CHMP2A is a core ESCRT-III subunit that functions in membrane scission events with reverse topology. Key roles include MVB biogenesis, cytokinetic abscission, nuclear envelope reformation, viral budding, autophagosome closure, and plasma membrane repair.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000815 ESCRT III complex | IBA GO_REF:0000033 | ACCEPT | Summary: CHMP2A is a core ESCRT-III subunit that copolymerizes with CHMP3. Reason: Definitional - CHMP2A is a bona fide ESCRT-III subunit (PMID:18687924). Supporting Evidence: PMID:18687924 We found that the ESCRT-III proteins CHMP2A and CHMP3 (charged multivesicular body proteins 2A and 3) could assemble in vitro into helical tubular structures file:human/CHMP2A/CHMP2A-deep-research-falcon.md model: Edison Scientific Literature |
| GO:0000815 ESCRT III complex | IDA PMID:18687924 Helical structures of ESCRT-III are disassembled by VPS4. | ACCEPT | Summary: Direct evidence for CHMP2A-CHMP3 copolymerization. Reason: Core function confirmed by structural studies. Supporting Evidence: PMID:18687924 Aug 7. Helical structures of ESCRT-III are disassembled by VPS4. |
| GO:0000815 ESCRT III complex | IDA PMID:26040712 Spastin and ESCRT-III coordinate mitotic spindle disassembly... | ACCEPT | Summary: ESCRT-III localization confirmed during NE sealing. Reason: Core function confirmed. Supporting Evidence: PMID:26040712 Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear envelope sealing. |
| GO:0000815 ESCRT III complex | TAS PMID:20588296 Membrane budding and scission by the ESCRT machinery: it's a... | ACCEPT | Summary: ESCRT-III role in membrane scission reviewed. Reason: Core complex membership. Supporting Evidence: PMID:20588296 Jun 30. Membrane budding and scission by the ESCRT machinery: it's all in the neck. |
| GO:0005771 multivesicular body | IBA GO_REF:0000033 | ACCEPT | Summary: CHMP2A localizes to MVB membranes during ILV formation. Reason: Core localization supported by literature (PMID:16554368). |
| GO:0032585 multivesicular body membrane | IDA PMID:16554368 The ESCRT-III subunit hVps24 is required for degradation but... | ACCEPT | Summary: ESCRT-III localizes to MVB membranes. Reason: Core localization - endogenous hVps24 localized to late endosomes. Supporting Evidence: PMID:16554368 Mar 22. The ESCRT-III subunit hVps24 is required for degradation but not silencing of the epidermal growth factor receptor. |
| GO:0032585 multivesicular body membrane | IEA GO_REF:0000117 | ACCEPT | Summary: ESCRT-III localization to MVB membrane. Reason: Consistent with core function. |
| GO:0071985 multivesicular body sorting pathway | IDA PMID:16554368 The ESCRT-III subunit hVps24 is required for degradation but... | ACCEPT | Summary: CHMP2A functions in MVB sorting. Reason: Core function - hVps24 depletion impairs EGFR degradation. Supporting Evidence: PMID:16554368 Mar 22. The ESCRT-III subunit hVps24 is required for degradation but not silencing of the epidermal growth factor receptor. |
| GO:0071985 multivesicular body sorting pathway | IEA GO_REF:0000117 | ACCEPT | Summary: ESCRT-III required for MVB sorting. Reason: Core function. |
| GO:0032509 endosome transport via multivesicular body sorting pathway | IBA GO_REF:0000033 | ACCEPT | Summary: CHMP2A required for MVB-mediated transport. Reason: Core function of ESCRT-III. |
| GO:0043162 ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway | IDA PMID:17984323 Functional multivesicular bodies are required for autophagic... | ACCEPT | Summary: ESCRT-III sorts ubiquitinated cargo for degradation. Reason: Core function. Supporting Evidence: PMID:17984323 Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease. |
| GO:0043162 ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway | IEA GO_REF:0000117 | ACCEPT | Summary: ESCRT-III required for ubiquitinated cargo degradation. Reason: Core function. |
| GO:0036258 multivesicular body assembly | TAS PMID:20588296 Membrane budding and scission by the ESCRT machinery: it's a... | ACCEPT | Summary: ESCRT-III is required for MVB assembly. Reason: Core function. Supporting Evidence: PMID:20588296 Jun 30. Membrane budding and scission by the ESCRT machinery: it's all in the neck. |
| GO:0036258 multivesicular body assembly | NAS PMID:16505166 Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a... | ACCEPT | Summary: ESCRT function required for MVB assembly. Reason: Core function. Supporting Evidence: PMID:16505166 Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a conserved VSL region in Vta1. |
| GO:0045324 late endosome to vacuole transport | IBA GO_REF:0000033 | ACCEPT | Summary: CHMP2A functions in late endosome maturation. Reason: ESCRT-III required for MVE-lysosome fusion (PMID:16554368). |
| GO:1902774 late endosome to lysosome transport | IMP PMID:17984323 Functional multivesicular bodies are required for autophagic... | ACCEPT | Summary: ESCRT-III required for late endosome to lysosome transport. Reason: Core function. Supporting Evidence: PMID:17984323 Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease. |
| GO:1902774 late endosome to lysosome transport | IEA GO_REF:0000117 | ACCEPT | Summary: ESCRT-III required for late endosome to lysosome transport. Reason: Core function. |
| GO:0061763 multivesicular body-lysosome fusion | NAS PMID:16505166 Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a... | ACCEPT | Summary: ESCRT function required for MVB-lysosome fusion. Reason: Core function. Supporting Evidence: PMID:16505166 Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a conserved VSL region in Vta1. |
| GO:0061952 midbody abscission | IMP PMID:20616062 Human ESCRT-III and VPS4 proteins are required for centrosom... | ACCEPT | Summary: CHMP2A required for cytokinetic abscission. Reason: Core function - ESCRT-III depletion inhibits abscission. Supporting Evidence: PMID:20616062 We found that depletion of VPS4A, VPS4B, or any of the 11 different human ESCRT-III (CHMP) proteins inhibited abscission |
| GO:0061952 midbody abscission | IEA GO_REF:0000117 | ACCEPT | Summary: CHMP2A required for cytokinetic abscission. Reason: Core function. |
| GO:0030496 midbody | IDA PMID:26040712 Spastin and ESCRT-III coordinate mitotic spindle disassembly... | ACCEPT | Summary: ESCRT-III localizes to midbody during cytokinesis. Reason: Core localization for abscission function. Supporting Evidence: PMID:26040712 Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear envelope sealing. |
| GO:0030496 midbody | IEA GO_REF:0000117 | ACCEPT | Summary: ESCRT-III localizes to midbody. Reason: Core localization. |
| GO:0031468 nuclear membrane reassembly | IMP PMID:26040712 Spastin and ESCRT-III coordinate mitotic spindle disassembly... | ACCEPT | Summary: ESCRT-III required for NE sealing during mitotic exit. Reason: Core function. Supporting Evidence: PMID:26040712 We propose that ESCRT-III, VPS4 and spastin cooperate to coordinate nuclear envelope sealing and spindle disassembly |
| GO:0031468 nuclear membrane reassembly | IMP PMID:26040713 ESCRT-III controls nuclear envelope reformation. | ACCEPT | Summary: ESCRT-III required for NE sealing. Reason: Core function. Supporting Evidence: PMID:26040713 The ESCRT-III component charged multivesicular body protein 2A (CHMP2A) is directed to the forming NE through binding to CHMP4B, and provides an activity essential for NE reformation. |
| GO:0031468 nuclear membrane reassembly | IEA GO_REF:0000117 | ACCEPT | Summary: ESCRT-III required for nuclear membrane reassembly. Reason: Core function. |
| GO:0005635 nuclear envelope | IDA PMID:26040712 Spastin and ESCRT-III coordinate mitotic spindle disassembly... | ACCEPT | Summary: ESCRT-III localizes to nuclear envelope during reformation. Reason: Core localization for NE sealing. Supporting Evidence: PMID:26040712 Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear envelope sealing. |
| GO:0005635 nuclear envelope | IEA GO_REF:0000044 | ACCEPT | Summary: ESCRT-III localization to nuclear envelope. Reason: Core localization. |
| GO:0010458 exit from mitosis | IMP PMID:26040712 Spastin and ESCRT-III coordinate mitotic spindle disassembly... | ACCEPT | Summary: ESCRT-III functions during mitotic exit. Reason: Core function. Supporting Evidence: PMID:26040712 Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear envelope sealing. |
| GO:0000785 chromatin | IDA PMID:28242692 LEM2 recruits CHMP7 for ESCRT-mediated nuclear envelope clos... | ACCEPT | Summary: CHMP2A recruited to chromatin disks during NE reformation. Reason: ESCRT-III recruited to anaphase chromatin for NE sealing. Supporting Evidence: PMID:28242692 LEM2 recruits CHMP7 for ESCRT-mediated nuclear envelope closure in fission yeast and human cells. |
| GO:0039702 viral budding via host ESCRT complex | IDA PMID:24878737 Structure of cellular ESCRT-III spirals and their relationsh... | ACCEPT | Summary: ESCRT-III forms spirals around nascent HIV Gag assemblies. Reason: Core function. Supporting Evidence: PMID:24878737 depleting Vps4 traps ESCRT-III filaments around nascent Gag assemblies |
| GO:0039702 viral budding via host ESCRT complex | IMP PMID:23051622 ESCRT-III CHMP2A and CHMP3 form variable helical polymers in... | ACCEPT | Summary: CHMP2A required for viral budding. Reason: Core function. Supporting Evidence: PMID:23051622 CHMP3 contributes synergistically to HIV-1 budding, and the CHMP3 contribution is ~ 10-fold more pronounced in concert with CHMP2A than with CHMP2B |
| GO:0039702 viral budding via host ESCRT complex | TAS PMID:20588296 Membrane budding and scission by the ESCRT machinery: it's a... | ACCEPT | Summary: ESCRT-III involved in viral budding. Reason: Core function. Supporting Evidence: PMID:20588296 Jun 30. Membrane budding and scission by the ESCRT machinery: it's all in the neck. |
| GO:0039702 viral budding via host ESCRT complex | IEA GO_REF:0000117 | ACCEPT | Summary: ESCRT-III required for viral budding. Reason: Core function. |
| GO:0039702 viral budding via host ESCRT complex | IGI PMID:24107264 ESCRT requirements for EIAV budding. | ACCEPT | Summary: CHMP2A genetic interaction in viral budding. Reason: Core function - EIAV budding requires CHMP2A-VPS4 interactions. Supporting Evidence: PMID:24107264 EIAV budding was inhibited by point mutations that abrogate the direct interactions between ALIX:CHMP4B, CHMP4B:CHMP2A, and CHMP2A:VPS4A/B |
| GO:0046761 viral budding from plasma membrane | IDA PMID:24878737 Structure of cellular ESCRT-III spirals and their relationsh... | ACCEPT | Summary: ESCRT-III functions at plasma membrane during viral budding. Reason: Core function. Supporting Evidence: PMID:24878737 Structure of cellular ESCRT-III spirals and their relationship to HIV budding. |
| GO:0046761 viral budding from plasma membrane | IMP PMID:14505570 The protein network of HIV budding. | ACCEPT | Summary: CHMP2A required for HIV-1 budding. Reason: Core function for viral infection. Supporting Evidence: PMID:14505570 dominant-negative mutants of late-acting human class E proteins arrested HIV-1 budding through plasmal and endosomal membranes |
| GO:0046761 viral budding from plasma membrane | IEA GO_REF:0000117 | ACCEPT | Summary: ESCRT-III required for viral budding from PM. Reason: Core function. |
| GO:0019076 viral release from host cell | IMP PMID:23051622 ESCRT-III CHMP2A and CHMP3 form variable helical polymers in... | ACCEPT | Summary: CHMP2A required for virus release. Reason: Core function for viral budding. Supporting Evidence: PMID:23051622 ESCRT-III CHMP2A and CHMP3 form variable helical polymers in vitro and act synergistically during HIV-1 budding. |
| GO:0019076 viral release from host cell | IGI PMID:23051622 ESCRT-III CHMP2A and CHMP3 form variable helical polymers in... | ACCEPT | Summary: Genetic interaction with CHMP4A in viral release. Reason: Core function. Supporting Evidence: PMID:23051622 ESCRT-III CHMP2A and CHMP3 form variable helical polymers in vitro and act synergistically during HIV-1 budding. |
| GO:0019076 viral release from host cell | IGI PMID:23051622 ESCRT-III CHMP2A and CHMP3 form variable helical polymers in... | ACCEPT | Summary: Genetic interaction with CHMP3 in viral release. Reason: Core function. Supporting Evidence: PMID:23051622 ESCRT-III CHMP2A and CHMP3 form variable helical polymers in vitro and act synergistically during HIV-1 budding. |
| GO:0097352 autophagosome maturation | IMP PMID:17984323 Functional multivesicular bodies are required for autophagic... | ACCEPT | Summary: ESCRT-III required for autophagosome maturation. Reason: Core function - needed for phagophore closure. Supporting Evidence: PMID:17984323 autophagic degradation is inhibited in cells depleted of ESCRT subunits |
| GO:0097352 autophagosome maturation | IEA GO_REF:0000117 | ACCEPT | Summary: ESCRT required for autophagosome maturation. Reason: Core function. |
| GO:0006914 autophagy | IMP PMID:17984323 Functional multivesicular bodies are required for autophagic... | ACCEPT | Summary: ESCRT depletion impairs autophagic degradation. Reason: Core function. Supporting Evidence: PMID:17984323 Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease. |
| GO:0016236 macroautophagy | TAS PMID:20588296 Membrane budding and scission by the ESCRT machinery: it's a... | ACCEPT | Summary: ESCRT-III required for macroautophagy. Reason: Core function. Supporting Evidence: PMID:20588296 Jun 30. Membrane budding and scission by the ESCRT machinery: it's all in the neck. |
| GO:0000421 autophagosome membrane | IDA PMID:17984323 Functional multivesicular bodies are required for autophagic... | ACCEPT | Summary: CHMP2A localizes to autophagosome membranes. Reason: Core localization. Supporting Evidence: PMID:17984323 Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease. |
| GO:1904930 amphisome membrane | IDA PMID:17984323 Functional multivesicular bodies are required for autophagic... | ACCEPT | Summary: CHMP2A localizes to amphisome membranes. Reason: ESCRT-III functions at autophagosome-endosome fusion sites. Supporting Evidence: PMID:17984323 Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease. |
| GO:1904930 amphisome membrane | IEA GO_REF:0000117 | ACCEPT | Summary: ESCRT-III localizes to amphisome membrane. Reason: Core localization. |
| GO:0001778 plasma membrane repair | IDA PMID:24482116 ESCRT machinery is required for plasma membrane repair. | ACCEPT | Summary: ESCRT machinery required for plasma membrane repair. Reason: Core function - ESCRT proteins recruited within seconds to wounds. Supporting Evidence: PMID:24482116 ESCRT proteins were recruited within seconds to plasma membrane wounds |
| GO:0001778 plasma membrane repair | IEA GO_REF:0000117 | ACCEPT | Summary: ESCRT machinery required for PM repair. Reason: Core function. |
| GO:0090148 membrane fission | IDA PMID:36604498 Structural basis of CHMP2A-CHMP3 ESCRT-III polymer assembly ... | ACCEPT | Summary: Direct evidence for CHMP2A membrane fission activity. Reason: Core function. Supporting Evidence: PMID:36604498 Epub 2023 Jan 5. Structural basis of CHMP2A-CHMP3 ESCRT-III polymer assembly and membrane cleavage. |
| GO:0090148 membrane fission | NAS PMID:19234443 Membrane scission by the ESCRT-III complex. | ACCEPT | Summary: ESCRT-III mediates membrane fission. Reason: Core function. Supporting Evidence: PMID:19234443 ESCRT-III has the instrinsic ability to drive the scission of membrane necks |
| GO:0180020 membrane bending activity | IDA PMID:36604498 Structural basis of CHMP2A-CHMP3 ESCRT-III polymer assembly ... | ACCEPT | Summary: Direct evidence for CHMP2A membrane bending. Reason: Core molecular function. Supporting Evidence: PMID:36604498 Epub 2023 Jan 5. Structural basis of CHMP2A-CHMP3 ESCRT-III polymer assembly and membrane cleavage. |
| GO:0010324 membrane invagination | IMP PMID:24878737 Structure of cellular ESCRT-III spirals and their relationsh... | ACCEPT | Summary: ESCRT-III induces membrane invagination. Reason: Core molecular function. Supporting Evidence: PMID:24878737 Structure of cellular ESCRT-III spirals and their relationship to HIV budding. |
| GO:0031210 phosphatidylcholine binding | IMP PMID:18687924 Helical structures of ESCRT-III are disassembled by VPS4. | ACCEPT | Summary: CHMP2A/CHMP3 polymers interact with lipid bilayers. Reason: Molecular function - ESCRT-III binds membrane lipids. Supporting Evidence: PMID:18687924 Aug 7. Helical structures of ESCRT-III are disassembled by VPS4. |
| GO:0051258 protein polymerization | IMP PMID:23051622 ESCRT-III CHMP2A and CHMP3 form variable helical polymers in... | ACCEPT | Summary: ESCRT-III polymerizes into helical structures. Reason: Core molecular activity. Supporting Evidence: PMID:23051622 ESCRT-III CHMP2A and CHMP3 form variable helical polymers in vitro and act synergistically during HIV-1 budding. |
| GO:0051258 protein polymerization | IMP PMID:24878737 Structure of cellular ESCRT-III spirals and their relationsh... | ACCEPT | Summary: ESCRT-III filament polymerization observed. Reason: Core molecular activity. Supporting Evidence: PMID:24878737 Structure of cellular ESCRT-III spirals and their relationship to HIV budding. |
| GO:0051260 protein homooligomerization | IMP PMID:18687924 Helical structures of ESCRT-III are disassembled by VPS4. | ACCEPT | Summary: CHMP2A can self-associate and copolymerize with CHMP3. Reason: Molecular property of ESCRT-III subunits. Supporting Evidence: PMID:18687924 Aug 7. Helical structures of ESCRT-III are disassembled by VPS4. |
| GO:0019904 protein domain specific binding | IPI PMID:17928862 ESCRT-III recognition by VPS4 ATPases. | ACCEPT | Summary: VPS4 recognizes CHMP2A through MIT-MIM domain interaction. Reason: Specific molecular function - CHMP2A contains MIM that binds VPS4 MIT domain. Supporting Evidence: PMID:17928862 the microtubule interacting and transport (MIT) domains of human VPS4A and VPS4B bind conserved sequence motifs located at the carboxy termini of the CHMP1-3 class of ESCRT-III proteins |
| GO:0019904 protein domain specific binding | IPI PMID:17928862 ESCRT-III recognition by VPS4 ATPases. | ACCEPT | Summary: VPS4B MIT domain binds CHMP2A MIM. Reason: Specific molecular function. Supporting Evidence: PMID:17928862 ESCRT-III recognition by VPS4 ATPases. |
| GO:1904903 ESCRT III complex disassembly | NAS PMID:20588296 Membrane budding and scission by the ESCRT machinery: it's a... | ACCEPT | Summary: VPS4-mediated ESCRT-III disassembly is required for function. Reason: Core regulatory process. Supporting Evidence: PMID:20588296 Jun 30. Membrane budding and scission by the ESCRT machinery: it's all in the neck. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-917700 | ACCEPT | Summary: CHMP2A is cytosolic in autoinhibited state before membrane recruitment. Reason: Accurate - ESCRT-III proteins exist in cytosol before activation. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3159232 | ACCEPT | Summary: CHMP2A cytosolic localization in ESCRT pathway. Reason: Core localization when inactive. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5671702 | ACCEPT | Summary: CHMP2A cytosolic localization. Reason: Core localization. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-917693 | ACCEPT | Summary: CHMP2A cytosolic localization. Reason: Core localization. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9668389 | ACCEPT | Summary: CHMP2A cytosolic localization. Reason: Core localization. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9668395 | ACCEPT | Summary: CHMP2A cytosolic localization. Reason: Core localization. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9668398 | ACCEPT | Summary: CHMP2A cytosolic localization. Reason: Core localization. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9668405 | ACCEPT | Summary: CHMP2A cytosolic localization. Reason: Core localization. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9668415 | ACCEPT | Summary: CHMP2A cytosolic localization. Reason: Core localization. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9668419 | ACCEPT | Summary: CHMP2A cytosolic localization. Reason: Core localization. |
| GO:0005829 cytosol | IEA GO_REF:0000107 | ACCEPT | Summary: CHMP2A cytosolic localization. Reason: Core localization when inactive. |
| GO:0005886 plasma membrane | IDA PMID:24878737 Structure of cellular ESCRT-III spirals and their relationsh... | ACCEPT | Summary: CHMP2A localizes to plasma membrane during viral budding. Reason: Core localization for viral budding function. Supporting Evidence: PMID:24878737 Structure of cellular ESCRT-III spirals and their relationship to HIV budding. |
| GO:0005765 lysosomal membrane | IDA PMID:17984323 Functional multivesicular bodies are required for autophagic... | ACCEPT | Summary: CHMP2A localizes to lysosomal membrane during autophagy. Reason: ESCRT-III functions at autophagosome/MVB-lysosome interface. Supporting Evidence: PMID:17984323 Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease. |
| GO:0005765 lysosomal membrane | IEA GO_REF:0000117 | ACCEPT | Summary: ESCRT-III localization to lysosomal membrane. Reason: Core localization. |
| GO:0031902 late endosome membrane | IEA GO_REF:0000044 | ACCEPT | Summary: CHMP2A localizes to late endosome/MVB membranes. Reason: Core localization. |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | ACCEPT | Summary: CHMP2A detected in membrane proteome. Reason: General but accurate. Supporting Evidence: PMID:19946888 Defining the membrane proteome of NK cells. |
| GO:0030117 membrane coat | IMP PMID:24878737 Structure of cellular ESCRT-III spirals and their relationsh... | ACCEPT | Summary: ESCRT-III forms coat-like structures on membranes. Reason: ESCRT-III polymers form membrane-associated coats/spirals. Supporting Evidence: PMID:24878737 Structure of cellular ESCRT-III spirals and their relationship to HIV budding. |
| GO:1903543 positive regulation of exosomal secretion | IMP PMID:22660413 Syndecan-syntenin-ALIX regulates the biogenesis of exosomes. | ACCEPT | Summary: ESCRT-III involved in exosome biogenesis. Reason: Core function - MVB-derived exosomes require ESCRT. Supporting Evidence: PMID:22660413 Syntenin exosomes depend on the availability of heparan sulphate, syndecans, ALIX and ESCRTs |
| GO:0070062 extracellular exosome | HDA PMID:23533145 In-depth proteomic analyses of exosomes isolated from expres... | KEEP AS NON CORE | Summary: CHMP2A detected in exosome proteomics. Reason: Detection expected given ESCRT role in exosome biogenesis. Supporting Evidence: PMID:23533145 2013 Apr 23. In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. |
| GO:0070062 extracellular exosome | HDA PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exos... | KEEP AS NON CORE | Summary: CHMP2A detected in exosome proteomics. Reason: Detection expected given ESCRT role in exosome biogenesis. Supporting Evidence: PMID:19056867 2008 Dec 3. Large-scale proteomics and phosphoproteomics of urinary exosomes. |
| GO:0070062 extracellular exosome | HDA PMID:20458337 MHC class II-associated proteins in B-cell exosomes and pote... | KEEP AS NON CORE | Summary: CHMP2A detected in exosome proteomics. Reason: Detection expected given ESCRT role in exosome biogenesis. Supporting Evidence: PMID:20458337 2010 May 11. MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. |
| GO:0000776 kinetochore | IDA PMID:26040712 Spastin and ESCRT-III coordinate mitotic spindle disassembly... | KEEP AS NON CORE | Summary: ESCRT-III proteins localize to kinetochores during mitosis. Reason: Non-core localization. Supporting Evidence: PMID:26040712 Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear envelope sealing. |
| GO:0000776 kinetochore | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ESCRT-III localization to kinetochore. Reason: Non-core localization. |
| GO:0005828 kinetochore microtubule | IDA PMID:26040712 Spastin and ESCRT-III coordinate mitotic spindle disassembly... | KEEP AS NON CORE | Summary: ESCRT-III recruited to sites where NE engulfs spindle microtubules. Reason: Non-core localization. Supporting Evidence: PMID:26040712 Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear envelope sealing. |
| GO:0005828 kinetochore microtubule | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ESCRT-III localization to kinetochore microtubule. Reason: Non-core localization. |
| GO:0005643 nuclear pore | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ESCRT-III implicated in NPC surveillance in yeast. Reason: Primary function is NE sealing rather than NPC-specific activity. |
| GO:0007080 mitotic metaphase chromosome alignment | IMP PMID:20616062 Human ESCRT-III and VPS4 proteins are required for centrosom... | KEEP AS NON CORE | Summary: CHMP2A depletion causes chromosome alignment defects. Reason: Secondary effect of centrosome/spindle defects. Supporting Evidence: PMID:20616062 Human ESCRT-III and VPS4 proteins are required for centrosome and spindle maintenance. |
| GO:0007080 mitotic metaphase chromosome alignment | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ESCRT-III role in chromosome alignment. Reason: Secondary effect. |
| GO:0006997 nucleus organization | IMP PMID:20616062 Human ESCRT-III and VPS4 proteins are required for centrosom... | KEEP AS NON CORE | Summary: ESCRT-III depletion causes nuclear morphology defects. Reason: Secondary effect of spindle/centrosome defects. Supporting Evidence: PMID:20616062 Human ESCRT-III and VPS4 proteins are required for centrosome and spindle maintenance. |
| GO:1901673 regulation of mitotic spindle assembly | IMP PMID:20616062 Human ESCRT-III and VPS4 proteins are required for centrosom... | KEEP AS NON CORE | Summary: CHMP2A depletion causes spindle defects. Reason: Secondary effect on spindles. Supporting Evidence: PMID:20616062 Human ESCRT-III and VPS4 proteins are required for centrosome and spindle maintenance. |
| GO:1901673 regulation of mitotic spindle assembly | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ESCRT-III role in spindle assembly regulation. Reason: Secondary effect. |
| GO:0010824 regulation of centrosome duplication | IMP PMID:20616062 Human ESCRT-III and VPS4 proteins are required for centrosom... | KEEP AS NON CORE | Summary: ESCRT-III depletion causes centrosome abnormalities. Reason: Non-core function. Supporting Evidence: PMID:20616062 Human ESCRT-III and VPS4 proteins are required for centrosome and spindle maintenance. |
| GO:1903723 negative regulation of centriole elongation | IMP PMID:20616062 Human ESCRT-III and VPS4 proteins are required for centrosom... | KEEP AS NON CORE | Summary: ESCRT-III may regulate centriole elongation. Reason: Indirect effect through centrosome maintenance. Supporting Evidence: PMID:20616062 Human ESCRT-III and VPS4 proteins are required for centrosome and spindle maintenance. |
| GO:0015031 protein transport | IBA GO_REF:0000033 | ACCEPT | Summary: CHMP2A participates in protein transport through MVB-mediated sorting. Reason: Broadly accurate but general. |
| GO:0015031 protein transport | IEA GO_REF:0000043 | ACCEPT | Summary: CHMP2A functions in protein transport. Reason: Broadly accurate. |
| GO:0007034 vacuolar transport | IEA GO_REF:0000002 | ACCEPT | Summary: CHMP2A functions in vacuolar/lysosomal transport. Reason: Core ESCRT-III function. |
| GO:0051469 vesicle fusion with vacuole | NAS PMID:16505166 Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a... | ACCEPT | Summary: ESCRT function required for MVB-lysosome fusion. Reason: Core function. Supporting Evidence: PMID:16505166 Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a conserved VSL region in Vta1. |
| GO:0045184 establishment of protein localization | IMP PMID:23045692 ESCRT-III binding protein MITD1 is involved in cytokinesis a... | KEEP AS NON CORE | Summary: CHMP2A involved in protein localization through MITD1 interaction. Reason: General term - more specific functions captured elsewhere. Supporting Evidence: PMID:23045692 the MIT domain binds to a subset of ESCRT-III subunits and that this interaction mediates MITD1 recruitment to the midbody during cytokinesis |
| GO:0005515 protein binding | IPI PMID:16730941 A systematic analysis of human CHMP protein interactions: ad... | MARK AS OVER ANNOTATED | Summary: CHMP2A interacts with MIT domain-containing proteins. Reason: Generic - specific interaction with MITD1 or VPS4 is more informative. Supporting Evidence: PMID:16730941 two further MIT domain-containing proteins (AMSH/STAMBP and LOC129531) interact with multiple components of the human ESCRT III complex |
| GO:0005515 protein binding | IPI PMID:19525971 Structural basis for ESCRT-III protein autoinhibition. | MARK AS OVER ANNOTATED | Summary: CHMP2A interacts with CHMP3. Reason: Generic - specific ESCRT-III complex membership is more informative. Supporting Evidence: PMID:19525971 Jun 14. Structural basis for ESCRT-III protein autoinhibition. |
| GO:0005515 protein binding | IPI PMID:23051622 ESCRT-III CHMP2A and CHMP3 form variable helical polymers in... | MARK AS OVER ANNOTATED | Summary: CHMP2A interacts with CHMP4B and CHMP3. Reason: Generic - specific ESCRT-III complex membership is more informative. Supporting Evidence: PMID:23051622 ESCRT-III CHMP2A and CHMP3 form variable helical polymers in vitro and act synergistically during HIV-1 budding. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | MARK AS OVER ANNOTATED | Summary: Protein interaction detected. Reason: Generic protein binding term. Supporting Evidence: PMID:25416956 A proteome-scale map of the human interactome network. |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | MARK AS OVER ANNOTATED | Summary: Protein interaction detected. Reason: Generic protein binding term. Supporting Evidence: PMID:26496610 Oct 22. A human interactome in three quantitative dimensions organized by stoichiometries and abundances. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | MARK AS OVER ANNOTATED | Summary: Protein interaction detected. Reason: Generic protein binding term. Supporting Evidence: PMID:28514442 Architecture of the human interactome defines protein communities and disease networks. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | MARK AS OVER ANNOTATED | Summary: Protein interaction detected. Reason: Generic protein binding term. Supporting Evidence: PMID:32296183 Apr 8. A reference map of the human binary protein interactome. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | MARK AS OVER ANNOTATED | Summary: Protein interaction detected. Reason: Generic protein binding term. Supporting Evidence: PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MARK AS OVER ANNOTATED | Summary: Protein interaction detected. Reason: Generic protein binding term. Supporting Evidence: PMID:33961781 2021 May 6. Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | MARK AS OVER ANNOTATED | Summary: Protein interaction detected. Reason: Generic protein binding term. Supporting Evidence: PMID:35271311 2022 Mar 11. OpenCell: Endogenous tagging for the cartography of human cellular organization. |
| GO:0005515 protein binding | IPI PMID:18687924 Helical structures of ESCRT-III are disassembled by VPS4. | MARK AS OVER ANNOTATED | Summary: CHMP2A interacts with CHMP3 and VPS4B. Reason: Generic - specific ESCRT-III polymerization and VPS4 interaction are more informative. Supporting Evidence: PMID:18687924 Aug 7. Helical structures of ESCRT-III are disassembled by VPS4. |
| GO:0005515 protein binding | IPI PMID:18385515 Novel interactions of ESCRT-III with LIP5 and VPS4 and their... | MARK AS OVER ANNOTATED | Summary: Protein interaction detected. Reason: Generic protein binding term. Supporting Evidence: PMID:18385515 Apr 2. Novel interactions of ESCRT-III with LIP5 and VPS4 and their implications for ESCRT-III disassembly. |
| GO:0005515 protein binding | IPI PMID:23105106 Interactions of the human LIP5 regulatory protein with endos... | MARK AS OVER ANNOTATED | Summary: Protein interaction detected. Reason: Generic protein binding term. Supporting Evidence: PMID:23105106 2012 Oct 26. Interactions of the human LIP5 regulatory protein with endosomal sorting complexes required for transport. |
| GO:0005515 protein binding | IPI PMID:14505570 The protein network of HIV budding. | MARK AS OVER ANNOTATED | Summary: CHMP2A interacts with VPS4 and other class E proteins. Reason: Generic - specific domain binding more informative. Supporting Evidence: PMID:14505570 These proteins were connected into a coherent network by 43 different protein-protein interactions |
| GO:0005515 protein binding | IPI PMID:14519844 Divergent retroviral late-budding domains recruit vacuolar p... | MARK AS OVER ANNOTATED | Summary: Protein interaction detected. Reason: Generic protein binding term. Supporting Evidence: PMID:14519844 Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins. |
| GO:0005515 protein binding | IPI PMID:21975012 ESCRT-III subunits Snf7-1 and Snf7-2 differentially regulate... | MARK AS OVER ANNOTATED | Summary: Protein interaction detected. Reason: Generic protein binding term. Supporting Evidence: PMID:21975012 ESCRT-III subunits Snf7-1 and Snf7-2 differentially regulate transmembrane cargos in hESC-derived human neurons. |
| GO:0005515 protein binding | IPI PMID:23045692 ESCRT-III binding protein MITD1 is involved in cytokinesis a... | MARK AS OVER ANNOTATED | Summary: CHMP2A interacts with MITD1. Reason: Generic - specific MIT-MIM domain interaction captured elsewhere. Supporting Evidence: PMID:23045692 ESCRT-III binding protein MITD1 is involved in cytokinesis and has an unanticipated PLD fold that binds membranes. |
| GO:0005515 protein binding | IPI PMID:21543490 Mechanism of inhibition of retrovirus release from cells by ... | MARK AS OVER ANNOTATED | Summary: Protein interaction detected. Reason: Generic protein binding term. Supporting Evidence: PMID:21543490 Mechanism of inhibition of retrovirus release from cells by interferon-induced gene ISG15. |
| GO:0005515 protein binding | IPI PMID:19129480 Essential role of hIST1 in cytokinesis. | MARK AS OVER ANNOTATED | Summary: Protein interaction detected. Reason: Generic protein binding term. Supporting Evidence: PMID:19129480 Jan 7. Essential role of hIST1 in cytokinesis. |
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