Detail Information for IndEnz0002011799
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