| IED ID | IndEnz0002016242 |
| Enzyme Type ID | protease016242 |
| Protein Name |
Ubiquitin carboxyl-terminal hydrolase MINDY-1 EC 3.4.19.12 Deubiquitinating enzyme MINDY-1 NF-E2 inducible protein Protein FAM63A |
| Gene Name | Mindy1 Fam63a Ni |
| 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 | MEQPQTENPAPSKATSAETVESENHEALSGPEKHPQDKDGADADGAAGEQEPGDQTLPPAQDGENLECPPPEASSSPPGPACGTSPKVETAEVCSRPQELPQSPRIQQPELDFYCVKWIPWKGERTPIITQSTNGPCPLLAIMNILFLQWKVKLPPQKEVITSDELLTHLGNCLLSIKPQEKSEGLQLNFQQNVDDAMTVLPKLATGLDVNVRFTGVSDFEYTPECSIFDLLGIPLYHGWLVDPQSPEAVSAVGKLSYNQLVEKIITCKHSSDSNLVTEGLVAEQFLETTAAQLTYHGLCELTAAATEDELSVFFRNNHFSTMTKHKSHLYLLVTDQGFLQEEQVVWESLHNVDGDSCFCDSDFHLSHSLGKSHGAEGGGGSPEKQLQVDQDYLIALSLQQQQQPQGTLGLSDLELAQQLQQEEYQQQQAVQPVRTRAPSPQGRGATSGRPAGERRQRSKTESDCVLL |
| Enzyme Length | 468 |
| Uniprot Accession Number | Q76LS9 |
| Absorption | |
| Active Site | ACT_SITE 137; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q8N5J2; ACT_SITE 319; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:Q8N5J2 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q8N5J2}; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Hydrolase that can specifically remove 'Lys-48'-linked conjugated ubiquitin from proteins. Has exodeubiquitinase activity and has a preference for long polyubiquitin chains. May play a regulatory role at the level of protein turnover. {ECO:0000250|UniProtKB:Q8N5J2}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (3); Chain (1); Compositional bias (2); Modified residue (2); Region (3); Sequence caution (1); Sequence conflict (2); Site (3) |
| Keywords | Alternative splicing;Hydrolase;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 103; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"; MOD_RES 440; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19144319" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11004510; 11217851; 12466851; 14610273; 14621295; 16481151; 17923245; 18799693; 21677750; 25849460; 26398943; 27626380; 29644784; |
| Motif | |
| Gene Encoded By | |
| Mass | 51,226 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |