Charged multivesicular body protein 3 (Protein name
), CHMP3_HUMAN from NCBI database.
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General Annotation
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Gene name:
VPS24(CGI-149;CGI-149;CHMP3;NEDF;VPS24);
Protein name:
Charged multivesicular body protein 3;
Alternative:
Neuroendocrine differentiation factor;Chromatin-modifying protein 3;Vacuolar protein sorting-associated protein 24(hVps24);
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
Probable core component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentally. Forms a metastable monomer in solution; its core structure (without part of the putative autoinhibitory C-terminal acidic region) oligomerizes into a flat lattice via two different dimerization interfaces. In vitro, heteromerizes with CHMP2A (but not CHMP4) to form helical tubular structures that expose membrane-interacting sites on the outside whereas VPS4B can associate on the inside of the tubule. May interact with IGFBP7; the relevance of such interaction however remains unclear. Interacts with CHMP2A. Interacts with CHMP4A; the interaction requires the release of CHMP4A autoinhibition. Interacts with VPS4A. Interacts with STAMBP; the interaction appears to relieve the autoinhibition of CHMP3.
Function:
Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Selectively binds to phosphatidylinositol 3,5-bisphosphate PtdIns(3,5)P2 and PtdIns(3,4)P2 in preference to other phosphoinositides tested. Involved in late stages of cytokinesis. Required for sorting/trafficking of EGF receptor.
Subcellular Location:
Cytoplasm
cytosol
Membrane
Lipid-anchor
Endosome
Late endosome membrane
Localizes to the midbody of dividing cells.
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);POSSIBLE INTERACTION WITH IGFBP7
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);FUNCTION;SUBCELLULAR LOCATION
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2);FUNCTION
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3)
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)
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Cited for: FUNCTION IN HIV-1 BUDDING;INTERACTION WITH CHMP4A
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Cited for: AUTOINHIBITORY MECHANISM;INTRAMOLECULAR INTERACTION;INTERACTION WITH STAMBP AND VPS4A;MUTAGENESIS OF 216-ARG-LEU-217; 221-ARG-SER-222 AND SER-222
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Cited for: INTERACTION WITH STAMBP;IDENTIFICATION BY MASS SPECTROMETRY
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Cited for: AUTOINHIBITORY MECHANISM;INTERACTION WITH CHMP4A;MUTAGENESIS OF 179-LYS--SER-222
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: AUTOINHIBITORY MECHANISM;INTERACTION WITH STAMBP
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 5-183;SUBUNIT;FUNCTION IN HIV-1 BUDDING;MUTAGENESIS OF 24-ARG-LYS-25; ARG-28; LYS-54; GLN-56; VAL-59; 62-VAL-LEU-63 AND 78-TYR-ALA-79
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Cited for: X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) OF 1-222;INTERACTION WITH CHMP2A;MUTAGENESIS OF VAL-48; VAL-59; VAL-62; ALA-64 AND 168-ILE-LEU-169
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Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 183-222 IN COMPLEX WITH STAMBP FRAGMENT