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.
The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation.
Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease.
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.
Ab initio protein modelling reveals novel human MIT domains.
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.
Toward an understanding of the protein interaction network of the human liver.
ESCRT-III governs the Aurora B-mediated abscission checkpoint through CHMP4C.
ALIX binds a YPX(3)L motif of the GPCR PAR1 and mediates ubiquitin-independent ESCRT-III/MVB sorting.
The chromosomal passenger complex controls the function of endosomal sorting complex required for transport-III Snf7 proteins during cytokinesis.
ESCRT machinery is required for plasma membrane repair.
ANCHR mediates Aurora-B-dependent abscission checkpoint control through retention of VPS4.
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.
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
Local curation notes for CHMP4C