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FAQ

Cleavage and polyadenylation specificity factor subunit 2


Known also as: Cleavage and polyadenylation specificity factor 100 kDa subunit
Known abbreviations: CPSF2, CPSF100, KIAA1367

Yeast homolog: CFT2

Protein




Models
Domains

Secondary structure

Disorder

Top 3 models:
Template: 2i7x, chain A
Method: hhsearch
Fragment: 5-600
Template: 3zq4, chain A
Method: mgenthreader
Fragment: 605-782
Template: 3zq4, chain A
Method: hhsearch
Fragment: 1-596


Sequence length:782 aa
Molecular weight:88.487 kDa
Isoelectric point:4.85

Sequence:
1........10........20........30........40........50........60........70........80........90........100.......110.......120.......130
MTSIIKLTTLSGVQEESALCYLLQVDEFRFLLDCGWDEHFSMDIIDSLRKHVHQIDAVLLSHPDPLHLGALPYAVGKLGLNCAIYATIPVYKMGQMFMYDLYQSRHNTEDFTLFTLDDVDAAFDKIQQLK
FSQIVNLKGKGHGLSITPLPAGHMIGGTIWKIVKDGEEEIVYAVDFNHKREIHLNGCSLEMLSRPSLLITDSFNATYVQPRRKQRDEQLLTNVLETLRGDGNVLIAVDTAGRVLELAQLLDQIWRTKDAG
LGVYSLALLNNVSYNVVEFSKSQVEWMSDKLMRCFEDKRNNPFQFRHLSLCHGLSDLARVPSPKVVLASQPDLECGFSRDLFIQWCQDPKNSIILTYRTTPGTLARFLIDNPSEKITEIELRKRVKLEGK
ELEEYLEKEKLKKEAAKKLEQSKEADIDSSDESDIEEDIDQPSAHKTKHDLMMKGEGSRKGSFFKQAKKSYPMFPAPEERIKWDEYGEIIKPEDFLVPELQATEEEKSKLESGLTNGDEPMDQDLSDVPT
KCISTTESIEIKARVTYIDYEGRSDGDSIKKIINQMKPRQLIIVHGPPEASQDLAECCRAFGGKDIKVYMPKLHETVDATSETHIYQVRLKDSLVSSLQFCKAKDAELAWIDGVLDMRVSKVDTGVILEE
GELKDDGEDSEMQVEAPSDSSVIAQQKAMKSLFGDDEKETGEESEIIPTLEPLPPHEVPGHQSVFMNEPRLSDFKQVLLREGIQAEFVGGVLVCNNQVAVRRTETGRIGLEGCLCQDFYRIRDLLYEQYA
IV


Gene location: 14q31.1


Summary
CPSF2 is a component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. Involved in the histone 3' end pre-mRNA processing.

The exact function of this protein in 3?-end processing is currently not known.

CPSF-100 has recognizable sequence homology to CPSF-73 (23% identity and 49% similarity for their metallo-?-lactamase domains).Therefore, CPSF-100 is also a member of the ?-CASP superfamily of proteins. However, the zinc-binding residues are not conserved in CPSF-100, and therefore CPSF-100 cannot bind zinc and is not expected to be catalytically active.

Interacts with CPSF3, CSTF2, Ssu72, SYMPK, Pcf11p of CF IA, and the CTD of PolII.

Like CPSF-73, CPSF-100 has a second isoform in humans, known as RC-74 or Int11, also with disrupted zinc binding sites.

See this protein in other databases:
         

Literature:

Additional computationally mapped references ...


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