| IED ID | IndEnz0002013517 |
| Enzyme Type ID | protease013517 |
| Protein Name |
Ubiquitin carboxyl-terminal hydrolase 21 EC 3.4.19.12 Deubiquitinating enzyme 21 Ubiquitin thioesterase 21 Ubiquitin-specific-processing protease 21 |
| Gene Name | Usp21 |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MPQASEHRLGRTREPPVNVQPRVGAKIPFPPRARSKERRNPVPGPNSMLRPLPPRPGPPDERLKKLDLGRGRTSGSRPRGPLRADHGVPLPGSPPPTVALPLPSRTNLTRSKSVSSGDLRPMGIALGGHRGTGELGAALSRLALRPEPPTLRRSTSLRRLGGFPGPPTLLSIRTEPPPSHGSFHMISARPSEPFYSDDKMAHHTLLLGSGHVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVPGGGRAQELTEAFADVIGALWHPDSCEAVNPTRFRAVFQKYVPSFSGYSQQDAQEFLKLLMERLHLEINRRGRRAPPILASGPVPSPPRRGGALHEEPELSDDDRANLMWKRYLEREDSKIVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGFAGGKVSLRDCFSLFTKEEELESENAPVCDRCRQKTRSTKKLTVQRFPRILVLHLNRFSTSRGSIKKSSVGVDFPLQRLSLGDFASDKVGSPVYQLYALCNHSGSVHYGHYTALCRCQTGWHVYNDSRVSPVSENQVASSEGYVLFYQLMQEPPRCL |
| Enzyme Length | 565 |
| Uniprot Accession Number | B2GUX4 |
| Absorption | |
| Active Site | ACT_SITE 221; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 518; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" |
| 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; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Deubiquitinates histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A releaves the repression of di- and trimethylation of histone H3 at 'Lys-4', resulting in regulation of transcriptional initiation. Regulates gene expression via histone H2A deubiquitination. Also capable of removing NEDD8 from NEDD8 conjugates but has no effect on Sentrin-1 conjugates. Deubiquitinates BAZ2A/TIP5 leading to its stabilization. {ECO:0000250|UniProtKB:Q9UK80}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (2); Domain (1); Metal binding (4); Motif (1); Region (2) |
| Keywords | Activator;Chromatin regulator;Cytoplasm;Hydrolase;Metal-binding;Nucleus;Protease;Reference proteome;Thiol protease;Transcription;Transcription regulation;Ubl conjugation pathway;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 22298430; |
| Motif | MOTIF 134..152; /note=Nuclear export signal; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 62,700 |
| Kinetics | |
| Metal Binding | METAL 384; /note=Zinc; /evidence=ECO:0000250; METAL 387; /note=Zinc; /evidence=ECO:0000250; METAL 437; /note=Zinc; /evidence=ECO:0000250; METAL 440; /note=Zinc; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |