P04370 (MBP_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 18, 2012.
Version 136.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Myelin basic protein Short name=MBP Alternative name(s): Myelin A1 protein | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus |
Protein attributes
| Sequence length | 250 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (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. 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. Ref.17 |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Isoform 13: Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Isoform 12: Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Isoform 11: Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Isoform 10: Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Isoform 9: Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Isoform 8: Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Isoform 7: Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Isoform 6: Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Isoform 5: Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Isoform 4: Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Isoform 3: Cytoplasm. Nucleus. |
| 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. Ref.16 |
| Post-translational modification | 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. Methylated on arginine residues; decreases with the age of the animal, making MBP more cationic. Phosphorylated by TAOK2, VRK2, MAPK11, MAPK12, MAPK14 and MINK1 By similarity. Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 |
| Involvement in disease | Note=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. |
| Sequence similarities | Belongs to the myelin basic protein family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell membrane Cytoplasm Membrane Nucleus |
| Coding sequence diversity | Alternative splicing |
| Disease | Autoimmune encephalomyelitis |
| PTM | Acetylation Citrullination Methylation Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological process | myelination Inferred from direct assay PubMed 14614079. Source: MGI response to toxinInferred from direct assay PubMed 20578039. Source: MGI |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell internode region of axonInferred from direct assay PubMed 16421295. Source: MGI neuronal cell bodyInferred from direct assay PubMed 16421295. Source: MGI nucleusInferred from electronic annotation. Source: UniProtKB-SubCell plasma membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | protease binding Inferred from physical interaction PubMed 12372841. Source: BHF-UCL |
| Complete GO annotation... | |
Alternative products
| This entry describes 13 isoforms produced by alternative splicing. [Align] [Select] Note: Additional isoforms seem to exist. | ||||||
| Isoform 1 (identifier: P04370-1) Also known as: Golli-MBP1; J37; 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. | ||||||
| Isoform 2 (identifier: P04370-2) Also known as: Golli-MBP2; BG21; HMBPR; The sequence of this isoform differs from the canonical sequence as follows: 191-250: DSHTRTTHYGSLPQKSQHGRTQDENPVVHFFKNIVTPRTPPPSQGKGGRDSRSGSPMARR → VSSEP | ||||||
| Isoform 3 (identifier: P04370-3) Also known as: Golli-MBP3; TP8; The sequence of this isoform differs from the canonical sequence as follows: 48-250: EADAIQNNGT...SRSGSPMARR → LTHENYPLWLPAPEVAARPDPR | ||||||
| Isoform 4 (identifier: P04370-4) Also known as: 21.5-kDa; The sequence of this isoform differs from the canonical sequence as follows: 1-133: Missing. 190-190: K → KVPWLKQSRSPLPSHARSRPGLCHMYK 236-236: K → KGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTLSKIFKL | ||||||
| Note: Met-1 is removed. Contains N-acetylalanine at position 2. | ||||||
| Isoform 5 (identifier: P04370-5) Also known as: 18.5-kDa; The sequence of this isoform differs from the canonical sequence as follows: 1-133: Missing. 236-236: K → KGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTLSKIFKL | ||||||
| Note: Met-1 is removed. Contains N-acetylalanine at position 2. | ||||||
| Isoform 6 (identifier: P04370-6) Also known as: 17-kDa-a; The sequence of this isoform differs from the canonical sequence as follows: 1-133: Missing. 190-190: K → KVPWLKQSRSPLPSHARSRPGLCHMYK 236-236: K → KGRGLSLSRFSW | ||||||
| Note: Met-1 is removed. Contains N-acetylalanine at position 2. | ||||||
| Isoform 7 (identifier: P04370-7) Also known as: 17-kDa-b; The sequence of this isoform differs from the canonical sequence as follows: 1-133: Missing. 236-236: K → KGAEGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTLSKIFKL | ||||||
| Note: Met-1 is removed. Contains N-acetylalanine at position 2. | ||||||
| Isoform 8 (identifier: P04370-8) Also known as: 14-kDa; The sequence of this isoform differs from the canonical sequence as follows: 1-133: Missing. 236-236: K → KGRGLSLSRFSW | ||||||
| Note: Met-1 is removed. Contains N-acetylalanine at position 2. | ||||||
| Isoform 9 (identifier: P04370-9) The sequence of this isoform differs from the canonical sequence as follows: 1-133: Missing. 190-190: K → KVPWLKQSRSPLPSHARSRPGLCHMYK 236-236: K → KGAEGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTLSKIFKL | ||||||
| Note: Met-1 is removed. Contains N-acetylalanine at position 2. | ||||||
| Isoform 10 (identifier: P04370-10) Also known as: 21-kDa; The sequence of this isoform differs from the canonical sequence as follows: 1-133: Missing. 236-236: K → KDFVPGDHHV...QGTLSKIFKL | ||||||
| Isoform 11 (identifier: P04370-11) Also known as: 19.7-kDa; The sequence of this isoform differs from the canonical sequence as follows: 1-133: Missing. 190-190: K → KVPWLKQSRSPLPSHARSRPGLCHMYK 236-236: K → KDFVPGDHHVNVSVVTVSFSSSQGRGLSLSRFSW | ||||||
| Isoform 12 (identifier: P04370-13) Also known as: 15.6-kDa; The sequence of this isoform differs from the canonical sequence as follows: 1-133: Missing. 190-190: K → KVPWLKQSRSPLPSHARSRPGLCHMYK | ||||||
| Isoform 13 (identifier: P04370-14) Also known as: 13-kDa; The sequence of this isoform differs from the canonical sequence as follows: 1-133: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 250 | 250 | Myelin basic protein | PRO_0000158991 | |||||
Amino acid modifications | |||||||||
| Modified residue | 96 | 1 | Phosphoserine Ref.24 | ||||||
| Modified residue | 141 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 144 | 1 | Phosphoserine Ref.18 | ||||||
| Modified residue | 157 | 1 | Citrulline By similarity | ||||||
| Modified residue | 163 | 1 | Citrulline By similarity | ||||||
| Modified residue | 167 | 1 | Phosphothreonine Ref.22 | ||||||
| Modified residue | 172 | 1 | Phosphoserine Ref.19 | ||||||
| Modified residue | 178 | 1 | Phosphoserine Ref.19 | ||||||
| Modified residue | 188 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 199 | 1 | Phosphotyrosine Ref.21 | ||||||
| Modified residue | 201 | 1 | Phosphoserine Ref.18 Ref.23 | ||||||
| Modified residue | 226 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 229 | 1 | Phosphothreonine Ref.18 | ||||||
| Modified residue | 234 | 1 | Deamidated glutamine By similarity | ||||||
| Modified residue | 239 | 1 | Citrulline By similarity | ||||||
| Modified residue | 241 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 245 | 1 | Phosphoserine Ref.20 | ||||||
| Modified residue | 250 | 1 | Citrulline By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 133 | 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 | |||||
| Alternative sequence | 48 – 250 | 203 | EADAI…PMARR → LTHENYPLWLPAPEVAARPD PR in isoform 3. | VSP_003313 | |||||
| Alternative sequence | 190 | 1 | K → KVPWLKQSRSPLPSHARSRP GLCHMYK in isoform 4, isoform 6, isoform 9, isoform 11 and isoform 12. | VSP_003315 | |||||
| Alternative sequence | 191 – 250 | 60 | DSHTR…PMARR → VSSEP in isoform 2. | VSP_003314 | |||||
| Alternative sequence | 236 | 1 | K → KDFVPGDHHVNVSVVTVSFS SSQGRGLSLSRFSWGAEGQK PGFGYGGRASDYKSAHKGFK GAYDAQGTLSKIFKL in isoform 10. | VSP_003317 | |||||
| Alternative sequence | 236 | 1 | K → KDFVPGDHHVNVSVVTVSFS SSQGRGLSLSRFSW in isoform 11. | VSP_003316 | |||||
| Alternative sequence | 236 | 1 | K → KGRGLSLSRFSWGAEGQKPG FGYGGRASDYKSAHKGFKGA YDAQGTLSKIFKL in isoform 4 and isoform 5. | VSP_003319 | |||||
| Alternative sequence | 236 | 1 | K → KGRGLSLSRFSW in isoform 6 and isoform 8. | VSP_003318 | |||||
| Alternative sequence | 236 | 1 | K → KGAEGQKPGFGYGGRASDYK SAHKGFKGAYDAQGTLSKIF KL in isoform 7 and isoform 9. | VSP_003320 | |||||
Experimental info | |||||||||
| Sequence conflict | 204 – 205 | 2 | QK → HN Ref.15 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "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." Takahashi N., Roach A., Teplow D.B., Prusiner S.B., Hood L.E. Cell 42:139-148(1985) [PubMed: 2410136] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Alternative splicing accounts for the four forms of myelin basic protein." de Ferra F., Engh H., Hudson L., Kamholz J., Puckett C., Molineaux S., Lazzarini R.A. Cell 43:721-727(1985) [PubMed: 2416470] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "Identification of a cDNA coding for a fifth form of myelin basic protein in mouse." Newman S., Kitamura K., Campagnoni A.T. Proc. Natl. Acad. Sci. U.S.A. 84:886-890(1987) [PubMed: 2433693] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 7), NUCLEOTIDE SEQUENCE [MRNA] OF 9-194. Strain: C57BL/6J. Tissue: Brain. |
| [4] | "Expression of a novel transcript of the myelin basic protein gene." Kitamura K., Newman S.L., Campagnoni C.W., Verdi J.M., Mohandas T., Handley V.W., Campagnoni A.T. J. Neurochem. 54:2032-2041(1990) [PubMed: 1692584] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8). |
| [5] | "A novel transcript overlapping the myelin basic protein gene." Grima B., Zelenika D., Pessac B. J. Neurochem. 59:2318-2323(1992) [PubMed: 1279125] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Strain: C57BL/6. Tissue: Bone marrow. |
| [6] | "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." 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. J. Biol. Chem. 268:4930-4938(1993) [PubMed: 7680345] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3). Strain: C57BL/6. Tissue: Brain. |
| [7] | "The transcriptional landscape of the mammalian genome." 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. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8). Strain: C57BL/6J. Tissue: Cerebellum. |
| [8] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9). Tissue: Mammary tumor. |
| [9] | "The promoter elements of the mouse myelin basic protein gene function efficiently in NG108-15 neuronal/glial cells." Miura M., Tamura T.A., Aoyama A., Mikoshiba K. Gene 75:31-38(1989) [PubMed: 2470651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 135-157. |
| [10] | Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 146-157; 164-175; 196-205 AND 211-222, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain. |
| [11] | "Gene organization and transcription of duplicated MBP genes of myelin deficient (shi(mld)) mutant mouse." Okano H., Tamura T., Miura M., Aoyama A., Ikenaka K., Oshimura M., Mikoshiba K. EMBO J. 7:77-83(1988) [PubMed: 2452084] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-224. |
| [12] | "Characterization of mouse myelin basic protein messenger RNAs with a myelin basic protein cDNA clone." Zeller N.K., Hunkeler M.J., Campagnoni A.T., Sprague J., Lazzarini R.A. Proc. Natl. Acad. Sci. U.S.A. 81:18-22(1984) [PubMed: 6198644] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 193-222. |
| [13] | "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: 2425357] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 6 AND 9). |
| [14] | "Identification of the new isoforms of mouse myelin basic protein: the existence of exon 5a." Aruga J., Okano H., Mikoshiba K. J. Neurochem. 56:1222-1226(1991) [PubMed: 1705957] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 10 AND 11). Tissue: Spinal cord. |
| [15] | "Novel isoforms of mouse myelin basic protein predominantly expressed in embryonic stage." Nakajima K., Ikenaka K., Kagawa T., Aruga J., Nakao J., Nakahira K., Shiota C., Kim S.U., Mikoshiba K. J. Neurochem. 60:1554-1563(1993) [PubMed: 7681106] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 12 AND 13). Tissue: Embryonic brain. |
| [16] | "Embryonic expression of the myelin basic protein gene: identification of a promoter region that targets transgene expression to pioneer neurons." Landry C.F., Pribyl T.M., Ellison J.A., Givogri M.I., Kampf K., Campagnoni C.W., Campagnoni A.T. J. Neurosci. 18:7315-7327(1998) [PubMed: 9736652] [Abstract] Cited for: DEVELOPMENTAL STAGE. |
| [17] | "The pathobiology of myelin mutants reveal novel biological functions of the MBP and PLP genes." Campagnoni A.T., Skoff R.P. Brain Pathol. 11:74-91(2001) [PubMed: 11145205] [Abstract] Cited for: FUNCTION. |
| [18] | "Proteomic analysis of in vivo phosphorylated synaptic proteins." Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., Blackstock W.P., Choudhary J.S., Grant S.G. J. Biol. Chem. 280:5972-5982(2005) [PubMed: 15572359] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144; SER-201 AND THR-229, MASS SPECTROMETRY. Tissue: Forebrain. |
| [19] | "Quantitative analysis of both protein expression and serine / threonine post-translational modifications through stable isotope labeling with dithiothreitol." Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L., Hart G.W., Burlingame A.L. Proteomics 5:388-398(2005) [PubMed: 15648052] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172 AND SER-178, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain. |
| [20] | "Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed: 16452087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, MASS SPECTROMETRY. Tissue: Brain. |
| [21] | "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-199, MASS SPECTROMETRY. Tissue: Brain. |
| [22] | Lubec G., Kang S. Submitted (APR-2007) to UniProtKB Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-167, MASS SPECTROMETRY. Tissue: Brain. |
| [23] | "Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, MASS SPECTROMETRY. Tissue: Melanoma. |
| [24] | "The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed: 19144319] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, MASS SPECTROMETRY. Tissue: Macrophage. |
| + | Additional computationally mapped references. |
Cross-references
Entry information
| Entry name | MBP_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P04370 Secondary accession number(s): Q01585 Q9QWP1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

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