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Literature summary extracted from

  • Brower, C.S.; Rosen, C.E.; Jones, R.H.; Wadas, B.C.; Piatkov, K.I.; Varshavsky, A.
    Liat1, an arginyltransferase-binding protein whose evolution among primates involved changes in the numbers of its 10-residue repeats (2014), Proc. Natl. Acad. Sci. USA, 111, E4936-E4945.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.2.8 expressed in Escherichia coli BL21(DE3) cells Mus musculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.2.8 59000
-
 x * 59000, SDS-PAGE Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.2.8 L-arginyl-tRNAArg + protein Mus musculus
-
 tRNAArg + L-arginyl-[protein]
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.8 Mus musculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.2.8 Mono-S column chromatography Mus musculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.8 L-arginyl-tRNAArg + protein
-
 Mus musculus tRNAArg + L-arginyl-[protein]
-
 ?
2.3.2.8 additional information Liat1 protein binds to the mouse Ate1 enzyme, but is apparently not arginylated by it Mus musculus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.2.8 ? x * 59000, SDS-PAGE Mus musculus

Synonyms

EC Number Synonyms Comment Organism
2.3.2.8 Arg-tRNA-protein transferase
-
 Mus musculus
2.3.2.8 Ate1
-
 Mus musculus
2.3.2.8 R-transferase
-
 Mus musculus