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Protein

Heat shock protein HSP 90-beta

Gene

hsp90ab1

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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. 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 (By similarity). Not required for myofibril formation in skeletal muscles.By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei45 – 451ATPBy similarity
Binding sitei87 – 871ATPBy similarity
Binding sitei106 – 1061ATPBy similarity
Binding sitei132 – 1321ATP; via amide nitrogenBy similarity
Binding sitei391 – 3911ATPBy similarity

GO - Molecular functioni

GO - Biological processi

  • blood vessel development Source: ZFIN
  • leukocyte migration Source: ZFIN
  • muscle organ development Source: UniProtKB-KW
  • protein folding Source: InterPro
  • response to estrogen Source: AgBase
  • response to stress Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Myogenesis, Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DRE-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-DRE-3371511. HSF1 activation.
R-DRE-3371568. Attenuation phase.
R-DRE-3371571. HSF1-dependent transactivation.
R-DRE-399954. Sema3A PAK dependent Axon repulsion.
R-DRE-844456. The NLRP3 inflammasome.
R-DRE-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock protein HSP 90-beta
Gene namesi
Name:hsp90ab1
Synonyms:hsp90b
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Chromosome 20

Organism-specific databases

ZFINiZDB-GENE-990415-95. hsp90ab1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 725725Heat shock protein HSP 90-betaPRO_0000062925Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei225 – 2251PhosphoserineBy similarity
Modified residuei254 – 2541PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO57521.
PRIDEiO57521.

Expressioni

Tissue specificityi

Detected throughout the embryo and in low levels in the musculature. Expressed predominantly in the developing brain, tail bud and cells surrounding the posterior margin of the yolk tube.2 Publications

Developmental stagei

Expressed throughout embryonic development.1 Publication

Inductioni

By heat shock during early embryogenesis.1 Publication

Gene expression databases

BgeeiO57521.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with unc45b.By similarity1 Publication

Protein-protein interaction databases

BioGridi78741. 1 interaction.
IntActiO57521. 1 interaction.
MINTiMINT-8283586.
STRINGi7955.ENSDARP00000014978.

Structurei

3D structure databases

ProteinModelPortaliO57521.
SMRiO57521. Positions 10-218, 284-687.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi721 – 7255TPR repeat-binding

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

eggNOGiKOG0019. Eukaryota.
KOG0020. Eukaryota.
COG0326. LUCA.
GeneTreeiENSGT00840000129758.
HOGENOMiHOG000031988.
HOVERGENiHBG007374.
InParanoidiO57521.
KOiK04079.
OMAiCKVMKDV.
OrthoDBiEOG780RM0.
PhylomeDBiO57521.
TreeFamiTF300686.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
HAMAPiMF_00505. HSP90.
InterProiIPR003594. HATPase_C.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR11528. PTHR11528. 1 hit.
PfamiPF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view]
PIRSFiPIRSF002583. Hsp90. 1 hit.
PRINTSiPR00775. HEATSHOCK90.
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiPS00298. HSP90. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O57521-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEEMRQEEE AETFAFQAEI AQLMSLIINT FYSNKEIFLR ELVSNASDAL
60 70 80 90 100
DKIRYESLTD PTKLDSGKDL KIDIIPNVQE RTLTLIDTGI GMTKADLINN
110 120 130 140 150
LGTIAKSGTK AFMEALQAGA DISMIGQFGV GFYSAYLVAE KVTVITKHND
160 170 180 190 200
DEQYAWESSA GGSFTVKVDH GEPIGRGTKV ILHLKEDQTE YIEEKRVKEV
210 220 230 240 250
VKKHSQFIGY PITLYVEKER DKEISDDEAE EEKAEKEEKE EEGEDKPKIE
260 270 280 290 300
DVGSDDEEDT KDKDKKKKKK IKEKYIDQEE LNKTKPIWTR NPDDISNEEY
310 320 330 340 350
GEFYKSLTND WEDHLAVKHF SVEGQLEFRA LLFIPRRAPF DLFENKKKKN
360 370 380 390 400
NIKLYVRRVF IMDNCEELIP EYLNFIRGVV DSEDLPLNIS REMLQQSKIL
410 420 430 440 450
KVIRKNIVKK CLELFAELAE DKDNYKKFYD AFSKNLKLGI HEDSQNRKKL
460 470 480 490 500
SELLRYQSSQ SGDEMTSLTE YVSRMKENQK SIYYITGESK DQVAHSAFVE
510 520 530 540 550
RVCKRGFEVL YMTEPIDEYC VQQLKDFDGK SLVSVTKEGL ELPEDEDEKK
560 570 580 590 600
KMEEDKAKFE NLCKLMKEIL DKKVEKVTVS NRLVSSPCCI VTSTYGWTAN
610 620 630 640 650
MERIMKAQAL RDNSTMGYMM AKKHLEINPD HPIMETLRQK AEADKNDKAV
660 670 680 690 700
KDLVILLFET ALLSSGFSLD DPQTHSNRIY RMIKLGLGID EDEDVPVEEP
710 720
SSAAAPEDIP PLEGDDDASR MEEVD
Length:725
Mass (Da):83,357
Last modified:May 30, 2006 - v2
Checksum:i97FACE5422684DF9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti98 – 981I → M in AAA97519 (PubMed:7980538).Curated
Sequence conflicti417 – 4182EL → DV in AAC21566 (PubMed:10364427).Curated
Sequence conflicti444 – 4441S → C in AAB96969 (Ref. 3) Curated
Sequence conflicti448 – 4481K → R in AAC21566 (PubMed:10364427).Curated
Sequence conflicti463 – 4631D → Y in AAC21566 (PubMed:10364427).Curated
Sequence conflicti622 – 6221K → N in AAB96969 (Ref. 3) Curated
Sequence conflicti647 – 6471D → T in AAB96969 (Ref. 3) Curated
Sequence conflicti701 – 7011S → T in AAB96969 (Ref. 3) Curated
Sequence conflicti703 – 7031Missing in AAC21566 (PubMed:10364427).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF068771 mRNA. Translation: AAC21566.1.
AF042108 mRNA. Translation: AAB96969.1.
BC065359 mRNA. Translation: AAH65359.1.
L35587 mRNA. Translation: AAA97519.1.
RefSeqiNP_571385.2. NM_131310.3.
UniGeneiDr.35688.

Genome annotation databases

EnsembliENSDART00000020084; ENSDARP00000014978; ENSDARG00000029150.
GeneIDi30573.
KEGGidre:30573.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF068771 mRNA. Translation: AAC21566.1.
AF042108 mRNA. Translation: AAB96969.1.
BC065359 mRNA. Translation: AAH65359.1.
L35587 mRNA. Translation: AAA97519.1.
RefSeqiNP_571385.2. NM_131310.3.
UniGeneiDr.35688.

3D structure databases

ProteinModelPortaliO57521.
SMRiO57521. Positions 10-218, 284-687.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi78741. 1 interaction.
IntActiO57521. 1 interaction.
MINTiMINT-8283586.
STRINGi7955.ENSDARP00000014978.

Proteomic databases

PaxDbiO57521.
PRIDEiO57521.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000020084; ENSDARP00000014978; ENSDARG00000029150.
GeneIDi30573.
KEGGidre:30573.

Organism-specific databases

CTDi3326.
ZFINiZDB-GENE-990415-95. hsp90ab1.

Phylogenomic databases

eggNOGiKOG0019. Eukaryota.
KOG0020. Eukaryota.
COG0326. LUCA.
GeneTreeiENSGT00840000129758.
HOGENOMiHOG000031988.
HOVERGENiHBG007374.
InParanoidiO57521.
KOiK04079.
OMAiCKVMKDV.
OrthoDBiEOG780RM0.
PhylomeDBiO57521.
TreeFamiTF300686.

Enzyme and pathway databases

ReactomeiR-DRE-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-DRE-3371511. HSF1 activation.
R-DRE-3371568. Attenuation phase.
R-DRE-3371571. HSF1-dependent transactivation.
R-DRE-399954. Sema3A PAK dependent Axon repulsion.
R-DRE-844456. The NLRP3 inflammasome.
R-DRE-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.

Miscellaneous databases

PROiO57521.

Gene expression databases

BgeeiO57521.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
HAMAPiMF_00505. HSP90.
InterProiIPR003594. HATPase_C.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR11528. PTHR11528. 1 hit.
PfamiPF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view]
PIRSFiPIRSF002583. Hsp90. 1 hit.
PRINTSiPR00775. HEATSHOCK90.
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiPS00298. HSP90. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Disruption of zebrafish somite development by pharmacologic inhibition of Hsp90."
    Lele Z., Hartson S.D., Martin C.C., Whitesell L., Matts R.L., Krone P.H.
    Dev. Biol. 210:56-70(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  2. "The UCS factor Steif/Unc-45b interacts with the heat shock protein Hsp90a during myofibrillogenesis."
    Etard C., Behra M., Fischer N., Hutcheson D., Geisler R., Strahle U.
    Dev. Biol. 308:133-143(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH UNC45B, TISSUE SPECIFICITY.
  3. "Molecular cloning of a cDNA encoding the Danio rerio hsp90 beta isoform."
    Coumailleau P., Angelier N.
    Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. NIH - Zebrafish Gene Collection (ZGC) project
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.
  5. "HSP 90 alpha and HSP 90 beta genes are present in the zebrafish and are differentially regulated in developing embryos."
    Krone P.H., Sass J.B.
    Biochem. Biophys. Res. Commun. 204:746-752(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-132, DEVELOPMENTAL STAGE, INDUCTION.
    Tissue: Embryo.
  6. "Specific localization of zebrafish hsp90 alpha mRNA to myoD-expressing cells suggests a role for hsp90 alpha during normal muscle development."
    Sass J.B., Weinberg E.S., Krone P.H.
    Mech. Dev. 54:195-204(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiHS90B_DANRE
AccessioniPrimary (citable) accession number: O57521
Secondary accession number(s): Q6P0Y9, Q90475
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 30, 2006
Last modified: June 8, 2016
This is version 119 of the entry and version 2 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.