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
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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The PAR3-PAR6-aPKC ternary complex localizes to the apical junctional region
"mammalian PAR-6 localizes to the apical junctional region together with aPKC and ASIP/PAR-3"
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aPKC is critical for tight junction formation and epithelial cell polarity
"aPKC is critically involved in the development of the epithelial junctional structures and controls the cell polarity of mammalian epithelial cells"
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PAR-6 colocalizes with aPKC and PAR-3 at tight junctions
"aPKC associates with not only ASIP/PAR-3, but also with a mammalian homologue of another par-gene product, PAR-6"
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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Identified three human PAR6 homologs including PAR6gamma (PARD6G)
"we have cloned cDNAs for three human homologues of PAR6, designated PAR6alpha, beta and gamma, comprising 345, 372 and 376 amino acids, respectively"
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PAR6 contains PDZ domain and CRIB-like motif
"The PAR6 proteins harbour a PDZ domain and a CRIB-like motif"
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PAR6 directly interacts with GTP-bound Rac and Cdc42 via CRIB motif
"directly interact with GTP-bound Rac and Cdc42 via this motif"
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PAR6 interacts with aPKC (PKCiota and PKCzeta) via N-terminal PB1 domain
"with the aPKC isoforms PKCiota/lambda and PKCzeta via the N-terminal head-to-head association"
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PAR6 forms ternary complex with GTPases and aPKC
"allowing the PAR6 proteins to form a ternary complex with the GTPases and aPKC, both in vitro and in vivo"
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PAR6 functions as adaptor linking activated Rac/Cdc42 to aPKC signaling
"Human PAR6 homologues most likely play an important role in the cell polarization of mammalian cells, by functioning as an adaptor protein that links activated Rac and Cdc42 to aPKC signalling"
Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network.
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Identified interconnected protein network around Par complex modules
"From these data we constructed a highly interconnected protein network consisting of three core complex"
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Par-3/Par-6 forms core complex module
"formed around MARK4 (Par-1), Par-3.Par-6, and LKB1 (Par-4)"
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14-3-3 proteins occur in multiple Par complex modules
"some of which, like the 14-3-3 phospho-protein scaffolds, occur in more than one distinct complex"
A distinct PAR complex associates physically with VE-cadherin in vertebrate endothelial cells.
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PAR-3 and PAR-6 associate with VE-cadherin in endothelial cells
"Both PAR-3 and PAR-6 associate directly with the adherens junction protein vascular endothelial cadherin (VE-cadherin)"
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The VE-cadherin-associated PAR complex lacks aPKC
"the VE-cadherin-associated PAR protein complex lacks aPKC"
Integrative analysis of kinase networks in TRAIL-induced apoptosis provides a source of potential targets for combination therapy.
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).
Kinase Interaction Network Expands Functional and Disease Roles of Human Kinases.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Recruitment of PAR-3:PAR-6:aPKC complex to tight junctions
Capture, mutual inhibition and release mechanism for aPKC-Par6 and its multisite polarity substrate Lgl
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Cryo-EM structure of aPKC-Par6-Llgl1 complex
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Par6 PDZ domain regulates capture-and-release of polarity substrates
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CDC42 and Crumbs promote complex disassembly and substrate release
Deep research review of PARD6G function and cell polarity
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PAR-6 proteins are polarity adaptors with PB1 and CRIB-PDZ domains
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CDC42-GTP binding promotes apical membrane recruitment
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Par6 regulates aPKC activity through multiple interaction interfaces
Cyberian deep research on PARD6G function