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Myelin basic protein (MBP) (Myelin A1 protein)

 MBP_MOUSE               Reviewed;         250 AA.
P04370; Q01585; Q03139; Q03176; Q61836; Q61837; Q99KE4; Q9QWP1;
20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
18-OCT-2001, sequence version 2.
22-NOV-2017, entry version 184.
RecName: Full=Myelin basic protein;
Short=MBP;
AltName: Full=Myelin A1 protein;
Name=Mbp; Synonyms=Shi;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2410136; DOI=10.1016/S0092-8674(85)80109-4;
Takahashi N., Roach A., Teplow D.B., Prusiner S.B., Hood L.E.;
"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.";
Cell 42:139-148(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2416470; DOI=10.1016/0092-8674(85)90245-4;
de Ferra F., Engh H., Hudson L., Kamholz J., Puckett C., Molineaux S.,
Lazzarini R.A.;
"Alternative splicing accounts for the four forms of myelin basic
protein.";
Cell 43:721-727(1985).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 7), AND NUCLEOTIDE SEQUENCE
[MRNA] OF 9-194.
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=2433693; DOI=10.1073/pnas.84.3.886;
Newman S., Kitamura K., Campagnoni A.T.;
"Identification of a cDNA coding for a fifth form of myelin basic
protein in mouse.";
Proc. Natl. Acad. Sci. U.S.A. 84:886-890(1987).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8).
PubMed=1692584; DOI=10.1111/j.1471-4159.1990.tb04908.x;
Kitamura K., Newman S.L., Campagnoni C.W., Verdi J.M., Mohandas T.,
Handley V.W., Campagnoni A.T.;
"Expression of a novel transcript of the myelin basic protein gene.";
J. Neurochem. 54:2032-2041(1990).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Bone marrow;
PubMed=1279125;
Grima B., Zelenika D., Pessac B.;
"A novel transcript overlapping the myelin basic protein gene.";
J. Neurochem. 59:2318-2323(1992).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=7680345;
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.;
"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.";
J. Biol. Chem. 268:4930-4938(1993).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
STRAIN=C57BL/6J; TISSUE=Cerebellum;
PubMed=16141072; DOI=10.1126/science.1112014;
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.,
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 135-157.
PubMed=2470651; DOI=10.1016/0378-1119(89)90380-6;
Miura M., Tamura T.A., Aoyama A., Mikoshiba K.;
"The promoter elements of the mouse myelin basic protein gene function
efficiently in NG108-15 neuronal/glial cells.";
Gene 75:31-38(1989).
[10]
PROTEIN SEQUENCE OF 146-157; 164-175; 196-205 AND 211-222, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-224.
PubMed=2452084;
Okano H., Tamura T., Miura M., Aoyama A., Ikenaka K., Oshimura M.,
Mikoshiba K.;
"Gene organization and transcription of duplicated MBP genes of myelin
deficient (shi(mld)) mutant mouse.";
EMBO J. 7:77-83(1988).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 193-222.
PubMed=6198644; DOI=10.1073/pnas.81.1.18;
Zeller N.K., Hunkeler M.J., Campagnoni A.T., Sprague J.,
Lazzarini R.A.;
"Characterization of mouse myelin basic protein messenger RNAs with a
myelin basic protein cDNA clone.";
Proc. Natl. Acad. Sci. U.S.A. 81:18-22(1984).
[13]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 6 AND 9).
PubMed=2425357; DOI=10.1073/pnas.83.13.4962;
Kamholz J., de Ferra F., Puckett C., Lazzarini R.A.;
"Identification of three forms of human myelin basic protein by cDNA
cloning.";
Proc. Natl. Acad. Sci. U.S.A. 83:4962-4966(1986).
[14]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 10 AND 11).
TISSUE=Spinal cord;
PubMed=1705957; DOI=10.1111/j.1471-4159.1991.tb11414.x;
Aruga J., Okano H., Mikoshiba K.;
"Identification of the new isoforms of mouse myelin basic protein: the
existence of exon 5a.";
J. Neurochem. 56:1222-1226(1991).
[15]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 12 AND 13).
TISSUE=Embryonic brain;
PubMed=7681106; DOI=10.1111/j.1471-4159.1993.tb03321.x;
Nakajima K., Ikenaka K., Kagawa T., Aruga J., Nakao J., Nakahira K.,
Shiota C., Kim S.U., Mikoshiba K.;
"Novel isoforms of mouse myelin basic protein predominantly expressed
in embryonic stage.";
J. Neurochem. 60:1554-1563(1993).
[16]
DEVELOPMENTAL STAGE.
PubMed=9736652;
Landry C.F., Pribyl T.M., Ellison J.A., Givogri M.I., Kampf K.,
Campagnoni C.W., Campagnoni A.T.;
"Embryonic expression of the myelin basic protein gene: identification
of a promoter region that targets transgene expression to pioneer
neurons.";
J. Neurosci. 18:7315-7327(1998).
[17]
FUNCTION.
PubMed=11145205;
Campagnoni A.T., Skoff R.P.;
"The pathobiology of myelin mutants reveal novel biological functions
of the MBP and PLP genes.";
Brain Pathol. 11:74-91(2001).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15648052; DOI=10.1002/pmic.200401066;
Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
Hart G.W., Burlingame A.L.;
"Quantitative analysis of both protein expression and serine /
threonine post-translational modifications through stable isotope
labeling with dithiothreitol.";
Proteomics 5:388-398(2005).
[19]
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),
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[20]
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), AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-40; SER-144;
SER-151; THR-167; SER-172; THR-197; SER-206; THR-211 AND THR-229, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[23]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-175 AND ARG-181, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- 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. {ECO:0000269|PubMed:11145205}.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 13: Myelin membrane; Peripheral
membrane protein; Cytoplasmic side.
-!- SUBCELLULAR LOCATION: Isoform 12: Myelin membrane; Peripheral
membrane protein; Cytoplasmic side.
-!- SUBCELLULAR LOCATION: Isoform 11: Myelin membrane; Peripheral
membrane protein; Cytoplasmic side.
-!- SUBCELLULAR LOCATION: Isoform 10: Myelin membrane; Peripheral
membrane protein; Cytoplasmic side.
-!- SUBCELLULAR LOCATION: Isoform 9: Myelin membrane; Peripheral
membrane protein; Cytoplasmic side.
-!- SUBCELLULAR LOCATION: Isoform 8: Myelin membrane; Peripheral
membrane protein; Cytoplasmic side.
-!- SUBCELLULAR LOCATION: Isoform 7: Myelin membrane; Peripheral
membrane protein; Cytoplasmic side.
-!- SUBCELLULAR LOCATION: Isoform 6: Myelin membrane; Peripheral
membrane protein; Cytoplasmic side.
-!- SUBCELLULAR LOCATION: Isoform 5: Myelin membrane; Peripheral
membrane protein; Cytoplasmic side.
-!- SUBCELLULAR LOCATION: Isoform 4: Myelin membrane; Peripheral
membrane protein; Cytoplasmic side.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Nucleus.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus.
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=13;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=Golli-MBP1, J37;
IsoId=P04370-1; Sequence=Displayed;
Name=2; Synonyms=Golli-MBP2, BG21, HMBPR;
IsoId=P04370-2; Sequence=VSP_003314;
Name=3; Synonyms=Golli-MBP3, TP8;
IsoId=P04370-3; Sequence=VSP_003313;
Name=4; Synonyms=21.5-kDa;
IsoId=P04370-4; Sequence=VSP_003312, VSP_003315, VSP_003319;
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.
{ECO:0000244|PubMed:16452087, ECO:0000244|PubMed:18034455,
ECO:0000250};
Name=5; Synonyms=18.5-kDa;
IsoId=P04370-5; Sequence=VSP_003312, VSP_003319;
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.
{ECO:0000244|PubMed:16452087, ECO:0000244|PubMed:18034455,
ECO:0000250};
Name=6; Synonyms=17-kDa-a;
IsoId=P04370-6; Sequence=VSP_003312, VSP_003315, VSP_003318;
Note=Initiator Met-1 is removed (By similarity). Contains a
N-acetylalanine at position 2 (By similarity). Contains a
phosphothreonine at position 122. {ECO:0000244|PubMed:16452087,
ECO:0000250};
Name=7; Synonyms=17-kDa-b;
IsoId=P04370-7; Sequence=VSP_003312, VSP_003320;
Note=Initiator Met-1 is removed. Contains a N-acetylalanine at
position 2. {ECO:0000250};
Name=8; Synonyms=14-kDa;
IsoId=P04370-8; Sequence=VSP_003312, VSP_003318;
Note=Initiator Met-1 is removed (By similarity). Contains a
N-acetylalanine at position 2 (By similarity). Contains a
phosphothreonine at position 96. {ECO:0000244|PubMed:16452087,
ECO:0000250};
Name=9;
IsoId=P04370-9; Sequence=VSP_003312, VSP_003315, VSP_003320;
Note=Initiator Met-1 is removed. Contains a N-acetylalanine at
position 2. {ECO:0000250};
Name=10; Synonyms=21-kDa;
IsoId=P04370-10; Sequence=VSP_003312, VSP_003317;
Note=Contains a phosphoserine at position 135. Contains a
phosphotyrosine at position 147. {ECO:0000244|PubMed:16452087,
ECO:0000244|PubMed:18034455};
Name=11; Synonyms=19.7-kDa;
IsoId=P04370-11; Sequence=VSP_003312, VSP_003315, VSP_003316;
Name=12; Synonyms=15.6-kDa;
IsoId=P04370-13; Sequence=VSP_003312, VSP_003315;
Name=13; Synonyms=13-kDa;
IsoId=P04370-14; Sequence=VSP_003312;
-!- 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. {ECO:0000269|PubMed:9736652}.
-!- PTM: As in other animals, several charge isomers may be produced
as a result of optional post-translational modifications, such as
phosphorylation of serine or threonine residues, deamidation of
glutamine or asparagine residues, citrullination and methylation
of arginine residues.
-!- PTM: Methylated on arginine residues; decreases with the age of
the animal, making MBP more cationic.
-!- PTM: Phosphorylated by TAOK2, VRK2, MAPK11, MAPK12, MAPK14 and
MINK1. {ECO:0000250}.
-!- 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.
-!- SIMILARITY: Belongs to the myelin basic protein family.
{ECO:0000305}.
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EMBL; M11533; AAA39496.1; -; Genomic_DNA.
EMBL; M11291; AAA39496.1; JOINED; Genomic_DNA.
EMBL; M11529; AAA39496.1; JOINED; Genomic_DNA.
EMBL; M11530; AAA39496.1; JOINED; Genomic_DNA.
EMBL; M11531; AAA39496.1; JOINED; Genomic_DNA.
EMBL; M11532; AAA39496.1; JOINED; Genomic_DNA.
EMBL; M11533; AAA39497.1; -; Genomic_DNA.
EMBL; M11291; AAA39497.1; JOINED; Genomic_DNA.
EMBL; M11529; AAA39497.1; JOINED; Genomic_DNA.
EMBL; M11530; AAA39497.1; JOINED; Genomic_DNA.
EMBL; M11531; AAA39497.1; JOINED; Genomic_DNA.
EMBL; L00404; AAA39499.1; -; Genomic_DNA.
EMBL; L00398; AAA39499.1; JOINED; Genomic_DNA.
EMBL; L00400; AAA39499.1; JOINED; Genomic_DNA.
EMBL; L00401; AAA39499.1; JOINED; Genomic_DNA.
EMBL; L00402; AAA39499.1; JOINED; Genomic_DNA.
EMBL; L00404; AAA39500.1; -; Genomic_DNA.
EMBL; L00398; AAA39500.1; JOINED; Genomic_DNA.
EMBL; L00399; AAA39500.1; JOINED; Genomic_DNA.
EMBL; L00400; AAA39500.1; JOINED; Genomic_DNA.
EMBL; L00401; AAA39500.1; JOINED; Genomic_DNA.
EMBL; L00402; AAA39500.1; JOINED; Genomic_DNA.
EMBL; L00404; AAA39501.1; -; Genomic_DNA.
EMBL; L00398; AAA39501.1; JOINED; Genomic_DNA.
EMBL; L00400; AAA39501.1; JOINED; Genomic_DNA.
EMBL; L00401; AAA39501.1; JOINED; Genomic_DNA.
EMBL; L00402; AAA39501.1; JOINED; Genomic_DNA.
EMBL; L00403; AAA39501.1; JOINED; Genomic_DNA.
EMBL; L00404; AAA39502.1; -; Genomic_DNA.
EMBL; L00398; AAA39502.1; JOINED; Genomic_DNA.
EMBL; L00399; AAA39502.1; JOINED; Genomic_DNA.
EMBL; L00400; AAA39502.1; JOINED; Genomic_DNA.
EMBL; L00401; AAA39502.1; JOINED; Genomic_DNA.
EMBL; L00402; AAA39502.1; JOINED; Genomic_DNA.
EMBL; L00403; AAA39502.1; JOINED; Genomic_DNA.
EMBL; M15060; AAB59711.1; -; mRNA.
EMBL; M15062; AAB59712.1; -; mRNA.
EMBL; X67319; CAA47733.1; -; mRNA.
EMBL; L07507; AAA37720.1; -; mRNA.
EMBL; L07508; AAA37721.1; -; mRNA.
EMBL; L07509; AAA37722.1; -; mRNA.
EMBL; L07505; AAA37719.1; -; Genomic_DNA.
EMBL; L07504; AAA37719.1; JOINED; Genomic_DNA.
EMBL; AK005129; BAB23830.1; -; mRNA.
EMBL; BC004704; AAH04704.1; -; mRNA.
EMBL; M24410; AAA39498.1; -; Genomic_DNA.
EMBL; M36275; AAA39504.1; -; Genomic_DNA.
EMBL; K00989; AAA39495.1; -; mRNA.
EMBL; M20010; AAA39503.1; -; mRNA.
CCDS; CCDS29373.1; -. [P04370-1]
CCDS; CCDS29374.1; -. [P04370-2]
CCDS; CCDS29376.1; -. [P04370-4]
CCDS; CCDS29377.1; -. [P04370-5]
CCDS; CCDS29378.1; -. [P04370-6]
CCDS; CCDS29379.1; -. [P04370-7]
CCDS; CCDS37875.1; -. [P04370-9]
PIR; A45421; MBMSB.
RefSeq; NP_001020416.1; NM_001025245.1. [P04370-2]
RefSeq; NP_001020422.1; NM_001025251.2. [P04370-4]
RefSeq; NP_001020425.1; NM_001025254.2. [P04370-9]
RefSeq; NP_001020426.1; NM_001025255.2. [P04370-5]
RefSeq; NP_001020427.1; NM_001025256.2. [P04370-6]
RefSeq; NP_001020429.1; NM_001025258.2. [P04370-7]
RefSeq; NP_001020430.1; NM_001025259.2. [P04370-8]
RefSeq; NP_034907.1; NM_010777.3. [P04370-1]
UniGene; Mm.252063; -.
UniGene; Mm.454459; -.
PDB; 1U3H; X-ray; 2.42 A; I/P=135-142.
PDB; 2LUG; NMR; -; A=206-245.
PDBsum; 1U3H; -.
PDBsum; 2LUG; -.
DisProt; DP01101; -.
ProteinModelPortal; P04370; -.
SMR; P04370; -.
BioGrid; 201336; 45.
IntAct; P04370; 31.
MINT; MINT-4101448; -.
STRING; 10090.ENSMUSP00000046185; -.
ChEMBL; CHEMBL1764935; -.
iPTMnet; P04370; -.
PhosphoSitePlus; P04370; -.
SwissPalm; P04370; -.
MaxQB; P04370; -.
PaxDb; P04370; -.
PeptideAtlas; P04370; -.
PRIDE; P04370; -.
Ensembl; ENSMUST00000047865; ENSMUSP00000046185; ENSMUSG00000041607. [P04370-1]
Ensembl; ENSMUST00000062446; ENSMUSP00000053495; ENSMUSG00000041607. [P04370-4]
Ensembl; ENSMUST00000075372; ENSMUSP00000074836; ENSMUSG00000041607. [P04370-7]
Ensembl; ENSMUST00000080658; ENSMUSP00000079488; ENSMUSG00000041607. [P04370-6]
Ensembl; ENSMUST00000091789; ENSMUSP00000089393; ENSMUSG00000041607. [P04370-2]
Ensembl; ENSMUST00000102812; ENSMUSP00000099876; ENSMUSG00000041607. [P04370-5]
Ensembl; ENSMUST00000114674; ENSMUSP00000110322; ENSMUSG00000041607. [P04370-9]
Ensembl; ENSMUST00000143506; ENSMUSP00000138313; ENSMUSG00000041607. [P04370-3]
GeneID; 17196; -.
KEGG; mmu:17196; -.
UCSC; uc008fts.1; mouse. [P04370-1]
UCSC; uc008ftu.1; mouse. [P04370-4]
UCSC; uc008ftv.1; mouse. [P04370-9]
UCSC; uc008ftw.1; mouse. [P04370-5]
UCSC; uc008fty.1; mouse. [P04370-7]
UCSC; uc029tqh.1; mouse. [P04370-14]
CTD; 4155; -.
MGI; MGI:96925; Mbp.
eggNOG; ENOG410IIUJ; Eukaryota.
eggNOG; ENOG4111PMJ; LUCA.
GeneTree; ENSGT00390000014772; -.
HOVERGEN; HBG008347; -.
InParanoid; P04370; -.
KO; K17269; -.
OrthoDB; EOG091G11QQ; -.
PhylomeDB; P04370; -.
TreeFam; TF333391; -.
ChiTaRS; Mbp; mouse.
PMAP-CutDB; P04370; -.
PRO; PR:P04370; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000041607; -.
CleanEx; MM_MBP; -.
ExpressionAtlas; P04370; baseline and differential.
Genevisible; P04370; MM.
GO; GO:0071944; C:cell periphery; IDA:MGI.
GO; GO:0042995; C:cell projection; IDA:MGI.
GO; GO:0043218; C:compact myelin; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0033269; C:internode region of axon; IDA:MGI.
GO; GO:0005622; C:intracellular; ISO:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
GO; GO:0043234; C:protein complex; IDA:CAFA.
GO; GO:0005516; F:calmodulin binding; IPI:CAFA.
GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
GO; GO:0019911; F:structural constituent of myelin sheath; IBA:GO_Central.
GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
GO; GO:0035633; P:maintenance of permeability of blood-brain barrier; ISO:MGI.
GO; GO:0000165; P:MAPK cascade; ISO:MGI.
GO; GO:0061024; P:membrane organization; IDA:MGI.
GO; GO:0042552; P:myelination; IDA:MGI.
GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; ISO:MGI.
GO; GO:1904209; P:positive regulation of chemokine (C-C motif) ligand 2 secretion; ISO:MGI.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; ISO:MGI.
GO; GO:1904685; P:positive regulation of metalloendopeptidase activity; ISO:MGI.
GO; GO:0009636; P:response to toxic substance; IDA:MGI.
GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
GO; GO:0021762; P:substantia nigra development; IEA:Ensembl.
InterPro; IPR000548; Myelin_BP.
PANTHER; PTHR11429; PTHR11429; 1.
Pfam; PF01669; Myelin_MBP; 1.
PRINTS; PR00212; MYELINMBP.
PROSITE; PS00569; MYELIN_MBP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing;
Autoimmune encephalomyelitis; Cell membrane; Citrullination;
Complete proteome; Cytoplasm; Direct protein sequencing; Membrane;
Methylation; Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 250 Myelin basic protein.
/FTId=PRO_0000158991.
MOD_RES 31 31 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 40 40 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 141 141 Phosphoserine.
{ECO:0000250|UniProtKB:P02687}.
MOD_RES 144 144 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 146 146 Phosphotyrosine.
{ECO:0000250|UniProtKB:P02688}.
MOD_RES 149 149 Phosphothreonine.
{ECO:0000250|UniProtKB:P02688}.
MOD_RES 151 151 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 152 152 Phosphothreonine.
{ECO:0000250|UniProtKB:P02688}.
MOD_RES 157 157 Citrulline. {ECO:0000250}.
MOD_RES 163 163 Citrulline. {ECO:0000250}.
MOD_RES 167 167 Phosphothreonine.
{ECO:0000244|PubMed:16452087,
ECO:0000244|PubMed:21183079}.
MOD_RES 172 172 Phosphoserine.
{ECO:0000244|PubMed:15648052,
ECO:0000244|PubMed:21183079}.
MOD_RES 175 175 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 181 181 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 188 188 Phosphoserine.
{ECO:0000250|UniProtKB:P02687}.
MOD_RES 197 197 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 199 199 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 206 206 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 211 211 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 226 226 Phosphothreonine.
{ECO:0000250|UniProtKB:P02688}.
MOD_RES 229 229 Phosphothreonine.
{ECO:0000244|PubMed:16452087,
ECO:0000244|PubMed:21183079}.
MOD_RES 234 234 Deamidated glutamine. {ECO:0000250}.
MOD_RES 239 239 Citrulline. {ECO:0000250}.
MOD_RES 241 241 Phosphoserine.
{ECO:0000250|UniProtKB:P02687}.
MOD_RES 245 245 Phosphoserine; by UHMK1.
{ECO:0000250|UniProtKB:P02687}.
MOD_RES 250 250 Citrulline. {ECO:0000250}.
VAR_SEQ 1 133 Missing (in isoform 4, isoform 5, isoform
6, isoform 7, isoform 8, isoform 9,
isoform 10, isoform 11, isoform 12 and
isoform 13).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:1692584,
ECO:0000303|PubMed:2433693}.
/FTId=VSP_003312.
VAR_SEQ 48 250 EADAIQNNGTSAEDTAVTDSKHTADPKNNWQGAHPADPGNR
PHLIRLFSRDAPGREDNTFKDRPSESDELQTIQEDPTAASG
GLDVMASQKRPSQRSKYLATASTMDHARHGFLPRHRDTGIL
DSIGRFFSGDRGAPKRGSGKDSHTRTTHYGSLPQKSQHGRT
QDENPVVHFFKNIVTPRTPPPSQGKGGRDSRSGSPMARR
-> LTHENYPLWLPAPEVAARPDPR (in isoform 3).
{ECO:0000303|PubMed:7680345}.
/FTId=VSP_003313.
VAR_SEQ 190 190 K -> KVPWLKQSRSPLPSHARSRPGLCHMYK (in
isoform 4, isoform 6, isoform 9, isoform
11 and isoform 12).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2433693}.
/FTId=VSP_003315.
VAR_SEQ 191 250 DSHTRTTHYGSLPQKSQHGRTQDENPVVHFFKNIVTPRTPP
PSQGKGGRDSRSGSPMARR -> VSSEP (in isoform
2). {ECO:0000303|PubMed:1279125,
ECO:0000303|PubMed:7680345}.
/FTId=VSP_003314.
VAR_SEQ 236 236 K -> KDFVPGDHHVNVSVVTVSFSSSQGRGLSLSRFSWGA
EGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTLSKIFKL
(in isoform 10). {ECO:0000305}.
/FTId=VSP_003317.
VAR_SEQ 236 236 K -> KDFVPGDHHVNVSVVTVSFSSSQGRGLSLSRFSW
(in isoform 11). {ECO:0000305}.
/FTId=VSP_003316.
VAR_SEQ 236 236 K -> KGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKG
FKGAYDAQGTLSKIFKL (in isoform 4 and
isoform 5). {ECO:0000305}.
/FTId=VSP_003319.
VAR_SEQ 236 236 K -> KGRGLSLSRFSW (in isoform 6 and
isoform 8). {ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:1692584,
ECO:0000303|PubMed:2433693}.
/FTId=VSP_003318.
VAR_SEQ 236 236 K -> KGAEGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTL
SKIFKL (in isoform 7 and isoform 9).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2433693}.
/FTId=VSP_003320.
CONFLICT 204 205 QK -> HN (in Ref. 15). {ECO:0000305}.
STRAND 209 211 {ECO:0000244|PDB:2LUG}.
HELIX 216 225 {ECO:0000244|PDB:2LUG}.
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


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