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P04370 (MBP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myelin basic protein

Short name=MBP
Alternative name(s):
Myelin A1 protein
Gene names
Name:Mbp
Synonyms:Shi
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length250 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The classic group of MBP isoforms (isoform 4-isoform13) 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-isoform3/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.

Isoform 2: Cytoplasm. Nucleus.

Isoform 1: Cytoplasm. Nucleus.

Tissue specificity

In the embryo, isoform 1-isoform3 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-isoform3 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-isoform13) 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.

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 componentCell membrane
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseAutoimmune encephalomyelitis
   PTMAcetylation
Citrullination
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processmembrane organization

Inferred from direct assay PubMed 20334434. Source: MGI

myelination

Inferred from direct assay PubMed 14614079. Source: MGI

negative regulation of axonogenesis

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from direct assay PubMed 20578039. Source: MGI

   Cellular_componentcell periphery

Inferred from direct assay PubMed 16723544. Source: MGI

cell projection

Inferred from direct assay PubMed 16421295. Source: MGI

compact myelin

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

internode region of axon

Inferred from direct assay PubMed 16421295. Source: MGI

myelin sheath

Inferred from direct assay PubMed 16405874PubMed 16421295PubMed 1694232PubMed 20578039. Source: MGI

neuronal cell body

Inferred from direct assay PubMed 16421295. Source: MGI

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionprotease binding

Inferred from physical interaction PubMed 12372841. Source: BHF-UCL

structural constituent of myelin sheath

Inferred from electronic annotation. Source: Ensembl

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: Initiator Met-1 is removed (By similarity). Contains a N-acetylalanine at position 2 (By similarity). Contains a phosphothreonine at position 122. Contains a phosphoserine at position 139. Contains a phosphotyrosine at position 151.
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: Initiator Met-1 is removed (By similarity). Contains a N-acetylalanine at position 2 (By similarity). Contains a phosphothreonine at position 96. Contains a phosphoserine at position 113. Contains a phosphotyrosine at position 125.
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: Initiator Met-1 is removed (By similarity). Contains a N-acetylalanine at position 2 (By similarity). Contains a phosphothreonine at position 122.
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: Initiator Met-1 is removed (By similarity). Contains a N-acetylalanine at position 2 (By similarity).
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: Initiator Met-1 is removed (By similarity). Contains a N-acetylalanine at position 2 (By similarity). Contains a phosphothreonine at position 96.
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: Initiator Met-1 is removed (By similarity). Contains a N-acetylalanine at position 2 (By similarity).
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
Note: Contains a phosphoserine at position 135. Contains a phosphotyrosine at position 147.
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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 250250Myelin basic protein
PRO_0000158991

Amino acid modifications

Modified residue1411Phosphoserine By similarity
Modified residue1571Citrulline By similarity
Modified residue1631Citrulline By similarity
Modified residue1671Phosphothreonine Ref.19
Modified residue1721Phosphoserine Ref.18
Modified residue1881Phosphoserine By similarity
Modified residue1991Phosphotyrosine Ref.20
Modified residue2261Phosphothreonine By similarity
Modified residue2291Phosphothreonine Ref.19
Modified residue2341Deamidated glutamine By similarity
Modified residue2391Citrulline By similarity
Modified residue2411Phosphoserine By similarity
Modified residue2451Phosphoserine; by UHMK1
Modified residue2501Citrulline By similarity

Natural variations

Alternative sequence1 – 133133Missing 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 sequence48 – 250203EADAI…PMARR → LTHENYPLWLPAPEVAARPD PR in isoform 3.
VSP_003313
Alternative sequence1901K → KVPWLKQSRSPLPSHARSRP GLCHMYK in isoform 4, isoform 6, isoform 9, isoform 11 and isoform 12.
VSP_003315
Alternative sequence191 – 25060DSHTR…PMARR → VSSEP in isoform 2.
VSP_003314
Alternative sequence2361K → KDFVPGDHHVNVSVVTVSFS SSQGRGLSLSRFSWGAEGQK PGFGYGGRASDYKSAHKGFK GAYDAQGTLSKIFKL in isoform 10.
VSP_003317
Alternative sequence2361K → KDFVPGDHHVNVSVVTVSFS SSQGRGLSLSRFSW in isoform 11.
VSP_003316
Alternative sequence2361K → KGRGLSLSRFSWGAEGQKPG FGYGGRASDYKSAHKGFKGA YDAQGTLSKIFKL in isoform 4 and isoform 5.
VSP_003319
Alternative sequence2361K → KGRGLSLSRFSW in isoform 6 and isoform 8.
VSP_003318
Alternative sequence2361K → KGAEGQKPGFGYGGRASDYK SAHKGFKGAYDAQGTLSKIF KL in isoform 7 and isoform 9.
VSP_003320

Experimental info

Sequence conflict204 – 2052QK → HN Ref.15

Secondary structure

....... 250
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Golli-MBP1) (J37) [UniParc].

Last modified October 18, 2001. Version 2.
Checksum: B418ED11C27B0C43

FASTA25027,168
        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 

« Hide

Isoform 2 (Golli-MBP2) (BG21) (HMBPR) [UniParc].

Checksum: 1C5C6AEFB561D2DA
Show »

FASTA19521,004
Isoform 3 (Golli-MBP3) (TP8) [UniParc].

Checksum: 067EABB28D687D99
Show »

FASTA697,498
Isoform 4 (21.5-kDa) [UniParc].

Checksum: 4B57CA6F06C4AC7D
Show »

FASTA19521,502
Isoform 5 (18.5-kDa) [UniParc].

Checksum: E609240A863F36CD
Show »

FASTA16918,488
Isoform 6 (17-kDa-a) [UniParc].

Checksum: 00F1F10ECF90421B
Show »

FASTA15417,225
Isoform 7 (17-kDa-b) [UniParc].

Checksum: 7AA39D2A263A2BF3
Show »

FASTA15817,240
Isoform 8 (14-kDa) [UniParc].

Checksum: E1DB77B2010455FB
Show »

FASTA12814,211
Isoform 9 [UniParc].

Checksum: B7F672275771E3F4
Show »

FASTA18420,255
Isoform 10 (21-kDa) [UniParc].

Checksum: D986AA8B506E2AE9
Show »

FASTA19120,814
Isoform 11 (19.7-kDa) [UniParc].

Checksum: 159154971A58A0CF
Show »

FASTA17619,552
Isoform 12 (15.6-kDa) [UniParc].

Checksum: 932F8612537F93E2
Show »

FASTA14315,978
Isoform 13 (13-kDa) [UniParc].

Checksum: 7FC65A7A1A8C7E53
Show »

FASTA11712,963

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-167 AND THR-229, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122 (ISOFORMS 4 AND 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 (ISOFORM 5), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-96 (ISOFORMS 5 AND 8), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[20]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-199, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-147 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-151 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-125 (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[21]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M11533 expand/collapse EMBL AC list , M11291, M11529, M11530, M11531, M11532 Genomic DNA. Translation: AAA39496.1.
M11533 expand/collapse EMBL AC list , M11291, M11529, M11530, M11531 Genomic DNA. Translation: AAA39497.1.
L00404 expand/collapse EMBL AC list , L00398, L00400, L00401, L00402 Genomic DNA. Translation: AAA39499.1.
L00404 expand/collapse EMBL AC list , L00398, L00399, L00400, L00401, L00402 Genomic DNA. Translation: AAA39500.1.
L00404 expand/collapse EMBL AC list , L00398, L00400, L00401, L00402, L00403 Genomic DNA. Translation: AAA39501.1.
L00404 expand/collapse EMBL AC list , L00398, L00399, L00400, L00401, L00402, L00403 Genomic DNA. Translation: AAA39502.1.
M15060 mRNA. Translation: AAB59711.1.
M15062 mRNA. Translation: AAB59712.1.
X67319 mRNA. Translation: CAA47733.1.
L07507 mRNA. Translation: AAA37720.1.
L07508 mRNA. Translation: AAA37721.1.
L07509 mRNA. Translation: AAA37722.1.
L07505, L07504 Genomic DNA. Translation: AAA37719.1.
AK005129 mRNA. Translation: BAB23830.1.
BC004704 mRNA. Translation: AAH04704.1.
M24410 Genomic DNA. Translation: AAA39498.1.
M36275 Genomic DNA. Translation: AAA39504.1.
K00989 mRNA. Translation: AAA39495.1.
M20010 mRNA. Translation: AAA39503.1.
PIRMBMSB. A45421.
RefSeqNP_001020416.1. NM_001025245.1.
NP_001020422.1. NM_001025251.2.
NP_001020425.1. NM_001025254.2.
NP_001020426.1. NM_001025255.2.
NP_001020427.1. NM_001025256.2.
NP_001020429.1. NM_001025258.2.
NP_001020430.1. NM_001025259.2.
NP_034907.1. NM_010777.3.
UniGeneMm.252063.
Mm.454459.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LUGNMR-A206-237[»]
DisProtDP00237.
ProteinModelPortalP04370.
SMRP04370. Positions 206-237.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201336. 42 interactions.
IntActP04370. 30 interactions.
MINTMINT-4101448.

Chemistry

ChEMBLCHEMBL1764935.

PTM databases

PhosphoSiteP04370.

Proteomic databases

PaxDbP04370.
PRIDEP04370.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000047865; ENSMUSP00000046185; ENSMUSG00000041607. [P04370-1]
ENSMUST00000062446; ENSMUSP00000053495; ENSMUSG00000041607. [P04370-4]
ENSMUST00000075372; ENSMUSP00000074836; ENSMUSG00000041607. [P04370-7]
ENSMUST00000080658; ENSMUSP00000079488; ENSMUSG00000041607. [P04370-6]
ENSMUST00000091789; ENSMUSP00000089393; ENSMUSG00000041607. [P04370-2]
ENSMUST00000102812; ENSMUSP00000099876; ENSMUSG00000041607. [P04370-5]
ENSMUST00000114674; ENSMUSP00000110322; ENSMUSG00000041607. [P04370-9]
ENSMUST00000143506; ENSMUSP00000138313; ENSMUSG00000041607. [P04370-3]
GeneID17196.
KEGGmmu:17196.
UCSCuc008fts.1. mouse. [P04370-1]
uc008ftu.1. mouse. [P04370-4]
uc008ftv.1. mouse. [P04370-9]
uc008ftw.1. mouse. [P04370-5]
uc008fty.1. mouse. [P04370-7]
uc029tqh.1. mouse. [P04370-14]

Organism-specific databases

CTD4155.
MGIMGI:96925. Mbp.

Phylogenomic databases

eggNOGNOG75180.
GeneTreeENSGT00390000014772.
HOVERGENHBG008347.
InParanoidP04370.
KOK17269.
OrthoDBEOG7M0NRZ.
PhylomeDBP04370.
TreeFamTF333391.

Gene expression databases

ArrayExpressP04370.
BgeeP04370.
CleanExMM_MBP.
GenevestigatorP04370.

Family and domain databases

InterProIPR000548. Myelin_BP.
[Graphical view]
PANTHERPTHR11429. PTHR11429. 1 hit.
PfamPF01669. Myelin_MBP. 1 hit.
[Graphical view]
PRINTSPR00212. MYELINMBP.
PROSITEPS00569. MYELIN_MBP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMBP. mouse.
NextBio291554.
PMAP-CutDBP04370.
PROP04370.
SOURCESearch...

Entry information

Entry nameMBP_MOUSE
AccessionPrimary (citable) accession number: P04370
Secondary accession number(s): Q01585 expand/collapse secondary AC list , Q03139, Q03176, Q61836, Q61837, Q99KE4, Q9QWP1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: October 18, 2001
Last modified: April 16, 2014
This is version 155 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot