| IED ID | IndEnz0002015532 |
| Enzyme Type ID | protease015532 |
| Protein Name |
Deubiquitinase MYSM1 2A-DUB EC 3.4.19.- Myb-like, SWIRM and MPN domain-containing protein 1 |
| Gene Name | MYSM1 KIAA1915 |
| 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 | MAAEEADVDIEGDVVAAAGAQPGSGENTASVLQKDHYLDSSWRTENGLIPWTLDNTISEENRAVIEKMLLEEEYYLSKKSQPEKVWLDQKEDDKKYMKSLQKTAKIMVHSPTKPASYSVKWTIEEKELFEQGLAKFGRRWTKISKLIGSRTVLQVKSYARQYFKNKVKCGLDKETPNQKTGHNLQVKNEDKGTKAWTPSCLRGRADPNLNAVKIEKLSDDEEVDITDEVDELSSQTPQKNSSSDLLLDFPNSKMHETNQGEFITSDSQEALFSKSSRGCLQNEKQDETLSSSEITLWTEKQSNGDKKSIELNDQKFNELIKNCNKHDGRGIIVDARQLPSPEPCEIQKNLNDNEMLFHSCQMVEESHEEEELKPPEQEIEIDRNIIQEEEKQAIPEFFEGRQAKTPERYLKIRNYILDQWEICKPKYLNKTSVRPGLKNCGDVNCIGRIHTYLELIGAINFGCEQAVYNRPQTVDKVRIRDRKDAVEAYQLAQRLQSMRTRRRRVRDPWGNWCDAKDLEGQTFEHLSAEELAKRREEEKGRPVKSLKVPRPTKSSFDPFQLIPCNFFSEEKQEPFQVKVASEALLIMDLHAHVSMAEVIGLLGGRYSEVDKVVEVCAAEPCNSLSTGLQCEMDPVSQTQASETLAVRGFSVIGWYHSHPAFDPNPSLRDIDTQAKYQSYFSRGGAKFIGMIVSPYNRNNPLPYSQITCLVISEEISPDGSYRLPYKFEVQQMLEEPQWGLVFEKTRWIIEKYRLSHSSVPMDKIFRRDSDLTCLQKLLECMRKTLSKVTNCFMAEEFLTEIENLFLSNYKSNQENGVTEENCTKELLM |
| Enzyme Length | 828 |
| Uniprot Accession Number | Q5VVJ2 |
| 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:24062447, PubMed:26220525, PubMed:28115216). Participates in the normal programming of B-cell responses to antigen after the maturation process (By similarity). Within the cytoplasm, plays critical roles in the repression of innate immunity and autoimmunity (PubMed:33086059). Removes 'Lys-63'-linked polyubiquitins from TRAF3 and TRAF6 complexes (By similarity). Attenuates NOD2-mediated inflammation and tissue injury by promoting 'Lys-63'-linked deubiquitination of RIPK2 component (By similarity). 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:24062447). Deubiquitinates monoubiquitinated histone H2A, a specific tag for epigenetic transcriptional repression, leading to dissociation of histone H1 from the nucleosome (PubMed:17707232). {ECO:0000250|UniProtKB:Q69Z66, ECO:0000269|PubMed:17707232, ECO:0000269|PubMed:22169041, ECO:0000269|PubMed:24062447, ECO:0000269|PubMed:26220525, ECO:0000269|PubMed:28115216, ECO:0000269|PubMed:33086059}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Beta strand (4); Chain (1); Cross-link (1); Domain (3); Erroneous initiation (2); Helix (8); Metal binding (3); Modified residue (6); Motif (2); Mutagenesis (1); Natural variant (5); Region (1); Sequence conflict (3); Turn (1) |
| Keywords | 3D-structure;Activator;Alternative splicing;Chromatin regulator;Cytoplasm;DNA-binding;Disease variant;Hydrolase;Immunity;Isopeptide bond;Metal-binding;Metalloprotease;Nucleus;Phosphoprotein;Protease;Reference proteome;Transcription;Transcription regulation;Ubl conjugation;Ubl conjugation pathway;Zinc |
| Interact With | Q5T2T1 |
| Induction | INDUCTION: By DNA from viral infection and intracellular DNA. {ECO:0000269|PubMed:33086059}. |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:17707232}. Cytoplasm {ECO:0000250|UniProtKB:Q69Z66}. Note=Localizes to the cytoplasm in response to bacterial infection. {ECO:0000250|UniProtKB:Q69Z66}. |
| Modified Residue | MOD_RES 110; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 218; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"; MOD_RES 236; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:19690332"; MOD_RES 242; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 267; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 340; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21406692" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (2) |
| Cross Reference PDB | 2CU7; 2DCE; |
| Mapped Pubmed ID | 27590507; 28498834; 31607324; 31761786; 32466590; |
| Motif | MOTIF 656..669; /note=JAMM motif; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; MOTIF 774..778; /note=LXXLL motif |
| Gene Encoded By | |
| Mass | 95,032 |
| Kinetics | |
| Metal Binding | METAL 656; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 658; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 669; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182 |
| Rhea ID | |
| Cross Reference Brenda |