BABA1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BABA1_MOUSE
• UniProt AC: Q3UI43
• Protein Name: BRISC and BRCA1-A complex member 1
• Gene Name: Babam1
• Organism: Mus musculus (Mouse).
• Sequence Length: 333
• 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 is required for the complex integrity and its localization at DSBs. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. In these 2 complexes, it is probably required to maintain the stability of BABAM2 and help the 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36 component. 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: MEVAEANSPTEEEEEEEEEGEETISEPRPHTRSNPEGAEDRALGAQASVGSRSEGEGEAATADGGAASVPGAGPKPWQVPASASEVQIRTPRVNCPEKVIICLDLSEEMSVPKLESFNGSRTNALNVSQKMVEMFVRTKHKIDKSHEFALVVVNDDSAWLSGLTSDPRELCSCLYDLETASCSTFNLEGLFSLIQQKTELPVTENVQTIPPPYVVRTILVYSRPPCQPQFSLTEPMKKMFQCPYFFFDIVYIHNGTEEKEEDMSWKDMFAFMGSLDTKGASYKYEVALAGPALELHNCMAKLLAHPLQRPCQTHASYSLLEEDEEAGEEEATV

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	-------MEVAEANS -------CCCCCCCC	9.37	-
8	Phosphorylation	MEVAEANSPTEEEEE CCCCCCCCCCHHHHH	40.00	25266776
10	Phosphorylation	VAEANSPTEEEEEEE CCCCCCCCHHHHHHH	56.71	25266776
33	Phosphorylation	EPRPHTRSNPEGAED CCCCCCCCCCCCHHH	58.87	25195567
48	Phosphorylation	RALGAQASVGSRSEG HHHCCCCCCCCCCCC	18.22	26824392
51	Phosphorylation	GAQASVGSRSEGEGE CCCCCCCCCCCCCCC	30.40	26643407
53	Phosphorylation	QASVGSRSEGEGEAA CCCCCCCCCCCCCCC	52.21	23684622
61	Phosphorylation	EGEGEAATADGGAAS CCCCCCCCCCCCCCC	32.12	21659605
68	Phosphorylation	TADGGAASVPGAGPK CCCCCCCCCCCCCCC	28.45	23984901
116	Phosphorylation	MSVPKLESFNGSRTN CCCCCHHHCCCCCCC	34.15	22817900
237	Ubiquitination	FSLTEPMKKMFQCPY CCCCHHHHHHHCCCH	52.37	22790023
274	Phosphorylation	DMFAFMGSLDTKGAS HHHHHHHCCCCCCCC	15.98	28576409

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

Oops, there are no upstream regulatory protein records of BABA1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BABA1_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 BABA1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of BABA1_MOUSE !!

Drug and Disease Associations

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