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    GUK1 guanylate kinase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 852065, updated on 9-Dec-2024

    Summary

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    Official Symbol
    GUK1
    Official Full Name
    guanylate kinase
    Primary source
    SGD:S000002862
    Locus tag
    YDR454C
    See related
    AllianceGenome:SGD:S000002862; FungiDB:YDR454C; VEuPathDB:YDR454C
    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
    BRA3; PUR5
    Summary
    Enables guanylate kinase activity. Involved in GDP biosynthetic process. Located in cytoplasm and nucleus. Used to study cancer. Orthologous to human GUK1 (guanylate kinase 1). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See GUK1 in Genome Data Viewer
    Location:
    chromosome: IV
    Exon count:
    1
    Sequence:
    Chromosome: IV; NC_001136.10 (1366264..1366827, complement)

    Chromosome IV - NC_001136.10Genomic Context describing neighboring genes Neighboring gene endopolyphosphatase Neighboring gene thioredoxin peroxidase TSA2 Neighboring gene bifunctional K:H/Na:H antiporter NHX1 Neighboring gene E3 ubiquitin-protein ligase TOM1

    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. Refined structure of the complex between guanylate kinase and its substrate GMP at 2.0 A resolution. Stehle T, et al. J Mol Biol, 1992 Apr 20. PMID 1314905
    2. Asymmetric effect of mechanical stress on the forward and reverse reaction catalyzed by an enzyme. Joseph C, et al. PLoS One, 2014. PMID 25000118, Free PMC Article
    3. Productive versus unproductive nucleotide binding in yeast guanylate kinase mutants: comparison of R41M with K14M by proton two dimensional transferred NOESY. Ray BD, et al. Biochemistry, 2009 Jun 23. PMID 19419194, Free PMC Article
    4. Conformations of nucleotides bound to wild type and Y78F mutant yeast guanylate kinase: proton two-dimensional transferred NOESY measurements. Ray BD, et al. Biochemistry, 2005 Oct 25. PMID 16229466
    5. Liposomes for microcompartmentation of enzymes and their influence on catalytic activity. Wichmann C, et al. Biochem Biophys Res Commun, 2003 Oct 31. PMID 14559229

    See all (53) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. In addition to the E3 ubiquitin ligase Ubr1, we identified the prefoldin chaperone subunit Gim3 as an important quality control factor. We found that Gim3 interacted with the Guk1 mutant allele and propose that prefoldin promotes the degradation of the unstable model substrate by maintaining the solubility of the misfolded protein
      Title: Prefoldin Promotes Proteasomal Degradation of Cytosolic Proteins with Missense Mutations by Maintaining Substrate Solubility.
    2. forward and reverse kinetics of the enzyme Guanylate Kinase from yeast
      Title: Asymmetric effect of mechanical stress on the forward and reverse reaction catalyzed by an enzyme.
    3. Productive versus unproductive nucleotide binding in yeast guanylate kinase mutants: comparison of R41M with K14M by proton two dimensional transferred NOESY
      Title: Productive versus unproductive nucleotide binding in yeast guanylate kinase mutants: comparison of R41M with K14M by proton two dimensional transferred NOESY.
    Submit: New GeneRIF Correction

    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
    		  
    enables guanylate kinase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables guanylate kinase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables guanylate kinase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables guanylate kinase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables kinase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in GDP biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in GMP metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in purine nucleotide metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in nucleus HDA PubMed 

    General protein information

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    Preferred Names
    guanylate kinase
    NP_010742.1
    • Guanylate kinase; converts GMP to GDP; required for growth and mannose outer chain elongation of cell wall N-linked glycoproteins

    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
      1366264..1366827 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001180762.1 → NP_010742.1  TPA: guanylate kinase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_010742.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VT79, P15454
      UniProtKB/TrEMBL
      A6ZZ45, B3LFK9, B5VGY4, C7GKP6, C8Z612, G2WBI5, N1P8Y7
      Conserved Domains (1) summary
      TIGR03263
      Location:3 → 185
      guanyl_kin; guanylate kinase
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P15454.2

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