Fig. 2: Domain architecture of PR-DUB components and frequent mutations in ASXL1. | Leukemia

Fig. 2: Domain architecture of PR-DUB components and frequent mutations in ASXL1.

From: The role of ASXL1, SRSF2, and EZH2 mutations in chromatin dysregulation of myelodysplastic neoplasia and acute myeloid leukemia

Fig. 2: Domain architecture of PR-DUB components and frequent mutations in ASXL1.

a Diagram of major ASXL1 domains. ASXN ASX N-terminal domain, ASXH BAP1 binding domain, ASXM1/2 ASX middle domain 1/2, PHD Plant homeodomain. b Locations of ASXL1 truncation mutations recurrently found in MDS/AML. The majority occur in exon 12, with G646Wfs recognized as the most frequently occurring variant (indicated in red). The relative frequency of each mutation is represented by the length of the line. Y591*: Nonsense mutation at position 591 results in a premature stop codon, replacing tyrosine. E635Rfs: Deletion of several nucleotides causes a glutamine-to-arginine substitution at position 635, leading to a frameshift and the generation of a premature stop codon. G646Wfs: Insertion of a single nucleotide causes a glycine-to-tryptophan substitution at position 646, leading to a frameshift and the generation of a premature stop codon. R693*: Nonsense mutation at position 591 results in a premature stop codon, replacing tyrosine. c Diagram of BAP1 domains. UCH domain: Ubiquitin C-terminal hydrolase domain, which exhibits deubiquitinating activity essential for PR-DUB complex function; CC1/2 domain: Coiled-coil 1 and coiled-coil 2 domain; ULD domain: Ubiquitin-like domain; CTE domain: C-terminal extension. d The ASXH domain of ASXL1 interacts with the ULD domain of BAP1, forming a ubiquitin-binding pocket.

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