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Literature summary for 3.2.1.143 extracted from

  • Dahl, M.; Maturi, V.; Loenn, P.; Papoutsoglou, P.; Zieba, A.; Vanlandewijck, M.; van der Heide, L.P.; Watanabe, Y.; Soederberg, O.; Hottiger, M.O.; Heldin, C.H.; Moustakas, A.
    Fine-tuning of Smad protein function by poly(ADP-ribose) polymerases and poly(ADP-ribose) glycohydrolase during transforming growth factor beta signaling (2014), PLoS ONE, 9, e103651.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
additional information enzyme knockdown using siRNA Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
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Source Tissue

Source Tissue Comment Organism Textmining
HaCaT cell
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 Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme can effectively process the added poly-/oligo(ADP-ribose) units from both GST-Smad3 and PARP-1, but fails to act as a mono(ADP-ribose) hydrolase, inability of the enzme to cleave the last ADP-ribose unit, which is coupled to the protein substrate Homo sapiens ?
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 ?

General Information

General Information Comment Organism
malfunction silencing of endogenous enzyme expression causes inhibition of TGFbeta-mediated transcription. This can be relieved after simultaneous depletion of poly(ADP-ribose) polymerase 1 Homo sapiens
metabolism poly(ADP-ribose) glycohydrolase partly controls the turnover of dynamic protein ADP-ribosylation mediated by poly(ADP-ribose) polymerase 1, PARP-1. Poly(ADP-ribose) glycohydrolase (PARG) can remove poly(ADP-ribose) chains from target proteins of PARP-1. Endogenous PARP-1 and the enzyme have opposing roles on TGFbeta-induced gene expression, overview Homo sapiens