PANTHER Family Review - Laminin/Netrin Extracellular Matrix (PTHR10574)
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NTN1/NTN3 have erroneous IBA annotations from PANTHER node PTN000180816 which incorrectly grouped netrins with POU-domain TFs
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PTHR10574 proteins are secreted ECM/guidance proteins with no DNA-binding domains
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Slit proteins bind Robo receptors and have an evolutionarily conserved role in repulsive axon guidance.
DSCAM functions as a netrin receptor in commissural axon pathfinding.
Netrin-1 up-regulation in inflammatory bowel diseases is required for colorectal cancer progression.
Transmembrane receptor DCC associates with protein synthesis machinery and regulates translation.
A Floor-Plate Extracellular Protein-Protein Interaction Screen Identifies Draxin as a Secreted Netrin-1 Antagonist.
Molecular characterization of Netrin-1 and APP receptor binding: New leads to block the progression of senile plaques in Alzheimer's disease.
Mutations in the netrin-1 gene cause congenital mirror movements.
Netrin-1 induced DCC clustering
DCC interaction with Netrin-1
DCC heterodimerizes with UNC-5:Netrin-1
DCC interaction with SIAH1
DCC interaction with SIAH2
Phosphorylation of DCC by Fyn
RhoGTPase GEF's recruited to DCC
Recruitment of Src and Fyn to DCC:FADK1
Recruitment and activation of N-WASP by Cdc42
Falcon deep research report for human NTN1
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NTN1 encodes secreted Netrin-1, an extracellular matrix-associated ligand that signals through DCC, NEO1, UNC5-family receptors, and context-specific integrins.
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The report supports Netrin-1 extracellular localization through secretion, ECM association, HSPG-dependent cell-surface organization, and receptor engagement in the extracellular microenvironment.
Nucleolar localization of a netrin-1 isoform enhances tumor cell proliferation.
Netrin1 establishes multiple boundaries for axon growth in the developing spinal cord.