Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
A comprehensive resource of interacting protein regions for refining human transcription factor networks.
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The study used large-scale in vitro mRNA display to map interacting regions for human transcription-factor-related proteins; therefore, the reported LONRF3-PHB1 association is a screen-derived binary interaction rather than evidence that PHB1 is a LONRF3 substrate.
"Here we present the first large-scale IR data set obtained using mRNA display for 50 human transcription factors (TFs), including 12 transcription-related proteins."
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The reported 70% verification rate applies to the screen's core data set and does not establish that the individual LONRF3-PHB1 pair was independently validated or has an in-cell functional consequence.
"The core data set (966 IRs; 943 PPIs) displays a verification rate of 70%."
A proteome-scale map of the human interactome network.
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This study generated a systematic human binary-interaction map; its LONRF3 associations with APPBP2 and NOTCH2NLA are candidate direct contacts, not evidence that either protein is a LONRF3 substrate.
"Here, we describe a systematic map of ?14,000 high-quality human binary protein-protein interactions."
A reference map of the human binary protein interactome.
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HuRI is an all-by-all systematic reference map of binary interactions; its LONRF3 associations with CYSRT1, desmin, CTAG1B and TRAF2 remain screen-derived candidate contacts without demonstrated LONRF3-dependent ubiquitylation or degradation.
"Here we present a human 'all-by-all' reference interactome map of human binary protein interactions, or 'HuRI'."
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The map is designed as a broad reference network rather than a gene-specific mechanistic characterization.
"HuRI is a systematic proteome-wide reference that links genomic variation to phenotypic outcomes."
LONRF3 comparative domain analysis results
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Both predicted LONRF3 RING regions retain dense Cys/His patterns and are strongly conserved in the reviewed mouse ortholog, supporting intact RING-family architecture.
"Both regions retain dense Cys/His patterns and are strongly conserved in reviewed mouse Lonrf3, supporting intact rather than degenerate RING-family architecture:"
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LONRF3 lacks the AAA+ ATPase and protease-domain machinery found in the LONP1 control, so its isolated Lon N-terminal domain does not support peptidase activity.
"More decisively, the targeted presence matrix finds no AAA+ ATPase domain/core (IPR003593/IPR003959), Lon protease family call (IPR004815), peptidase S16 active site (IPR008268), or Lon proteolytic domain (IPR008269) in LONRF3. All five are present in the LONP1 control."
Induction of IL-17 and nonclassical T-cell activation by HIV-Tat protein.
UniProtKB entry Q496Y0 (LONF3_HUMAN)