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Protein

Heat shock protein HSP 90-alpha 1

Gene

hsp90a.1

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (By similarity). Plays a key role in slow and fast muscle development in the embryo. Plays a role in myosin expression and assembly (PubMed:10364427, PubMed:17586488, PubMed:18182494, PubMed:18256191).By similarity4 Publications

Activity regulationi

In the resting state, through the dimerization of its C-terminal domain, HSP90 forms a homodimer which is defined as the open conformation. Upon ATP-binding, the N-terminal domain undergoes significant conformational changes and comes in contact to form an active closed conformation. After HSP90 finishes its chaperoning tasks of assisting the proper folding, stabilization and activation of client proteins under the active state, ATP molecule is hydrolyzed to ADP which then dissociates from HSP90 and directs the protein back to the resting state.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei48ATPBy similarity1
Binding sitei90ATPBy similarity1
Binding sitei109ATPBy similarity1
Binding sitei135ATP; via amide nitrogenBy similarity1
Binding sitei393ATPBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChaperone
Biological processMyogenesis, Stress response
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DRE-1227986 Signaling by ERBB2
R-DRE-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation
R-DRE-2029482 Regulation of actin dynamics for phagocytic cup formation
R-DRE-203615 eNOS activation
R-DRE-2565942 Regulation of PLK1 Activity at G2/M Transition
R-DRE-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-DRE-3371511 HSF1 activation
R-DRE-3371568 Attenuation phase
R-DRE-3371571 HSF1-dependent transactivation
R-DRE-380259 Loss of Nlp from mitotic centrosomes
R-DRE-380270 Recruitment of mitotic centrosome proteins and complexes
R-DRE-380320 Recruitment of NuMA to mitotic centrosomes
R-DRE-3928662 EPHB-mediated forward signaling
R-DRE-399954 Sema3A PAK dependent Axon repulsion
R-DRE-4420097 VEGFA-VEGFR2 Pathway
R-DRE-5218920 VEGFR2 mediated vascular permeability
R-DRE-5620912 Anchoring of the basal body to the plasma membrane
R-DRE-6798695 Neutrophil degranulation
R-DRE-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-DRE-8854518 AURKA Activation by TPX2
R-DRE-8863795 Downregulation of ERBB2 signaling
R-DRE-8939211 ESR-mediated signaling
R-DRE-9018519 Estrogen-dependent gene expression

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock protein HSP 90-alpha 1
Gene namesi
Name:hsp90a.1
Synonyms:hsp90, hsp90a, hsp90aa1
ORF Names:zgc:86652
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Chromosome 20

Organism-specific databases

ZFINiZDB-GENE-990415-94 hsp90aa1.1

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi94G → D in slou45; absence of thick filaments leading to loss of filamentous organization of myofibrils. 1 Publication1
Mutagenesisi721 – 725Missing : Reduced binding to unc45b. 1 Publication5

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000629241 – 725Heat shock protein HSP 90-alpha 1Add BLAST725

Proteomic databases

PaxDbiQ90474
PRIDEiQ90474

Expressioni

Tissue specificityi

Strongly expressed in the early embryos within the somitic slow muscle progenitors, the adaxial cells that lie on either side of the notochord but not the notochord. Also expressed during the early differentiation of fast fibers. Detected in developing cardiac muscles and pectoral fin primordia. Not detected in mature muscle fibers.3 Publications

Developmental stagei

Barely detectable during embryogenesis at control temperatures. Distributed throughout the cytoplasm of early developing myocytes at 24 hours post fertilization (hpf).2 Publications

Inductioni

Up-regulated by heat shock in embryos and larvae with highest levels of expression in 3 day old larvae.2 Publications

Gene expression databases

BgeeiENSDARG00000010478 Expressed in 40 organ(s), highest expression level in muscle tissue

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with unc45b and myosin.By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

ELMiQ90474
STRINGi7955.ENSDARP00000022302

Structurei

3D structure databases

ProteinModelPortaliQ90474
SMRiQ90474
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni675 – 725Required for homodimerizationBy similarityAdd BLAST51

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi716 – 725TPR repeat-bindingBy similarity10

Domaini

The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.By similarity

Sequence similaritiesi

Belongs to the heat shock protein 90 family.Curated

Phylogenomic databases

eggNOGiKOG0020 Eukaryota
COG0326 LUCA
GeneTreeiENSGT00920000149016
HOGENOMiHOG000031988
HOVERGENiHBG007374
InParanoidiQ90474
KOiK04079
OMAiYCEEKRV
OrthoDBiEOG091G0270
PhylomeDBiQ90474
TreeFamiTF300686

Family and domain databases

CDDicd00075 HATPase_c, 1 hit
Gene3Di1.20.120.790, 1 hit
3.30.565.10, 1 hit
HAMAPiMF_00505 HSP90, 1 hit
InterProiView protein in InterPro
IPR003594 HATPase_C
IPR036890 HATPase_C_sf
IPR019805 Heat_shock_protein_90_CS
IPR037196 HSP90_C
IPR001404 Hsp90_fam
IPR020575 Hsp90_N
IPR020568 Ribosomal_S5_D2-typ_fold
PANTHERiPTHR11528 PTHR11528, 1 hit
PfamiView protein in Pfam
PF02518 HATPase_c, 1 hit
PF00183 HSP90, 1 hit
PIRSFiPIRSF002583 Hsp90, 1 hit
PRINTSiPR00775 HEATSHOCK90
SMARTiView protein in SMART
SM00387 HATPase_c, 1 hit
SUPFAMiSSF110942 SSF110942, 1 hit
SSF54211 SSF54211, 1 hit
SSF55874 SSF55874, 1 hit
PROSITEiView protein in PROSITE
PS00298 HSP90, 1 hit

Sequencei

Sequence statusi: Complete.

Q90474-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPEKSAQPVM EEEVETFAFQ AEIAQLMSLI INTFYSNKEI FLRELISNSS
60 70 80 90 100
DALDKIRYES LTDPSKLDSC KDLKIELIPD QKERTLTIID TGIGMTKADL
110 120 130 140 150
INNLGTIAKS GTKAFMEALQ AGADISMIGQ FGVGFYSAYL VAEKVTVITK
160 170 180 190 200
HNDDEQYIWE SAAGGSFTVK PDFGESIGRG TKVILHLKED QSEYVEEKRI
210 220 230 240 250
KEVVKKHSQF IGYPITLYIE KQREKEVDLE EGEKQEEEEV AAGEDKDKPK
260 270 280 290 300
IEDLGADEDE DSKDGKNKRK KKVKEKYIDA QELNKTKPIW TRNPDDITNE
310 320 330 340 350
EYGEFYKSLS NDWEDHLAVK HFSVEGQLEF RALLFVPRRA AFDLFENKKK
360 370 380 390 400
RNNIKLYVRR VFIMDNCEEL IPEYLNFIKG VVDSEDLPLN ISREMLQQSK
410 420 430 440 450
ILKVIRKNLV KKCLDLFTEL AEDKDNYKKY YEQFSKNIKL GIHEDSQNRK
460 470 480 490 500
KLSDLLRYYT SASGDEMVSL KDYVSRMKDT QKHIYYITGE TKDQVANSAF
510 520 530 540 550
VERLRKAGLE VIYMIEPIDE YCVQQLKEYD GKNLVSVTKE GLELPEDEEE
560 570 580 590 600
KKKQDELKAK YENLCKIMKD ILDKKIEKVT VSNRLVSSPC CIVTSTYGWT
610 620 630 640 650
ANMERIMKSQ ALRDNSTMGY MTAKKHLEIN PAHPIVETLR EKAEADKNDK
660 670 680 690 700
AVKDLVILLF ETALLSSGFT LDDPQTHANR IYRMIKLGLG IDDDDSVVEE
710 720
ISQPAEEDMP VLEGDDDTSR MEEVD
Length:725
Mass (Da):83,319
Last modified:May 30, 2006 - v3
Checksum:i78CB3B97976531A7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4 – 11KSAQPVME → AHEQQMMED in AAC21567 (PubMed:10364427).Curated8
Sequence conflicti217L → F in AAH75757 (Ref. 5) Curated1
Sequence conflicti300E → D in AAH75757 (Ref. 5) Curated1
Sequence conflicti447Q → R in AAH75757 (Ref. 5) Curated1
Sequence conflicti646D → E in AAC21567 (PubMed:10364427).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF068773 mRNA Translation: AAC21567.1
CR381646 Genomic DNA Translation: CAI21043.1
BC075757 mRNA Translation: AAH75757.1
L35586 mRNA Translation: AAA97518.1
PIRiJC2343
RefSeqiNP_571403.1, NM_131328.1
UniGeneiDr.75834

Genome annotation databases

EnsembliENSDART00000004756; ENSDARP00000022302; ENSDARG00000010478
ENSDART00000170138; ENSDARP00000138112; ENSDARG00000010478
GeneIDi30591
KEGGidre:30591

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF068773 mRNA Translation: AAC21567.1
CR381646 Genomic DNA Translation: CAI21043.1
BC075757 mRNA Translation: AAH75757.1
L35586 mRNA Translation: AAA97518.1
PIRiJC2343
RefSeqiNP_571403.1, NM_131328.1
UniGeneiDr.75834

3D structure databases

ProteinModelPortaliQ90474
SMRiQ90474
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

ELMiQ90474
STRINGi7955.ENSDARP00000022302

Proteomic databases

PaxDbiQ90474
PRIDEiQ90474

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000004756; ENSDARP00000022302; ENSDARG00000010478
ENSDART00000170138; ENSDARP00000138112; ENSDARG00000010478
GeneIDi30591
KEGGidre:30591

Organism-specific databases

CTDi30591
ZFINiZDB-GENE-990415-94 hsp90aa1.1

Phylogenomic databases

eggNOGiKOG0020 Eukaryota
COG0326 LUCA
GeneTreeiENSGT00920000149016
HOGENOMiHOG000031988
HOVERGENiHBG007374
InParanoidiQ90474
KOiK04079
OMAiYCEEKRV
OrthoDBiEOG091G0270
PhylomeDBiQ90474
TreeFamiTF300686

Enzyme and pathway databases

ReactomeiR-DRE-1227986 Signaling by ERBB2
R-DRE-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation
R-DRE-2029482 Regulation of actin dynamics for phagocytic cup formation
R-DRE-203615 eNOS activation
R-DRE-2565942 Regulation of PLK1 Activity at G2/M Transition
R-DRE-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-DRE-3371511 HSF1 activation
R-DRE-3371568 Attenuation phase
R-DRE-3371571 HSF1-dependent transactivation
R-DRE-380259 Loss of Nlp from mitotic centrosomes
R-DRE-380270 Recruitment of mitotic centrosome proteins and complexes
R-DRE-380320 Recruitment of NuMA to mitotic centrosomes
R-DRE-3928662 EPHB-mediated forward signaling
R-DRE-399954 Sema3A PAK dependent Axon repulsion
R-DRE-4420097 VEGFA-VEGFR2 Pathway
R-DRE-5218920 VEGFR2 mediated vascular permeability
R-DRE-5620912 Anchoring of the basal body to the plasma membrane
R-DRE-6798695 Neutrophil degranulation
R-DRE-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-DRE-8854518 AURKA Activation by TPX2
R-DRE-8863795 Downregulation of ERBB2 signaling
R-DRE-8939211 ESR-mediated signaling
R-DRE-9018519 Estrogen-dependent gene expression

Miscellaneous databases

PROiPR:Q90474

Gene expression databases

BgeeiENSDARG00000010478 Expressed in 40 organ(s), highest expression level in muscle tissue

Family and domain databases

CDDicd00075 HATPase_c, 1 hit
Gene3Di1.20.120.790, 1 hit
3.30.565.10, 1 hit
HAMAPiMF_00505 HSP90, 1 hit
InterProiView protein in InterPro
IPR003594 HATPase_C
IPR036890 HATPase_C_sf
IPR019805 Heat_shock_protein_90_CS
IPR037196 HSP90_C
IPR001404 Hsp90_fam
IPR020575 Hsp90_N
IPR020568 Ribosomal_S5_D2-typ_fold
PANTHERiPTHR11528 PTHR11528, 1 hit
PfamiView protein in Pfam
PF02518 HATPase_c, 1 hit
PF00183 HSP90, 1 hit
PIRSFiPIRSF002583 Hsp90, 1 hit
PRINTSiPR00775 HEATSHOCK90
SMARTiView protein in SMART
SM00387 HATPase_c, 1 hit
SUPFAMiSSF110942 SSF110942, 1 hit
SSF54211 SSF54211, 1 hit
SSF55874 SSF55874, 1 hit
PROSITEiView protein in PROSITE
PS00298 HSP90, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiH90A1_DANRE
AccessioniPrimary (citable) accession number: Q90474
Secondary accession number(s): Q5RG13, Q6DI33
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 30, 2006
Last modified: September 12, 2018
This is version 143 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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Main funding by: National Institutes of Health

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