MBP_HUMAN
ID MBP_HUMAN Reviewed; 304 AA.
AC P02686; A4FU54; A6NI84; A8MY86; A8MYL4; B3KY66; B7ZKS2; B7ZKS4; Q15337;
AC Q15338; Q15339; Q15340; Q59GX3; Q65ZS4; Q6AI64; Q6FH37; Q6FI04; Q6PK23;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 3.
DT 03-AUG-2022, entry version 234.
DE RecName: Full=Myelin basic protein;
DE Short=MBP;
DE AltName: Full=Myelin A1 protein;
DE AltName: Full=Myelin membrane encephalitogenic protein;
GN Name=MBP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP PROTEIN SEQUENCE (ISOFORM 5).
RX PubMed=4108501; DOI=10.1042/bj1230057;
RA Carnegie P.R.;
RT "Amino acid sequence of the encephalitogenic basic protein from human
RT myelin.";
RL Biochem. J. 123:57-67(1971).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
RC TISSUE=Embryonic spinal cord;
RX PubMed=2427738; DOI=10.1002/jnr.490160120;
RA Roth H.J., Kronquist K.E., Pretorius P.J., Crandall B.F., Campagnoni A.T.;
RT "Isolation and characterization of a cDNA coding for a novel human 17.3K
RT myelin basic protein (MBP) variant.";
RL J. Neurosci. Res. 16:227-238(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 5).
RX PubMed=2425357; DOI=10.1073/pnas.83.13.4962;
RA Kamholz J., de Ferra F., Puckett C., Lazzarini R.A.;
RT "Identification of three forms of human myelin basic protein by cDNA
RT cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:4962-4966(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5 AND 6).
RC TISSUE=Embryonic spinal cord;
RX PubMed=2442403; DOI=10.1002/jnr.490170402;
RA Roth H.J., Kronquist K.E., de Rosbo N., Crandall B.F., Campagnoni A.T.;
RT "Evidence for the expression of four myelin basic protein variants in the
RT developing human spinal cord through cDNA cloning.";
RL J. Neurosci. Res. 17:321-328(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 3; 4; 5 AND 6).
RX PubMed=2472816; DOI=10.1515/bchm3.1989.370.1.503;
RA Streicher R., Stoffel W.;
RT "The organization of the human myelin basic protein gene. Comparison with
RT the mouse gene.";
RL Biol. Chem. Hoppe-Seyler 370:503-510(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=7504278; DOI=10.1073/pnas.90.22.10695;
RA Pribyl T.M., Campagnoni C.W., Kampf K., Kashima T., Handley V.W.,
RA McMahon J., Campagnoni A.T.;
RT "The human myelin basic protein gene is included within a 179-kilobase
RT transcription unit: expression in the immune and central nervous systems.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:10695-10699(1993).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3), FUNCTION, DIMERIZATION, AND
RP MUTAGENESIS.
RX PubMed=8544862; DOI=10.1016/0161-5890(95)00066-6;
RA Nye S.H., Pelfrey C.M., Burkwit J.J., Voskuhl R.R., Lenardo M.J.,
RA Mueller J.P.;
RT "Purification of immunologically active recombinant 21.5 kDa isoform of
RT human myelin basic protein.";
RL Mol. Immunol. 32:1131-1141(1995).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Hippocampus, and Subthalamic nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 5 AND 6).
RC TISSUE=Brain, Lung, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 135-192.
RX PubMed=1689270; DOI=10.1016/0888-7543(90)90443-x;
RA Boylan K.B., Ayres T.M., Popko B., Takahashi N., Hood L.E., Prusiner S.B.;
RT "Repetitive DNA (TGGA)n 5' to the human myelin basic protein gene: a new
RT form of oligonucleotide repetitive sequence showing length polymorphism.";
RL Genomics 6:16-22(1990).
RN [15]
RP PROTEIN SEQUENCE OF 135-178 AND 224-304 (ISOFORM 3), AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=2426402; DOI=10.1111/j.1471-4159.1986.tb04544.x;
RA Scoble H.A., Whitaker J.N., Biemann K.;
RT "Analysis of the primary sequence of human myelin basic protein peptides 1-
RT 44 and 90-170 by fast atom bombardment mass spectrometry.";
RL J. Neurochem. 47:614-616(1986).
RN [16]
RP PROTEIN SEQUENCE OF 148-304 (ISOFORM 5), AND CITRULLINATION AT ARG-159;
RP ARG-165; ARG-256; ARG-264; ARG-293 AND ARG-304.
RC TISSUE=Brain;
RX PubMed=2466844; DOI=10.1016/s0021-9258(18)83707-3;
RA Wood D.D., Moscarello M.A.;
RT "The isolation, characterization, and lipid-aggregating properties of a
RT citrulline containing myelin basic protein.";
RL J. Biol. Chem. 264:5121-5127(1989).
RN [17]
RP PROTEIN SEQUENCE OF 156-172 AND 302-304, AND CHARACTERIZATION OF C8.
RC TISSUE=Brain;
RX PubMed=7574672; DOI=10.1006/abbi.1995.1449;
RA Boulias C., Pang H., Mastronardi F., Moscarello M.A.;
RT "The isolation and characterization of four myelin basic proteins from the
RT unbound fraction during CM52 chromatography.";
RL Arch. Biochem. Biophys. 322:174-182(1995).
RN [18]
RP PROTEIN SEQUENCE OF 179-223 (ISOFORM 5), AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=6201481; DOI=10.1016/s0021-9258(17)42950-4;
RA Gibson B.W., Gilliom R.D., Whitaker J.N., Biemann K.;
RT "Amino acid sequence of human myelin basic protein peptide 45-89 as
RT determined by mass spectrometry.";
RL J. Biol. Chem. 259:5028-5031(1984).
RN [19]
RP PROTEIN SEQUENCE OF 179-222 (ISOFORM 5), AND SEQUENCE REVISION.
RA Shapira R., McKneally S.S., Chou F., Kibler R.F.;
RT "Encephalitogenic fragment of myelin basic protein. Amino acid sequence of
RT bovine, rabbit, guinea pig, monkey, and human fragments.";
RL J. Biol. Chem. 246:4630-4640(1971).
RN [20]
RP PROTEIN SEQUENCE OF 246-269 (ISOFORM 3), AND ENCEPHALITOGENIC PEPTIDE.
RX PubMed=4099924;
RA Lennon V.A., Wilks A.V., Carnegie P.R.;
RT "Immunologic properties of the main encephalitogenic peptide from the basic
RT protein of human myelin.";
RL J. Immunol. 105:1223-1230(1970).
RN [21]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=7685161; DOI=10.1006/bbrc.1993.1540;
RA Proost P., Van Damme J., Opdenakker G.;
RT "Leukocyte gelatinase B cleavage releases encephalitogens from human myelin
RT basic protein.";
RL Biochem. Biophys. Res. Commun. 192:1175-1181(1993).
RN [22]
RP METHYLATION AT ARG-241.
RX PubMed=5128665; DOI=10.1042/bj1230069;
RA Baldwin G.S., Carnegie P.R.;
RT "Isolation and partial characterization of methylated arginines from the
RT encephalitogenic basic protein of myelin.";
RL Biochem. J. 123:69-74(1971).
RN [23]
RP PHOSPHORYLATION BY MAPK11; MAPK12 AND MAPK14.
RX PubMed=9430721; DOI=10.1074/jbc.273.3.1741;
RA Enslen H., Raingeaud J., Davis R.J.;
RT "Selective activation of p38 mitogen-activated protein (MAP) kinase
RT isoforms by the MAP kinase kinases MKK3 and MKK6.";
RL J. Biol. Chem. 273:1741-1748(1998).
RN [24]
RP PHOSPHORYLATION AT SER-299 BY UMHK1.
RX PubMed=10880969; DOI=10.1046/j.1432-1327.2000.01493.x;
RA Maucuer A., Le Caer J.P., Manceau V., Sobel A.;
RT "Specific Ser-Pro phosphorylation by the RNA-recognition motif containing
RT kinase KIS.";
RL Eur. J. Biochem. 267:4456-4464(2000).
RN [25]
RP PHOSPHORYLATION BY TAOK2.
RX PubMed=10660600; DOI=10.1074/jbc.275.6.4311;
RA Moore T.M., Garg R., Johnson C., Coptcoat M.J., Ridley A.J., Morris J.D.H.;
RT "PSK, a novel STE20-like kinase derived from prostatic carcinoma that
RT activates the JNK MAPK pathway and regulates actin cytoskeletal
RT organisation.";
RL J. Biol. Chem. 275:4311-4322(2000).
RN [26]
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=15100291; DOI=10.4049/jimmunol.172.9.5495;
RA Burster T., Beck A., Tolosa E., Marin-Esteban V., Roetzschke O., Falk K.,
RA Lautwein A., Reich M., Brandenburg J., Schwarz G., Wiendl H., Melms A.,
RA Lehmann R., Stevanovic S., Kalbacher H., Driessen C.;
RT "Cathepsin G, and not the asparagine-specific endoprotease, controls the
RT processing of myelin basic protein in lysosomes from human B lymphocytes.";
RL J. Immunol. 172:5495-5503(2004).
RN [27]
RP PHOSPHORYLATION BY MINK1.
RX PubMed=16337592; DOI=10.1016/j.molcel.2005.10.038;
RA Nicke B., Bastien J., Khanna S.J., Warne P.H., Cowling V., Cook S.J.,
RA Peters G., Delpuech O., Schulze A., Berns K., Mullenders J.,
RA Beijersbergen R.L., Bernards R., Ganesan T.S., Downward J., Hancock D.C.;
RT "Involvement of MINK, a Ste20 family kinase, in Ras oncogene-induced growth
RT arrest in human ovarian surface epithelial cells.";
RL Mol. Cell 20:673-685(2005).
RN [28]
RP PHOSPHORYLATION BY VRK2.
RX PubMed=16704422; DOI=10.1111/j.1742-4658.2006.05256.x;
RA Blanco S., Klimcakova L., Vega F.M., Lazo P.A.;
RT "The subcellular localization of vaccinia-related kinase-2 (VRK2) isoforms
RT determines their different effect on p53 stability in tumour cell lines.";
RL FEBS J. 273:2487-2504(2006).
RN [29]
RP PHOSPHORYLATION BY TAOK2.
RX PubMed=17158878; DOI=10.1074/jbc.m608336200;
RA Zihni C., Mitsopoulos C., Tavares I.A., Baum B., Ridley A.J., Morris J.D.;
RT "Prostate-derived sterile 20-like kinase 1-alpha induces apoptosis.
RT JNK- and caspase-dependent nuclear localization is a requirement for
RT membrane blebbing.";
RL J. Biol. Chem. 282:6484-6493(2007).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [31]
RP SUBCELLULAR LOCATION (ISOFORM 3).
RX PubMed=22609403; DOI=10.1016/j.bbrc.2012.05.051;
RA Smith G.S., Seymour L.V., Boggs J.M., Harauz G.;
RT "The 21.5-kDa isoform of myelin basic protein has a non-traditional PY-
RT nuclear-localization signal.";
RL Biochem. Biophys. Res. Commun. 422:670-675(2012).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [33]
RP CITRULLINATION AT ARG-167; ARG-199; ARG-231; ARG-264; ARG-296 AND ARG-303.
RX PubMed=23828821; DOI=10.1002/pmic.201300064;
RA Jin Z., Fu Z., Yang J., Troncosco J., Everett A.D., Van Eyk J.E.;
RT "Identification and Characterization of citrulline-modified brain proteins
RT by combining HCD and CID fragmentation.";
RL Proteomics 13:2682-2691(2013).
RN [34]
RP STRUCTURE BY NMR OF 135-148, CLEAVAGE OF INITIATOR METHIONINE (ISOFORMS 3;
RP 4; 5 AND 6), AND ACETYLATION AT ALA-2 (ISOFORMS 3; 4; 5 AND 6).
RX PubMed=7544282; DOI=10.1111/j.1432-1033.1995.tb20745.x;
RA Mendz G.L., Barden J.A., Martenson R.E.;
RT "Conformation of a tetradecapeptide epitope of myelin basic protein.";
RL Eur. J. Biochem. 231:659-666(1995).
RN [35]
RP 3D-STRUCTURE MODELING OF 135-279 (ISOFORM 5).
RX PubMed=9020143; DOI=10.1074/jbc.272.7.4269;
RA Ridsdale R.A., Beniac D.R., Tompkins T.A., Moscarello M.A., Harauz G.;
RT "Three-dimensional structure of myelin basic protein. II. Molecular
RT modeling and considerations of predicted structures in multiple
RT sclerosis.";
RL J. Biol. Chem. 272:4269-4275(1997).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 218-237 IN COMPLEX WITH
RP HLA-DRA/HLA-DRB5 HETERODIMER.
RX PubMed=11080454; DOI=10.1006/jmbi.2000.4198;
RA Li Y., Li H., Martin R., Mariuzza R.A.;
RT "Structural basis for the binding of an immunodominant peptide from myelin
RT basic protein in different registers by two HLA-DR2 proteins.";
RL J. Mol. Biol. 304:177-188(2000).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 221-233 IN COMPLEX WITH
RP HLA-DRA/HLA-DRB5 HETERODIMER AND STREPTOCOCCUS PYOGENES SPEC PEPTIDE.
RX PubMed=11163233; DOI=10.1016/s1074-7613(01)00092-9;
RA Li Y., Li H., Dimasi N., McCormick J.K., Martin R., Schuck P.,
RA Schlievert P.M., Mariuzza R.A.;
RT "Crystal structure of a superantigen bound to the high-affinity, zinc-
RT dependent site on MHC class II.";
RL Immunity 14:93-104(2001).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 221-233 IN COMPLEX WITH
RP HLA-DRA/HLA-DRB5 HETERODIMER AND TRAC.
RX PubMed=16079912; DOI=10.1038/sj.emboj.7600771;
RA Li Y., Huang Y., Lue J., Quandt J.A., Martin R., Mariuzza R.A.;
RT "Structure of a human autoimmune TCR bound to a myelin basic protein self-
RT peptide and a multiple sclerosis-associated MHC class II molecule.";
RL EMBO J. 24:2968-2979(2005).
CC -!- FUNCTION: The classic group of MBP isoforms (isoform 4-isoform 14) are
CC with PLP the most abundant protein components of the myelin membrane in
CC the CNS. They have a role in both its formation and stabilization. The
CC smaller isoforms might have an important role in remyelination of
CC denuded axons in multiple sclerosis. The non-classic group of MBP
CC isoforms (isoform 1-isoform 3/Golli-MBPs) may preferentially have a
CC role in the early developing brain long before myelination, maybe as
CC components of transcriptional complexes, and may also be involved in
CC signaling pathways in T-cells and neural cells. Differential splicing
CC events combined with optional post-translational modifications give a
CC wide spectrum of isomers, with each of them potentially having a
CC specialized function. Induces T-cell proliferation.
CC {ECO:0000269|PubMed:8544862}.
CC -!- SUBUNIT: Homodimer. Isoform 3 exists as a homodimer.
CC {ECO:0000269|PubMed:11080454, ECO:0000269|PubMed:11163233,
CC ECO:0000269|PubMed:16079912}.
CC -!- INTERACTION:
CC P02686; Q9GZU7: CTDSP1; NbExp=4; IntAct=EBI-947410, EBI-751587;
CC P02686-1; Q8I629: PF3D7_1201600; Xeno; NbExp=2; IntAct=EBI-7056012, EBI-7056031;
CC P02686-1; Q64702: Plk4; Xeno; NbExp=2; IntAct=EBI-7056012, EBI-2552433;
CC P02686-2; P05067: APP; NbExp=3; IntAct=EBI-12159027, EBI-77613;
CC P02686-2; Q9GZU7: CTDSP1; NbExp=4; IntAct=EBI-12159027, EBI-751587;
CC P02686-2; O15194-2: CTDSPL; NbExp=3; IntAct=EBI-12159027, EBI-12134515;
CC P02686-2; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-12159027, EBI-742388;
CC P02686-5; P62158: CALM3; NbExp=2; IntAct=EBI-15973992, EBI-397435;
CC -!- SUBCELLULAR LOCATION: Myelin membrane; Peripheral membrane protein;
CC Cytoplasmic side. Note=Cytoplasmic side of myelin.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus
CC {ECO:0000269|PubMed:22609403}. Note=Targeted to nucleus in
CC oligodendrocytes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Golli-MBP1, HOG7;
CC IsoId=P02686-1; Sequence=Displayed;
CC Name=2; Synonyms=Golli-MBP2, HOG5;
CC IsoId=P02686-2; Sequence=VSP_003311;
CC Name=3; Synonyms=MBP1, 21.5 kDa;
CC IsoId=P02686-3; Sequence=VSP_003308, VSP_003309;
CC Name=4; Synonyms=MBP2, 20.2 kDa;
CC IsoId=P02686-4; Sequence=VSP_003308, VSP_003309, VSP_003310;
CC Name=5; Synonyms=MBP3, 18.5 kDa;
CC IsoId=P02686-5; Sequence=VSP_003308;
CC Name=6; Synonyms=MBP4, 17.2 kDa;
CC IsoId=P02686-6; Sequence=VSP_003308, VSP_003310;
CC -!- TISSUE SPECIFICITY: MBP isoforms are found in both the central and the
CC peripheral nervous system, whereas Golli-MBP isoforms are expressed in
CC fetal thymus, spleen and spinal cord, as well as in cell lines derived
CC from the immune system. {ECO:0000269|PubMed:7504278}.
CC -!- DEVELOPMENTAL STAGE: Expression begins abruptly in 14-16 week old
CC fetuses. Even smaller isoforms seem to be produced during
CC embryogenesis; some of these persisting in the adult. Isoform 4
CC expression is more evident at 16 weeks and its relative proportion
CC declines thereafter.
CC -!- PTM: Several charge isomers of MBP; C1 (the most cationic, least
CC modified, and most abundant form), C2, C3, C4, C5, C6, C7, C8-A and C8-
CC B (the least cationic form); are produced as a result of optional PTM,
CC such as phosphorylation, deamidation of glutamine or asparagine,
CC arginine citrullination and methylation. C8-A and C8-B contain each two
CC mass isoforms termed C8-A(H), C8-A(L), C8-B(H) and C8-B(L), (H)
CC standing for higher and (L) for lower molecular weight. C3, C4 and C5
CC are phosphorylated. The ratio of methylated arginine residues decreases
CC during aging, making the protein more cationic.
CC {ECO:0000269|PubMed:23828821, ECO:0000269|PubMed:2466844,
CC ECO:0000269|PubMed:5128665}.
CC -!- PTM: The N-terminal alanine is acetylated (isoform 3, isoform 4,
CC isoform 5 and isoform 6).
CC -!- PTM: Arg-241 was found to be 6% monomethylated and 60% symmetrically
CC dimethylated.
CC -!- PTM: Proteolytically cleaved in B cell lysosomes by cathepsin CTSG
CC which degrades the major immunogenic MBP epitope and prevents the
CC activation of MBP-specific autoreactive T cells.
CC {ECO:0000269|PubMed:15100291}.
CC -!- PTM: Phosphorylated by TAOK2, VRK2, MAPK11, MAPK12, MAPK14 and MINK1.
CC -!- DISEASE: Note=The reduction in the surface charge of citrullinated
CC and/or methylated MBP could result in a weakened attachment to the
CC myelin membrane. This mechanism could be operative in demyelinating
CC diseases such as chronical multiple sclerosis (MS), and fulminating MS
CC (Marburg disease).
CC -!- MISCELLANEOUS: [Isoform 3]: Contains a non-traditional PY nuclear
CC localization signal. Mutagenesis of Cys-81 to Ser prevents
CC dimerization. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the myelin basic protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC41944.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. The C-terminus contains a Histidine tag.; Evidence={ECO:0000305};
CC Sequence=BAD92223.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAH10359.1; Type=Miscellaneous discrepancy; Note=wrong intron-exon boundaries.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Myelin basic protein entry;
CC URL="https://en.wikipedia.org/wiki/Myelin_basic_protein";
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DR EMBL; M30047; AAA59559.1; -; mRNA.
DR EMBL; M20009; AAA59561.1; -; mRNA.
DR EMBL; M13577; AAA59562.1; -; mRNA.
DR EMBL; M30516; AAA59563.1; -; mRNA.
DR EMBL; M30515; AAA59564.1; -; mRNA.
DR EMBL; X17286; CAA35179.1; -; Genomic_DNA.
DR EMBL; X17287; CAA35179.1; JOINED; Genomic_DNA.
DR EMBL; X17290; CAA35179.1; JOINED; Genomic_DNA.
DR EMBL; X17288; CAA35179.1; JOINED; Genomic_DNA.
DR EMBL; X17369; CAA35179.1; JOINED; Genomic_DNA.
DR EMBL; X17289; CAA35179.1; JOINED; Genomic_DNA.
DR EMBL; L18862; AAA72008.1; -; Genomic_DNA.
DR EMBL; L18864; AAA72009.1; -; Genomic_DNA.
DR EMBL; L18865; AAA72010.1; -; Genomic_DNA.
DR EMBL; L18866; AAA72011.1; -; Genomic_DNA.
DR EMBL; L41657; AAC41944.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CR536534; CAG38771.1; -; mRNA.
DR EMBL; CR541919; CAG46717.1; -; mRNA.
DR EMBL; CR627018; CAH10359.1; ALT_SEQ; mRNA.
DR EMBL; AK128770; BAG54728.1; -; mRNA.
DR EMBL; AK128788; BAG54734.1; -; mRNA.
DR EMBL; AB208986; BAD92223.1; ALT_INIT; mRNA.
DR EMBL; AC018529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008749; AAH08749.3; -; mRNA.
DR EMBL; BC065248; AAH65248.1; -; mRNA.
DR EMBL; BC080654; AAH80654.1; -; mRNA.
DR EMBL; BC101771; AAI01772.1; -; mRNA.
DR EMBL; BC101773; AAI01774.1; -; mRNA.
DR EMBL; BC143348; AAI43349.1; -; mRNA.
DR EMBL; BC143350; AAI43351.1; -; mRNA.
DR EMBL; M63599; AAA59560.1; -; Genomic_DNA.
DR CCDS; CCDS12011.1; -. [P02686-4]
DR CCDS; CCDS32847.1; -. [P02686-3]
DR CCDS; CCDS42448.1; -. [P02686-6]
DR CCDS; CCDS42449.1; -. [P02686-5]
DR CCDS; CCDS42450.1; -. [P02686-2]
DR PIR; A49635; A49635.
DR PIR; S10482; MBHUB.
DR RefSeq; NP_001020252.1; NM_001025081.1. [P02686-3]
DR RefSeq; NP_001020261.1; NM_001025090.1. [P02686-5]
DR RefSeq; NP_001020263.1; NM_001025092.1. [P02686-6]
DR RefSeq; NP_001020271.1; NM_001025100.1. [P02686-2]
DR RefSeq; NP_001020272.1; NM_001025101.1. [P02686-1]
DR RefSeq; NP_002376.1; NM_002385.2. [P02686-4]
DR RefSeq; XP_016881269.1; XM_017025780.1. [P02686-2]
DR PDB; 1BX2; X-ray; 2.60 A; C/F=217-231.
DR PDB; 1FV1; X-ray; 1.90 A; C/F=218-237.
DR PDB; 1HQR; X-ray; 3.20 A; C=221-233.
DR PDB; 1K2D; X-ray; 2.20 A; P=135-144.
DR PDB; 1YMM; X-ray; 3.50 A; C=217-240.
DR PDB; 1ZGL; X-ray; 2.80 A; C/F/I/L=221-233.
DR PDBsum; 1BX2; -.
DR PDBsum; 1FV1; -.
DR PDBsum; 1HQR; -.
DR PDBsum; 1K2D; -.
DR PDBsum; 1YMM; -.
DR PDBsum; 1ZGL; -.
DR AlphaFoldDB; P02686; -.
DR BMRB; P02686; -.
DR SMR; P02686; -.
DR BioGRID; 110325; 115.
DR DIP; DIP-36624N; -.
DR IntAct; P02686; 26.
DR MINT; P02686; -.
DR STRING; 9606.ENSP00000380958; -.
DR GlyGen; P02686; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P02686; -.
DR PhosphoSitePlus; P02686; -.
DR SwissPalm; P02686; -.
DR BioMuta; MBP; -.
DR EPD; P02686; -.
DR jPOST; P02686; -.
DR MassIVE; P02686; -.
DR MaxQB; P02686; -.
DR PeptideAtlas; P02686; -.
DR PRIDE; P02686; -.
DR ProteomicsDB; 51547; -. [P02686-1]
DR ProteomicsDB; 51548; -. [P02686-2]
DR ProteomicsDB; 51549; -. [P02686-3]
DR ProteomicsDB; 51550; -. [P02686-4]
DR ProteomicsDB; 51551; -. [P02686-5]
DR ProteomicsDB; 51552; -. [P02686-6]
DR ABCD; P02686; 5 sequenced antibodies.
DR Antibodypedia; 3704; 1328 antibodies from 50 providers.
DR DNASU; 4155; -.
DR Ensembl; ENST00000355994.7; ENSP00000348273.2; ENSG00000197971.16. [P02686-1]
DR Ensembl; ENST00000359645.7; ENSP00000352667.3; ENSG00000197971.16. [P02686-4]
DR Ensembl; ENST00000382582.7; ENSP00000372025.3; ENSG00000197971.16. [P02686-3]
DR Ensembl; ENST00000397860.7; ENSP00000380958.3; ENSG00000197971.16. [P02686-2]
DR Ensembl; ENST00000397863.5; ENSP00000380961.1; ENSG00000197971.16. [P02686-2]
DR Ensembl; ENST00000397865.9; ENSP00000380963.5; ENSG00000197971.16. [P02686-6]
DR Ensembl; ENST00000397866.8; ENSP00000380964.4; ENSG00000197971.16. [P02686-5]
DR Ensembl; ENST00000580402.5; ENSP00000462223.1; ENSG00000197971.16. [P02686-1]
DR GeneID; 4155; -.
DR KEGG; hsa:4155; -.
DR MANE-Select; ENST00000355994.7; ENSP00000348273.2; NM_001025101.2; NP_001020272.1.
DR UCSC; uc002lml.4; human. [P02686-1]
DR CTD; 4155; -.
DR DisGeNET; 4155; -.
DR GeneCards; MBP; -.
DR HGNC; HGNC:6925; MBP.
DR HPA; ENSG00000197971; Group enriched (brain, choroid plexus).
DR MIM; 159430; gene.
DR neXtProt; NX_P02686; -.
DR OpenTargets; ENSG00000197971; -.
DR PharmGKB; PA30667; -.
DR VEuPathDB; HostDB:ENSG00000197971; -.
DR eggNOG; ENOG502S4SJ; Eukaryota.
DR GeneTree; ENSGT00390000014772; -.
DR InParanoid; P02686; -.
DR OMA; TKIFKMG; -.
DR PhylomeDB; P02686; -.
DR TreeFam; TF333391; -.
DR PathwayCommons; P02686; -.
DR Reactome; R-HSA-9619665; EGR2 and SOX10-mediated initiation of Schwann cell myelination.
DR SignaLink; P02686; -.
DR SIGNOR; P02686; -.
DR BioGRID-ORCS; 4155; 14 hits in 1071 CRISPR screens.
DR ChiTaRS; MBP; human.
DR EvolutionaryTrace; P02686; -.
DR GeneWiki; Myelin_basic_protein; -.
DR GenomeRNAi; 4155; -.
DR Pharos; P02686; Tbio.
DR PRO; PR:P02686; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; P02686; protein.
DR Bgee; ENSG00000197971; Expressed in pons and 212 other tissues.
DR ExpressionAtlas; P02686; baseline and differential.
DR Genevisible; P02686; HS.
DR GO; GO:0071944; C:cell periphery; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; ISS:ARUK-UCL.
DR GO; GO:0043218; C:compact myelin; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0033269; C:internode region of axon; IBA:GO_Central.
DR GO; GO:0043209; C:myelin sheath; IDA:CAFA.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005516; F:calmodulin binding; IPI:CAFA.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0019911; F:structural constituent of myelin sheath; IBA:GO_Central.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0008366; P:axon ensheathment; TAS:ProtInc.
DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; IDA:CAFA.
DR GO; GO:0000165; P:MAPK cascade; IDA:CAFA.
DR GO; GO:0061024; P:membrane organization; IEA:Ensembl.
DR GO; GO:0042552; P:myelination; IBA:GO_Central.
DR GO; GO:0050771; P:negative regulation of axonogenesis; IEA:Ensembl.
DR GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; IDA:CAFA.
DR GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; IDA:CAFA.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:CAFA.
DR GO; GO:1904685; P:positive regulation of metalloendopeptidase activity; IDA:CAFA.
DR GO; GO:0070542; P:response to fatty acid; IEA:Ensembl.
DR GO; GO:0046689; P:response to mercury ion; IEA:Ensembl.
DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR GO; GO:0034612; P:response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR DisProt; DP00236; -.
DR DisProt; DP02078; -. [P02686-5]
DR InterPro; IPR000548; Myelin_BP.
DR PANTHER; PTHR11429; PTHR11429; 1.
DR Pfam; PF01669; Myelin_MBP; 1.
DR PRINTS; PR00212; MYELINMBP.
DR PROSITE; PS00569; MYELIN_MBP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing;
KW Autoimmune encephalomyelitis; Cell membrane; Citrullination;
KW Direct protein sequencing; Membrane; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..304
FT /note="Myelin basic protein"
FT /id="PRO_0000158990"
FT REGION 1..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..222
FT /note="Induces experimental autoimmune encephalomyelitis
FT (EAE) 1"
FT REGION 180..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..256
FT /note="Induces experimental autoimmune encephalomyelitis
FT (EAE) 2"
FT COMPBIAS 1..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 224..225
FT /note="Cleavage; by CTSG"
FT /evidence="ECO:0000269|PubMed:15100291"
FT SITE 248..249
FT /note="Cleavage; by CTSG"
FT /evidence="ECO:0000269|PubMed:15100291"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 148
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P02688"
FT MOD_RES 151
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02688"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 154
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02688"
FT MOD_RES 159
FT /note="Citrulline; in form C8"
FT /evidence="ECO:0000269|PubMed:2466844"
FT MOD_RES 165
FT /note="Citrulline; in form C8"
FT /evidence="ECO:0000269|PubMed:2466844"
FT MOD_RES 167
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:23828821"
FT MOD_RES 169
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 177
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 183
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 199
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:23828821"
FT MOD_RES 203
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 214
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 229
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02688"
FT MOD_RES 231
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:23828821"
FT MOD_RES 232
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 237
FT /note="Deamidated glutamine"
FT /evidence="ECO:0000250"
FT MOD_RES 241
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:5128665"
FT MOD_RES 241
FT /note="Symmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:5128665"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25274"
FT MOD_RES 256
FT /note="Citrulline; in form C8"
FT /evidence="ECO:0000269|PubMed:2466844"
FT MOD_RES 264
FT /note="Citrulline; in form C8"
FT /evidence="ECO:0000269|PubMed:23828821,
FT ECO:0000269|PubMed:2466844"
FT MOD_RES 281
FT /note="Deamidated glutamine"
FT /evidence="ECO:0000250"
FT MOD_RES 293
FT /note="Citrulline; in form C8"
FT /evidence="ECO:0000269|PubMed:2466844"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 296
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:23828821"
FT MOD_RES 299
FT /note="Phosphoserine; by UHMK1"
FT /evidence="ECO:0000269|PubMed:10880969"
FT MOD_RES 303
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:23828821"
FT MOD_RES 304
FT /note="Citrulline; in form C8"
FT /evidence="ECO:0000269|PubMed:2466844"
FT VAR_SEQ 1..133
FT /note="Missing (in isoform 3, isoform 4, isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:2425357,
FT ECO:0000303|PubMed:2427738, ECO:0000303|PubMed:2442403,
FT ECO:0000303|PubMed:4108501, ECO:0000303|Ref.8"
FT /id="VSP_003308"
FT VAR_SEQ 192
FT /note="K -> KVPWLKPGRSPLPSHARSQPGLCNMYK (in isoform 3 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:2425357,
FT ECO:0000303|PubMed:2442403"
FT /id="VSP_003309"
FT VAR_SEQ 193..304
FT /note="DSHHPARTAHYGSLPQKSHGRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLS
FT LSRFSWGAEGQRPGFGYGGRASDYKSAHKGFKGVDAQGTLSKIFKLGGRDSRSGSPMAR
FT R -> VSSEE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.11"
FT /id="VSP_003311"
FT VAR_SEQ 240..250
FT /note="Missing (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:2427738, ECO:0000303|PubMed:2442403,
FT ECO:0000303|Ref.8"
FT /id="VSP_003310"
FT CONFLICT 300
FT /note="P -> T (in Ref. 8; CAG38771)"
FT /evidence="ECO:0000305"
FT INIT_MET P02686-3:1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7544282"
FT MOD_RES P02686-3:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:7544282"
FT INIT_MET P02686-4:1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7544282"
FT MOD_RES P02686-4:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:7544282"
FT INIT_MET P02686-5:1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7544282"
FT MOD_RES P02686-5:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:7544282"
FT INIT_MET P02686-6:1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7544282"
FT MOD_RES P02686-6:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:7544282"
SQ 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
