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Myelin basic protein (MBP) (Myelin A1 protein) (Myelin membrane encephalitogenic protein)

 MBP_HUMAN               Reviewed;         304 AA.
P02686; A4FU54; A6NI84; A8MY86; A8MYL4; B3KY66; B7ZKS2; B7ZKS4;
Q15337; Q15338; Q15339; Q15340; Q59GX3; Q65ZS4; Q6AI64; Q6FH37;
Q6FI04; Q6PK23;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
18-OCT-2001, sequence version 3.
20-JUN-2018, entry version 207.
RecName: Full=Myelin basic protein;
Short=MBP;
AltName: Full=Myelin A1 protein;
AltName: Full=Myelin membrane encephalitogenic protein;
Name=MBP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
PROTEIN SEQUENCE (ISOFORM 5).
PubMed=4108501; DOI=10.1042/bj1230057;
Carnegie P.R.;
"Amino acid sequence of the encephalitogenic basic protein from human
myelin.";
Biochem. J. 123:57-67(1971).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
TISSUE=Embryonic spinal cord;
PubMed=2427738; DOI=10.1002/jnr.490160120;
Roth H.J., Kronquist K.E., Pretorius P.J., Crandall B.F.,
Campagnoni A.T.;
"Isolation and characterization of a cDNA coding for a novel human
17.3K myelin basic protein (MBP) variant.";
J. Neurosci. Res. 16:227-238(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 5).
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5 AND 6).
TISSUE=Embryonic spinal cord;
PubMed=2442403; DOI=10.1002/jnr.490170402;
Roth H.J., Kronquist K.E., de Rosbo N., Crandall B.F.,
Campagnoni A.T.;
"Evidence for the expression of four myelin basic protein variants in
the developing human spinal cord through cDNA cloning.";
J. Neurosci. Res. 17:321-328(1987).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 3; 4; 5 AND 6).
PubMed=2472816;
Streicher R., Stoffel W.;
"The organization of the human myelin basic protein gene. Comparison
with the mouse gene.";
Biol. Chem. Hoppe-Seyler 370:503-510(1989).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), AND TISSUE
SPECIFICITY.
TISSUE=Brain;
PubMed=7504278; DOI=10.1073/pnas.90.22.10695;
Pribyl T.M., Campagnoni C.W., Kampf K., Kashima T., Handley V.W.,
McMahon J., Campagnoni A.T.;
"The human myelin basic protein gene is included within a 179-kilobase
transcription unit: expression in the immune and central nervous
systems.";
Proc. Natl. Acad. Sci. U.S.A. 90:10695-10699(1993).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3), FUNCTION, DIMERIZATION,
AND MUTAGENESIS.
PubMed=8544862; DOI=10.1016/0161-5890(95)00066-6;
Nye S.H., Pelfrey C.M., Burkwit J.J., Voskuhl R.R., Lenardo M.J.,
Mueller J.P.;
"Purification of immunologically active recombinant 21.5 kDa isoform
of human myelin basic protein.";
Mol. Immunol. 32:1131-1141(1995).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Amygdala;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Hippocampus, and Subthalamic nucleus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 5 AND 6).
TISSUE=Brain, Lung, and Skin;
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).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 135-192.
PubMed=1689270; DOI=10.1016/0888-7543(90)90443-X;
Boylan K.B., Ayres T.M., Popko B., Takahashi N., Hood L.E.,
Prusiner S.B.;
"Repetitive DNA (TGGA)n 5' to the human myelin basic protein gene: a
new form of oligonucleotide repetitive sequence showing length
polymorphism.";
Genomics 6:16-22(1990).
[15]
PROTEIN SEQUENCE OF 135-178 AND 224-304 (ISOFORM 3), AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=2426402; DOI=10.1111/j.1471-4159.1986.tb04544.x;
Scoble H.A., Whitaker J.N., Biemann K.;
"Analysis of the primary sequence of human myelin basic protein
peptides 1-44 and 90-170 by fast atom bombardment mass spectrometry.";
J. Neurochem. 47:614-616(1986).
[16]
PROTEIN SEQUENCE OF 148-304 (ISOFORM 5), AND CITRULLINATION AT
ARG-159; ARG-165; ARG-256; ARG-264; ARG-293 AND ARG-304.
TISSUE=Brain;
PubMed=2466844;
Wood D.D., Moscarello M.A.;
"The isolation, characterization, and lipid-aggregating properties of
a citrulline containing myelin basic protein.";
J. Biol. Chem. 264:5121-5127(1989).
[17]
PROTEIN SEQUENCE OF 156-172 AND 302-304, AND CHARACTERIZATION OF C8.
TISSUE=Brain;
PubMed=7574672; DOI=10.1006/abbi.1995.1449;
Boulias C., Pang H., Mastronardi F., Moscarello M.A.;
"The isolation and characterization of four myelin basic proteins from
the unbound fraction during CM52 chromatography.";
Arch. Biochem. Biophys. 322:174-182(1995).
[18]
PROTEIN SEQUENCE OF 179-223 (ISOFORM 5), AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=6201481;
Gibson B.W., Gilliom R.D., Whitaker J.N., Biemann K.;
"Amino acid sequence of human myelin basic protein peptide 45-89 as
determined by mass spectrometry.";
J. Biol. Chem. 259:5028-5031(1984).
[19]
PROTEIN SEQUENCE OF 179-222 (ISOFORM 5), AND SEQUENCE REVISION.
Shapira R., McKneally S.S., Chou F., Kibler R.F.;
"Encephalitogenic fragment of myelin basic protein. Amino acid
sequence of bovine, rabbit, guinea pig, monkey, and human fragments.";
J. Biol. Chem. 246:4630-4640(1971).
[20]
PROTEIN SEQUENCE OF 246-269 (ISOFORM 3), AND ENCEPHALITOGENIC PEPTIDE.
PubMed=4099924;
Lennon V.A., Wilks A.V., Carnegie P.R.;
"Immunologic properties of the main encephalitogenic peptide from the
basic protein of human myelin.";
J. Immunol. 105:1223-1230(1970).
[21]
PARTIAL PROTEIN SEQUENCE.
TISSUE=Brain;
PubMed=7685161; DOI=10.1006/bbrc.1993.1540;
Proost P., Van Damme J., Opdenakker G.;
"Leukocyte gelatinase B cleavage releases encephalitogens from human
myelin basic protein.";
Biochem. Biophys. Res. Commun. 192:1175-1181(1993).
[22]
METHYLATION AT ARG-241.
PubMed=5128665; DOI=10.1042/bj1230069;
Baldwin G.S., Carnegie P.R.;
"Isolation and partial characterization of methylated arginines from
the encephalitogenic basic protein of myelin.";
Biochem. J. 123:69-74(1971).
[23]
PHOSPHORYLATION BY MAPK11; MAPK12 AND MAPK14.
PubMed=9430721; DOI=10.1074/jbc.273.3.1741;
Enslen H., Raingeaud J., Davis R.J.;
"Selective activation of p38 mitogen-activated protein (MAP) kinase
isoforms by the MAP kinase kinases MKK3 and MKK6.";
J. Biol. Chem. 273:1741-1748(1998).
[24]
PHOSPHORYLATION AT SER-299 BY UMHK1.
PubMed=10880969; DOI=10.1046/j.1432-1327.2000.01493.x;
Maucuer A., Le Caer J.P., Manceau V., Sobel A.;
"Specific Ser-Pro phosphorylation by the RNA-recognition motif
containing kinase KIS.";
Eur. J. Biochem. 267:4456-4464(2000).
[25]
PHOSPHORYLATION BY TAOK2.
PubMed=10660600; DOI=10.1074/jbc.275.6.4311;
Moore T.M., Garg R., Johnson C., Coptcoat M.J., Ridley A.J.,
Morris J.D.H.;
"PSK, a novel STE20-like kinase derived from prostatic carcinoma that
activates the JNK MAPK pathway and regulates actin cytoskeletal
organisation.";
J. Biol. Chem. 275:4311-4322(2000).
[26]
PHOSPHORYLATION BY MINK1.
PubMed=16337592; DOI=10.1016/j.molcel.2005.10.038;
Nicke B., Bastien J., Khanna S.J., Warne P.H., Cowling V., Cook S.J.,
Peters G., Delpuech O., Schulze A., Berns K., Mullenders J.,
Beijersbergen R.L., Bernards R., Ganesan T.S., Downward J.,
Hancock D.C.;
"Involvement of MINK, a Ste20 family kinase, in Ras oncogene-induced
growth arrest in human ovarian surface epithelial cells.";
Mol. Cell 20:673-685(2005).
[27]
PHOSPHORYLATION BY VRK2.
PubMed=16704422; DOI=10.1111/j.1742-4658.2006.05256.x;
Blanco S., Klimcakova L., Vega F.M., Lazo P.A.;
"The subcellular localization of vaccinia-related kinase-2 (VRK2)
isoforms determines their different effect on p53 stability in tumour
cell lines.";
FEBS J. 273:2487-2504(2006).
[28]
PHOSPHORYLATION BY TAOK2.
PubMed=17158878; DOI=10.1074/jbc.M608336200;
Zihni C., Mitsopoulos C., Tavares I.A., Baum B., Ridley A.J.,
Morris J.D.;
"Prostate-derived sterile 20-like kinase 1-alpha induces apoptosis.
JNK-and caspase-dependent nuclear localization is a requirement for
membrane blebbing.";
J. Biol. Chem. 282:6484-6493(2007).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[30]
SUBCELLULAR LOCATION (ISOFORM 3).
PubMed=22609403; DOI=10.1016/j.bbrc.2012.05.051;
Smith G.S., Seymour L.V., Boggs J.M., Harauz G.;
"The 21.5-kDa isoform of myelin basic protein has a non-traditional
PY-nuclear-localization signal.";
Biochem. Biophys. Res. Commun. 422:670-675(2012).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[32]
CITRULLINATION AT ARG-167; ARG-199; ARG-231; ARG-264; ARG-296 AND
ARG-303.
PubMed=23828821; DOI=10.1002/pmic.201300064;
Jin Z., Fu Z., Yang J., Troncosco J., Everett A.D., Van Eyk J.E.;
"Identification and Characterization of citrulline-modified brain
proteins by combining HCD and CID fragmentation.";
Proteomics 13:2682-2691(2013).
[33]
STRUCTURE BY NMR OF 135-148, CLEAVAGE OF INITIATOR METHIONINE
(ISOFORMS 3; 4; 5 AND 6), AND ACETYLATION AT ALA-2 (ISOFORMS 3; 4; 5
AND 6).
PubMed=7544282; DOI=10.1111/j.1432-1033.1995.tb20745.x;
Mendz G.L., Barden J.A., Martenson R.E.;
"Conformation of a tetradecapeptide epitope of myelin basic protein.";
Eur. J. Biochem. 231:659-666(1995).
[34]
3D-STRUCTURE MODELING OF 135-279 (ISOFORM 5).
PubMed=9020143; DOI=10.1074/jbc.272.7.4269;
Ridsdale R.A., Beniac D.R., Tompkins T.A., Moscarello M.A., Harauz G.;
"Three-dimensional structure of myelin basic protein. II. Molecular
modeling and considerations of predicted structures in multiple
sclerosis.";
J. Biol. Chem. 272:4269-4275(1997).
[35]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 218-237 IN COMPLEX WITH
HLA-DRA/HLA-DRB5 HETERODIMER.
PubMed=11080454; DOI=10.1006/jmbi.2000.4198;
Li Y., Li H., Martin R., Mariuzza R.A.;
"Structural basis for the binding of an immunodominant peptide from
myelin basic protein in different registers by two HLA-DR2 proteins.";
J. Mol. Biol. 304:177-188(2000).
[36]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 221-233 IN COMPLEX WITH
HLA-DRA/HLA-DRB5 HETERODIMER AND STREPTOCOCCUS PYOGENES SPEC PEPTIDE.
PubMed=11163233; DOI=10.1016/S1074-7613(01)00092-9;
Li Y., Li H., Dimasi N., McCormick J.K., Martin R., Schuck P.,
Schlievert P.M., Mariuzza R.A.;
"Crystal structure of a superantigen bound to the high-affinity, zinc-
dependent site on MHC class II.";
Immunity 14:93-104(2001).
[37]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 221-233 IN COMPLEX WITH
HLA-DRA/HLA-DRB5 HETERODIMER AND TRAC.
PubMed=16079912; DOI=10.1038/sj.emboj.7600771;
Li Y., Huang Y., Lue J., Quandt J.A., Martin R., Mariuzza R.A.;
"Structure of a human autoimmune TCR bound to a myelin basic protein
self-peptide and a multiple sclerosis-associated MHC class II
molecule.";
EMBO J. 24:2968-2979(2005).
-!- FUNCTION: The classic group of MBP isoforms (isoform 4-isoform 14)
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 smaller isoforms might have an important role
in remyelination of denuded axons in multiple sclerosis. 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 with
optional post-translational modifications give a wide spectrum of
isomers, with each of them potentially having a specialized
function. Induces T-cell proliferation.
{ECO:0000269|PubMed:8544862}.
-!- SUBUNIT: Homodimer. Isoform 3 exists as a homodimer.
{ECO:0000269|PubMed:11080454, ECO:0000269|PubMed:11163233,
ECO:0000269|PubMed:16079912}.
-!- INTERACTION:
P0DP25:CALM3; NbExp=2; IntAct=EBI-15973992, EBI-397435;
Q9GZU7:CTDSP1; NbExp=3; IntAct=EBI-947410, EBI-751587;
Q8I629:PF3D7_1201600 (xeno); NbExp=2; IntAct=EBI-7056012, EBI-7056031;
Q64702:Plk4 (xeno); NbExp=2; IntAct=EBI-7056012, EBI-2552433;
-!- SUBCELLULAR LOCATION: Myelin membrane; Peripheral membrane
protein; Cytoplasmic side. Note=Cytoplasmic side of myelin.
-!- SUBCELLULAR LOCATION: Isoform 3: Nucleus
{ECO:0000269|PubMed:22609403}. Note=Targeted to nucleus in
oligodendrocytes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=Golli-MBP1, HOG7;
IsoId=P02686-1; Sequence=Displayed;
Name=2; Synonyms=Golli-MBP2, HOG5;
IsoId=P02686-2; Sequence=VSP_003311;
Name=3; Synonyms=MBP1, 21.5 kDa;
IsoId=P02686-3; Sequence=VSP_003308, VSP_003309;
Note=Initiator Met-1 is removed. Contains a N-acetylalanine at
position 2. Contains a non-traditional PY nuclear localization
signal. Mutagenesis of Cys-81 to Ser prevents dimerization.
{ECO:0000269|PubMed:7544282};
Name=4; Synonyms=MBP2, 20.2 kDa;
IsoId=P02686-4; Sequence=VSP_003308, VSP_003309, VSP_003310;
Note=Initiator Met-1 is removed. Contains a N-acetylalanine at
position 2. {ECO:0000269|PubMed:7544282};
Name=5; Synonyms=MBP3, 18.5 kDa;
IsoId=P02686-5; Sequence=VSP_003308;
Note=Initiator Met-1 is removed. Contains a N-acetylalanine at
position 2. {ECO:0000269|PubMed:7544282};
Name=6; Synonyms=MBP4, 17.2 kDa;
IsoId=P02686-6; Sequence=VSP_003308, VSP_003310;
Note=Initiator Met-1 is removed. Contains a N-acetylalanine at
position 2. {ECO:0000269|PubMed:7544282};
-!- TISSUE SPECIFICITY: MBP isoforms are found in both the central and
the peripheral nervous system, whereas Golli-MBP isoforms are
expressed in fetal thymus, spleen and spinal cord, as well as in
cell lines derived from the immune system.
{ECO:0000269|PubMed:7504278}.
-!- DEVELOPMENTAL STAGE: Expression begins abruptly in 14-16 week old
fetuses. Even smaller isoforms seem to be produced during
embryogenesis; some of these persisting in the adult. Isoform 4
expression is more evident at 16 weeks and its relative proportion
declines thereafter.
-!- PTM: Several charge isomers of MBP; C1 (the most cationic, least
modified, and most abundant form), C2, C3, C4, C5, C6, C7, C8-A
and C8-B (the least cationic form); are produced as a result of
optional PTM, such as phosphorylation, deamidation of glutamine or
asparagine, arginine citrullination and methylation. C8-A and C8-B
contain each two mass isoforms termed C8-A(H), C8-A(L), C8-B(H)
and C8-B(L), (H) standing for higher and (L) for lower molecular
weight. C3, C4 and C5 are phosphorylated. The ratio of methylated
arginine residues decreases during aging, making the protein more
cationic. {ECO:0000269|PubMed:23828821,
ECO:0000269|PubMed:2466844, ECO:0000269|PubMed:5128665}.
-!- PTM: The N-terminal alanine is acetylated (isoform 3, isoform 4,
isoform 5 and isoform 6).
-!- PTM: Arg-241 was found to be 6% monomethylated and 60%
symmetrically dimethylated.
-!- PTM: Phosphorylated by TAOK2, VRK2, MAPK11, MAPK12, MAPK14 and
MINK1.
-!- DISEASE: Note=The reduction in the surface charge of citrullinated
and/or methylated MBP could result in a weakened attachment to the
myelin membrane. This mechanism could be operative in
demyelinating diseases such as chronical multiple sclerosis (MS),
and fulminating MS (Marburg disease).
-!- SIMILARITY: Belongs to the myelin basic protein family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC41944.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. The C-terminus contains a Histidine tag.; Evidence={ECO:0000305};
Sequence=BAD92223.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAH10359.1; Type=Miscellaneous discrepancy; Note=wrong intron-exon boundaries.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Myelin basic protein entry;
URL="https://en.wikipedia.org/wiki/Myelin_basic_protein";
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EMBL; M30047; AAA59559.1; -; mRNA.
EMBL; M20009; AAA59561.1; -; mRNA.
EMBL; M13577; AAA59562.1; -; mRNA.
EMBL; M30516; AAA59563.1; -; mRNA.
EMBL; M30515; AAA59564.1; -; mRNA.
EMBL; X17286; CAA35179.1; -; Genomic_DNA.
EMBL; X17287; CAA35179.1; JOINED; Genomic_DNA.
EMBL; X17290; CAA35179.1; JOINED; Genomic_DNA.
EMBL; X17288; CAA35179.1; JOINED; Genomic_DNA.
EMBL; X17369; CAA35179.1; JOINED; Genomic_DNA.
EMBL; X17289; CAA35179.1; JOINED; Genomic_DNA.
EMBL; L18862; AAA72008.1; -; Genomic_DNA.
EMBL; L18864; AAA72009.1; -; Genomic_DNA.
EMBL; L18865; AAA72010.1; -; Genomic_DNA.
EMBL; L18866; AAA72011.1; -; Genomic_DNA.
EMBL; L41657; AAC41944.1; ALT_SEQ; Genomic_DNA.
EMBL; CR536534; CAG38771.1; -; mRNA.
EMBL; CR541919; CAG46717.1; -; mRNA.
EMBL; CR627018; CAH10359.1; ALT_SEQ; mRNA.
EMBL; AK128770; BAG54728.1; -; mRNA.
EMBL; AK128788; BAG54734.1; -; mRNA.
EMBL; AB208986; BAD92223.1; ALT_INIT; mRNA.
EMBL; AC018529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC093330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC008749; AAH08749.3; -; mRNA.
EMBL; BC065248; AAH65248.1; -; mRNA.
EMBL; BC080654; AAH80654.1; -; mRNA.
EMBL; BC101771; AAI01772.1; -; mRNA.
EMBL; BC101773; AAI01774.1; -; mRNA.
EMBL; BC143348; AAI43349.1; -; mRNA.
EMBL; BC143350; AAI43351.1; -; mRNA.
EMBL; M63599; AAA59560.1; -; Genomic_DNA.
CCDS; CCDS12011.1; -. [P02686-4]
CCDS; CCDS32847.1; -. [P02686-3]
CCDS; CCDS42448.1; -. [P02686-6]
CCDS; CCDS42449.1; -. [P02686-5]
CCDS; CCDS42450.1; -. [P02686-2]
PIR; A49635; A49635.
PIR; S10482; MBHUB.
RefSeq; NP_001020252.1; NM_001025081.1. [P02686-3]
RefSeq; NP_001020261.1; NM_001025090.1. [P02686-5]
RefSeq; NP_001020263.1; NM_001025092.1. [P02686-6]
RefSeq; NP_001020271.1; NM_001025100.1. [P02686-2]
RefSeq; NP_001020272.1; NM_001025101.1. [P02686-1]
RefSeq; NP_002376.1; NM_002385.2. [P02686-4]
RefSeq; XP_016881269.1; XM_017025780.1. [P02686-2]
UniGene; Hs.551713; -.
PDB; 1BX2; X-ray; 2.60 A; C/F=217-231.
PDB; 1FV1; X-ray; 1.90 A; C/F=218-237.
PDB; 1HQR; X-ray; 3.20 A; C=221-233.
PDB; 1K2D; X-ray; 2.20 A; P=135-144.
PDB; 1QCL; Model; -; A=135-304.
PDB; 1YMM; X-ray; 3.50 A; C=217-240.
PDB; 1ZGL; X-ray; 2.80 A; C/F/I/L=221-233.
PDBsum; 1BX2; -.
PDBsum; 1FV1; -.
PDBsum; 1HQR; -.
PDBsum; 1K2D; -.
PDBsum; 1QCL; -.
PDBsum; 1YMM; -.
PDBsum; 1ZGL; -.
DisProt; DP00236; -.
ProteinModelPortal; P02686; -.
SMR; P02686; -.
BioGrid; 110325; 87.
DIP; DIP-36624N; -.
IntAct; P02686; 17.
MINT; P02686; -.
iPTMnet; P02686; -.
PhosphoSitePlus; P02686; -.
SwissPalm; P02686; -.
BioMuta; MBP; -.
EPD; P02686; -.
MaxQB; P02686; -.
PeptideAtlas; P02686; -.
PRIDE; P02686; -.
ProteomicsDB; 51547; -.
ProteomicsDB; 51548; -. [P02686-2]
ProteomicsDB; 51549; -. [P02686-3]
ProteomicsDB; 51550; -. [P02686-4]
ProteomicsDB; 51551; -. [P02686-5]
ProteomicsDB; 51552; -. [P02686-6]
DNASU; 4155; -.
Ensembl; ENST00000355994; ENSP00000348273; ENSG00000197971. [P02686-1]
Ensembl; ENST00000359645; ENSP00000352667; ENSG00000197971. [P02686-4]
Ensembl; ENST00000382582; ENSP00000372025; ENSG00000197971. [P02686-3]
Ensembl; ENST00000397860; ENSP00000380958; ENSG00000197971. [P02686-2]
Ensembl; ENST00000397863; ENSP00000380961; ENSG00000197971. [P02686-2]
Ensembl; ENST00000397865; ENSP00000380963; ENSG00000197971. [P02686-6]
Ensembl; ENST00000397866; ENSP00000380964; ENSG00000197971. [P02686-5]
Ensembl; ENST00000580402; ENSP00000462223; ENSG00000197971. [P02686-1]
GeneID; 4155; -.
KEGG; hsa:4155; -.
UCSC; uc002lml.4; human. [P02686-1]
CTD; 4155; -.
DisGeNET; 4155; -.
EuPathDB; HostDB:ENSG00000197971.14; -.
GeneCards; MBP; -.
HGNC; HGNC:6925; MBP.
HPA; CAB002300; -.
HPA; HPA049222; -.
HPA; HPA064368; -.
MIM; 159430; gene.
neXtProt; NX_P02686; -.
OpenTargets; ENSG00000197971; -.
PharmGKB; PA30667; -.
GeneTree; ENSGT00390000014772; -.
HOVERGEN; HBG008347; -.
InParanoid; P02686; -.
KO; K17269; -.
OMA; LMASQKR; -.
OrthoDB; EOG091G11QQ; -.
PhylomeDB; P02686; -.
TreeFam; TF333391; -.
SIGNOR; P02686; -.
ChiTaRS; MBP; human.
EvolutionaryTrace; P02686; -.
GeneWiki; Myelin_basic_protein; -.
GenomeRNAi; 4155; -.
PMAP-CutDB; A8MYL4; -.
PRO; PR:P02686; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000197971; -.
CleanEx; HS_MBP; -.
ExpressionAtlas; P02686; baseline and differential.
Genevisible; P02686; HS.
GO; GO:0071944; C:cell periphery; IBA:GO_Central.
GO; GO:0043218; C:compact myelin; IBA:GO_Central.
GO; GO:0033269; C:internode region of axon; IBA:GO_Central.
GO; GO:0005622; C:intracellular; IDA:CAFA.
GO; GO:0043209; C:myelin sheath; IDA:CAFA.
GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
GO; GO:0005516; F:calmodulin binding; IPI:CAFA.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0019911; F:structural constituent of myelin sheath; IBA:GO_Central.
GO; GO:0008366; P:axon ensheathment; TAS:ProtInc.
GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0035633; P:maintenance of permeability of blood-brain barrier; IDA:CAFA.
GO; GO:0000165; P:MAPK cascade; IDA:CAFA.
GO; GO:0061024; P:membrane organization; IEA:Ensembl.
GO; GO:0042552; P:myelination; IBA:GO_Central.
GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; IDA:CAFA.
GO; GO:1904209; P:positive regulation of chemokine (C-C motif) ligand 2 secretion; IDA:CAFA.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; IDA:CAFA.
GO; GO:1904685; P:positive regulation of metalloendopeptidase activity; IDA:CAFA.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
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; Direct protein sequencing; Membrane; Methylation;
Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 304 Myelin basic protein.
/FTId=PRO_0000158990.
REGION 179 222 Induces experimental autoimmune
encephalomyelitis (EAE) 1.
REGION 246 256 Induces experimental autoimmune
encephalomyelitis (EAE) 2.
MOD_RES 96 96 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 141 141 Phosphoserine.
{ECO:0000250|UniProtKB:P02687}.
MOD_RES 146 146 Phosphoserine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 148 148 Phosphotyrosine.
{ECO:0000250|UniProtKB:P02688}.
MOD_RES 151 151 Phosphothreonine.
{ECO:0000250|UniProtKB:P02688}.
MOD_RES 153 153 Phosphoserine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 154 154 Phosphothreonine.
{ECO:0000250|UniProtKB:P02688}.
MOD_RES 159 159 Citrulline; in form C8.
{ECO:0000269|PubMed:2466844}.
MOD_RES 165 165 Citrulline; in form C8.
{ECO:0000269|PubMed:2466844}.
MOD_RES 167 167 Citrulline.
{ECO:0000269|PubMed:23828821}.
MOD_RES 169 169 Phosphothreonine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 174 174 Phosphoserine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 177 177 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 183 183 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 190 190 Phosphoserine.
{ECO:0000250|UniProtKB:P02687}.
MOD_RES 199 199 Citrulline.
{ECO:0000269|PubMed:23828821}.
MOD_RES 203 203 Phosphotyrosine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 210 210 Phosphoserine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 214 214 Phosphothreonine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 229 229 Phosphothreonine.
{ECO:0000250|UniProtKB:P02688}.
MOD_RES 231 231 Citrulline.
{ECO:0000269|PubMed:23828821}.
MOD_RES 232 232 Phosphothreonine.
{ECO:0000250|UniProtKB:P02687}.
MOD_RES 237 237 Deamidated glutamine. {ECO:0000250}.
MOD_RES 241 241 Omega-N-methylarginine; alternate.
{ECO:0000269|PubMed:5128665}.
MOD_RES 241 241 Symmetric dimethylarginine; alternate.
{ECO:0000269|PubMed:5128665}.
MOD_RES 249 249 Phosphoserine.
{ECO:0000250|UniProtKB:P25274}.
MOD_RES 256 256 Citrulline; in form C8.
{ECO:0000269|PubMed:2466844}.
MOD_RES 264 264 Citrulline; in form C8.
{ECO:0000269|PubMed:23828821,
ECO:0000269|PubMed:2466844}.
MOD_RES 281 281 Deamidated glutamine. {ECO:0000250}.
MOD_RES 293 293 Citrulline; in form C8.
{ECO:0000269|PubMed:2466844}.
MOD_RES 295 295 Phosphoserine.
{ECO:0000250|UniProtKB:P02687}.
MOD_RES 296 296 Citrulline.
{ECO:0000269|PubMed:23828821}.
MOD_RES 299 299 Phosphoserine; by UHMK1.
{ECO:0000269|PubMed:10880969}.
MOD_RES 303 303 Citrulline.
{ECO:0000269|PubMed:23828821}.
MOD_RES 304 304 Citrulline; in form C8.
{ECO:0000269|PubMed:2466844}.
VAR_SEQ 1 133 Missing (in isoform 3, isoform 4, isoform
5 and isoform 6).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2425357,
ECO:0000303|PubMed:2427738,
ECO:0000303|PubMed:2442403,
ECO:0000303|PubMed:4108501,
ECO:0000303|Ref.8}.
/FTId=VSP_003308.
VAR_SEQ 192 192 K -> KVPWLKPGRSPLPSHARSQPGLCNMYK (in
isoform 3 and isoform 4).
{ECO:0000303|PubMed:2425357,
ECO:0000303|PubMed:2442403}.
/FTId=VSP_003309.
VAR_SEQ 193 304 DSHHPARTAHYGSLPQKSHGRTQDENPVVHFFKNIVTPRTP
PPSQGKGRGLSLSRFSWGAEGQRPGFGYGGRASDYKSAHKG
FKGVDAQGTLSKIFKLGGRDSRSGSPMARR -> VSSEE
(in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.11}.
/FTId=VSP_003311.
VAR_SEQ 240 250 Missing (in isoform 4 and isoform 6).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2427738,
ECO:0000303|PubMed:2442403,
ECO:0000303|Ref.8}.
/FTId=VSP_003310.
CONFLICT 300 300 P -> T (in Ref. 8; CAG38771).
{ECO:0000305}.
SEQUENCE 304 AA; 33117 MW; 4AD7305C1D5434C4 CRC64;
MGNHAGKREL NAEKASTNSE TNRGESEKKR NLGELSRTTS EDNEVFGEAD ANQNNGTSSQ
DTAVTDSKRT ADPKNAWQDA HPADPGSRPH LIRLFSRDAP GREDNTFKDR PSESDELQTI
QEDSAATSES LDVMASQKRP SQRHGSKYLA TASTMDHARH GFLPRHRDTG ILDSIGRFFG
GDRGAPKRGS GKDSHHPART AHYGSLPQKS HGRTQDENPV VHFFKNIVTP RTPPPSQGKG
RGLSLSRFSW GAEGQRPGFG YGGRASDYKS AHKGFKGVDA QGTLSKIFKL GGRDSRSGSP
MARR


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