IED ID | IndEnz0002013576 |
Enzyme Type ID | protease013576 |
Protein Name |
Myelin basic protein MBP Myelin A1 protein |
Gene Name | Mbp Shi |
Organism | Mus musculus (Mouse) |
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 Mus Mus Mus musculus (Mouse) |
Enzyme Sequence | MGNHSGKRELSAEKASKDGEIHRGEAGKKRSVGKLSQTASEDSDVFGEADAIQNNGTSAEDTAVTDSKHTADPKNNWQGAHPADPGNRPHLIRLFSRDAPGREDNTFKDRPSESDELQTIQEDPTAASGGLDVMASQKRPSQRSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFSGDRGAPKRGSGKDSHTRTTHYGSLPQKSQHGRTQDENPVVHFFKNIVTPRTPPPSQGKGGRDSRSGSPMARR |
Enzyme Length | 250 |
Uniprot Accession Number | P04370 |
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 13) 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 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 to optional post-translational modifications give a wide spectrum of isomers, with each of them potentially having a specialized function. {ECO:0000269|PubMed:11145205}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Alternative sequence (9); Beta strand (1); Chain (1); Compositional bias (5); Helix (1); Initiator methionine (6); Modified residue (42); Region (2); Sequence conflict (1); Site (1) |
Keywords | 3D-structure;Acetylation;Alternative splicing;Autoimmune encephalomyelitis;Cell membrane;Citrullination;Cytoplasm;Direct protein sequencing;Membrane;Methylation;Nucleus;Phosphoprotein;Reference proteome |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: [Isoform 13]: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: [Isoform 12]: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: [Isoform 11]: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: [Isoform 10]: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: [Isoform 9]: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: [Isoform 8]: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: [Isoform 7]: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: [Isoform 6]: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: [Isoform 5]: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: [Isoform 4]: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. Nucleus.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Nucleus. |
Modified Residue | MOD_RES 31; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 40; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 141; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P02687"; MOD_RES 144; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 146; /note="Phosphotyrosine"; /evidence="ECO:0000250|UniProtKB:P02688"; MOD_RES 149; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:P02688"; MOD_RES 151; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 152; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:P02688"; MOD_RES 157; /note="Citrulline"; /evidence="ECO:0000250"; MOD_RES 163; /note="Citrulline"; /evidence="ECO:0000250"; MOD_RES 167; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:16452087, ECO:0007744|PubMed:21183079"; MOD_RES 172; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:15648052, ECO:0007744|PubMed:21183079"; MOD_RES 175; /note="Omega-N-methylarginine"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 181; /note="Omega-N-methylarginine"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 188; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P02687"; MOD_RES 197; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 199; /note="Phosphotyrosine"; /evidence="ECO:0007744|PubMed:18034455"; MOD_RES 206; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 211; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 226; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:P02688"; MOD_RES 229; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:16452087, ECO:0007744|PubMed:21183079"; MOD_RES 234; /note="Deamidated glutamine"; /evidence="ECO:0000250"; MOD_RES 239; /note="Citrulline"; /evidence="ECO:0000250"; MOD_RES 241; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P02687"; MOD_RES 245; /note="Phosphoserine; by UHMK1"; /evidence="ECO:0000250|UniProtKB:P02687"; MOD_RES 250; /note="Citrulline"; /evidence="ECO:0000250"; MOD_RES P04370-4:2; /note="N-acetylalanine"; /evidence="ECO:0000250|UniProtKB:P02686"; MOD_RES P04370-4:122; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:16452087"; MOD_RES P04370-4:139; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:16452087"; MOD_RES P04370-4:151; /note="Phosphotyrosine"; /evidence="ECO:0007744|PubMed:18034455"; MOD_RES P04370-5:2; /note="N-acetylalanine"; /evidence="ECO:0000250|UniProtKB:P02686"; MOD_RES P04370-5:96; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:16452087"; MOD_RES P04370-5:113; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:16452087"; MOD_RES P04370-5:125; /note="Phosphotyrosine"; /evidence="ECO:0007744|PubMed:18034455"; MOD_RES P04370-6:2; /note="N-acetylalanine"; /evidence="ECO:0000250|UniProtKB:P02686"; MOD_RES P04370-6:122; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:16452087"; MOD_RES P04370-7:2; /note="N-acetylalanine"; /evidence="ECO:0000305"; MOD_RES P04370-8:2; /note="N-acetylalanine"; /evidence="ECO:0000250|UniProtKB:P02686"; MOD_RES P04370-8:96; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:16452087"; MOD_RES P04370-9:2; /note="N-acetylalanine"; /evidence="ECO:0000305"; MOD_RES P04370-10:135; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:16452087"; MOD_RES P04370-10:147; /note="Phosphotyrosine"; /evidence="ECO:0007744|PubMed:18034455" |
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.; PTM: Methylated on arginine residues; decreases with the age of the animal, making MBP more cationic.; 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 | NMR spectroscopy (1); X-ray crystallography (1) |
Cross Reference PDB | 1U3H; 2LUG; |
Mapped Pubmed ID | 10049721; 10077700; 10359833; 10366625; 10415003; 10457012; 10460234; 10460258; 10501973; 10512984; 10594919; 10640866; 10686606; 10706738; 10707971; 10725249; 10739574; 10843682; 10845771; 10854769; 10884306; 10903450; 11165432; 11173922; 11217851; 11264304; 11336692; 11390667; 11435472; 11526078; 11535634; 11746780; 11799060; 11809732; 11830569; 11841829; 11869044; 11950511; 11955448; 12012374; 12176974; 12186854; 12372841; 12374744; 12466851; 12490199; 12643284; 12718855; 12799019; 1280107; 1281368; 12837627; 12842915; 12843252; 1285071; 12901870; 12902388; 12966208; 12971894; 1302014; 1311971; 1318958; 1319776; 1353738; 1354640; 1354644; 1358813; 1370079; 1371758; 1377283; 1396170; 14534257; 14602683; 14613971; 14614079; 14630913; 14685273; 15102707; 15139287; 15146180; 15226307; 15312649; 15326615; 15372074; 15485773; 15509523; 15522783; 15525335; 15528192; 15531362; 15544353; 15546149; 15579137; 15601927; 15629701; 15659488; 15664161; 15713637; 1572638; 15731004; 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19642704; 19692707; 19723505; 19739253; 19741146; 19799774; 19805360; 19806666; 1981056; 19838178; 19855925; 19892785; 19896473; 19903451; 19935654; 1996138; 20091777; 20111592; 20144603; 20169373; 20171203; 20181595; 20308050; 20334434; 20457761; 20526343; 20578039; 20593886; 20607717; 20648636; 20713009; 20805985; 20807757; 20825492; 20831157; 20862255; 20925061; 20925478; 21085684; 2113569; 21144847; 21185260; 21210220; 21220101; 21238928; 21248112; 21267068; 21285371; 21389218; 21472765; 21525285; 21536740; 21593306; 21613327; 21637753; 2165966; 21670295; 2167232; 21824506; 21844226; 21864586; 21887699; 21889463; 22028197; 22042377; 22046273; 22056141; 22128153; 22303455; 22337526; 22365546; 22447683; 22496821; 22522171; 22529900; 22542597; 22609403; 22627280; 22728818; 22806269; 22807310; 22844494; 2289413; 22947219; 22998872; 23184356; 23308235; 23332759; 23396245; 23482494; 23575864; 23583582; 23637331; 23678945; 23744272; 23762018; 23861868; 23891804; 2410137; 24101522; 24115331; 2411865; 2414073; 24151333; 24154525; 24227784; 24257626; 2427738; 2429310; 24301385; 2432182; 2434242; 2434243; 24355921; 24391449; 2440764; 2441806; 24423059; 2442307; 24439382; 24449836; 24459152; 24507192; 24512632; 24599474; 2465759; 24671420; 24713852; 24762439; 2483096; 24849898; 24863526; 24917498; 24931760; 24948802; 24952961; 24956930; 24979729; 24997765; 25079316; 25131634; 25138526; 25343306; 25382142; 25401469; 25429065; 25450959; 2547434; 25568100; 25680202; 25708149; 25754822; 25762662; 2579195; 25810530; 25834054; 25849768; 25988834; 26077106; 26081148; 26115514; 26166300; 26212662; 26305941; 26317513; 26345464; 26497031; 26507463; 26525805; 26604141; 26637354; 26733804; 26745185; 26746235; 26798014; 26801084; 26937016; 26940020; 26961956; 27144456; 27149841; 27213272; 27294512; 27307230; 27346352; 27416896; 27470661; 27532821; 27573615; 27614087; 27680501; 27816769; 27829055; 27862528; 27997532; 28063167; 28076777; 28193690; 2831467; 28320842; 28336932; 28344592; 28513333; 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Motif | |
Gene Encoded By | |
Mass | 27,168 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |