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 Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Electronic Gene Ontology annotations created by ARBA machine learning models
Membrane-associated guanylate kinase with inverted orientation (MAGI)-1/brain angiogenesis inhibitor 1-associated protein (BAP1) as a scaffolding molecule for Rap small G protein GDP/GTP exchange protein at tight junctions.
Association of the kinesin superfamily motor protein KIF1Balpha with postsynaptic density-95 (PSD-95), synapse-associated protein-97, and synaptic scaffolding molecule PSD-95/discs large/zona occludens-1 proteins.
Chimaeric HPV E6 proteins allow dissection of the proteolytic pathways regulating different E6 cellular target proteins.
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Papillomavirus E6 PDZ-binding sequences confer MAGI1 binding, with virus-type- specific consequences for MAGI1 degradation.
"enables them to bind Dlg and a second MAGUK family member, MAGI-1"
Carom: a novel membrane-associated guanylate kinase-interacting protein with two SH3 domains.
Proteomic analysis of beta1-adrenergic receptor interactions with PDZ scaffold proteins.
Postsynaptic recruitment of Dendrin depends on both dendritic mRNA transport and synaptic anchoring.
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Dendrin associates with MAGI/S-SCAM, which retains it in the cytoplasm and contributes to postsynaptic recruitment.
"Dendrin interacts with the cytoskeletal components alpha-actinin and Maguk"
Structures of a human papillomavirus (HPV) E6 polypeptide bound to MAGUK proteins: mechanisms of targeting tumor suppressors by a high-risk HPV oncoprotein.
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Crystal structures define direct HPV18 E6 peptide recognition by MAGI1 PDZ domains and the molecular determinants of E6-mediated targeting.
"peptide from HPV18 E6 bound to three PDZ domains from MAGI-1"
Interaction of endothelial cell-selective adhesion molecule and MAGI-1 promotes mature cell-cell adhesion via activation of RhoA.
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ESAM recruits MAGI1 to cell contacts, where the complex activates RhoA, promotes actin polymerization, and strengthens cell-cell adhesion.
"Interaction of ESAM with MAGI-1 activated RhoA"
IQGAP1 interacts with components of the slit diaphragm complex in podocytes and is involved in podocyte migration and permeability in vitro.
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MAGI1 localizes to the membrane and cytoplasmic extensions of human podocytes and associates with IQGAP1 in immunoprecipitation and proximity assays.
"MAGI-1 was localized at cell membrane and cytoplasmic extensions."
Comparative analysis of virus-host interactomes with a mammalian high-throughput protein complementation assay based on Gaussia princeps luciferase.
Cellular localization and characterization of cytosolic binding partners for Gla domain-containing proteins PRRG4 and PRRG2.
Proteome-wide analysis of phospho-regulated PDZ domain interactions.
The ATPase ATP6V1A facilitates rabies virus replication by promoting virion uncoating and interacting with the viral matrix protein.
Host PDZ-containing proteins targeted by SARS-CoV-2.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
OpenCell: Endogenous tagging for the cartography of human cellular organization.
Differential CFTR-Interactome Proximity Labeling Procedures Identify Enrichment in Multiple SLC Transporters.
Quantitative fragmentomics allow affinity mapping of interactomes.
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Quantitative fragmentomics measures a large PDZ-PBM affinity landscape that includes extensive MAGI1 domain interactions.
"65,000 interactions involving PDZ domains and their target PDZ-binding motifs"
Large-scale phage-based screening reveals extensive pan-viral mimicry of host short linear motifs.
Atrophin-1, the DRPLA gene product, interacts with two families of WW domain-containing proteins.
Cloning and characterization of BAI-associated protein 1: a PDZ domain-containing protein that interacts with BAI1.
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The original human MAGI1/BAP1 study identifies PDZ-dependent BAI1 binding and colocalization at the plasma membrane, especially cell-cell junctions.
"both products were co-localized at the cytoplasmic membrane"
Interaction of two actin-binding proteins, synaptopodin and alpha-actinin-4, with the tight junction protein MAGI-1.
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MAGI1 binds synaptopodin through WW2 and alpha-actinin-4 through PDZ5, and all three proteins colocalize at epithelial tight junctions.
"alpha-actinin-4 is also capable of binding to MAGI-1"
A systematic analysis of human papillomavirus (HPV) E6 PDZ substrates identifies MAGI-1 as a major target of HPV type 16 (HPV-16) and HPV-18 whose loss accompanies disruption of tight junctions.
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HPV16/18 E6 degrades MAGI1 at nuclear and membrane sites; MAGI1 loss disrupts tight-junction integrity and MAGI1 is required for junction restoration.
"restoration is dependent on the presence of MAGI-1"
Identification of MAGI1 as a tumor-suppressor protein induced by cyclooxygenase-2 inhibitors in colorectal cancer cells.
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MAGI1 gain and loss reciprocally regulate E-cadherin/beta-catenin junctional localization, actin organization, adhesion, Wnt signaling, migration, and invasion.
"stabilized E-cadherin and beta-catenin localization at cell-cell junctions"
UniProt entry Q96QZ7 (MAGI1_HUMAN), Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1
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Reviewed UniProt identifies six PDZ domains, two WW domains, a guanylate- kinase-like domain, tight-junction/cell-membrane localization, and numerous domain-mapped interaction partners.
"Localizes to epithelial cells tight junctions."
MAGI1 manual literature and annotation synthesis
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Manual synthesis identifies junctional molecular-adaptor activity as the best-supported core function and separates it from generic interaction records.
"The best-supported core role is organization of cell-cell junction complexes."