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.
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.
CHMP7, a novel ESCRT-III-related protein, associates with CHMP4b and functions in the endosomal sorting pathway.
Human ESCRT-II complex and its role in human immunodeficiency virus type 1 release.
Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease.
Two distinct modes of ESCRT-III recognition are required for VPS4 functions in lysosomal protein targeting and HIV-1 budding.
Large-scale proteomics and phosphoproteomics of urinary exosomes.
Membrane scission by the ESCRT-III complex.
Defining the membrane proteome of NK cells.
MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis.
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.
Mechanism of inhibition of retrovirus release from cells by interferon-induced gene ISG15.
Syndecan-syntenin-ALIX regulates the biogenesis of exosomes.
ESCRT machinery is required for plasma membrane repair.
Structure of cellular ESCRT-III spirals and their relationship to HIV budding.
Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear envelope sealing.
ESCRT-III controls nuclear envelope reformation.
A reference map of the human binary protein interactome.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
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
UniProtKB entry Q96FZ7 (CHMP6)
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CHMP6 is a probable ESCRT-III component involved in MVB formation and cargo sorting and probably serves as an ESCRT-II acceptor on endosomal membranes.
"probably serves as an acceptor for the ESCRT-II complex on endosomal membranes"
CHMP6 review notes
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CHMP6 core function is ESCRT-II-to-ESCRT-III handoff and MVB cargo sorting rather than generic protein binding or broad ESCRT pleiotropy.
"CHMP6 is the human Vps20 ortholog and a core ESCRT-III pathway component."
Human CHMP6, a myristoylated ESCRT-III protein, interacts directly with an ESCRT-II component EAP20 and regulates endosomal cargo sorting.
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CHMP6 is myristoylated, interacts with EAP20 and CHMP4b, localizes to endosomal/MVB membranes, and regulates cargo sorting.
"CHMP6 acts as an acceptor for ESCRT-II on endosomal membranes and regulates cargo sorting"
Structure/function analysis of four core ESCRT-III proteins reveals common regulatory role for extreme C-terminal domain.
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Core ESCRT-III proteins including hVps20/CHMP6 are autoinhibited and can assemble on endosomal membranes when the C-terminal inhibitory region is removed.
"removing approximately 40 amino acids from the C-terminus of each protein unmasks a common ability to associate with endosomal membranes and assemble into large polymeric complexes"