FERMT2
Fermitin family homolog 2 (FERMT2) also known as pleckstrin homology domain-containing family C member 1 (PLEKHC1) is a protein that in humans is encoded by the FERMT2 gene.[1][2][3]
Function
FERMT2 is a component of extracellular matrix structures in mammalian cells and is required for proper control of cell shape change.[4]
Interactions
FERMT2 has been shown to interact with FBLIM1.[4]
External links
References
- ^ Wick M, Bürger C, Brüsselbach S, Lucibello FC, Müller R (January 1994). "Identification of serum-inducible genes: different patterns of gene regulation during G0-->S and G1-->S progression". J. Cell. Sci. 107 ( Pt 1): 227–39. PMID 8175911. http://jcs.biologists.org/cgi/content/abstract/107/1/227.
- ^ Weinstein EJ, Bourner M, Head R, Zakeri H, Bauer C, Mazzarella R (April 2003). "URP1: a member of a novel family of PH and FERM domain-containing membrane-associated proteins is significantly over-expressed in lung and colon carcinomas". Biochim. Biophys. Acta 1637 (3): 207–16. doi:10.1016/S0925-4439(03)00035-8. PMID 12697302.
- ^ "Entrez Gene: FERMT2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10979.
- ^ a b Tu Y, Wu S, Shi X, Chen K, Wu C (April 2003). "Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation". Cell 113 (1): 37–47. doi:10.1016/S0092-8674(03)00163-6. PMID 12679033.
Further reading
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Heilig R, Eckenberg R, Petit JL, et al. (2003). "The DNA sequence and analysis of human chromosome 14.". Nature 421 (6923): 601–7. doi:10.1038/nature01348. PMID 12508121.
- Tu Y, Wu S, Shi X, et al. (2003). "Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation.". Cell 113 (1): 37–47. doi:10.1016/S0092-8674(03)00163-6. PMID 12679033.
- Siegel DH, Ashton GH, Penagos HG, et al. (2003). "Loss of kindlin-1, a human homolog of the Caenorhabditis elegans actin-extracellular-matrix linker protein UNC-112, causes Kindler syndrome.". Am. J. Hum. Genet. 73 (1): 174–87. doi:10.1086/376609. PMC 1180579. PMID 12789646. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1180579.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Kato K, Shiozawa T, Mitsushita J, et al. (2004). "Expression of the mitogen-inducible gene-2 (mig-2) is elevated in human uterine leiomyomas but not in leiomyosarcomas.". Hum. Pathol. 35 (1): 55–60. doi:10.1016/j.humpath.2003.08.019. PMID 14745725.
- 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
- 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.
- Olsen JV, Blagoev B, Gnad F, et al. (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.