These transcription factors possess a central theme of cellular proliferation, cell cycle regulation, apoptosis, and differentiation.

The DEP domain is primarily found in proteins involved in G-protein signalling pathways and regulation of GTPase.

[16][17] As well, experimental evidence suggests that the DEP domain determines the subcellular target of some GTPase Activating proteins.

[23] A single palmitoylation site, found within the RhoGAP domain, indicates the possible interaction of the DEPDC1B protein product with a membrane via lipid anchor.

High level of gene expression is observed in all periods of life, except early zygote stages.

[33] Also, DEPDC1B expression decreases in environments of beta-catenin depletion in multiple myeloma cell lines[34] No interactions of DEPDC1B within any other protein product characterized by experimentation have been verified.

[35] Medium coexpression of DEPDC1B with ECT2 in cell cycle regulation and DNA synthesis was verified by similarity of expression in various tissues.

DEPDC1B is unique to Chordates in Kingdom Animalia[36] Multiple sequence alignments verify that DEPDC1B is highly conserved among orthologs.

High expression of the protein in Multiple Myeloma (MM) malignant plasma cells is associated with patient fatality.

The high expression has been confirmed using conditional lentiviral vector delivery “to inhibit growth of human melanoma cell lines (HMCLs), with a block in G2 phase of the cell cycle, p53 phosphorylation and stabilization, and p21Cip1 accumulation”9.

[42] In the same study it was concluded that DEPDC1A may contribute to the plasmablast features of MM cells, blocking differentiation.

Using microarray and northern blotting confirmed the presence of unsubstantial amounts of the protein within the normal tissues, excluding the testis.