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    RGLG1 RING domain ligase1 [ Arabidopsis thaliana (thale cress) ]

    Gene ID: 819911, updated on 18-Sep-2024

    Summary

    Official Symbol
    RGLG1
    Official Full Name
    RING domain ligase1
    Primary source
    TAIR:AT3G01650
    Locus tag
    AT3G01650
    See related
    Araport:AT3G01650
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Arabidopsis thaliana (ecotype: Columbia)
    Lineage
    Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis
    Also known as
    F4P13.19; F4P13_19; RING domain ligase1
    Summary
    Encodes RGLG1 (RING domain ligase 1), a RING domain ubiquitin E3 ligase that negatively regulates the drought stress response by mediating ERF53 transcriptional activity.
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    Genomic context

    See RGLG1 in Genome Data Viewer
    Location:
    chromosome: 3
    Exon count:
    11
    Sequence:
    Chromosome: 3; NC_003074.8 (241739..245284)

    Chromosome 3 - NC_003074.8Genomic Context describing neighboring genes Neighboring gene Major facilitator superfamily protein Neighboring gene glucuronokinase G Neighboring gene S-adenosyl-L-methionine-dependent methyltransferases superfamily protein Neighboring gene sieve element occlusion protein

    Bibliography

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?

    Interactions

    Products Interactant Other Gene Complex Source Pubs Description

    General protein information

    Preferred Names
    RING domain ligase1
    NP_186814.1
    • RING domain ligase1 (RGLG1); FUNCTIONS IN: zinc ion binding; INVOLVED IN: N-terminal protein myristoylation, cytokinin metabolic process, auxin metabolic process; LOCATED IN: plasma membrane; EXPRESSED IN: 28 plant structures; EXPRESSED DURING: 15 growth stages; CONTAINS InterPro DOMAIN/s: Zinc finger, RING-type (InterPro:IPR001841), Copine (InterPro:IPR010734), von Willebrand factor, type A (InterPro:IPR002035); BEST Arabidopsis thaliana protein match is: RING domain ligase2 (TAIR:AT5G14420.2); Has 24426 Blast hits to 13505 proteins in 916 species: Archae - 24; Bacteria - 3147; Metazoa - 7235; Fungi - 3380; Plants - 4548; Viruses - 743; Other Eukaryotes - 5349 (source: NCBI BLink).

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

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

    Reference assembly

    Genomic

    1. NC_003074.8 Reference assembly

      Range
      241739..245284
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_111031.4NP_186814.1  RING domain ligase1 [Arabidopsis thaliana]

      See identical proteins and their annotated locations for NP_186814.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      Q9SS90
      UniProtKB/TrEMBL
      A0A178VGS3, A0A5S9X885
      Conserved Domains (2) summary
      cd16729
      Location:445489
      RING-HC_RGLG_plant; RING finger, HC subclass, found in RING domain ligase RGLG1, RGLG2 and similar proteins from plant
      cl00057
      Location:133383
      vWFA; Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of ...
    2. NM_001337352.1NP_001325948.1  RING domain ligase1 [Arabidopsis thaliana]

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      Q9SS90
      UniProtKB/TrEMBL
      A0A178VGS3, A0A5S9X885
      Conserved Domains (2) summary
      cd16729
      Location:445489
      RING-HC_RGLG_plant; RING finger, HC subclass, found in RING domain ligase RGLG1, RGLG2 and similar proteins from plant
      cl00057
      Location:133383
      vWFA; Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of ...