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General Information
Symbol
Dmel\Hsp70Bb
Species
D. melanogaster
Name
Heat-shock-protein-70Bb
Annotation Symbol
CG31359
Feature Type
FlyBase ID
FBgn0013278
Gene Model Status
Stock Availability
Enzyme Name (EC)
Adenosinetriphosphatase (3.6.1.3)
Gene Snapshot
Heat-shock-protein-70Bb (Hsp70Bb) encodes a protein involved in response to hypoxia heat shock and . [Date last reviewed: 2019-08-01]
Also Known As
hsp70, Hsp70B, hsp-70, heat-shock protein 70, Hsp70Bc
Key Links
Genomic Location
Cytogenetic map
Sequence location
3R:12,505,793..12,508,139 [+]
Recombination map
3-52
Sequence
Other Genome Views
The following external sites may use different assemblies or annotations than FlyBase.
Function
GO Summary Ribbons
Protein Family (UniProt)
Belongs to the heat shock protein 70 family. (Q9BIS2)
Catalytic Activity (EC)
Experimental Evidence
-
Predictions / Assertions
ATP + H(2)O = ADP + phosphate (3.6.1.3)
Summaries
Gene Group (FlyBase)
HEAT SHOCK PROTEIN 70 CHAPERONES -
The Heat Shock Protein 70 (Hsp70) superfamily of chaperones assist in numerous folding processes and are upregulated by heat stress and toxic chemicals. Hsp70 chaperones share a highly conserved bipartite domain structure composed of an ATPase domain and a substrate-binding domain. (Adapted from PMID:17441502, FBrf0232269 and FBrf0174945).
Phenotypic Description (Red Book; Lindsley and Zimm 1992)
Hsp70
The structural genes that code for the 70,000 dalton heat-shock protein (HSP70), the most abundant of the heat-shock proteins. HSP70 returns to preshock levels more rapidly than other heat-shock proteins following return to 25 (DiDomenico, Bugaisky, and Lindquist, 1982, Proc. Nat. Acad. Sci. USA 79: 6181-85). The protein becomes concentrated in nuclei during heat shock; disperses to cytoplasm during recovery; returns to nucleus upon further heat shock (Velazquez and Lindquist, 1984, Cell 36: 655-62). Appears not to be expressed in the testis in response to heat-shock stimulation (Bonner, Parks, Parker-Thornberg, Mortin, and Pelham, 1984, Cell 37: 979-91). Deletion of either the 87A7 or the 87C1 sequences does not eliminate the HSP70 heat-shock response; simultaneous deletion of both sequences does eliminate the HSP70 heat-shock response (Ish-Horowitz et al., 1979).
Gene Model and Products
Number of Transcripts
1
Number of Unique Polypeptides
1

Please see the GBrowse view of Dmel\Hsp70Bb or the JBrowse view of Dmel\Hsp70Bb for information on other features

To submit a correction to a gene model please use the Contact FlyBase form

Protein Domains (via Pfam)
Isoform displayed:
Pfam protein domains
InterPro name
classification
start
end
Protein Domains (via SMART)
Isoform displayed:
SMART protein domains
InterPro name
classification
start
end
Comments on Gene Model
Gene model reviewed during 5.50
Sequence Ontology: Class of Gene
Transcript Data
Annotated Transcripts
Name
FlyBase ID
RefSeq ID
Length (nt)
Assoc. CDS (aa)
FBtr0082637
2347
641
Additional Transcript Data and Comments
Reported size (kB)
2.55 (northern blot)
Comments
External Data
Crossreferences
Polypeptide Data
Annotated Polypeptides
Name
FlyBase ID
Predicted MW (kDa)
Length (aa)
Theoretical pI
RefSeq ID
GenBank
FBpp0082106
70.2
641
5.49
Polypeptides with Identical Sequences

There is only one protein coding transcript and one polypeptide associated with this gene

Additional Polypeptide Data and Comments
Reported size (kDa)
Comments
External Data
Linkouts
Sequences Consistent with the Gene Model
Mapped Features

Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Hsp70Bb using the Feature Mapper tool.

External Data
Crossreferences
Eukaryotic Promoter Database - A collection of databases of experimentally validated promoters for selected model organisms.
Linkouts
Gene Ontology (20 terms)
Molecular Function (7 terms)
Terms Based on Experimental Evidence (0 terms)
Terms Based on Predictions or Assertions (7 terms)
CV Term
Evidence
References
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
Biological Process (9 terms)
Terms Based on Experimental Evidence (3 terms)
CV Term
Evidence
References
inferred from mutant phenotype
inferred from expression pattern
inferred from mutant phenotype
Terms Based on Predictions or Assertions (7 terms)
CV Term
Evidence
References
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
non-traceable author statement
(assigned by UniProt )
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
non-traceable author statement
(assigned by UniProt )
inferred from biological aspect of ancestor with PANTHER:PTN002500132
(assigned by GO_Central )
Cellular Component (4 terms)
Terms Based on Experimental Evidence (0 terms)
Terms Based on Predictions or Assertions (4 terms)
CV Term
Evidence
References
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN002500132
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN002500132
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN002500132
(assigned by GO_Central )
Expression Data
Expression Summary Ribbons
Colored tiles in ribbon indicate that expression data has been curated by FlyBase for that anatomical location. Colorless tiles indicate that there is no curated data for that location.
For complete stage-specific expression data, view the modENCODE Development RNA-Seq section under High-Throughput Expression below.
Transcript Expression
Additional Descriptive Data
Marker for
 
Subcellular Localization
CV Term
Polypeptide Expression
mass spectroscopy
Stage
Tissue/Position (including subcellular localization)
Reference
Additional Descriptive Data
Marker for
 
Subcellular Localization
CV Term
Evidence
References
Expression Deduced from Reporters
High-Throughput Expression Data
Associated Tools

GBrowse - Visual display of RNA-Seq signals

View Dmel\Hsp70Bb in GBrowse 2
RNA-Seq by Region - Search RNA-Seq expression levels by exon or genomic region
Reference
See Gelbart and Emmert, 2013 for analysis details and data files for all genes.
Developmental Proteome: Life Cycle
Developmental Proteome: Embryogenesis
External Data and Images
Linkouts
FLIGHT - Cell culture data for RNAi and other high-throughput technologies
FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
Images
Alleles, Insertions, and Transgenic Constructs
Classical and Insertion Alleles ( 0 )
For All Classical and Insertion Alleles Show
 
Other relevant insertions
Transgenic Constructs ( 10 )
For All Alleles Carried on Transgenic Constructs Show
Transgenic constructs containing/affecting coding region of Hsp70Bb
Transgenic constructs containing regulatory region of Hsp70Bb
Deletions and Duplications ( 3 )
Phenotypes
For more details about a specific phenotype click on the relevant allele symbol.
Other Phenotypes
Allele
Phenotype manifest in
Allele
Orthologs
Human Orthologs (via DIOPT v7.1)
Homo sapiens (Human) (11)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Alignment
Complementation?
Transgene?
5 of 15
Yes
Yes
 
5 of 15
Yes
No
4 of 15
No
No
 
4 of 15
No
No
3 of 15
No
No
3 of 15
No
No
3 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
Yes
1 of 15
No
No
Model Organism Orthologs (via DIOPT v7.1)
Mus musculus (laboratory mouse) (10)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Alignment
Complementation?
Transgene?
5 of 15
Yes
No
4 of 15
No
No
3 of 15
No
No
3 of 15
No
No
3 of 15
No
No
3 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
Yes
1 of 15
No
No
Rattus norvegicus (Norway rat) (10)
4 of 13
Yes
No
3 of 13
No
Yes
3 of 13
No
No
3 of 13
No
No
3 of 13
No
No
3 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
Yes
1 of 13
No
Yes
Xenopus tropicalis (Western clawed frog) (10)
3 of 12
Yes
No
3 of 12
Yes
No
3 of 12
Yes
No
2 of 12
No
No
2 of 12
No
No
2 of 12
No
No
2 of 12
No
No
1 of 12
No
No
1 of 12
No
Yes
1 of 12
No
No
Danio rerio (Zebrafish) (13)
4 of 15
Yes
No
4 of 15
Yes
No
4 of 15
Yes
Yes
 
3 of 15
No
No
3 of 15
No
No
3 of 15
No
No
2 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
Yes
1 of 15
No
No
Caenorhabditis elegans (Nematode, roundworm) (8)
4 of 15
Yes
Yes
4 of 15
Yes
No
4 of 15
Yes
No
2 of 15
No
No
2 of 15
No
No
2 of 15
No
No
1 of 15
No
No
1 of 15
No
Yes
Arabidopsis thaliana (thale-cress) (9)
2 of 9
Yes
No
1 of 9
No
No
1 of 9
No
No
1 of 9
No
No
1 of 9
No
No
1 of 9
No
No
1 of 9
No
No
1 of 9
No
No
1 of 9
No
No
Saccharomyces cerevisiae (Brewer's yeast) (8)
4 of 15
Yes
No
4 of 15
Yes
No
4 of 15
Yes
No
4 of 15
Yes
Yes
4 of 15
Yes
Yes
3 of 15
No
No
3 of 15
No
No
2 of 15
No
No
Schizosaccharomyces pombe (Fission yeast) (6)
3 of 12
Yes
Yes
2 of 12
No
No
2 of 12
No
No
2 of 12
No
No
1 of 12
No
No
1 of 12
No
No
Orthologs in Drosophila Species (via OrthoDB v9.1) ( EOG091905D7 )
Organism
Common Name
Gene
AAA Syntenic Ortholog
Multiple Dmel Genes in this Orthologous Group
Drosophila melanogaster
fruit fly
Drosophila melanogaster
fruit fly
Drosophila melanogaster
fruit fly
Drosophila melanogaster
fruit fly
Drosophila melanogaster
fruit fly
Drosophila melanogaster
fruit fly
Drosophila suzukii
Spotted wing Drosophila
Drosophila suzukii
Spotted wing Drosophila
Drosophila suzukii
Spotted wing Drosophila
Drosophila suzukii
Spotted wing Drosophila
Drosophila suzukii
Spotted wing Drosophila
Drosophila simulans
Drosophila simulans
Drosophila simulans
Drosophila simulans
Drosophila simulans
Drosophila simulans
Drosophila sechellia
Drosophila sechellia
Drosophila erecta
Drosophila erecta
Drosophila erecta
Drosophila erecta
Drosophila erecta
Drosophila yakuba
Drosophila yakuba
Drosophila ananassae
Drosophila ananassae
Drosophila ananassae
Drosophila ananassae
Drosophila ananassae
Drosophila ananassae
Drosophila ananassae
Drosophila pseudoobscura pseudoobscura
Drosophila persimilis
Drosophila willistoni
Drosophila willistoni
Drosophila virilis
Drosophila virilis
Drosophila virilis
Drosophila virilis
Drosophila virilis
Drosophila virilis
Drosophila virilis
Drosophila virilis
Drosophila virilis
Drosophila virilis
Drosophila mojavensis
Drosophila mojavensis
Drosophila mojavensis
Drosophila mojavensis
Drosophila mojavensis
Drosophila grimshawi
Drosophila grimshawi
Drosophila grimshawi
Drosophila grimshawi
Orthologs in non-Drosophila Dipterans (via OrthoDB v9.1) ( EOG091502IF )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Musca domestica
House fly
Musca domestica
House fly
Musca domestica
House fly
Musca domestica
House fly
Musca domestica
House fly
Musca domestica
House fly
Glossina morsitans
Tsetse fly
Lucilia cuprina
Australian sheep blowfly
Mayetiola destructor
Hessian fly
Mayetiola destructor
Hessian fly
Aedes aegypti
Yellow fever mosquito
Aedes aegypti
Yellow fever mosquito
Aedes aegypti
Yellow fever mosquito
Aedes aegypti
Yellow fever mosquito
Aedes aegypti
Yellow fever mosquito
Aedes aegypti
Yellow fever mosquito
Aedes aegypti
Yellow fever mosquito
Anopheles darlingi
American malaria mosquito
Anopheles darlingi
American malaria mosquito
Anopheles darlingi
American malaria mosquito
Anopheles darlingi
American malaria mosquito
Culex quinquefasciatus
Southern house mosquito
Culex quinquefasciatus
Southern house mosquito
Culex quinquefasciatus
Southern house mosquito
Culex quinquefasciatus
Southern house mosquito
Orthologs in non-Dipteran Insects (via OrthoDB v9.1) ( EOG090W02J2 )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Bombyx mori
Silkmoth
Bombyx mori
Silkmoth
Bombyx mori
Silkmoth
Danaus plexippus
Monarch butterfly
Danaus plexippus
Monarch butterfly
Danaus plexippus
Monarch butterfly
Danaus plexippus
Monarch butterfly
Danaus plexippus
Monarch butterfly
Danaus plexippus
Monarch butterfly
Heliconius melpomene
Postman butterfly
Heliconius melpomene
Postman butterfly
Heliconius melpomene
Postman butterfly
Heliconius melpomene
Postman butterfly
Heliconius melpomene
Postman butterfly
Apis florea
Little honeybee
Apis florea
Little honeybee
Apis florea
Little honeybee
Apis mellifera
Western honey bee
Apis mellifera
Western honey bee
Apis mellifera
Western honey bee
Bombus impatiens
Common eastern bumble bee
Bombus impatiens
Common eastern bumble bee
Bombus impatiens
Common eastern bumble bee
Bombus terrestris
Buff-tailed bumblebee
Bombus terrestris
Buff-tailed bumblebee
Bombus terrestris
Buff-tailed bumblebee
Linepithema humile
Argentine ant
Linepithema humile
Argentine ant
Linepithema humile
Argentine ant
Megachile rotundata
Alfalfa leafcutting bee
Megachile rotundata
Alfalfa leafcutting bee
Megachile rotundata
Alfalfa leafcutting bee
Megachile rotundata
Alfalfa leafcutting bee
Nasonia vitripennis
Parasitic wasp
Nasonia vitripennis
Parasitic wasp
Nasonia vitripennis
Parasitic wasp
Nasonia vitripennis
Parasitic wasp
Nasonia vitripennis
Parasitic wasp
Nasonia vitripennis
Parasitic wasp
Dendroctonus ponderosae
Mountain pine beetle
Dendroctonus ponderosae
Mountain pine beetle
Dendroctonus ponderosae
Mountain pine beetle
Dendroctonus ponderosae
Mountain pine beetle
Dendroctonus ponderosae
Mountain pine beetle
Tribolium castaneum
Red flour beetle
Tribolium castaneum
Red flour beetle
Tribolium castaneum
Red flour beetle
Tribolium castaneum
Red flour beetle
Tribolium castaneum
Red flour beetle
Tribolium castaneum
Red flour beetle
Pediculus humanus
Human body louse
Pediculus humanus
Human body louse
Pediculus humanus
Human body louse
Pediculus humanus
Human body louse
Rhodnius prolixus
Kissing bug
Rhodnius prolixus
Kissing bug
Rhodnius prolixus
Kissing bug
Cimex lectularius
Bed bug
Cimex lectularius
Bed bug
Cimex lectularius
Bed bug
Cimex lectularius
Bed bug
Cimex lectularius
Bed bug
Cimex lectularius
Bed bug
Cimex lectularius
Bed bug
Acyrthosiphon pisum
Pea aphid
Acyrthosiphon pisum
Pea aphid
Acyrthosiphon pisum
Pea aphid
Acyrthosiphon pisum
Pea aphid
Acyrthosiphon pisum
Pea aphid
Acyrthosiphon pisum
Pea aphid
Acyrthosiphon pisum
Pea aphid
Acyrthosiphon pisum
Pea aphid
Acyrthosiphon pisum
Pea aphid
Acyrthosiphon pisum
Pea aphid
Zootermopsis nevadensis
Nevada dampwood termite
Zootermopsis nevadensis
Nevada dampwood termite
Zootermopsis nevadensis
Nevada dampwood termite
Orthologs in non-Insect Arthropods (via OrthoDB v9.1) ( EOG090X02GG )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Strigamia maritima
European centipede
Strigamia maritima
European centipede
Strigamia maritima
European centipede
Ixodes scapularis
Black-legged tick
Ixodes scapularis
Black-legged tick
Ixodes scapularis
Black-legged tick
Ixodes scapularis
Black-legged tick
Stegodyphus mimosarum
African social velvet spider
Stegodyphus mimosarum
African social velvet spider
Stegodyphus mimosarum
African social velvet spider
Stegodyphus mimosarum
African social velvet spider
Stegodyphus mimosarum
African social velvet spider
Stegodyphus mimosarum
African social velvet spider
Stegodyphus mimosarum
African social velvet spider
Stegodyphus mimosarum
African social velvet spider
Stegodyphus mimosarum
African social velvet spider
Stegodyphus mimosarum
African social velvet spider
Tetranychus urticae
Two-spotted spider mite
Tetranychus urticae
Two-spotted spider mite
Tetranychus urticae
Two-spotted spider mite
Daphnia pulex
Water flea
Daphnia pulex
Water flea
Daphnia pulex
Water flea
Daphnia pulex
Water flea
Orthologs in non-Arthropod Metazoa (via OrthoDB v9.1) ( EOG091G03SF )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Strongylocentrotus purpuratus
Purple sea urchin
Strongylocentrotus purpuratus
Purple sea urchin
Strongylocentrotus purpuratus
Purple sea urchin
Strongylocentrotus purpuratus
Purple sea urchin
Strongylocentrotus purpuratus
Purple sea urchin
Strongylocentrotus purpuratus
Purple sea urchin
Strongylocentrotus purpuratus
Purple sea urchin
Strongylocentrotus purpuratus
Purple sea urchin
Ciona intestinalis
Vase tunicate
Ciona intestinalis
Vase tunicate
Ciona intestinalis
Vase tunicate
Gallus gallus
Domestic chicken
Gallus gallus
Domestic chicken
Gallus gallus
Domestic chicken
Gallus gallus
Domestic chicken
Paralogs
Paralogs (via DIOPT v7.1)
Drosophila melanogaster (Fruit fly) (12)
6 of 10
6 of 10
6 of 10
6 of 10
6 of 10
6 of 10
5 of 10
5 of 10
5 of 10
5 of 10
3 of 10
2 of 10
Human Disease Associations
FlyBase Human Disease Model Reports
    Disease Model Summary Ribbon
    Disease Ontology (DO) Annotations
    Models Based on Experimental Evidence ( 0 )
    Allele
    Disease
    Evidence
    References
    Potential Models Based on Orthology ( 0 )
    Human Ortholog
    Disease
    Evidence
    References
    Modifiers Based on Experimental Evidence ( 0 )
    Allele
    Disease
    Interaction
    References
    Comments on Models/Modifiers Based on Experimental Evidence ( 0 )
     
    Disease Associations of Human Orthologs (via DIOPT v7.1 and OMIM)
    Note that ortholog calls supported by only 1 or 2 algorithms (DIOPT score < 3) are not shown.
    Functional Complementation Data
    Functional complementation data is computed by FlyBase using a combination of the orthology data obtained from DIOPT and OrthoDB and the allele-level genetic interaction data curated from the literature.
    Interactions
    Summary of Physical Interactions
    esyN Network Diagram
    Interactions Browser
    Summary of Genetic Interactions
    esyN Network Diagram
    Starting gene(s)
    Interaction type
    Interacting gene(s)
    Reference
    Starting gene(s)
    Interaction type
    Interacting gene(s)
    Reference
    External Data
    Linkouts
    BioGRID - A database of protein and genetic interactions.
    DroID - A comprehensive database of gene and protein interactions.
    InterologFinder - Protein-protein interactions (PPI) from both known and predicted PPI data sets.
    MIST (protein-protein) - An integrated Molecular Interaction Database
    Pathways
    Gene Group - Pathway Membership (FlyBase)
    External Data
    Genomic Location and Detailed Mapping Data
    Chromosome (arm)
    3R
    Recombination map
    3-52
    Cytogenetic map
    Sequence location
    3R:12,505,793..12,508,139 [+]
    FlyBase Computed Cytological Location
    Cytogenetic map
    Evidence for location
    87B14-87B14
    Limits computationally determined from genome sequence between P{PZ}svp07842 and P{lacW}Vha55j2E9
    Experimentally Determined Cytological Location
    Cytogenetic map
    Notes
    References
    87C1-87C1
    (determined by in situ hybridisation)
    87C-87C
    (determined by in situ hybridisation)
    Experimentally Determined Recombination Data
    Location
    Left of (cM)
    Right of (cM)
    Notes
    Stocks and Reagents
    Stocks (2)
    Genomic Clones (13)
     

    Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete

    cDNA Clones (94)
     

    Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.

    cDNA clones, fully sequences
    Drosophila Genomics Resource Center cDNA clones

    For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.

    cDNA Clones, End Sequenced (ESTs)
    RNAi and Array Information
    Linkouts
    DRSC - Results frm RNAi screens
    GenomeRNAi - A database for cell-based and in vivo RNAi phenotypes and reagents
    Antibody Information
    Laboratory Generated Antibodies
     
    Commercially Available Antibodies
     
    Other Information
    Relationship to Other Genes
    Source for database identify of
    Source for database merge of
    Additional comments
    Other Comments
    Flies with no copies of the Hsp70 genes (Hsp70Aa, Hsp70Ab, Hsp70Ba, Hsp70Bb, Hsp70Bbb and Hsp70Bc) are unable to survive a severe heat shock. These flies show a lengthened heat-shock response and developmental delay following a non-lethal heat shock.
    Flies with no copies of the Hsp70 genes (Hsp70Aa, Hsp70Ab, Hsp70Ba, Hsp70Bb, Hsp70Bbb and Hsp70Bc) are viable and fertile.
    Some Drosophila strains, including that sequenced in the Drosophila genome project have three, not two, tandemly repeated Hsp70 genes at 87C1 (in addition to a reverse orientation Hsp70 gene, Hsp70Ba, approximately 40kb upstream). The distal-most gene of the three tandem copies is Hsp70Bc. The inner two tandem copies are Hsp70Bb and Hsp70Bbb.
    The D.melanogaster strain used for sequencing the genome contains an additional, third tandem copy of an Hsp70 gene at 87C as well as the two tandemly repeated copies (Hsp70Bb and Hsp70Bc) which are found in many strains. This additional copy is named "Hsp70Bbb" (see FBrf0137034 and Bettencourt, 2002.1.16, personal communication to FlyBase).
    New annotation (CG31359) in release 3 of the genome annotation.
    Nucleosomes are not required for polymerase pausing on the Hsp70Bb promoter.
    Variation in copy number of Hsp70Bb and Hsp70Bc demonstrates while extra Hsp70 provides additional protection against the immediate damage from heat stress, abnormally high concentrations can decrease growth, development and survival to adulthood.
    Natural variation in Hsp70 expression is analysed to study thermotolerance.
    The rate and intensity of Hsp70Bb protein expression has been compared with tissue damage after heat shock.
    Expression is rapidly induced in the testis after heat stress. Activation of Hsp70 in testes and heads necessitates the presence of a functional Hsf.
    There is significant variation among 74 different 2nd chromosome lines and 70 different 3rd chromosome lines in response to heat shock, measured by mRNA accumulation.
    Species-wide analysis demonstrates a characteristic of heat-shock-inducible genes is the absence of introns.
    Construct analysis reveals deletion of the TATA box or the upstream region greatly inhibits transcription under heat shock conditions. Analysis of DNase I hypersensitivity reveals non-histone protein interactions on the mutant promoters. Paused polymerase and Tbp on the Hsp70Bb promoter is detected in intact salivary glands, but not on a promoter lacking the TATA box.
    d(GA.TC)n sequences can be found in the promoters of Hsp26 and the Hsp70 genes. In vitro assembly of mononucleosomes into short DNA fragments carrying d(GA.TC)n sequences of different lengths is very efficient. Nucleosome assembly is inhibited strongly when the d(GA.TC)n sequence forms a triple-stranded conformation. Triplex formation requires partial destabilisation of the nucleosome. Results indicate nucleosome assembly and triplex formation are competing processes.
    Variation in copy number of Hsp70Bb and Hsp70Bc affects Hsp70 protein concentration in whole larvae and pupae, which in turn affects their tolerance of natural thermal stress and, potentially, their fitness.
    Minimal secondary structure is a key determinant of preferential translation during heat shock and the specific location of a cap-proximal portion of the leader influences initiation and a cap-independent mode of translation in unlikely. Heat shock reduces the capacity to unwind 5'-UTR secondary structure, allowing only mRNAs with minimal 5'-UTR secondary structure to be efficiently translated.
    RNA polymerase pauses on the Hsp70Bb and His3 promoters in a nuclear extract derived from embryos. Analysis of the transcripts produced from the Hsp70Bb promoter indicates that more than 50% of the polymerases that initiate fail to elongate beyond 40 nucleotides. Permanganate assay also detects a paused polymerase.
    Chromosome homologies of Muller's element D (J chromosome in the Paleartic species and XR chromosome arm in Nearctic species) and of element E (O chromosome in the Paleartic species and 2 chromosome in Nearctic species) have been confirmed by single copy probes in the species of the obscura group and in D.melanogaster.
    Sodium salicylate induces activation of Hsf binding activity in salivary gland cells and Schneider SL2 tissue cells. Puffing of heat shock gene loci occurs in salivary glands but Hsp70 transcription is not induced suggesting puffing and transcription are separable events.
    The in vitro binding of Hsf protein to the promoter region of a number of heat shock genes has been analysed.
    UV cross linking technique has been used to study the in vivo distribution of Trl protein on Hsp70 and Hsp26. Prior to heat shock Trl protein is associated with the promoter regions of the uninduced Hsp70 and Hsp26 genes. Upon heat shock induction Trl protein is recruited to their transcription units with its distribution coincident with that of RNA polymerase II.
    Analysis of transgenic lines containing altered Hsp70Bb promoters (fused to reporter gene Yp1), analysed for their ability to bind Hsf protein, indicates that at least three promoter sequences facilitate the binding of Hsf to chromatin, including binding sites for Trl, Tbp and RNA polymerase II.
    The molecular architecture of the Hsp70Bb promoter has been analysed by genomic footprinting.
    RNA levels do not increase with age, so the observed increase in protein levels is due to post-transcriptional regulation. Aging-specific expression may be a result of oxidative damage.
    Analysis of Hsp70Bb-Ecol\lacZ constructs in which the spacing between HSEs (heat shock elements) I and II, and between HSEII and the TATA box are altered suggests that Hsf binds cooperatively to the Hsp70Bb promoter.
    Heat-induced alterations in RNA-binding proteins do not mediate preferential translation of heat stress mRNAs or repression of normal mRNAs.
    Synthesis of heat shock proteins is inhibited by both short-chain fatty acids and their corresponding alcohols, compounds which have no observable effect on histone acetylation.
    Gene contains an RNA polymerase II complex which pauses after synthesis of a short transcript. In vivo ultraviolet crosslinking techniques demonstrate phosphorylation of the carboxy terminal domain (CTD) of the large subunit of RNA polymerase II could either regulate the transition of polymerase from a paused to an elongated complex or be a consequence of the transition from paused to elongated.
    The TFIID complex interacts with the promoter of Hsp70Bb making contacts at the TATA element, initiator, +18 and +28 regions. The complex recognises a sequence within the context of the promoter region that corresponds to an initiator consensus sequence.
    Chromosome staining reveals that Trl and heat shock transcription factors (HSF) colocalises at Hsp70Bb.
    The 87A7 Hsp70B region is bordered on the proximal and distal sides by two special chromatin structures, scs and scs'. An enhancer blocking assay based on the w gene demonstrates that the two nuclease hypersensitive regions that define part of the scs chromatin structure are essential for the blocking activity. The DNA sequence spanning the nuclease resistant core located between the two hypersensitive regions is dispensable.
    In vivo crosslinking studies demonstrate that endogenous eve and ftz protein significantly interacts with the promoter region, although this is not an expected target gene.
    The transcription of heat shock proteins, except Hsp83, is independent of the p200 subunit of initiation factor eIF-4F, eIF-4G.
    RNA polymerase distribution on uninduced Hsp70 genes has been compared with the distribution of RNA polymerase on DRB (5,6,-Dichloro-1-β-D-ribofuranosylbenzimidazole)-inhibited induced Hsp70 genes.
    In vivo UV cross-linking and nuclear run-on assays shows that RNA polymerase II density on the Hsp70Bb gene is rapidly increased by heat shock.
    Hsp70 proteins are of prime importance to heat tolerance.
    TATA complex formation on the Hsp70Bb core promoter shows sequence dependence at the TATA element, at the transcription start site and further downstream. Hydroxyl radical interference assays show that these sequences contribute to the TATA complex. The TATA complex contains Tbp. Methylation interference shows that protein contact at the TATA element is in the minor groove. Similar interactions contribute to TATA complexes formed on the Hsp26 and His4 promoters.
    Members of the hsc70 gene family (heat shock cognate genes) that reside within the same intracellular compartment in different organisms share greater amino acid identity than hsc70 proteins from the same organism but different organelles. This pattern of conservation indicates specialisation of hsc70 function.
    Identified in 2D gels of CMW W2 wing imaginal disc cell proteins.
    Nascent chain nuclear run-on assays in KC161 cells reveal different responses to heat shock for different genes. Transcription of His1 is severely inhibited under mild heat shocks, of Act5C decreases proportionally with increasing temperature while that of the core histone genes or the heat shock cognates is repressed only under extreme heat shock. In unshocked cells Hsp83 is moderately transcribed while transcription from the other heat shock genes is undetectable. Engaged but paused RNA molecules are found at the various Hsp70 and Hsp26 genes but not at the other heat shock genes. Increased transcription of the heat shock genes is observed within 1-2 mins of heat shock and maximal rates were reached within 2-5 minutes. Rates of transcription vary over a 20-fold range. Hsrω is transcribed at a very high rate under non-heat shock conditions, and its response to elevated temperatures is different from that of the protein coding heat shock genes.
    Expression of transgenes carrying Hsp70Bb and Hsp70Bc demonstrate that at early embryonic stages the accumulation of Hsp70 is a rate-limiting factor in the acquisition of thermotolerance. Genetic manipulation can improve stress tolerance.
    Hsp70 promoter driven expression in heat induced and non-heat induced conditions is more efficient in D.melanogaster embryos than in L.cuprina embryos.
    The interaction of Top1 and Top2 gene products with transcriptionally active and inactive Hsp70B has been compared. Topoisomerase I binding sites are found in the transcribed portions of the Hsp70B gene, and only when Hsp70B is transcriptionally active. Topoisomerase II binding to Hsp70B sequences occurs on both transcriptionally active and inactive chromatin. An unusual type of topoisomerase II binding site is associated with the 5' ends of inactive Hsp70 gene, suggesting that this enzyme may be associated with repression of gene transcription.
    Using Yp1 reporter gene constructs distal and proximal regions of the Hsp70 promoter have been identified that are required for formation of paused RNA polymerase II, the polymerase is transcriptionally engaged but paused about 25 nucleotides from the start site of Hsp70.
    The effect of aging on the expression of the "Hsp70" genes (Hsp70Aa, Hsp70Ab, Hsp70Ba, Hsp70Bb and Hsp70Bc) has been studied.
    Pausing of RNA polymerase II on the Hsp70Bb gene is not restricted to uninduced cells. A number of paused and elongating RNA polymerase II molecules are detected at the 5' end of Hsp70Bb when transcribed at intermediate levels. Elongation of polymerase from the pause remains the rate limiting step in transcription.
    Translation of Hsp70 mRNAs and to a lesser extent the mRNAs for the small heat shock proteins is almost independent of eIF-4E.
    Induction of heat shock protein after metal ion exposure is studied.
    A TATA-dependent protein-DNA complex is found in fractionated embryonic nuclear extracts. DNase I footprint analysis identifies polypeptides (including Taf12, Tbp and RpII140) that require the Hsp70Bb TATA element for binding to regions of the Hsp70Bb promoter.
    Analysis of Hsp70-Adh and Hsp70-Ecol\CAT constructs suggests that the Hsp70 3' untranslated region is required for the instability of Hsp70 mRNA seen at normal growth temperatures and for the selective degradation of Hsp70 mRNA seen during recovery from heat shock.
    Nuclear run-on experiments investigate the interaction between RNA polymerase II and the uninduced Hsp70Bb promoter.
    Deletion analysis of the 5' side of Hsp70Bb demonstrates that two nuclease-hypersensitive sites in chromatin exist upstream of Hsp70Bb. It is proposed that the hypersensitive sites are generated through the binding of a protein that renders the flanking sequence more accessible to nucleases, perhaps by preventing normal chromatin packaging.
    Studies demonstrate that heat shock puffs at the site of a construct insertion can be formed if the inserted segment contains a functional heat shock promoter and the active promoter is joined to long transcription units.
    Sequences located 5' to Sgs7, Sgs8, Sgs3, the Hsp70 genes at 87A and 87C and the copia coding region are similar to the sequence at -405 from Sgs4.
    initiates the heat-shock response. A restricted subset of genes, the Hsp genes, is activated and the majority of transcription and translation is shut down. However, mitochondrial- and histone-gene activities persist (Spradling, Pardue and Penman, 1977). This response follows a pulse of 36oC to 40oC; treatments above 40oC inhibit all activity and lead to death; treatments of 30oC-35oC induce heat-shock-protein synthesis without repressing normal protein synthesis (Tissieres, Mitchell and Tracy, 1974). Similar response inducible by other stressful treatments. The response may be elicited at all stages of the life cycle and in cultured cells. Stage specific phenocopies result from heat shocking early stages of Drosophila development (Mitchell and Petersen, 1982). In polytene cells existing puffs regress and a novel group quickly appears at 33B, 63C, 64F, 67B, 70A, 87A, 87C, 93D, 95D (Ashburner, 1970; Tissieres, Mitchell and Tracy, 1974). Activation of transcription of Hsp genes apparently involves the sequential binding of two or more protein factors in vicinity of TATA box (Wu, 1984). Binding sites for these proteins are multiple short upstream sequence elements called HSEs or heat shock consensus elements (Pelham, 1982; Xiao and Lis, 1988). Polymerase II dissociates from most chromosome regions and accumulates at the new puff sites (Bonner and Kerby, 1982). 3H-uridine incorporation ceases at its usual positions and commences at new puff sites. Preexisting polysomes disaggregate and within a few minutes a new population of polysomes appears containing newly transcribed mRNA; this RNA hybridizes to some of the heat-shock puffs. The effects of heat shock may be abrogated to some degree by pretreatment with a pulse of a slightly lower temperature (Mitchell, Moller, Petersen and Lipps-Sarmiento, 1979; Peterson and Mitchell, 1981). For reviews of the heat-shock response see Ashburner and Bonner (1978).
    One of five structural genes (in two clusters, Hsp70A, Hsp70B) that code for the 70,000 dalton heat-shock protein (HSP70), the most abundant of the heat-shock proteins. Hsp70B usually includes three HSP70 encoding genes (Hsp70Ba (proximal), Hsp70Bb (middle), Hsp70Bc (distal)) (Holmgren et al., 1979) with slightly different restriction maps (Artavanis-Tsakonas et al., 1978). HSP70 returns to preshock levels more rapidly than other heat-shock proteins following return to 25oC (DiDomenico, Bugaisky and Lindquist, 1982). The protein becomes concentrated in nuclei during heat shock; disperses to cytoplasm during recovery; returns to nucleus upon further heat shock (Velazquez and Lindquist, 1984). Appears not to be expressed in the testis in response to heat-shock stimulation (Bonner, Parks, Parker-Thornberg, Mortin and Pelham, 1984). Deletion of either Hsp70A or Hsp70B does not eliminate the HSP70 heat-shock response; simultaneous deletion of both does (Ish-Horowicz et al., 1979).
    Origin and Etymology
    Discoverer
    Etymology
    Identification
    External Crossreferences and Linkouts ( 73 )
    Sequence Crossreferences
    NCBI Gene - Gene integrates information from a wide range of species. A record may include nomenclature, Reference Sequences (RefSeqs), maps, pathways, variations, phenotypes, and links to genome-, phenotype-, and locus-specific resources worldwide.
    GenBank Protein - A collection of sequences from several sources, including translations from annotated coding regions in GenBank, RefSeq and TPA, as well as records from SwissProt, PIR, PRF, and PDB.
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    UniProt/Swiss-Prot - Manually annotated and reviewed records of protein sequence and functional information
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    Drosophila Genomics Resource Center - Drosophila Genomics Resource Center (DGRC) cDNA clones
    Eukaryotic Promoter Database - A collection of databases of experimentally validated promoters for selected model organisms.
    GenomeRNAi - A database for cell-based and in vivo RNAi phenotypes and reagents
    iBeetle-Base - RNAi phenotypes in the red flour beetle (Tribolium castaneum)
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    FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
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    MIST (protein-protein) - An integrated Molecular Interaction Database
    Synonyms and Secondary IDs (28)
    Reported As
    Symbol Synonym
    Hsp70
    (Gumeni et al., 2019, Prasad et al., 2019, Rajak et al., 2018, Shakya and Siddique, 2018, Berson et al., 2017, Dutta et al., 2017, Khanam et al., 2017, Li et al., 2017, Donovan and Marr, 2016, Hosamani et al., 2016, Zatsepina et al., 2016, Zhang et al., 2016, Zhang et al., 2016, Alaraby et al., 2015, Danish et al., 2015, Fuda et al., 2015, Funikov et al., 2015, Lashmanova et al., 2015, Zabidi et al., 2015, Maheshwari et al., 2014, Marr et al., 2014, Siddique et al., 2014, Tower et al., 2014, Zhang et al., 2014, Colinet et al., 2013, Siddique et al., 2013, Sinadinos et al., 2013, Calabria et al., 2012, Fredriksson et al., 2012, Schneiderman et al., 2012, Morettini et al., 2011, Takahashi et al., 2011, Ahamed et al., 2010, Bartkowiak et al., 2010, Hrizo and Palladino, 2010, Jensen et al., 2010, Kwon et al., 2010, Tian et al., 2010, Udaka et al., 2010, Zobeck et al., 2010, Zobeck et al., 2010, Ardehali et al., 2009, Baker and Russell, 2009, Chopra et al., 2009, Posgai et al., 2009, Sørensen et al., 2009, Bhargav et al., 2008, Brandt and Corces, 2008, Cai et al., 2008, Casas-Tinto et al., 2008, Cobreros et al., 2008, Duncan, 2008, Fujikake et al., 2008, Gilchrist et al., 2008, Hanyu-Nakamura et al., 2008, Ni et al., 2008, Smith et al., 2008, Ahrens et al., 2007, Eissenberg et al., 2007, Fernandez-Funez et al., 2007, Mito et al., 2007, Pappas et al., 2007, Rezaval et al., 2007, Yao et al., 2007, Behr et al., 2006, Kalosaka et al., 2006, Neal et al., 2006, Papaconstantinou et al., 2006, Sengupta and Lakhotia, 2006, Shilova et al., 2006, Tenney et al., 2006, Auluck et al., 2005, Duncan, 2005, Gupta et al., 2005, Huen and Chan, 2005, Iijima-Ando et al., 2005, Klose et al., 2005, Newman et al., 2005, Nielsen et al., 2005, Overgaard et al., 2005, Scholz et al., 2005, Ahmed and Duncan, 2004, Jennings et al., 2004, Marsh and Thompson, 2004, Morrow et al., 2004, Sathyanarayanan et al., 2004, Temme et al., 2004, Zhai et al., 2004, Auluck and Bonini, 2003, Caletka and Fry, 2003, Canamasas et al., 2003, Gruntenko et al., 2003, Jin et al., 2003, Kristensen et al., 2003, Norry and Loeschcke, 2003, Rutherford, 2003, Sejerkilde et al., 2003, Auluck et al., 2002, Bonini, 2002, Isaenko et al., 2002, Lakhotia et al., 2002, Shaw et al., 2002, Bulgheresi et al., 2001, de Carcer et al., 2001, Ekengren and Hultmark, 2001, Kelty and Lee, 2001, Krebs and Holbrook, 2001, Krebs et al., 2001, Mok et al., 2001, Rajendra et al., 2001, Sorensen and Loeschcke, 2001, Wu et al., 2001, Zatsepina et al., 2001, Andrulis et al., 2000, Gunawardena and Rykowski, 2000, Silbermann and Tatar, 2000, Bettencourt and Feder, 1999, Elefant and Palter, 1999, Feder, 1999, Krebs, 1999, Lerman and Feder, 1999, White et al., 1999, Ashburner et al., 1998, Cossins, 1998, Dahlgaard et al., 1998, Gu, 1998, Jazwinski, 1998, Krebs and Feder, 1998, Krebs et al., 1998, Wang and Lindquist, 1998, Krebs and Feder, 1997, Krebs and Feder, 1997, Krebs and Feder, 1997, Michaud et al., 1997, Espinas et al., 1996, Hess and Duncan, 1996, Kingston et al., 1996, Winegarden et al., 1996, Duncan, 1995, Engel and Cornelius, 1995, Gehring and Wehner, 1995, Li and Duncan, 1995, O'Brien et al., 1995, Song et al., 1995, Weber and Gilmour, 1995, Fernandes et al., 1994, Lis and Wu, 1994, Parsell et al., 1993, Evgen'ev and Denisenko, 1990)
    Hsp70(87C)
    Hsp70A7d
    hsp70
    (Roy et al., 2018, Sharma et al., 2018, Pereira and Paro, 2017, Tsakiri et al., 2017, Xu et al., 2016, Rahul et al., 2015, Kust et al., 2014, Shukla et al., 2014, Lagha et al., 2013, Soh et al., 2013, Shakya et al., 2012, Sharma et al., 2012, Siddique and Afzal, 2012, Siddique et al., 2012, Ardehali et al., 2011, Boeke et al., 2011, Chan et al., 2011, Ghosh et al., 2011, Juge et al., 2010, Kopytova et al., 2010, Kotova et al., 2010, Melnikova et al., 2010, Pankotai et al., 2010, Grover et al., 2009, Siddique et al., 2009, Singh et al., 2009, Tombácz et al., 2009, Yang and Tower, 2009, Grover et al., 2008, Hsu et al., 2008, Lee et al., 2008, Piel et al., 2008, Siddique et al., 2008, Smith et al., 2008, Behm-Ansmant et al., 2007, Gupta et al., 2007, Halfon and Arnosti, 2007, Ivaldi et al., 2007, Kurshakova et al., 2007, Lebedeva et al., 2007, Ullah et al., 2007, Vazquez-Pianzola et al., 2007, Buszczak and Spradling, 2006, Graves and Tamkun, 2006, Yao et al., 2006, Zhao et al., 2006, Adelman et al., 2005, Kim and Lis, 2005, Saunders et al., 2005, Wu et al., 2005, Zhao et al., 2005, Bhole et al., 2004, Goodman et al., 2004, Landis et al., 2004, Lehmann, 2004, Matsumoto and Hirose, 2004, Ni et al., 2004, Poels et al., 2004, Smith et al., 2004, Venkaiah et al., 2004, Wang et al., 2004, Feder, 2003, Gilmour, 2003.4.18, Gong and Golic, 2003, Goodman et al., 2003, Helfand and Rogina, 2003, Kellum, 2003, Nazir et al., 2003, Saunders et al., 2003, Shaw and Franken, 2003, Tulin and Spradling, 2003, Viswanathan et al., 2003, Weisbrot et al., 2003, Wimmer, 2003, Aigaki et al., 2002, Andrulis et al., 2002, Kazantsev et al., 2002, Lakhotia and Prasanth, 2002, Badenhorst and Wu, 2001, Biggin, 2001, Crevel et al., 2001, Gatfield et al., 2001, Herold et al., 2001, Li et al., 2001, Mahowald, 2001, Tatar and Yin, 2001, Bettencourt and Feder, 2000, Christoffels et al., 2000, Farkas et al., 2000, Geyer et al., 2000, Leach et al., 2000, Luckinbill and Foley, 2000, Yueh and Schneider, 2000, Agianian et al., 1999, Bonini, 1999, Carr and Biggin, 1999, Feder, 1999, Hirayoshi and Lis, 1999, Karunanithi et al., 1999, Katsani et al., 1999, King and Tower, 1999, Lakhotia et al., 1999, Mannervik, 1999, Sah et al., 1999, Tatar, 1999, Wilkins and Lis, 1999, Zhao and Eggleston, 1999, Benjamin and Gilmour, 1998, Gdula et al., 1998, Gregory and Horz, 1998, John and Workman, 1998, Liang and Biggin, 1998, Liang and Biggin, 1998, Lis, 1998, Marino et al., 1998, Martinez-Balbas et al., 1998, Nevo, 1998, Sun et al., 1998, Vernick and McCutchan, 1998, Wilkins and Lis, 1998, Wu et al., 1998, Burke and Kadonaga, 1997, Curtsinger et al., 1997, Elgin et al., 1997, Finch and Tanzi, 1997, Greenblatt, 1997, Otsuka et al., 1997, Wilkins and Lis, 1997, Wu and Fallon, 1997, Yiangou et al., 1997, Li et al., 1996, Segarra et al., 1996, Shopland and Lis, 1996, Tower, 1996, Wheeler et al., 1996, Elefant and Palter, 1995, Fernandes et al., 1995, Granok et al., 1995, Rasmussen and Lis, 1995, Shopland et al., 1995, Wheeler et al., 1995, Amin et al., 1994, Munks and Turner, 1994, O'Brien et al., 1994, Sandaltzopoulos et al., 1994, Zapata et al., 1994, Fuller, 1993, Giardina and Lis, 1993, Heikkila, 1993, Kroeger et al., 1993, Krumm et al., 1993, Lakhotia et al., 1993, Molto et al., 1993, O'Brien and Lis, 1993, Papaceit and Juan, 1993, Parsell and Lindquist, 1993, Purnell and Gilmour, 1993, Soeller et al., 1993, Vazquez et al., 1993, Atkinson and O'Brochta, 1992, Feder et al., 1992, Fleming et al., 1992, Lee et al., 1992, Morse, 1992, Pauli et al., 1992, Read and Manley, 1992, Becker et al., 1991, Bendena et al., 1991, Niedzwiecki et al., 1991, O'Brien and Lis, 1991, Sorger, 1991, Zapata et al., 1991, Elgin, 1990, Gilmour et al., 1990, Helms and Rottman, 1990, Karlin et al., 1990, Ohkuma et al., 1990, Ornelles and Penman, 1990, Perkins et al., 1990, Spencer and Groudine, 1990, Menke and Petersen, 1989, Petersen and Lindquist, 1989, Petersen and Lindquist, 1988)
    Name Synonyms
    Heat shock protein 70
    Heat-shock-protein-70Bb
    heat shock protein 70
    Secondary FlyBase IDs
    • FBgn0001232
    • FBgn0051359
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    References (571)