| Name | abraxas 2, BRISC complex subunit |
| Description | Enables microtubule binding activity and polyubiquitin modification-dependent protein binding activity. Involved in nuclear chromosome segregation; protein K63-linked deubiquitination; and response to ischemia. Located in cytoplasm; microtubule cytoskeleton; and midbody. Part of BRISC complex. [provided by Alliance of Genome Resources, Mar 2025] |
| Summary |
{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n ABRAXAS2 (commonly referred to as ABRO1) functions as a critical scaffold protein that directs the assembly and compartmentalization of BRCC36‐containing deubiquitinase complexes. In the cytoplasm, ABRAXAS2 forms the BRISC complex, thereby conferring specificity for the removal of Lys63‐linked ubiquitin chains on a variety of substrates. Through its assembling role, ABRAXAS2 modulates key cellular processes such as inflammatory signaling – for instance, by promoting optimal NLRP3 inflammasome activation via deubiquitination events"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "– and regulates interferon receptor turnover by coordinating with metabolic enzymes like SHMT2."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": " Furthermore, ABRAXAS2 contributes to tumor suppression by stabilizing p53 through facilitating its interaction with USP7, and is implicated in protecting against replicative stress‐induced genome instability"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": ";."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": " Its ability to assemble distinct BRCC36 complexes in the cytoplasm, as opposed to nuclear complexes formed via ABRAXAS, underscores its role in directing substrate selectivity and subcellular targeting"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": ";."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": " Additional studies reveal that ABRAXAS2 can modulate deubiquitinase activity by competing with E3 ubiquitin ligases to stabilize other DUB components, such as BRCC3"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": ", and by interacting with transcription factors including members of the AP‐1 family to promote cytoprotective responses under stress conditions."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": " Collectively, these findings indicate that ABRAXAS2 is an essential regulatory adaptor that not only organizes deubiquitination at specific subcellular sites but also integrates diverse stress, inflammatory, and tumor‐suppressive signals to maintain cellular homeostasis"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "9"}]}, {"type": "t", "text": ";"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "10"}]}, {"type": "t", "text": ";."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "11"}]}, {"type": "t", "text": "\n "}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Guangming Ren, Xuanyi Zhang, Yang Xiao, et al. "}, {"type": "b", "children": [{"type": "t", "text": "ABRO1 promotes NLRP3 inflammasome activation through regulation of NLRP3 deubiquitination."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "EMBO J (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.15252/embj.2018100376"}], "href": "https://doi.org/10.15252/embj.2018100376"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30787184"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30787184"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Hui Zheng, Vibhor Gupta, Jeffrey Patterson-Fortin, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A BRISC-SHMT complex deubiquitinates IFNAR1 and regulates interferon responses."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Rep (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.celrep.2013.08.025"}], "href": "https://doi.org/10.1016/j.celrep.2013.08.025"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24075985"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24075985"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Jianhong Zhang, Mengmeng Cao, Jiahong Dong, et al. "}, {"type": "b", "children": [{"type": "t", "text": "ABRO1 suppresses tumourigenesis and regulates the DNA damage response by stabilizing p53."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ncomms6059"}], "href": "https://doi.org/10.1038/ncomms6059"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25283148"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25283148"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Shengfeng Xu, Xiao Wu, Ling Wu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Abro1 maintains genome stability and limits replication stress by protecting replication fork stability."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Genes Dev (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1101/gad.299172.117"}], "href": "https://doi.org/10.1101/gad.299172.117"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28860160"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28860160"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Xin Hu, Jin Ah Kim, Andy Castillo, et al. "}, {"type": "b", "children": [{"type": "t", "text": "NBA1/MERIT40 and BRE interaction is required for the integrity of two distinct deubiquitinating enzyme BRCC36-containing complexes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M110.200857"}], "href": "https://doi.org/10.1074/jbc.M110.200857"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21282113"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21282113"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Julius Rabl, Richard D Bunker, Andreas D Schenk, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structural Basis of BRCC36 Function in DNA Repair and Immune Regulation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molcel.2019.06.002"}], "href": "https://doi.org/10.1016/j.molcel.2019.06.002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31253574"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31253574"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Wen Zhang, Shou-Song Tao, Ting Wang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "ABRO1 stabilizes the deubiquitinase BRCC3 through inhibiting its degradation mediated by the E3 ubiquitin ligase WWP2."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS Lett (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/1873-3468.13970"}], "href": "https://doi.org/10.1002/1873-3468.13970"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33107021"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33107021"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Camilla T Ambivero, Lucia Cilenti, Antonis S Zervos "}, {"type": "b", "children": [{"type": "t", "text": "ATF4 interacts with Abro1/KIAA0157 scaffold protein and participates in a cytoprotective pathway."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochim Biophys Acta (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbamcr.2012.08.020"}], "href": "https://doi.org/10.1016/j.bbamcr.2012.08.020"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22974638"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22974638"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Elton Zeqiraj, Lei Tian, Christopher A Piggott, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Higher-Order Assembly of BRCC36-KIAA0157 Is Required for DUB Activity and Biological Function."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molcel.2015.07.028"}], "href": "https://doi.org/10.1016/j.molcel.2015.07.028"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26344097"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26344097"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Lucia Cilenti, Meenakshi P Balakrishnan, Xiao-Liang Wang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Regulation of Abro1/KIAA0157 during myocardial infarction and cell death reveals a novel cardioprotective mechanism for Lys63-specific deubiquitination."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Mol Cell Cardiol (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.yjmcc.2010.12.015"}], "href": "https://doi.org/10.1016/j.yjmcc.2010.12.015"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21195082"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21195082"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Jeffrey Patterson-Fortin, Genze Shao, Heidi Bretscher, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Differential regulation of JAMM domain deubiquitinating enzyme activity within the RAP80 complex."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M110.135319"}], "href": "https://doi.org/10.1074/jbc.M110.135319"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20656689"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20656689"}]}]}]}
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| NCBI Gene ID | 23172 |
| API | |
| Download Associations | |
| Predicted Functions |
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| Co-expressed Genes |
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| Expression in Tissues and Cell Lines |
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ABRAXAS2 has 1,402 functional associations with biological entities spanning 5 categories (chemical, functional term, phrase or reference, disease, phenotype or trait, cell line, cell type or tissue, gene, protein or microRNA) extracted from 42 datasets.
Click the + buttons to view associations for ABRAXAS2 from the datasets below.
If available, associations are ranked by standardized value
| Dataset | Summary | |
|---|---|---|
| Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles | tissue samples with high or low expression of ABRAXAS2 gene relative to other tissue samples from the Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles dataset. | |
| Carcinogenome Chemical Perturbation Carcinogenicity Signatures | small molecule perturbations changing expression of ABRAXAS2 gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset. | |
| CCLE Cell Line Proteomics | Cell lines associated with ABRAXAS2 protein from the CCLE Cell Line Proteomics dataset. | |
| CellMarker Gene-Cell Type Associations | cell types associated with ABRAXAS2 gene from the CellMarker Gene-Cell Type Associations dataset. | |
| ChEA Transcription Factor Targets 2022 | transcription factors binding the promoter of ABRAXAS2 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset. | |
| CM4AI KOLF21J CRISPRi Gene Perturbation Atlas | gene perturbations changing expression of ABRAXAS2 gene from the CM4AI KOLF21J CRISPRi Gene Perturbation Atlas dataset. | |
| COMPARTMENTS Curated Protein Localization Evidence Scores 2025 | cellular components containing ABRAXAS2 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset. | |
| COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 | cellular components co-occuring with ABRAXAS2 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset. | |
| DeepCoverMOA Drug Mechanisms of Action | small molecule perturbations with high or low expression of ABRAXAS2 protein relative to other small molecule perturbations from the DeepCoverMOA Drug Mechanisms of Action dataset. | |
| DepMap CRISPR Gene Dependency | cell lines with fitness changed by ABRAXAS2 gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset. | |
| DISEASES Experimental Gene-Disease Association Evidence Scores 2025 | diseases associated with ABRAXAS2 gene in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores 2025 dataset. | |
| DISEASES Text-mining Gene-Disease Association Evidence Scores 2025 | diseases co-occuring with ABRAXAS2 gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset. | |
| DisGeNET Gene-Disease Associations | diseases associated with ABRAXAS2 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset. | |
| DisGeNET Gene-Phenotype Associations | phenotypes associated with ABRAXAS2 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Phenoptype Associations dataset. | |
| GO Biological Process Annotations 2023 | biological processes involving ABRAXAS2 gene from the curated GO Biological Process Annotations 2023 dataset. | |
| GO Biological Process Annotations 2025 | biological processes involving ABRAXAS2 gene from the curated GO Biological Process Annotations2025 dataset. | |
| GO Cellular Component Annotations 2023 | cellular components containing ABRAXAS2 protein from the curated GO Cellular Component Annotations 2023 dataset. | |
| GO Cellular Component Annotations 2025 | cellular components containing ABRAXAS2 protein from the curated GO Cellular Component Annotations 2025 dataset. | |
| GO Molecular Function Annotations 2023 | molecular functions performed by ABRAXAS2 gene from the curated GO Molecular Function Annotations 2023 dataset. | |
| GO Molecular Function Annotations 2025 | molecular functions performed by ABRAXAS2 gene from the curated GO Molecular Function Annotations 2025 dataset. | |
| GTEx Tissue Gene Expression Profiles 2023 | tissues with high or low expression of ABRAXAS2 gene relative to other tissues from the GTEx Tissue Gene Expression Profiles 2023 dataset. | |
| GTEx Tissue-Specific Aging Signatures | tissue samples with high or low expression of ABRAXAS2 gene relative to other tissue samples from the GTEx Tissue-Specific Aging Signatures dataset. | |
| GWAS Catalog SNP-Phenotype Associations 2025 | phenotypes associated with ABRAXAS2 gene in GWAS datasets from the GWAS Catalog SNP-Phenotype Associations 2025 dataset. | |
| JASPAR Predicted Human Transcription Factor Targets 2025 | transcription factors regulating expression of ABRAXAS2 gene predicted using known transcription factor binding site motifs from the JASPAR Predicted Human Transcription Factor Targets dataset. | |
| JASPAR Predicted Mouse Transcription Factor Targets 2025 | transcription factors regulating expression of ABRAXAS2 gene predicted using known transcription factor binding site motifs from the JASPAR Predicted Mouse Transcription Factor Targets 2025 dataset. | |
| Kinase Library Tyrosine Kinome Atlas | kinases that phosphorylate ABRAXAS2 protein from the Kinase Library Tyrosine Kinome Atlas dataset. | |
| LINCS L1000 CMAP Chemical Perturbation Consensus Signatures | small molecule perturbations changing expression of ABRAXAS2 gene from the LINCS L1000 CMAP Chemical Perturbations Consensus Signatures dataset. | |
| LINCS L1000 CMAP CRISPR Knockout Consensus Signatures | gene perturbations changing expression of ABRAXAS2 gene from the LINCS L1000 CMAP CRISPR Knockout Consensus Signatures dataset. | |
| NIBR DRUG-seq U2OS MoA Box Gene Expression Profiles | drug perturbations changing expression of ABRAXAS2 gene from the NIBR DRUG-seq U2OS MoA Box dataset. | |
| PFOCR Pathway Figure Associations 2023 | pathways involving ABRAXAS2 protein from the PFOCR Pathway Figure Associations 2023 dataset. | |
| PFOCR Pathway Figure Associations 2024 | pathways involving ABRAXAS2 protein from the Wikipathways PFOCR 2024 dataset. | |
| Reactome Pathways 2024 | pathways involving ABRAXAS2 protein from the Reactome Pathways 2024 dataset. | |
| Replogle et al., Cell, 2022 K562 Essential Perturb-seq Gene Perturbation Signatures | gene perturbations changing expression of ABRAXAS2 gene from the Replogle et al., Cell, 2022 K562 Essential Perturb-seq Gene Perturbation Signatures dataset. | |
| Replogle et al., Cell, 2022 K562 Genome-wide Perturb-seq Gene Perturbation Signatures | gene perturbations changing expression of ABRAXAS2 gene from the Replogle et al., Cell, 2022 K562 Genome-wide Perturb-seq Gene Perturbation Signatures dataset. | |
| Replogle et al., Cell, 2022 RPE1 Essential Perturb-seq Gene Perturbation Signatures | gene perturbations changing expression of ABRAXAS2 gene from the Replogle et al., Cell, 2022 RPE1 Essential Perturb-seq Gene Perturbation Signatures dataset. | |
| Rummagene Transcription Factor Associations 2026 | transcription factors regulating expression of ABRAXAS2 gene from the Rummagene Transcription Factor Associations 2026 dataset. | |
| RummaGEO Drug Perturbation Signatures | drug perturbations changing expression of ABRAXAS2 gene from the RummaGEO Drug Perturbation Signatures dataset. | |
| RummaGEO Gene Perturbation Signatures | gene perturbations changing expression of ABRAXAS2 gene from the RummaGEO Gene Perturbation Signatures dataset. | |
| Sci-Plex Drug Perturbation Signatures | drug perturbations changing expression of ABRAXAS2 gene from the Sci-Plex Drug Perturbation Signatures dataset. | |
| TISSUES Curated Tissue Protein Expression Evidence Scores 2025 | tissues with high expression of ABRAXAS2 protein from the TISSUES Curated Tissue Protein Expression Evidence Scores 2025 dataset. | |
| TISSUES Experimental Tissue Protein Expression Evidence Scores 2025 | tissues with high expression of ABRAXAS2 protein in proteomics datasets from the TISSUES Experimental Tissue Protein Expression Evidence Scores 2025 dataset. | |
| TISSUES Text-mining Tissue Protein Expression Evidence Scores 2025 | tissues co-occuring with ABRAXAS2 protein in abstracts of biomedical publications from the TISSUES Text-mining Tissue Protein Expression Evidence Scores 2025 dataset. | |