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P02686 (MBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 169. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myelin basic protein

Short name=MBP
Alternative name(s):
Myelin A1 protein
Myelin membrane encephalitogenic protein
Gene names
Name:MBP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length304 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The classic group of MBP isoforms (isoform 4-isoform14) 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-isoform3/Golli-MBPs) may preferentially have a role in the early developing brain long before myelination, maybe as components of transcriptional complexes, and may also be involved in signaling pathways in T-cells and neural cells. Differential splicing events combined 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. Ref.30

Isoform 3: Nucleus. Note: Targeted to nucleus in oligodendrocytes. Ref.30

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) Ref.32

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

myelination

Inferred from electronic annotation. Source: Ensembl

negative regulation of axonogenesis

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

substantia nigra development

Inferred from expression pattern PubMed 22926577. Source: UniProt

synaptic transmission

Traceable author statement PubMed 2434243. Source: ProtInc

   Cellular_componentcompact myelin

Inferred from electronic annotation. Source: Ensembl

internode region of axon

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionstructural constituent of myelin sheath

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

nek-3Q8I6292EBI-7056012,EBI-7056031From a different organism.
Plk4Q647022EBI-7056012,EBI-2552433From a different organism.

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. Contains a non-traditional PY nuclear localization signal. 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 304304Myelin basic protein
PRO_0000158990

Regions

Region179 – 22244Induces experimental autoimmune encephalomyelitis (EAE) 1
Region246 – 25611Induces experimental autoimmune encephalomyelitis (EAE) 2

Amino acid modifications

Modified residue1411Phosphoserine By similarity
Modified residue1591Citrulline; in form C8
Modified residue1651Citrulline; in form C8
Modified residue1671Citrulline
Modified residue1691Phosphothreonine By similarity
Modified residue1741Phosphoserine By similarity
Modified residue1901Phosphoserine By similarity
Modified residue1991Citrulline
Modified residue2031Phosphotyrosine By similarity
Modified residue2291Phosphothreonine By similarity
Modified residue2311Citrulline
Modified residue2321Phosphothreonine By similarity
Modified residue2371Deamidated glutamine By similarity
Modified residue2411Omega-N-methylarginine; alternate Ref.22
Modified residue2411Symmetric dimethylarginine; alternate Ref.22
Modified residue2491Phosphoserine By similarity
Modified residue2561Citrulline; in form C8
Modified residue2641Citrulline; in form C8
Modified residue2811Deamidated glutamine By similarity
Modified residue2931Citrulline; in form C8
Modified residue2951Phosphoserine By similarity
Modified residue2961Citrulline
Modified residue2991Phosphoserine; by UHMK1 Ref.24
Modified residue3031Citrulline
Modified residue3041Citrulline; in form C8

Natural variations

Alternative sequence1 – 133133Missing in isoform 3, isoform 4, isoform 5 and isoform 6.
VSP_003308
Alternative sequence1921K → KVPWLKPGRSPLPSHARSQP GLCNMYK in isoform 3 and isoform 4.
VSP_003309
Alternative sequence193 – 304112DSHHP…PMARR → VSSEE in isoform 2.
VSP_003311
Alternative sequence240 – 25011Missing in isoform 4 and isoform 6.
VSP_003310

Experimental info

Sequence conflict3001P → T in CAG38771. Ref.8

Secondary structure

........... 304
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Golli-MBP1) (HOG7) [UniParc].

Last modified October 18, 2001. Version 3.
Checksum: 4AD7305C1D5434C4

FASTA30433,117
        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 

« Hide

Isoform 2 (Golli-MBP2) (HOG5) [UniParc].

Checksum: 0B2F47BA214706F2
Show »

FASTA19721,522
Isoform 3 (MBP1) (21.5 kDa) [UniParc].

Checksum: 230FD99ECEC75FC5
Show »

FASTA19721,493
Isoform 4 (MBP2) (20.2 kDa) [UniParc].

Checksum: 6CCF96DD90FE1CEB
Show »

FASTA18620,246
Isoform 5 (MBP3) (18.5 kDa) [UniParc].

Checksum: 8E73B56787611054
Show »

FASTA17118,591
Isoform 6 (MBP4) (17.2 kDa) [UniParc].

Checksum: 0107AAD603FCD876
Show »

FASTA16017,343

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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), IDENTIFICATION BY 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), IDENTIFICATION BY 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]"The 21.5-kDa isoform of myelin basic protein has a non-traditional PY-nuclear-localization signal."
Smith G.S., Seymour L.V., Boggs J.M., Harauz G.
Biochem. Biophys. Res. Commun. 422:670-675(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION (ISOFORM 3).
[31]"Identification and Characterization of citrulline-modified brain proteins by combining HCD and CID fragmentation."
Jin Z., Fu Z., Yang J., Troncosco J., Everett A.D., Van Eyk J.E.
Proteomics 13:2682-2691(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: CITRULLINATION AT ARG-167; ARG-199; ARG-231; ARG-264; ARG-296 AND ARG-303.
[32]"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.
[33]"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).
[34]"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.
[35]"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.
[36]"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 expand/collapse EMBL AC list , 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.
PIRA49635.
MBHUB. S10482.
RefSeqNP_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.
UniGeneHs.551713.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BX2X-ray2.60C/F217-231[»]
1FV1X-ray1.90C/F218-237[»]
1HQRX-ray3.20C221-233[»]
1QCLmodel-A135-304[»]
1YMMX-ray3.50C217-231[»]
1ZGLX-ray2.80C/F/I/L221-233[»]
DisProtDP00236.
ProteinModelPortalP02686.
SMRP02686. Positions 211-244.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110325. 72 interactions.
DIPDIP-36624N.
IntActP02686. 13 interactions.
MINTMINT-5005920.

PTM databases

PhosphoSiteP02686.

Proteomic databases

PaxDbP02686.
PRIDEP02686.

Protocols and materials databases

DNASU4155.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355994; ENSP00000348273; ENSG00000197971. [P02686-1]
ENST00000359645; ENSP00000352667; ENSG00000197971. [P02686-4]
ENST00000382582; ENSP00000372025; ENSG00000197971. [P02686-3]
ENST00000397860; ENSP00000380958; ENSG00000197971. [P02686-2]
ENST00000397863; ENSP00000380961; ENSG00000197971. [P02686-2]
ENST00000397865; ENSP00000380963; ENSG00000197971. [P02686-6]
ENST00000397866; ENSP00000380964; ENSG00000197971. [P02686-5]
ENST00000580402; ENSP00000462223; ENSG00000197971. [P02686-1]
GeneID4155.
KEGGhsa:4155.
UCSCuc002lml.3. human. [P02686-3]
uc002lmn.3. human. [P02686-4]
uc002lmp.3. human. [P02686-6]
uc002lmr.3. human. [P02686-2]
uc010xfd.2. human. [P02686-1]

Organism-specific databases

CTD4155.
GeneCardsGC18M074690.
HGNCHGNC:6925. MBP.
HPACAB002300.
HPA049222.
MIM159430. gene.
neXtProtNX_P02686.
PharmGKBPA30667.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG75180.
HOVERGENHBG008347.
InParanoidP02686.
KOK17269.
OMAYKDSHHA.
OrthoDBEOG7M0NRZ.
PhylomeDBP02686.
TreeFamTF333391.

Gene expression databases

ArrayExpressP02686.
BgeeP02686.
CleanExHS_MBP.
GenevestigatorP02686.

Family and domain databases

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

Other

ChiTaRSMBP. human.
EvolutionaryTraceP02686.
GeneWikiMyelin_basic_protein.
GenomeRNAi4155.
NextBio16362.
PMAP-CutDBA8MYL4.
PROP02686.
SOURCESearch...

Entry information

Entry nameMBP_HUMAN
AccessionPrimary (citable) accession number: P02686
Secondary accession number(s): A4FU54 expand/collapse secondary AC list , 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 16, 2014
This is version 169 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM