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SQS1 Sqs1p [ Saccharomyces cerevisiae S288C ]

Gene ID: 855497, updated on 18-Sep-2024

Summary

Official Symbol
SQS1
Official Full Name
Sqs1p
Primary source
SGD:S000005168
Locus tag
YNL224C
See related
AllianceGenome:SGD:S000005168; FungiDB:YNL224C; VEuPathDB:YNL224C
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
PFA1
Summary
Predicted to enable nucleic acid binding activity. Involved in RNA processing; positive regulation of ATPase activity; and positive regulation of helicase activity. Located in cytoplasm and nucleolus. Part of 90S preribosome; preribosome, large subunit precursor; and preribosome, small subunit precursor. Orthologous to human GPATCH2 (G-patch domain containing 2). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

See SQS1 in Genome Data Viewer
Location:
chromosome: XIV
Exon count:
1
Sequence:
Chromosome: XIV; NC_001146.8 (224796..227099, complement)

Chromosome XIV - NC_001146.8Genomic Context describing neighboring genes Neighboring gene Jjj1p Neighboring gene Cnm67p Neighboring gene cysteine protease ATG4 Neighboring gene RNA polymerase II subunit A C-terminal domain phosphatase

Bibliography

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables enzyme activator activity IDA
Inferred from Direct Assay
more info
PubMed 
enables enzyme activator activity IMP
Inferred from Mutant Phenotype
more info
PubMed 
enables nucleic acid binding IEA
Inferred from Electronic Annotation
more info
 
Process Evidence Code Pubs
involved_in RNA splicing IEA
Inferred from Electronic Annotation
more info
 
involved_in mRNA processing IEA
Inferred from Electronic Annotation
more info
 
involved_in mRNA splicing, via spliceosome IGI
Inferred from Genetic Interaction
more info
PubMed 
involved_in maturation of SSU-rRNA IGI
Inferred from Genetic Interaction
more info
PubMed 
involved_in rRNA processing IGI
Inferred from Genetic Interaction
more info
PubMed 
Component Evidence Code Pubs
part_of 90S preribosome IDA
Inferred from Direct Assay
more info
PubMed 
located_in cytoplasm HDA PubMed 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
 
located_in nucleolus HDA PubMed 
located_in nucleus HDA PubMed 
is_active_in nucleus IBA
Inferred from Biological aspect of Ancestor
more info
 
located_in nucleus IEA
Inferred from Electronic Annotation
more info
 
part_of preribosome, large subunit precursor IDA
Inferred from Direct Assay
more info
PubMed 
part_of preribosome, small subunit precursor IDA
Inferred from Direct Assay
more info
PubMed 

General protein information

Preferred Names
Sqs1p
NP_014175.1
  • Protein that stimulates the ATPase and helicase activities of Prp43p; acts with Prp43p to stimulate 18s rRNA maturation by Nob1p; overexpression antagonizes the suppression of splicing defects by spp382 mutants; component of pre-ribosomal particles; relocalizes from nucleus to nucleolus upon DNA replication stress

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_001146.8 Reference assembly

    Range
    224796..227099 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001183062.1NP_014175.1  TPA: Sqs1p [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_014175.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    A6ZRL6, D6W0W6, P53866
    UniProtKB/TrEMBL
    B3LP68, N1NY27
    Conserved Domains (2) summary
    cd02646
    Location:597654
    R3H_G-patch; R3H domain of a group of fungal and plant proteins with unknown function, who also contain a G-patch domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the R3H ...
    pfam01585
    Location:721764
    G-patch; G-patch domain