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FAQ

Cleavage stimulation factor subunit 1


Known also as: CF-1 50 kDa subunit, Cleavage stimulation factor 50 kDa subunit
Known abbreviations: CSTF1, CstF-50, CstFp50

Yeast homolog: not known

Protein




Models
Domains

Secondary structure

Disorder

Top 3 models:
Template: 1nr0, chain A
Method: hhsearch
Fragment: 5-111
Template: 4ery, chain A
Method: pdbblast
Fragment: 104-432
Template: 1nr0, chain A
Method: phyre
Fragment: 4-425


Sequence length:431 aa
Molecular weight:48.358 kDa
Isoelectric point:6.3

Sequence:
1........10........20........30........40........50........60........70........80........90........100.......110.......120.......130
MYRTKVGLKDRQQLYKLIISQLLYDGYISIANGLINEIKPQSVCAPSEQLLHLIKLGMENDDTAVQYAIGRSDTVAPGTGIDLEFDADVQTMSPEASEYETCYVTSHKGPCRVATYSRDGQLIATGSADA
SIKILDTERMLAKSAMPIEVMMNETAQQNMENHPVIRTLYDHVDEVTCLAFHPTEQILASGSRDYTLKLFDYSKPSAKRAFKYIQEAEMLRSISFHPSGDFILVGTQHPTLRLYDINTFQCFVSCNPQDQ
HTDAICSVNYNSSANMYVTGSKDGCIKLWDGVSNRCITTFEKAHDGAEVCSAIFSKNSKYILSSGKDSVAKLWEISTGRTLVRYTGAGLSGRQVHRTQAVFNHTEDYVLLPDERTISLCCWDSRTAERRN
LLSLGHNNIVRCIVHSPTNPGFMTCSDDFRARFWYRRSTTD


Gene location: 20q13.2


Summary
One of the protein of CSTF complex. Required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. May be responsible for the interaction of CSTF with other factors to form a stable complex on the pre-mRNA.

It contains seven WD-40 repeats that begin about 90 residues from the N-terminus . The WD-40 repeats are required for interaction with CstF-77, and deletion of the last repeat reduces binding. CstF-50 also can self-associate and only the N-terminal region is required for this interaction. CstF-50 does not appear to have a sequence homolog in yeast.

WD6 repeat of CstF-50 interacts with protein BARD1, which associates with the tumor suppressor BRCA1. This interaction inhibits 3?-end cleavage of pre-mRNAs in vitro.

WD domains are responsible for interaction with CSTF3. Similar to mammalian G protein beta subunits, this protein contains transducin-like repeats.

Both CstF-50 and CstF-77 bind specifically to the CTD of PolII but CstF-50 binds with a higher efficiency. This binding is significantly reduced upon deletion of the first 91 amino acids of CstF-50, indicating that the WD-40 repeats are not sufficient for interaction. RNAi experiments showed that CstF-50 also interacts with the splicing co-activator SRm160, establishing another link between 3?-end processing and transcription.

Interacts directly with CSTF3.
Interacts with BARD1.


Acts as homodimer (N-terminus mediates homodimerization).

See this protein in other databases:
         

Literature:

Additional computationally mapped references ...


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