Detail Information for IndEnz0002008868
IED ID IndEnz0002008868
Enzyme Type ID protease008868
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 PP1490
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 MPQASEHRLGRTREPPVNIQPRVGSKLPFAPRARSKERRNPASGPNPMLRPLPPRPGLPDERLKKLELGRGRTSGPRPRGPLRADHGVPLPGSPPPTVALPLPSRTNLARSKSVSSGDLRPMGIALGGHRGTGELGAALSRLALRPEPPTLRRSTSLRRLGGFPGPPTLFSIRTEPPASHGSFHMISARSSEPFYSDDKMAHHTLLLGSGHVGLRNLGNTCFLNAVLQCLSSTRPLRDFCLRRDFRQEVPGGGRAQELTEAFADVIGALWHPDSCEAVNPTRFRAVFQKYVPSFSGYSQQDAQEFLKLLMERLHLEINRRGRRAPPILANGPVPSPPRRGGALLEEPELSDDDRANLMWKRYLEREDSKIVDLFVGQLKSCLKCQACGYRSTTFEVFCDLSLPIPKKGFAGGKVSLRDCFNLFTKEEELESENAPVCDRCRQKTRSTKKLTVQRFPRILVLHLNRFSASRGSIKKSSVGVDFPLQRLSLGDFASDKAGSPVYQLYALCNHSGSVHYGHYTALCRCQTGWHVYNDSRVSPVSENQVASSEGYVLFYQLMQEPPRCL
Enzyme Length 565
Uniprot Accession Number Q9UK80
Absorption
Active Site ACT_SITE 221; /note="Nucleophile"; 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 (By similarity). Also capable of removing NEDD8 from NEDD8 conjugates but has no effect on Sentrin-1 conjugates (PubMed:10799498). Deubiquitinates BAZ2A/TIP5 leading to its stabilization (PubMed:26100909). {ECO:0000250|UniProtKB:Q9QZL6, ECO:0000269|PubMed:10799498, ECO:0000269|PubMed:26100909}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Alternative sequence (3); Beta strand (14); Chain (1); Compositional bias (1); Domain (1); Erroneous initiation (1); Frameshift (2); Helix (13); Metal binding (4); Motif (1); Mutagenesis (1); Natural variant (3); Region (1); Sequence conflict (3); Turn (1)
Keywords 3D-structure;Activator;Alternative splicing;Chromatin regulator;Cytoplasm;Hydrolase;Metal-binding;Nucleus;Protease;Reference proteome;Thiol protease;Transcription;Transcription regulation;Ubl conjugation pathway;Zinc
Interact With Q6UY14-3; Q16630-2; O95967; Q9NYD6; Q7L273; Q6A162; P09936
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21888622}. Nucleus {ECO:0000269|PubMed:21888622}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (3)
Cross Reference PDB 2Y5B; 3I3T; 3MTN;
Mapped Pubmed ID 12887920; 15231747; 16260783; 16603398; 16953224; 18172164; 18178551; 19615732; 19910467; 20467438; 22179575; 22435550; 22848449; 23287719; 23313255; 23395819; 24098568; 24493797; 25197364; 25305019; 25416956; 28254948;
Motif MOTIF 134..152; /note=Nuclear export signal
Gene Encoded By
Mass 62,656
Kinetics
Metal Binding METAL 384; /note=Zinc; METAL 387; /note=Zinc; METAL 437; /note=Zinc; METAL 440; /note=Zinc
Rhea ID
Cross Reference Brenda 3.4.19.12;