| Interacting proteins: Q01081 and P26368 |
Pubmed |
SVM Score :0.0 |
| U 2 small nuclear ribonucleoprotein auxiliary factor ( U2AF ) , an essential mammalian splicing factor , is composed of two subunits : a 65 kDa protein ( U2AF65 ) , which binds the pre mRNA polypyrimidine tract and is required for in vitro splicing , and an associated 35 kDa protein ( U2AF35 ) . ^^^ We show directly that U2AF65 and U2AF35 interact with each other and delineate the regions of both proteins that mediate this interaction . ^^^ Using anti peptide antibodies against U2AF35 , we show that the protein has the intracellular distribution characteristic of U2AF65 . ^^^ Both U2AF65 and U2AF35 are concentrated in a small number of nuclear foci corresponding to coiled bodies , subnuclear organelles first identified by light microscopy in 1903 . . ^^^ |
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| Interacting proteins: Q01081 and P26368 |
Pubmed |
SVM Score :0.0 |
| The splicing factor U2AF ( U 2 snRNP auxiliary factor ) is a heterodimer with subunits of 65 and 35 kD ( U2AF65 and U2AF35 ) . ^^^ U2AF65 binds specifically to 3 ' splice sites , but previous studies failed to demonstrate a function for U2AF35 . ^^^ In vitro protein RNA interaction studies with pre mRNAs containing either a constitutive or regulated splicing enhancer revealed that U2AF35 directly mediates interactions between U2AF65 and proteins bound to the enhancers . ^^^ Thus , U2AF35 functions as a bridge between U2AF65 and the enhancer complex to recruit U2AF65 to the adjacent intron . . ^^^ |
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| Interacting proteins: Q01081 and P26368 |
Pubmed |
SVM Score :0.0 |
| This protein protein interaction profile is different from those of prototypical SR proteins SC 35 and ASF / SF2 , both of which interact with U 1 70K and U2AF35 but not with U2AF65 . p 54 promotes the use of the distal 5 ' splice site in E1A pre mRNA alternative splicing , while the same site is suppressed by ASF / SF2 and SC 35 . ^^^ |
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| Interacting proteins: Q01081 and P26368 |
Pubmed |
SVM Score :0.0 |
| Furthermore , transient expression assays using epitope tagged deletion mutants of U2AF65 indicate that targeting of the protein to nuclear speckles is not affected by removing either the RNA binding domain , the RS domain , or the region required for interaction with U2AF35 . ^^^ |
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| Interacting proteins: Q01081 and P26368 |
Pubmed |
SVM Score :0.0 |
| A protein related to splicing factor U2AF35 that interacts with U2AF65 and SR proteins in splicing of pre mRNA . ^^^ Recognition of a functional 3 ' splice site in pre mRNA splicing requires a heterodimer of the proteins U2AF65 / U2AF35 . ^^^ U2AF65 binds to RNA at the polypyrimidine tract , whereas U2AF35 is thought to interact through its arginine / serine rich ( RS ) domain with other RS domain containing factors bound at the 5 ' splice site , assembled in splicing enhancer complexes , or associated with the U4 / U6 . ^^^ Co immunodepletion showed that Urp is associated with the U2AF65 / U2AF35 heterodimer . ^^^ Binding studies revealed that Urp specifically interacts with U2AF65 through a U2AF35 homologous region and with SR proteins ( a large family of RS domain containing proteins ) through its RS domain . ^^^ |
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| Interacting proteins: Q01081 and P26368 |
Pubmed |
SVM Score :0.0 |
| This reaction is dependent upon the presence of the large subunit of U2AF , U2AF65 , but not the small subunit U2AF35 . ^^^ |
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| Interacting proteins: Q01081 and P26368 |
Pubmed |
SVM Score :0.0 |
| U2AF is a heterodimer comprising a large subunit , U2AF65 , and a small subunit , U2AF35 . ^^^ |
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| Interacting proteins: Q01081 and P26368 |
Pubmed |
SVM Score :0.0 |
| The U2AF subunit with a relative molecular mass ( Mr 65K ) of 65 , 000 ( U2AF65 ) binds to the poly ( Y ) tract , whereas the role of the 35K subunit ( U2AF35 ) has not been clearly defined . ^^^ Our results suggest that the U2AF65 U2AF35 complex identifies the U4CAG / R , with U2AF35 being responsible for recognition of the canonical AG . . ^^^ |
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| Interacting proteins: Q01081 and P26368 |
Pubmed |
SVM Score :0.0 |
| The role of U2AF35 and U2AF65 in enhancer dependent splicing . ^^^ Most importantly , we find that splicing activators promote the binding of both U2AF65 and U2AF35 to weak 3 ' splice sites under splicing conditions . ^^^ |
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| Interacting proteins: Q01081 and P26368 |
Pubmed |
SVM Score :0.0 |
| A novel peptide recognition mode revealed by the 10 ray structure of a core U2AF35 / U2AF65 heterodimer . ^^^ The 10 ray structure of the human core U2AF heterodimer , consisting of the U2AF35 central domain and a proline rich region of U2AF65 , has been determined at 2 . 2 A resolution . ^^^ The structure reveals a novel protein protein recognition strategy , in which an atypical RNA recognition motif ( RRM ) of U2AF35 and the U2AF65 polyproline segment interact via reciprocal `` tongue in groove ' ' tryptophan residues . ^^^ |
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| Interacting proteins: Q01081 and P26368 |
Pubmed |
SVM Score :0.0 |
| We further found in human cells that the exogenously expressed large U2AF subunit , U2AF65 , accumulates in spliced mRNP , leading to the recruitment of U2AF35 and TAP . ^^^ |
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| Interacting proteins: Q01081 and P26368 |
Pubmed |
SVM Score :0.0 |
| Induced folding of the U2AF35 RRM upon binding to U2AF65 . ^^^ Copurification of the recombinant U2AF35 RNA recognition motif ( U2AF35 RRM ) and full length U2AF65 yields a soluble and functionally active minimal U2AF heterodimer . ^^^ Recombinant U2AF35 RRM protein free and in complex with three different regions of U2AF65 was characterized by nuclear magnetic resonance spectroscopy . ^^^ We found that the recombinant U2AF35 RRM is unstructured in solution but its tertiary structure is induced upon binding to U2AF65 . ^^^ |
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| Interacting proteins: Q01081 and P26368 |
Pubmed |
SVM Score :0.0 |
| This sequence can bind to the essential heterodimeric splicing factor U2AF , with U2AF65 contacting the U tract and U2AF35 contacting the splice site itself ( AG / R ) . ^^^ |
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| Interacting proteins: Q01081 and P26368 |
Pubmed |
SVM Score :0.0 |
| FRET analyses of the U2AF complex localize the U2AF35 / U2AF65 interaction in vivo and reveal a novel self interaction of U2AF35 . ^^^ We have analyzed the interaction between the U2AF subunits U2AF35 and U2AF65 in vivo using fluorescence resonance energy transfer ( FRET ) microscopy . ^^^ U 2 snRNP Auxiliary Factor ( U2AF ) is an essential pre mRNA splicing factor complex , comprising 35 kDa ( U2AF35 ) and 65 kDa ( U2AF65 ) subunits . ^^^ U2AF65 interacts directly with the polypyrimidine tract and promotes binding of U 2 snRNP to the pre mRNA branchpoint , while U2AF35 associates with the conserved AG dinucleotide at the 3 ' end of the intron and has multiple functions in the splicing process . ^^^ Using two different approaches for measuring FRET , we have identified and spatially localized sites of direct interaction between U2AF35 and U2AF65 in vivo in live cell nuclei . ^^^ |
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| Interacting proteins: Q01081 and P26368 |
Pubmed |
SVM Score :0.0 |
| The 65 and 35 kD subunits of the splicing factor U2AF , U2AF65 and U2AF35 , recognize , respectively , the pyrimidine rich tract and the conserved terminal AG present at metazoan 3 ' splice sites . ^^^ DEK phosphorylated at serines 19 and 32 associates with U2AF35 , facilitates the U2AF35 AG interaction and prevents binding of U2AF65 to pyrimidine tracts not followed by AG . ^^^ |
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| Interacting proteins: Q01081 and P26368 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q01081 and P26368 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q01081 and P26368 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q01081 and P26368 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q01081 and P26368 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q01081 and P26368 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q01081 and P26368 |
Pubmed |
SVM Score :0.0 |
| NA |
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