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Gene Review

KTI11  -  Kti11p

Saccharomyces cerevisiae S288c

Synonyms: DPH3, Diphthamide biosynthesis protein 3, Kluyveromyces lactis toxin-insensitive protein 11, YBL071W-A
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Disease relevance of KTI11


High impact information on KTI11


Biological context of KTI11


Associations of KTI11 with chemical compounds

  • We present the first experimental evidence that Kti11p can bind a single Zn(2+) ion by its four conserved cysteine residues [3].

Other interactions of KTI11

  • Using TAP tagging, Kti11p contacts Elongator and translational proteins (Rps7Ap, Rps19Ap Eft2p, Yil103wp, Dph2p) [2].

Analytical, diagnostic and therapeutic context of KTI11


  1. KTI11 and KTI13, Saccharomyces cerevisiae genes controlling sensitivity to G1 arrest induced by Kluyveromyces lactis zymocin. Fichtner, L., Schaffrath, R. Mol. Microbiol. (2002) [Pubmed]
  2. Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification. Fichtner, L., Jablonowski, D., Schierhorn, A., Kitamoto, H.K., Stark, M.J., Schaffrath, R. Mol. Microbiol. (2003) [Pubmed]
  3. Solution structure of Kti11p from Saccharomyces cerevisiae reveals a novel zinc-binding module. Sun, J., Zhang, J., Wu, F., Xu, C., Li, S., Zhao, W., Wu, Z., Wu, J., Zhou, C.Z., Shi, Y. Biochemistry (2005) [Pubmed]
  4. Dph3, a small protein required for diphthamide biosynthesis, is essential in mouse development. Liu, S., Wiggins, J.F., Sreenath, T., Kulkarni, A.B., Ward, J.M., Leppla, S.H. Mol. Cell. Biol. (2006) [Pubmed]
  5. The yeast elongator histone acetylase requires Sit4-dependent dephosphorylation for toxin-target capacity. Jablonowski, D., Fichtner, L., Stark, M.J., Schaffrath, R. Mol. Biol. Cell (2004) [Pubmed]
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