TWF1

From Wikipedia, the free encyclopedia


Twinfilin, actin-binding protein, homolog 1 (Drosophila)
PDB rendering based on 1m4j.
Available structures: 1m4j, 2d8b, 2hd7
Identifiers
Symbol(s) TWF1; A6; MGC23788; MGC41876; PTK9
External IDs MGI1100520 HomoloGene48140
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 5756 19230
Ensembl ENSG00000151239 ENSMUSG00000022451
Uniprot Q12792 Q91YR1
Refseq XM_001127231 (mRNA)
XP_001127231 (protein)
NM_008971 (mRNA)
NP_032997 (protein)
Location Chr 12: 42.47 - 42.49 Mb Chr 15: 94.41 - 94.42 Mb
Pubmed search [1] [2]

Twinfilin, actin-binding protein, homolog 1 (Drosophila), also known as TWF1, is a human gene.[1]

This gene encodes twinfilin, an actin monomer-binding protein conserved from yeast to mammals. Studies of the mouse counterpart suggest that this protein may be an actin monomer-binding protein, and its localization to cortical G-actin-rich structures may be regulated by the small GTPase RAC1.[1]

[edit] References

[edit] Further reading

  • Palmgren S, Vartiainen M, Lappalainen P (2002). "Twinfilin, a molecular mailman for actin monomers.". J. Cell. Sci. 115 (Pt 5): 881-6. PMID 11870207. 
  • Hassel S, Eichner A, Yakymovych M, et al. (2004). "Proteins associated with type II bone morphogenetic protein receptor (BMPR-II) and identified by two-dimensional gel electrophoresis and mass spectrometry.". Proteomics 4 (5): 1346-58. doi:10.1002/pmic.200300770. PMID 15188402. 
  • 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. 
  • Vartiainen MK, Sarkkinen EM, Matilainen T, et al. (2003). "Mammals have two twinfilin isoforms whose subcellular localizations and tissue distributions are differentially regulated.". J. Biol. Chem. 278 (36): 34347-55. doi:10.1074/jbc.M303642200. PMID 12807912. 
  • Galey D, Becker K, Haughey N, et al. (2003). "Differential transcriptional regulation by human immunodeficiency virus type 1 and gp120 in human astrocytes.". J. Neurovirol. 9 (3): 358-71. PMID 12775419. 
  • 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. 
  • Ojala PJ, Paavilainen VO, Vartiainen MK, et al. (2003). "The two ADF-H domains of twinfilin play functionally distinct roles in interactions with actin monomers.". Mol. Biol. Cell 13 (11): 3811-21. doi:10.1091/mbc.E02-03-0157. PMID 12429826. 
  • Paavilainen VO, Merckel MC, Falck S, et al. (2003). "Structural conservation between the actin monomer-binding sites of twinfilin and actin-depolymerizing factor (ADF)/cofilin.". J. Biol. Chem. 277 (45): 43089-95. doi:10.1074/jbc.M208225200. PMID 12207032. 
  • Beeler JF, LaRochelle WJ, Chedid M, et al. (1994). "Prokaryotic expression cloning of a novel human tyrosine kinase.". Mol. Cell. Biol. 14 (2): 982-8. PMID 7507208.