Septins are a conserved family of GTP-binding proteins that assemble into cytoskeletal filaments to function in a highly sophisticated and physiologically regulated manner. Septins are highly conserved from yeast to humans and have gradually been accepted as a new class of cytoskeletal proteins. Mammalian septins have several functions in addition to their role in mitosis. They regulate cell polarity, cytoskeletal organization, vesicle trafficking, ciliogenesis and cell-pathogen interactions. At present, 13 septins have been identified from human. The human septins are classified into four groups based on sequence homology: SEPT2 (SEPT1, 2, 4, 5), SEPT3 (SEPT3, 9, 12), SEPT6 (SEPT6, 8, 10, 11, 14) and SEPT7 (SEPT7) groups. SEPT2, a member of the septin family, is involved in diverse cellular processes. These include the cell stiffness and plasma membrane rigidity observed in yeast, the chromosome segregation, microtubule regulation, and actin dynamics, and also the cytokinesis occurring in mammalian cells. SEPT2 plays a crucial role in tumorigenesis and tumor development. This review summarizes the current knowledge about the role of SEPT2 in tumors and supports its potential as a biomarker for certain types of tumors. After in-depth analysis, it provides new perspectives for oncology.