P02686 (MBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Myelin basic protein
Short name=MBP

Alternative name(s):
Myelin A1 protein
Myelin membrane encephalitogenic protein

Gene names

Name:

MBP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	304 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.7
Subunit structure	Homodimer. Isoform 3 exists as a homodimer. Ref.7
Subcellular location	Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Note: Cytoplasmic side of myelin.
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. Ref.6
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.
Post-translational modification	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. Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 The N-terminal alanine is acetylated (isoform 3, isoform 4, isoform 5 and isoform 6). Arg-241 was found to be 6% monomethylated and 60% symmetrically dimethylated. Ref.22 Phosphorylated by TAOK2, VRK2, MAPK11, MAPK12, MAPK14 and MINK1. Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28
Involvement in disease	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).
Sequence similarities	Belongs to the myelin basic protein family.
Sequence caution	The sequence AAC41944.1 differs from that shown. Reason: Contaminating sequence. The C-terminus contains a Histidine tag. The sequence BAD92223.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAH10359.1 differs from that shown. Reason: wrong intron-exon boundaries.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Disease	Autoimmune encephalomyelitis
PTM	Acetylation Citrullination Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	axon ensheathment Traceable author statement PubMed 2434243. Source: ProtInc central nervous system development Traceable author statement PubMed 2434243. Source: ProtInc immune response Traceable author statement Ref.6. Source: ProtInc membrane organization Inferred from electronic annotation. Source: Compara myelination Inferred from electronic annotation. Source: Compara negative regulation of axonogenesis Inferred from electronic annotation. Source: Compara response to toxin Inferred from electronic annotation. Source: Compara synaptic transmission Traceable author statement PubMed 2434243. Source: ProtInc
Cellular_component	compact myelin Inferred from electronic annotation. Source: Compara internode region of axon Inferred from electronic annotation. Source: Compara neuronal cell body Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	structural constituent of myelin sheath Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P02686-1)

Also known as: Golli-MBP1; HOG7;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P02686-2)

Also known as: Golli-MBP2; HOG5;

The sequence of this isoform differs from the canonical sequence as follows:
     193-304: DSHHPARTAH...SRSGSPMARR → VSSEE

Isoform 3 (identifier: P02686-3)

Also known as: MBP1; 21.5 kDa;

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.
     192-192: K → KVPWLKPGRSPLPSHARSQPGLCNMYK

Note: Initiator Met-1 is removed. Contains a N-acetylalanine at position 2. Mutagenesis of Cys-81 to Ser prevents dimerization.

Isoform 4 (identifier: P02686-4)

Also known as: MBP2; 20.2 kDa;

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.
     192-192: K → KVPWLKPGRSPLPSHARSQPGLCNMYK
     240-250: Missing.

Note: Initiator Met-1 is removed. Contains a N-acetylalanine at position 2.

Isoform 5 (identifier: P02686-5)

Also known as: MBP3; 18.5 kDa;

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.

Note: Initiator Met-1 is removed. Contains a N-acetylalanine at position 2.

Isoform 6 (identifier: P02686-6)

Also known as: MBP4; 17.2 kDa;

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.
     240-250: Missing.

Note: Initiator Met-1 is removed. Contains a N-acetylalanine at position 2.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 304

304

Myelin basic protein

PRO_0000158990

Regions

Region

179 – 222

44

Induces experimental autoimmune encephalomyelitis (EAE) 1

Region

246 – 256

11

Induces experimental autoimmune encephalomyelitis (EAE) 2

Amino acid modifications

Modified residue

96

1

Phosphoserine By similarity

Modified residue

141

1

Phosphoserine By similarity

Modified residue

146

1

Phosphoserine By similarity

Modified residue

159

1

Citrulline; in form C8

Modified residue

165

1

Citrulline; in form C8

Modified residue

169

1

Phosphothreonine By similarity

Modified residue

174

1

Phosphoserine By similarity

Modified residue

190

1

Phosphoserine By similarity

Modified residue

203

1

Phosphotyrosine By similarity

Modified residue

205

1

Phosphoserine By similarity

Modified residue

229

1

Phosphothreonine By similarity

Modified residue

232

1

Phosphothreonine By similarity

Modified residue

237

1

Deamidated glutamine By similarity

Modified residue

241

1

Omega-N-methylarginine; alternate Ref.22

Modified residue

241

1

Symmetric dimethylarginine; alternate Ref.22

Modified residue

249

1

Phosphoserine By similarity

Modified residue

256

1

Citrulline; in form C8

Modified residue

264

1

Citrulline; in form C8

Modified residue

281

1

Deamidated glutamine By similarity

Modified residue

293

1

Citrulline; in form C8

Modified residue

295

1

Phosphoserine By similarity

Modified residue

299

1

Phosphoserine; by UHMK1 Ref.24

Modified residue

304

1

Citrulline; in form C8

Natural variations

Alternative sequence

1 – 133

133

Missing in isoform 3, isoform 4, isoform 5 and isoform 6.

VSP_003308

Alternative sequence

192

1

K → KVPWLKPGRSPLPSHARSQP GLCNMYK in isoform 3 and isoform 4.

VSP_003309

Alternative sequence

193 – 304

112

DSHHP…PMARR → VSSEE in isoform 2.

VSP_003311

Alternative sequence

240 – 250

11

Missing in isoform 4 and isoform 6.

VSP_003310

Experimental info

Sequence conflict

300

1

P → T in CAG38771. Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

304

Helix Strand Turn

Details...

Beta strand

146 – 154

9

Beta strand

160 – 162

3

Beta strand

173 – 179

7

Beta strand

241 – 248

8

Beta strand

284 – 289

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Golli-MBP1) (HOG7) [UniParc]. Last modified October 18, 2001. Version 3. Checksum: 4AD7305C1D5434C4	FASTA	304	33,117
	10 20 30 40 50 60 MGNHAGKREL NAEKASTNSE TNRGESEKKR NLGELSRTTS EDNEVFGEAD ANQNNGTSSQ 70 80 90 100 110 120 DTAVTDSKRT ADPKNAWQDA HPADPGSRPH LIRLFSRDAP GREDNTFKDR PSESDELQTI 130 140 150 160 170 180 QEDSAATSES LDVMASQKRP SQRHGSKYLA TASTMDHARH GFLPRHRDTG ILDSIGRFFG 190 200 210 220 230 240 GDRGAPKRGS GKDSHHPART AHYGSLPQKS HGRTQDENPV VHFFKNIVTP RTPPPSQGKG 250 260 270 280 290 300 RGLSLSRFSW GAEGQRPGFG YGGRASDYKS AHKGFKGVDA QGTLSKIFKL GGRDSRSGSP MARR
	Isoform 2 (Golli-MBP2) (HOG5) [UniParc]. Checksum: 0B2F47BA214706F2	FASTA	197	21,522
	10 20 30 40 50 60 MGNHAGKREL NAEKASTNSE TNRGESEKKR NLGELSRTTS EDNEVFGEAD ANQNNGTSSQ 70 80 90 100 110 120 DTAVTDSKRT ADPKNAWQDA HPADPGSRPH LIRLFSRDAP GREDNTFKDR PSESDELQTI 130 140 150 160 170 180 QEDSAATSES LDVMASQKRP SQRHGSKYLA TASTMDHARH GFLPRHRDTG ILDSIGRFFG 190 GDRGAPKRGS GKVSSEE
	Isoform 3 (MBP1) (21.5 kDa) [UniParc]. Checksum: 230FD99ECEC75FC5	FASTA	197	21,493
	10 20 30 40 50 60 MASQKRPSQR HGSKYLATAS TMDHARHGFL PRHRDTGILD SIGRFFGGDR GAPKRGSGKV 70 80 90 100 110 120 PWLKPGRSPL PSHARSQPGL CNMYKDSHHP ARTAHYGSLP QKSHGRTQDE NPVVHFFKNI 130 140 150 160 170 180 VTPRTPPPSQ GKGRGLSLSR FSWGAEGQRP GFGYGGRASD YKSAHKGFKG VDAQGTLSKI 190 FKLGGRDSRS GSPMARR
	Isoform 4 (MBP2) (20.2 kDa) [UniParc]. Checksum: 6CCF96DD90FE1CEB	FASTA	186	20,246
	10 20 30 40 50 60 MASQKRPSQR HGSKYLATAS TMDHARHGFL PRHRDTGILD SIGRFFGGDR GAPKRGSGKV 70 80 90 100 110 120 PWLKPGRSPL PSHARSQPGL CNMYKDSHHP ARTAHYGSLP QKSHGRTQDE NPVVHFFKNI 130 140 150 160 170 180 VTPRTPPPSQ GKGAEGQRPG FGYGGRASDY KSAHKGFKGV DAQGTLSKIF KLGGRDSRSG SPMARR
	Isoform 5 (MBP3) (18.5 kDa) [UniParc]. Checksum: 8E73B56787611054	FASTA	171	18,591
	10 20 30 40 50 60 MASQKRPSQR HGSKYLATAS TMDHARHGFL PRHRDTGILD SIGRFFGGDR GAPKRGSGKD 70 80 90 100 110 120 SHHPARTAHY GSLPQKSHGR TQDENPVVHF FKNIVTPRTP PPSQGKGRGL SLSRFSWGAE 130 140 150 160 170 GQRPGFGYGG RASDYKSAHK GFKGVDAQGT LSKIFKLGGR DSRSGSPMAR R
	Isoform 6 (MBP4) (17.2 kDa) [UniParc]. Checksum: 0107AAD603FCD876	FASTA	160	17,343
	10 20 30 40 50 60 MASQKRPSQR HGSKYLATAS TMDHARHGFL PRHRDTGILD SIGRFFGGDR GAPKRGSGKD 70 80 90 100 110 120 SHHPARTAHY GSLPQKSHGR TQDENPVVHF FKNIVTPRTP PPSQGKGAEG QRPGFGYGGR 130 140 150 160 ASDYKSAHKG FKGVDAQGTL SKIFKLGGRD SRSGSPMARR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Amino acid sequence of the encephalitogenic basic protein from human myelin." Carnegie P.R. Biochem. J. 123:57-67(1971) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE (ISOFORM 5).
[2]	"Isolation and characterization of a cDNA coding for a novel human 17.3K myelin basic protein (MBP) variant." Roth H.J., Kronquist K.E., Pretorius P.J., Crandall B.F., Campagnoni A.T. J. Neurosci. Res. 16:227-238(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6). Tissue: Embryonic spinal cord.
[3]	"Identification of three forms of human myelin basic protein by cDNA cloning." Kamholz J., de Ferra F., Puckett C., Lazzarini R.A. Proc. Natl. Acad. Sci. U.S.A. 83:4962-4966(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 5).
[4]	"Evidence for the expression of four myelin basic protein variants in the developing human spinal cord through cDNA cloning." Roth H.J., Kronquist K.E., de Rosbo N., Crandall B.F., Campagnoni A.T. J. Neurosci. Res. 17:321-328(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5 AND 6). Tissue: Embryonic spinal cord.
[5]	"The organization of the human myelin basic protein gene. Comparison with the mouse gene." Streicher R., Stoffel W. Biol. Chem. Hoppe-Seyler 370:503-510(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 3; 4; 5 AND 6).
[6]	"The human myelin basic protein gene is included within a 179-kilobase transcription unit: expression in the immune and central nervous systems." Pribyl T.M., Campagnoni C.W., Kampf K., Kashima T., Handley V.W., McMahon J., Campagnoni A.T. Proc. Natl. Acad. Sci. U.S.A. 90:10695-10699(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY. Tissue: Brain.
[7]	"Purification of immunologically active recombinant 21.5 kDa isoform of human myelin basic protein." Nye S.H., Pelfrey C.M., Burkwit J.J., Voskuhl R.R., Lenardo M.J., Mueller J.P. Mol. Immunol. 32:1131-1141(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3), FUNCTION, DIMERIZATION, MUTAGENESIS.
[8]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
[9]	"The full-ORF clone resource of the German cDNA consortium." 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. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Amygdala.
[10]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). Tissue: Hippocampus and Subthalamic nucleus.
[11]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[12]	"DNA sequence and analysis of human chromosome 18." 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. Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 5 AND 6). Tissue: Brain, Lung and Skin.
[14]	"Repetitive DNA (TGGA)n 5' to the human myelin basic protein gene: a new form of oligonucleotide repetitive sequence showing length polymorphism." Boylan K.B., Ayres T.M., Popko B., Takahashi N., Hood L.E., Prusiner S.B. Genomics 6:16-22(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 135-192.
[15]	"Analysis of the primary sequence of human myelin basic protein peptides 1-44 and 90-170 by fast atom bombardment mass spectrometry." Scoble H.A., Whitaker J.N., Biemann K. J. Neurochem. 47:614-616(1986) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 135-178 AND 224-304 (ISOFORM 3), MASS SPECTROMETRY.
[16]	"The isolation, characterization, and lipid-aggregating properties of a citrulline containing myelin basic protein." Wood D.D., Moscarello M.A. J. Biol. Chem. 264:5121-5127(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 148-304 (ISOFORM 5), CITRULLINATION OF C8. Tissue: Brain.
[17]	"The isolation and characterization of four myelin basic proteins from the unbound fraction during CM52 chromatography." Boulias C., Pang H., Mastronardi F., Moscarello M.A. Arch. Biochem. Biophys. 322:174-182(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 156-172 AND 302-304, CHARACTERIZATION OF C8. Tissue: Brain.
[18]	"Amino acid sequence of human myelin basic protein peptide 45-89 as determined by mass spectrometry." Gibson B.W., Gilliom R.D., Whitaker J.N., Biemann K. J. Biol. Chem. 259:5028-5031(1984) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 179-223 (ISOFORM 5), MASS SPECTROMETRY.
[19]	"Encephalitogenic fragment of myelin basic protein. Amino acid sequence of bovine, rabbit, guinea pig, monkey, and human fragments." Shapira R., McKneally S.S., Chou F., Kibler R.F. J. Biol. Chem. 246:4630-4640(1971) Cited for: PROTEIN SEQUENCE OF 179-222 (ISOFORM 5), SEQUENCE REVISION.
[20]	"Immunologic properties of the main encephalitogenic peptide from the basic protein of human myelin." Lennon V.A., Wilks A.V., Carnegie P.R. J. Immunol. 105:1223-1230(1970) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 246-269 (ISOFORM 3), ENCEPHALITOGENIC PEPTIDE.
[21]	"Leukocyte gelatinase B cleavage releases encephalitogens from human myelin basic protein." Proost P., Van Damme J., Opdenakker G. Biochem. Biophys. Res. Commun. 192:1175-1181(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Tissue: Brain.
[22]	"Isolation and partial characterization of methylated arginines from the encephalitogenic basic protein of myelin." Baldwin G.S., Carnegie P.R. Biochem. J. 123:69-74(1971) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT ARG-241.
[23]	"Selective activation of p38 mitogen-activated protein (MAP) kinase isoforms by the MAP kinase kinases MKK3 and MKK6." Enslen H., Raingeaud J., Davis R.J. J. Biol. Chem. 273:1741-1748(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY MAPK11; MAPK12 AND MAPK14.
[24]	"Specific Ser-Pro phosphorylation by the RNA-recognition motif containing kinase KIS." Maucuer A., Le Caer J.P., Manceau V., Sobel A. Eur. J. Biochem. 267:4456-4464(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-299.
[25]	"PSK, a novel STE20-like kinase derived from prostatic carcinoma that activates the JNK MAPK pathway and regulates actin cytoskeletal organisation." Moore T.M., Garg R., Johnson C., Coptcoat M.J., Ridley A.J., Morris J.D.H. J. Biol. Chem. 275:4311-4322(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY TAOK2.
[26]	"Involvement of MINK, a Ste20 family kinase, in Ras oncogene-induced growth arrest in human ovarian surface epithelial cells." 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. Mol. Cell 20:673-685(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY MINK1.
[27]	"The subcellular localization of vaccinia-related kinase-2 (VRK2) isoforms determines their different effect on p53 stability in tumour cell lines." Blanco S., Klimcakova L., Vega F.M., Lazo P.A. FEBS J. 273:2487-2504(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY VRK2.
[28]	"Prostate-derived sterile 20-like kinase 1-alpha induces apoptosis. JNK-and caspase-dependent nuclear localization is a requirement for membrane blebbing." Zihni C., Mitsopoulos C., Tavares I.A., Baum B., Ridley A.J., Morris J.D. J. Biol. Chem. 282:6484-6493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY TAOK2.
[29]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[30]	"Conformation of a tetradecapeptide epitope of myelin basic protein." Mendz G.L., Barden J.A., Martenson R.E. Eur. J. Biochem. 231:659-666(1995) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 135-148, ACETYLATION.
[31]	"Three-dimensional structure of myelin basic protein. II. Molecular modeling and considerations of predicted structures in multiple sclerosis." Ridsdale R.A., Beniac D.R., Tompkins T.A., Moscarello M.A., Harauz G. J. Biol. Chem. 272:4269-4275(1997) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 135-279 (ISOFORM 5).
[32]	"Structural basis for the binding of an immunodominant peptide from myelin basic protein in different registers by two HLA-DR2 proteins." Li Y., Li H., Martin R., Mariuzza R.A. J. Mol. Biol. 304:177-188(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 218-237 IN COMPLEX WITH HLA-DRA/HLA-DRB5 HETERODIMER.
[33]	"Crystal structure of a superantigen bound to the high-affinity, zinc-dependent site on MHC class II." Li Y., Li H., Dimasi N., McCormick J.K., Martin R., Schuck P., Schlievert P.M., Mariuzza R.A. Immunity 14:93-104(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 221-233 IN COMPLEX WITH HLA-DRA/HLA-DRB5 HETERODIMER AND STREPTOCOCCUS PYOGENES SPEC PEPTIDE.
[34]	"Structure of a human autoimmune TCR bound to a myelin basic protein self-peptide and a multiple sclerosis-associated MHC class II molecule." Li Y., Huang Y., Lue J., Quandt J.A., Martin R., Mariuzza R.A. EMBO J. 24:2968-2979(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 221-233 IN COMPLEX WITH HLA-DRA/HLA-DRB5 HETERODIMER AND TRAC.
+	Additional computationally mapped references.

Web resources

Wikipedia

Myelin basic protein entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M30047 mRNA. Translation: AAA59559.1.
M20009 mRNA. Translation: AAA59561.1.
M13577 mRNA. Translation: AAA59562.1.
M30516 mRNA. Translation: AAA59563.1.
M30515 mRNA. Translation: AAA59564.1.
X17286 , X17287, X17290, X17288, X17369, X17289 Genomic DNA. Translation: CAA35179.1.
L18862 Genomic DNA. Translation: AAA72008.1.
L18864 Genomic DNA. Translation: AAA72009.1.
L18865 Genomic DNA. Translation: AAA72010.1.
L18866 Genomic DNA. Translation: AAA72011.1.
L41657 Genomic DNA. Translation: AAC41944.1. Sequence problems.
CR536534 mRNA. Translation: CAG38771.1.
CR541919 mRNA. Translation: CAG46717.1.
CR627018 mRNA. Translation: CAH10359.1. Sequence problems.
AK128770 mRNA. Translation: BAG54728.1.
AK128788 mRNA. Translation: BAG54734.1.
AB208986 mRNA. Translation: BAD92223.1. Different initiation.
AC018529 Genomic DNA. No translation available.
AC093330 Genomic DNA. No translation available.
BC008749 mRNA. Translation: AAH08749.3.
BC065248 mRNA. Translation: AAH65248.1.
BC080654 mRNA. Translation: AAH80654.1.
BC101771 mRNA. Translation: AAI01772.1.
BC101773 mRNA. Translation: AAI01774.1.
BC143348 mRNA. Translation: AAI43349.1.
BC143350 mRNA. Translation: AAI43351.1.
M63599 Genomic DNA. Translation: AAA59560.1.

IPI

IPI00021907.
IPI00216474.
IPI00216475.
IPI00216477.
IPI00216478.
IPI00607642.
IPI00718832.

PIR

A49635.
MBHUB. S10482.

RefSeq

NP_001020252.1. NM_001025081.1.
NP_001020261.1. NM_001025090.1.
NP_001020263.1. NM_001025092.1.
NP_001020271.1. NM_001025100.1.
NP_001020272.1. NM_001025101.1.
NP_002376.1. NM_002385.2.

UniGene

Hs.551713.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BX2	X-ray	2.60	C/F	217-231	[»]
1FV1	X-ray	1.90	C/F	218-237	[»]
1HQR	X-ray	3.20	C	221-233	[»]
1QCL	model	-	A	135-304	[»]
1YMM	X-ray	3.50	C	217-231	[»]
1ZGL	X-ray	2.80	C/F/I/L	221-233	[»]

DisProt

DP00236.

ProteinModelPortal

P02686.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36624N.

IntAct

P02686. 7 interactions.

MINT

MINT-5005920.

PTM databases

PhosphoSite

P02686.

Polymorphism databases

DMDM

17378805.

Proteomic databases

PaxDb

P02686.

PRIDE

P02686.

Protocols and materials databases

DNASU

4155.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000355994; ENSP00000348273; ENSG00000197971.
ENST00000359645; ENSP00000352667; ENSG00000197971.
ENST00000382582; ENSP00000372025; ENSG00000197971.
ENST00000397860; ENSP00000380958; ENSG00000197971.
ENST00000397863; ENSP00000380961; ENSG00000197971.
ENST00000397865; ENSP00000380963; ENSG00000197971.
ENST00000397866; ENSP00000380964; ENSG00000197971.
ENST00000580402; ENSP00000462223; ENSG00000197971.

GeneID

4155.

KEGG

hsa:4155.

UCSC

uc002lml.3. human.
uc002lmn.3. human.
uc002lmp.3. human.
uc002lmr.3. human.
uc010xfd.2. human.

Organism-specific databases

CTD

4155.

GeneCards

GC18M074690.

HGNC

HGNC:6925. MBP.

HPA

CAB002300.

MIM

159430. gene.

neXtProt

NX_P02686.

PharmGKB

PA30667.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG75180.

HOVERGEN

HBG008347.

InParanoid

P02686.

OMA

HARSQPG.

OrthoDB

EOG4S1T86.

Gene expression databases

ArrayExpress

P02686.

Bgee

P02686.

CleanEx

HS_MBP.

Genevestigator

P02686.

GermOnline

ENSG00000197971. Homo sapiens.

Family and domain databases

InterPro

IPR000548. Myelin_BP.
[Graphical view]

PANTHER

PTHR11429. PTHR11429. 1 hit.

Pfam

PF01669. Myelin_MBP. 1 hit.
[Graphical view]

PRINTS

PR00212. MYELINMBP.

PROSITE

PS00569. MYELIN_MBP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

MBP. human.

EvolutionaryTrace

P02686.

GenomeRNAi

4155.

NextBio

16362.

PMAP-CutDB

A8MYL4.

SOURCE

Search...

Entry information

Entry name

MBP_HUMAN

Accession

Primary (citable) accession number: P02686
Secondary accession number(s): A4FU54 , A6NI84, A8MY86, A8MYL4, B3KY66, B7ZKS2, B7ZKS4, Q15337, Q15338, Q15339, Q15340, Q59GX3, Q65ZS4, Q6AI64, Q6FH37, Q6FI04, Q6PK23

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	October 18, 2001
Last modified:	April 3, 2013
This is version 160 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.