CHMP1B
Charged multivesicular body protein 1b is a protein that in humans is encoded by the CHMP1B gene.[1][2]
References
- ↑ Reid E, Connell J, Edwards TL, Duley S, Brown SE, Sanderson CM (Dec 2004). “The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B”. Hum Mol Genet. 14 (1): 19–38. doi:10.1093/hmg/ddi003. PMID 15537668.
- ↑ “Entrez Gene: CHMP1B chromatin modifying protein 1B”.
External links
- Human C10orf2 genome location and C10orf2 gene details page in the UCSC Genome Browser.
- Human CHMP1B genome location and CHMP1B gene details page in the UCSC Genome Browser.
Further reading
- Vuoristo JT, Berrettini WH, Ala-Kokko L (2001). “C18orf2, a novel, highly conserved intronless gene within intron 5 of the GNAL gene on chromosome 18p11”. Cytogenet. Cell Genet. 93 (1–2): 19–22. doi:10.1159/000056940. PMID 11474171.
- Stauffer DR, Howard TL, Nyun T, Hollenberg SM (2002). “CHMP1 is a novel nuclear matrix protein affecting chromatin structure and cell-cycle progression”. J. Cell Sci. 114 (Pt 13): 2383–93. PMID 11559747.
- Howard TL, Stauffer DR, Degnin CR, Hollenberg SM (2002). “CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins”. J. Cell Sci. 114 (Pt 13): 2395–404. PMID 11559748.
- 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.
- 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.
- Scott A, Gaspar J, Stuchell-Brereton MD, et al. (2005). “Structure and ESCRT-III protein interactions of the MIT domain of human VPS4A”. Proc. Natl. Acad. Sci. U.S.A. 102 (39): 13813–8. doi:10.1073/pnas.0502165102. PMC 1236530. PMID 16174732.
- Tsang HT, Connell JW, Brown SE, et al. (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.
- Row PE, Liu H, Hayes S, et al. (2007). “The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation”. J. Biol. Chem. 282 (42): 30929–37. doi:10.1074/jbc.M704009200. PMID 17711858.
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