Death domain-associated protein 6 (DAXX)

Death domain-associated protein 6 (DAXX) is a multifunctional nuclear and cytoplasmic protein that acts principally as a histone chaperone specific for the replication-independent histone variant H3.3, regulating chromatin assembly and structure, gene transcription, and apoptosis[1][2][3][4]. DAXX interacts with ATRX to mediate H3.3 deposition at pericentromeric heterochromatin and telomeres, thereby affecting genome stability and telomere maintenance[1][2][3][4]. In the nucleus, DAXX also functions as a potent transcriptional corepressor through interaction with sumoylated transcription factors and chromatin proteins and localizes to promyelocytic leukemia nuclear bodies (PML-NBs)[1][3]. In the cytoplasm, DAXX was initially identified as a Fas-interacting protein that promotes apoptosis through the JNK pathway but can also mediate anti-apoptotic effects depending on context, such as its subcellular localization and binding partners[3][5]. Dysregulation, mislocalization, or overexpression of DAXX is implicated in multiple cancer types and may be linked to disease progression, prognosis, and potential therapeutic targeting[5].

Other names

DAXXDAP6hDaxxBING2EAP1SMIM40ETS1-associated protein 1Fas death domain-associated proteinFas-binding proteinCENP-C binding protein