World Library  
Flag as Inappropriate
Email this Article


Article Id: WHEBN0014156018
Reproduction Date:

Title: Fhl2  
Author: World Heritage Encyclopedia
Language: English
Subject: ZNF638, FHL3, CREB1, EIF6, CD29
Publisher: World Heritage Encyclopedia


Four and a half LIM domains 2

PDB rendering based on 1x4k.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols  ; AAG11; DRAL; FHL-2; SLIM-3; SLIM3
External IDs GeneCards:
RNA expression pattern
Species Human Mouse
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

Four and a half LIM domains protein 2 is a protein that in humans is encoded by the FHL2 gene.[1] LIM proteins contain a highly conserved double zinc finger motif called the LIM domain.[supplied by OMIM][2]


FHL2 has been shown to interact with Beta-catenin,[3] Titin,[4] Zinc finger and BTB domain-containing protein 16,[5] Integrin, beta 6,[6] Androgen receptor,[7] ITGA7,[8] CREB1,[9] MAPK1,[10] CD49c,[6] ZNF638,[11] BRCA1,[12][13] FHL3,[9][14] IGFBP5,[15] TRAF6,[16] EIF6,[6] CD18,[6] CD29[6] and PSEN2.[17]


  1. ^ 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.  
  2. ^ "Entrez Gene: FHL2 four and a half LIM domains 2". 
  3. ^ Wei, Yu; Renard Claire-Angélique; Labalette Charlotte; Wu Yuanfei; Lévy Laurence; Neuveut Christine; Prieur Xavier; Flajolet Marc; Prigent Sylvie; Buendia Marie-Annick (February 2003). "Identification of the LIM protein FHL2 as a coactivator of beta-catenin". J. Biol. Chem. (United States) 278 (7): 5188–94.  
  4. ^ Lange, Stephan; Auerbach Daniel; McLoughlin Patricia; Perriard Evelyne; Schäfer Beat W; Perriard Jean-Claude; Ehler Elisabeth (December 2002). "Subcellular targeting of metabolic enzymes to titin in heart muscle may be mediated by DRAL/FHL-2". J. Cell. Sci. (England) 115 (Pt 24): 4925–36.  
  5. ^ McLoughlin, Patricia; Ehler Elisabeth; Carlile Graeme; Licht Jonathan D; Schäfer Beat W (October 2002). "The LIM-only protein DRAL/FHL2 interacts with and is a corepressor for the promyelocytic leukemia zinc finger protein". J. Biol. Chem. (United States) 277 (40): 37045–53.  
  6. ^ a b c d e Wixler, V; Geerts D; Laplantine E; Westhoff D; Smyth N; Aumailley M; Sonnenberg A; Paulsson M (October 2000). "The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes". J. Biol. Chem. (UNITED STATES) 275 (43): 33669–78.  
  7. ^ Müller, J M; Isele U; Metzger E; Rempel A; Moser M; Pscherer A; Breyer T; Holubarsch C; Buettner R; Schüle R (February 2000). "FHL2, a novel tissue-specific coactivator of the androgen receptor". EMBO J. (ENGLAND) 19 (3): 359–69.  
  8. ^ Samson, Thomas; Smyth Neil; Janetzky Stefanie; Wendler Olaf; Müller Judith M; Schüle Roland; von der Mark Helga; von der Mark Klaus; Wixler Viktor (July 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.  
  9. ^ a b Fimia, G M; 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. (UNITED STATES) 20 (22): 8613–22.  
  10. ^ Purcell, Nicole H; Darwis Dina; Bueno Orlando F; Müller Judith M; Schüle Roland; Molkentin Jeffery D (February 2004). "Extracellular Signal-Regulated Kinase 2 Interacts with and Is Negatively Regulated by the LIM-Only Protein FHL2 in Cardiomyocytes". Mol. Cell. Biol. (United States) 24 (3): 1081–95.  
  11. ^ Ng, Enders Kai On; Chan Kwok Keung; Wong Chi Hang; Tsui Stephen Kwok Wing; Ngai Sai Ming; Lee Simon Ming Yuen; Kotaka Masayo; Lee Cheuk Yu; Waye Mary Miu Yee; Fung Kwok Pui (2002). "Interaction of the heart-specific LIM domain protein, FHL2, with DNA-binding nuclear protein, hNP220". J. Cell. Biochem. (United States) 84 (3): 556–66.  
  12. ^ Yan, Jinghua; Zhu Jianhua; Zhong Hongjun; Lu Qiujun; Huang Cuifen; Ye Qinong (October 2003). "BRCA1 interacts with FHL2 and enhances FHL2 transactivation function". FEBS Lett. (Netherlands) 553 (1–2): 183–9.  
  13. ^ Yan, Jing-Hua; Ye Qi-Nong; Zhu Jian-Hua; Zhong Hong-Jun; Zheng Hui-Yong; Huang Cui-Fen (December 2003). "[Isolation and characterization of a BRCA1-interacting protein]". Yi Chuan Xue Bao (China) 30 (12): 1161–6.  
  14. ^ 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.  
  15. ^ Amaar, Yousef G; Thompson Garrett R; Linkhart Thomas A; Chen Shin-Tai; Baylink David J; Mohan Subburaman (April 2002). "Insulin-like growth factor-binding protein 5 (IGFBP-5) interacts with a four and a half LIM protein 2 (FHL2)". J. Biol. Chem. (United States) 277 (14): 12053–60.  
  16. ^ Bai, Shuting; Zha Jikun; Zhao Haibo; Ross F Patrick; Teitelbaum Steven L (November 2008). "Tumor Necrosis Factor Receptor-associated Factor 6 Is an Intranuclear Transcriptional Coactivator in Osteoclasts". J. Biol. Chem. (United States) 283 (45): 30861–7.  
  17. ^ Tanahashi, H; Tabira T (September 2000). "Alzheimer's disease-associated presenilin 2 interacts with DRAL, an LIM-domain protein". Hum. Mol. Genet. (ENGLAND) 9 (15): 2281–9.  

Further reading

External links

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

This article was sourced from Creative Commons Attribution-ShareAlike License; additional terms may apply. World Heritage Encyclopedia content is assembled from numerous content providers, Open Access Publishing, and in compliance with The Fair Access to Science and Technology Research Act (FASTR), Wikimedia Foundation, Inc., Public Library of Science, The Encyclopedia of Life, Open Book Publishers (OBP), PubMed, U.S. National Library of Medicine, National Center for Biotechnology Information, U.S. National Library of Medicine, National Institutes of Health (NIH), U.S. Department of Health & Human Services, and, which sources content from all federal, state, local, tribal, and territorial government publication portals (.gov, .mil, .edu). Funding for and content contributors is made possible from the U.S. Congress, E-Government Act of 2002.
Crowd sourced content that is contributed to World Heritage Encyclopedia is peer reviewed and edited by our editorial staff to ensure quality scholarly research articles.
By using this site, you agree to the Terms of Use and Privacy Policy. World Heritage Encyclopedia™ is a registered trademark of the World Public Library Association, a non-profit organization.

Copyright © World Library Foundation. All rights reserved. eBooks from Project Gutenberg are sponsored by the World Library Foundation,
a 501c(4) Member's Support Non-Profit Organization, and is NOT affiliated with any governmental agency or department.