U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

    AOS1 E1 ubiquitin-activating protein AOS1 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 856310, updated on 2-Nov-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    AOS1
    Official Full Name
    E1 ubiquitin-activating protein AOS1
    Primary source
    SGD:S000006384
    Locus tag
    YPR180W
    See related
    AllianceGenome:SGD:S000006384; FungiDB:YPR180W; VEuPathDB:YPR180W
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Also known as
    RHC31
    Summary
    Contributes to SUMO activating enzyme activity. Involved in protein sumoylation. Located in cytosol and nucleus. Part of SUMO activating enzyme complex. Orthologous to human SAE1 (SUMO1 activating enzyme subunit 1). [provided by Alliance of Genome Resources, Nov 2024]
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    Go to the top of the page Help
    See AOS1 in Genome Data Viewer
    Location:
    chromosome: XVI
    Exon count:
    1
    Sequence:
    Chromosome: XVI; NC_001148.4 (895961..897004)

    Chromosome XVI - NC_001148.4Genomic Context describing neighboring genes Neighboring gene U4/U6-U5 snRNP complex subunit PRP4 Neighboring gene Hda3p Neighboring gene GTPase-activating protein SEC23 Neighboring gene mRNA splicing protein SMX3

    Genomic regions, transcripts, and products

    Go to the top of the page Help
    Genomic Sequence:
    NC_001148.4

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

    Go to the top of the pageHelp

    Related articles in PubMed

    1. Purification of SUMO conjugating enzymes and kinetic analysis of substrate conjugation. Yunus AA, et al. Methods Mol Biol, 2009. PMID 19107417, Free PMC Article
    2. The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer. Johnson ES, et al. EMBO J, 1997 Sep 15. PMID 9312010, Free PMC Article
    3. Crystal structure of UBA2(ufd)-Ubc9: insights into E1-E2 interactions in Sumo pathways. Wang J, et al. PLoS One, 2010 Dec 30. PMID 21209884, Free PMC Article
    4. SUMO conjugation and deconjugation. Schwienhorst I, et al. Mol Gen Genet, 2000 Jun. PMID 10905345
    5. A Chemical and Enzymatic Approach to Study Site-Specific Sumoylation. Albuquerque CP, et al. PLoS One, 2015. PMID 26633173, Free PMC Article

    See all (36) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Pathways from PubChem

    Go to the top of the page

    Interactions

    Go to the top of the page Help
    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Go to the top of the page Help

    Homology

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    contributes_to SUMO activating enzyme activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ubiquitin-like modifier activating enzyme activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in DNA damage response IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in macromolecule modification IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein sumoylation IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in protein sumoylation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Component Evidence Code Pubs
    part_of SUMO activating enzyme complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of SUMO activating enzyme complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in nucleus HDA PubMed 
    located_in nucleus IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

    Go to the top of the page Help
    Preferred Names
    E1 ubiquitin-activating protein AOS1
    NP_015506.1
    • Subunit of heterodimeric nuclear SUMO activating enzyme E1 with Uba2p; activates Smt3p (SUMO) before its conjugation to proteins (sumoylation), which may play a role in protein targeting; essential for viability; relocalizes to the cytosol in response to hypoxia

    NCBI Reference Sequences (RefSeq)

    Go to the top of the page Help

    NEW Try the new Transcript table

    Genome Annotation

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

    Reference assembly

    Genomic

    1. NC_001148.4 Reference assembly

      Range
      895961..897004
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001184277.1 → NP_015506.1  TPA: E1 ubiquitin-activating protein AOS1 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_015506.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W4I0, Q06624
      UniProtKB/TrEMBL
      B3LKD9, B5VTW1, C7GP62, C8ZJK9, N1P2H9
      Conserved Domains (1) summary
      cd01492
      Location:13 → 345
      Aos1_SUMO; Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating enzyme (E1), specific for the SUMO family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to ...
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q06624.1

    Gene LinkOut

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

    Other Literature Sources
    Molecular Biology Databases
    Research Materials
    Tools
    Miscellaneous