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
The protein network of HIV budding.
Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins.
Towards a proteome-scale map of the human protein-protein interaction network.
Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a conserved VSL region in Vta1.
The ESCRT-III subunit hVps24 is required for degradation but not silencing of the epidermal growth factor receptor.
A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex.
Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding.
Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease.
Plasma membrane deformation by circular arrays of ESCRT-III protein filaments.
ALIX-CHMP4 interactions in the human ESCRT pathway.
Differential requirements for Alix and ESCRT-III in cytokinesis and HIV-1 release.
Membrane scission by the ESCRT-III complex.
Membrane budding and scission by the ESCRT machinery: it's all in the neck.
Human ESCRT-III and VPS4 proteins are required for centrosome and spindle maintenance.
ESCRT-III subunits Snf7-1 and Snf7-2 differentially regulate transmembrane cargos in hESC-derived human neurons.
The chromosomal passenger complex controls the function of endosomal sorting complex required for transport-III Snf7 proteins during cytokinesis.
ESCRT requirements for EIAV budding.
ESCRT machinery is required for plasma membrane repair.
Structure of cellular ESCRT-III spirals and their relationship to HIV budding.
A proteome-scale map of the human interactome network.
Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear envelope sealing.
ESCRT-III controls nuclear envelope reformation.
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
Comprehensive analysis of the human ESCRT-III-MIT domain interactome reveals new cofactors for cytokinetic abscission.
Recruitment Of HIV Virion Budding Machinery
VPS4 binds ESCRT-III assemblies at nuclear envelope (NE) fenestrations
CHMP7 binds CHMP4B, which recruits other subunits of the ESCRT-III complex
SPAST (spastin) binds the IST1 subunit of ESCRT-III at the sites of microtubule attachment to chromatin
VPS4 mediates disassembly of ESCRTIII subunits to promote sealing of holes in the nuclear envelope
SPAST (spastin) mediates the severing of microtubules at chromosome attachment sites
UniProt entry for CHMP4A (Q9BY43)
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CHMP4A is a probable core ESCRT-III component involved in MVB formation, endosomal cargo sorting, membrane fission, and exosomal release.
Local curation notes for CHMP4A