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    Ate1 arginyltransferase 1 [ Mus musculus (house mouse) ]

    Gene ID: 11907, updated on 28-Oct-2024

    Summary

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    Official Symbol
    Ate1provided by MGI
    Official Full Name
    arginyltransferase 1provided by MGI
    Primary source
    MGI:MGI:1333870
    See related
    Ensembl:ENSMUSG00000030850 AllianceGenome:MGI:1333870
    Gene type
    protein coding
    RefSeq status
    VALIDATED
    Organism
    Mus musculus
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
    Summary
    Enables arginyl-tRNA--protein transferase activity. Involved in ubiquitin-dependent protein catabolic process. Acts upstream of or within protein arginylation. Located in cytoplasm and nucleus. Is expressed in several structures, including embryo mesenchyme; eye; heart; nervous system; and notochord. Orthologous to human ATE1 (arginyltransferase 1). [provided by Alliance of Genome Resources, Oct 2024]
    Expression
    Ubiquitous expression in placenta adult (RPKM 5.0), CNS E18 (RPKM 4.1) and 28 other tissues See more
    Orthologs
    human all
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    Genomic context

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    See Ate1 in Genome Data Viewer
    Location:
    7 F3; 7 73.19 cM
    Exon count:
    17
    Annotation release Status Assembly Chr Location
    RS_2024_02 current GRCm39 (GCF_000001635.27) 7 NC_000073.7 (129993219..130122349, complement)
    108.20200622 previous assembly GRCm38.p6 (GCF_000001635.26) 7 NC_000073.6 (130391493..130520619, complement)

    Chromosome 7 - NC_000073.7Genomic Context describing neighboring genes Neighboring gene predicted gene, 33661 Neighboring gene predicted gene, 39097 Neighboring gene ring finger and WD repeat domain 3 pseudogene Neighboring gene STARR-seq mESC enhancer starr_20244 Neighboring gene VISTA enhancer mm938 Neighboring gene STARR-seq mESC enhancer starr_20245 Neighboring gene STARR-seq mESC enhancer starr_20247 Neighboring gene predicted gene 4275 Neighboring gene NSE4 homolog A, SMC5-SMC6 complex component Neighboring gene transforming, acidic coiled-coil containing protein 2 Neighboring gene STARR-seq mESC enhancer starr_20252 Neighboring gene predicted gene, 34365

    Genomic regions, transcripts, and products

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    Go to nucleotide: Graphics FASTA GenBank

    Expression

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    • Project title: Mouse ENCODE transcriptome data Mouse ENCODE transcriptome data
    • Description: RNA profiling data sets generated by the Mouse ENCODE project.
    • BioProject: PRJNA66167
    • Publication: PMID 25409824
    • Analysis date: n/a

    Bibliography

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    Related articles in PubMed

    1. Target site specificity and in vivo complexity of the mammalian arginylome. Wang J, et al. Sci Rep, 2018 Nov 1. PMID 30385798, Free PMC Article
    2. Reduced passive force in skeletal muscles lacking protein arginylation. Leite FS, et al. Am J Physiol Cell Physiol, 2016 Jan 15. PMID 26511365, Free PMC Article
    3. Ablation of arginylation in the mouse N-end rule pathway: loss of fat, higher metabolic rate, damaged spermatogenesis, and neurological perturbations. Brower CS, et al. PLoS One, 2009 Nov 13. PMID 19915679, Free PMC Article
    4. Ablation of Arg-tRNA-protein transferases results in defective neural tube development. Kim E, et al. BMB Rep, 2016 Aug. PMID 27345715, Free PMC Article
    5. Analyzing N-terminal Arginylation through the Use of Peptide Arrays and Degradation Assays. Wadas B, et al. J Biol Chem, 2016 Sep 30. PMID 27510035, Free PMC Article

    See all (64) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. The Final Maturation State of beta-actin Involves N-terminal Acetylation by NAA80, not N-terminal Arginylation by ATE1.
      Title: The Final Maturation State of β-actin Involves N-terminal Acetylation by NAA80, not N-terminal Arginylation by ATE1.
    2. ATE1-Mediated Post-Translational Arginylation Is an Essential Regulator of Eukaryotic Cellular Homeostasis.
      Title: ATE1-Mediated Post-Translational Arginylation Is an Essential Regulator of Eukaryotic Cellular Homeostasis.
    3. Results strongly suggest that, the inhibition of ATE1 enzyme or knockout of Ate1 gene in pre-adipocytes can suppress adipogenesis via regulation of PPARgamma expression at transcript as well as protein level.
      Title: Arginylation regulates adipogenesis by regulating expression of PPARγ at transcript and protein level.
    4. Our analysis reveals multiple proteins with potential ATE1 target sites and expand our understanding of the biological complexity of the intracellular arginylome.
      Title: Target site specificity and in vivo complexity of the mammalian arginylome.
    5. study revealed a novel role of Ate1 in suppressing prostate cancer metastasis, which has a profound significance for establishing metastatic indicators for prostate cancer, and for finding potential treatments to prevent its metastasis.
      Title: Reduced Arginyltransferase 1 is a driver and a potential prognostic indicator of prostate cancer metastasis.
    6. This study clarifies the role of Ate1/arginylation in stress response.
      Title: Posttranslational arginylation enzyme Ate1 affects DNA mutagenesis by regulating stress response.
    7. zipcode-mediated co-targeting of Ate1 and beta-actin mRNA leads to localized co-translational arginylation of beta-actin that drives the growth cone migration and neurite outgrowth.
      Title: Arginyltransferase ATE1 is targeted to the neuronal growth cones and regulates neurite outgrowth during brain development.
    8. Ate1 is downregulated in several types of human cancer samples at the protein level, and that its transcription level inversely correlates with metastatic progression and patient survival.
      Title: Arginyltransferase suppresses cell tumorigenic potential and inversely correlates with metastases in human cancers.
    9. four major isoforms of mouse R-transferase have similar Nt-arginylation specificities in vitro, contrary to the claim about the specificity of some Ate1 isoforms for N-terminal Cys
      Title: Analyzing N-terminal Arginylation through the Use of Peptide Arrays and Degradation Assays.
    10. the crucial role of ATE1 in neural tube development is directly related to proper turn-over of the RGS4 protein, which participate in the oxygen-sensing mechanism in the cells.
      Title: Ablation of Arg-tRNA-protein transferases results in defective neural tube development.
    Submit: New GeneRIF Correction See all GeneRIFs (24)

    Variation

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    Alleles

    Alleles of this type are documented at Mouse Genome Informatics  (MGI)
    • Endonuclease-mediated (2) 
    • Targeted (4)  1 citation

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Markers

    Homology

    Gene Ontology Provided by MGI

    Function Evidence Code Pubs
    enables arginyl-tRNA--protein transferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables arginyl-tRNA--protein transferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables arginyl-tRNA--protein transferase activity ISO
    Inferred from Sequence Orthology
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in proteasomal protein catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within proteasomal protein catabolic process ISO
    Inferred from Sequence Orthology
    more info
    		 PubMed 
    acts_upstream_of_or_within protein arginylation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in protein arginylation IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in ubiquitin-dependent protein catabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in ubiquitin-dependent protein catabolic process ISO
    Inferred from Sequence Orthology
    more info
    		  
    Component Evidence Code Pubs
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytoplasm ISO
    Inferred from Sequence Orthology
    more info
    		  
    located_in nucleus IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in nucleus ISO
    Inferred from Sequence Orthology
    more info
    		  

    General protein information

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    Preferred Names
    arginyl-tRNA--protein transferase 1
    Names
    R-transferase 1
    arginine-tRNA--protein transferase 1
    NP_001025066.1
    NP_001129526.1
    NP_001258272.1
    NP_001389570.1
    NP_001389571.1
    NP_001389572.1
    NP_001389573.1
    NP_001389574.1
    NP_001389575.1
    NP_001389576.1
    NP_001389577.1
    NP_038827.2
    XP_011239961.1
    XP_036008502.1
    XP_036008503.1
    XP_036008504.1

    NCBI Reference Sequences (RefSeq)

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    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_001029895.4 → NP_001025066.1  arginyl-tRNA--protein transferase 1 isoform 3

      See identical proteins and their annotated locations for NP_001025066.1

      Status: VALIDATED

      Description
      Transcript Variant: This variant (3) uses an alternate 5' structure, compared to variant 1. This difference causes translation initiation at an upstream AUG and results in an isoform (3) that has a distinct N-terminus and is shorter, compared to isoform 1.
      Source sequence(s)
      AC122258, AC157606
      Consensus CDS
      CCDS21901.1
      UniProtKB/TrEMBL
      Q4FCQ7, Q80YP1, Q8BP95
      Related
      ENSMUSP00000091556.4, ENSMUST00000094017.5
      Conserved Domains (2) summary
      pfam04376
      Location:16 → 85
      ATE_N; Arginine-tRNA-protein transferase, N terminus
      pfam04377
      Location:281 → 422
      ATE_C; Arginine-tRNA-protein transferase, C terminus

    2. NM_001136054.3 → NP_001129526.1  arginyl-tRNA--protein transferase 1 isoform 4

      See identical proteins and their annotated locations for NP_001129526.1

      Status: VALIDATED

      Description
      Transcript Variant: This variant (4) uses an alternate in-frame exon in the coding region, compared to variant 1. It encodes isoform 4.
      Source sequence(s)
      AC122258, AC157606
      Consensus CDS
      CCDS52414.1
      UniProtKB/TrEMBL
      Q80YP1
      Related
      ENSMUSP00000043365.8, ENSMUST00000035458.15
      Conserved Domains (2) summary
      pfam04376
      Location:20 → 92
      ATE_N; Arginine-tRNA-protein transferase, N terminus
      pfam04377
      Location:288 → 429
      ATE_C; Arginine-tRNA-protein transferase, C terminus

    3. NM_001271343.2 → NP_001258272.1  arginyl-tRNA--protein transferase 1 isoform 2

      Status: VALIDATED

      Description
      Transcript Variant: This variant (2) uses an alternate 5' structure and an alternate in-frame exon in the coding region, compared to variant 1. These differences cause translation initiation at an upstream AUG and result in an isoform (2) that has a distinct N-terminus and is shorter, compared to isoform 1.
      Source sequence(s)
      AC122258, AC157606
      Consensus CDS
      CCDS72051.1
      UniProtKB/TrEMBL
      J3QNU1
      Related
      ENSMUSP00000136956.2, ENSMUST00000178534.8
      Conserved Domains (2) summary
      pfam04376
      Location:16 → 85
      ATE_N; Arginine-tRNA-protein transferase, N-terminus
      pfam04377
      Location:282 → 420
      ATE_C; Arginine-tRNA-protein transferase, C-terminus

    4. NM_001402641.1 → NP_001389570.1  arginyl-tRNA--protein transferase 1 isoform 5

      Status: VALIDATED

      Source sequence(s)
      AC122258, AC157606
      UniProtKB/TrEMBL
      A0A1L1SQ41
      Related
      ENSMUSP00000148888.2, ENSMUST00000216011.2

    5. NM_001402642.1 → NP_001389571.1  arginyl-tRNA--protein transferase 1 isoform 6

      Status: VALIDATED

      Source sequence(s)
      AC122258, AC157606

    6. NM_001402643.1 → NP_001389572.1  arginyl-tRNA--protein transferase 1 isoform 7

      Status: VALIDATED

      Source sequence(s)
      AC122258, AC157606

    7. NM_001402644.1 → NP_001389573.1  arginyl-tRNA--protein transferase 1 isoform 8

      Status: VALIDATED

      Source sequence(s)
      AC122258, AC157606

    8. NM_001402645.1 → NP_001389574.1  arginyl-tRNA--protein transferase 1 isoform 9

      Status: VALIDATED

      Source sequence(s)
      AC122258, AC157606

    9. NM_001402646.1 → NP_001389575.1  arginyl-tRNA--protein transferase 1 isoform 10

      Status: VALIDATED

      Source sequence(s)
      AC122258

    10. NM_001402647.1 → NP_001389576.1  arginyl-tRNA--protein transferase 1 isoform 11

      Status: VALIDATED

      Source sequence(s)
      AC122258

    11. NM_001402648.1 → NP_001389577.1  arginyl-tRNA--protein transferase 1 isoform 12

      Status: VALIDATED

      Source sequence(s)
      AC122258

    12. NM_013799.4 → NP_038827.2  arginyl-tRNA--protein transferase 1 isoform 1

      See identical proteins and their annotated locations for NP_038827.2

      Status: VALIDATED

      Description
      Transcript Variant: This variant (1) encodes isoform 1.
      Source sequence(s)
      AC122258, AC157606
      Consensus CDS
      CCDS21902.1
      UniProtKB/Swiss-Prot
      Q4FCQ6, Q4FCQ7, Q8CFP7, Q9Z2A4, Q9Z2A5
      Related
      ENSMUSP00000033139.8, ENSMUST00000033139.15
      Conserved Domains (2) summary
      pfam04376
      Location:23 → 92
      ATE_N; Arginine-tRNA-protein transferase, N-terminus
      pfam04377
      Location:288 → 427
      ATE_C; Arginine-tRNA-protein transferase, C-terminus

    RNA

    1. NR_175281.1 RNA Sequence

      Status: VALIDATED

      Source sequence(s)
      AC122258, AC157606

    RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference GRCm39 C57BL/6J

    Genomic

    1. NC_000073.7 Reference GRCm39 C57BL/6J

      Range
      129993219..130122349 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_036152610.1 → XP_036008503.1  arginyl-tRNA--protein transferase 1 isoform X5

      Conserved Domains (2) summary
      pfam04376
      Location:23 → 92
      ATE_N; Arginine-tRNA-protein transferase, N-terminus
      pfam04377
      Location:288 → 418
      ATE_C; Arginine-tRNA-protein transferase, C-terminus

    2. XM_036152609.1 → XP_036008502.1  arginyl-tRNA--protein transferase 1 isoform X3

      Conserved Domains (2) summary
      pfam04376
      Location:23 → 92
      ATE_N; Arginine-tRNA-protein transferase, N-terminus
      pfam04377
      Location:331 → 461
      ATE_C; Arginine-tRNA-protein transferase, C-terminus

    3. XM_036152611.1 → XP_036008504.1  arginyl-tRNA--protein transferase 1 isoform X7

      Conserved Domains (1) summary
      pfam04377
      Location:34 → 173
      ATE_C; Arginine-tRNA-protein transferase, C-terminus

    4. XM_011241659.1 → XP_011239961.1  arginyl-tRNA--protein transferase 1 isoform X4

      Conserved Domains (2) summary
      pfam04376
      Location:23 → 92
      ATE_N; Arginine-tRNA-protein transferase, N-terminus
      pfam04377
      Location:331 → 460
      ATE_C; Arginine-tRNA-protein transferase, C-terminus

    RNA

    1. XR_004934000.1 RNA Sequence

    2. XR_004933999.1 RNA Sequence

    3. XR_004934001.1 RNA Sequence

    Nucleotide Protein Strain
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q9Z2A5.2 GenPept UniProtKB/Swiss-Prot:Q9Z2A5

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

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