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GLC7 type 1 serine/threonine-protein phosphatase catalytic subunit GLC7 [ Saccharomyces cerevisiae S288C ]

Gene ID: 856870, updated on 30-Jul-2025

In addition, your package will include a detailed data report in both TSV and JSONL formats.

Official Symbol
GLC7
Official Full Name
type 1 serine/threonine-protein phosphatase catalytic subunit GLC7
Primary source
SGD:S000000935
Locus tag
YER133W
See related
AllianceGenome:SGD:S000000935; FungiDB:YER133W; VEuPathDB:YER133W
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
CID1; DIS2
Summary
Enables protein serine/threonine phosphatase activity. Involved in several processes, including DNA metabolic process; negative regulation of cell cycle phase transition; and positive regulation of cellular component organization. Acts upstream of or within positive regulation of exit from mitosis. Located in several cellular components, including kinetochore; mating projection base; and spindle pole body. Part of mRNA cleavage and polyadenylation specificity factor complex and protein phosphatase type 1 complex. Used to study cancer. Human ortholog(s) of this gene implicated in Noonan syndrome-like disorder with loose anagen hair 2. Orthologous to several human genes including PPP1CA (protein phosphatase 1 catalytic subunit alpha) and PPP1CC (protein phosphatase 1 catalytic subunit gamma). [provided by Alliance of Genome Resources, Jul 2025]
Orthologs
all
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See GLC7 in Genome Data Viewer
Location:
chromosome: V
Exon count:
2
Sequence:
Chromosome: V; NC_001137.3 (432495..433958)

Chromosome V - NC_001137.3Genomic Context describing neighboring genes

Genomic Sequence:
NC_001137.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Cellular mechanisms regulating protein phosphatase-1. A key functional interaction between inhibitor-2 and the type 1 protein phosphatase catalytic subunit. Connor JH, et al. J Biol Chem, 2000 Jun 23. PMID 10748125
  2. The Glc7 type 1 protein phosphatase of Saccharomyces cerevisiae is required for cell cycle progression in G2/M. Hisamoto N, et al. Mol Cell Biol, 1994 May. PMID 8164671, Free PMC Article
  3. Function of protein phosphatase-1, Glc7, in Saccharomyces cerevisiae. Cannon JF. Adv Appl Microbiol, 2010. PMID 20800758
  4. Expression of human protein phosphatase-1 in Saccharomyces cerevisiae highlights the role of phosphatase isoforms in regulating eukaryotic functions. Gibbons JA, et al. J Biol Chem, 2007 Jul 27. PMID 17545157
  5. Proteins interacting with Saccharomyces cerevisiae type 1 protein phosphatase catalytic subunit identified by single-step affinity purification and mass spectrometry. Walsh EP, et al. Methods Mol Biol, 2007. PMID 17200566

See all (253) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Analog-sensitive Cdk1 as a tool to study mitotic exit: protein phosphatase 1 is required downstream from Cdk1 inactivation in budding yeast.
    Title: Analog-sensitive Cdk1 as a tool to study mitotic exit: protein phosphatase 1 is required downstream from Cdk1 inactivation in budding yeast.
  2. Protein phosphatase 1 in association with Bud14 inhibits mitotic exit in Saccharomyces cerevisiae.
    Title: Protein phosphatase 1 in association with Bud14 inhibits mitotic exit in Saccharomyces cerevisiae.
  3. recruitment of PP1 to Spc105/Knl1 is carefully regulated to ensure that chromosome biorientation precedes SAC silencing, thereby ensuring accurate chromosome segregation
    Title: Delineating the contribution of Spc105-bound PP1 to spindle checkpoint silencing and kinetochore microtubule attachment regulation.
  4. While ubiquitylation likely regulates Ipl1 protein stability via the canonical proteasomal degradation pathway, a non-canonical ubiquitin-dependent pathway maintains normal Glc7 localization and activity.
    Title: New ubiquitin-dependent mechanisms regulating the Aurora B-protein phosphatase 1 balance in Saccharomyces cerevisiae.
  5. Rif1 controls telomere length by recruiting PP1 to directly suppress telomerase-mediated TG repeat lengthening.
    Title: Rif1 acts through Protein Phosphatase 1 but independent of replication timing to suppress telomere extension in budding yeast.
  6. Genetic analysis suggests that a Gip1-Glc7 phosphatase complex regulates prospore membrane extension in parallel to the previously reported Vps13, Spo71, Spo73 pathway.
    Title: Dynamic localization of a yeast development-specific PP1 complex during prospore membrane formation is dependent on multiple localization signals and complex formation.
  7. We deleted the novel intronic RNA structure within the GLC7 intron and showed that this region, rather than the intron itself, is responsible for the cell's ability to respond to salt stress. We also showed a direct association between the in cis presence of the intronic RNA and GLC7 expression
    Title: Novel Intronic RNA Structures Contribute to Maintenance of Phenotype in Saccharomyces cerevisiae.
  8. These data suggest that the repression of origin activation by Rif1-Glc7 is important to avoid the deleterious accumulation of stalled replication forks at the rDNA RFB, which become lethal when fork stability is compromised. Finally, we show that Rif1-Glc7, unlike Sir2, has an important effect on origin firing outside of the rDNA locus that serves to prevent activation of the DNA replication checkpoint
    Title: Budding Yeast Rif1 Controls Genome Integrity by Inhibiting rDNA Replication.
  9. Data link Rif1 to negative regulation of replication origin firing through recruitment of the Glc7 phosphatase.
    Title: Rif1 controls DNA replication timing in yeast through the PP1 phosphatase Glc7.
  10. Replacement of the N terminus of eIF2gamma with the GLC7-binding domain from GAC1 or fusion of heterologous dimerization domains to eIF2gamma and GLC7, respectively, maintained eIF2alpha phosphorylation at basal levels
    Title: Protein phosphatase PP1/GLC7 interaction domain in yeast eIF2γ bypasses targeting subunit requirement for eIF2α dephosphorylation.
Products Interactant Other Gene Complex Source Pubs Description

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
enables phosphoprotein phosphatase activity IEA
Inferred from Electronic Annotation
more info
enables protein binding IPI
Inferred from Physical Interaction
more info
PubMed
enables protein serine/threonine phosphatase activity IBA
Inferred from Biological aspect of Ancestor
more info
enables protein serine/threonine phosphatase activity IDA
Inferred from Direct Assay
more info
PubMed
enables protein serine/threonine phosphatase activity IEA
Inferred from Electronic Annotation
more info
Process Evidence Code Pubs
involved_in DNA damage checkpoint signaling IMP
Inferred from Mutant Phenotype
more info
PubMed
involved_in DNA replication checkpoint signaling IGI
Inferred from Genetic Interaction
more info
PubMed
involved_in DNA replication checkpoint signaling IMP
Inferred from Mutant Phenotype
more info
PubMed
involved_in ascospore formation IMP
Inferred from Mutant Phenotype
more info
PubMed
involved_in cell division IEA
Inferred from Electronic Annotation
more info
involved_in cellular bud site selection NAS
Non-traceable Author Statement
more info
PubMed
involved_in chitin biosynthetic process IDA
Inferred from Direct Assay
more info
PubMed
involved_in chromosome organization NAS
Non-traceable Author Statement
more info
PubMed
involved_in chromosome segregation IBA
Inferred from Biological aspect of Ancestor
more info
involved_in chromosome segregation IMP
Inferred from Mutant Phenotype
more info
PubMed
involved_in glycogen metabolic process IEA
Inferred from Electronic Annotation
more info
involved_in intracellular monoatomic ion homeostasis IMP
Inferred from Mutant Phenotype
more info
PubMed
involved_in mRNA processing IEA
Inferred from Electronic Annotation
more info
involved_in meiotic cell cycle IPI
Inferred from Physical Interaction
more info
PubMed
involved_in mitotic spindle assembly checkpoint signaling IMP
Inferred from Mutant Phenotype
more info
PubMed
involved_in negative regulation of actin filament polymerization NAS
Non-traceable Author Statement
more info
PubMed
involved_in positive regulation of clathrin-dependent endocytosis IGI
Inferred from Genetic Interaction
more info
PubMed
acts_upstream_of_or_within positive regulation of exit from mitosis IGI
Inferred from Genetic Interaction
more info
PubMed
involved_in positive regulation of mitotic actomyosin contractile ring assembly IMP
Inferred from Mutant Phenotype
more info
PubMed
involved_in positive regulation of transcription by RNA polymerase II NAS
Non-traceable Author Statement
more info
PubMed
involved_in protein localization to kinetochore IMP
Inferred from Mutant Phenotype
more info
PubMed
involved_in regulation of cell budding IMP
Inferred from Mutant Phenotype
more info
PubMed
involved_in regulation of cell cycle IMP
Inferred from Mutant Phenotype
more info
PubMed
involved_in regulation of cell shape IGI
Inferred from Genetic Interaction
more info
PubMed
involved_in regulation of cellular response to glucose starvation NAS
Non-traceable Author Statement
more info
PubMed
involved_in regulation of glycogen biosynthetic process NAS
Non-traceable Author Statement
more info
PubMed
involved_in regulation of glycogen metabolic process IMP
Inferred from Mutant Phenotype
more info
PubMed
involved_in regulation of mitotic cell cycle IBA
Inferred from Biological aspect of Ancestor
more info
involved_in regulation of mitotic cell cycle IMP
Inferred from Mutant Phenotype
more info
PubMed
involved_in regulation of protein localization to cell division site involved in cytokinesis IMP
Inferred from Mutant Phenotype
more info
PubMed
involved_in replication fork processing IMP
Inferred from Mutant Phenotype
more info
PubMed
involved_in response to heat IMP
Inferred from Mutant Phenotype
more info
PubMed
involved_in response to unfolded protein IMP
Inferred from Mutant Phenotype
more info
PubMed
involved_in telomere maintenance IGI
Inferred from Genetic Interaction
more info
PubMed
involved_in termination of RNA polymerase II transcription, poly(A)-coupled NAS
Non-traceable Author Statement
more info
PubMed
Component Evidence Code Pubs
located_in cell division site IDA
Inferred from Direct Assay
more info
PubMed
located_in cellular bud neck IDA
Inferred from Direct Assay
more info
PubMed
located_in cellular bud neck septin collar IDA
Inferred from Direct Assay
more info
PubMed
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
located_in incipient cellular bud site IDA
Inferred from Direct Assay
more info
PubMed
located_in kinetochore IDA
Inferred from Direct Assay
more info
PubMed
part_of mRNA cleavage and polyadenylation specificity factor complex IDA
Inferred from Direct Assay
more info
PubMed
part_of mRNA cleavage and polyadenylation specificity factor complex IPI
Inferred from Physical Interaction
more info
PubMed
located_in mating projection base IDA
Inferred from Direct Assay
more info
PubMed
located_in nucleolus IDA
Inferred from Direct Assay
more info
PubMed
is_active_in nucleus 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
located_in nucleus NAS
Non-traceable Author Statement
more info
PubMed
part_of protein phosphatase type 1 complex IDA
Inferred from Direct Assay
more info
PubMed
part_of protein phosphatase type 1 complex IEA
Inferred from Electronic Annotation
more info
part_of protein phosphatase type 1 complex IPI
Inferred from Physical Interaction
more info
PubMed
located_in spindle pole body IDA
Inferred from Direct Assay
more info
PubMed
Preferred Names
type 1 serine/threonine-protein phosphatase catalytic subunit GLC7
NP_011059.3
  • Type 1 S/T protein phosphatase (PP1) catalytic subunit; involved in glycogen metabolism, sporulation and mitotic progression; interacts with multiple regulatory subunits; regulates actomyosin ring formation; subunit of CPF; recruited to mating projections by Afr1p interaction; regulates nucleocytoplasmic shuttling of Hxk2p; import into the nucleus is inhibited during spindle assembly checkpoint arrest; involved in dephosphorylating Rps6a/b and Bnr1p

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Genome Annotation

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

This section includes genomic Reference Sequences (RefSeqs) from all assemblies on which this gene is annotated, such as RefSeqs for chromosomes and scaffolds (contigs) from both reference and alternate assemblies. Model RNAs and proteins are also reported here.

Reference assembly

Genomic

  1. NC_001137.3 Reference assembly

    Range
    432495..433958
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001179023.3NP_011059.3 TPA: type 1 serine/threonine-protein phosphatase catalytic subunit GLC7

    See identical proteins and their annotated locations for NP_011059.3

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D3DM39, P32598
    UniProtKB/TrEMBL
    A6ZR87, B3LRP8, C7GKX9, C8Z7F0, G2WCZ2, N1P3L5
    Conserved Domains (1) summary
    cd07414
    Location:7297
    MPP_PP1_PPKL; PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P32598.1

Gene LinkOut

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Molecular Biology Databases
Research Materials

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