Overexpression of HK3 has resulted in increased ATP levels, decreased reactive oxygen species (ROS) production, attenuated reduction in the mitochondrial membrane potential, and enhanced mitochondrial biogenesis. Overall, HK3 may promote cell survival by controlling ROS levels and boosting energy production. Currently, only hypoxia is known to induce HK3 expression through a HIF-dependent pathway. The inducible expression of HK3 indicates its adaptive role in metabolic responses to changes in the cellular environment. In particular, HK3 is ubiquitously expressed in tissues, albeit at relatively low abundance. Higher abundance levels have been cited in lung, kidney, and liver tissue. Within cells, HK3 localizes to the cytoplasm and putatively binds the perinuclear envelope. HK3 is the predominant hexokinase in myeloid cells, particularly granulocytes. HK3 is found to be overexpressed in malignant follicular thyroid nodules. In conjunction with cyclin A and galectin-3, HK3 could be used as diagnostic biomarker to screen for malignancy in patients. Meanwhile, HK3 was found to be repressed in acute myeloid leukemia (AML) blast cells and acute promyelocytic leukemia (APL) patients. The transcription factor PU.1 is known to directly activate transcription of the antiapoptotic "BCL2A1" gene or inhibit transcription of the p53 tumor suppressor to promote cell survival, and is proposed to also directly activate "HK3" transcription during neutrophil differentiation to support short-term cell survival of mature neutrophils. Regulators repressing HK3 expression in AML include PML-RARA and CEBPA. Regarding acute lymphoblastic leukemia (ALL), functional enrichment analysis revealed "HK3" as a key gene and suggests that HK3 shares antiapoptotic function with HK1 and HK2. The "HK3" promoter is known to interact with PU.1, PML-RARA, and CEBPA.