CHMP1A
Charged multivesicular body protein 1a is a protein that in humans is encoded by the CHMP1A gene.[1][2][3]
Function
This gene encodes a member of the CHMP/Chmp family of proteins which are involved in multivesicular body sorting of proteins to the interiors of lysosomes. The initial prediction of the protein sequence encoded by this gene suggested that the encoded protein was a metallopeptidase. The nomenclature has been updated recently to reflect the correct biological function of this encoded protein.[3]
Interactions
CHMP1A has been shown to interact with VPS4A.[1]
References
- ↑ 1.0 1.1 Howard TL, Stauffer DR, Degnin CR, Hollenberg SM (Jul 2001). "CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins". Journal of Cell Science 114 (Pt 13): 2395–404. PMID 11559748.
- ↑ Stauffer DR, Howard TL, Nyun T, Hollenberg SM (Jul 2001). "CHMP1 is a novel nuclear matrix protein affecting chromatin structure and cell-cycle progression". Journal of Cell Science 114 (Pt 13): 2383–93. PMID 11559747.
- ↑ 3.0 3.1 "Entrez Gene: PCOLN3 procollagen (type III) N-endopeptidase".
Further reading
- Nomura N, Nagase T, Miyajima N, Sazuka T, Tanaka A, Sato S et al. (1995). "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1". DNA Research 1 (5): 223–9. doi:10.1093/dnares/1.5.223. PMID 7584044.
- Scott IC, Halila R, Jenkins JM, Mehan S, Apostolou S, Winqvist R et al. (Sep 1996). "Molecular cloning, expression and chromosomal localization of a human gene encoding a 33 kDa putative metallopeptidase (PRSM1)". Gene 174 (1): 135–43. doi:10.1016/0378-1119(96)00510-0. PMID 8863740.
- Yoshida H, Haze K, Yanagi H, Yura T, Mori K (Dec 1998). "Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors". The Journal of Biological Chemistry 273 (50): 33741–9. doi:10.1074/jbc.273.50.33741. PMID 9837962.
- Tong WY, Nagano-Fujii M, Hidajat R, Deng L, Takigawa Y, Hotta H (Dec 2002). "Physical interaction between hepatitis C virus NS4B protein and CREB-RP/ATF6beta". Biochemical and Biophysical Research Communications 299 (3): 366–72. doi:10.1016/S0006-291X(02)02638-4. PMID 12445808.
- Strack B, Calistri A, Craig S, Popova E, Göttlinger HG (Sep 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. Vancouver style error (help)
- von Schwedler UK, Stuchell M, Müller B, Ward DM, Chung HY, Morita E et al. (Sep 2003). "The protein network of HIV budding". Cell 114 (6): 701–13. doi:10.1016/S0092-8674(03)00714-1. PMID 14505570. Vancouver style error (help)
- Martin-Serrano J, Yarovoy A, Perez-Caballero D, Bieniasz PD, Yaravoy A (Oct 2003). "Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins". Proceedings of the National Academy of Sciences of the United States of America 100 (21): 12414–9. doi:10.1073/pnas.2133846100. PMC 218772. PMID 14519844.
- Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
- Row PE, Liu H, Hayes S, Welchman R, Charalabous P, Hofmann K et al. (Oct 2007). "The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation". The Journal of Biological Chemistry 282 (42): 30929–37. doi:10.1074/jbc.M704009200. PMID 17711858.