M20010; AAA39503.1; -; mRNA.
DR CCDS; CCDS29373.1; -. [P04370-1]
DR CCDS; CCDS29374.1; -. [P04370-2]
DR CCDS; CCDS29376.1; -. [P04370-4]
DR CCDS; CCDS29377.1; -. [P04370-5]
DR CCDS; CCDS29378.1; -. [P04370-6]
DR CCDS; CCDS29379.1; -. [P04370-7]
DR CCDS; CCDS37875.1; -. [P04370-9]
DR CCDS; CCDS89290.1; -. [P04370-8]
DR PIR; A45421; MBMSB.
DR RefSeq; NP_001020416.1; NM_001025245.1. [P04370-2]
DR RefSeq; NP_001020422.1; NM_001025251.2. [P04370-4]
DR RefSeq; NP_001020425.1; NM_001025254.2. [P04370-9]
DR RefSeq; NP_001020426.1; NM_001025255.2. [P04370-5]
DR RefSeq; NP_001020427.1; NM_001025256.2. [P04370-6]
DR RefSeq; NP_001020429.1; NM_001025258.2. [P04370-7]
DR RefSeq; NP_001020430.1; NM_001025259.2. [P04370-8]
DR RefSeq; NP_034907.1; NM_010777.3. [P04370-1]
DR PDB; 1U3H; X-ray; 2.42 A; I/P=135-142.
DR PDB; 2LUG; NMR; -; A=206-237.
DR PDBsum; 1U3H; -.
DR PDBsum; 2LUG; -.
DR AlphaFoldDB; P04370; -.
DR BMRB; P04370; -.
DR SMR; P04370; -.
DR BioGRID; 201336; 61.
DR IntAct; P04370; 30.
DR MINT; P04370; -.
DR STRING; 10090.ENSMUSP00000046185; -.
DR ChEMBL; CHEMBL1764935; -.
DR iPTMnet; P04370; -.
DR PhosphoSitePlus; P04370; -.
DR SwissPalm; P04370; -.
DR EPD; P04370; -.
DR jPOST; P04370; -.
DR MaxQB; P04370; -.
DR PaxDb; P04370; -.
DR PeptideAtlas; P04370; -.
DR PRIDE; P04370; -.
DR ProteomicsDB; 293422; -. [P04370-1]
DR ProteomicsDB; 293423; -. [P04370-2]
DR ProteomicsDB; 293424; -. [P04370-3]
DR ProteomicsDB; 293425; -. [P04370-4]
DR ProteomicsDB; 293426; -. [P04370-5]
DR ProteomicsDB; 293427; -. [P04370-6]
DR ProteomicsDB; 293428; -. [P04370-7]
DR ProteomicsDB; 293429; -. [P04370-8]
DR ProteomicsDB; 293430; -. [P04370-9]
DR ProteomicsDB; 293431; -. [P04370-10]
DR ProteomicsDB; 293432; -. [P04370-11]
DR ProteomicsDB; 293433; -. [P04370-13]
DR ProteomicsDB; 293434; -. [P04370-14]
DR Antibodypedia; 3704; 1328 antibodies from 50 providers.
DR DNASU; 17196; -.
DR Ensembl; ENSMUST00000047865; ENSMUSP00000046185; ENSMUSG00000041607. [P04370-1]
DR Ensembl; ENSMUST00000062446; ENSMUSP00000053495; ENSMUSG00000041607. [P04370-11]
DR Ensembl; ENSMUST00000075372; ENSMUSP00000074836; ENSMUSG00000041607. [P04370-14]
DR Ensembl; ENSMUST00000091789; ENSMUSP00000089393; ENSMUSG00000041607. [P04370-2]
DR Ensembl; ENSMUST00000102812; ENSMUSP00000099876; ENSMUSG00000041607. [P04370-10]
DR Ensembl; ENSMUST00000114674; ENSMUSP00000110322; ENSMUSG00000041607. [P04370-13]
DR Ensembl; ENSMUST00000123251; ENSMUSP00000121855; ENSMUSG00000041607. [P04370-4]
DR Ensembl; ENSMUST00000132369; ENSMUSP00000114230; ENSMUSG00000041607. [P04370-7]
DR Ensembl; ENSMUST00000133193; ENSMUSP00000116019; ENSMUSG00000041607. [P04370-8]
DR Ensembl; ENSMUST00000142850; ENSMUSP00000115082; ENSMUSG00000041607. [P04370-5]
DR Ensembl; ENSMUST00000143506; ENSMUSP00000138313; ENSMUSG00000041607. [P04370-3]
DR Ensembl; ENSMUST00000152071; ENSMUSP00000115409; ENSMUSG00000041607. [P04370-6]
DR Ensembl; ENSMUST00000153478; ENSMUSP00000114630; ENSMUSG00000041607. [P04370-9]
DR GeneID; 17196; -.
DR KEGG; mmu:17196; -.
DR UCSC; uc008fts.1; mouse. [P04370-1]
DR UCSC; uc008ftu.1; mouse. [P04370-4]
DR UCSC; uc008ftv.1; mouse. [P04370-9]
DR UCSC; uc008ftw.1; mouse. [P04370-5]
DR UCSC; uc008fty.1; mouse. [P04370-7]
DR UCSC; uc029tqh.1; mouse. [P04370-14]
DR CTD; 4155; -.
DR MGI; MGI:96925; Mbp.
DR VEuPathDB; HostDB:ENSMUSG00000041607; -.
DR eggNOG; ENOG502S4SJ; Eukaryota.
DR GeneTree; ENSGT00390000014772; -.
DR HOGENOM; CLU_118634_0_0_1; -.
DR InParanoid; P04370; -.
DR OMA; TKIFKMG; -.
DR OrthoDB; 872191at2759; -.
DR PhylomeDB; P04370; -.
DR TreeFam; TF333391; -.
DR BioGRID-ORCS; 17196; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Mbp; mouse.
DR PRO; PR:P04370; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P04370; protein.
DR Bgee; ENSMUSG00000041607; Expressed in globus pallidus and 263 other tissues.
DR ExpressionAtlas; P04370; baseline and differential.
DR Genevisible; P04370; MM.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0042995; C:cell projection; IDA:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0043218; C:compact myelin; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033269; C:internode region of axon; IDA:MGI.
DR GO; GO:0043209; C:myelin sheath; IDA:CAFA.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0005516; F:calmodulin binding; IPI:CAFA.
DR GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
DR GO; GO:0019911; F:structural constituent of myelin sheath; ISO:MGI.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; ISO:MGI.
DR GO; GO:0000165; P:MAPK cascade; ISO:MGI.
DR GO; GO:0061024; P:membrane organization; IDA:MGI.
DR GO; GO:0042552; P:myelination; IDA:MGI.
DR GO; GO:0050771; P:negative regulation of axonogenesis; ISO:MGI.
DR GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; ISO:MGI.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:MGI.
DR GO; GO:1904685; P:positive regulation of metalloendopeptidase activity; ISO:MGI.
DR GO; GO:0032570; P:response to progesterone; ISO:MGI.
DR GO; GO:0009636; P:response to toxic substance; IDA:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR DisProt; DP01101; -. [P04370-5]
DR InterPro; IPR000548; Myelin_BP.
DR PANTHER; PTHR11429; PTHR11429; 1.
DR Pfam; PF01669; Myelin_MBP; 1.
DR PRINTS; PR00212; MYELINMBP.
DR PROSITE; PS00569; MYELIN_MBP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing;
KW Autoimmune encephalomyelitis; Cell membrane; Citrullination; Cytoplasm;
KW Direct protein sequencing; Membrane; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..250
FT /note="Myelin basic protein"
FT /id="PRO_0000158991"
FT REGION 1..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 221..222
FT /note="Cleavage; by CTSG"
FT /evidence="ECO:0000250|UniProtKB:P02686"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 146
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P02688"
FT MOD_RES 149
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02688"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 152
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02688"
FT MOD_RES 157
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 163
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 167
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15648052,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 175
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 181
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 197
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 199
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 211
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 226
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02688"
FT MOD_RES 229
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 234
FT /note="Deamidated glutamine"
FT /evidence="ECO:0000250"
FT MOD_RES 239
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 245
FT /note="Phosphoserine; by UHMK1"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 250
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..133
FT /note="Missing (in isoform 4, isoform 5, isoform 6, isoform
FT 7, isoform 8, isoform 9, isoform 10, isoform 11, isoform 12
FT and isoform 13)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:1692584,
FT ECO:0000303|PubMed:2433693"
FT /id="VSP_003312"
FT VAR_SEQ 48..250
FT /note="EADAIQNNGTSAEDTAVTDSKHTADPKNNWQGAHPADPGNRPHLIRLFSRDA
FT PGREDNTFKDRPSESDELQTIQEDPTAASGGLDVMASQKRPSQRSKYLATASTMDHARH
FT GFLPRHRDTGILDSIGRFFSGDRGAPKRGSGKDSHTRTTHYGSLPQKSQHGRTQDENPV
FT VHFFKNIVTPRTPPPSQGKGGRDSRSGSPMARR -> LTHENYPLWLPAPEVAARPDPR
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:7680345"
FT /id="VSP_003313"
FT VAR_SEQ 190
FT /note="K -> KVPWLKQSRSPLPSHARSRPGLCHMYK (in isoform 4,
FT isoform 6, isoform 9, isoform 11 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:2433693"
FT /id="VSP_003315"
FT VAR_SEQ 191..250
FT /note="DSHTRTTHYGSLPQKSQHGRTQDENPVVHFFKNIVTPRTPPPSQGKGGRDSR
FT SGSPMARR -> VSSEP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1279125,
FT ECO:0000303|PubMed:7680345"
FT /id="VSP_003314"
FT VAR_SEQ 236
FT /note="K -> KDFVPGDHHVNVSVVTVSFSSSQGRGLSLSRFSWGAEGQKPGFGYGG
FT RASDYKSAHKGFKGAYDAQGTLSKIFKL (in isoform 10)"
FT /evidence="ECO:0000305"
FT /id="VSP_003317"
FT VAR_SEQ 236
FT /note="K -> KDFVPGDHHVNVSVVTVSFSSSQGRGLSLSRFSW (in isoform
FT 11)"
FT /evidence="ECO:0000305"
FT /id="VSP_003316"
FT VAR_SEQ 236
FT /note="K -> KGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTL
FT SKIFKL (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_003319"
FT VAR_SEQ 236
FT /note="K -> KGRGLSLSRFSW (in isoform 6 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:1692584, ECO:0000303|PubMed:2433693"
FT /id="VSP_003318"
FT VAR_SEQ 236
FT /note="K -> KGAEGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTLSKIFKL (in
FT isoform 7 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:2433693"
FT /id="VSP_003320"
FT CONFLICT 204..205
FT /note="QK -> HN (in Ref. 15)"
FT /evidence="ECO:0000305"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:2LUG"
FT HELIX 216..225
FT /evidence="ECO:0007829|PDB:2LUG"
FT INIT_MET P04370-4:1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02686"
FT MOD_RES P04370-4:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P02686"
FT MOD_RES P04370-4:122
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES P04370-4:139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES P04370-4:151
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT INIT_MET P04370-5:1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02686"
FT MOD_RES P04370-5:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P02686"
FT MOD_RES P04370-5:96
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES P04370-5:113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES P04370-5:125
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT INIT_MET P04370-6:1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02686"
FT MOD_RES P04370-6:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P02686"
FT MOD_RES P04370-6:122
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT INIT_MET P04370-7:1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT MOD_RES P04370-7:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000305"
FT INIT_MET P04370-8:1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02686"
FT MOD_RES P04370-8:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P02686"
FT MOD_RES P04370-8:96
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT INIT_MET P04370-9:1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT MOD_RES P04370-9:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000305"
FT MOD_RES P04370-10:135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES P04370-10:147
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
SQ SEQUENCE 250 AA; 27168 MW; B418ED11C27B0C43 CRC64;
MGNHSGKREL SAEKASKDGE IHRGEAGKKR SVGKLSQTAS EDSDVFGEAD AIQNNGTSAE
DTAVTDSKHT ADPKNNWQGA HPADPGNRPH LIRLFSRDAP GREDNTFKDR PSESDELQTI
QEDPTAASGG LDVMASQKRP SQRSKYLATA STMDHARHGF LPRHRDTGIL DSIGRFFSGD
RGAPKRGSGK DSHTRTTHYG SLPQKSQHGR TQDENPVVHF FKNIVTPRTP PPSQGKGGRD
SRSGSPMARR
