Reviewed, UniProtKB/Swiss-Prot P04370 (MBP_MOUSE)

Names and origin

Protein names

Recommended name:
    Myelin basic protein
      Short name=MBP
Alternative name(s):
    Myelin A1 protein

Gene names

Name:	Mbp
Synonyms:	Shi

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

Protein attributes

Sequence length	250 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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, 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 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. Isoform 2: Cytoplasm. Nucleus. Isoform 1: 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.
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.
Involvement in 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.
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
Molecular function	Structural protein
PTM	Acetylation Citrullination Methylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	myelination Inferred from direct assay. Source: MGI
Cellular component	cell soma Inferred from direct assay. Source: MGI internode region of axon Inferred from direct assay. Source: MGI myelin sheath Inferred from direct assay. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 13 isoforms produced by alternative splicing. [Align] [Select]

Notes: 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

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

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

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

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

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

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
Molecule processing
	Chain	1 – 250	250	Myelin basic protein
Amino acid modifications
	Modified residue	96	1	Phosphoserine By similarity
	Modified residue	135	1	N-acetylalanine; in isoform 4, isoform 5, isoform 6, isoform 7, isoform 8 and isoform 9 By similarity
	Modified residue	141	1	Phosphoserine By similarity
	Modified residue	144	1	Phosphoserine
	Modified residue	157	1	Citrulline By similarity
	Modified residue	163	1	Citrulline By similarity
	Modified residue	167	1	Phosphothreonine
	Modified residue	172	1	Phosphoserine
	Modified residue	178	1	Phosphoserine
	Modified residue	188	1	Phosphoserine By similarity
	Modified residue	199	1	Phosphotyrosine
	Modified residue	201	1	Phosphoserine
	Modified residue	226	1	Phosphothreonine By similarity
	Modified residue	229	1	Phosphothreonine
	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
	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.
	Alternative sequence	48 – 250	203	EADAI…PMARR → LTHENYPLWLPAPEVAARPD PR in isoform 3.
	Alternative sequence	190	1	K → KVPWLKQSRSPLPSHARSRP GLCHMYK in isoform 4, isoform 6, isoform 9, isoform 11 and isoform 12.
	Alternative sequence	191 – 250	60	DSHTR…PMARR → VSSEP in isoform 2.
	Alternative sequence	236	1	K → KDFVPGDHHVNVSVVTVSFS SSQGRGLSLSRFSWGAEGQK PGFGYGGRASDYKSAHKGFK GAYDAQGTLSKIFKL in isoform 10.
	Alternative sequence	236	1	K → KDFVPGDHHVNVSVVTVSFS SSQGRGLSLSRFSW in isoform 11.
	Alternative sequence	236	1	K → KGRGLSLSRFSWGAEGQKPG FGYGGRASDYKSAHKGFKGA YDAQGTLSKIFKL in isoform 4 and isoform 5.
	Alternative sequence	236	1	K → KGRGLSLSRFSW in isoform 6 and isoform 8.
	Alternative sequence	236	1	K → KGAEGQKPGFGYGGRASDYK SAHKGFKGAYDAQGTLSKIF KL in isoform 7 and isoform 9.
Experimental info
	Sequence conflict	204 – 205	2	QK → HN Ref.15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Golli-MBP1) (J37) [UniParc]. Last modified October 18, 2001. Version 2. Checksum: B418ED11C27B0C43	FASTA	250	27,168
	10 20 30 40 50 60 MGNHSGKREL SAEKASKDGE IHRGEAGKKR SVGKLSQTAS EDSDVFGEAD AIQNNGTSAE 70 80 90 100 110 120 DTAVTDSKHT ADPKNNWQGA HPADPGNRPH LIRLFSRDAP GREDNTFKDR PSESDELQTI 130 140 150 160 170 180 QEDPTAASGG LDVMASQKRP SQRSKYLATA STMDHARHGF LPRHRDTGIL DSIGRFFSGD 190 200 210 220 230 240 RGAPKRGSGK DSHTRTTHYG SLPQKSQHGR TQDENPVVHF FKNIVTPRTP PPSQGKGGRD 250 SRSGSPMARR
	Isoform 2 (Golli-MBP2) (BG21) (HMBPR) [UniParc]. Checksum: 1C5C6AEFB561D2DA		195	21,004
	10 20 30 40 50 60 MGNHSGKREL SAEKASKDGE IHRGEAGKKR SVGKLSQTAS EDSDVFGEAD AIQNNGTSAE 70 80 90 100 110 120 DTAVTDSKHT ADPKNNWQGA HPADPGNRPH LIRLFSRDAP GREDNTFKDR PSESDELQTI 130 140 150 160 170 180 QEDPTAASGG LDVMASQKRP SQRSKYLATA STMDHARHGF LPRHRDTGIL DSIGRFFSGD 190 RGAPKRGSGK VSSEP
	Isoform 3 (Golli-MBP3) (TP8) [UniParc]. Checksum: 067EABB28D687D99		69	7,498
	10 20 30 40 50 60 MGNHSGKREL SAEKASKDGE IHRGEAGKKR SVGKLSQTAS EDSDVFGLTH ENYPLWLPAP EVAARPDPR
	Isoform 4 (21.5-kDa) [UniParc]. Checksum: 4B57CA6F06C4AC7D		195	21,502
	10 20 30 40 50 60 MASQKRPSQR SKYLATASTM DHARHGFLPR HRDTGILDSI GRFFSGDRGA PKRGSGKVPW 70 80 90 100 110 120 LKQSRSPLPS HARSRPGLCH MYKDSHTRTT HYGSLPQKSQ HGRTQDENPV VHFFKNIVTP 130 140 150 160 170 180 RTPPPSQGKG RGLSLSRFSW GAEGQKPGFG YGGRASDYKS AHKGFKGAYD AQGTLSKIFK 190 LGGRDSRSGS PMARR
	Isoform 5 (18.5-kDa) [UniParc]. Checksum: E609240A863F36CD		169	18,488
	10 20 30 40 50 60 MASQKRPSQR SKYLATASTM DHARHGFLPR HRDTGILDSI GRFFSGDRGA PKRGSGKDSH 70 80 90 100 110 120 TRTTHYGSLP QKSQHGRTQD ENPVVHFFKN IVTPRTPPPS QGKGRGLSLS RFSWGAEGQK 130 140 150 160 PGFGYGGRAS DYKSAHKGFK GAYDAQGTLS KIFKLGGRDS RSGSPMARR
	Isoform 6 (17-kDa-a) [UniParc]. Checksum: 00F1F10ECF90421B		154	17,225
	10 20 30 40 50 60 MASQKRPSQR SKYLATASTM DHARHGFLPR HRDTGILDSI GRFFSGDRGA PKRGSGKVPW 70 80 90 100 110 120 LKQSRSPLPS HARSRPGLCH MYKDSHTRTT HYGSLPQKSQ HGRTQDENPV VHFFKNIVTP 130 140 150 RTPPPSQGKG RGLSLSRFSW GGRDSRSGSP MARR
	Isoform 7 (17-kDa-b) [UniParc]. Checksum: 7AA39D2A263A2BF3		158	17,240
	10 20 30 40 50 60 MASQKRPSQR SKYLATASTM DHARHGFLPR HRDTGILDSI GRFFSGDRGA PKRGSGKDSH 70 80 90 100 110 120 TRTTHYGSLP QKSQHGRTQD ENPVVHFFKN IVTPRTPPPS QGKGAEGQKP GFGYGGRASD 130 140 150 YKSAHKGFKG AYDAQGTLSK IFKLGGRDSR SGSPMARR
	Isoform 8 (14-kDa) [UniParc]. Checksum: E1DB77B2010455FB		128	14,211
	10 20 30 40 50 60 MASQKRPSQR SKYLATASTM DHARHGFLPR HRDTGILDSI GRFFSGDRGA PKRGSGKDSH 70 80 90 100 110 120 TRTTHYGSLP QKSQHGRTQD ENPVVHFFKN IVTPRTPPPS QGKGRGLSLS RFSWGGRDSR SGSPMARR
	Isoform 9 [UniParc]. Checksum: B7F672275771E3F4		184	20,255
	10 20 30 40 50 60 MASQKRPSQR SKYLATASTM DHARHGFLPR HRDTGILDSI GRFFSGDRGA PKRGSGKVPW 70 80 90 100 110 120 LKQSRSPLPS HARSRPGLCH MYKDSHTRTT HYGSLPQKSQ HGRTQDENPV VHFFKNIVTP 130 140 150 160 170 180 RTPPPSQGKG AEGQKPGFGY GGRASDYKSA HKGFKGAYDA QGTLSKIFKL GGRDSRSGSP MARR
	Isoform 10 (21-kDa) [UniParc]. Checksum: D986AA8B506E2AE9		191	20,814
	10 20 30 40 50 60 MASQKRPSQR SKYLATASTM DHARHGFLPR HRDTGILDSI GRFFSGDRGA PKRGSGKDSH 70 80 90 100 110 120 TRTTHYGSLP QKSQHGRTQD ENPVVHFFKN IVTPRTPPPS QGKDFVPGDH HVNVSVVTVS 130 140 150 160 170 180 FSSSQGRGLS LSRFSWGAEG QKPGFGYGGR ASDYKSAHKG FKGAYDAQGT LSKIFKLGGR 190 DSRSGSPMAR R
	Isoform 11 (19.7-kDa) [UniParc]. Checksum: 159154971A58A0CF		176	19,552
	10 20 30 40 50 60 MASQKRPSQR SKYLATASTM DHARHGFLPR HRDTGILDSI GRFFSGDRGA PKRGSGKVPW 70 80 90 100 110 120 LKQSRSPLPS HARSRPGLCH MYKDSHTRTT HYGSLPQKSQ HGRTQDENPV VHFFKNIVTP 130 140 150 160 170 RTPPPSQGKD FVPGDHHVNV SVVTVSFSSS QGRGLSLSRF SWGGRDSRSG SPMARR
	Isoform 12 (15.6-kDa) [UniParc]. Checksum: 932F8612537F93E2		143	15,978
	10 20 30 40 50 60 MASQKRPSQR SKYLATASTM DHARHGFLPR HRDTGILDSI GRFFSGDRGA PKRGSGKVPW 70 80 90 100 110 120 LKQSRSPLPS HARSRPGLCH MYKDSHTRTT HYGSLPQKSQ HGRTQDENPV VHFFKNIVTP 130 140 RTPPPSQGKG GRDSRSGSPM ARR
	Isoform 13 (13-kDa) [UniParc]. Checksum: 7FC65A7A1A8C7E53		117	12,963
	10 20 30 40 50 60 MASQKRPSQR SKYLATASTM DHARHGFLPR HRDTGILDSI GRFFSGDRGA PKRGSGKDSH 70 80 90 100 110 TRTTHYGSLP QKSQHGRTQD ENPVVHFFKN IVTPRTPPPS QGKGGRDSRS GSPMARR

References

	« Hide 'large scale' referencesShow '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. , 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.,