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Cleavage stimulation factor subunit 3Known also as: Cleavage stimulation factor 77 kDa subunit Known abbreviations: CSTF3, CstF-77 Yeast homolog: RNA14 Protein
Top 3 models:
This protein has alternative isoforms: Isoform 1:
1........10........20........30........40........50........60........70........80........90........100.......110.......120.......130 MSGDGATEQAAEYVPEKVKKAEKKLEENPYDLDAWSILIREAQNQPIDKARKTYERLVAQFPSSGRFWKLYIEAEIKAKNYDKVEKLFQRCLMKVLHIDLWKCYLSYVRETKGKLPSYKEKMAQAYDFAL DKIGMEIMSYQIWVDYINFLKGVEAVGSYAENQRITAVRRVYQRGCVNPMINIEQLWRDYNKYEEGINIHLAKKMIEDRSRDYMNARRVAKEYETVMKGLDRNAPSVPPQNTPQEAQQVDMWKKYIQWEK SNPLRTEDQTLITKRVMFAYEQCLLVLGHHPDIWYEAAQYLEQSSKLLAEKGDMNNAKLFSDEAANIYERAISTLLKKNMLLYFAYADYEESRMKYEKVHSIYNRLLAIEDIDPTLVYIQYMKFARRAEG IKSGRMIFKKAREDTRTRHHVYVTAALMEYYCSKDKSVAFKIFELGLKKYGDIPEYVLAYIDYLSHLNEDNNTRVLFERVLTSGSLPPEKSGEIWARFLAFESNIGDLASILKVEKRRFTAFKEEYEGKE TALLVDRYKFMDLYPCSASELKALGYKDVSRAKLAAIIPDPVVAPSIVPVLKDEVDRKPEYPKPDTQQMIPFQPRHLAPPGLHPVPGGVFPVPPAAVVLMKLLPPPICFQGPFVQVDELMEIFRRCKIPN TVEEAVRIITGGAPELAVEGNGPVESNAVLTKAVKRPNEDSDEDEEKGAVVPPVHDIYRARQQKRIR Isoform 2:
1........10........20........30........40........50........60........70........80........90........100.......110.......120.......130 MSGDGATEQAAEYVPEKVKKAEKKLEENPYDLDAWSILIREAQNQPIDKARKTYERLVAQFPSSGRFWKLYIEAEVTILFYFFLYQYCSIHCSDRKQVRNIAN Gene location: 11p13 Summary The CSTF-77 protein functions as a homodimer and interacts directly with both CSTF1 and CSTF2 in the CSTF complex. CstF-77 is required for proper 3?-end cleavage. Mutation of the Drosophila homolog of CstF-77, suppressor of forked su(f), results in the utilization of alternative poly(A) sites. This defect can be rescued by the addition of human CstF-77. CstF-77 contains 12 repeated sequences at the N-terminus, which are called HAT (half a TPR) motifs for their similarity to tetratricopeptide repeat (TPR) motifs. TPR motifs often mediate protein-protein interactions. Structural and biochemical data suggest that the HAT domain can be further divided into two sub-domains, HAT-N domain (residues 1– 240, with HAT motifs 1 through 5) and HAT-C domain (residues 241–549, HAT motifs 6 through 12). Most importantly, the structures reveal that the HAT domain is an intimately associated dimer, mediated by the HAT-C domain. The data suggest that CstF-77 may function as a dimer at a crucial stage in pre-mRNA 3?-end processing. The HAT domain is followed by a proline-rich segment in CstF-77. Far Western experiments showed that this segment binds the hinge region of CstF-64 and the WD-40 repeats of CstF-50. Electron microscopy and AUC experiments showed that Rna14p and Rna15p can form a heterotetramer. CstF-77 binds specifically to the CTD of PolII but with less efficiency than CstF-50. Rna14p binds to unphosphorylated CTD, but the binding increases upon phosphorylation of the CTD. Acts as a homodimer. CSTF3 directly interacts with CSTF1 and CSTF2. Interacts with FIP1L1. See this protein in other databases: Literature:
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