VPS24

CHMP3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2XZE, 3FRT, 3FRV, 2GD5
Identifiers
Aliases	CHMP3, NEDF, VPS24, CGI-149, charged multivesicular body protein 3
External IDs	OMIM: 610052 MGI: 1913950 HomoloGene: 6368 GeneCards: CHMP3
Gene location (Human) Chr. Chromosome 2 (human) Band 2p11.2 Start 86,503,430 bp End 86,563,479 bp
Gene location (Mouse) Chr. Chromosome 6 (mouse) Band 6 C1|6 32.17 cM Start 71,520,781 bp End 71,559,593 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon secondary oocyte cerebellar vermis nipple urethra saphenous vein parotid gland rectum spongy bone right ventricle Top expressed in seminal vesicula superior frontal gyrus spermatocyte lip esophagus yolk sac duodenum saccule spermatid cerebellar cortex More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding phosphatidylcholine binding protein homodimerization activity ubiquitin-specific protease binding identical protein binding Cellular component cytoplasm membrane plasma membrane endosome late endosome membrane extracellular exosome ESCRT III complex cytosol intracellular anatomical structure late endosome cytoplasmic vesicle multivesicular body Biological process autophagosome maturation viral life cycle protein polymerization multivesicular body assembly cell cycle cell division regulation of mitotic spindle assembly endosomal transport regulation of centrosome duplication apoptotic process protein heterooligomerization vacuolar transport septum digestion after cytokinesis protein transport nucleus organization mitotic metaphase plate congression multivesicular body sorting pathway regulation of exosomal secretion macroautophagy multivesicular body-lysosome fusion regulation of early endosome to late endosome transport transport viral budding via host ESCRT complex endosome transport via multivesicular body sorting pathway late endosome to vacuole transport midbody abscission Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 51652 66700 Ensembl ENSG00000115561 ENSMUSG00000053119 UniProt Q9Y3E7 Q9CQ10 RefSeq (mRNA) NM_001005753 NM_001193517 NM_016079 NM_025783 NM_001355674 NM_001355675 NM_001361405 RefSeq (protein) NP_001005753 NP_001180446 NP_057163 NP_080059 NP_001342603 NP_001342604 NP_001348334 Location (UCSC) Chr 2: 86.5 – 86.56 Mb Chr 6: 71.52 – 71.56 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Charged multivesicular body protein 3 is a protein that in humans is encoded by the VPS24 gene.

Function

This gene encodes a protein that acts in the sorting of transmembrane proteins into lysosomes/vacuoles via the multivesicular body (MVB) pathway. This protein, along with other soluble coiled-coil containing proteins, forms part of the ESCRT-III protein complex that binds to the endosomal membrane and recruits additional cofactors for protein sorting into the MVB. This protein may also co-immunoprecipitate with a member of the IFG-binding protein superfamily. Alternative splicing results in multiple transcript variants encoding different isoforms.

Interactions

VPS24 has been shown to interact with IGFBP7.

Further reading

• Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W (2000). "Identification of Novel Human Genes Evolutionarily Conserved in Caenorhabditis elegans by Comparative Proteomics". Genome Res. 10 (5): 703–13. doi:10.1101/gr.10.5.703. PMC 310876. PMID 10810093.
• Babst M, Katzmann DJ, Estepa-Sabal EJ, Meerloo T, Emr SD (2002). "Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting". Dev. Cell. 3 (2): 271–82. doi:10.1016/S1534-5807(02)00220-4. PMID 12194857.
• Su ZZ, Kang DC, Chen Y, Pekarskaya O, Chao W, Volsky DJ, Fisher PB (2003). "Identification of gene products suppressed by human immunodeficiency virus type 1 infection or gp120 exposure of primary human astrocytes by rapid subtraction hybridization". J. Neurovirol. 9 (3): 372–89. doi:10.1080/13550280390201263. PMID 12775420. S2CID 12205568.
• Strack B, Calistri A, Craig S, Popova E, Göttlinger HG (2003). "AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding". Cell. 114 (6): 689–99. doi:10.1016/S0092-8674(03)00653-6. PMID 14505569. S2CID 10733770.
• von Schwedler UK, Stuchell M, Müller B, Ward DM, Chung HY, Morita E, Wang HE, Davis T, He GP, Cimbora DM, Scott A, Kräusslich HG, Kaplan J, Morham SG, Sundquist WI (2003). "The protein network of HIV budding". Cell. 114 (6): 701–13. doi:10.1016/S0092-8674(03)00714-1. PMID 14505570. S2CID 16894972.
• Martin-Serrano J, Yarovoy A, Perez-Caballero D, Bieniasz PD, Yaravoy A (2003). "Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins". Proc. Natl. Acad. Sci. U.S.A. 100 (21): 12414–9. Bibcode:2003PNAS..10012414M. doi:10.1073/pnas.2133846100. PMC 218772. PMID 14519844.
• Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (2004). "Functional Proteomics Mapping of a Human Signaling Pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
• Lin Y, Kimpler LA, Naismith TV, Lauer JM, Hanson PI (2005). "Interaction of the mammalian endosomal sorting complex required for transport (ESCRT) III protein hSnf7-1 with itself, membranes, and the AAA+ ATPase SKD1". J. Biol. Chem. 280 (13): 12799–809. doi:10.1074/jbc.M413968200. PMID 15632132.
• Yan Q, Hunt PR, Frelin L, Vida TA, Pevsner J, Bean AJ (2005). "mVps24p functions in EGF receptor sorting/trafficking from the early endosome". Exp. Cell Res. 304 (1): 265–73. doi:10.1016/j.yexcr.2004.11.003. PMID 15707591.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Walker GE, Antoniono RJ, Ross HJ, Paisley TE, Oh Y (2006). "Neuroendocrine-like differentiation of non-small cell lung carcinoma cells: regulation by cAMP and the interaction of mac25/IGFBP-rP1 and 25.1". Oncogene. 25 (13): 1943–54. doi:10.1038/sj.onc.1209213. PMID 16302002.
• Bache KG, Stuffers S, Malerød L, Slagsvold T, Raiborg C, Lechardeur D, Wälchli S, Lukacs GL, Brech A, Stenmark H (2006). "The ESCRT-III Subunit hVps24 Is Required for Degradation but Not Silencing of the Epidermal Growth Factor Receptor". Mol. Biol. Cell. 17 (6): 2513–23. doi:10.1091/mbc.E05-10-0915. PMC 1474783. PMID 16554368.
• Tsang HT, Connell JW, Brown SE, Thompson A, Reid E, Sanderson CM (2006). "A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex". Genomics. 88 (3): 333–46. doi:10.1016/j.ygeno.2006.04.003. PMID 16730941.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.
• Zamborlini A, Usami Y, Radoshitzky SR, Popova E, Palu G, Göttlinger H (2007). "Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding". Proc. Natl. Acad. Sci. U.S.A. 103 (50): 19140–5. doi:10.1073/pnas.0603788103. PMC 1748189. PMID 17146056.