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DANRE:H90A1

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Species (Taxon ID) Danio rerio (Zebrafish) (Brachydanio rerio). (7955)
Gene Name(s) hsp90a.1 (synonyms: hsp90, hsp90a, hsp90aa1)
Protein Name(s) Heat shock protein HSP 90-alpha 1
External Links
UniProt Q90474
EMBL AF068773
CR381646
BC075757
L35586
PIR JC2343
RefSeq NP_571403.1
UniGene Dr.75834
ProteinModelPortal Q90474
SMR Q90474
PRIDE Q90474
Ensembl ENSDART00000004756
GeneID 30591
KEGG dre:30591
CTD 30591
ZFIN ZDB-GENE-990415-94
eggNOG COG0326
GeneTree ENSGT00760000119253
HOGENOM HOG000031988
HOVERGEN HBG007374
InParanoid Q90474
KO K04079
OMA EDISRME
OrthoDB EOG780RM0
PhylomeDB Q90474
TreeFam TF300686
NextBio 20806959
Proteomes UP000000437
Bgee Q90474
GO GO:0031672
GO:0042470
GO:0048471
GO:0030018
GO:0005524
GO:0030235
GO:0007517
GO:0030239
GO:0045429
GO:0006457
GO:0050790
GO:0006950
GO:0048769
GO:0030241
GO:0030240
GO:0014866
GO:0071688
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:0006950

response to stress

PMID:25366476[1]

ECO:0000314

P

Figure 1 HSP90 reduced infarct size shows inflammatory response signalling pathway inhibited by 17-DMAG in TCC-stained mouse brain section

complete
CACAO 10293

enables

GO:0016887

ATPase activity

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P07900

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P07900

F

Seeded From UniProt

complete

involved_in

GO:0045429

positive regulation of nitric oxide biosynthetic process

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P07901

P

Seeded From UniProt

complete

enables

GO:0030235

nitric-oxide synthase regulator activity

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P07901

F

Seeded From UniProt

complete

involved_in

GO:0071688

striated muscle myosin thick filament assembly

PMID:20049323[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

ZFIN:ZDB-GENO-980202-1042

P

Seeded From UniProt

complete

involved_in

GO:0050900

leukocyte migration

PMID:25810397[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

ZFIN:ZDB-MRPHLNO-070912-2

P

Seeded From UniProt

complete

involved_in

GO:0048769

sarcomerogenesis

PMID:18256191[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

ZFIN:ZDB-GENO-080401-1

P

Seeded From UniProt

complete

involved_in

GO:0030241

skeletal muscle myosin thick filament assembly

PMID:18256191[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

ZFIN:ZDB-GENO-080401-1

P

Seeded From UniProt

complete

involved_in

GO:0030240

skeletal muscle thin filament assembly

PMID:20049323[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

ZFIN:ZDB-GENO-980202-1042

P

Seeded From UniProt

complete

involved_in

GO:0030239

myofibril assembly

PMID:17586488[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

ZFIN:ZDB-MRPHLNO-071128-2

P

Seeded From UniProt

complete

part_of

GO:0030018

Z disc

PMID:18347070[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0014866

skeletal myofibril assembly

PMID:18182494[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

ZFIN:ZDB-MRPHLNO-080405-1

P

Seeded From UniProt

complete

involved_in

GO:0010038

response to metal ion

PMID:26354112[8]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0097718

disordered domain specific binding

PMID:21873635[9]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000163632
UniProtKB:P07900
UniProtKB:Q76LV2

F

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:21873635[9]

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[9]

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[9]

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

part_of

GO:0043209

myelin sheath

PMID:21873635[9]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002609464
RGD:631409

C

Seeded From UniProt

complete

part_of

GO:0043025

neuronal cell body

PMID:21873635[9]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:96250
PANTHER:PTN002609464
RGD:631409
UniProtKB:P11501

C

Seeded From UniProt

complete

involved_in

GO:0034605

cellular response to heat

PMID:21873635[9]

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[9]

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[9]

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[9]

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

involved_in

GO:0006457

protein folding

PMID:21873635[9]

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[9]

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[9]

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[9]

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

part_of

GO:0005634

nucleus

PMID:21873635[9]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:96250
PANTHER:PTN002609464
UniProtKB:P11501

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

PMID:21873635[9]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000163632
RGD:631409
UniProtKB:P07900

F

Seeded From UniProt

complete

involved_in

GO:0050790

regulation of catalytic activity

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0030235

P

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

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963

C

Seeded From UniProt

complete

involved_in

GO:0007517

muscle organ development

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0517

P

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:0031672

A band

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0476

C

Seeded From UniProt

complete

part_of

GO:0042470

melanosome

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0161

C

Seeded From UniProt

complete

part_of

GO:0030018

Z disc

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0314

C

Seeded From UniProt

complete

part_of

GO:0048471

perinuclear region of cytoplasm

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0198

C

Seeded From UniProt

complete

edit table

Notes

References

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

  1. ↑ Qi, J et al. (2014) 17-Dimethylaminoethylamino-17-demethoxygeldanamycin attenuates inflammatory responses in experimental stroke. Biol. Pharm. Bull. 37 1713-8 PubMed GONUTS page
  2. ↑ 2.0 2.1 Codina, M et al. (2010) Loss of Smyhc1 or Hsp90alpha1 function results in different effects on myofibril organization in skeletal muscles of zebrafish embryos. PLoS ONE 5 e8416 PubMed GONUTS page
  3. ↑ Ye, BX et al. (2015) Vibsanin B preferentially targets HSP90β, inhibits interstitial leukocyte migration, and ameliorates experimental autoimmune encephalomyelitis. J. Immunol. 194 4489-97 PubMed GONUTS page
  4. ↑ 4.0 4.1 Hawkins, TA et al. (2008) The ATPase-dependent chaperoning activity of Hsp90a regulates thick filament formation and integration during skeletal muscle myofibrillogenesis. Development 135 1147-56 PubMed GONUTS page
  5. ↑ Etard, C et al. (2007) The UCS factor Steif/Unc-45b interacts with the heat shock protein Hsp90a during myofibrillogenesis. Dev. Biol. 308 133-43 PubMed GONUTS page
  6. ↑ Etard, C et al. (2008) Shuttling of the chaperones Unc45b and Hsp90a between the A band and the Z line of the myofibril. J. Cell Biol. 180 1163-75 PubMed GONUTS page
  7. ↑ Du, SJ et al. (2008) Heat-shock protein 90alpha1 is required for organized myofibril assembly in skeletal muscles of zebrafish embryos. Proc. Natl. Acad. Sci. U.S.A. 105 554-9 PubMed GONUTS page
  8. ↑ Redelstein, R et al. (2015) Bioaccumulation and molecular effects of sediment-bound metals in zebrafish embryos. Environ Sci Pollut Res Int 22 16290-304 PubMed GONUTS page
  9. ↑ 9.00 9.01 9.02 9.03 9.04 9.05 9.06 9.07 9.08 9.09 9.10 9.11 9.12 9.13 9.14 9.15 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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