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
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
A proteome-scale map of the human interactome network.
GRAM domain proteins specialize functionally distinct ER-PM contact sites in human cells.
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GRAMD1a and GRAMD2a localize to distinct ER-PM contact sites
"Our analysis of the human family members, GRAMD1a and GRAMD2a, demonstrates that they are ER-PM MCS proteins, which mark separate regions of the plasma membrane (PM) and perform distinct functions in vivo"
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GRAMD1a localizes to ER-PM contacts in a PI(4,5)P2-independent manner
"GRAMD1a marks distinct ER-PM contacts in a PI(4,5)P2-independent manner"
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GRAM domain mediates PM association
"GRAM domain-dependent targeting of GRAMD1a and GRAMD2a to ER-PM MCSs"
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GRAMD1a co-localizes with ER marker Sec61beta
"GRAMD1a-eGFP with mCherry-Sec61beta and lyn-mCherry Z-stack, sample images are displayed in Figure 1C"
Aster proteins facilitate nonvesicular plasma membrane to ER cholesterol transport in mammalian cells.
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Established Aster nomenclature (GRAMD1A = Aster-A)
"three ER-resident proteins (Aster-A, -B, -C) that bind cholesterol and facilitate its removal from the plasma membrane"
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VASt domain binds cholesterol
"three ER-resident proteins (Aster-A, -B, -C) that bind cholesterol"
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Asters mediate PM to ER cholesterol transport
"Aster Proteins Facilitate Nonvesicular Plasma Membrane to ER Cholesterol Transport in Mammalian Cells"
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GRAM domain senses accessible cholesterol
"Aster N-terminal GRAM domain binds phosphatidylserine and mediates Aster recruitment to plasma membrane-ER contact sites in response to cholesterol accumulation in the plasma membrane"
The cholesterol transfer protein GRAMD1A regulates autophagosome biogenesis.
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Reports GRAMD1A affects autophagosome biogenesis
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Effect is mediated through cholesterol transfer activity
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Represents secondary function, not core role
Movement of accessible plasma membrane cholesterol by the GRAMD1 lipid transfer protein complex.
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GRAMD1 proteins move accessible PM cholesterol to ER
"endoplasmic reticulum (ER)-anchored lipid transfer proteins, the GRAMD1s, sense and transport accessible PM cholesterol to the ER"
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Transfer suppresses SREBP-2 activation
"Cells that lack all three GRAMD1s exhibit striking expansion of the accessible pool of PM cholesterol as a result of less efficient PM to ER transport of accessible cholesterol"
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GRAM domain is coincidence detector for cholesterol and PS
"GRAMD1s bind to one another and populate ER-PM contacts by sensing a transient expansion of the accessible pool of PM cholesterol via their GRAM domains"
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GRAMD1A forms complexes with GRAMD1B/C
"GRAMD1s bind to one another and populate ER-PM contacts"
A reference map of the human binary protein interactome.
Regulation of cellular cholesterol distribution via non-vesicular lipid transport at ER-Golgi contact sites.
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GRAMD1s also function at ER-Golgi contacts
"GRAMD1s transport excess cholesterol from the Golgi to the ER, thereby preventing its build-up"
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Export excess Golgi cholesterol to ER
"GRAMD1s transport excess cholesterol from the Golgi to the ER"
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Prevents chronic SREBP-2 activation
"This is accompanied by chronic activation of the SREBP-2 signalling pathway"
Deep research report on GRAMD1A