BRCA1-A complex subunit Abraxas 1

UniProt Q6UWZ7 Organism Homo sapiens Gene ABRA1, ABRAXAS1, CCDC98, FAM175A

Also known as: ABRA1, ABRAXAS1, CCDC98, FAM175A

Function

Involved in DNA damage response and double-strand break (DSB) repair. Component of the BRCA1-A complex, acting as a central scaffold protein that assembles the various components of the complex and mediates the recruitment of BRCA1. The BRCA1-A complex specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at DSBs. This complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX.

Classification

Family (Pfam): PF21125 MPN_2A_DUB_like
InterPro: BRISC_Abraxas1, FAM175, MPN
Functional cluster: Zinc-Finger & Chromatin Regulatory Proteins

Experimental structures · PDB · 4

4JLU X-ray 3.50A
4U4A X-ray 3.51A
4Y18 X-ray 3.50A
4Y2G X-ray 2.50A

A predicted model is available from AlphaFold.

Gene Ontology · 15

Disease associations

hereditary breast carcinoma MONDO:0016419

Neighborhood · nearest proteins

Nearest neighbours of BRCA1-A complex subunit Abraxas 1: 3 by sequence/function similarity (left); 3 co-cited in the literature (right).

Related proteins · sequence + function similarity

Co-cited proteins · studied together in the literature

BRCA1-A complex subunit RAP80 9 shared papers
Breast cancer type 1 susceptibility protein 8 shared papers
Lys-63-specific deubiquitinase BRCC36 5 shared papers
BRISC and BRCA1-A complex member 1 4 shared papers
BRISC and BRCA1-A complex member 2 4 shared papers
BRCA1-associated RING domain protein 1 2 shared papers
BRISC complex subunit Abraxas 2 3 shared papers
E3 ubiquitin-protein ligase RNF8 1 shared papers
BRISC complex subunit Abraxas 2 1 shared papers
Interferon alpha/beta receptor 1 1 shared papers
Serine hydroxymethyltransferase, cytosolic 1 shared papers
Serine hydroxymethyltransferase, mitochondrial 1 shared papers

Literature · 22 cited papers

Structure of BRCA1-BRCT/Abraxas complex reveals phosphorylation-dependent BRCT dimerization at DNA damage sites. Mol. Cell · 2016
Mislocalization of BRCA1-complex due to ABRAXAS Arg361Gln mutation. J. Biomol. Struct. Dyn. · 2015
Preliminary crystallographic studies of BRCA1 BRCT-ABRAXAS complex. Acta Crystallogr. F · 2013
A BRISC-SHMT complex deubiquitinates IFNAR1 and regulates interferon responses. Cell Rep. · 2013
Toward a comprehensive characterization of a human cancer cell phosphoproteome. J. Proteome Res. · 2013
Breast cancer-associated Abraxas mutation disrupts nuclear localization and DNA damage response functions. Sci. Transl. Med. · 2012
System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci. Signal. · 2011
Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci. Signal. · 2010
Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci. Signal. · 2009
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal. Chem. · 2009
NBA1, a new player in the Brca1 A complex, is required for DNA damage resistance and checkpoint control. Genes Dev. · 2009
MERIT40 facilitates BRCA1 localization and DNA damage repair. Genes Dev. · 2009
… and 10 more in the literature graph

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