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GUK1 guanylate kinase [ Saccharomyces cerevisiae S288C ]

Gene ID: 852065, updated on 14-Nov-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, Nov 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

Gene LinkOut

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