Anti-BAP1 antibody

Target data

Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1 (PubMed : 12485996, PubMed : 18757409, PubMed : 20436459, PubMed : 25451922, PubMed : 35051358). Catalytic component of the polycomb repressive deubiquitinase (PR-DUB) complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-120' (H2AK119ub1) (PubMed : 20436459, PubMed : 25451922, PubMed : 30664650, PubMed : 35051358). Does not deubiquitinate monoubiquitinated histone H2B (PubMed : 20436459, PubMed : 30664650). The PR-DUB complex is an epigenetic regulator of gene expression and acts as a transcriptional coactivator, affecting genes involved in development, cell communication, signaling, cell proliferation and cell viability (PubMed : 20805357, PubMed : 30664650, PubMed : 36180891). Antagonizes PRC1 mediated H2AK119ub1 monoubiquitination (PubMed : 30664650). As part of the PR-DUB complex, associates with chromatin enriched in histone marks H3K4me1, H3K4me3, and H3K27Ac, but not in H3K27me3 (PubMed : 36180891). Recruited to specific gene-regulatory regions by YY1 (PubMed : 20805357). Acts as a regulator of cell growth by mediating deubiquitination of HCFC1 N-terminal and C-terminal chains, with some specificity toward 'Lys-48'-linked polyubiquitin chains compared to 'Lys-63'-linked polyubiquitin chains (PubMed : 19188440, PubMed : 19815555). Deubiquitination of HCFC1 does not lead to increase stability of HCFC1 (PubMed : 19188440, PubMed : 19815555). Interferes with the BRCA1 and BARD1 heterodimer activity by inhibiting their ability to mediate ubiquitination and autoubiquitination (PubMed : 19117993). It however does not mediate deubiquitination of BRCA1 and BARD1 (PubMed : 19117993). Able to mediate autodeubiquitination via intramolecular interactions to counteract monoubiquitination at the nuclear localization signal (NLS), thereby protecting it from cytoplasmic sequestration (PubMed : 24703950). Negatively regulates epithelial-mesenchymal transition (EMT) of trophoblast stem cells during placental development by regulating genes involved in epithelial cell integrity, cell adhesion and cytoskeletal organization (PubMed : 34170818).