| IED ID | IndEnz0002001285 |
| Enzyme Type ID | protease001285 |
| Protein Name |
Myelin basic protein MBP |
| Gene Name | Mbp |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MASQKRPSQRHGSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFSGDRGAPKRGSGKVPWLKQSRSPLPSHARSRPGLCHMYKDSHTRTTHYGSLPQKSQRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTLSKIFKLGGRDSRSGSPMARR |
| Enzyme Length | 195 |
| Uniprot Accession Number | P02688 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | 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). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (3); Chain (1); Initiator methionine (1); Modified residue (31); Region (2); Sequence conflict (6); Site (2) |
| Keywords | Acetylation;Alternative splicing;Autoimmune encephalomyelitis;Cell membrane;Citrullination;Direct protein sequencing;Membrane;Methylation;Phosphoprotein;Reference proteome |
| Interact With | Q62976 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic side of myelin. |
| Modified Residue | MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000269|PubMed:4141893; MOD_RES 8; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P02687; MOD_RES 13; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P04370; MOD_RES 15; /note=Phosphotyrosine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 18; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 20; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 21; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 26; /note=Citrulline; /evidence=ECO:0000250; MOD_RES 32; /note=Citrulline; /evidence=ECO:0000250; MOD_RES 36; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 41; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 44; /note=Omega-N-methylarginine; /evidence=ECO:0000250|UniProtKB:P04370; MOD_RES 50; /note=Omega-N-methylarginine; /evidence=ECO:0000250|UniProtKB:P04370; MOD_RES 57; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P02687; MOD_RES 92; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P04370; MOD_RES 94; /note=Phosphotyrosine; /evidence=ECO:0000250|UniProtKB:P04370; MOD_RES 101; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P04370; MOD_RES 104; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P04370; MOD_RES 119; /note=Phosphothreonine; /evidence=ECO:0000269|Ref.10; MOD_RES 122; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P02687; MOD_RES 127; /note=Deamidated glutamine; /evidence=ECO:0000250; MOD_RES 131; /note=Omega-N-methylarginine; alternate; /evidence=ECO:0000269|PubMed:4141893; MOD_RES 131; /note=Symmetric dimethylarginine; alternate; /evidence=ECO:0000269|PubMed:4141893; MOD_RES 139; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P25274; MOD_RES 146; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P02687; MOD_RES 154; /note=Citrulline; /evidence=ECO:0000250; MOD_RES 172; /note=Deamidated glutamine; /evidence=ECO:0000250; MOD_RES 184; /note=Citrulline; /evidence=ECO:0000250; MOD_RES 186; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P02687; MOD_RES 190; /note=Phosphoserine; by UHMK1; /evidence=ECO:0000250|UniProtKB:P02687; MOD_RES 195; /note=Citrulline; /evidence=ECO:0000250 |
| Post Translational Modification | PTM: As in other animals, several charge isomers may be produced as a result of optional post-translational modifications, such as phosphorylation of serine or threonine residues, deamidation of glutamine or asparagine residues, citrullination and methylation of arginine residues. {ECO:0000269|PubMed:4141893, ECO:0000269|Ref.10}.; PTM: Arg-131 was found to be 44% monomethylated and 11% symmetrically dimethylated.; PTM: Phosphorylated by TAOK2, VRK2, MAPK11, MAPK12, MAPK14 and MINK1. {ECO:0000250}.; PTM: Proteolytically cleaved in B cell lysosomes by cathepsin CTSG which degrades the major immunogenic MBP epitope and prevents the activation of MBP-specific autoreactive T cells. {ECO:0000250|UniProtKB:P02686}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10212300; 10537049; 11460777; 11592121; 12210134; 12390518; 12887683; 15695521; 15869936; 16773652; 17610306; 17960831; 18583256; 18821983; 19026719; 19178193; 19211156; 19855925; 20637745; 20882567; 21357748; 21401967; 21479584; 21892882; 21906685; 21996274; 22676642; 22750584; 22835759; 23146304; 23245577; 23614640; 23667870; 23715956; 23727401; 23735240; 24026164; 24321769; 24524292; 2462020; 25003183; 25282817; 25512606; 25847153; 26002313; 27230884; 27346352; 29073112; 29742816; 30926549; 31885393; |
| Motif | |
| Gene Encoded By | |
| Mass | 21,502 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |