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FAQ

Cleavage stimulation factor subunit 3


Known also as: Cleavage stimulation factor 77 kDa subunit
Known abbreviations: CSTF3, CstF-77

Yeast homolog: RNA14

Protein

1
717
Suf



Models
Domains

Secondary structure

Disorder

Top 3 models:
Template: 2ooe, chain A
Method: mgenthreader
Fragment: 20-548
Template: 2pff, chain A
Method: compass
Fragment: 286-704
Template: 2uy1, chain A
Method: hhsearch
Fragment: 32-580


This protein has alternative isoforms:
Isoform 1:
Sequence length:717 aa
Molecular weight:82.922 kDa
Isoelectric point:8.06
Sequence:
1........10........20........30........40........50........60........70........80........90........100.......110.......120.......130
MSGDGATEQAAEYVPEKVKKAEKKLEENPYDLDAWSILIREAQNQPIDKARKTYERLVAQFPSSGRFWKLYIEAEIKAKNYDKVEKLFQRCLMKVLHIDLWKCYLSYVRETKGKLPSYKEKMAQAYDFAL
DKIGMEIMSYQIWVDYINFLKGVEAVGSYAENQRITAVRRVYQRGCVNPMINIEQLWRDYNKYEEGINIHLAKKMIEDRSRDYMNARRVAKEYETVMKGLDRNAPSVPPQNTPQEAQQVDMWKKYIQWEK
SNPLRTEDQTLITKRVMFAYEQCLLVLGHHPDIWYEAAQYLEQSSKLLAEKGDMNNAKLFSDEAANIYERAISTLLKKNMLLYFAYADYEESRMKYEKVHSIYNRLLAIEDIDPTLVYIQYMKFARRAEG
IKSGRMIFKKAREDTRTRHHVYVTAALMEYYCSKDKSVAFKIFELGLKKYGDIPEYVLAYIDYLSHLNEDNNTRVLFERVLTSGSLPPEKSGEIWARFLAFESNIGDLASILKVEKRRFTAFKEEYEGKE
TALLVDRYKFMDLYPCSASELKALGYKDVSRAKLAAIIPDPVVAPSIVPVLKDEVDRKPEYPKPDTQQMIPFQPRHLAPPGLHPVPGGVFPVPPAAVVLMKLLPPPICFQGPFVQVDELMEIFRRCKIPN
TVEEAVRIITGGAPELAVEGNGPVESNAVLTKAVKRPNEDSDEDEEKGAVVPPVHDIYRARQQKRIR



Isoform 2:
Sequence length:103 aa
Molecular weight:12.102 kDa
Isoelectric point:6.94
Sequence:
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:

Additional computationally mapped references ...


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