FBP antikoerper, FUBP antikoerper, fbp antikoerper, fubp antikoerper, MGC53183 antikoerper, MGC75632 antikoerper, FUBP1 antikoerper, DKFZp468N0812 antikoerper, 9530027K12Rik antikoerper, D3Ertd330e antikoerper, Fubp antikoerper, Fubp4 antikoerper, MGC78835 antikoerper, wu:fa92h11 antikoerper, wu:fb24h11 antikoerper, wu:fc26f06 antikoerper, zgc:66046 antikoerper, far upstream element binding protein 1 antikoerper, far upstream element (FUSE) binding protein 1 S homeolog antikoerper, far upstream element (FUSE) binding protein 1 antikoerper, far upstream element binding protein 1 L homeolog antikoerper, FUBP1 antikoerper, fubp1.S antikoerper, fubp1 antikoerper, Fubp1 antikoerper, fubp1.L antikoerper
Hintergrund
The protein encoded by this gene is a single stranded DNA-binding protein that binds to multiple DNA elements, including the far upstream element (FUSE) located upstream of c-myc. Binding to FUSE occurs on the non-coding strand, and is important to the regulation of c-myc in undifferentiated cells. This protein contains three domains, an amphipathic helix N-terminal domain, a DNA-binding central domain, and a C-terminal transactivation domain that contains three tyrosine-rich motifs. The N-terminal domain is thought to repress the activity of the C-terminal domain. This protein is also thought to bind RNA, and contains 3'-5' helicase activity with in vitro activity on both DNA-DNA and RNA-RNA duplexes. Aberrant expression of this gene has been found in malignant tissues, and this gene is important to neural system and lung development. Binding of this protein to viral RNA is thought to play a role in several viral diseases, including hepatitis C and hand, foot and mouth disease. Alternative splicing results in multiple transcript variants.