TMSB4X

From Wikipedia, the free encyclopedia


Thymosin, beta 4, X-linked
Identifiers
Symbol(s) TMSB4X; FX; PTMB4; TB4X; TMSB4
External IDs OMIM: 300159
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 7114 n/a
Ensembl ENSG00000205542 n/a
Uniprot P62328 n/a
Refseq NM_021109 (mRNA)
NP_066932 (protein)		 n/a (mRNA)
n/a (protein)
Location Chr X: 12.9 - 12.91 Mb n/a
Pubmed search [1] n/a

Thymosin, beta 4, X-linked, also known as TMSB4X, is a human gene.[1]

This gene encodes an actin sequestering protein which plays a role in regulation of actin polymerization. The protein is also involved in cell proliferation, migration, and differentiation. This gene escapes X inactivation and has a homolog on chromosome Y.[1]

[edit] See also

[edit] References

  1. ^ a b Entrez Gene: TMSB4X thymosin, beta 4, X-linked.

[edit] Further reading

  • Huff T, Müller CS, Otto AM, et al. (2001). "beta-Thymosins, small acidic peptides with multiple functions.". Int. J. Biochem. Cell Biol. 33 (3): 205–20. PMID 11311852. 
  • Bubb MR (2003). "Thymosin beta 4 interactions.". Vitam. Horm. 66: 297–316. PMID 12852258. 
  • Goldschmidt-Clermont PJ, Furman MI, Wachsstock D, et al. (1992). "The control of actin nucleotide exchange by thymosin beta 4 and profilin. A potential regulatory mechanism for actin polymerization in cells.". Mol. Biol. Cell 3 (9): 1015–24. PMID 1330091. 
  • Sanders MC, Goldstein AL, Wang YL (1992). "Thymosin beta 4 (Fx peptide) is a potent regulator of actin polymerization in living cells.". Proc. Natl. Acad. Sci. U.S.A. 89 (10): 4678–82. PMID 1584803. 
  • Safer D, Elzinga M, Nachmias VT (1991). "Thymosin beta 4 and Fx, an actin-sequestering peptide, are indistinguishable.". J. Biol. Chem. 266 (7): 4029–32. PMID 1999398. 
  • Clauss IM, Wathelet MG, Szpirer J, et al. (1991). "Human thymosin-beta 4/6-26 gene is part of a multigene family composed of seven members located on seven different chromosomes.". Genomics 9 (1): 174–80. PMID 2004759. 
  • Gómez-Márquez J, Dosil M, Segade F, et al. (1989). "Thymosin-beta 4 gene. Preliminary characterization and expression in tissues, thymic cells, and lymphocytes.". J. Immunol. 143 (8): 2740–4. PMID 2677145. 
  • Soma G, Murata M, Kitahara N, et al. (1985). "Detection of a countertranscript in promyelocytic leukemia cells HL60 during early differentiation by TPA.". Biochem. Biophys. Res. Commun. 132 (1): 100–9. PMID 2998351. 
  • Gondo H, Kudo J, White JW, et al. (1988). "Differential expression of the human thymosin-beta 4 gene in lymphocytes, macrophages, and granulocytes.". J. Immunol. 139 (11): 3840–8. PMID 3500230. 
  • Friedman RL, Manly SP, McMahon M, et al. (1984). "Transcriptional and posttranscriptional regulation of interferon-induced gene expression in human cells.". Cell 38 (3): 745–55. PMID 6548414. 
  • Erickson-Viitanen S, Ruggieri S, Natalini P, Horecker BL (1983). "Distribution of thymosin beta 4 in vertebrate classes.". Arch. Biochem. Biophys. 221 (2): 570–6. PMID 6838210. 
  • Pantaloni D, Carlier MF (1994). "How profilin promotes actin filament assembly in the presence of thymosin beta 4.". Cell 75 (5): 1007–14. PMID 8252614. 
  • Van Troys M, Dewitte D, Goethals M, et al. (1996). "The actin binding site of thymosin beta 4 mapped by mutational analysis.". EMBO J. 15 (2): 201–10. PMID 8617195. 
  • Feinberg J, Heitz F, Benyamin Y, Roustan C (1996). "The N-terminal sequences (5-20) of thymosin beta 4 binds to monomeric actin in an alpha-helical conformation.". Biochem. Biophys. Res. Commun. 222 (1): 127–32. PMID 8630056. 
  • Safer D, Sosnick TR, Elzinga M (1997). "Thymosin beta 4 binds actin in an extended conformation and contacts both the barbed and pointed ends.". Biochemistry 36 (19): 5806–16. doi:10.1021/bi970185v. PMID 9153421. 
  • Malinda KM, Goldstein AL, Kleinman HK (1997). "Thymosin beta 4 stimulates directional migration of human umbilical vein endothelial cells.". FASEB J. 11 (6): 474–81. PMID 9194528. 
  • Lahn BT, Page DC (1997). "Functional coherence of the human Y chromosome.". Science 278 (5338): 675–80. PMID 9381176. 
  • Chen J, Peterson RT, Schreiber SL (1998). "Alpha 4 associates with protein phosphatases 2A, 4, and 6.". Biochem. Biophys. Res. Commun. 247 (3): 827–32. doi:10.1006/bbrc.1998.8792. PMID 9647778. 
  • Huff T, Ballweber E, Humeny A, et al. (2000). "Thymosin beta(4) serves as a glutaminyl substrate of transglutaminase. Labeling with fluorescent dansylcadaverine does not abolish interaction with G-actin.". FEBS Lett. 464 (1-2): 14–20. PMID 10611475. 
  • De La Cruz EM, Ostap EM, Brundage RA, et al. (2000). "Thymosin-beta(4) changes the conformation and dynamics of actin monomers.". Biophys. J. 78 (5): 2516–27. PMID 10777749. 
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