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Literature summary for 3.1.5.B1 extracted from

  • Lee, E.J.; Seo, J.H.; Park, J.H.; Vo, T.T.L.; An, S.; Bae, S.J.; Le, H.; Lee, H.S.; Wee, H.J.; Lee, D.; Chung, Y.H.; Kim, J.A.; Jang, M.K.; Ryu, S.H.; Yu, E.; Jang, S.H.; Park, Z.Y.; Kim, K.W.
    SAMHD1 acetylation enhances its deoxynucleotide triphosphohydrolase activity and promotes cancer cell proliferation (2017), Oncotarget, 8, 68517-68529 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
K405R mutant cannot be acetylated, reduced activity compared to acetylated wild-type protein. K405R mutant expressing cancer cells show reduced G1/S transition and slower proliferation compared to wildtype Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9Y3Z3
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Posttranslational Modification

Posttranslational Modification Comment Organism
acetylation SAMHD1 is acetylated at residue K405 in vitro and in vivo by acetylatransferase arrest defective protein ARD1. Acetylated SAMHD1 wildtype proteins have enhanced dNTPase activity in vitro. SAMHD1 acetylation levels are strongest during the G1 phase Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
hepatocarcinoma cell
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Homo sapiens
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liver
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Homo sapiens
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