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BRENDA support

Literature summary for 2.7.7.8 extracted from

  • French, S.W.; Dawson, D.W.; Chen, H.; Rainey, R.N.; Sievers, S.A.; Balatoni, C.E.; Wong, L.; Troke, J.J.; Nguyen, M.T.; Koehler, C.M.; Teitell, M.A.
    The TCL1 oncoprotein binds the RNase PH domains of the PNPase exoribonuclease without affecting its RNA degrading activity (2007), Cancer Lett., 248, 198-210.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Homo sapiens Q8TCS8
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Source Tissue

Source Tissue Comment Organism Textmining
HEK-293T cell
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Homo sapiens
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NALM-6 cell pre-B cell Homo sapiens
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Subunits

Subunits Comment Organism
More enzyme interacts with AKT kinase coactivator TCL1. The AKT interaction domain on TCL1 binds either Rnase PH repeat domain on PNPase without influencing its RNA degrading activity Homo sapiens
More polyribonucleotide phosphorylase interacts with AKT kinase coactivator TCL1. The AKT interaction domain on TCL1 binds either polyribonucleotide phosphorylase PH repeat domain without influencing its RNA degrading activity, compatible with predicted docking models for a TCL1-PNPase complex Homo sapiens