Major phosphorylation of SF1 on adjacent Ser-Pro motifs enhances interaction with U2AF65.
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Mammalian splicing factor SF1 interacts with SURP domains of U2 snRNP-associated proteinsPhosphorylation-mediated regulation of alternative splicing in cancerDimerization and protein binding specificity of the U2AF homology motif of the splicing factor Puf60Structure, phosphorylation and U2AF65 binding of the N-terminal domain of splicing factor 1 during 3'-splice site recognitionStructure of Phosphorylated SF1 Bound to U2AF65 in an Essential Splicing Factor ComplexCancer-relevant Splicing Factor CAPERα Engages the Essential Splicing Factor SF3b155 in a Specific Ternary ComplexProtein kinase KIS localizes to RNA granules and enhances local translationSignaling from the secretory granule to the nucleus: Uhmk1 and PAMFormation of nuclear bodies by the lncRNA Gomafu-associating proteins Celf3 and SF1Elucidating the CXCL12/CXCR4 signaling network in chronic lymphocytic leukemia through phosphoproteomics analysisThe protein kinase KIS impacts gene expression during development and fear conditioning in adult mice.RNA induces conformational changes in the SF1/U2AF65 splicing factor complexPurification, crystallization and preliminary X-ray crystallographic analysis of a central domain of human splicing factor 1.Structural basis for regulation of RNA-binding proteins by phosphorylation.Large-scale phosphorylation analysis of mouse liverCorrelated Evolution of Nucleotide Positions within Splice Sites in Mammals.Large-scale comparative analysis of splicing signals and their corresponding splicing factors in eukaryotes.UHM-ULM interactions in the RBM39-U2AF65 splicing-factor complex.Different requirements of the kinase and UHM domains of KIS for its nuclear localization and binding to splicing factors.Interactome for auxiliary splicing factor U2AF(65) suggests diverse roles.Expression of kinase interacting with stathmin (KIS, UHMK1) in human brain and lymphoblasts: Effects of schizophrenia and genotype.Recognition of the 3' splice site RNA by the U2AF heterodimer involves a dynamic population shiftSR protein kinases promote splicing of nonconsensus introns.Diverse regulation of 3' splice site usage.SF1 Phosphorylation Enhances Specific Binding to U2AF65 and Reduces Binding to 3'-Splice-Site RNA.Unmasking the U2AF homology motif family: a bona fide protein-protein interaction motif in disguise.Cancer-Associated Mutations Mapped on High-Resolution Structures of the U2AF2 RNA Recognition Motifs.Post-Translational Modifications and RNA-Binding Proteins.
P2860
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P2860
Major phosphorylation of SF1 on adjacent Ser-Pro motifs enhances interaction with U2AF65.
description
2006 nî lūn-bûn
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2006年の論文
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name
Major phosphorylation of SF1 on adjacent Ser-Pro motifs enhances interaction with U2AF65.
@ast
Major phosphorylation of SF1 on adjacent Ser-Pro motifs enhances interaction with U2AF65.
@en
type
label
Major phosphorylation of SF1 on adjacent Ser-Pro motifs enhances interaction with U2AF65.
@ast
Major phosphorylation of SF1 on adjacent Ser-Pro motifs enhances interaction with U2AF65.
@en
prefLabel
Major phosphorylation of SF1 on adjacent Ser-Pro motifs enhances interaction with U2AF65.
@ast
Major phosphorylation of SF1 on adjacent Ser-Pro motifs enhances interaction with U2AF65.
@en
P2093
P2860
P1433
P1476
Major phosphorylation of SF1 on adjacent Ser-Pro motifs enhances interaction with U2AF65.
@en
P2093
Alexandre Maucuer
André Sobel
Jean-Pierre Le Caer
Matthew Swenson
Valérie Manceau
P2860
P304
P356
10.1111/J.1742-4658.2005.05091.X
P407
P577
2006-02-01T00:00:00Z