Relation Results

Summary

Name U2AF1/U2AF2
Primary ID SIGNOR-C78
Links CPX-1921
Type complex
Formed by U2AF1, U2AF2
Relations 4

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Type: Score: Layout: SPV 
0.70.20.20.338U2AF1/U2AF2Spliceosomal_snRNP_assemblyU2AF2U2AF1SRP54

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Relations
Regulator
Mechanism
target
score ℹ
+ U2AF1/U2AF2up-regulates img/indirect-activation.png Spliceosomal_snRNP_assembly 0.7
Identifier Residue Sequence Organism Cell Line
SIGNOR-263945 Homo sapiens
pmid sentence
The essential splicing factor U2AF (U2 auxiliary factor) is a heterodimer composed of 65-kDa (U2AF(65)) and 35-kDa (U2AF(35)) subunits. U2AF(35) has multiple functions in pre-mRNA splicing. First, U2AF(35) has been shown to function by directly interacting with the AG at the 3' splice site. Second, U2AF(35) is thought to play a role in the recruitment of U2AF(65) by serine-arginine-rich (SR) proteins in enhancer-dependent splicing.
Publications: 1 Organism: Homo Sapiens
+ U2AF2form complex img/form-complex.png binding U2AF1/U2AF2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-41948 Homo sapiens
pmid sentence
The splicing factor u2af (u2 snrnp auxiliary factor) is a heterodimer with subunits of 65 and 35 kd (u2af65 and u2af35).
Publications: 1 Organism: Homo Sapiens
+ U2AF1form complex img/form-complex.png binding U2AF1/U2AF2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-41945 Homo sapiens
pmid sentence
The splicing factor u2af (u2 snrnp auxiliary factor) is a heterodimer with subunits of 65 and 35 kd (u2af65 and u2af35).
Publications: 1 Organism: Homo Sapiens
+ SRP54up-regulates activity img/direct-activation.png binding U2AF1/U2AF2 0.338
Identifier Residue Sequence Organism Cell Line
SIGNOR-261162 in vitro
pmid sentence
We have now demonstrated that p54 interacts not only with SC35 and ASF/SF2 but also with U2AF. Pairwise interactions between p54 and other RS domain-containing spliceosomal proteins in comparison with SC35 and ASF/SF2 as detected by the yeast two-hybrid interaction assay. . It is conceivable that p54 can mediate 59 and 39 splice site interaction by interacting directly with U2AF65 associated with the 39 splice site and at the same time interact with other SR proteins, such as ASF/SF2 and SC35, which in turn interact with U1-70K. In this scenario, p54 is different from SC35 or ASF/SF2 in that it cannot directly interact with the 59 component (U1-70K) but can interact with the protein associated with the 39 splice site (U2AF65).
Publications: 1 Organism: In Vitro
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