| IED ID | IndEnz0002015533 |
| Enzyme Type ID | protease015533 |
| Protein Name |
Deubiquitinase MYSM1 2A-DUB EC 3.4.19.- Myb-like, SWIRM and MPN domain-containing protein 1 |
| Gene Name | Mysm1 Kiaa1915 |
| 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 | MEAEEADVDVEGDVAAAAQPGNDESTASVFQDHYLDSTWRRENGCLPWTLDSTISDENRAIIEKMLLEEEYYLSNKSLPGKFWVNQKEDNKKYTNSLQKSSKAMVDSPAKPASHSVKWTVEEKELFEQGLAKFGRRWTKIATLLKSRTVLQVKSYARQYFKNKVKWDVEKETPTQKSSSDLQVKNKDDRTKAWAAACLRGSADPCLNAVKIEKLSDDEDVDITDELDELTSQTSQNSGSHLTLDVPNSKMYTTNQGELCQEGPLAKSSGESLQNVKQGEGEACSSSEIASWAEKQKSTDKNSAELNEKYNKVVEEHTLHRGEVREEAKHSPSPEPCERQDSSGNEMLLPPCQIEEENHEGEELKPPEQEVEIDRNVIQEEEKQAIPEFFEGRQTKTPERYLKIRNYILDQWEICKPKYLNKTSVRPGLKNCGDVNCIGRIHTYLELIGAINFGCEQAVYNRPQPLDKVRAADRKDAEAAYQLAWRLQSMRTRRRRVRDPWGNWCDAKDLEGQTFEHLSVEEMARRKEEEKCKPIKFSKASKLPKSSLDPFQLIPCNFFSEEKQEPFQVKVAAEALLIMNLHAHVSMAEVIGLLGGRYSEADKVLEVCAAEPCNSLSTGLQCEMDPVSQTQASETLALRGYSVIGWYHSHPAFDPNPSLRDIDTQAKYQSYFSRGGAKFIGMIVSPYNRSNPLPYSQITCLVISEEVSPDGTYRLPYKFEVQQMLEEPQWELVFEKTRWIIEKYRLSNSSVPMDRIFRRDSDLTCLQKLLECLRKTLSKVANCFIAEEFLTQIENLFLSNYKSKEENGLAEEDSTKELFM |
| Enzyme Length | 819 |
| Uniprot Accession Number | Q69Z66 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.19.- |
| Enzyme Function | FUNCTION: Metalloprotease with deubiquitinase activity that plays important regulator roles in hematopoietic stem cell function, blood cell production and immune response (PubMed:26474655, PubMed:27895164, PubMed:30405132). Participates in the normal programming of B-cell responses to antigen after the maturation process (PubMed:27895164). Within the cytoplasm, plays critical roles in the repression of innate immunity and autoimmunity (PubMed:26474655, PubMed:30405132). Removes 'Lys-63'-linked polyubiquitins from TRAF3 and TRAF6 complexes (PubMed:26474655). Attenuates NOD2-mediated inflammation and tissue injury by promoting 'Lys-63'-linked deubiquitination of RIPK2 component (PubMed:30405132). Suppresses the CGAS-STING1 signaling pathway by cleaving STING1 'Lys-63'-linked ubiquitin chains (PubMed:33086059). In the nucleus, acts as a hematopoietic transcription regulator derepressing a range of genes essential for normal stem cell differentiation including EBF1 and PAX5 in B-cells, ID2 in NK-cell progenitor or FLT3 in dendritic cell precursors (PubMed:22169041, PubMed:24062447, PubMed:25217698 PubMed:26348977). Deubiquitinates monoubiquitinated histone H2A, a specific tag for epigenetic transcriptional repression, leading to dissociation of histone H1 from the nucleosome (By similarity). {ECO:0000250|UniProtKB:Q5VVJ2, ECO:0000269|PubMed:22169041, ECO:0000269|PubMed:24062447, ECO:0000269|PubMed:25217698, ECO:0000269|PubMed:26348977, ECO:0000269|PubMed:26474655, ECO:0000269|PubMed:27895164, ECO:0000269|PubMed:30405132}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Chain (1); Compositional bias (1); Cross-link (1); Domain (3); Metal binding (3); Modified residue (4); Motif (2); Region (4); Sequence conflict (4) |
| Keywords | Activator;Alternative splicing;Chromatin regulator;Cytoplasm;DNA-binding;Hydrolase;Immunity;Isopeptide bond;Metal-binding;Metalloprotease;Nucleus;Phosphoprotein;Protease;Reference proteome;Transcription;Transcription regulation;Ubl conjugation;Ubl conjugation pathway;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26474655, ECO:0000269|PubMed:30405132}. Cytoplasm {ECO:0000269|PubMed:26474655, ECO:0000269|PubMed:30405132}. Note=Localizes to the cytoplasm in response to bacterial infection. {ECO:0000269|PubMed:26474655}. |
| Modified Residue | MOD_RES 107; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q5VVJ2; MOD_RES 215; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q5VVJ2; MOD_RES 233; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q5VVJ2; MOD_RES 332; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q5VVJ2 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12466851; 12520002; 14610273; 20799038; 21518438; 21677750; 22184403; 24014243; 24721909; 25340873; 25613381; 25710881; 26125289; 26768662; 26915790; 27277682; 27833034; 28066899; 28978033; 29203593; 29495602; 30895711; 32466590; 32641579; 33660780; |
| Motif | MOTIF 647..660; /note=JAMM motif; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; MOTIF 765..769; /note=LXXLL motif |
| Gene Encoded By | |
| Mass | 93,475 |
| Kinetics | |
| Metal Binding | METAL 647; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 649; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 660; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182 |
| Rhea ID | |
| Cross Reference Brenda |