IED ID | IndEnz0002011799 |
Enzyme Type ID | protease011799 |
Protein Name |
Ubiquitin carboxyl-terminal hydrolase 16 EC 3.4.19.12 Deubiquitinating enzyme 16 Ubiquitin thioesterase 16 Ubiquitin-specific-processing protease 16 |
Gene Name | Usp16 |
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 | MGKKRTKGKSVPEKASSESTEPMCRHLRKGLEQGNLKKALVNVEWNICQDCKTDNKVKDKSEEEAEDPSVWLCLKCGHQGCGRDSQEQHALKHYTTPRSEPHYLVLSLDNWSVWCYKCDEEIKYCSSNRLGQVVDYVRKQAGRITSKPAEKNNGHIELENKKLEKESKNEQEREKSESMAKENIPLDSASQITVKGLSNLGNTCFFNAVMQNLSQTPVLRELLKEVKMSGTIVKIEPPDLALTEPLEVNLEPPGPLTLAMSQFLNEMQENKKRIVTPKELFSQVCKKATRFKGYQQQDSQELLRYLLDGMRAEEHQRVSKGILKAFGNSTEKLDEEVKNKVKDYEKKKAIPSFVDRIFGGELTSTIMCDDCRTVSLVHESFLDLSLPVLDDQSGKKNINDKNVKKTMEEEDKDSEEEKDDSYMKTRSDVPSGTSKHTQKKAKKQAKKQAKNQRRQQKIQERFLHFNEICTTNYTEDNDHEAETALPGEGEVDTEFNRGSQEELTQTELCANQKDVNGQEEMIESAADERKCPEHPEVKSVSTESDLGSLTSAPECPRDLNGAFLEERTSGELDITNGLKNLTLNAAVDPDEISIEILNDSHSPALKVYEVMNEDPETAFCTLANREAFSTDECSIQHCLYQFTRNEKLQDANKLLCEVCTRRQCNGPKANIKGERKHVYTNAKKQMLVSLAPPVLTLHLKRFQQAGFNLRKVNKHIKFPEILDLAPFCTLKCKNVAEESTRVLYSLYGVVEHSGTMRSGHYTAYAKERTASCHLSNLVLHGDIPQDCEMESTKGQWFHISDTHVQAVPITKVLNSQAYLLFYERIL |
Enzyme Length | 826 |
Uniprot Accession Number | Q2KJ09 |
Absorption | |
Active Site | ACT_SITE 204; /note=Nucleophile; /evidence=ECO:0000255|HAMAP-Rule:MF_03062; ACT_SITE 760; /note=Proton acceptor; /evidence=ECO:0000255|HAMAP-Rule:MF_03062 |
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:0000255|HAMAP-Rule:MF_03062}; |
DNA Binding | |
EC Number | 3.4.19.12 |
Enzyme Function | FUNCTION: Specifically deubiquitinates 'Lys-120' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3 (H3S10ph), and is required for chromosome segregation when cells enter into mitosis. In resting B- and T-lymphocytes, phosphorylation by AURKB leads to enhance its activity, thereby maintaining transcription in resting lymphocytes. Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B. {ECO:0000255|HAMAP-Rule:MF_03062}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Alternative sequence (1); Chain (1); Compositional bias (4); Cross-link (1); Domain (1); Metal binding (12); Modified residue (2); Region (4); Sequence caution (1); Zinc finger (1) |
Keywords | Activator;Alternative splicing;Cell cycle;Cell division;Chromatin regulator;Hydrolase;Isopeptide bond;Metal-binding;Mitosis;Nucleus;Phosphoprotein;Protease;Reference proteome;Thiol protease;Transcription;Transcription regulation;Ubl conjugation;Ubl conjugation pathway;Zinc;Zinc-finger |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03062}. |
Modified Residue | MOD_RES 188; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9Y5T5; MOD_RES 414; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903 |
Post Translational Modification | PTM: Phosphorylated at the onset of mitosis and dephosphorylated during the metaphase/anaphase transition. Phosphorylation by AURKB enhances the deubiquitinase activity. {ECO:0000255|HAMAP-Rule:MF_03062}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 93,762 |
Kinetics | |
Metal Binding | METAL 24; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 26; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 48; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 51; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 73; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 76; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 81; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 89; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 93; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 102; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 115; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 118; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502 |
Rhea ID | |
Cross Reference Brenda |