Detail Information for IndEnz0002011614
IED ID IndEnz0002011614
Enzyme Type ID protease011614
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 Usp23
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 MPQASEHRLGRTREPPVNVQPRVGAKIPFPPRARSKERRNPVPGPNSMLRPLPPRPGPPDERLKKLELGRGRTSGSRPRGPLRADHGVPLPGSPPPAVALPLPSRTNLARSKSVSSGDLRPMGIALGGHRGAGELGAALSRLALRPEPPTLRRSTSLRRLGGFPGPPTLLSIRTEPPTSHGSFHMISARPSEPFYSDDKMAHHTLLLGSGHVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVPGGGRAQELTEAFADVIGALWHPDSCEAVNPTRFRAVFQKYVPSFSGYSQQDAQEFLKLLMERLHLEINRRGRRAPPILASGPVPSPPRRGGGALHEEPELSDDDRANLMWKRYLEREDSKIVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGFAGGKVSLRDCFSLFTKEEELESENAPVCDRCRQKTRSTKKLTVQRFPRILVLHLNRFSTSRGSIKKSSVGVDFPLQRLSLGDFASDKAGSPVYQLYALCNHSGSVHYGHYTALCRCQTGWHVYNDSRVSPVSENQVASSEGYVLFYQLMQEPLRCL
Enzyme Length 566
Uniprot Accession Number Q9QZL6
Absorption
Active Site ACT_SITE 221; /note="Nucleophile"; ACT_SITE 519; /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; Evidence={ECO:0000269|PubMed:18172164};
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 (By similarity). {ECO:0000250|UniProtKB:Q9UK80, ECO:0000269|PubMed:18172164}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Compositional bias (1); Domain (1); Metal binding (4); Motif (1); Mutagenesis (3); Region (3); Sequence conflict (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 10051400; 11217851; 12466851; 14610273; 15687484; 19910467; 21267068; 21677750; 24493797; 25680095; 27621083; 27857073; 27886188; 28254948; 33628844;
Motif MOTIF 134..152; /note=Nuclear export signal; /evidence=ECO:0000250
Gene Encoded By
Mass 62,673
Kinetics
Metal Binding METAL 385; /note=Zinc; /evidence=ECO:0000250; METAL 388; /note=Zinc; /evidence=ECO:0000250; METAL 438; /note=Zinc; /evidence=ECO:0000250; METAL 441; /note=Zinc; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda