protein
BRISC and BRCA1-A complex member 1
Gene
BABAM1
Organism
Homo sapiens(9606)
Length
329 aa
Mass
36,560 Da
BABAM1 (BRISC and BRCA1-A complex member 1) is a 329-amino acid scaffolding protein that functions as a component of two multiprotein complexes involved in DNA damage response and protein deubiquitination (UniProt: Q9NWV8). Within the BRCA1-A complex, it recognizes Lys-63-linked ubiquitinated histones at double-strand breaks and helps target BRCA1-BARD1 to DNA damage sites. As part of the BRISC complex, BABAM1 maintains stability of BABAM2 and supports Lys-63-selective deubiquitinase activity, with known roles in mitotic spindle assembly and interferon signaling through IFNAR1 deubiquitination (UniProt: Q9NWV8).
No primary disease associations are documented in UniProt for BABAM1. However, the protein demonstrates altered expression in Alzheimer's disease. In human post-mortem AD brain tissue compared to age-matched controls, BABAM1 is significantly down-regulated (mean log2 fold-change: −0.58; Chaparral AD proteomics). This reduction was observed via TMT-labeled quantitative proteomics across four subcellular fractions, suggesting potential impairment of DNA repair and deubiquitination capacity in AD pathology.
Generated from the curated entity record below. May contain errors — verify against source links.
Proteomics Evidence · AD
↓ Down in ADP3
-0.576
P2
not detected
S2
not detected
S3
not detected
Mean log₂FC across detected fractions: -0.5756 (1 of 4 fractions detected)
Human post-mortem AD brain vs age-matched controls, TMT-labeled, 4 subcellular fractions (P2, P3, S2, S3), DDA proteomics.
Related Publications
Browse all →Tau molecular diversity contributes to clinical heterogeneity in Alzheimer's disease.
Dujardin Simon et al.Nature medicine2020PMID 32572268Deep Multilayer Brain Proteomics Identifies Molecular Networks in Alzheimer's Disease Progression.
Bai Bing et al.Neuron2020PMID 31926610A Multi-network Approach Identifies Protein-Specific Co-expression in Asymptomatic and Symptomatic Alzheimer's Disease.
Seyfried Nicholas T et al.Cell systems2017PMID 27989508Large-scale deep multi-layer analysis of Alzheimer's disease brain reveals strong proteomic disease-related changes not observed at the RNA level.
Johnson Erik C B et al.Nature neuroscience2022PMID 35115731Organization and regulation of gene transcription.
Cramer PatrickNature2019PMID 31462772
Function
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 (PubMed:24075985, PubMed:26195665). 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 (PubMed:26195665). 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 (PubMed:24075985). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (PubMed:24075985)
Sources
Last updated 5/8/2026, 6:25:56 AM