CHMP5

Charged multivesicular body protein 5 is a protein that in humans is encoded by the CHMP5 gene.[5][6][7]

CHMP5
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2LXM, 3ULY, 3UM0, 3UM1, 3UM2, 4TXR
Identifiers
Aliases	CHMP5, C9orf83, HSPC177, PNAS-2, SNF7DC2, Vps60, CGI-34, charged multivesicular body protein 5
External IDs	OMIM: 610900 MGI: 1924209 HomoloGene: 5757 GeneCards: CHMP5
Gene location (Human) Chr. Chromosome 9 (human)[1] Band 9p13.3 Start 33,264,879 bp[1] End 33,282,070 bp[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4|4 A5 Start 40,948,407 bp[2] End 40,965,303 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0001948 protein binding • cadherin binding Cellular component • cytoplasm • cytosol • endosome • membrane • endosome membrane • extracellular exosome • cell nucleus Biological process • regulation of centrosome duplication • GO:0019067 viral life cycle • nucleus organization • multivesicular body sorting pathway • endosome to lysosome transport • multivesicular body assembly • regulation of mitotic spindle assembly • endosomal transport • protein transport • cell separation after cytokinesis • mitotic metaphase plate congression • regulation of receptor recycling • lysosome organization • vacuolar transport • ESCRT III complex disassembly • transport • midbody abscission • cellular response to lipopolysaccharide • cellular response to muramyl dipeptide Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	51510	76959
Ensembl	ENSG00000086065	ENSMUSG00000028419
UniProt	Q9NZZ3	Q9D7S9
RefSeq (mRNA)	NM_016410 NM_001195536	NM_029814
RefSeq (protein)	NP_001182465 NP_057494	NP_084090
Location (UCSC)	Chr 9: 33.26 – 33.28 Mb	Chr 4: 40.95 – 40.97 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

CHMP5 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, is required for both MVB formation and regulation of cell cycle progression.[7][8]

References

1. GRCh38: Ensembl release 89: ENSG00000086065 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000028419 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Ward DM, Vaughn MB, Shiflett SL, White PL, Pollock AL, Hill J, Schnegelberger R, Sundquist WI, Kaplan J (Mar 2005). "The role of LIP5 and CHMP5 in multivesicular body formation and HIV-1 budding in mammalian cells". J Biol Chem. 280 (11): 10548–55. doi:10.1074/jbc.M413734200. PMID 15644320.
6. Howard TL, Stauffer DR, Degnin CR, Hollenberg SM (Sep 2001). "CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins". J Cell Sci. 114 (Pt 13): 2395–404. PMID 11559748.
7. "Entrez Gene: CHMP5 chromatin modifying protein 5".
8. Tsang HT, Connell JW, Brown SE, Thompson A, Reid E, Sanderson CM (September 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.

External links

• Human CHMP5 genome location and CHMP5 gene details page in the UCSC Genome Browser.

Further reading

• Lai CH, Chou CY, Ch'ang LY, et al. (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.
• Zhang QH, Ye M, Wu XY, et al. (2001). "Cloning and Functional Analysis of cDNAs with Open Reading Frames for 300 Previously Undefined Genes Expressed in CD34+ Hematopoietic Stem/Progenitor Cells". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Strack B, Calistri A, Craig S, et al. (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.
• von Schwedler UK, Stuchell M, Müller B, et al. (2003). "The protein network of HIV budding". Cell. 114 (6): 701–13. doi:10.1016/S0092-8674(03)00714-1. PMID 14505570.
• Martin-Serrano J, Yarovoy A, Perez-Caballero D, et al. (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. doi:10.1073/pnas.2133846100. PMC 218772. PMID 14519844.
• Humphray SJ, Oliver K, Hunt AR, et al. (2004). "DNA sequence and analysis of human chromosome 9". Nature. 429 (6990): 369–74. doi:10.1038/nature02465. PMC 2734081. PMID 15164053.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.