P81558 (MBP_PIG) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 64.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Myelin basic protein Short name=MBP | ||
| Gene names |
| ||
| Organism | Sus scrofa (Pig) [Reference proteome] | ||
| Taxonomic identifier | 9823 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus![]() |
Protein attributes
| Sequence length | 171 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 By similarity. |
| Subcellular location | Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Note: Cytoplasmic side of myelin. |
| Post-translational modification | As in other animals, several charge isomers may be 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. |
| Sequence similarities | Belongs to the myelin basic protein family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell membrane Membrane |
| 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 membraneInferred 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 – 171 | 171 | Myelin basic protein | PRO_0000158993 | |||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylalanine | ||||||
| Modified residue | 7 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 12 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 25 | 1 | Citrulline By similarity | ||||||
| Modified residue | 31 | 1 | Citrulline By similarity | ||||||
| Modified residue | 35 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 39 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 55 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 68 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 70 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 95 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 98 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 103 | 1 | Deamidated glutamine By similarity | ||||||
| Modified residue | 107 | 1 | Omega-N-methylarginine; alternate Ref.1 | ||||||
| Modified residue | 107 | 1 | Symmetric dimethylarginine; alternate Ref.1 | ||||||
| Modified residue | 115 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 122 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 130 | 1 | Citrulline By similarity | ||||||
| Modified residue | 148 | 1 | Deamidated glutamine By similarity | ||||||
| Modified residue | 160 | 1 | Citrulline By similarity | ||||||
| Modified residue | 162 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 166 | 1 | Phosphoserine; by UHMK1 By similarity | ||||||
| Modified residue | 171 | 1 | Citrulline By similarity | ||||||
Sequences
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References
| [1] | "Amino acid sequence of porcine myelin basic protein." Kira J., Deibler G.E., Krutzsch H.C., Martenson R.E. J. Neurochem. 44:134-142(1985) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE, METHYLATION AT ARG-107. Tissue: Brain. |
| [2] | Erratum Kira J., Deibler G.E., Krutzsch H.C., Martenson R.E. J. Neurochem. 44:1663-1663(1985) |
Cross-references
Sequence databases | |
|---|---|
| PIR | MBPGB. A61640. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| HOVERGEN | HBG008347. |
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... |
Entry information
| Entry name | MBP_PIG | ||||||||
| Accession | Primary (citable) accession number: P81558 Secondary accession number(s): P98189 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
