Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods
Cer1p functions as a molecular chaperone in the endoplasmic reticulum of Saccharomyces cerevisiae.
Coordinated activation of Hsp70 chaperones.
An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell.
Nucleotide binding by Lhs1p is essential for its nucleotide exchange activity and for function in vivo.
The Lhs1/GRP170 chaperones facilitate the endoplasmic reticulum-associated degradation of the epithelial sodium channel.
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Yeast Lhs1 is required for maximal ERAD turnover of alphaENaC in a holdase-linked manner.
"a conserved Hsp70-like chaperone, Lhs1, is required for maximal turnover"
CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abundance and cell-cycle progression.
Lhs1 dependent ERAD is determined by transmembrane domain context.
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Lhs1 selects a subset of Hrd1-dependent ERAD substrates whose dependence is determined by transmembrane-domain context.
"Lhs1 is required for a subset of ERAD substrates that also require the Hrd1 ubiquitin ligase."
One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy.
A novel Hsp70 of the yeast ER lumen is required for the efficient translocation of a number of protein precursors.
SSI1 encodes a novel Hsp70 of the Saccharomyces cerevisiae endoplasmic reticulum.
The Hsp70 homologue Lhs1p is involved in a novel function of the yeast endoplasmic reticulum, refolding and stabilization of heat-denatured protein aggregates.
Falcon deep research synthesis for LHS1
PANTHER family PTHR45639 Hsp70/Hsp110 metadata
Gene Ontology annotation through association of InterPro records with GO terms