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Four and a half LIM domains 3

PDB rendering based on 1wyh.
Available structures
1wyh, 2cuq
Identifiers
Symbols FHL3; MGC19547; MGC23614; MGC8696; SLIM2
External IDs OMIM602790 MGI1341092 HomoloGene37928 GeneCards: FHL3 Gene
RNA expression pattern
PBB GE FHL3 218818 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 2275 14201
Ensembl ENSG00000183386 n/a
UniProt Q13643 n/a
RefSeq (mRNA) NM_004468 XM_906783
RefSeq (protein) NP_004459 XP_911876
Location (UCSC) Chr 1:
38.24 - 38.24 Mb
n/a
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]

Contents

Interactions

FHL3 has been shown to interact with FHL2,[4][5] CTBP2,[6] KLF3,[6] ITGA7[7] and CREB1.[4]

References

  1. ^ Morgan MJ, Madgwick AJ (Oct 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.  
  2. ^ Lee SM, Tsui SK, Chan KK, Kotaka M, Li HY, Chim SS, Waye MM, Fung KP, Lee CY (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. PMID 10226657.  
  3. ^ a b "Entrez Gene: FHL3 four and a half LIM domains 3". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2275.  
  4. ^ a b Fimia, G M; De Cesare D, Sassone-Corsi P (Nov. 2000). "A family of LIM-only transcriptional coactivators: tissue-specific expression and selective activation of CREB and CREM". Mol. Cell. Biol. (UNITED STATES) 20 (22): 8613–22. ISSN 0270-7306. PMID 11046156.  
  5. ^ Li, H Y; Ng E K, Lee S M, Kotaka M, Tsui S K, Lee C Y, Fung K P, Waye M M (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. (United States) 80 (3): 293–303. ISSN 0730-2312. PMID 11135358.  
  6. ^ a b Turner, Jeremy; Nicholas Hannah, Bishop David, Matthews Jacqueline M, Crossley Merlin (Apr. 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. (United States) 278 (15): 12786–95. doi:10.1074/jbc.M300587200. ISSN 0021-9258. PMID 12556451.  
  7. ^ Samson, Thomas; Smyth Neil, Janetzky Stefanie, Wendler Olaf, Müller Judith M, Schüle Roland, von der Mark Helga, von der Mark Klaus, Wixler Viktor (Jul. 2004). "The LIM-only proteins FHL2 and FHL3 interact with alpha- and beta-subunits of the muscle alpha7beta1 integrin receptor". J. Biol. Chem. (United States) 279 (27): 28641–52. doi:10.1074/jbc.M312894200. ISSN 0021-9258. 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, 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.  
  • 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. 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:10.1074/jbc.M300587200. 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. doi:10.1016/S0014-4827(03)00018-1. 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:10.1074/jbc.M213259200. 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. doi:10.1128/MCB.24.3.1081-1095.2004. 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: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. 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:10.1016/j.molcel.2004.11.039. 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:10.1038/nature04209. 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:10.1242/jcs.004739. PMID 17389685.  

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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