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
The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42.
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Par6 is a key adaptor that links Cdc42 and atypical PKCs to Par3
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Par6 forms a complex with Cdc42-GTP, with PAR-3 and with aPKC regulatory domains
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Assembly implicated in formation of normal tight junctions
The mammalian homologue of the Caenorhabditis elegans polarity protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and Rac1.
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PAR-6 interacted with Cdc42 and Rac1 in yeast two-hybrid and in vitro binding assays
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Endogenous PAR-6 present in tight junctions and nucleus in MDCK cells
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PAR-6 and PAR-3 form a direct complex
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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aPKC forms ternary complex with ASIP/PAR-3 and PAR-6
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Complex localizes to apical junctional region
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aPKC critical for tight junction formation and cell polarity
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 directly interact with GTP-bound Rac and Cdc42 via CRIB-like motif
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PAR6 interacts with aPKC via N-terminal head-to-head association
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PAR6 functions as adaptor linking activated Rac/Cdc42 to aPKC signalling
Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network.
CRB3 binds directly to Par6 and regulates the morphogenesis of the tight junctions in mammalian epithelial cells.
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CRB3 directly interacts with Par6 via ERLI motif and PDZ domain
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CRB3 regulates tight junction morphogenesis through Par6
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Par6 acts as adaptor connecting CRB3 to polarity machinery
Structure of a cell polarity regulator, a complex between atypical PKC and Par6 PB1 domains.
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Crystal structure of PKCiota-Par6alpha PB1 domain complex at 1.5 A
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Both PB1 domains adopt ubiquitin fold
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PB1-PB1 interaction via OPCA motif and conserved lysine
Regulation of the polarity protein Par6 by TGFbeta receptors controls epithelial cell plasticity.
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Par6 interacts with TGFbeta receptors
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Par6 is phosphorylated by TbetaRII
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Phosphorylation controls SMURF1 interaction and EMT
G-protein-activated phospholipase C-beta, new partners for cell polarity proteins Par3 and Par6.
Towards a proteome-scale map of the human protein-protein interaction network.
A distinct PAR complex associates physically with VE-cadherin in vertebrate endothelial cells.
PKCzetaII is a target for degradation through the tumour suppressor protein pVHL.
Ect2 links the PKCiota-Par6alpha complex to Rac1 activation and cellular transformation.
Par6 alpha interacts with the dynactin subunit p150 Glued and is a critical regulator of centrosomal protein recruitment.
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Par6alpha localizes to centrosome and centriolar satellites
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Par6alpha interacts with PCM-1 and p150Glued
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Depletion causes mislocalization of centrosomal proteins
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Par6alpha critical for centrosome organization and cell division
Next-generation sequencing to generate interactome datasets.
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.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the PDZ domain of cellular proteins.
Disassembly of tight junctions
SMURF1 binds phosphorylated PARD6A
SMURF1 ubiquitinates RHOA
Recruitment of PAR-3:PAR-6:aPKC complex to tight junctions
DVL2 is phosphorylated after WNT5A binding to FZD
SMURF1/2 ubiquitinates PRICKLE1
SMURF1/2 are recruited to the DVL2:PARD6A complex
RAC1 binds effectors at the plasma membrane
CDC42 binds effectors at the plasma membrane
RHOU binds effectors at the plasma membrane
Deep research report on PARD6A
Cyberian deep research on PARD6A function