| IED ID | IndEnz0002009843 |
| Enzyme Type ID | protease009843 |
| Protein Name |
Ubiquitin carboxyl-terminal hydrolase 11 EC 3.4.19.12 Deubiquitinating enzyme 11 Ubiquitin thioesterase 11 Ubiquitin-specific-processing protease 11 Fragment |
| Gene Name | USP11 |
| Organism | Canis lupus familiaris (Dog) (Canis familiaris) |
| 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 Laurasiatheria Carnivora Caniformia Canidae (dog coyote wolf fox) Canis Canis lupus (Gray wolf) Canis lupus familiaris (Dog) (Canis familiaris) |
| Enzyme Sequence | NSARADLCVALAKHTGMSPERMMVADVFSHRFYKIYQLEESLSSILDRDDIFIYEVSGRSAIGENSREDVVLPIYLRERTPARDYNNSYYGLMLFGHPLLVSVPRDRLSWDALYHILLYRLSRYVTRPSSDDEDDGDEKDIEDKDNIPKPGHVAGASSQDSGAGSGGAQLWSRRRKPAPVDNSPGPSHWPQRARRKHLFTLQTVNSNGTSDRSTFNEDTHAQPYIAIDWEPEMKKRYYDEVEAEGYVKHDCVGYVLKKAPVRLQECIELFTTVETLEKENPWFCPTCKQHQLATKKLDLWMLPETLIIHLKRFSYTKFSREKLDTLVEFPIRDLDFSEFVIKPQNESAPELYKYDLIAVSNHYGGLRDGHYTTFACNKDSGQSDYFDDNSVSPVTENQIESKAAYVLFYQRQDVARRLQPQPSSSDPPASPACGSPPNSEFMDVN |
| Enzyme Length | 445 |
| Uniprot Accession Number | Q01988 |
| Absorption | |
| Active Site | ACT_SITE 362; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 370; /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:0000250|UniProtKB:P51784}; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Protease that can remove conjugated ubiquitin from target proteins and polyubiquitin chains. Inhibits the degradation of target proteins by the proteasome. Cleaves preferentially 'Lys-6' and 'Lys-63'-linked ubiquitin chains. Has lower activity with 'Lys-11' and 'Lys-33'-linked ubiquitin chains, and extremely low activity with 'Lys-27', 'Lys-29' and 'Lys-48'-linked ubiquitin chains (in vitro). Plays a role in the regulation of pathways leading to NF-kappa-B activation. Plays a role in the regulation of DNA repair after double-stranded DNA breaks. Acts as a chromatin regulator via its association with the Polycomb group (PcG) multiprotein PRC1-like complex; may act by deubiquitinating components of the PRC1-like complex. Promotes cell proliferation by deubiquitinating phosphorylated E2F1. {ECO:0000250|UniProtKB:P51784}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (1); Modified residue (2); Non-terminal residue (1); Region (2) |
| Keywords | Chromosome;Cytoplasm;Hydrolase;Nucleus;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51784}. Cytoplasm {ECO:0000250|UniProtKB:P51784}. Chromosome {ECO:0000250|UniProtKB:P51784}. Note=Predominantly nuclear. Associates with chromatin. {ECO:0000250|UniProtKB:P51784}. |
| Modified Residue | MOD_RES 130; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P51784; MOD_RES 430; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P51784 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 50,892 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |