Gene Ontology annotation through association of InterPro records with GO terms
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
Electronic Gene Ontology annotations created by ARBA machine learning models
AP-4, a novel protein complex related to clathrin adaptors.
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Biochemical studies identify epsilon within the AP-4 heterotetramer in human cells.
"beta4 is a component of a
multisubunit complex (AP-4) that also contains the sigma4 polypeptide and two
additional adaptor subunit homologs named mu4 (mu-ARP2) and epsilon."
Characterization of a fourth adaptor-related protein complex.
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AP-4 forms nonclathrin carriers near the TGN; mu4 supplies the characterized cargo-motif interaction.
"Immunogold electron microscopy indicates that AP-4 is associated
with nonclathrin-coated vesicles in the region of the trans-Golgi network."
A human interactome in three quantitative dimensions organized by stoichiometries and abundances.
Bivalent Motif-Ear Interactions Mediate the Association of the Accessory Protein Tepsin with the AP-4 Adaptor Complex.
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Two distinct tepsin peptide–ear contacts support its recruitment to the AP-4 coat.
"Both peptide-ear interactions are required for efficient
association of tepsin with AP-4, and for recruitment of tepsin to the TGN."
The FTS-Hook-FHIP (FHF) complex interacts with AP-4 to mediate perinuclear distribution of AP-4 and its cargo ATG9A.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
AP4 transports APP from trans-Golgi network to endosome lumen
Functional and physical interactions of the adaptor protein complex AP-4 with ADP-ribosylation factors (ARFs).
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In-vitro-translated epsilon trunk co-precipitates with activated ARF1 but not the GDP-preferring comparator.
"ARF1Δ17-Q71L-myc but not ARF1Δ17-T31N-myc was found to co-precipitate with ε 1–727"
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The human epsilon construct was cloned from HeLa-cell RNA; this establishes reagent provenance separately from the binding result.
"The cDNA for the ε subunit of AP-4 was obtained by RT–PCR using gene-specific primers and total HeLa cell RNA."
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ARF1 switch-region substitutions abolish epsilon binding, supporting an activated-ARF1 effector interaction.
"placement of additional I49T, F51Y or Y81H mutations in the ARF1Δ17-Q71L protein abolished the interaction with both full-length ε and ε 1–727 in two-hybrid experiments"
Sorting of the Alzheimer's disease amyloid precursor protein mediated by the AP-4 complex.
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The APP cargo-recognition motif binds mu4, rather than establishing epsilon as the direct cargo-recognition subunit.
"we report the interaction of an YKFFE sequence from the
cytosolic tail of the Alzheimer's disease amyloid precursor protein (APP) with
the mu4 subunit of AP-4."
Structural basis for the dynamic conformations of AP-4 and its association with ARF1.
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Human epsilon has an experimentally supported direct ARF1 interface that recruits the AP-4 core to membranes.
"Collectively, our structural and biochemical data demonstrated direct interaction between the N-terminal region of ε and ARF1 in the AP-4/ARF1 complex."
AP4E1 primary evidence, construct boundaries and annotation decisions