| IED ID | IndEnz0002015529 |
| Enzyme Type ID | protease015529 |
| Protein Name |
Histone H2A deubiquitinase MYSM1 2A-DUB EC 3.4.19.- Myb-like, SWIRM and MPN domain-containing protein 1 |
| Gene Name | MYSM1 BRAFLDRAFT_86936 |
| Organism | Branchiostoma floridae (Florida lancelet) (Amphioxus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Cephalochordata Leptocardii Amphioxiformes Branchiostomidae Branchiostoma Branchiostoma floridae (Florida lancelet) (Amphioxus) |
| Enzyme Sequence | MADDEEIDIEGDDDAPLLFDHKDDALALPDLPGYEPNWMFDHGQEIYGRSWTSISQFVQTRTPLQVKNYARHFFKTKVVQKVEEGEDEDVDIEGEESGEEAVMELRSTCGLNPAQPAVVTSDDTSTGENVMEETEAVTEDHPSLDNLVQDDREMPQQETTGDGEQYPMDEHFLPVFPWQPDDTQNRVIVERIEGSVGLGSVRGDKDVRPVPGVEQNTYGPHTDMFQVQNTLLAFEKQVGADRIFEGPSXSKNEATDTQTEVSETKTEVIERQTESQVDATHMHTYGDGLMGSIERLTESVSSSELKEDLKTGIEYVEKDDATDSSSTAKGYDNYTLDHPEDRSKPDSVVSEKWSCEEAMSSHTDGRTFSDSDSGKETYDLPRYNTTIFQGHSEDETSDAGQAEEETFFTFKKPTEEVVLDRSVITEEEKEVHKEFFDGRQTKTPERYLKIRNHLLDCWERTKPEYLRKTVARAGLRNCGDVNCIGRIHGYLERIGAINFGCEEANRGEFPVAKVGVKRNPQGHGEQLALQAARLESMHVTSDELEKQDGGVSQIRPNRSRAARTNLNSFSYDPFKLVPCKRFSEESPAPFSVKIHATALVTIDMHAHISTAEVIGLLGGVFHRDPGALEVASAEPCNSLSTGMQCEMDPVSQTQASEALSQAGYSVVGWYHSHPTFAPNPSVRDIETQTKFQEWFAQGGSPFIGIIVNPYSSTRISPLSRVTCLTISSEWNPPAIQRVKLLSRYAGHTDTTYMDKMLYSLSGHLCRGNADSDEDGNSESLTLLTDIRDIFANSWTSSLGTTPRSSIASL |
| Enzyme Length | 809 |
| Uniprot Accession Number | B6MUN4 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.19.- |
| Enzyme Function | FUNCTION: Metalloprotease that specifically deubiquitinates monoubiquitinated histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Preferentially deubiquitinates monoubiquitinated H2A in hyperacetylated nucleosomes. Deubiquitination of histone H2A leads to facilitate the phosphorylation and dissociation of histone H1 from the nucleosome. Acts as a coactivator by participating in the initiation and elongation steps of androgen receptor (AR)-induced gene activation (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (1); Domain (3); Metal binding (3); Motif (1); Region (3) |
| Keywords | Activator;Chromatin regulator;DNA-binding;Hydrolase;Metal-binding;Metalloprotease;Nucleus;Protease;Reference proteome;Transcription;Transcription regulation;Ubl conjugation pathway;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 671..684; /note=JAMM motif; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182 |
| Gene Encoded By | |
| Mass | 90,132 |
| Kinetics | |
| Metal Binding | METAL 671; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 673; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 684; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182 |
| Rhea ID | |
| Cross Reference Brenda |