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    UBA2 E1 ubiquitin-activating protein UBA2 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 851998, updated on 2-Nov-2024

    Summary

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    Official Symbol
    UBA2
    Official Full Name
    E1 ubiquitin-activating protein UBA2
    Primary source
    SGD:S000002798
    Locus tag
    YDR390C
    See related
    AllianceGenome:SGD:S000002798; FungiDB:YDR390C; VEuPathDB:YDR390C
    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
    UAL1
    Summary
    Contributes to SUMO activating enzyme activity. Involved in protein sumoylation. Located in nucleus. Part of SUMO activating enzyme complex. Orthologous to human UBA2 (ubiquitin like modifier activating enzyme 2). [provided by Alliance of Genome Resources, Nov 2024]
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    Genomic context

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    See UBA2 in Genome Data Viewer
    Location:
    chromosome: IV
    Exon count:
    1
    Sequence:
    Chromosome: IV; NC_001136.10 (1254937..1256847, complement)

    Chromosome IV - NC_001136.10Genomic Context describing neighboring genes Neighboring gene amphiphysin Neighboring gene GTPase-activating protein SAC7 Neighboring gene tRNA-Gly Neighboring gene uncharacterized protein

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001136.10

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. NMR assignments of ubiquitin fold domain (UFD) in SUMO-activating enzyme subunit 2 from rice. Suzuki R, et al. Biomol NMR Assign, 2011 Oct. PMID 21523438
    2. An essential yeast gene encoding a homolog of ubiquitin-activating enzyme. Dohmen RJ, et al. J Biol Chem, 1995 Jul 28. PMID 7629121
    3. Identification of a multifunctional binding site on Ubc9p required for Smt3p conjugation. Bencsath KP, et al. J Biol Chem, 2002 Dec 6. PMID 12354763
    4. Purification of SUMO conjugating enzymes and kinetic analysis of substrate conjugation. Yunus AA, et al. Methods Mol Biol, 2009. PMID 19107417, Free PMC Article
    5. UBC9 autosumoylation negatively regulates sumoylation of septins in Saccharomyces cerevisiae. Ho CW, et al. J Biol Chem, 2011 Jun 17. PMID 21518767, Free PMC Article

    See all (54) citations in PubMed

    GeneRIFs: Gene References Into Functions

    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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    Homology

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    contributes_to SUMO activating enzyme activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables SUMO activating enzyme activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    contributes_to SUMO activating enzyme activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables zinc ion binding RCA
    inferred from Reviewed Computational Analysis
    more info
    		 PubMed 
    Process Evidence Code Pubs
    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 
    involved_in protein sumoylation IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein sumoylation IMP
    Inferred from Mutant Phenotype
    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 nucleus IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in nucleus IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    E1 ubiquitin-activating protein UBA2
    NP_010678.3
    • Subunit of heterodimeric nuclear SUMO activating enzyme E1 with Aos1p; activates Smt3p (SUMO) before its conjugation to proteins (sumoylation), which may play a role in protein targeting; essential for viability

    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_001136.10 Reference assembly

      Range
      1254937..1256847 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001180698.3 → NP_010678.3  TPA: E1 ubiquitin-activating protein UBA2 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_010678.3

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VT24, P52488
      UniProtKB/TrEMBL
      B3LFR0, B5VGS0, C7GSD2, C8Z5V4, N1PAJ2
      Conserved Domains (3) summary
      cd01489
      Location:23 → 438
      Uba2_SUMO; Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 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 ...
      pfam10585
      Location:183 → 370
      UBA_e1_thiolCys; Ubiquitin-activating enzyme active site
      cl39046
      Location:453 → 518
      UAE_UbL; Ubiquitin/SUMO-activating enzyme ubiquitin-like domain
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P52488.1

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