FB2019_06, released Dec 19, 2019

Gene: Dmel\Hsp70Ba

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General Information
Symbol
Dmel\Hsp70Ba
Species
D. melanogaster
Name
Heat-shock-protein-70Ba
Annotation Symbol
CG31449
Feature Type
protein_coding_gene
FlyBase ID
FBgn0013277
Gene Model Status
Current
Stock Availability
4 publicly available
Enzyme Name (EC)
Adenosinetriphosphatase (3.6.1.3)
Gene Snapshot
Heat-shock-protein-70Ba (Hsp70Ba) encodes a protein involved in response to heat shock and hypoxia. [Date last reviewed: 2019-08-01]
Other Summaries
Also Known As
hsp70, Hsp70B, hsp-70, hsp70 87C, heat-shock protein 70
Key Links
Genomic Location
Cytogenetic map
87B12-87B12
Sequence location
3R:12,465,453..12,467,776 [-]
Recombination map
3-52
Sequence
Get Decorated FASTA
Genomic Maps
Other Genome Views
The following external sites may use different assemblies or annotations than FlyBase.
NCBI
UCSC
Ensembl
PopFly
Function
GO Summary Ribbons
Gene Group (FlyBase)
Protein Family (UniProt)
Belongs to the heat shock protein 70 family. (Q8INI8)
Protein Signatures (InterPro)
Molecular Function (GO)
[Detailed GO annotations]
Experimental Evidence
-
Predictions / Assertions
ATP binding; ATPase activity; ATPase activity, coupled; heat shock protein binding; misfolded protein binding; protein folding chaperone; unfolded protein binding
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\Hsp70Ba or the JBrowse view of Dmel\Hsp70Ba 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
nuclear_gene
protein_coding_gene
Transcript Data
Annotated Transcripts
Name
FlyBase ID
RefSeq ID
Length (nt)
Assoc. CDS (aa)
Hsp70Ba-RA
FBtr0082679
NM_169469
2324
641
Additional Transcript Data and Comments
Reported size (kB)
2.55 (northern blot)
(Holmgren et al., 1979)
Comments
External Data
Crossreferences
Polypeptide Data
Annotated Polypeptides
Name
FlyBase ID
Predicted MW (kDa)
Length (aa)
Theoretical pI
RefSeq ID
GenBank
Hsp70Ba-PA
FBpp0082147
70.2
641
5.49
NP_731716
AAN13545
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)
641 (aa); 70.27 (kD predicted)
(Ingolia et al., 1980)
70 (kD)
(Holmgren et al., 1979)
Comments
External Data
Crossreferences
InterPro - A database of protein families, domains and functional sites
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\Hsp70Ba 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 (19 terms)
Molecular Function (7 terms)
Terms Based on Experimental Evidence (0 terms)
Terms Based on Predictions or Assertions (7 terms)
CV Term
Evidence
References
ATP binding
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
(Gaudet et al., 2011)
ATPase activity
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
(Gaudet et al., 2011)
ATPase activity, coupled
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
(Gaudet et al., 2011)
heat shock protein binding
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
(Gaudet et al., 2011)
misfolded protein binding
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
(Gaudet et al., 2011)
protein folding chaperone
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
(Gaudet et al., 2011)
unfolded protein binding
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
(Gaudet et al., 2011)
Biological Process (8 terms)
Terms Based on Experimental Evidence (3 terms)
CV Term
Evidence
References
heat shock-mediated polytene chromosome puffing
inferred from mutant phenotype
(Gong and Golic, 2006)
response to heat
inferred from mutant phenotype
(Gong and Golic, 2006)
response to hypoxia
inferred from expression pattern
(Azad et al., 2009)
inferred from mutant phenotype
(Azad et al., 2009)
Terms Based on Predictions or Assertions (6 terms)
CV Term
Evidence
References
cellular response to unfolded protein
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
(Gaudet et al., 2011)
chaperone cofactor-dependent protein refolding
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
(Gaudet et al., 2011)
protein refolding
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
(Gaudet et al., 2011)
response to heat
non-traceable author statement
(assigned by UniProt )
(Ingolia et al., 1980)
response to unfolded protein
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
(Gaudet et al., 2011)
non-traceable author statement
(assigned by UniProt )
(Ingolia et al., 1980)
vesicle-mediated transport
inferred from biological aspect of ancestor with PANTHER:PTN002500132
(assigned by GO_Central )
(Gaudet et al., 2011)
Cellular Component (4 terms)
Terms Based on Experimental Evidence (0 terms)
Terms Based on Predictions or Assertions (4 terms)
CV Term
Evidence
References
cytoplasm
inferred from biological aspect of ancestor with PANTHER:PTN002321897
(assigned by GO_Central )
(Gaudet et al., 2011)
cytosol
inferred from biological aspect of ancestor with PANTHER:PTN002500132
(assigned by GO_Central )
(Gaudet et al., 2011)
nucleus
inferred from biological aspect of ancestor with PANTHER:PTN002500132
(assigned by GO_Central )
(Gaudet et al., 2011)
plasma membrane
inferred from biological aspect of ancestor with PANTHER:PTN002500132
(assigned by GO_Central )
(Gaudet et al., 2011)
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
day 5 of adulthood & male -- day 7 of adulthood & male
spermatozoon
(Dorus et al., 2006)
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\Hsp70Ba in GBrowse 2
RNA-Seq by Region - Search RNA-Seq expression levels by exon or genomic region
Bulk Downloads
RNA-Seq RPKM values for all genes
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
Flygut - An atlas of the Drosophila adult midgut
Images
FlyBase Wiki
Image Based Resources
Alleles, Insertions, and Transgenic Constructs
Classical and Insertion Alleles ( 4 )
For All Classical and Insertion Alleles Show
 
Other relevant insertions
Transgenic Constructs ( 3 )
For All Alleles Carried on Transgenic Constructs Show
Transgenic constructs containing/affecting coding region of Hsp70Ba
Transgenic constructs containing regulatory region of Hsp70Ba
Deletions and Duplications ( 16 )
Phenotypes
For more details about a specific phenotype click on the relevant allele symbol.
Lethality
Allele
viable
Other Phenotypes
Allele
heat stress response defective
Phenotype manifest in
Allele
Orthologs
Downloads
Download All DIOPT Orthologs
Download All OrthoDB Orthologs
Human Orthologs (via DIOPT v7.1)
Homo sapiens (Human) (13)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Source
Compara
eggNOG
Hieranoid
Homologene
Inparanoid
Isobase
OMA
OrthoDB
OrthoFinder
OrthoInspector
orthoMCL
Panther
Phylome
RoundUp
TreeFam
ZFIN
Alignment
Complementation?
Transgene?
Hsap\HSPA1B
6 of 15
Yes
No
Hsap\HSPA1A
5 of 15
No
Yes
 
Hsap\HSPA1L
5 of 15
No
No
 
Hsap\HSPA6
5 of 15
No
No
Hsap\HSPA2
4 of 15
No
No
Hsap\HSPA5
4 of 15
No
No
Hsap\HSPA8
4 of 15
No
No
 
Hsap\HSPA12A
1 of 15
No
No
Hsap\HSPA12B
1 of 15
No
No
Hsap\HSPA13
1 of 15
No
Yes
Hsap\HSPA14
1 of 15
No
No
Hsap\NCKAP1
1 of 15
No
No
Hsap\NCKAP1L
1 of 15
No
No
Model Organism Orthologs (via DIOPT v7.1)
Mus musculus (laboratory mouse) (12)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Source
Compara
eggNOG
Hieranoid
Homologene
Inparanoid
Isobase
OMA
OrthoDB
OrthoFinder
OrthoInspector
orthoMCL
Panther
Phylome
RoundUp
TreeFam
ZFIN
Alignment
Complementation?
Transgene?
Mmus\Hspa1a
6 of 15
Yes
No
Mmus\Hspa1b
4 of 15
No
No
Mmus\Hspa1l
4 of 15
No
No
Mmus\Hspa2
4 of 15
No
No
Mmus\Hspa5
4 of 15
No
No
Mmus\Hspa8
4 of 15
No
No
Mmus\Hspa12a
1 of 15
No
No
Mmus\Hspa12b
1 of 15
No
No
Mmus\Hspa13
1 of 15
No
Yes
Mmus\Hspa14
1 of 15
No
No
Mmus\Nckap1l
1 of 15
No
No
Mmus\Nckap1
1 of 15
No
No
Rattus norvegicus (Norway rat) (11)
Rnor\Hspa1a
5 of 13
Yes
Yes
Rnor\Hspa1l
4 of 13
No
No
Rnor\Hspa2
4 of 13
No
No
Rnor\Hspa5
4 of 13
No
No
Rnor\Hspa1b
3 of 13
No
Yes
Rnor\Hspa8
3 of 13
No
No
Rnor\Hspa12a
1 of 13
No
No
Rnor\Hspa14
1 of 13
No
No
Rnor\LOC689955
1 of 13
No
Yes
Rnor\LOC108348108
1 of 13
No
Yes
Rnor\Nckap1l
1 of 13
No
No
Xenopus tropicalis (Western clawed frog) (10)
Xtro\hsp70
4 of 12
Yes
No
Xtro\hspa1a
3 of 12
No
No
Xtro\hspa1b
3 of 12
No
No
Xtro\hspa1l
3 of 12
No
No
Xtro\hspa2
3 of 12
No
No
Xtro\hspa5
3 of 12
No
No
Xtro\hspa8
2 of 12
No
No
Xtro\hspa12b
1 of 12
No
No
Xtro\hspa13
1 of 12
No
Yes
Xtro\hspa14
1 of 12
No
No
Danio rerio (Zebrafish) (15)
Drer\hsc70
5 of 15
Yes
No
Drer\hsp70.3
5 of 15
Yes
No
Drer\si:ch211-199o1.2
5 of 15
Yes
No
Drer\hsp70.3
4 of 15
No
No
Drer\hsp70l
4 of 15
No
Yes
 
Drer\hspa5
4 of 15
No
No
Drer\hspa8
4 of 15
No
No
Drer\si:dkey-4p15.3
4 of 15
No
No
Drer\hsp70.2
3 of 15
No
No
Drer\hspa12a
2 of 15
No
Yes
Drer\hspa12b
1 of 15
No
No
Drer\hspa13
1 of 15
No
Yes
Drer\hspa14
1 of 15
No
No
Drer\nckap1
1 of 15
No
No
Drer\zgc:172352
1 of 15
No
No
Caenorhabditis elegans (Nematode, roundworm) (10)
Cele\F44E5.5
6 of 15
Yes
Yes
Cele\hsp-70
6 of 15
Yes
Yes
Cele\F44E5.4
4 of 15
No
Yes
Cele\hsp-1
3 of 15
No
No
Cele\hsp-3
3 of 15
No
No
Cele\hsp-4
3 of 15
No
No
Cele\F11F1.1
2 of 15
No
No
Cele\F44F4.10
1 of 15
No
Yes
Cele\gex-3
1 of 15
No
No
Cele\stc-1
1 of 15
No
Yes
Arabidopsis thaliana (thale-cress) (9)
Atha\Hsp70-2
4 of 9
Yes
No
Atha\AT3G09440
3 of 9
No
No
Atha\ERD2
3 of 9
No
No
Atha\HSC70-1
3 of 9
No
No
Atha\HSP70
3 of 9
No
No
Atha\Hsp70b
3 of 9
No
No
Atha\BIP1
2 of 9
No
No
Atha\BIP2
2 of 9
No
No
Atha\BIP3
2 of 9
No
No
Saccharomyces cerevisiae (Brewer's yeast) (8)
Scer\SSA3
7 of 15
Yes
No
Scer\SSA4
7 of 15
Yes
No
Scer\SSA1
6 of 15
No
No
Scer\SSA2
6 of 15
No
No
Scer\KAR2
5 of 15
No
No
Scer\SSB1
4 of 15
No
Yes
Scer\SSB2
4 of 15
No
Yes
Scer\SSZ1
2 of 15
No
No
Schizosaccharomyces pombe (Fission yeast) (6)
Spom\ssa1
4 of 12
Yes
No
Spom\ssa2
4 of 12
Yes
No
Spom\bip1
3 of 12
No
No
Spom\sks2
3 of 12
No
Yes
Spom\lsh1
1 of 12
No
No
Spom\SPAC57A7.12
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
Dmel\Hsp70Aa
Drosophila melanogaster
fruit fly
Dmel\Hsp70Bbb
Drosophila melanogaster
fruit fly
Dmel\Hsp70Ba
Drosophila melanogaster
fruit fly
Dmel\Hsp70Ab
Drosophila melanogaster
fruit fly
Dmel\Hsp70Bc
Drosophila melanogaster
fruit fly
Dmel\Hsp70Bb
Drosophila suzukii
Spotted wing Drosophila
Dsuz\DS10_00010335
Drosophila suzukii
Spotted wing Drosophila
Dsuz\DS10_00013303
Drosophila suzukii
Spotted wing Drosophila
Dsuz\DS10_00013301
Drosophila suzukii
Spotted wing Drosophila
Dsuz\DS10_00012259
Drosophila suzukii
Spotted wing Drosophila
Dsuz\DS10_00013302
Drosophila simulans
Dsim\Hsp70Ba
Drosophila simulans
Dsim\Hsp70Ab
Drosophila simulans
Dsim\GD27509
Drosophila simulans
Dsim\GD28100
Drosophila simulans
Dsim\Hsp70Bb
Drosophila simulans
Dsim\Hsp70Aa
Drosophila sechellia
Dsec\GM23988
Drosophila sechellia
Dsec\GM26058
Drosophila erecta
Dere\GG17178
Drosophila erecta
Dere\GG19049
Drosophila erecta
Dere\GG18520
Drosophila erecta
Dere\GG17119
Drosophila erecta
Dere\GG19004
Drosophila yakuba
Dyak\GE28717
Drosophila yakuba
Dyak\GE29027
Drosophila ananassae
Dana\GF18384
Drosophila ananassae
Dana\GF16630
Drosophila ananassae
Dana\GF18385
Drosophila ananassae
Dana\GF16631
Drosophila ananassae
Dana\GF19283
Drosophila ananassae
Dana\GF16629
Drosophila ananassae
Dana\GF15894
Drosophila pseudoobscura pseudoobscura
Dpse\GA19632
Drosophila persimilis
Dper\GL27169
Drosophila willistoni
Dwil\GK27741
Drosophila willistoni
Dwil\GK13736
Drosophila virilis
Dvir\GJ25783
Drosophila virilis
Dvir\Hsp70g
Drosophila virilis
Dvir\Hsp70e
Drosophila virilis
Dvir\Hsp70f
Drosophila virilis
Dvir\Hsp70b
Drosophila virilis
Dvir\GJ10098
Drosophila virilis
Dvir\GJ14116
Drosophila virilis
Dvir\GJ10102
Drosophila virilis
Dvir\GJ18387
Drosophila virilis
Dvir\GJ16355
Drosophila mojavensis
Dmoj\GI10253
Drosophila mojavensis
Dmoj\GI10256
Drosophila mojavensis
Dmoj\GI22499
Drosophila mojavensis
Dmoj\GI10255
Drosophila mojavensis
Dmoj\GI10254
Drosophila grimshawi
Dgri\GH17332
Drosophila grimshawi
Dgri\GH15224
Drosophila grimshawi
Dgri\GH23796
Drosophila grimshawi
Dgri\GH15213
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
Mdoa\17008612
Musca domestica
House fly
Mdoa\17013981
Musca domestica
House fly
Mdoa\17005774
Musca domestica
House fly
Mdoa\17008614
Musca domestica
House fly
Mdoa\17006254
Musca domestica
House fly
Mdoa\17008613
Glossina morsitans
Tsetse fly
Gmor\GMOY009493
Lucilia cuprina
Australian sheep blowfly
Lcup\FF38_03660
Mayetiola destructor
Hessian fly
Mdes\Mdes000202
Mayetiola destructor
Hessian fly
Mdes\Mdes011175
Aedes aegypti
Yellow fever mosquito
Aaeg\HSP70Ba
Aedes aegypti
Yellow fever mosquito
Aaeg\HSP70Ab
Aedes aegypti
Yellow fever mosquito
Aaeg\HSP70Ab_prime_
Aedes aegypti
Yellow fever mosquito
Aaeg\HSP70Aa
Aedes aegypti
Yellow fever mosquito
Aaeg\HSP70Cb
Aedes aegypti
Yellow fever mosquito
Aaeg\HSP70Aa_prime_
Aedes aegypti
Yellow fever mosquito
Aaeg\HSP70Bb
Anopheles darlingi
American malaria mosquito
Adar\ADAC003118
Anopheles darlingi
American malaria mosquito
Adar\ADAC005660
Anopheles darlingi
American malaria mosquito
Adar\ADAC004661
Anopheles darlingi
American malaria mosquito
Adar\ADAC002898
Culex quinquefasciatus
Southern house mosquito
Cqui\CPIJ014283
Culex quinquefasciatus
Southern house mosquito
Cqui\CPIJ011082
Culex quinquefasciatus
Southern house mosquito
Cqui\CPIJ011083
Culex quinquefasciatus
Southern house mosquito
Cqui\CPIJ011081
Orthologs in non-Dipteran Insects (via OrthoDB v9.1) ( EOG090W02J2 )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Bombyx mori
Silkmoth
Bmor\BGIBMGA002428
Bombyx mori
Silkmoth
Bmor\BGIBMGA014536
Bombyx mori
Silkmoth
Bmor\BmHSC70-4
Danaus plexippus
Monarch butterfly
Dple\DPOGS208954-PA
Danaus plexippus
Monarch butterfly
Dple\DPOGS210048-PA
Danaus plexippus
Monarch butterfly
Dple\DPOGS213900-PA
Danaus plexippus
Monarch butterfly
Dple\DPOGS212775-PA
Danaus plexippus
Monarch butterfly
Dple\DPOGS213925-PA
Danaus plexippus
Monarch butterfly
Dple\DPOGS210250-PA
Heliconius melpomene
Postman butterfly
Hmel\Hem
Heliconius melpomene
Postman butterfly
Hmel\HMEL010425
Heliconius melpomene
Postman butterfly
Hmel\HMEL014657
Heliconius melpomene
Postman butterfly
Hmel\HMEL014163
Heliconius melpomene
Postman butterfly
Hmel\HMEL006064
Apis florea
Little honeybee
Aflo\2484227444
Apis florea
Little honeybee
Aflo\2994796276
Apis florea
Little honeybee
Aflo\2354233092
Apis mellifera
Western honey bee
Amel\LOC410620
Apis mellifera
Western honey bee
Amel\GB50246
Apis mellifera
Western honey bee
Amel\Hsc70-4
Bombus impatiens
Common eastern bumble bee
Bimp\BIMP16151
Bombus impatiens
Common eastern bumble bee
Bimp\BIMP14904
Bombus impatiens
Common eastern bumble bee
Bimp\BIMP25428
Bombus terrestris
Buff-tailed bumblebee
Bter\15203980
Bombus terrestris
Buff-tailed bumblebee
Bter\15207411
Bombus terrestris
Buff-tailed bumblebee
Bter\15209666
Linepithema humile
Argentine ant
Lhum\LH12354
Linepithema humile
Argentine ant
Lhum\LH21302
Linepithema humile
Argentine ant
Lhum\LH21803
Megachile rotundata
Alfalfa leafcutting bee
Mrot\MROTU:001e42
Megachile rotundata
Alfalfa leafcutting bee
Mrot\MROTU:002430
Megachile rotundata
Alfalfa leafcutting bee
Mrot\MROTU:002c83
Megachile rotundata
Alfalfa leafcutting bee
Mrot\MROTU:001ed9
Nasonia vitripennis
Parasitic wasp
Nvit\Nasvi2EG008319
Nasonia vitripennis
Parasitic wasp
Nvit\Nasvi2EG002344
Nasonia vitripennis
Parasitic wasp
Nvit\Nasvi2EG002830
Nasonia vitripennis
Parasitic wasp
Nvit\Nasvi2EG007999
Nasonia vitripennis
Parasitic wasp
Nvit\Nasvi2EG003712
Nasonia vitripennis
Parasitic wasp
Nvit\Nasvi2EG002346
Dendroctonus ponderosae
Mountain pine beetle
Dpod\YQE_11145
Dendroctonus ponderosae
Mountain pine beetle
Dpod\YQE_06831
Dendroctonus ponderosae
Mountain pine beetle
Dpod\YQE_06803
Dendroctonus ponderosae
Mountain pine beetle
Dpod\YQE_01683
Dendroctonus ponderosae
Mountain pine beetle
Dpod\YQE_06804
Tribolium castaneum
Red flour beetle
Tcas\TC033493
Tribolium castaneum
Red flour beetle
Tcas\TC010172
Tribolium castaneum
Red flour beetle
Tcas\TC031639
Tribolium castaneum
Red flour beetle
Tcas\hsp68b
Tribolium castaneum
Red flour beetle
Tcas\Hem
Tribolium castaneum
Red flour beetle
Tcas\TC000188
Pediculus humanus
Human body louse
Phum\PHUM126800
Pediculus humanus
Human body louse
Phum\PHUM333930
Pediculus humanus
Human body louse
Phum\PHUM588610
Pediculus humanus
Human body louse
Phum\PHUM018540
Rhodnius prolixus
Kissing bug
Rpro\RPRC004310
Rhodnius prolixus
Kissing bug
Rpro\RPRC009759
Rhodnius prolixus
Kissing bug
Rpro\RPRC012193
Cimex lectularius
Bed bug
Clec\CLEC002869
Cimex lectularius
Bed bug
Clec\CLEC002762
Cimex lectularius
Bed bug
Clec\CLEC010952
Cimex lectularius
Bed bug
Clec\CLEC025196
Cimex lectularius
Bed bug
Clec\CLEC010950
Cimex lectularius
Bed bug
Clec\CLEC005841
Cimex lectularius
Bed bug
Clec\CLEC025196-PB
Acyrthosiphon pisum
Pea aphid
Apim\ACYPI007961
Acyrthosiphon pisum
Pea aphid
Apim\ACYPI000474
Acyrthosiphon pisum
Pea aphid
Apim\ACYPI000903
Acyrthosiphon pisum
Pea aphid
Apim\ACYPI001597
Acyrthosiphon pisum
Pea aphid
Apim\ACYPI080190
Acyrthosiphon pisum
Pea aphid
Apim\ACYPI008763
Acyrthosiphon pisum
Pea aphid
Apim\ACYPI004809
Acyrthosiphon pisum
Pea aphid
Apim\ACYPI067751
Acyrthosiphon pisum
Pea aphid
Apim\ACYPI073873
Acyrthosiphon pisum
Pea aphid
Apim\ACYPI080139
Zootermopsis nevadensis
Nevada dampwood termite
Znev\Znev_05273
Zootermopsis nevadensis
Nevada dampwood termite
Znev\Znev_04366
Zootermopsis nevadensis
Nevada dampwood termite
Znev\Znev_06862
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
Smar\SMAR004960
Strigamia maritima
European centipede
Smar\SMAR013707
Strigamia maritima
European centipede
Smar\SMAR004796
Ixodes scapularis
Black-legged tick
Isca\ISCW009279
Ixodes scapularis
Black-legged tick
Isca\ISCW024910
Ixodes scapularis
Black-legged tick
Isca\ISCW017456
Ixodes scapularis
Black-legged tick
Isca\ISCW011425
Stegodyphus mimosarum
African social velvet spider
Smim\KFM80380.1
Stegodyphus mimosarum
African social velvet spider
Smim\KFM78034.1
Stegodyphus mimosarum
African social velvet spider
Smim\KFM83474.1
Stegodyphus mimosarum
African social velvet spider
Smim\KFM76829.1
Stegodyphus mimosarum
African social velvet spider
Smim\KFM83484.1
Stegodyphus mimosarum
African social velvet spider
Smim\KFM78035.1
Stegodyphus mimosarum
African social velvet spider
Smim\KFM69762.1
Stegodyphus mimosarum
African social velvet spider
Smim\KFM83486.1
Stegodyphus mimosarum
African social velvet spider
Smim\KFM57777.1
Stegodyphus mimosarum
African social velvet spider
Smim\KFM69761.1
Tetranychus urticae
Two-spotted spider mite
Turt\tetur03g03320
Tetranychus urticae
Two-spotted spider mite
Turt\tetur11g01700
Tetranychus urticae
Two-spotted spider mite
Turt\tetur03g03330
Daphnia pulex
Water flea
Dpux\DAPPUDRAFT_227800
Daphnia pulex
Water flea
Dpux\DAPPUDRAFT_302856
Daphnia pulex
Water flea
Dpux\DAPPUDRAFT_303127
Daphnia pulex
Water flea
Dpux\DAPPUDRAFT_256736
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
Spur\Sp-Hsp701E
Strongylocentrotus purpuratus
Purple sea urchin
Spur\Sp-Hsp701C
Strongylocentrotus purpuratus
Purple sea urchin
Spur\Sp-Hsp701A
Strongylocentrotus purpuratus
Purple sea urchin
Spur\Sp-Hsp701D
Strongylocentrotus purpuratus
Purple sea urchin
Spur\Sp-Hsp703A
Strongylocentrotus purpuratus
Purple sea urchin
Spur\Sp-Hsp701B
Strongylocentrotus purpuratus
Purple sea urchin
Spur\Sp-Nckap1_1
Strongylocentrotus purpuratus
Purple sea urchin
Spur\Sp-Nckap1
Ciona intestinalis
Vase tunicate
Cint\LOC100187210
Ciona intestinalis
Vase tunicate
Cint\ENSCING00000003184
Ciona intestinalis
Vase tunicate
Cint\hsp70
Gallus gallus
Domestic chicken
Ggal\NCKAP1
Gallus gallus
Domestic chicken
Ggal\ENSGALG00000027417
Gallus gallus
Domestic chicken
Ggal\HSP70
Gallus gallus
Domestic chicken
Ggal\HSPA8
Paralogs
Downloads
Download All DIOPT Paralogs
Paralogs (via DIOPT v7.1)
Drosophila melanogaster (Fruit fly) (13)
Gene Symbol
Score
Source
Compara
eggNOG
Homologene
Inparanoid
Isobase
OrthoDB
OrthoFinder
orthoMCL
Panther
RoundUp
Alignment
Hsp68
7 of 10
Hsp70Aa
7 of 10
Hsp70Bbb
7 of 10
Hsp70Bc
7 of 10
Hsc70-1
6 of 10
Hsc70-2
6 of 10
Hsc70-3
6 of 10
Hsc70-4
6 of 10
Hsp70Ab
6 of 10
Hsp70Bb
6 of 10
CG7182
3 of 10
Hsc70-5
2 of 10
Hem
1 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
    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.
    Homo sapiens (Human)
    Gene name
    Score
    OMIM
    OMIM Phenotype
    DO term
    Complementation?
    Transgene?
    HSPA1B; heat shock protein family A (Hsp70) member 1B
    6 of 15
    603012
        HSPA1A; heat shock protein family A (Hsp70) member 1A
        5 of 15
        140550
             
            HSPA1L; heat shock protein family A (Hsp70) member 1 like
            5 of 15
            140559
                 
                HSPA6; heat shock protein family A (Hsp70) member 6
                5 of 15
                140555
                    HSPA2; heat shock protein family A (Hsp70) member 2
                    4 of 15
                    140560
                        HSPA5; heat shock protein family A (Hsp70) member 5
                        4 of 15
                        138120
                            HSPA8; heat shock protein family A (Hsp70) member 8
                            4 of 15
                            600816
                                 
                                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
                                Show neighbor-neighbor interactions:
                                Select Layout:
                                Legend:
                                Protein
                                RNA
                                Selected Interactor(s)
                                Interactions Browser
                                View in Interactions Browser
                                Please see the Physical Interaction reports below for full details
                                protein-protein
                                Physical Interaction
                                Assay
                                References
                                Hsp70Ba - Hsp27
                                experimental knowledge based
                                (Guruharsha et al., 2011)
                                Hsp70Ba - Hsp70Aa
                                experimental knowledge based
                                (Guruharsha et al., 2011)
                                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
                                Signaling Pathways (FlyBase)
                                Metabolic Pathways
                                External Data
                                Genomic Location and Detailed Mapping Data
                                Chromosome (arm)
                                3R
                                Recombination map
                                3-52
                                Cytogenetic map
                                87B12-87B12
                                Sequence location
                                3R:12,465,453..12,467,776 [-]
                                FlyBase Computed Cytological Location
                                Cytogenetic map
                                Evidence for location
                                87B12-87B12
                                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)
                                (Ranz et al., 1997, Lis et al., 1981, Ish-Horowicz et al., 1979, Schedl et al., 1978)
                                87C-87C
                                (determined by in situ hybridisation)
                                (Segarra et al., 1996, Papaceit and Juan, 1993)
                                Experimentally Determined Recombination Data
                                Location
                                3-52
                                (FlyBase, 2016)
                                3-49.5
                                (Comeron et al., 2012)
                                Left of (cM)
                                Right of (cM)
                                Notes
                                Stocks and Reagents
                                Stocks (4)
                                Genomic Clones (10)
                                 

                                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
                                BDGP DGC clones
                                Other clones
                                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)
                                BDGP DGC clones
                                Other clones
                                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
                                Member gene of
                                Hsp70
                                (Nikolaidis and Nei, 2004)
                                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.
                                (Gong and Golic, 2006)
                                Flies with no copies of the Hsp70 genes (Hsp70Aa, Hsp70Ab, Hsp70Ba, Hsp70Bb, Hsp70Bbb and Hsp70Bc) are viable and fertile.
                                (Gong and Golic, 2004)
                                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.
                                (Bettencourt, 2002.1.16)
                                New annotation (CG31449) in release 3 of the genome annotation.
                                (FlyBase Genome Annotators, 2002-2003)
                                Area matching Drosophila heat shock gene at 87c,proximal end, Acc. No. K01294.
                                (Davies, 2001.3.15)
                                Natural variation in Hsp70 expression is analysed to study thermotolerance.
                                (Krebs and Feder, 1997)
                                The rate and intensity of Hsp70Ba protein expression has been compared with tissue damage after heat shock.
                                (Krebs and Feder, 1997)
                                Expression is rapidly induced in the testis after heat stress. Activation of Hsp70 in testes and heads necessitates the presence of a functional Hsf.
                                (Michaud et al., 1997)
                                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.
                                (Otsuka et al., 1997)
                                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.
                                (Espinas et al., 1996)
                                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.
                                (Segarra et al., 1996)
                                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.
                                (Winegarden et al., 1996)
                                The in vitro binding of Hsf protein to the promoter region of a number of heat shock genes has been analysed.
                                (Fernandes et al., 1995)
                                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.
                                (O'Brien et al., 1995)
                                The molecular architecture of the Hsp70Ba promoter has been analysed by genomic footprinting.
                                (Weber and Gilmour, 1995)
                                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.
                                (Wheeler et al., 1995)
                                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.
                                (Munks and Turner, 1994)
                                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.
                                (O'Brien et al., 1994)
                                Chromosome staining reveals that Trl and heat shock transcription factors (HSF) colocalises at Hsp70Ba.
                                (Tsukiyama et al., 1994)
                                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.
                                (Vazquez and Schedl, 1994)
                                The transcription of heat shock proteins, except Hsp83, is independent of the p200 subunit of initiation factor eIF-4F, eIF-4G.
                                (Zapata et al., 1994)
                                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.
                                (Giardina and Lis, 1993)
                                Hsp70 proteins are of prime importance to heat tolerance.
                                (Parsell et al., 1993)
                                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.
                                (Rubin et al., 1993)
                                Identified in 2D gels of CMW W2 wing imaginal disc cell proteins.
                                (Santaren et al., 1993)
                                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.
                                (Vazquez et al., 1993)
                                Hsp70 promoter driven expression in heat induced and non-heat induced conditions is more efficient in D.melanogaster embryos than in L.cuprina embryos.
                                (Atkinson and O'Brochta, 1992)
                                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.
                                (Kroeger and Rowe, 1992)
                                The effect of aging on the expression of the "Hsp70" genes (Hsp70Aa, Hsp70Ab, Hsp70Ba, Hsp70Bb and Hsp70Bc) has been studied.
                                (Niedzwiecki et al., 1991)
                                Translation of Hsp70 mRNAs and to a lesser extent the mRNAs for the small heat shock proteins is almost independent of eIF-4E.
                                (Zapata et al., 1991)
                                Induction of heat shock protein after metal ion exposure is studied.
                                (Bournias-Vardiabasis et al., 1990)
                                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.
                                (Shermoen and Beckendorf, 1982)
                                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 and 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, Livak, Morimoto, Freund, and Meselson, 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 ( 74 )
                                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 Nucleotide - A collection of sequences from several sources, including GenBank, RefSeq, TPA, and PDB.
                                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.
                                RefSeq - A comprehensive, integrated, non-redundant, well-annotated set of reference sequences including genomic, transcript, and protein.
                                UniProt/Swiss-Prot - Manually annotated and reviewed records of protein sequence and functional information
                                Other crossreferences
                                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.
                                Flygut - An atlas of the Drosophila adult midgut
                                GenomeRNAi - A database for cell-based and in vivo RNAi phenotypes and reagents
                                iBeetle-Base - RNAi phenotypes in the red flour beetle (Tribolium castaneum)
                                InterPro - A database of protein families, domains and functional sites
                                KEGG Genes - Molecular building blocks of life in the genomic space.
                                modMine - A data warehouse for the modENCODE project
                                Linkouts
                                BioGRID - A database of protein and genetic interactions.
                                DroID - A comprehensive database of gene and protein interactions.
                                DRSC - Results frm RNAi screens
                                FLIGHT - Cell culture data for RNAi and other high-throughput technologies
                                FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
                                FlyCyc Genes - Genes from a BioCyc PGDB for Dmel
                                FlyMine - An integrated database for Drosophila genomics
                                InterologFinder - Protein-protein interactions (PPI) from both known and predicted PPI data sets.
                                KEGG Pathways - Wiring diagrams of molecular interactions, reactions and relations.
                                MIST (protein-protein) - An integrated Molecular Interaction Database
                                Synonyms and Secondary IDs (25)
                                Reported As
                                Symbol Synonym
                                CG31449
                                (Jensen et al., 2013, Ni et al., 2011.7.19, Ni et al., 2010.12.1, Hughes et al., 2008, Neal et al., 2006)
                                Dm-hsp70
                                (Hernandez et al., 2004)
                                HSP70
                                (Nelson et al., 2016, Doganlar and Doganlar, 2015, Olalekan Abolaji et al., 2014, Schriner et al., 2014, Todd et al., 2013, Hurt et al., 2009, Farny et al., 2008, Sakaguchi et al., 2008, Chartier et al., 2006, Folk et al., 2006, Warrick and Boyd, 2006, Gerber et al., 2005, Papaconstantinou et al., 2005, Driscoll and Gerstbrein, 2003, Bondinas et al., 2002, Garbuz et al., 2002, Mitchell-Olds and Knight, 2002, Zoghbi and Botas, 2002, Bondinas et al., 2001, Foley and Luckinbill, 2001, Aalfs and Kingston, 2000, Takada et al., 2000, Mantovani, 1999, Takahashi and Fujiwara, 1999, Warrick et al., 1999, Karlin and Brocchieri, 1998, Ogbourne and Antalis, 1998, Jedlicka et al., 1997, Nover and Scharf, 1997, Singh and Lakhotia, 1995, Rubin et al., 1993)
                                Hsp 70
                                (Zuckerkandl, 1997)
                                Hsp-70
                                (Pimenta de Castro et al., 2012)
                                Hsp70
                                (Gumeni et al., 2019, Prasad et al., 2019, Berson 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, Fuda et al., 2015, Funikov et al., 2015, Lashmanova et al., 2015, Maheshwari et al., 2014, Tower et al., 2014, Zhang et al., 2014, Sinadinos et al., 2013, Calabria et al., 2012, Fredriksson et al., 2012, Schneiderman et al., 2012, Morettini et al., 2011, Bartkowiak et al., 2010, Hrizo and Palladino, 2010, Jensen et al., 2010, Kwon et al., 2010, Tian 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, Bhargav et al., 2008, Brandt and Corces, 2008, Cai 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, 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, 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 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, Kingston et al., 1996, Winegarden et al., 1996, Engel and Cornelius, 1995, Gehring and Wehner, 1995, Li and Duncan, 1995, O'Brien 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)
                                (Henikoff, 1990)
                                Hsp70B
                                (Sørensen et al., 2019, Yan et al., 2017, Buchon et al., 2009, Meisel, 2009, Chen et al., 2008, Ranz et al., 2001, Ranz et al., 2001, Whitfield, 2001.1.4, Ashburner, 2000.10.30, Ranz et al., 1997, Ruiz et al., 1997)
                                Hsp70Ba
                                (Engel et al., 2019, Kennerdell et al., 2018, Leow et al., 2018, Seong et al., 2017, DeSalvo et al., 2014, Kim et al., 2014, Taylor et al., 2014, Azad and Haddad, 2013, Jensen et al., 2013, O'Sullivan et al., 2013, Stefanatos et al., 2013, Telonis-Scott et al., 2013, Japanese National Institute of Genetics, 2012.5.21, Cernilogar et al., 2011, Shieh and Bonini, 2011, Takahashi et al., 2011, Kong et al., 2010, Takahashi et al., 2010, Tian et al., 2010, Azad et al., 2009, Haney and Feder, 2009, Kuan et al., 2009, Moskalev et al., 2009, Xia and Holcik, 2009, Bettencourt et al., 2008, Fisher et al., 2008, Huang et al., 2008, Xi et al., 2008, Baird et al., 2006, Bergman et al., 2006, Dorus et al., 2006, Korol et al., 2006, Shilova et al., 2006, Nikolaidis and Nei, 2004)
                                dHsp70
                                (Bell et al., 2007)
                                dhsp70
                                (Rabindran et al., 1994)
                                hsp-70
                                (Belikov et al., 1990, Luis et al., 1990)
                                hsp70
                                (Hu et al., 2019, Sharma et al., 2018, Pereira and Paro, 2017, Tsakiri et al., 2017, Xu et al., 2016, Shukla et al., 2014, Soh et al., 2013, 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, Pankotai et al., 2010, 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, 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, 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, Boehm et al., 2003, Feder, 2003, Gilmour, 2003.4.18, Gong and Golic, 2003, Goodman et al., 2003, Helfand and Rogina, 2003, Kellum, 2003, Saunders et al., 2003, Schwartz 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, 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, Gdula et al., 1998, Gregory and Horz, 1998, John and Workman, 1998, Liang and Biggin, 1998, Lis, 1998, Martinez-Balbas et al., 1998, Nevo, 1998, Vernick and McCutchan, 1998, Wilkins and Lis, 1998, Wu et al., 1998, Curtsinger 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, Segarra et al., 1996, Shopland and Lis, 1996, Tower, 1996, Elefant and Palter, 1995, Fernandes et al., 1995, Granok et al., 1995, Rasmussen and Lis, 1995, Wheeler et al., 1995, 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, 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, Soeller et al., 1993, Vazquez et al., 1993, Atkinson and O'Brochta, 1992, Fleming 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, Sorger, 1991, Zapata et al., 1991, Elgin, 1990, Helms and Rottman, 1990, Karlin 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)
                                hsp70 87C
                                (Shermoen and Beckendorf, 1982)
                                hsp70 Ba
                                (Kellett and McKechnie, 2005)
                                hsp70B
                                (Olovnikov et al., 2013, Huang et al., 2008, Gong and Golic, 2004)
                                hsp70Ba
                                (Ryazansky et al., 2016, Jevtov et al., 2015, Lerman and Feder, 2005, Lerman et al., 2003, Bettencourt, 2002.1.16, Bettencourt and Feder, 2002, Lerman et al., 2002, Bettencourt and Feder, 2001, Bettencourt et al., 1999)
                                hsp70b
                                (Yagi and Ip, 2005)
                                hsp70ba
                                (Ou et al., 2016)
                                Name Synonyms
                                87C locus
                                (Lakhotia et al., 1990)
                                Heat-shock-protein-70Ba
                                Protein 70
                                (Bournias-Vardiabasis et al., 1990)
                                heat shock 70
                                (Lo et al., 2002)
                                heat shock protein 70BA
                                (Mosqueira et al., 2010)
                                heat-shock protein 70
                                (Farny et al., 2008, Iijima-Ando et al., 2005)
                                hsp70 87C
                                (Casper et al., 2011)
                                Secondary FlyBase IDs
                                • FBgn0001232
                                • FBgn0051449
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                                Experimental Role
                                Project
                                Project Type
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                                References (492)