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SCHPO:HSP90

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Species (Taxon ID) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). (284812)
Gene Name(s) swo1 (synonyms: hsp90)
Protein Name(s) Heat shock protein 90 homolog
External Links
UniProt P41887
EMBL L35550
CU329670
PIR S51795
T39202
RefSeq NP_594365.1
ProteinModelPortal P41887
SMR P41887
BioGrid 279956
IntAct P41887
STRING 4896.SPAC926.04c.1
iPTMnet P41887
MaxQB P41887
PaxDb P41887
PRIDE P41887
EnsemblFungi SPAC926.04c.1
GeneID 2543539
KEGG spo:SPAC926.04c
EuPathDB FungiDB:SPAC926.04c
PomBase SPAC926.04c
HOGENOM HOG000031988
InParanoid P41887
KO K04079
OMA VKRHSEF
PhylomeDB P41887
Reactome R-SPO-3371497
R-SPO-3371571
R-SPO-6798695
R-SPO-844456
PRO PR:P41887
Proteomes UP000002485
GO GO:0009986
GO:0005737
GO:0005829
GO:0009277
GO:0005739
GO:0048471
GO:0005886
GO:0032991
GO:0005524
GO:0016887
GO:0042623
GO:0051082
GO:0006458
GO:0034605
GO:0061077
GO:0070924
GO:0006457
GO:0050821
GO:0009408
CDD cd00075
Gene3D 1.20.120.790
3.30.565.10
HAMAP MF_00505
InterPro IPR003594
IPR036890
IPR019805
IPR037196
IPR001404
IPR020575
IPR020568
PANTHER PTHR11528
Pfam PF02518
PF00183
PIRSF PIRSF002583
PRINTS PR00775
SMART SM00387
SUPFAM SSF110942
SSF54211
SSF55874
PROSITE PS00298

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0061077

chaperone-mediated protein folding

PMID:23664927[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Fig. 6 shows the addition of Hsp90 resulted in the refolding of denatured luciferase. Amount refolded was measured through a measurment of bioluminescence.

complete
CACAO 8907

GO:0016887

ATPase activity

PMID:23664927[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Fig. 4 shows ATPase activity of Hsp90 under conditions of high temperature with and without co-chaperones.

complete
CACAO 8909

GO:0051085

chaperone cofactor-dependent protein refolding

PMID:23664927[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Fig. 4 shows ATPase activity of Hsp90 under conditions of high temperature with and without co-chaperones.

complete
CACAO 9106

enables

GO:0016887

ATPase activity

PMID:23664927[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0061077

chaperone-mediated protein folding

PMID:23664927[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0070924

heterochromatin assembly involved in chromatin silencing by small RNA

PMID:29866182[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0061077

chaperone-mediated protein folding

GO_REF:0000051

ECO:0000303

author statement without traceable support used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:23664927[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0016887

ATPase activity

PMID:23664927[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006458

'de novo' protein folding

GO_REF:0000024

ECO:0000266

sequence orthology evidence used in manual assertion

SGD:S000006161

P

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

PMID:11791728[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

PMID:23664927[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:16823372[4]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

GO_REF:0000024

ECO:0000266

sequence orthology evidence used in manual assertion

SGD:S000004798

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

PMID:23664927[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0001233
PANTHER:PTN000163527
PomBase:SPAC926.04c
SGD:S000004798
SGD:S000006161

F

Seeded From UniProt

complete

involved_in

GO:0050821

protein stabilization

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000163629
UniProtKB:P07900
UniProtKB:P11501

P

Seeded From UniProt

complete

part_of

GO:0048471

perinuclear region of cytoplasm

PMID:21873635[5]

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

enables

GO:0042623

ATPase activity, coupled

PMID:21873635[5]

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[5]

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[5]

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[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

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

C

Seeded From UniProt

complete

part_of

GO:0009277

fungal-type cell wall

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000201062
PANTHER:PTN000898156
UniProtKB:P40292

C

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000201062
EcoGene:EG10461
PANTHER:PTN000163527
PomBase:SPAC926.04c
SGD:S000004798
SGD:S000006161
WB:WBGene00000915

P

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:21873635[5]

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[5]

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[5]

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[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000898156
PomBase:SPAC926.04c

F

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

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

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

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

edit table

Notes

References

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

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 1.8 Ishida, M et al. (2013) Biochemical characterization and cooperation with co-chaperones of heat shock protein 90 from Schizosaccharomyces pombe. J. Biosci. Bioeng. 116 444-8 PubMed GONUTS page
  2. ↑ Okazaki, K et al. (2018) RNAi-dependent heterochromatin assembly in fission yeast Schizosaccharomyces pombe requires heat-shock molecular chaperones Hsp90 and Mas5. Epigenetics Chromatin 11 26 PubMed GONUTS page
  3. ↑ Ki, SW et al. (2001) Radicicol binding to Swo1/Hsp90 and inhibition of growth of specific temperature-sensitive cell cycle mutants of fission yeast. Biosci. Biotechnol. Biochem. 65 2528-34 PubMed GONUTS page
  4. ↑ Matsuyama, A et al. (2006) ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe. Nat. Biotechnol. 24 841-7 PubMed GONUTS page
  5. ↑ 5.00 5.01 5.02 5.03 5.04 5.05 5.06 5.07 5.08 5.09 5.10 5.11 5.12 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
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