Recombinant Human DPY30 protein (Tagged-His Tag)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

DPY30 also known as Dpy-30-like protein or DPy-30 homolog is a component of the MLL/SET1 histone methyltransferase complexes implicated in histone H3 lysine 4 (H3K4) methylation. This protein has an estimated molecular mass of approximately 9 kDa. It is widely expressed in different tissues which indicates its importance across various cellular environments. The primary role of DPY30 involves facilitating the catalytic activity within these complexes influencing the transcriptional states by modulating chromatin structure.

Biological function summary

DPY30 functions as a core component of the SET1A and SET1B complexes participating in the regulation of gene expression by promoting the trimethylation of H3K4. This histone modification is associated with transcriptionally active chromatin influencing gene activation. DPY30 cooperates with other components like RBBP5 and WDR5 to achieve this modification. By modulating gene expression DPY30 is critical in processes like differentiation and development.

Pathways

DPY30 is deeply involved in chromatin modification and gene transcription pathways. It plays a significant role in the Wnt signaling pathway known for its involvement in developmental processes and cell growth. DPY30 interacts with related proteins within these pathways such as ASH2L which functions as another component of the SET1/MLL complexes to exert its effects on chromatin dynamics and transcription regulation.

DPY30 has been linked to certain cancers particularly acute myeloid leukemia (AML). Research indicates that abnormal activity of the SET1/MLL complexes possibly involving DPY30 may contribute to the leukemogenic process. Additionally it has connections to developmental disorders where mutations impacting histone modification processes disrupt normal developmental signaling pathways. The connection to proteins like MEN1 which interacts with histone modification complexes highlights its role in disease progression.