Sequence Detail

ID/Version

Q9Z2A5 Q9Z2A4 Q4FCQ7 Q8CFP7 Q4FCQ6 (UniProt | EBI)

Last sequence update: 2011-07-27
Last annotation update: 2025-02-05

Sequence description from provider

RecName: Full=Arginyl-tRNA--protein transferase 1; Short=Arginyltransferase 1; Short=R-transferase 1; EC=2.3.2.8 {ECO:0000269|PubMed:25369936};AltName: Full=Arginine-tRNA--protein transferase 1;

Provider

SWISS-PROT

Sequence

Polypeptide 516 aa

Source

Organism mouse

See UniProt | EBI for source

Annotated genes and markers

Follow the symbol links to get more information on the GO terms, expression assays, orthologs, phenotypic alleles, and other information for the genes or markers below.

Type	Symbol	Name	GO Terms	Expression Assays	Orthologs	Phenotypic Alleles
Gene	Ate1	arginyltransferase 1	23	102	3	7

Sequence references in MGI

J:51609 Kwon YT, et al., Alternative splicing results in differential expression, activity, and localization of the two forms of arginyl-tRNA-protein transferase, a component of the N-end rule pathway. Mol Cell Biol. 1999 Jan;19(1):182-93
J:99680 The FANTOM Consortium and RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group), The Transcriptional Landscape of the Mammalian Genome. Science. 2005;309(5740):1559-1563
J:100170 Rai R, et al., Identification of mammalian arginyltransferases that modify a specific subset of protein substrates. Proc Natl Acad Sci U S A. 2005 Jul 19;102(29):10123-8
J:216283 Brower CS, et al., Liat1, an arginyltransferase-binding protein whose evolution among primates involved changes in the numbers of its 10-residue repeats. Proc Natl Acad Sci U S A. 2014 Nov 18;111(46):E4936-45
J:292518 Huttlin EL, et al., A tissue-specific atlas of mouse protein phosphorylation and expression. Cell. 2010 Dec 23;143(7):1174-89
J:335510 Arva A, et al., The Ligand of Ate1 is intrinsically disordered and participates in nucleolar phase separation regulated by Jumonji Domain Containing 6. Proc Natl Acad Sci U S A. 2021 Jan 5;118(1):e2015887118
J:347318 Heo AJ, et al., The N-terminal cysteine is a dual sensor of oxygen and oxidative stress. Proc Natl Acad Sci U S A. 2021 Dec 14;118(50)