Human Gene CHMP2A (ENST00000312547.6) Description and Page Index
Description: Homo sapiens charged multivesicular body protein 2A (CHMP2A), transcript variant 2, mRNA. (from RefSeq NM_014453) RefSeq Summary (NM_014453): CHMP2A belongs to the chromatin-modifying protein/charged multivesicular body protein (CHMP) family. These proteins are components of ESCRT-III (endosomal sorting complex required for transport III), a complex involved in degradation of surface receptor proteins and formation of endocytic multivesicular bodies (MVBs). Some CHMPs have both nuclear and cytoplasmic/vesicular distributions, and one such CHMP, CHMP1A (MIM 164010), is required for both MVB formation and regulation of cell cycle progression (Tsang et al., 2006 [PubMed 16730941]).[supplied by OMIM, Mar 2008]. Gencode Transcript: ENST00000312547.6 Gencode Gene: ENSG00000130724.8 Transcript (Including UTRs) Position: hg38 chr19:58,551,566-58,555,124 Size: 3,559 Total Exon Count: 6 Strand: - Coding Region Position: hg38 chr19:58,551,649-58,554,212 Size: 2,564 Coding Exon Count: 5
ID:CHM2A_HUMAN DESCRIPTION: RecName: Full=Charged multivesicular body protein 2a; AltName: Full=Chromatin-modifying protein 2a; Short=CHMP2a; AltName: Full=Putative breast adenocarcinoma marker BC-2; AltName: Full=Vacuolar protein sorting-associated protein 2-1; Short=Vps2-1; Short=hVps2-1; 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. Involved in HIV- 1 p6- and p9-dependent virus release. SUBUNIT: 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. In vitro, heteromerizes with CHMP3 (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. Interacts with CHMP1B, CHMP2B, CHMP3, CHMP4A, CHMP4B, CHMP4C and CHMP5. Interacts with VPS4A; the interaction is direct. Interacts with VPS4B; the interaction is direct. Interacts with MITD1. Interacts with VTA1; the interaction probably involves the open conformation of CHMP2A. INTERACTION: Q8NF50-2:DOCK8; NbExp=3; IntAct=EBI-2692789, EBI-10174653; SUBCELLULAR LOCATION: Late endosome membrane ; Peripheral membrane protein ytoplasmic side Note=Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Fleming body. DOMAIN: The acidic C-terminus and the basic N-termminus are thought to render the protein in a closed, soluble and inactive conformation through an autoinhibitory intramolecular interaction. The open and active conformation, which enables membrane binding and oligomerization, is achieved by interaction with other cellular binding partners, probably including other ESCRT components. PTM: ISGylated in a CHMP5-dependent manner. Isgylation weakens and inhibits its interactions with VPS4A and VTA1 respectively. MISCELLANEOUS: Its overexpression strongly inhibits HIV-1 release. SIMILARITY: Belongs to the SNF7 family.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on O43633
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Gene Ontology (GO) Annotations with Structured Vocabulary
Molecular Function: GO:0005515 protein binding GO:0019904 protein domain specific binding
Biological Process: GO:0000920 cytokinetic cell separation GO:0006810 transport GO:0006997 nucleus organization GO:0007034 vacuolar transport GO:0007080 mitotic metaphase plate congression GO:0010824 regulation of centrosome duplication GO:0015031 protein transport GO:0016032 viral process GO:0016197 endosomal transport GO:0019058 viral life cycle GO:0039702 viral budding via host ESCRT complex GO:0045184 establishment of protein localization GO:0050792 regulation of viral process GO:0060548 negative regulation of cell death GO:0061024 membrane organization GO:1901673 regulation of spindle assembly involved in mitosis GO:1902188 positive regulation of viral release from host cell GO:1903543 positive regulation of exosomal secretion GO:1903723 negative regulation of centriole elongation
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