BABA2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BABA2_MOUSE
• UniProt AC: Q8K3W0
• Protein Name: BRISC and BRCA1-A complex member 2
• Gene Name: Babam2
• Organism: Mus musculus (Mouse).
• Sequence Length: 383
• Subcellular Localization: Cytoplasm . Nucleus . Localizes at sites of DNA damage at double-strand breaks (DSBs).
• Protein Description: 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). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it acts as an adapter that bridges the interaction between BABAM1/NBA1 and the rest of the complex, thereby being required for the complex integrity and modulating the E3 ubiquitin ligase activity of the BRCA1-BARD1 heterodimer. Probably also plays a role as a component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin (By similarity). May regulate TNF-alpha signaling through its interactions with TNFRSF1A.; 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). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it acts as an adapter that bridges the interaction between BABAM1/NBA1 and the rest of the complex, thereby being required for the complex integrity and modulating the E3 ubiquitin ligase activity of the BRCA1-BARD1 heterodimer. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Within the BRISC complex, acts as an adapter that bridges the interaction between BABAM1/NBA1 and the rest of the complex, thereby being required for the complex integrity. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. The BRISC complex 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. May play a role in homeostasis or cellular differentiation in cells of neural, epithelial and germline origins (By similarity). May also act as a death receptor-associated anti-apoptotic protein, which inhibits the mitochondrial apoptotic pathway. May regulate TNF-alpha signaling through its interactions with TNFRSF1A; however these effects may be indirect. [PubMed: 9737713]
• Protein Sequence: MSPEIALNRISPMLSPFISSVVRNGKVGLDATNCLRITDLKSGCTSLTPGPNCDRFKLHIPYAGETLKWDIIFNAQYPELPPDFIFGEDAEFLPDPSALHNLASWNPSNPECLLLVVKELVQQYHQFQCGRLRESSRLMFEYQTLLEEPQYGENMEIYAGKKNNWTGEFSARFLLKLPVDFSNIPTYLLKDVNEDPGEDVALLSVSFEDTEATQVYPKLYLSPRIEHALGGSSALHIPAFPGGGCLIDYVPQVCHLLTNKVQYVIQGYHKRREYIAAFLSHFGTGVVEYDAEGFTKLTLLLMWKDFCFLVHIDLPLFFPRDQPTLTFQSVYHFTNSGQLYSQAQKNYPYSPRWDGNEMAKRAKAYFKTFVPQFQEAAFANGKL

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
1	Acetylation	-------MSPEIALN -------CCHHHHHH		-
2	Phosphorylation	------MSPEIALNR ------CCHHHHHHH		26824392
15	Phosphorylation	NRISPMLSPFISSVV HHHHHHHHHHHHHHH		26745281
26	Acetylation	SSVVRNGKVGLDATN HHHHHCCCCCCCCCC		19846515
34	S-palmitoylation	VGLDATNCLRITDLK CCCCCCCCEEEEECC		28526873
41	Ubiquitination	CLRITDLKSGCTSLT CEEEEECCCCCCCCC		22790023
222	Phosphorylation	VYPKLYLSPRIEHAL CCCEEEECCCHHHHC		-
249	Phosphorylation	GGGCLIDYVPQVCHL CCCCHHCCHHHHHHH		-
263	Phosphorylation	LLTNKVQYVIQGYHK HHHCHHHHHHCCHHH		-
350	Phosphorylation	AQKNYPYSPRWDGNE HHHHCCCCCCCCHHH		-
382	Ubiquitination	EAAFANGKL------ HHHHHCCCC------		-

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

Oops, there are no upstream regulatory protein records of BABA2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BABA2_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 BABA2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of BABA2_MOUSE !!

Drug and Disease Associations

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