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CNOT4  -  CCR4-NOT transcription complex, subunit 4

Homo sapiens

Synonyms: CCR4-NOT transcription complex subunit 4, CCR4-associated factor 4, CLONE243, E3 ubiquitin-protein ligase CNOT4, NOT4, ...
 
 
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High impact information on CNOT4

  • NMR experiments using a (113)Cd-substituted hNOT4 RING finger showed that two metal ions are bound through cysteine residues in a cross-brace manner [1].
  • The NOT4 protein is a component of the CCR4.NOT complex, a global regulator of RNA polymerase II transcription [1].
  • To understand the basis for this interaction, we identified several basic residues of UbcH5B important for binding to CNOT4 by mutational analysis [2].
  • Structural model of the UbcH5B/CNOT4 complex revealed by combining NMR, mutagenesis, and docking approaches [3].
 

Other interactions of CNOT4

  • Concomitant charge-alteration of E49 of CNOT4 and K63 of UbcH5B restored binding and re-created a functional enzyme pair, indicative of an electrostatic interaction between these residues [2].

References

  1. The structure of the C4C4 ring finger of human NOT4 reveals features distinct from those of C3HC4 RING fingers. Hanzawa, H., de Ruwe, M.J., Albert, T.K., van Der Vliet, P.C., Timmers, H.T., Boelens, R. J. Biol. Chem. (2001) [Pubmed]
  2. An altered-specificity ubiquitin-conjugating enzyme/ubiquitin-protein ligase pair. Winkler, G.S., Albert, T.K., Dominguez, C., Legtenberg, Y.I., Boelens, R., Timmers, H.T. J. Mol. Biol. (2004) [Pubmed]
  3. Structural model of the UbcH5B/CNOT4 complex revealed by combining NMR, mutagenesis, and docking approaches. Dominguez, C., Bonvin, A.M., Winkler, G.S., van Schaik, F.M., Timmers, H.T., Boelens, R. Structure (Camb.) (2004) [Pubmed]
 
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