Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Towards a proteome-scale map of the human protein-protein interaction network.
Architecture of the human interactome defines protein communities and disease networks.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
TSSC4 is a component of U5 snRNP that promotes tri-snRNP formation.
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TSSC4 is a U5 snRNP component and specific chaperone acting in de novo U5 snRNP biogenesis and in post-splicing recycling.
"TSSC4 emerges as a specific chaperone that acts in U5 snRNP de novo"
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TSSC4 interacts with the U5-specific proteins PRPF8, EFTUD2 and SNRNP200 - the same particle and overlapping partners as AAR2.
"Specifically, TSSC4 interacts with U5-specific proteins PRPF8, EFTUD2"
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EAPP is described in the U5 literature as a putative chaperone interacting with PRPF8 and EFTUD2, so the AAR2-EAPP interactions are not cross-pathway artefacts even though they remain uncharacterised.
"a putative chaperone EAPP that has been shown to interact with U5 proteins PRPF8 and EFTUD2"
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Human and yeast differ in when AAR2 leaves: yeast Aar2p is exchanged for Brr2p, whereas human AAR2 co-purifies with all four RNA-free heterotetrameric complex members.
"In yeast, Aar2p is exchanged with Brr2p13,14, while in humans AAR2 co-purifies with all four RHC members12, which indicates that AAR2 stays associated until the whole RHC is formed."
Structural and functional investigation of the human snRNP assembly factor AAR2 in complex with the RNase H-like domain of PRPF8.
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In vitro, human AAR2 locks the PRPF8 RNase H domain in a conformation compatible only with the first transesterification step of splicing, blocking the switch to the step-2 conformation - a regulatory role beyond acting as an SNRNP200 placeholder.
"seems to lock PRPF8 RH in a conformation that is only compatible with the first"
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Size-exclusion interaction studies of AAR2 with U5 proteins show similarities and marked differences relative to yeast Aar2p, and imply phosphorylation-dependent regulation analogous to that in yeast.
"Protein-interaction studies of AAR2 with U5 proteins using size-exclusion chromatography reveal similarities and marked differences in the interaction patterns compared with yeast Aar2p"
Crystallization and biochemical characterization of the human spliceosomal Aar2-Prp8(RNaseH) complex.
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Human C20ORF4 is a true Aar2 orthologue that binds the RNase H domain of PRP8, establishing an evolutionary link between yeast and human AAR2 function and providing the human AAR2-PRPF8 complex structure.
"as a true Aar2 orthologue which binds to the RH domain (hsRH) of Prp8 and"
Affinage mechanistic annotation for AAR2 (human)
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Machine-fetched Affinage record describing AAR2 as a U5 snRNP assembly factor that binds the PRPF8 RNase H domain, sterically occludes the SNRNP200/Brr2 binding sites and blocks U4/U6 di-snRNA loading, preventing premature spliceosome activation, with the handoff governed by phosphorylation.
"sterically occludes the binding sites for the Brr2/SNRNP200 helicase while also occupying the RNase H RNA-binding surface to block U4/U6 di-snRNA loading, thereby preventing premature spliceosome activation"