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Literature summary for 3.1.5.B1 extracted from

  • Bloch, N.; Glaesker, S.; Sitaram, P.; Hofmann, H.; Shepard, C.N.; Schultz, M.L.; Kim, B.; Landau, N.R.
    A highly active isoform of lentivirus restriction factor SAMHD1 in mouse (2017), J. Biol. Chem., 292, 1068-1080 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.5.B1

Activating Compound

Activating Compound Comment Organism Structure
dGTP dGTP causes ISF1 to tetramerize, activating its catalytic activity. Isoform ISF2 has dGTP-independent catalytic activity Mus musculus

Cloned(Commentary)

Cloned (Comment) Organism
expression in 293T cell Mus musculus

Protein Variants

Protein Variants Comment Organism
P635A mutation retains antiviral activity of ISF1, and increased its catalytic activity to that of ISF2 Mus musculus
T634A mutation retains antiviral activity of ISF1 Mus musculus
T634E mutation in ISF1, mimics phosphorylated SAMHD1. Mutant is inactive Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus Q60710 isoform 1
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein isoform ISF1 is phosphorylated at amino acids Ser49, Thr52, Ser55, Thr56, Thr310, and Thr634 with frequencies ranging from 21% to 56% Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining

General Information

General Information Comment Organism
physiological function in the mouse, SAMHD1 is expressed as isoforms ISF1 and ISF2 that differ at the carboxyl terminus due to alternative splicing of the last coding exon. Both isoforms are antiviral in nondividing cells. Phosphomimetic mutation at Thr-634 of ISF1 ablates its antiviral activity but has little effect on phosphohydrolase activity in vitro. dGTP causes ISF1 to tetramerize, activating its catalytic activity. Isoform ISF2 lacks the phosphorylation site, is significantly more active, tetramerizes, and is active without added dGTP. Mouse SAMHD1 does not degrade HIV-1 genomic viral RNA Mus musculus