FHL3
From Wikipedia, the free encyclopedia
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Four and a half LIM domains 3
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| PDB rendering based on 1wyh. | ||||||||||||||
| Available structures: 1wyh, 2cuq | ||||||||||||||
| Identifiers | ||||||||||||||
| Symbol(s) | FHL3; MGC19547; MGC23614; MGC8696; SLIM2 | |||||||||||||
| External IDs | OMIM: 602790 MGI: 1341092 HomoloGene: 37928 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
| Orthologs | ||||||||||||||
| Human | Mouse | |||||||||||||
| Entrez | 2275 | 14201 | ||||||||||||
| Ensembl | ENSG00000183386 | n/a | ||||||||||||
| Uniprot | Q13643 | n/a | ||||||||||||
| Refseq | NM_004468 (mRNA) NP_004459 (protein) |
XM_906783 (mRNA) XP_911876 (protein) |
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| Location | Chr 1: 38.24 - 38.24 Mb | n/a | ||||||||||||
| Pubmed search | [1] | [2] | ||||||||||||
Four and a half LIM domains 3, also known as FHL3, is a human gene.[1]
LIM proteins are defined by the possession of a highly conserved double zinc finger motif called the LIM domain.[supplied by OMIM][1]
[edit] References
[edit] Further reading
- Morgan MJ, Madgwick AJ (1996). "Slim defines a novel family of LIM-proteins expressed in skeletal muscle.". Biochem. Biophys. Res. Commun. 225 (2): 632-8. doi:. PMID 8753811.
- Morgan MJ, Madgwick AJ (1999). "The LIM proteins FHL1 and FHL3 are expressed differently in skeletal muscle.". Biochem. Biophys. Res. Commun. 255 (2): 245-50. doi:. PMID 10049693.
- Lee SM, Tsui SK, Chan KK, et al. (1999). "Chromosomal mapping of a skeletal muscle specific LIM-only protein FHL3 to the distal end of the short arm of human chromosome 1.". Somat. Cell Mol. Genet. 24 (3): 197-202. PMID 10226657.
- Li HY, Ng EK, Lee SM, et al. (2001). "Protein-protein interaction of FHL3 with FHL2 and visualization of their interaction by green fluorescent proteins (GFP) two-fusion fluorescence resonance energy transfer (FRET).". J. Cell. Biochem. 80 (3): 293-303. PMID 11135358.
- 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:. PMID 12477932.
- Turner J, Nicholas H, Bishop D, et al. (2003). "The LIM protein FHL3 binds basic Krüppel-like factor/Krüppel-like factor 3 and its co-repressor C-terminal-binding protein 2.". J. Biol. Chem. 278 (15): 12786-95. doi:. PMID 12556451.
- Mils V, Lee SM, Joly W, et al. (2003). "LIM-only protein FHL3 interacts with CDC25B2 phosphatase.". Exp. Cell Res. 285 (1): 99-106. PMID 12681290.
- Coghill ID, Brown S, Cottle DL, et al. (2003). "FHL3 is an actin-binding protein that regulates alpha-actinin-mediated actin bundling: FHL3 localizes to actin stress fibers and enhances cell spreading and stress fiber disassembly.". J. Biol. Chem. 278 (26): 24139-52. doi:. PMID 12704194.
- Purcell NH, Darwis D, Bueno OF, et al. (2004). "Extracellular signal-regulated kinase 2 interacts with and is negatively regulated by the LIM-only protein FHL2 in cardiomyocytes.". Mol. Cell. Biol. 24 (3): 1081-95. PMID 14729955.
- Samson T, Smyth N, Janetzky S, et al. (2004). "The LIM-only proteins FHL2 and FHL3 interact with alpha- and beta-subunits of the muscle alpha7beta1 integrin receptor.". J. Biol. Chem. 279 (27): 28641-52. doi:. PMID 15117962.
- Takahashi K, Matsumoto C, Ra C (2005). "FHL3 negatively regulates human high-affinity IgE receptor beta-chain gene expression by acting as a transcriptional co-repressor of MZF-1.". Biochem. J. 386 (Pt 1): 191-200. doi:. PMID 15453830.
- Philippar U, Schratt G, Dieterich C, et al. (2005). "The SRF target gene Fhl2 antagonizes RhoA/MAL-dependent activation of SRF.". Mol. Cell 16 (6): 867-80. doi:. PMID 15610731.
- 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:. PMID 16189514.
- Cottle DL, McGrath MJ, Cowling BS, et al. (2007). "FHL3 binds MyoD and negatively regulates myotube formation.". J. Cell. Sci. 120 (Pt 8): 1423-35. doi:. PMID 17389685.
[edit] External links
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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