BRCC3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BRCC3_MOUSE
• UniProt AC: P46737
• Protein Name: Lys-63-specific deubiquitinase BRCC36
• Gene Name: Brcc3
• Organism: Mus musculus (Mouse).
• Sequence Length: 291
• Subcellular Localization: Nucleus . Cytoplasm . Cytoplasm, cytoskeleton, spindle pole . Localizes at sites of DNA damage at double-strand breaks (DSBs). Interaction with ABRAXAS2 retains BRCC3 in the cytoplasm.
• Protein Description: 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..
• Protein Sequence: MAVQVVQAVQAVHLESDAFLVCLNHALSTEKEEVMGLCIGELNDDIRSDSKFTYTGTEMRTVQEKMDTIRIVHIHSVIILRRSDKRKDRVEISPEQLSAASTEAERLAELTGRPMRVVGWYHSHPHITVWPSHVDVRTQAMYQMMDQGFVGLIFSCFIEDKNTKTGRVLYTCFQSIQAQKSSEYERIEIPIHIVPHITIGKVCLESAVELPKILCQEEQDAYRRIHSLTHLDSVTKIHNGSVFTKNLCSQMSAVSGPLLQWLEDRLEQNQQHLQELQQEKEELMEELSSLE

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAVQVVQAV ------CHHHHHHHH	10.64	-
51	Acetylation	DDIRSDSKFTYTGTE CCCCCCCCCEECCCC	46.87	22826441
51	Ubiquitination	DDIRSDSKFTYTGTE CCCCCCCCCEECCCC	46.87	27667366
53	Phosphorylation	IRSDSKFTYTGTEMR CCCCCCCEECCCCCC	24.74	25367039
54	Phosphorylation	RSDSKFTYTGTEMRT CCCCCCEECCCCCCC	13.30	25367039
55	Phosphorylation	SDSKFTYTGTEMRTV CCCCCEECCCCCCCH	34.27	25367039
57	Phosphorylation	SKFTYTGTEMRTVQE CCCEECCCCCCCHHH	20.86	25367039
65	Ubiquitination	EMRTVQEKMDTIRIV CCCCHHHHHCEEEEE	25.61	-
180	Ubiquitination	FQSIQAQKSSEYERI HHHHHHHCCCCCEEE	59.99	-
227	Phosphorylation	DAYRRIHSLTHLDSV HHHHHHHHHHCHHHC	32.37	29899451
233	Phosphorylation	HSLTHLDSVTKIHNG HHHHCHHHCEEEECC	37.74	29899451
280	Acetylation	LQELQQEKEELMEEL HHHHHHHHHHHHHHH	52.75	23954790
288	Phosphorylation	EELMEELSSLE---- HHHHHHHHCCC----	35.84	28066266
289	Phosphorylation	ELMEELSSLE----- HHHHHHHCCC-----	49.49	28066266

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of BRCC3_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BRCC3_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of BRCC3_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of BRCC3_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.