Detail Information for IndEnz0002014590
IED ID IndEnz0002014590
Enzyme Type ID protease014590
Protein Name Lys-63-specific deubiquitinase BRCC36
EC 3.4.19.-
Gene Name BRCC3 BRCC36 EAG_15736
Organism Camponotus floridanus (Florida carpenter ant)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Hymenoptera Apocrita (wasps ants and bees) Aculeata Formicoidea Formicidae Formicinae Camponotini Camponotus (carpenter ants) Camponotus floridanus (Florida carpenter ant)
Enzyme Sequence MDDSSLQKVELQTDVYMVCLQHALSTENFEVMGLLIGNFACGIAKISAVIILRRLDKKKDRVEISSEQLLKAAAEAERLTVELNRPMRVLGWYHSHPHITVCPSHVDVRTQATYQTMDHSFVGLIFSVFSEGKESKEHEIFLNCFQSDNGEATEIPLEIVHTPDISDRCLRTMTDLSKILVQEEEDMAEACKDHPDVLASIHNNAVRTRALIHITDIITKPLVQTFEKRIALNKLRATHLQRQLQELQKMCNG
Enzyme Length 253
Uniprot Accession Number E2AXC7
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.19.-
Enzyme Function FUNCTION: Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains, leaving the last ubiquitin chain attached to its substrates. Catalytic subunit of the BRISC complex; does not have activity by itself, but needs to be associated into a heterotetramer with ABRAXAS2 for minimal in vitro activity (PubMed:26344097). Plays a role in regulating the onset of apoptosis via its role in modulating 'Lys-63'-linked ubiquitination of target proteins (By similarity). Required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating spindle assembly factors (By similarity). {ECO:0000250|UniProtKB:Q15018, ECO:0000250|UniProtKB:Q3TCJ1, ECO:0000269|PubMed:26344097}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (9); Chain (1); Coiled coil (1); Domain (1); Helix (6); Metal binding (3); Motif (1); Mutagenesis (8); Turn (1)
Keywords 3D-structure;Cell cycle;Cell division;Coiled coil;Cytoplasm;Cytoskeleton;Hydrolase;Metal-binding;Metalloprotease;Mitosis;Nucleus;Protease;Ubl conjugation pathway;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P46736}. Nucleus {ECO:0000250|UniProtKB:P46736}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q15018}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q15018}. Note=A minor proportion is detected in the nucleus. Translocates into the nucleus in response to DNA damage. Directly binds to microtubules and is detected at the minus end of K-fibers. {ECO:0000250|UniProtKB:Q15018}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (3)
Cross Reference PDB 5CW3; 5CW4; 5CW5;
Mapped Pubmed ID -
Motif MOTIF 94..107; /note=JAMM motif; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182
Gene Encoded By
Mass 28,745
Kinetics
Metal Binding METAL 94; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 96; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 107; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182
Rhea ID
Cross Reference Brenda