Detail Information for IndEnz0002011102
IED ID IndEnz0002011102
Enzyme Type ID protease011102
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 Xenopus laevis (African clawed frog)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Xenopus Xenopus laevis (African clawed frog)
Enzyme Sequence MVKKRGTNLPAQDFLDAEPVCKHLRKALDDGSVKRALVNVEWTMCQDCQADNKEKNNSEDESAEDPSVWLCLKCGHRGCGRNSVAQHALNHYNTPRSEPHCLVLNVDMWSAWCYLCDNEVPYNRTSRLGQLVDYLQRKAKAKNKNSNSVVSNEEVKTEIVTENEVKKIQYQDEKPDVQAKQEKASSTQKISTEPTVKGLSNLGNTCFFNAVMQNLSQTPALSELLNEVKTFRKPVTVLLPDSSSPKILEVNLEQQPGPLTLAMWQFLTEMHETKKGVVTPKELFSQVCKKAIRFKGYQQQDSQELLRYLLDGMRGEEIQRVTLAMSKSLQSTLDEEEIKKIVKDYEKRRTIPNFVDCLFGGELTSTIMCEECHTVSLVHEPFLDLSLPVLDDLIVKKNSKSTPPARERKEEEEEEENDDDRYVKERDEVSPGASKHLQKKAKKAAKKQAKNQRRQQKWQGKTVLFTDLAKQECSEDEEEVSQTKTNTRPDNETPTADGLNTMETDLSTLENGNEESADGLNTMETDLSTLENGNEEMAGGFKTMEMDLSTLENGSETIKSAVEGITEHTDLDSSVHNNVGSVETNALVGNMENNNNIEVNKTPERTAGSGGDSMEAMAAVENGNADAVNVDDTEAVNGLIDSANMDHELTNSLNRLQLSSDLEPTQVEIEILPDKEQPHTQVYEVVNEDPKTAFSTLSNRKDLPIDEFSVLSCLYQFTHKETLTGNNKLLCNVCTRKQASRLNNSNKGEKKFVYTNAKKQMLVSNPSPILTLHLKRFQQNGFNLRKINRHIKFPEVLDLAPFCTAKCKNVPEGESRLLYSLYGVIEHSGSMRSGHYTAFVKLRHPNQQLCKMLFTGVIPEVSGSEPGQGSWYHISDSHVQAVSLSRVLSSQAYLLFYERML
Enzyme Length 901
Uniprot Accession Number Q6PAW2
Absorption
Active Site ACT_SITE 206; /note=Nucleophile; /evidence=ECO:0000255|HAMAP-Rule:MF_03062; ACT_SITE 835; /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. Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B. {ECO:0000255|HAMAP-Rule:MF_03062, ECO:0000269|PubMed:17914355}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Compositional bias (2); Domain (1); Metal binding (12); Region (1); Zinc finger (1)
Keywords Activator;Cell cycle;Cell division;Chromatin regulator;Hydrolase;Metal-binding;Mitosis;Nucleus;Protease;Thiol protease;Transcription;Transcription regulation;Ubl conjugation pathway;Zinc;Zinc-finger
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03062}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 101,293
Kinetics
Metal Binding METAL 21; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 23; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 45; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 48; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 71; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 74; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 79; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 87; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 91; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 100; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 113; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 116; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502
Rhea ID
Cross Reference Brenda