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 24-JAN-2024, entry version 221. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 62. DR IntAct; P04370; 30. DR MINT; P04370; -. DR STRING; 10090.ENSMUSP00000046185; -. DR ChEMBL; CHEMBL1764935; -. DR GlyGen; P04370; 7 sites, 1 O-linked glycan (7 sites). DR iPTMnet; P04370; -. DR PhosphoSitePlus; P04370; -. DR SwissPalm; P04370; -. DR EPD; P04370; -. DR jPOST; P04370; -. DR MaxQB; P04370; -. DR PaxDb; 10090-ENSMUSP00000046185; -. DR PeptideAtlas; 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; 1467 antibodies from 50 providers. DR DNASU; 17196; -. DR Ensembl; ENSMUST00000047865.14; ENSMUSP00000046185.8; ENSMUSG00000041607.18. [P04370-1] DR Ensembl; ENSMUST00000062446.15; ENSMUSP00000053495.9; ENSMUSG00000041607.18. [P04370-11] DR Ensembl; ENSMUST00000075372.13; ENSMUSP00000074836.7; ENSMUSG00000041607.18. [P04370-14] DR Ensembl; ENSMUST00000091789.11; ENSMUSP00000089393.5; ENSMUSG00000041607.18. [P04370-2] DR Ensembl; ENSMUST00000102812.12; ENSMUSP00000099876.6; ENSMUSG00000041607.18. [P04370-10] DR Ensembl; ENSMUST00000114674.11; ENSMUSP00000110322.5; ENSMUSG00000041607.18. [P04370-13] DR Ensembl; ENSMUST00000123251.9; ENSMUSP00000121855.3; ENSMUSG00000041607.18. [P04370-4] DR Ensembl; ENSMUST00000132369.3; ENSMUSP00000114230.3; ENSMUSG00000041607.18. [P04370-7] DR Ensembl; ENSMUST00000133193.9; ENSMUSP00000116019.3; ENSMUSG00000041607.18. [P04370-8] DR Ensembl; ENSMUST00000142850.9; ENSMUSP00000115082.3; ENSMUSG00000041607.18. [P04370-5] DR Ensembl; ENSMUST00000143506.8; ENSMUSP00000138313.2; ENSMUSG00000041607.18. [P04370-3] DR Ensembl; ENSMUST00000152071.9; ENSMUSP00000115409.3; ENSMUSG00000041607.18. [P04370-6] DR Ensembl; ENSMUST00000153478.9; ENSMUSP00000114630.3; ENSMUSG00000041607.18. [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 AGR; MGI:96925; -. 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; FRTIGNQ; -. DR OrthoDB; 4317156at2759; -. DR PhylomeDB; P04370; -. DR TreeFam; TF333391; -. DR BioGRID-ORCS; 17196; 4 hits in 76 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 267 other cell types or tissues. DR ExpressionAtlas; P04370; baseline and differential. 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:0008289; F:lipid binding; ISO:MGI. 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: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; MYELIN BASIC PROTEIN; 1. DR PANTHER; PTHR11429:SF0; MYELIN BASIC PROTEIN; 1. DR Pfam; PF01669; Myelin_MBP; 1. DR PRINTS; PR00212; MYELINMBP. DR PROSITE; PS00569; MYELIN_MBP; 1. DR Genevisible; P04370; MM. 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 //