Detail Information for IndEnz0002004868
IED ID IndEnz0002004868
Enzyme Type ID protease004868
Protein Name Lys-63-specific deubiquitinase BRCC36
EC 3.4.19.-
BRCA1-A complex subunit BRCC36
BRCA1/BRCA2-containing complex subunit 3
BRCA1/BRCA2-containing complex subunit 36
BRISC complex subunit BRCC36
Gene Name brcc3 brcc36
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 MAVQAVHIQGDAFLVCVTHSLSTEREEVMGLCIGEVDTQKLVHIHSVIILRRSDKRKDRVEISPEQLSAATIEADRLADITGRPMRVVGWYHSHPHITVWPSHVDVRTQAMYQMMDVGFVGLIFSCFIEDKNTKTGRILYTCFQSVQAQKSSEYERIEVPLHVVPHNTIRKVCLESAVELPRILCQEEQDAYRRIHSLGHLDSITKIHNGSVFTKNLCGQMSAISGPLLQWLEDRLEQNRQRAQELQSEKEQLLQELKTLG
Enzyme Length 261
Uniprot Accession Number Q66GV6
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. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the brca1-bard1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the rnf8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating numa1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor ifnar1; deubiquitination increases ifnar1 activity by enhancing its stability and cell surface expression. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in ifnar1 deubiquitination. {ECO:0000250|UniProtKB:P46736}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Domain (1); Metal binding (3); Motif (1)
Keywords Cell cycle;Cell division;Chromatin regulator;Cytoplasm;Cytoskeleton;DNA damage;DNA repair;Hydrolase;Metal-binding;Metalloprotease;Mitosis;Nucleus;Protease;Ubl conjugation pathway;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P46736}. Cytoplasm {ECO:0000250|UniProtKB:P46736}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P46736}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). Interaction with abraxas2 retains brcc3 in the cytoplasm. {ECO:0000250|UniProtKB:P46736}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 92..105; /note=JAMM motif; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182
Gene Encoded By
Mass 29,789
Kinetics
Metal Binding METAL 92; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 94; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 105; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182
Rhea ID
Cross Reference Brenda