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    Sars1 seryl-tRNA synthetase 1 [ Mus musculus (house mouse) ]

    Gene ID: 20226, updated on 27-Nov-2024

    Summary

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    Official Symbol
    Sars1provided by MGI
    Official Full Name
    seryl-tRNA synthetase 1provided by MGI
    Primary source
    MGI:MGI:102809
    See related
    Ensembl:ENSMUSG00000068739 AllianceGenome:MGI:102809
    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
    Also known as
    Sars; Strs; serRS
    Summary
    Predicted to enable several functions, including aminoacyl-tRNA ligase activity; nucleic acid binding activity; and protein homodimerization activity. Predicted to be involved in several processes, including negative regulation of angiogenesis; negative regulation of macromolecule biosynthetic process; and translation. Located in mitochondrion. Is expressed in several structures, including alimentary system; central nervous system; early conceptus; exocrine system; and genitourinary system. Human ortholog(s) of this gene implicated in intellectual disability. Orthologous to human SARS1 (seryl-tRNA synthetase 1). [provided by Alliance of Genome Resources, Nov 2024]
    Expression
    Ubiquitous expression in CNS E14 (RPKM 31.6), CNS E11.5 (RPKM 30.2) and 28 other tissues See more
    Orthologs
    human all
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    Genomic context

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    See Sars1 in Genome Data Viewer
    Location:
    3 F3; 3 47.08 cM
    Exon count:
    12
    Annotation release Status Assembly Chr Location
    RS_2024_02 current GRCm39 (GCF_000001635.27) 3 NC_000069.7 (108332180..108352575, complement)
    108.20200622 previous assembly GRCm38.p6 (GCF_000001635.26) 3 NC_000069.6 (108424864..108445259, complement)

    Chromosome 3 - NC_000069.7Genomic Context describing neighboring genes Neighboring gene STARR-seq mESC enhancer starr_08685 Neighboring gene STARR-positive B cell enhancer ABC_E2094 Neighboring gene proline/serine-rich coiled-coil 1 Neighboring gene cadherin, EGF LAG seven-pass G-type receptor 2 Neighboring gene predicted gene, 52630 Neighboring gene STARR-seq mESC enhancer starr_08687 Neighboring gene STARR-positive B cell enhancer mm9_chr3:108248013-108248314 Neighboring gene STARR-seq mESC enhancer starr_08688 Neighboring gene predicted gene, 22942 Neighboring gene endosome-lysosome associated apoptosis and autophagy regulator 1 Neighboring gene predicted gene, 23336 Neighboring gene STARR-seq mESC enhancer starr_08689 Neighboring gene STARR-positive B cell enhancer ABC_E4574 Neighboring gene cilia and flagella associated protein 276

    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
    • 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. Aminoacyl-tRNA synthetases: a family of expanding functions. Mittelwihr, France, October 10-15, 1999. Martinis SA, et al. EMBO J, 1999 Sep 1. PMID 10469639, Free PMC Article
    2. Mammalian seryl-tRNA synthetase associates with mRNA in vivo and has homology to elongation factor 1 alpha. Miseta A, et al. J Biol Chem, 1991 Oct 15. PMID 1918033
    3. Glucose-sensitive acetylation of Seryl tRNA synthetase regulates lipid synthesis in breast cancer. Zhao J, et al. Signal Transduct Target Ther, 2021 Aug 16. PMID 34400610, Free PMC Article
    4. Oxidative stress diverts tRNA synthetase to nucleus for protection against DNA damage. Wei N, et al. Mol Cell, 2014 Oct 23. PMID 25284223, Free PMC Article
    5. 140 mouse brain proteins identified by Ca2+-calmodulin affinity chromatography and tandem mass spectrometry. Berggård T, et al. J Proteome Res, 2006 Mar. PMID 16512683

    See all (36) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Glucose-sensitive acetylation of Seryl tRNA synthetase regulates lipid synthesis in breast cancer.
      Title: Glucose-sensitive acetylation of Seryl tRNA synthetase regulates lipid synthesis in breast cancer.
    Submit: New GeneRIF Correction

    Variation

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    Alleles

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

    Pathways from PubChem

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    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 ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables RNA polymerase II cis-regulatory region sequence-specific DNA binding ISO
    Inferred from Sequence Orthology
    more info
    		  
    enables RNA polymerase II cis-regulatory region sequence-specific DNA binding ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  
    enables enzyme binding ISO
    Inferred from Sequence Orthology
    more info
    		  
    enables molecular adaptor activity ISO
    Inferred from Sequence Orthology
    more info
    		  
    enables protein homodimerization activity ISO
    Inferred from Sequence Orthology
    more info
    		  
    enables selenocysteine-tRNA ligase activity ISO
    Inferred from Sequence Orthology
    more info
    		  
    enables selenocysteine-tRNA ligase activity ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  
    enables serine-tRNA ligase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables serine-tRNA ligase activity ISO
    Inferred from Sequence Orthology
    more info
    		  
    enables serine-tRNA ligase activity ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  
    enables tRNA binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    Process Evidence Code Pubs
    involved_in cytoplasmic translation ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in cytoplasmic translation ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  
    involved_in negative regulation of angiogenesis ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in negative regulation of angiogenesis ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  
    involved_in negative regulation of transcription by RNA polymerase II ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in negative regulation of transcription by RNA polymerase II ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  
    involved_in negative regulation of vascular endothelial growth factor production ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in negative regulation of vascular endothelial growth factor production ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  
    involved_in selenocysteine incorporation ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in selenocysteine incorporation ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  
    involved_in seryl-tRNA aminoacylation IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in seryl-tRNA aminoacylation ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in seryl-tRNA aminoacylation ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  
    involved_in tRNA modification ISO
    Inferred from Sequence Orthology
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm ISO
    Inferred from Sequence Orthology
    more info
    		  
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytosol ISO
    Inferred from Sequence Orthology
    more info
    		  
    located_in cytosol ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  
    located_in mitochondrion HDA PubMed 
    located_in nucleus ISO
    Inferred from Sequence Orthology
    more info
    		  
    located_in nucleus ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  

    General protein information

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    Preferred Names
    serine--tRNA ligase, cytoplasmic
    Names
    seryl-aminoacyl-tRNA synthetase 1
    seryl-tRNA synthetase, cytoplasmic
    seryl-tRNA(Ser/Sec) synthetase
    NP_001191908.1
    NP_035449.1

    NCBI Reference Sequences (RefSeq)

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    NEW Try the new Transcript table

    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_001204979.1 → NP_001191908.1  serine--tRNA ligase, cytoplasmic isoform 2

      See identical proteins and their annotated locations for NP_001191908.1

      Status: VALIDATED

      Description
      Transcript Variant: This variant (2) lacks an in-frame exon in the 3' coding region, compared to variant 1. The encoded isoform (2) is shorter than isoform 1.
      Source sequence(s)
      AK028358, AK075827, BP765728, BY034232
      Consensus CDS
      CCDS57254.1
      UniProtKB/Swiss-Prot
      A2AFR8, P26638
      UniProtKB/TrEMBL
      Q3U6F6
      Related
      ENSMUSP00000088041.6, ENSMUST00000090553.12
      Conserved Domains (3) summary
      PLN02678
      Location:3 → 486
      PLN02678; seryl-tRNA synthetase
      cd00770
      Location:152 → 460
      SerRS_core; Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the attachment of serine to the 3' OH group of ribose of the appropriate tRNA. This domain It is primarily responsible for ATP-dependent formation of the enzyme bound ...
      pfam02403
      Location:3 → 109
      Seryl_tRNA_N; Seryl-tRNA synthetase N-terminal domain

    2. NM_011319.3 → NP_035449.1  serine--tRNA ligase, cytoplasmic isoform 1

      See identical proteins and their annotated locations for NP_035449.1

      Status: VALIDATED

      Description
      Transcript Variant: This variant (1) represents the longer transcript and encodes the longer isoform (1).
      Source sequence(s)
      AK028358, AK082793, BP765728, BY034232
      Consensus CDS
      CCDS17760.1
      UniProtKB/TrEMBL
      Q3U6F6, Q8C483
      Related
      ENSMUSP00000099685.5, ENSMUST00000102625.11
      Conserved Domains (3) summary
      PLN02678
      Location:3 → 510
      PLN02678; seryl-tRNA synthetase
      cd00770
      Location:152 → 484
      SerRS_core; Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the attachment of serine to the 3' OH group of ribose of the appropriate tRNA. This domain It is primarily responsible for ATP-dependent formation of the enzyme bound ...
      pfam02403
      Location:3 → 109
      Seryl_tRNA_N; Seryl-tRNA synthetase N-terminal domain

    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_000069.7 Reference GRCm39 C57BL/6J

      Range
      108332180..108352575 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)
    Nucleotide Protein Strain
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P26638.3 GenPept UniProtKB/Swiss-Prot:P26638

    Gene LinkOut

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

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