SAFB2 belongs to the scaffold attachment factor B (SAFB) family. It shares protein sequence similarity with SAFB1. Like SAFB1, it also has functions in transcriptional repression and RNA splicing []. Both SAFB1 and SAFB2 play an important role in cancer, particularly in breast tumorigenesis []. Nevertheless, SAFB2 seems to have non-redundant functions in mouse male reproductive tract compared to SAFB1 [].Scaffold attachment factor B (SAFB) family members include SAFB1, SAFB2 and SAFB-like transcriptional modulator, SLTM. They contain an N-terminal DNA-binding (SAF-A/B, Acinus and PIAS, SAP) domain, an RNA-binding domain (RBD) and an C-terminal arginine/glycine motif RGG/RG domain. Their RGG/RG domain, which partially overlaps with a putative coiled-coil domain, is most conserved and is likely to be involved in protein-protein interactions [].
SLTM belongs to the scaffold attachment factor B (SAFB) family. When overexpressed, it acts as a general inhibitor of transcription that eventually leads to apoptosis [, ].Scaffold attachment factor B (SAFB) family members include SAFB1, SAFB2 and SAFB-like transcriptional modulator, SLTM. They contain an N-terminal DNA-binding (SAF-A/B, Acinus and PIAS, SAP) domain, an RNA-binding domain (RBD) and an C-terminal arginine/glycine motif RGG/RG domain. Their RGG/RG domain, which partially overlaps with a putative coiled-coil domain, is most conserved and is likely to be involved in protein-protein interactions [].
SAFB1 belongs to the scaffold attachment factor B (SAFB) family. It has many functions such as transcriptional repression and RNA splicing. It may also have a role in chromatin organization. It is involved in in numerous cellular processes including cell growth, stress response, and apoptosis []. It plays an important role in cancer, particularly in breast tumorigenesis []. Scaffold attachment factor B (SAFB) family members include SAFB1, SAFB2 and SAFB-like transcriptional modulator, SLTM. They contain an N-terminal DNA-binding (SAF-A/B, Acinus and PIAS, SAP) domain, an RNA-binding domain (RBD) and an C-terminal arginine/glycine motif RGG/RG domain. Their RGG/RG domain, which partially overlaps with a putative coiled-coil domain, is most conserved and is likely to be involved in protein-protein interactions [].
