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CANAL:HSP90

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Species (Taxon ID) Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast). (237561)
Gene Name(s) HSP90
Protein Name(s) Heat shock protein 90 homolog
External Links
UniProt P46598
EMBL X81025
AP006852
AACQ01000020
AACQ01000016
RefSeq XP_720840.1
XP_721353.1
XP_888823.1
ProteinModelPortal P46598
SMR P46598
BioGrid 1220601
STRING 5476.CAL0003079
BindingDB P46598
COMPLUYEAST-2DPAGE P46598
PRIDE P46598
GeneID 3636951
3637507
3704128
KEGG cal:CaO19.13868
cal:CaO19.6515
cal:CaO19_6515
CGD CAL0003079
eggNOG COG0326
InParanoid P46598
KO K04079
OrthoDB EOG7BP8B5
Proteomes UP000000559
GO GO:0009986
GO:0005737
GO:0009277
GO:0030446
GO:0016020
GO:0005886
GO:0005524
GO:0042623
GO:0006200
GO:0035690
GO:0034605
GO:0030447
GO:0044182
GO:0030518
GO:1900429
GO:0009405
GO:0006457
GO:0042981
Gene3D 3.30.565.10
HAMAP MF_00505
InterPro IPR003594
IPR019805
IPR001404
IPR020575
IPR020568
PANTHER PTHR11528
Pfam PF02518
PF00183
PIRSF PIRSF002583
PRINTS PR00775
SMART SM00387
SUPFAM SSF54211
SSF55874
PROSITE PS00298

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0048523

negative regulation of cellular process

PMID:23300438[1]

ECO:0000314

P

Hsf1 downregulats Hsp90 in C.albicans as shown in figure 1 by Western Blot

complete
CACAO 9290

enables

GO:0051082

unfolded protein binding

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0001233
PANTHER:PTN000163629
PomBase:SPAC926.04c
SGD:S000004798
SGD:S000006161

F

Seeded From UniProt

complete

involved_in

GO:0050821

protein stabilization

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000163629
UniProtKB:P07900
UniProtKB:P11501

P

Seeded From UniProt

complete

GO:0080135

regulation of cellular response to stress

PMID:23300438[1]

ECO:0000314

P

Hsp90 in C. albicans regulates the stress response of the cells (heat shock and non-heat shock). In figure 8, Hsp90 was depleted from the cell using the drug doxycycline. When Hsp90 was depleted, the cells were less stress resistance. The stress resistance was measured by CFU (Colony-forming Unit) measurement.

complete
CACAO 9301

part_of

GO:0048471

perinuclear region of cytoplasm

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0001233
MGI:MGI:96250
PANTHER:PTN000163629
RGD:631409
WB:WBGene00000915

C

Seeded From UniProt

complete

GO:0048523

negative regulation of cellular process

PMID:23300438[1]

ECO:0000314

P

Hsp90 in C. albicans down-regulates Hsp104 under heat shock conditions as shown in Figure 1. Hsp90 was depleted using doxycycline and mRNA levels were measured through Western Blot.

complete
CACAO 9296

enables

GO:0042623

ATPase activity, coupled

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000201062
PANTHER:PTN000898156
SGD:S000006161

F

Seeded From UniProt

complete

involved_in

GO:0034605

cellular response to heat

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000201062
PANTHER:PTN000163629
SGD:S000004798

P

Seeded From UniProt

complete

part_of

GO:0032991

protein-containing complex

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000163629
RGD:631409
UniProtKB:P07900
UniProtKB:P11501
WB:WBGene00000915

C

Seeded From UniProt

complete

part_of

GO:0009986

cell surface

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000201062
PANTHER:PTN000163629
RGD:631409
UniProtKB:P11501

C

Seeded From UniProt

complete

involved_in

GO:0009408

response to heat

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000201062
FB:FBgn0001233
PANTHER:PTN000163629
RGD:631409
SGD:S000004798
UniProtKB:P11501

P

Seeded From UniProt

complete

part_of

GO:0009277

fungal-type cell wall

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000201062
PANTHER:PTN000898156
UniProtKB:P40292

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000201062
MGI:MGI:96250
PANTHER:PTN000163629
RGD:631409
TAIR:locus:2161775
TAIR:locus:2161790
UniProtKB:P11501

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:96250
PANTHER:PTN000163629
RGD:631409
TAIR:locus:2161775
UniProtKB:P11501
UniProtKB:P40292
dictyBase:DDB_G0267400

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000201062
FB:FBgn0001233
MGI:MGI:96250
PANTHER:PTN000163629
RGD:631409
SGD:S000006161
TAIR:locus:2161775
TAIR:locus:2161790
UniProtKB:P07900
UniProtKB:P11501
UniProtKB:P40292
UniProtKB:Q76LV2
UniProtKB:Q8I0V4
WB:WBGene00000915
ZFIN:ZDB-GENE-990415-94
dictyBase:DDB_G0267400

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000898156
PomBase:SPAC926.04c

F

Seeded From UniProt

complete

involved_in

GO:1900429

negative regulation of filamentous growth of a population of unicellular organisms

PMID:22365851[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0044182

filamentous growth of a population of unicellular organisms

PMID:22365851[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0044182

filamentous growth of a population of unicellular organisms

PMID:22090345[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042981

regulation of apoptotic process

PMID:23028789[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042623

ATPase activity, coupled

PMID:10627043[6]

ECO:0000316

genetic interaction evidence used in manual assertion

SGD:S000004798
SGD:S000006161

F

Seeded From UniProt

complete

involved_in

GO:0035690

cellular response to drug

PMID:22365851[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0035690

cellular response to drug

PMID:19649312[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0035690

cellular response to drug

PMID:19196973[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0035690

cellular response to drug

PMID:16195452[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0034605

cellular response to heat

PMID:22365851[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0034605

cellular response to heat

PMID:7591093[10]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0030518

intracellular steroid hormone receptor signaling pathway

PMID:10627043[6]

ECO:0000316

genetic interaction evidence used in manual assertion

SGD:S000004798
SGD:S000006161

P

Seeded From UniProt

complete

involved_in

GO:0030447

filamentous growth

PMID:22365851[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0030447

filamentous growth

PMID:22090345[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0030447

filamentous growth

PMID:19327993[11]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0030446

hyphal cell wall

PMID:12782322[12]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

PMID:16534748[13]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0009986

cell surface

PMID:12782322[12]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0009405

pathogenesis

PMID:19327993[11]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009405

pathogenesis

PMID:19196973[8]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0009277

fungal-type cell wall

PMID:12661902[14]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

PMID:10627043[6]

ECO:0000316

genetic interaction evidence used in manual assertion

SGD:S000004798
SGD:S000006161

P

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:19824013[15]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:12661902[14]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001404
InterPro:IPR019805

F

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001404
InterPro:IPR019805

P

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001404
InterPro:IPR019805

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 1.2 Leach, MD et al. (2012) Hsp90 orchestrates transcriptional regulation by Hsf1 and cell wall remodelling by MAPK signalling during thermal adaptation in a pathogenic yeast. PLoS Pathog. 8 e1003069 PubMed GONUTS page
  2. ↑ 2.00 2.01 2.02 2.03 2.04 2.05 2.06 2.07 2.08 2.09 2.10 2.11 2.12 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  3. ↑ 3.0 3.1 3.2 3.3 3.4 Shapiro, RS et al. (2012) Pho85, Pcl1, and Hms1 signaling governs Candida albicans morphogenesis induced by high temperature or Hsp90 compromise. Curr. Biol. 22 461-70 PubMed GONUTS page
  4. ↑ 4.0 4.1 Senn, H et al. (2012) Cdc28 provides a molecular link between Hsp90, morphogenesis, and cell cycle progression in Candida albicans. Mol. Biol. Cell 23 268-83 PubMed GONUTS page
  5. ↑ Dai, B et al. (2012) Hsp90 is involved in apoptosis of Candida albicans by regulating the calcineurin-caspase apoptotic pathway. PLoS ONE 7 e45109 PubMed GONUTS page
  6. ↑ 6.0 6.1 6.2 Panaretou, B et al. (1999) The Hsp90 of Candida albicans can confer Hsp90 functions in Saccharomyces cerevisiae: a potential model for the processes that generate immunogenic fragments of this molecular chaperone in C. albicans infections. Microbiology (Reading, Engl.) 145 ( Pt 12) 3455-63 PubMed GONUTS page
  7. ↑ Singh, SD et al. (2009) Hsp90 governs echinocandin resistance in the pathogenic yeast Candida albicans via calcineurin. PLoS Pathog. 5 e1000532 PubMed GONUTS page
  8. ↑ 8.0 8.1 Cowen, LE et al. (2009) Harnessing Hsp90 function as a powerful, broadly effective therapeutic strategy for fungal infectious disease. Proc. Natl. Acad. Sci. U.S.A. 106 2818-23 PubMed GONUTS page
  9. ↑ Cowen, LE & Lindquist, S (2005) Hsp90 potentiates the rapid evolution of new traits: drug resistance in diverse fungi. Science 309 2185-9 PubMed GONUTS page
  10. ↑ Swoboda, RK et al. (1995) Structure and regulation of the HSP90 gene from the pathogenic fungus Candida albicans. Infect. Immun. 63 4506-14 PubMed GONUTS page
  11. ↑ 11.0 11.1 Shapiro, RS et al. (2009) Hsp90 orchestrates temperature-dependent Candida albicans morphogenesis via Ras1-PKA signaling. Curr. Biol. 19 621-9 PubMed GONUTS page
  12. ↑ 12.0 12.1 Urban, C et al. (2003) Identification of cell surface determinants in Candida albicans reveals Tsa1p, a protein differentially localized in the cell. FEBS Lett. 544 228-35 PubMed GONUTS page
  13. ↑ Insenser, M et al. (2006) Proteomic analysis of detergent-resistant membranes from Candida albicans. Proteomics 6 Suppl 1 S74-81 PubMed GONUTS page
  14. ↑ 14.0 14.1 Burt, ET et al. (2003) Isolation and partial characterization of Hsp90 from Candida albicans. Ann. Clin. Lab. Sci. 33 86-93 PubMed GONUTS page
  15. ↑ Cabezón, V et al. (2009) Analysis of Candida albicans plasma membrane proteome. Proteomics 9 4770-86 PubMed GONUTS page
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