Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on Enzyme Commission mapping
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Characterization of human LNX, a novel ligand of Numb protein X that is downregulated in human gliomas.
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The abstract reports that human LNX binds Ski-interacting protein/SNW1 through its PDZ domains.
"It showed that human LNX interacted with Ski interacting protein (SKIP) via PDZ domains."
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The interaction was supported by co-immunoprecipitation in HEK293 cells.
"The co-immunoprecipitation results suggested that LNX interacted with SKIP in HEK293 cells."
Towards a proteome-scale map of the human protein-protein interaction network.
A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration.
c-Src is a PDZ interaction partner and substrate of the E3 ubiquitin ligase Ligand-of-Numb protein X1.
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SRC recruitment depends on its C-terminal PDZ ligand.
"We demonstrate that the interaction of c-Src with LNX1 depends on the C-terminal PDZ ligand of c-Src."
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LNX1 ubiquitinates SRC.
"Moreover, c-Src itself is ubiquitinated by LNX1, suggesting an interdependent regulation of c-Src and LNX1."
MAGE-RING protein complexes comprise a family of E3 ubiquitin ligases.
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MAGEB18 binds a RING-containing E3 protein through its MAGE homology domain; the paper maps that partner as LNX1.
"MAGE-B18, MAGE-C2, and MAGE-G1 all bind E3 RING proteins through their MAGE homology domain"
Next-generation sequencing to generate interactome datasets.
Large-scale interaction profiling of PDZ domains through proteomic peptide-phage display using human and viral phage peptidomes.
A proteome-scale map of the human interactome network.
Widespread macromolecular interaction perturbations in human genetic disorders.
Pooled-matrix protein interaction screens using Barcode Fusion Genetics.
An interactome perturbation framework prioritizes damaging missense mutations for developmental disorders.
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
A reference map of the human binary protein interactome.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Quantitative fragmentomics allow affinity mapping of interactomes.
LNX functions as a RING type E3 ubiquitin ligase that targets the cell fate determinant Numb for ubiquitin-dependent degradation.
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The isolated LNX RING domain has E2-dependent E3 ligase activity, and a conserved-cysteine mutation abolishes it.
"The isolated RING finger domain was able to function as an E2-dependent, E3 ubiquitin ligase in vitro and mutation of a conserved cysteine residue within the RING domain abolished its activity"
Structure of LNX1:Ubc13~Ubiquitin Complex Reveals the Role of Additional Motifs for the E3 Ligase Activity of LNX1.
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Both zinc-finger motifs flanking the human LNX1 RING domain are required for ubiquitination activity.
"The RING domain of LNX1 is embedded between two zinc-finger motifs (Zn-RING-Zn), both of which are crucial for its ubiquitination activity."
Proteomic analysis reveals novel ligands and substrates for LNX1 E3 ubiquitin ligase.
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Human-cell assays identify PPFIA1, KLHL11, KIF7, and ERC2 as LNX1 ubiquitination substrates.
"We show that PPFIA1 (liprin-α1), KLHL11, KIF7 and ERC2 are substrates for ubiquitination by LNX1."
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LNX1p70 can act as a scaffold that promotes ubiquitination through recruitment of other E3 ligases.
"On this basis we propose a model whereby LNX1p70, despite lacking a catalytic RING domain, may function as a scaffold to promote ubiquitination of its ligands through recruitment of other E3-ligases."
Proteomics strategy to identify substrates of LNX, a PDZ domain-containing E3 ubiquitin ligase.
Positive feedback of SuFu negating protein 1 on Hedgehog signaling promotes colorectal tumor growth.
Activation of RhoC by regulatory ubiquitination is mediated by LNX1 and suppressed by LIS1.
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LNX1 robustly monoubiquitinates RHOC in human HEK293T cells without reducing total RHOC abundance.
"Co-transfection of HEK293T cells with 3xHA-RhoC and LNX1, LNX2 or Smurf1 followed by HA co-immunoprecipitation (IP), revealed robust monoubiquitination by LNX1, and to a lesser degree by LNX2 (Fig. 1B and S1B)."
UniProt record for human LNX1 (Q8TBB1)