Gene Ontology annotation through association of InterPro records with GO terms

Annotation inferences using phylogenetic trees

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

Gene Ontology annotation based on curation of immunofluorescence data

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara

Electronic Gene Ontology annotations created by ARBA machine learning models

Come forth CD1d: Hsp110 in the regulation of intestinal epithelial CD1d expression.

A novel HSF1-mediated death pathway that is suppressed by heat shock proteins.

MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis.

The diverse members of the mammalian HSP70 machine show distinct chaperone-like activities.

A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity.

Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro.

A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways.

Molecular cloning, expression and localization of human 105 kDa heat shock protein, hsp105.

SCARF1:ligand is endocytosed

HSP110s exchange ATP for ADP on HSP70s:ADP

Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s.

The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system.

Metazoan Hsp70 machines use Hsp110 to power protein disaggregation.

Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation.

Human and yeast Hsp110 chaperones exhibit functional differences.

Structure of the Hsp110:Hsc70 nucleotide exchange machine.

Hsp110 protects heat-denatured proteins and confers cellular thermoresistance.

Modulation of the chaperone activities of Hsc70/Hsp40 by Hsp105alpha and Hsp105beta.

Hsp105alpha suppresses Hsc70 chaperone activity by inhibiting Hsc70 ATPase activity.

Identification of alpha-tubulin as an hsp105alpha-binding protein by the yeast two-hybrid system.

Expression of a mutant HSP110 sensitizes colorectal cancer cells to chemotherapy and improves disease prognosis.

The distribution and localization of hsp110 in brain.

UniProtKB Q92598 (HS105_HUMAN) flat file

PAINT ancestral-node annotations for PANTHER family PTHR45639