Four and a half LIM domains 3 | |||||||||||||
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PDB rendering based on 1wyh. |
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Identifiers | |||||||||||||
Symbols | FHL3 ; SLIM2 | ||||||||||||
External IDs | OMIM: 602790 MGI: 1341092 HomoloGene: 37928 GeneCards: FHL3 Gene | ||||||||||||
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RNA expression pattern | |||||||||||||
More reference expression data | |||||||||||||
Orthologs | |||||||||||||
Species | Human | Mouse | |||||||||||
Entrez | 2275 | 14201 | |||||||||||
Ensembl | ENSG00000183386 | ENSMUSG00000032643 | |||||||||||
UniProt | Q13643 | Q9R059 | |||||||||||
RefSeq (mRNA) | NM_001243878 | NM_010213 | |||||||||||
RefSeq (protein) | NP_001230807 | NP_034343 | |||||||||||
Location (UCSC) | Chr 1: 38.46 – 38.47 Mb |
Chr 4: 124.7 – 124.71 Mb |
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PubMed search | [1] | [2] | |||||||||||
Four and a half LIM domains protein 3 is a protein that in humans is encoded by the FHL3 gene.[1][2][3]
LIM proteins are defined by the possession of a highly conserved double zinc finger motif called the LIM domain.[supplied by OMIM][3]
Interactions
FHL3 has been shown to interact with:
References
- ^ Morgan MJ, Madgwick AJ (October 1996). "Slim defines a novel family of LIM-proteins expressed in skeletal muscle". Biochem Biophys Res Commun 225 (2): 632–8. doi:10.1006/bbrc.1996.1222. PMID 8753811.
- ^ Lee SM, Tsui SK, Chan KK, Kotaka M, Li HY, Chim SS et al. (May 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. doi:10.1023/B:SCAM.0000007122.03392.4b. PMID 10226657.
- ^ a b "Entrez Gene: FHL3 four and a half LIM domains 3".
- ^ a b Fimia GM, De Cesare D, Sassone-Corsi P (November 2000). "A family of LIM-only transcriptional coactivators: tissue-specific expression and selective activation of CREB and CREM". Mol. Cell. Biol. 20 (22): 8613–22. doi:10.1128/mcb.20.22.8613-8622.2000. PMC 102166. PMID 11046156.
- ^ a b Turner J, Nicholas H, Bishop D, Matthews JM, Crossley M (April 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:10.1074/jbc.M300587200. PMID 12556451.
- ^ Li HY, Ng EK, Lee SM, Kotaka M, Tsui SK, Lee CY et al. "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. doi:10.1002/1097-4644(20010301)80:3<293::aid-jcb10>3.3.co;2-l. PMID 11135358.
- ^ Samson T, Smyth N, Janetzky S, Wendler O, Müller JM, Schüle R et al. (July 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:10.1074/jbc.M312894200. PMID 15117962.
Further reading
- 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:10.1006/bbrc.1999.0179. PMID 10049693.
- Li HY, Ng EK, Lee SM, Kotaka M, Tsui SK, Lee CY 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. doi:10.1002/1097-4644(20010301)80:3<293::AID-JCB10>3.0.CO;2-U. PMID 11135358.
- Turner J, Nicholas H, Bishop D, Matthews JM, Crossley M (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:10.1074/jbc.M300587200. PMID 12556451.
- Mils V, Lee SM, Joly W, Hang EW, Baldin V, Waye MM et al. (2003). "LIM-only protein FHL3 interacts with CDC25B2 phosphatase.". Exp. Cell Res. 285 (1): 99–106. doi:10.1016/S0014-4827(03)00018-1. PMID 12681290.
- Coghill ID, Brown S, Cottle DL, McGrath MJ, Robinson PA, Nandurkar HH 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:10.1074/jbc.M213259200. PMID 12704194.
- Purcell NH, Darwis D, Bueno OF, Müller JM, Schüle R, Molkentin JD (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. doi:10.1128/MCB.24.3.1081-1095.2004. PMC 321437. PMID 14729955.
- Samson T, Smyth N, Janetzky S, Wendler O, Müller JM, Schüle R 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:10.1074/jbc.M312894200. 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:10.1042/BJ20040775. PMC 1134781. PMID 15453830.
- Philippar U, Schratt G, Dieterich C, Müller JM, Galgóczy P, Engel FB et al. (2005). "The SRF target gene Fhl2 antagonizes RhoA/MAL-dependent activation of SRF.". Mol. Cell 16 (6): 867–80. doi:10.1016/j.molcel.2004.11.039. PMID 15610731.
- Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N 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.
- Cottle DL, McGrath MJ, Cowling BS, Coghill ID, Brown S, Mitchell CA (2007). "FHL3 binds MyoD and negatively regulates myotube formation.". J. Cell. Sci. 120 (Pt 8): 1423–35. doi:10.1242/jcs.004739. PMID 17389685.
External links
- FHL3 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
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This article incorporates text from the United States National Library of Medicine, which is in the public domain.