P02687 (MBP_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Myelin basic protein
Short name=MBP

Alternative name(s):
20 kDa microtubule-stabilizing protein
Myelin A1 protein

Gene names

Name:

MBP

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	169 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Is, with PLP, the most abundant protein component of the myelin membrane in the CNS. Has a role in both the formation and stabilization of this compact multilayer arrangement of bilayers. Each splice variant and charge isomer may have a specialized function in the assembly of an optimized, biochemically functional myelin membrane By similarity.
Subunit structure	Homodimer; self-associates in the presence of lysolipid. Ref.12
Subcellular location	Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Note: Cytoplasmic side of myelin.
Tissue specificity	Found in both the central and the peripheral nervous system.
Post-translational modification	At least 6 charge isomers; C1 (the most cationic and least modified form), C2, C3, C4, C5 and C6 (the least cationic form); are produced as a result of optional post-translatonial modifications, such as phosphorylation of serine or threonine residues, deamidation of glutamine or asparagine residues, citrullination and methylation of arginine residues. Phosphorylated by TAOK2, VRK2, MAPK11, MAPK12, MAPK14 and MINK1 By similarity. Ref.10
Sequence similarities	Belongs to the myelin basic protein family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Disease	Autoimmune encephalomyelitis
PTM	Acetylation Citrullination Methylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	myelin sheath Inferred from electronic annotation. Source: UniProtKB-SubCell 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 169	169	Myelin basic protein		PRO_0000158987
Regions
	Region	43 – 87	45	Induces experimental autoimmune encephalomyelitis (EAE) 1
	Region	114 – 122	9	Induces experimental autoimmune encephalomyelitis (EAE) 2
Amino acid modifications
	Modified residue	1	1	N-acetylalanine
	Modified residue	7	1	Phosphoserine; in C5 and C6
	Modified residue	10	1	Phosphoserine By similarity
	Modified residue	23	1	Citrulline By similarity
	Modified residue	29	1	Citrulline By similarity
	Modified residue	33	1	Phosphothreonine By similarity
	Modified residue	38	1	Phosphoserine By similarity
	Modified residue	54	1	Phosphoserine; in C4, C5 and C6
	Modified residue	67	1	Phosphotyrosine By similarity
	Modified residue	69	1	Phosphoserine By similarity
	Modified residue	94	1	Phosphothreonine By similarity
	Modified residue	97	1	Phosphothreonine; by MAPK; in C3, C4, C5 and C6 Ref.10
	Modified residue	102	1	Deamidated glutamine; in form C5
	Modified residue	106	1	Omega-N-methylarginine; alternate Ref.8
	Modified residue	106	1	Symmetric dimethylarginine; alternate Ref.8
	Modified residue	114	1	Phosphoserine By similarity
	Modified residue	129	1	Citrulline By similarity
	Modified residue	146	1	Deamidated glutamine; in form C2
	Modified residue	158	1	Citrulline By similarity
	Modified residue	160	1	Phosphoserine; in C4 and C6
	Modified residue	164	1	Phosphoserine; in C3, C5 and C6
	Modified residue	169	1	Citrulline Probable

Sequences

	Sequence		Length	Mass (Da)
	P02687 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 8E1157B7A1978484	FASTA	169	18,323
	10 20 30 40 50 60 AAQKRPSQRS KYLASASTMD HARHGFLPRH RDTGILDSLG RFFGSDRGAP KRGSGKDGHH 70 80 90 100 110 120 AARTTHYGSL PQKAQGHRPQ DENPVVHFFK NIVTPRTPPP SQGKGRGLSL SRFSWGAEGQ 130 140 150 160 KPGFGYGGRA SDYKSAHKGL KGHDAQGTLS KIFKLGGRDS RSGSPMARR

References

[1]	"Basic A1 protein of the myelin membrane. The complete amino acid sequence." Eylar E.H., Brostoff S.W., Hashim G., Caccam J., Burnett P. J. Biol. Chem. 246:5770-5784(1971) [PubMed: 5096093] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"Specific cleavage of the A1 protein from myelin with cathepsin D." Brostoff S.W., Reuter W., Hichens M., Eylar E.H. J. Biol. Chem. 249:559-567(1974) [PubMed: 4129204] [Abstract] Cited for: SEQUENCE REVISION.
[3]	"A new MBP allele in Bos taurus is characterized by BseNI PCR-RFLP." Pietrowski D., Medugorac I., Foerster M. Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-56.
[4]	"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.C.-H., Kibler R.F. J. Biol. Chem. 246:4630-4640(1971) Cited for: PROTEIN SEQUENCE OF 43-87.
[5]	"Ca(2+)-calmodulin regulated effectors of microtubule stability in bovine brain." Pirollet F., Derancourt J., Haiech J., Job D., Margolis R.L. Biochemistry 31:8849-8855(1992) [PubMed: 1382581] [Abstract] Cited for: PROTEIN SEQUENCE OF 38-58 AND 119-141. Tissue: Brain.
[6]	"Purification of a new clathrin assembly protein from bovine brain coated vesicles and its identification as myelin basic protein." Prasad K., Barouch W., Martin B.M., Greene L.E., Eisenberg E. J. Biol. Chem. 270:30551-30556(1995) [PubMed: 8530487] [Abstract] Cited for: PROTEIN SEQUENCE OF 30-42; 74-89 AND 114-129.
[7]	"Experimental allergic encephalomyelitis: synthesis of disease-inducing site of the basic protein." Eylar E.H., Caccam J., Jackson J.J., Westall F.C., Robinson A.B. Science 168:1220-1223(1970) [PubMed: 5442707] [Abstract] Cited for: SYNTHESIS OF ALLERGIC ENCEPHALOMYELITIS INDUCING REGION.
[8]	"Localization of methylated arginine in the A1 protein from myelin." Brostoff S.W., Eylar E.H. Proc. Natl. Acad. Sci. U.S.A. 68:765-769(1971) [PubMed: 4994464] [Abstract] Cited for: METHYLATION AT ARG-106.
[9]	"Basis of microheterogeneity of myelin basic protein." Chou F.C.-H., Chou C.-H.J., Shapira R., Kibler R.F. J. Biol. Chem. 251:2671-2679(1976) [PubMed: 57115] [Abstract] Cited for: POST-TRANSLATIONAL MODIFICATIONS.
[10]	"Identification by mass spectrometry of threonine 97 in bovine myelin basic protein as a specific phosphorylation site for mitogen-activated protein kinase." Erickson A.K., Payne D.M., Martino P.A., Rossomando A.J., Shabanowitz J., Weber M.J., Hunt D.F., Sturgill T.W. J. Biol. Chem. 265:19728-19735(1990) [PubMed: 1700979] [Abstract] Cited for: PROTEIN SEQUENCE OF 97-104, PHOSPHORYLATION AT THR-97.
[11]	"Determination of the sites of posttranslational modifications in the charge isomers of bovine myelin basic protein by capillary electrophoresis-mass spectroscopy." Zand R., Li M.X., Jin X., Lubman D. Biochemistry 37:2441-2449(1998) [PubMed: 9485392] [Abstract] Cited for: POST-TRANSLATIONAL MODIFICATIONS.
[12]	"Sedimentation analysis of the self-association of bovine myelin basic protein." Smith R. Biochemistry 19:1826-1831(1980) [PubMed: 6155143] [Abstract] Cited for: DIMERIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF226693 mRNA. Translation: AAK00645.1.
IPI	IPI00827370.
PIR	MBBOB. A92089.
UniGene	Bt.64741.
3D structure databases
DisProt	DP00047.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29967N.
IntAct	P02687. 3 interactions.
STRING	P02687.
Proteomic databases
PRIDE	P02687.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	maNOG17514.
GeneTree	ENSGT00390000014772.
HOVERGEN	HBG008347.
InParanoid	P02687.
OrthoDB	EOG4S1T86.
Family and domain databases
InterPro	IPR000548. Myelin_BP. [Graphical view]
PANTHER	PTHR11429. Myelin_BP. 1 hit.
Pfam	PF01669. Myelin_MBP. 1 hit. [Graphical view]
PRINTS	PR00212. MYELINMBP.
PROSITE	PS00569. MYELIN_MBP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
PMAP-CutDB	P02687.

Entry information

Entry name

MBP_BOVIN

Accession

Primary (citable) accession number: P02687
Secondary accession number(s): Q9BGM8, Q9TS63, Q9TSA6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	January 25, 2012
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program