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
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
Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures.
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PAR-6 localizes to the apical junctional region with aPKC and PAR-3
"mammalian PAR-6 localizes to the apical junctional region together with aPKC and ASIP/PAR-3"
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aPKC forms a ternary complex with PAR-3 and PAR-6
"aPKC is critically involved in the development of the epithelial junctional structures and controls the cell polarity of mammalian epithelial cells, probably by forming a ternary complex with ASIP/PAR-3 and PAR-6"
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The PAR complex is required for tight junction formation and epithelial cell polarity
"aPKCkn blocks the completion of tight junction formation after calcium switch"
Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C.
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PAR6 proteins function as adaptors linking CDC42/RAC1 to aPKC signaling
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PAR6 binds GTP-bound Rac and Cdc42 via CRIB-like motif
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PAR6 binds aPKC (PKCiota/lambda and PKCzeta) via N-terminal association
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PAR6 forms ternary complex with GTPases and aPKC in vitro and in vivo
Direct interaction of two polarity complexes implicated in epithelial tight junction assembly.
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Par6 interacts directly with PALS1
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Par6-PALS1 interaction links Crumbs and Par3-Par6-aPKC complexes
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Par6 is required for tight junction assembly
Mammalian Lgl forms a protein complex with PAR-6 and aPKC independently of PAR-3 to regulate epithelial cell polarity.
Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network.
Nucleotide exchange factor ECT2 interacts with the polarity protein complex Par6/Par3/protein kinase Czeta (PKCzeta) and regulates PKCzeta activity.
Large-scale proteomics and phosphoproteomics of urinary exosomes.
A human MAP kinase interactome.
A proteome-scale map of the human interactome network.
Integrative analysis of kinase networks in TRAIL-induced apoptosis provides a source of potential targets for combination therapy.
A human interactome in three quantitative dimensions organized by stoichiometries and abundances.
Pooled-matrix protein interaction screens using Barcode Fusion Genetics.
Architecture of the human interactome defines protein communities and disease networks.
Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRAS(G13D).
A reference map of the human binary protein interactome.
Kinase Interaction Network Expands Functional and Disease Roles of Human Kinases.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
OpenCell: Endogenous tagging for the cartography of human cellular organization.
Recruitment of PAR-3:PAR-6:aPKC complex to tight junctions
Deep research report on PARD6B
Cyberian deep research on PARD6B function