| IED ID | IndEnz0002016096 |
| Enzyme Type ID | protease016096 |
| Protein Name |
Myelin basic protein MBP Myelin A1 protein Myelin membrane encephalitogenic protein |
| Gene Name | MBP |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MGNHAGKRELNAEKASTNSETNRGESEKKRNLGELSRTTSEDNEVFGEADANQNNGTSSQDTAVTDSKRTADPKNAWQDAHPADPGSRPHLIRLFSRDAPGREDNTFKDRPSESDELQTIQEDSAATSESLDVMASQKRPSQRHGSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFGGDRGAPKRGSGKDSHHPARTAHYGSLPQKSHGRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQRPGFGYGGRASDYKSAHKGFKGVDAQGTLSKIFKLGGRDSRSGSPMARR |
| Enzyme Length | 304 |
| Uniprot Accession Number | P02686 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: The classic group of MBP isoforms (isoform 4-isoform 14) 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-isoform 3/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. {ECO:0000269|PubMed:8544862}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (4); Chain (1); Compositional bias (4); Erroneous initiation (1); Initiator methionine (4); Modified residue (39); Region (4); Sequence caution (2); Sequence conflict (1); Site (2) |
| Keywords | 3D-structure;Acetylation;Alternative splicing;Autoimmune encephalomyelitis;Cell membrane;Citrullination;Direct protein sequencing;Membrane;Methylation;Nucleus;Phosphoprotein;Reference proteome |
| Interact With | Q9GZU7; Q8I629; Q64702; P05067; Q9GZU7; O15194-2; Q9H8W4; P0DP24 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic side of myelin.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus {ECO:0000269|PubMed:22609403}. Note=Targeted to nucleus in oligodendrocytes. |
| Modified Residue | MOD_RES 96; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 141; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P02687"; MOD_RES 146; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P04370"; MOD_RES 148; /note="Phosphotyrosine"; /evidence="ECO:0000250|UniProtKB:P02688"; MOD_RES 151; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:P02688"; MOD_RES 153; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P04370"; MOD_RES 154; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:P02688"; MOD_RES 159; /note="Citrulline; in form C8"; /evidence="ECO:0000269|PubMed:2466844"; MOD_RES 165; /note="Citrulline; in form C8"; /evidence="ECO:0000269|PubMed:2466844"; MOD_RES 167; /note="Citrulline"; /evidence="ECO:0000269|PubMed:23828821"; MOD_RES 169; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:P04370"; MOD_RES 174; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P04370"; MOD_RES 177; /note="Omega-N-methylarginine"; /evidence="ECO:0000250|UniProtKB:P04370"; MOD_RES 183; /note="Omega-N-methylarginine"; /evidence="ECO:0000250|UniProtKB:P04370"; MOD_RES 190; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P02687"; MOD_RES 199; /note="Citrulline"; /evidence="ECO:0000269|PubMed:23828821"; MOD_RES 203; /note="Phosphotyrosine"; /evidence="ECO:0000250|UniProtKB:P04370"; MOD_RES 210; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P04370"; MOD_RES 214; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:P04370"; MOD_RES 229; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:P02688"; MOD_RES 231; /note="Citrulline"; /evidence="ECO:0000269|PubMed:23828821"; MOD_RES 232; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:P02687"; MOD_RES 237; /note="Deamidated glutamine"; /evidence="ECO:0000250"; MOD_RES 241; /note="Omega-N-methylarginine; alternate"; /evidence="ECO:0000269|PubMed:5128665"; MOD_RES 241; /note="Symmetric dimethylarginine; alternate"; /evidence="ECO:0000269|PubMed:5128665"; MOD_RES 249; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P25274"; MOD_RES 256; /note="Citrulline; in form C8"; /evidence="ECO:0000269|PubMed:2466844"; MOD_RES 264; /note="Citrulline; in form C8"; /evidence="ECO:0000269|PubMed:23828821, ECO:0000269|PubMed:2466844"; MOD_RES 281; /note="Deamidated glutamine"; /evidence="ECO:0000250"; MOD_RES 293; /note="Citrulline; in form C8"; /evidence="ECO:0000269|PubMed:2466844"; MOD_RES 295; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P02687"; MOD_RES 296; /note="Citrulline"; /evidence="ECO:0000269|PubMed:23828821"; MOD_RES 299; /note="Phosphoserine; by UHMK1"; /evidence="ECO:0000269|PubMed:10880969"; MOD_RES 303; /note="Citrulline"; /evidence="ECO:0000269|PubMed:23828821"; MOD_RES 304; /note="Citrulline; in form C8"; /evidence="ECO:0000269|PubMed:2466844"; MOD_RES P02686-3:2; /note="N-acetylalanine"; /evidence="ECO:0000269|PubMed:7544282"; MOD_RES P02686-4:2; /note="N-acetylalanine"; /evidence="ECO:0000269|PubMed:7544282"; MOD_RES P02686-5:2; /note="N-acetylalanine"; /evidence="ECO:0000269|PubMed:7544282"; MOD_RES P02686-6:2; /note="N-acetylalanine"; /evidence="ECO:0000269|PubMed:7544282" |
| Post Translational Modification | PTM: 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. {ECO:0000269|PubMed:23828821, ECO:0000269|PubMed:2466844, ECO:0000269|PubMed:5128665}.; PTM: The N-terminal alanine is acetylated (isoform 3, isoform 4, isoform 5 and isoform 6).; PTM: Arg-241 was found to be 6% monomethylated and 60% symmetrically dimethylated.; 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:0000269|PubMed:15100291}.; PTM: Phosphorylated by TAOK2, VRK2, MAPK11, MAPK12, MAPK14 and MINK1. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (6) |
| Cross Reference PDB | 1BX2; 1FV1; 1HQR; 1K2D; 1YMM; 1ZGL; |
| Mapped Pubmed ID | 10727776; 10779557; 11295122; 11356866; 11402450; 12150894; 12626795; 12939427; 14714495; 15695336; 15821740; 16049941; 16319321; 16713569; 1691612; 16923174; 17415991; 18007657; 18563468; 18634568; 1939237; 19494339; 20195357; 21131964; 23260142; 24412244; 25416956; 7515903; 7523603; 7685461; 7935840; 9460711; 9482678; 9782128; |
| Motif | |
| Gene Encoded By | |
| Mass | 33,117 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |