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
Ancient ubiquitous protein 1 binds to the conserved membrane-proximal sequence of the cytoplasmic tail of the integrin alpha subunits that plays a crucial role in the inside-out signaling of alpha IIbbeta 3.
Proteomic analysis of exosomes from human neural stem cells by flow field-flow fractionation and nanoflow liquid chromatography-tandem mass spectrometry.
SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins.
Defining the membrane proteome of NK cells.
Ancient ubiquitous protein 1 (AUP1) localizes to lipid droplets and binds the E2 ubiquitin conjugase G2 (Ube2g2) via its G2 binding region.
Dual role of ancient ubiquitous protein 1 (AUP1) in lipid droplet accumulation and endoplasmic reticulum (ER) protein quality control.
Defining human ERAD networks through an integrative mapping strategy.
Monotopic topology is required for lipid droplet targeting of ancient ubiquitous protein 1.
Ancient ubiquitous protein-1 mediates sterol-induced ubiquitination of 3-hydroxy-3-methylglutaryl CoA reductase in lipid droplet-associated endoplasmic reticulum membranes.
MOR is not enough: identification of novel mu-opioid receptor interacting proteins using traditional and modified membrane yeast two-hybrid screens.
Monoubiquitination of ancient ubiquitous protein 1 promotes lipid droplet clustering.
Identification of ERAD components essential for dislocation of the null Hong Kong variant of α-1-antitrypsin (NHK).
AUP1 (Ancient Ubiquitous Protein 1) Is a Key Determinant of Hepatic Very-Low-Density Lipoprotein Assembly and Secretion.
Flaviviruses Exploit the Lipid Droplet Protein AUP1 to Trigger Lipophagy and Drive Virus Production.
A reference map of the human binary protein interactome.
A structurally conserved site in AUP1 binds the E2 enzyme UBE2G2 and is essential for ER-associated degradation.
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The 27-residue G2BR of AUP1 binds the backside of the ERAD E2 enzyme UBE2G2 with low-nanomolar affinity; this interaction maintains cellular UBE2G2 levels by preventing its rapid degradation, recruits UBE2G2 to the ER membrane, and allosterically activates ubiquitination in conjunction with ERAD E3 ligases.
AUP1 Regulates the Endoplasmic Reticulum-Associated Degradation and Polyubiquitination of NKCC2.
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AUP1 interacts with the ER-resident form of the kidney Na-K-2Cl cotransporter NKCC2 (SLC12A1) and with the ER lectin OS9, enhances NKCC2 ER retention and ERAD in a proteasome- and mannosidase-dependent manner, and is required for NKCC2 polyubiquitination; AUP1 also downregulates the related cotransporter NCC, indicating a broader role in ERAD of sodium-dependent chloride cotransporters relevant to antenatal Bartter syndrome type 1.