HSP98 — Candida albicans

Summary

CR_08250C_A (HSP98, also known as HSP104) in Candida albicans encodes a protein with ATP-dependent protein disaggregase activity, misfolded protein binding, chaperone protein binding, ADP binding, identical protein binding, and ATP hydrolase activity. This gene is associated with cellular thermotolerance, response to heat, stress granule disassembly, protein stabilization and refolding, protein unfolding, translation termination, quorum sensing, sumoylation, nucleocytoplasmic transport, mycose metabolism, iron transport, cell cycle control, and biofilm formation. It localizes to the cytoplasm, cytosol, nucleus, nuclear periphery, nuclear envelope, protein aggregate center, and mitochondrial lumen. Phenotypic associations include abnormal chemical compound excretion, nitrogen source utilization, protein activity, prion inheritance and formation, biofilm formation, cell fusion, and anaerobic growth, with normal vegetative growth and acquired thermotolerance.

Annotations

Chromosome
8
Related genes
B0383, B4034, HSP98, hsp98, SES1, CIT1, HOF1, PIL1
GO terms
Cell Cycle, Cell Growth, Biofilm Formation, Secretion, Cellular Response To Misfolded Protein, Misfolded Protein Binding, ATP Binding, Nucleus
Publications
28357333, 19214209, 27840029, 34849884, 28520713, 22244335, 27571477, 22244334
Traits
RESISTANCE TO CHEMICALS: DECREASED, COMPETITIVE FITNESS: DECREASED, STRESS RESISTANCE: DECREASED, INVIABLE, RESISTANCE TO CHEMICALS: INCREASED, CELL CYCLE PROGRESSION: ABNORMAL, UTILIZATION OF CARBON SOURCE: INCREASED RATE, NUCLEAR POSITION: ABNORMAL