| IED ID | IndEnz0002003765 |
| Enzyme Type ID | protease003765 |
| Protein Name |
Ubiquitin carboxyl-terminal hydrolase MINDY-1 EC 3.4.19.12 Deubiquitinating enzyme MINDY-1 Protein FAM63A |
| Gene Name | MINDY1 FAM63A KIAA1390 |
| 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 | MEYHQPEDPAPGKAGTAEAVIPENHEVLAGPDEHPQDTDARDADGEAREREPADQALLPSQCGDNLESPLPEASSAPPGPTLGTLPEVETIRACSMPQELPQSPRTRQPEPDFYCVKWIPWKGEQTPIITQSTNGPCPLLAIMNILFLQWKVKLPPQKEVITSDELMAHLGNCLLSIKPQEKSEGLQLNFQQNVDDAMTVLPKLATGLDVNVRFTGVSDFEYTPECSVFDLLGIPLYHGWLVDPQSPEAVRAVGKLSYNQLVERIITCKHSSDTNLVTEGLIAEQFLETTAAQLTYHGLCELTAAAKEGELSVFFRNNHFSTMTKHKSHLYLLVTDQGFLQEEQVVWESLHNVDGDSCFCDSDFHLSHSLGKGPGAEGGSGSPETQLQVDQDYLIALSLQQQQPRGPLGLTDLELAQQLQQEEYQQQQAAQPVRMRTRVLSLQGRGATSGRPAGERRQRPKHESDCILL |
| Enzyme Length | 469 |
| Uniprot Accession Number | Q8N5J2 |
| Absorption | |
| Active Site | ACT_SITE 137; /note=Nucleophile; /evidence=ECO:0000305|PubMed:27292798; ACT_SITE 319; /note=Proton acceptor; /evidence=ECO:0000305|PubMed:27292798 |
| 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:0000269|PubMed:27292798}; |
| 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:0000269|PubMed:27292798, ECO:0000269|PubMed:28082312}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (3); Beta strand (10); Chain (1); Compositional bias (2); Erroneous initiation (1); Helix (10); Modified residue (2); Mutagenesis (30); Natural variant (1); Region (3); Sequence conflict (3); Site (3); Turn (1) |
| Keywords | 3D-structure;Alternative splicing;Hydrolase;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway |
| Interact With | Q53SE7; P55212; P36544; Q15038; Q96IK5 |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 103; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 441; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (8) |
| Cross Reference PDB | 5JKN; 5JQS; 5MN9; 6TUV; 6TXB; 6Y6R; 6YJG; 6Z90; |
| Mapped Pubmed ID | 15231747; 20711500; 25416956; 34529927; |
| Motif | |
| Gene Encoded By | |
| Mass | 51,778 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |