Hmdb loader
Identification
HMDB Protein ID HMDBP13780
Secondary Accession Numbers None
Name BRISC and BRCA1-A complex member 2
Synonyms
  1. BRCA1-A complex subunit BRE
  2. BRCA1/BRCA2-containing complex subunit 45
  3. Brain and reproductive organ-expressed protein
Gene Name BABAM2
Protein Type Unknown
Biological Properties
General Function Not Available
Specific 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 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).
Pathways
  • Homologous recombination
Reactions Not Available
GO Classification
Biological Process
signal transduction involved in G2 DNA damage checkpoint
apoptotic process
response to DNA damage stimulus
negative regulation of apoptotic process
cell cycle
cell division
response to ionizing radiation
double-strand break repair
positive regulation of DNA repair
chromatin organization
Cellular Component
cytoplasm
nuclear ubiquitin ligase complex
BRCA1-A complex
BRISC complex
nucleus
cytosol
Molecular Function
polyubiquitin binding
tumor necrosis factor receptor binding
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 383
Molecular Weight 43544.32
Theoretical pI 5.938
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q8K3W0
UniProtKB/Swiss-Prot Entry Name BABA2_MOUSE
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
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  3. Huttlin EL, Jedrychowski MP, Elias JE, Goswami T, Rad R, Beausoleil SA, Villen J, Haas W, Sowa ME, Gygi SP: A tissue-specific atlas of mouse protein phosphorylation and expression. Cell. 2010 Dec 23;143(7):1174-89. doi: 10.1016/j.cell.2010.12.001. [PubMed:21183079 ]
  4. Ching AK, Li Q, Lim PL, Chan JY, Chui YL: Expression of a conserved mouse stress-modulating gene, Bre: comparison with the human ortholog. DNA Cell Biol. 2003 Aug;22(8):497-504. doi: 10.1089/10445490360708900. [PubMed:14565866 ]
  5. Gu C, Castellino A, Chan JY, Chao MV: BRE: a modulator of TNF-alpha action. FASEB J. 1998 Sep;12(12):1101-8. doi: 10.1096/fasebj.12.12.1101. [PubMed:9737713 ]
  6. Ching AK, Li PS, Li Q, Chan BC, Chan JY, Lim PL, Pang JC, Chui YL: Expression of human BRE in multiple isoforms. Biochem Biophys Res Commun. 2001 Nov 2;288(3):535-45. doi: 10.1006/bbrc.2001.5801. [PubMed:11676476 ]