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Protein

Myelin basic protein

Gene

MBP

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Myelin basic protein
Short name:
MBP
Alternative name(s):
20 kDa microtubule-stabilizing protein
Myelin A1 protein
Gene namesi
Name:MBP
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Keywords - Diseasei

Autoimmune encephalomyelitis

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001589871 – 169Myelin basic proteinAdd BLAST169

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylalanine1 Publication1
Modified residuei7Phosphoserine; in C5 and C61 Publication1
Modified residuei10PhosphoserineBy similarity1
Modified residuei12PhosphotyrosineBy similarity1
Modified residuei17PhosphoserineBy similarity1
Modified residuei18PhosphothreonineBy similarity1
Modified residuei23Citrulline; in form C8b1 Publication1
Modified residuei29CitrullineBy similarity1
Modified residuei33PhosphothreonineBy similarity1
Modified residuei38PhosphoserineBy similarity1
Modified residuei41Citrulline; alternate1 Publication1
Modified residuei41Omega-N-methylarginine; alternateBy similarity1
Modified residuei47Citrulline; in form C8b1 Publication1
Modified residuei47Omega-N-methylarginineBy similarity1
Modified residuei54Phosphoserine; in C4, C5 and C61 Publication1
Modified residuei63Citrulline1 Publication1
Modified residuei65PhosphothreonineBy similarity1
Modified residuei67PhosphotyrosineBy similarity1
Modified residuei94PhosphothreonineBy similarity1
Modified residuei96Citrulline; in form C2, C3, C8a and C8b2 Publications1
Modified residuei97Phosphothreonine; by MAPK; in C3, C4, C5 and C63 Publications1
Modified residuei102Deamidated glutamine; in form C51 Publication1
Modified residuei106Citrulline; alternate1 Publication1
Modified residuei106Omega-N-methylarginine; alternate3 Publications1
Modified residuei106Symmetric dimethylarginine; alternate3 Publications1
Modified residuei112Citrulline1 Publication1
Modified residuei114PhosphoserineBy similarity1
Modified residuei120Deamidated glutamine; in form C31 Publication1
Modified residuei121N6-acetyllysine1 Publication1
Modified residuei129Citrulline1 Publication1
Modified residuei146Deamidated glutamine; in form C21 Publication1
Modified residuei158CitrullineBy similarity1
Modified residuei160Phosphoserine; in C4 and C61 Publication1
Modified residuei161Citrulline; in form C32 Publications1
Modified residuei164Phosphoserine; in form C3, C5 and C61 Publication1
Modified residuei168Citrulline1 Publication1
Modified residuei169Citrulline1 Publication1

Post-translational modificationi

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.4 Publications
Phosphorylated by TAOK2, VRK2, MAPK11, MAPK12, MAPK14 and MINK1.By similarity

Keywords - PTMi

Acetylation, Citrullination, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP02687.
PRIDEiP02687.

PTM databases

iPTMnetiP02687.

Miscellaneous databases

PMAP-CutDBP02687.

Expressioni

Tissue specificityi

Found in both the central and the peripheral nervous system.

Interactioni

Subunit structurei

Homodimer; self-associates in the presence of lysolipid.

Binary interactionsi

WithEntry#Exp.IntActNotes
dclk2aA2A1214EBI-908215,EBI-9006039From a different organism.
LRRK2Q5S0073EBI-908215,EBI-5323863From a different organism.
MAPK1P284822EBI-908215,EBI-959949From a different organism.

Protein-protein interaction databases

DIPiDIP-29967N.
IntActiP02687. 35 interactors.
STRINGi9913.ENSBTAP00000002984.

Structurei

3D structure databases

DisProtiDP00047.
ProteinModelPortaliP02687.
SMRiP02687.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni43 – 87Induces experimental autoimmune encephalomyelitis (EAE) 1Add BLAST45
Regioni114 – 122Induces experimental autoimmune encephalomyelitis (EAE) 29

Sequence similaritiesi

Belongs to the myelin basic protein family.Curated

Phylogenomic databases

eggNOGiENOG410IIUJ. Eukaryota.
ENOG4111PMJ. LUCA.
HOGENOMiHOG000293395.
HOVERGENiHBG008347.
InParanoidiP02687.

Family and domain databases

InterProiIPR000548. Myelin_BP.
[Graphical view]
PANTHERiPTHR11429. PTHR11429. 1 hit.
PfamiPF01669. Myelin_MBP. 1 hit.
[Graphical view]
PRINTSiPR00212. MYELINMBP.
PROSITEiPS00569. MYELIN_MBP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P02687-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
AAQKRPSQRS KYLASASTMD HARHGFLPRH RDTGILDSLG RFFGSDRGAP
60 70 80 90 100
KRGSGKDGHH AARTTHYGSL PQKAQGHRPQ DENPVVHFFK NIVTPRTPPP
110 120 130 140 150
SQGKGRGLSL SRFSWGAEGQ KPGFGYGGRA SDYKSAHKGL KGHDAQGTLS
160
KIFKLGGRDS RSGSPMARR
Length:169
Mass (Da):18,323
Last modified:July 21, 1986 - v1
Checksum:i8E1157B7A1978484
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF226693 mRNA. Translation: AAK00645.1.
PIRiA92089. MBBOB.
UniGeneiBt.64741.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF226693 mRNA. Translation: AAK00645.1.
PIRiA92089. MBBOB.
UniGeneiBt.64741.

3D structure databases

DisProtiDP00047.
ProteinModelPortaliP02687.
SMRiP02687.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29967N.
IntActiP02687. 35 interactors.
STRINGi9913.ENSBTAP00000002984.

PTM databases

iPTMnetiP02687.

Proteomic databases

PaxDbiP02687.
PRIDEiP02687.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IIUJ. Eukaryota.
ENOG4111PMJ. LUCA.
HOGENOMiHOG000293395.
HOVERGENiHBG008347.
InParanoidiP02687.

Miscellaneous databases

PMAP-CutDBP02687.

Family and domain databases

InterProiIPR000548. Myelin_BP.
[Graphical view]
PANTHERiPTHR11429. PTHR11429. 1 hit.
PfamiPF01669. Myelin_MBP. 1 hit.
[Graphical view]
PRINTSiPR00212. MYELINMBP.
PROSITEiPS00569. MYELIN_MBP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMBP_BOVIN
AccessioniPrimary (citable) accession number: P02687
Secondary accession number(s): Q9BGM8, Q9TS63, Q9TSA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 2, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.