Detail Information for IndEnz0002015983
IED ID IndEnz0002015983
Enzyme Type ID protease015983
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 Callithrix jacchus (White-tufted-ear marmoset)
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 Primates Haplorrhini Simiiformes Platyrrhini (New World monkeys) Cebidae Callitrichinae (marmosets and tamarins) Callithrix Callithrix Callithrix jacchus (White-tufted-ear marmoset)
Enzyme Sequence MAVQVVQAVQAVHLESDAFLVCLNHALSTEKEEVMGLCIGELNDDTRSDSKFAYTGTEMRTVAEKVDAVRIVHIHSVIILRRSDKRKDRVEISPEQLSAASTEAERLAELTGRPMRVVGWYHSHPHITVWPSHVDVRTQAMYQMMDQGFVGLIFSCFIEDKNTKTGRVLYTCFQSIQAQKSSESLHGPRDFWSSSKHISIEGQKEEERYERIEIPIHIVPHVTIGKVCLESAVELPKILCQEEQDAYRRIHSLTHLDSVTKIHNGSVFTKNLCSQMSAVSGPLLQWLEDRLEQNQQHLRELQQEKEELMQELSSLE
Enzyme Length 316
Uniprot Accession Number B0KWU8
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 (By similarity). Deubiquitinates HDAC1 and PWWP2B leading to their stabilization (By similarity). {ECO:0000250|UniProtKB:P46736, ECO:0000250|UniProtKB:P46737}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Domain (1); Initiator methionine (1); Metal binding (3); Modified residue (2); Motif (1)
Keywords Acetylation;Cell cycle;Cell division;Chromatin regulator;Cytoplasm;Cytoskeleton;DNA damage;DNA repair;Hydrolase;Metal-binding;Metalloprotease;Mitosis;Nucleus;Phosphoprotein;Protease;Reference proteome;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 MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000250|UniProtKB:P46736; MOD_RES 258; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P46736
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 122..135; /note=JAMM motif; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182
Gene Encoded By
Mass 36,100
Kinetics
Metal Binding METAL 122; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 124; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 135; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182
Rhea ID
Cross Reference Brenda