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SSA4 Hsp70 family chaperone SSA4 [ Saccharomyces cerevisiae S288C ]

Gene ID: 856840, updated on 8-Oct-2017
Gene symbol
SSA4
Gene description
Hsp70 family chaperone SSA4
Primary source
SGD:S000000905
Locus tag
YER103W
Gene type
protein coding
RNA name
Hsp70 family chaperone SSA4
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288c)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as
YG107
See SSA4 in Map Viewer
Location:
chromosome: V
Exon count:
1
Sequence:
Chromosome: V; NC_001137.3 (364589..366517)

Chromosome V - NC_001137.3Genomic Context describing neighboring genes Neighboring gene Ast2p Neighboring gene ribosomal 40S subunit protein S8B Neighboring gene Rtt105p Neighboring gene Nup157p

  • Endocytosis, organism-specific biosystem (from KEGG)
    Endocytosis, organism-specific biosystemEndocytosis is a mechanism for cells to remove ligands, nutrients, and plasma membrane (PM) proteins, and lipids from the cell surface, bringing them into the cell interior. Transmembrane proteins en...
  • Endocytosis, conserved biosystem (from KEGG)
    Endocytosis, conserved biosystemEndocytosis is a mechanism for cells to remove ligands, nutrients, and plasma membrane (PM) proteins, and lipids from the cell surface, bringing them into the cell interior. Transmembrane proteins en...
  • Longevity regulating pathway - multiple species, organism-specific biosystem (from KEGG)
    Longevity regulating pathway - multiple species, organism-specific biosystemAging is a complex process of accumulation of molecular, cellular, and organ damage, leading to loss of function and increased vulnerability to disease and death. Despite the complexity of aging, rec...
  • Longevity regulating pathway - multiple species, conserved biosystem (from KEGG)
    Longevity regulating pathway - multiple species, conserved biosystemAging is a complex process of accumulation of molecular, cellular, and organ damage, leading to loss of function and increased vulnerability to disease and death. Despite the complexity of aging, rec...
  • Protein processing in endoplasmic reticulum, organism-specific biosystem (from KEGG)
    Protein processing in endoplasmic reticulum, organism-specific biosystemThe endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylate...
  • Protein processing in endoplasmic reticulum, conserved biosystem (from KEGG)
    Protein processing in endoplasmic reticulum, conserved biosystemThe endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylate...
  • Spliceosome, organism-specific biosystem (from KEGG)
    Spliceosome, organism-specific biosystemAfter transcription, eukaryotic mRNA precursors contain protein-coding exons and noncoding introns. In the following splicing, introns are excised and exons are joined by a macromolecular complex, th...
  • Spliceosome, conserved biosystem (from KEGG)
    Spliceosome, conserved biosystemAfter transcription, eukaryotic mRNA precursors contain protein-coding exons and noncoding introns. In the following splicing, introns are excised and exons are joined by a macromolecular complex, th...
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by GO

Function Evidence Code Pubs
ATP binding IEA
Inferred from Electronic Annotation
more info
 
ATPase activity ISS
Inferred from Sequence or Structural Similarity
more info
PubMed 
nucleotide binding IEA
Inferred from Electronic Annotation
more info
 
unfolded protein binding IGI
Inferred from Genetic Interaction
more info
PubMed 
unfolded protein binding ISS
Inferred from Sequence or Structural Similarity
more info
PubMed 
Process Evidence Code Pubs
SRP-dependent cotranslational protein targeting to membrane, translocation IMP
Inferred from Mutant Phenotype
more info
PubMed 
cellular response to heat IEP
Inferred from Expression Pattern
more info
PubMed 
protein folding IGI
Inferred from Genetic Interaction
more info
PubMed 
Component Evidence Code Pubs
cytoplasm IDA
Inferred from Direct Assay
more info
PubMed 
cytoplasm IEA
Inferred from Electronic Annotation
more info
 
nucleus IDA
Inferred from Direct Assay
more info
PubMed 
Names
Hsp70 family chaperone SSA4
NP_011029.3
  • Heat shock protein that is highly induced upon stress; plays a role in SRP-dependent cotranslational protein-membrane targeting and translocation; member of the HSP70 family; cytoplasmic protein that concentrates in nuclei upon starvation; SSA4 has a paralog, SSA3, that arose from the whole genome duplication

Genome Annotation

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

Reference assembly

Genomic

  1. NC_001137.3 Reference assembly

    Range
    364589..366517
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001178994.3NP_011029.3  TPA: Hsp70 family chaperone SSA4 [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_011029.3

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    P22202
    Conserved Domains (2) summary
    cd10233
    Location:4379
    HSPA1-2_6-8-like_NBD; Nucleotide-binding domain of HSPA1-A, -B, -L, HSPA-2, -6, -7, -8, and similar proteins
    PTZ00009
    Location:4642
    PTZ00009; heat shock 70 kDa protein; Provisional
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