FB2026_01 , released March 12, 2026
FB2026_01 , released March 12, 2026
Gene: Dmel\Hsp27
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General Information
Symbol
Dmel\Hsp27
Species
D. melanogaster
Name
Heat shock protein 27
Annotation Symbol
CG4466
Feature Type
protein_coding_gene
FlyBase ID
FBgn0289994
Gene Model Status
Current
Stock Availability
13 publicly available
Gene Summary
Heat shock protein 27 (Hsp27) encodes a member of the ATP-independent, small heat shock protein family. It contributes to regulation of eye morphology, polyglutamine toxicity, lifespan and starvation tolerance. [Date last reviewed: 2019-03-07] (FlyBase Gene Snapshot)
All Summaries
Also Known As

Hsp28, DmHsp27, Dhsp27, Hsp 27

Key Links
Genomic Location
Cytogenetic map
67B3-67B3
Sequence location
Recombination map
3-29
RefSeq locus
NT_037436 REGION:9384063..9385694
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
Gene Ontology (GO) Annotations (13 terms)
Molecular Function (3 terms)
Terms Based on Experimental Evidence (3 terms)
CV Term
Evidence
References
enables protein binding
inferred from physical interaction with FLYBASE:lwr; FB:FBgn0010602
(Joanisse et al., 1998)
enables protein folding chaperone
inferred from direct assay
(Morrow et al., 2006)
enables unfolded protein binding
inferred from direct assay
(Morrow et al., 2006)
Terms Based on Predictions or Assertions (1 term)
CV Term
Evidence
References
enables unfolded protein binding
inferred from sequence model
(Li et al., 2009)
inferred from biological aspect of ancestor with PANTHER:PTN000897708
(GO Reference Genome Project, 2011-)
Biological Process (7 terms)
Terms Based on Experimental Evidence (7 terms)
CV Term
Evidence
References
involved_in behavioral response to starvation
inferred from mutant phenotype
(Hao et al., 2007)
involved_in defense response to bacterium
inferred from mutant phenotype
(Chen et al., 2010)
involved_in defense response to fungus
inferred from mutant phenotype
(Chen et al., 2010)
involved_in determination of adult lifespan
inferred from mutant phenotype
(Wang et al., 2004)
involved_in protein folding
inferred from direct assay
(Morrow et al., 2006)
involved_in protein refolding
inferred from direct assay
(Vos et al., 2016)
involved_in response to heat
inferred from direct assay
(Vos et al., 2016)
Terms Based on Predictions or Assertions (3 terms)
CV Term
Evidence
References
involved_in protein folding
inferred from sequence model
(Li et al., 2009)
involved_in protein refolding
inferred from biological aspect of ancestor with PANTHER:PTN000897708
(GO Reference Genome Project, 2011-)
involved_in response to heat
inferred from biological aspect of ancestor with PANTHER:PTN000897708
(GO Reference Genome Project, 2011-)
Cellular Component (3 terms)
Terms Based on Experimental Evidence (3 terms)
CV Term
Evidence
References
located_in cytoplasm
inferred from high throughput direct assay
(Lee et al., 2014)
part_of endoplasmic reticulum chaperone complex
inferred from physical interaction with FLYBASE:Hsp83; FB:FBgn0001233,FLYBASE:Xport-A; FB:FBgn0038749
(Rosenbaum et al., 2011)
located_in nucleus
inferred from high throughput direct assay
(Lee et al., 2014)
Terms Based on Predictions or Assertions (2 terms)
CV Term
Evidence
References
is_active_in cytoplasm
inferred from biological aspect of ancestor with PANTHER:PTN000897708
(GO Reference Genome Project, 2011-)
is_active_in nucleus
inferred from biological aspect of ancestor with PANTHER:PTN000897708
(GO Reference Genome Project, 2011-)
Gene Group (FlyBase)
Protein Family (UniProt)
Belongs to the small heat shock protein (HSP20) family. (P02518)
Protein Signatures (InterPro)
Summaries
Gene Snapshot
Heat shock protein 27 (Hsp27) encodes a member of the ATP-independent, small heat shock protein family. It contributes to regulation of eye morphology, polyglutamine toxicity, lifespan and starvation tolerance. [Date last reviewed: 2019-03-07]
Gene Group (FlyBase)
SMALL HEAT SHOCK PROTEINS -
The small Heat Shock Protein (sHSP) family is characterized by the presence of an α-crystallin domain. sHSPs play a crucial role in protein folding. Most sHSPs have the ability to prevent protein aggregation and to maintain substrate proteins in a refoldable state. (Adapted from FBrf0228040 and FBrf0231212).
Phenotypic Description (Red Book; Lindsley and Zimm 1992)
Hsp22 - Hsp-G3
There are seven closely related heat-shock genes at 67B (Ayme and Tissieres, 1985; Pauli, Arrigo, Vasquez, Tonka, and Tissieres, 1989, Genome 31: 671-76). In addition to the four small heat-shock genes previously identified (Hsp22, Hsp23, Hsp26, and Hsp27), three more genes (Hsp-G1, Hsp-G2, and Hsp-G3, formerly called Gene1, Gene2, and Gene3) have been found clustered within 15 kb of DNA at the same 67B cytological location. All seven genes are heat-shock inducible in almost all cells at the stages tested (Ayme and Tissieres, 1985). The genes are also transcribed during certain developmental stages in the absence of heat shock (Sirotkin and Davidson, 1982, Dev. Biol. 89: 196-210). Pauli et al (1989) report that the maximum accumulation of developmental rRNA in a majority of these small heat-shock genes occurs in the white pupae stage; in Hsp-G2, however, a small transcipt is found in embryos, first and second instar larvae, and young pupae; and a larger transcript in the pupal and adult stages of males (Pauli and Tonka, 1987, J. Mol. Biol. 198: 235-40; Pauli, Tonka, and Ayme-Southgate, 1988, J. Mol. Biol. 200: 47-53). In absence of stress, the expression of Hsp26 has been observed in spermatocytes, nurse cells, epithelium, imaginal discs, proventriculus, and neurocytes (Glaser, Wolfner, and Lis, 1986, EMBO 5: 747-54). Transcripts of Hsp26 and Hsp27 accumulate in adult ovaries, apparently originating in nurse cells (Zimmerman, Petri, and Meselson, 1983, Cell 32: 1161-70).
Gene Model and Products
Number of Transcripts
2
Number of Unique Polypeptides
1

Please see the JBrowse view of Dmel\Hsp27 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
Structure
Protein 3D structure   (Predicted by AlphaFold)   (AlphaFold entry P02518)

If you don't see a structure in the viewer, refresh your browser.
Model Confidence:
  • Very high (pLDDT > 90)
  • Confident (90 > pLDDT > 70)
  • Low (70 > pLDDT > 50)
  • Very low (pLDDT < 50)

AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Some regions with low pLDDT may be unstructured in isolation.

Experimentally Determined Structures
Crossreferences
Comments on Gene Model

Gene model reviewed during 5.41

Gene model reviewed during 5.46

Gene model reviewed during 5.56

Transcript Data
Annotated Transcripts
Name
FlyBase ID
RefSeq ID
Length (nt)
Assoc. CDS (aa)
Hsp27-RA
FBtr0076454
NM_079276
1220
213
Hsp27-RB
FBtr0346541
NM_001300072
1632
213
Additional Transcript Data and Comments
Reported size (kB)

1.25 (northern blot)

(Corces et al., 1980)
Comments
External Data
Crossreferences
Polypeptide Data
Annotated Polypeptides
Name
FlyBase ID
Predicted MW (kDa)
Length (aa)
Theoretical pI
UniProt
RefSeq ID
GenBank
Hsp27-PA
FBpp0076182
23.6
213
7.50
P02518
NP_524000
AAF50285
Hsp27-PB
FBpp0312159
23.6
213
7.50
P02518
NP_001287001
AHN58026
Polypeptides with Identical Sequences

The group(s) of polypeptides indicated below share identical sequence to each other.

213 aa isoforms: Hsp27-PA, Hsp27-PB
Additional Polypeptide Data and Comments
Reported size (kDa)

213 (aa); 23.62 (kD predicted)

(Southgate et al., 1983)

27.091 (kD predicted)

(Ingolia and Craig, 1982)

27 (kD observed)

(Craig and McCarthy, 1980)
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\Hsp27 using the Feature Mapper tool.

External Data
Crossreferences
Linkouts
Expression Data
Testis-specificity index

The testis specificity index was calculated from modENCODE tissue expression data by Vedelek et al., 2018 to indicate the degree of testis enrichment compared to other tissues. Scores range from -2.52 (underrepresented) to 5.2 (very high testis bias).

-0.03

Transcript Expression
in situ
Stage
Tissue/Position (including subcellular localization)
Reference
embryonic stage
ventral midline of embryo
(Wheeler et al., 2009)
embryonic stage 1 -- 3
organism | posterior

Comment: maternally deposited

(Fisher et al., 2012)
embryonic stage 4 -- 6
primordial germ cell
(Fisher et al., 2012)
embryonic stage 7 -- 8
primordial germ cell
(Fisher et al., 2012)
embryonic stage 9 -- 10
germline cell
(Fisher et al., 2012)
embryonic stage 11 -- 12
antennal primordium

Comment: reported as procephalon primordium

(Fisher et al., 2012)
central brain primordium

Comment: reported as procephalon primordium

(Fisher et al., 2012)
dorsal head epidermis primordium

Comment: reported as procephalon primordium

(Fisher et al., 2012)
lateral head epidermis primordium

Comment: reported as procephalon primordium

(Fisher et al., 2012)
ventral head epidermis primordium

Comment: reported as procephalon primordium

(Fisher et al., 2012)
visual primordium

Comment: reported as procephalon primordium

(Fisher et al., 2012)
embryonic central brain glial cell
(Fisher et al., 2012)
embryonic ganglion mother cell
(Fisher et al., 2012)
embryonic neuroblast of ventral nerve cord primordium
(Fisher et al., 2012)
germline cell
(Fisher et al., 2012)
larval lateral VNC glial cell
(Fisher et al., 2012)
larval ventral midline glial cell
(Fisher et al., 2012)
mushroom body primordium
(Fisher et al., 2012)
pars intercerebralis primordium
(Fisher et al., 2012)
procephalic neuroblast
(Fisher et al., 2012)
ventral nerve cord primordium
(Fisher et al., 2012)
embryonic stage 13 -- 16
embryonic brain
(Fisher et al., 2012)
embryonic central brain neuron
(Fisher et al., 2012)
embryonic pars intercerebralis
(Fisher et al., 2012)
embryonic central brain surface glial cell
(Fisher et al., 2012)
larval nervous system
(Fisher et al., 2012)
germline cell
(Fisher et al., 2012)
lateral cord neuron
(Fisher et al., 2012)
larval lateral VNC surface glial cell
(Fisher et al., 2012)
ventral midline of embryo
(Fisher et al., 2012)
larval ventral nerve cord
(Fisher et al., 2012)
northern blot
Stage
Tissue/Position (including subcellular localization)
Reference
embryonic stage 1 -- 6

Comment: reference states <=2-3 hr AEL

(Pauli et al., 1989)
wandering third instar larval stage
organism
(Pauli et al., 1989)
prepupal stage
(Pauli et al., 1989)
Additional Descriptive Data

Hsp27 transcripts are initially detected in early embryogenesis, and subsequently disappear. Hsp27 transcripts reappear starting at late third larval instar, and a second peak is observed in white prepupae.

(Pauli et al., 1989)
Marker for
 
Subcellular Localization
CV Term
Polypeptide Expression
mass spectroscopy
Stage
Tissue/Position (including subcellular localization)
Reference
adult stage
adult head
• membrane
(Aradska et al., 2015)
western blot
Stage
Tissue/Position (including subcellular localization)
Reference
embryonic stage
(Pauli et al., 1989)
first instar larval stage
(Pauli et al., 1989)
pupal stage
(Pauli et al., 1989)
Additional Descriptive Data

Hsp27 protein is first detected in embryos and first larval instar. The protein is detected at very low levels in prepupae, and peaks at mid-pupal stages, when Hsp27 transcript has almost disappeared.

(Pauli et al., 1989)
Marker for
 
Subcellular Localization
CV Term
Evidence
References
located_in cytoplasm
inferred from high throughput direct assay
(Lee et al., 2014)
part_of endoplasmic reticulum chaperone complex
inferred from physical interaction with FLYBASE:Hsp83; FB:FBgn0001233,FLYBASE:Xport-A; FB:FBgn0038749
(Rosenbaum et al., 2011)
located_in nucleus
inferred from high throughput direct assay
(Lee et al., 2014)
Expression Deduced from Reporters
High-Throughput Expression Data
Associated Tools

JBrowse - Visual display of RNA-Seq signals

View Dmel\Hsp27 in JBrowse
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
DRscDB - A single-cell RNA-seq resource for data mining and data comparison across species
EMBL-EBI Single Cell Expression Atlas - Single cell expression across species
FlyAtlas2 - A Drosophila melanogaster expression atlas with RNA-Seq, miRNA-Seq and sex-specific data
Fly-FISH - A database of Drosophila embryo and larvae mRNA localization patterns
Images
FlyBase Wiki
Image Based Resources
Alleles, Insertions, Transgenic Constructs, and Aberrations
Classical and Insertion Alleles ( 16 )
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 Hsp27
Transgenic constructs containing regulatory region of Hsp27
Aberrations (Deficiencies and Duplications) ( 1 )
Inferred from experimentation ( 1 )
Gene disrupted in
Df(3L)sHSP
(Greenblatt et al., 2019)
Inferred from location ( 5 )
Variants
Variant Molecular Consequences
Alleles Representing Disease-Implicated Variants
Phenotypes
Orthologs
Downloads
Download All DIOPT Orthologs
Human Orthologs (via DIOPT v9.1)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Source
Compara
Domainoid
eggNOG
Hieranoid
Homologene
Inparanoid
OMA
OrthoDB
OrthoFinder
OrthoInspector
orthoMCL
Panther
Phylome
SonicParanoid
Alignment
Complementation?
Transgene?
Homo sapiens (Human) (11)
Hsap\CRYAA2
7 of 14
Yes
No
Hsap\CRYAA
7 of 14
Yes
No
Hsap\HSPB6
7 of 14
Yes
No
Hsap\CRYAB
6 of 14
No
No
6  
Hsap\HSPB1
3 of 14
No
No
3  
Hsap\HSPB2
3 of 14
No
No
Hsap\HSPB3
3 of 14
No
No
2  
Hsap\HSPB8
3 of 14
No
No
7  
Hsap\HSPB7
2 of 14
No
No
3  
Hsap\HSPB9
2 of 14
No
No
Hsap\ODF1
1 of 14
No
Yes
Model Organism Orthologs (via DIOPT v9.1)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Source
Compara
Domainoid
eggNOG
Hieranoid
Homologene
Inparanoid
OMA
OrthoDB
OrthoFinder
OrthoInspector
orthoMCL
Panther
Phylome
SonicParanoid
Alignment
Complementation?
Transgene?
Rattus norvegicus (Norway rat) (10)
Rnor\Hspb6
8 of 14
Yes
No
Rnor\Cryaa
7 of 14
No
No
Rnor\Cryab
7 of 14
No
No
Rnor\Hspb1
3 of 14
No
No
Rnor\Hspb2
3 of 14
No
No
Rnor\Hspb3
3 of 14
No
No
Rnor\Hspb8
3 of 14
No
No
Rnor\Hspb7
2 of 14
No
No
Rnor\Hspb9
2 of 14
No
No
Rnor\Odf1
1 of 14
No
Yes
Mus musculus (laboratory mouse) (10)
Mmus\Hspb6
8 of 14
Yes
No
Mmus\Cryaa
7 of 14
No
No
Mmus\Cryab
7 of 14
No
No
Mmus\Hspb1
3 of 14
No
No
Mmus\Hspb2
3 of 14
No
No
Mmus\Hspb3
3 of 14
No
No
Mmus\Hspb7
2 of 14
No
No
Mmus\Hspb8
2 of 14
No
No
Mmus\Hspb9
1 of 14
No
No
Mmus\Odf1
1 of 14
No
Yes
Xenopus tropicalis (Western clawed frog) (13)
Xtro\cryaa
6 of 13
Yes
No
Xtro\cryab
6 of 13
Yes
No
Xtro\hspb6
6 of 13
Yes
No
Xtro\LOC100489058
3 of 13
No
Yes
Xtro\LOC100489207
3 of 13
No
Yes
Xtro\LOC100491399
3 of 13
No
Yes
Xtro\hsp30d
2 of 13
No
Yes
Xtro\hspb1
2 of 13
No
No
Xtro\hspb2
2 of 13
No
Yes
Xtro\hspb3
2 of 13
No
Yes
Xtro\hspb8
2 of 13
No
Yes
Xtro\cblb
1 of 13
No
No
Xtro\hsp30e
1 of 13
No
Yes
Danio rerio (Zebrafish) (13)
Drer\cryaa
7 of 14
Yes
No
Drer\cryaba
7 of 14
Yes
No
Drer\hspb6
7 of 14
Yes
No
Drer\cryabb
6 of 14
No
No
Drer\hspb1
5 of 14
No
No
Drer\hspb15
5 of 14
No
No
Drer\si:dkey-1k23.3
4 of 14
No
No
Drer\hspb3
3 of 14
No
No
Drer\hspb8
3 of 14
No
No
Drer\hspb11
3 of 14
No
No
Drer\hspb2
2 of 14
No
No
Drer\hspb9
2 of 14
No
No
Drer\hspb7
1 of 14
No
No
Caenorhabditis elegans (Nematode, roundworm) (19)
Cele\hsp-17
8 of 14
Yes
Yes
Cele\F08H9.3
6 of 14
No
No
Cele\hsp-12.2
6 of 14
No
No
Cele\hsp-16.1
6 of 14
No
No
Cele\hsp-16.2
6 of 14
No
No
Cele\hsp-16.11
6 of 14
No
No
Cele\hsp-16.41
6 of 14
No
No
Cele\hsp-16.48
6 of 14
No
No
Cele\hsp-16.49
6 of 14
No
No
Cele\F08H9.4
5 of 14
No
No
Cele\hsp-12.1
5 of 14
No
No
Cele\hsp-12.3
5 of 14
No
No
Cele\hsp-12.6
5 of 14
No
No
Cele\sip-1
5 of 14
No
No
Cele\ZK1128.7
5 of 14
No
Yes
Cele\Y55F3BR.6
4 of 14
No
No
Cele\hsp-43
3 of 14
No
Yes
Cele\hsp-25
2 of 14
No
No
Cele\F58H7.1
1 of 14
No
Yes
Anopheles gambiae (African malaria mosquito) (8)
Agam\AgaP_AGAP005547
7 of 12
Yes
Yes
Agam\AgaP_AGAP005548
7 of 12
Yes
Yes
Agam\AgaP_AGAP007158
6 of 12
No
Yes
Agam\AgaP_AGAP007159
6 of 12
No
Yes
Agam\AgaP_AGAP007161
6 of 12
No
No
Agam\AgaP_AGAP007160
5 of 12
No
Yes
Agam\AgaP_AGAP007162
5 of 12
No
No
Agam\AgaP_AGAP000941
2 of 12
No
No
Arabidopsis thaliana (thale-cress) (17)
Atha\AT1G07400
4 of 13
Yes
No
Atha\AT1G53540
4 of 13
Yes
No
Atha\AT1G59860
4 of 13
Yes
No
Atha\AT2G29500
4 of 13
Yes
No
Atha\AT5G37670
4 of 13
Yes
Yes
Atha\HSP17.4
4 of 13
Yes
No
Atha\HSP18.2
4 of 13
Yes
No
Atha\HSP21
4 of 13
Yes
No
Atha\AT1G52560
3 of 13
No
No
Atha\AT4G21870
3 of 13
No
No
Atha\ATHSP22.0
3 of 13
No
No
Atha\HSP17.6A
3 of 13
No
No
Atha\HSP17.6II
3 of 13
No
No
Atha\HSP23.6-MITO
3 of 13
No
No
Atha\AT1G54050
2 of 13
No
No
Atha\AT5G51440
2 of 13
No
No
Atha\AT2G19310
1 of 13
No
No
Saccharomyces cerevisiae (Brewer's yeast) (0)
Schizosaccharomyces pombe (Fission yeast) (2)
Spom\hsp16
1 of 12
Yes
No
Spom\SPCC338.06c
1 of 12
Yes
Yes
Escherichia coli (enterobacterium) (2)
Ecol\ibpA
2 of 11
Yes
No
Ecol\ibpB
2 of 11
Yes
No
Other Organism Orthologs (via OrthoDB)
Data provided directly from OrthoDB:Hsp27. Refer to their site for version information.
Paralogs
Downloads
Download All DIOPT Paralogs
Paralogs (via DIOPT v9.1)
Gene Symbol
Score
Source
Compara
Domainoid
eggNOG
Homologene
Inparanoid
OMA
OrthoDB
OrthoFinder
OrthoInspector
orthoMCL
Panther
Phylome
SonicParanoid
Alignment
Drosophila melanogaster (Fruit fly) (10)
Hsp67Bc
10 of 13
l(2)efl
10 of 13
Hsp23
9 of 13
Hsp26
9 of 13
Hsp67Ba
9 of 13
CG4461
8 of 13
CG7409
7 of 13
CG13133
7 of 13
CG14207
7 of 13
Hsp22
7 of 13
Human Disease Associations
FlyBase Human Disease Model Reports
    Disease Ontology (DO) Annotations
    Models Based on Experimental Evidence ( 0 )
    Allele
    Disease
    Evidence
    References
    Potential Models Based on Orthology ( 1 )
    Human Ortholog
    Disease
    Evidence
    References
    CRYAA; crystallin alpha A
    model of  cataract 9 multiple types
    IEA
    (FlyBase, 2019-)
    Modifiers Based on Experimental Evidence ( 4 )
    Disease Associations of Human Orthologs (via DIOPT v9.1 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?
    Hsap\CRYAA2
    7 of 14
        CRYAA; crystallin alpha A
        7 of 14
        123580
        HSPB6; heat shock protein family B (small) member 6
        7 of 14
        610695
            CRYAB; crystallin alpha B
            6 of 14
            CRYSTALLIN, ALPHA-B; CRYAB
             
            HSPB1; heat shock protein family B (small) member 1
            3 of 14
            HEAT-SHOCK 27-KD PROTEIN 1; HSPB1
             
            HSPB2; heat shock protein family B (small) member 2
            3 of 14
            602179
                HSPB3; heat shock protein family B (small) member 3
                3 of 14
                HEAT-SHOCK 27-KD PROTEIN 3; HSPB3
                 
                HSPB8; heat shock protein family B (small) member 8
                3 of 14
                HEAT-SHOCK 22-KD PROTEIN 8; HSPB8
                 
                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
                Interaction Browsers
                View in FlyBase Interactions Browser   View in MIST tool (external link)
                Please see the Physical Interaction reports below for full details
                protein-protein
                Physical Interaction
                Assay
                References
                Hsp27
                dynamic light scattering, molecular sieving, molecular weight estimation by staining, classical fluorescence spectroscopy, comigration in non denaturing gel electrophoresis
                (Moutaoufik et al., 2017)
                Hsp27 - CG18004
                experimental knowledge based
                (Guruharsha et al., 2011)
                Hsp27 - CG32313
                experimental knowledge based
                (Guruharsha et al., 2011)
                Hsp27 - CG3434
                experimental knowledge based
                (Guruharsha et al., 2011)
                Hsp27 - CG3726
                anti tag coimmunoprecipitation, peptide massfingerprinting, experimental knowledge based
                (Rhee et al., 2014)
                Hsp27 - E(z)
                tandem affinity purification, Identification by mass spectrometry
                (Kang et al., 2015)
                Hsp27 - GstE8
                experimental knowledge based
                (Guruharsha et al., 2011)
                Hsp27 - Gtf3c3
                anti tag coimmunoprecipitation, peptide massfingerprinting, experimental knowledge based
                (Rhee et al., 2014)
                Hsp27 - Hsp22
                experimental knowledge based
                (Guruharsha et al., 2011)
                Hsp27 - Hsp23
                experimental knowledge based
                (Guruharsha et al., 2011)
                Hsp27 - Hsp26
                experimental knowledge based
                (Guruharsha et al., 2011)
                Hsp27 - Hsp68
                experimental knowledge based
                (Guruharsha et al., 2011)
                Hsp27 - Hsp70Aa
                experimental knowledge based
                (Guruharsha et al., 2011)
                Hsp27 - Hsp70Ba
                experimental knowledge based
                (Guruharsha et al., 2011)
                Hsp27 - Phb2
                experimental knowledge based
                (Guruharsha et al., 2011)
                Hsp27 - Rpt1
                experimental knowledge based
                (Guruharsha et al., 2011)
                Hsp27 - Tgt
                experimental knowledge based
                (Guruharsha et al., 2011)
                Hsp27 - Trmt6
                experimental knowledge based
                (Guruharsha et al., 2011)
                Hsp27 - Xport-A
                western blot, anti bait coimmunoprecipitation
                (Rosenbaum et al., 2011)
                Hsp27 - cnn
                anti bait coimmunoprecipitation, peptide massfingerprinting
                (Habermann et al., 2012)
                Hsp27 - p53
                anti bait coimmunoprecipitation, western blot
                (Lei et al., 2017)
                Hsp27 - ref(2)P
                experimental knowledge based
                (Guruharsha et al., 2011)
                Summary of Genetic Interactions
                Interaction Browsers
                View in FlyBase Interactions Browser   View in MIST tool (external link)
                Please look at the allele data for full details of the genetic interactions
                Starting gene(s)
                Interaction type
                Interacting gene(s)
                Reference
                Hsp27
                suppressible
                Atg7
                (Chen et al., 2012)
                Starting gene(s)
                Interaction type
                Interacting gene(s)
                Reference
                brm
                suppressible
                Hsp27
                (Tegeder et al., 2019)
                slbo
                suppressible
                Hsp27
                (Rorth et al., 1998)
                External Data
                Linkouts
                Pathways
                Signaling Pathways (FlyBase)
                Metabolic Pathways
                FlyBase
                External Links
                External Data
                Linkouts
                Class of Gene
                Genomic Location and Detailed Mapping Data
                Chromosome (arm)
                3L
                Recombination map
                3-29
                Cytogenetic map
                67B3-67B3
                Sequence location
                FlyBase Computed Cytological Location
                Cytogenetic map
                Evidence for location
                67B3-67B3
                Limits computationally determined from genome sequence between P{EP}Hsp26EP3336&P{EP}Hsp26EP3315 and P{PZ}fry02240
                Experimentally Determined Cytological Location
                Cytogenetic map
                Notes
                References
                67B1-67B2
                (determined by in situ hybridisation)
                (Cuenca et al., 1998)
                67B-67B
                (determined by in situ hybridisation)
                (Segarra et al., 1996, Papaceit and Juan, 1993, Voellmy et al., 1981)
                Experimentally Determined Recombination Data
                Location

                3-29

                (FlyBase, 2016)

                3-23.0

                (Comeron et al., 2012)
                Left of (cM)
                Right of (cM)
                (Peterson et al., 1979)
                Notes
                Stocks and Reagents
                Stocks (13)
                Genomic Clones (17)
                 

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

                cDNA Clones (127)
                 

                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 JBrowse for alignment of the cDNAs and ESTs to the gene model.

                cDNA clones, fully sequenced
                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
                    Antibody Information
                    Laboratory Generated Antibodies
                     

                    polyclonal

                    (Greenblatt et al., 2019)

                    monoclonal

                    (Moutaoufik et al., 2017)
                    Commercially Available Antibodies
                     
                    Cell Line Information
                    Publicly Available Cell Lines
                     
                      Other Stable Cell Lines
                       
                        Other Comments

                        Expression is enriched in embryonic gonads.

                        (Shigenobu et al., 2006)

                        Co-immunoprecipitation with an antibody raised against lwr confirms interaction with Hsp23 and Hsp26 and preferentially with Hsp27.

                        (Joanisse et al., 1998)

                        Heat shock does not appreciably affect the expression pattern of the small heat shock proteins and the same cell-specific pattern is observed after heat shock. Hsp23 and Hsp27 show cell-specific pattern of expression in the testes, the relative amount of Hsf also varies in the different cell types. Cells that do not express the proteins in the absence of stress are similarly unable to mount a heat shock response.

                        (Michaud et al., 1997)

                        In murine L929 fibrosarcoma cells the constitutive expression of Hsp27 significantly decreases the intracellular levels of ROS and therefore rendered the burst of these reactive species caused by tumour necrosis factor (TNFα) harmless. The protective mechanism (raising the intracellular concentration of glutathione) of Hsp27 differs from that mediated by Hsp70 proteins.

                        (Mehlen et al., 1996)

                        The DNA between the TATA box and the heat shock elements (HSEs) is constitutively organised by a positioned nucleosome, effectively shortening the distance between the distal HSEs and the TATA box.

                        (Quivy and Becker, 1996)

                        Expression of Hsp27 in human L929 fibrosarcoma cells confers resistance to tumor necrosis factor (TNF) and protects cells against oxidative stress induced by hydrogen peroxide or menadione.

                        (Mehlen et al., 1995)

                        Hsp27 RNA levels do not increase with age.

                        (Wheeler et al., 1995)

                        DNase hypersensitive sites (DHS) in the 5' regions of Hsp27 and Hsp23 are mapped in salivary glands developmentally exposed to ecdysone during larval-prepupal transition. The DHSs reveal the sites that correlate with the hormonal induction of tissue-specific expression.

                        (Dubrovsky et al., 1994)

                        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)

                        Chromosome staining reveals that Trl and heat shock transcription factors (HSF) colocalises at Hsp27.

                        (Tsukiyama et al., 1994)

                        Biochemical fractionation and indirect immunofluorescence analysis indicates that the protective function of Hsp27 is localised at the level of the nucleus.

                        (Mehlen et al., 1993)

                        RNA polymerase II density on the Hsp27 gene is rapidly increased by heat shock.

                        (O'Brien and Lis, 1993)

                        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.

                        (Vazquez et al., 1993)

                        Sequences that regulate hormone-dependent Hsp27 expression have been studied using reporter genes.

                        (Berger et al., 1992)

                        Exposure of cells to pulses of elevated temperature 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. 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. Similar response inducible by other stressful treatments. The response may be elicited at all stages of the life cycle and in cultured cells.

                        (Lindsley and Zimm, 1992)

                        Immunoblot analysis demonstrates that Hsp27 protein can confer thermal resistance in Chinese hamster O23 cells following 3.5 hours of heat treatment at 44oC.

                        (Rollet et al., 1992)

                        Response elements of Hsp27 and Hsp23 can confer hormonal regulation on a basal promoter in vivo and render transcription in vitro dependent on purified ecdysterone receptor.

                        (Luo et al., 1991)

                        Sequences that regulate ecdysone-responsive Hsp27 expression have been studied using reporter genes.

                        (Martinez et al., 1991)

                        EcR binds as a dimer to an imperfect palindromic sequence (GGTTCAATGCACT) in the Hsp27 promoter region.

                        (Ozyhar 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)

                        Mutations at br reduce the transcription rate or stability of the small heat shock protein mRNAs.

                        (Dubrovsky et al., 1990)

                        The binding sites for the protein factors required for activation of transcription of Hsp genes are multiple short upstream sequence elements called HSEs or heat shock consensus elements.

                        (Xiao and Lis, 1988, Pelham, 1982)

                        Ecol\CAT transient assay in culture cells shows the ecdysone response of the Hsp27 promoter is mediated by multiple regulatory elements clustered 500bp 5' to the gene. Heat induction depends on three heat shock regulatory elements (HSE) at about position -300.

                        (Riddihough and Pelham, 1986)

                        Heat-shock inducible in almost all cells at the stages tested.

                        (Ayme-Southgate and Tissieres, 1985)

                        Activation of transcription of Hsp genes apparently involves the sequential binding of two or more protein factors in vicinity of TATA box.

                        (Wu, 1984)

                        Transcripts of Hsp26 and Hsp27 accumulate in adult ovaries, apparently originating in nurse cells.

                        (Zimmerman et al., 1983)

                        Polymerase II dissociates from most chromosome regions and accumulates at the new heat shock puff sites upon heat shock.

                        (Bonner and Kerby, 1982)

                        Hsp27 is transcribed during certain developmental stages in the absence of heat shock.

                        (Sirotkin and Davidson, 1982)

                        The effects of heat shock may be abrogated to some degree by pretreatment with a pulse of a slightly lower temperature.

                        (Petersen and Mitchell, 1981, Mitchell et al., 1979)

                        Mitochondrial and histone-gene activities persist transcription and translation.

                        (Spradling et al., 1977)

                        In polytene cells, during heat shock response, existing puffs regress and a novel group quickly appear at 33B, 63C, 64F, 67B, 70A, 87A, 87C, 93D, 95D.

                        (Tissieres et al., 1974)

                        The heat shock 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 et al., 1974)

                        In polytene cells, during heat shock response, existing puffs regress and a novel group quickly appear at cytological locations 33B, 63C, 64F, 67B, 70A, 87A, 87C, 93D, 95D.

                        (Ashburner, 1970)
                        Relationship to Other Genes
                        Source for database merge of

                        Source for merge of: Hsp27 BG00737

                        (Lavagnino et al., 2013)

                        Source for merge of: Hsp27 anon-WO0140519.69

                        (FlyBase, 1996-)
                        Additional comments

                        Source for merge of Hsp27 anon-WO0140519.69 was sequence comparison ( date:051113 ).

                        (FlyBase, 1996-)
                        Nomenclature History
                        Source for database identify of
                        Nomenclature comments
                        Etymology
                        Synonyms and Secondary IDs (29)
                        Reported As
                        Symbol Synonym
                        27
                        (Frydenberg et al., 2010)
                        27K
                        (Chung et al., 1993)
                        28
                        (Petersen and Lindquist, 1988)
                        BG00737
                        CG4466
                        (Çiçek et al., 2016, Vos et al., 2016, Rosa-Ferreira et al., 2015, Lim et al., 2011, Müller et al., 2010, Ni et al., 2010.12.1, Keleman et al., 2009.8.5, Hughes et al., 2008, Talamillo et al., 2008, Pal et al., 2007, Fakhouri et al., 2006, Lundgren et al., 2005)
                        Dhsp27
                        (Mehlen et al., 1996, Mehlen et al., 1995, Mehlen et al., 1993)
                        DmHSP27
                        (Zhang et al., 2011)
                        DmHsp27
                        (Moutaoufik et al., 2017, Wang et al., 2014, Morrow et al., 2000)
                        Dmel23.6
                        (Li et al., 2009)
                        HSP27
                        (Samson et al., 2025, Ecker et al., 2017, Vos et al., 2016, Olalekan Abolaji et al., 2014, Lundgren et al., 2005, Nover and Scharf, 1997)
                        HSP28
                        (Bondinas et al., 2002)
                        Hsp 27
                        (Carreira et al., 2011)
                        Hsp27
                        (Proshkina et al., 2025, Whitmore et al., 2025, Hersperger et al., 2024, Scharenbrock et al., 2024, Wu et al., 2024, Floc'hlay et al., 2023, Lee et al., 2023, Saini et al., 2023, Yheskel et al., 2023, Zheng et al., 2023, Gallo et al., 2022, Golubev et al., 2022, Gupta et al., 2022, Känel et al., 2022, Perlegos et al., 2022, Cattenoz et al., 2021, Faragó et al., 2021, Kong et al., 2021, Moutaoufik and Tanguay, 2021, Shaposhnikov et al., 2021, Xie et al., 2021, Yamaguchi et al., 2021, Yi et al., 2021, Cho et al., 2020, Ramond et al., 2020, Santana et al., 2020, Seong et al., 2020, Engel et al., 2019, Erwin and Blumenstiel, 2019, Greenblatt et al., 2019, Kockel et al., 2019, Rivera et al., 2019, Singh and Tapadia, 2019, Sørensen et al., 2019, Hemphill et al., 2018, Jagla et al., 2018, Kennerdell et al., 2018, Lei et al., 2017, Wu et al., 2017, Yang and Veraksa, 2017, Donovan and Marr, 2016, Fabre et al., 2016, Gajan et al., 2016, Maistrenko et al., 2016, Pandey et al., 2016, Chen et al., 2015, Hull et al., 2015, Kang et al., 2015, Štětina et al., 2015, Van Bortle et al., 2015, Xie et al., 2015, Faisal et al., 2014, Lee et al., 2014, Marr et al., 2014, Mulakkal et al., 2014, Shlyueva et al., 2014, Sopko et al., 2014, Taylor et al., 2014, Toshima et al., 2014, Kwon et al., 2013, Lavagnino et al., 2013, Stefanatos et al., 2013, Telonis-Scott et al., 2013, Chauhan et al., 2012, Chen et al., 2012, Eleftherianos and Castillo, 2012, Fredriksson et al., 2012, Habermann et al., 2012, Japanese National Institute of Genetics, 2012.5.21, Kellner et al., 2012, Stern et al., 2012, Franco et al., 2011, Friedman et al., 2011, Handler et al., 2011, Ren et al., 2011, Rosenbaum et al., 2011, Wang et al., 2011, Arancio et al., 2010, Bina et al., 2010, Blanco et al., 2010, Chen et al., 2010, Colinet et al., 2010, Kallappagoudar et al., 2010, Kong et al., 2010, Mosqueira et al., 2010, Müller et al., 2010, Tian et al., 2010, Bernardo et al., 2009, Takemori and Yamamoto, 2009, Wheeler et al., 2009, Bettencourt et al., 2008, Blanco et al., 2008, Fisher et al., 2008, Hanyu-Nakamura et al., 2008, Hoopfer et al., 2008, Liu and Lehmann, 2008, Mensch et al., 2008, Michaud et al., 2008, Xi et al., 2008, Ahrens et al., 2007, Muse et al., 2007, Muse et al., 2007, Pal et al., 2007, Tadros et al., 2007, Baird et al., 2006, Neal et al., 2006, Shigenobu et al., 2006, Walser et al., 2006, Birch-Machin et al., 2005, Lundgren et al., 2005, Geiger-Thornsberry and Mackay, 2004, Loop et al., 2004, Gim et al., 2001)
                        Hsp28
                        (Gallo et al., 2022, Duncan, 2008, Duncan, 2005, Ahmed and Duncan, 2004, Bondinas et al., 2001, Cuenca et al., 1998, Molto et al., 1994, Molto et al., 1992)
                        anon-WO0140519.69
                        dHSP27
                        (Mordes et al., 2018)
                        hsp 27
                        (Jongens et al., 1988)
                        hsp-27
                        (Wang et al., 2000)
                        hsp26
                        (Dubrovsky et al., 1994)
                        hsp27
                        (Golubev et al., 2025, Eickelberg et al., 2022, Sirocko et al., 2022, Geronikolou et al., 2018, Sharma et al., 2018, Jevtov et al., 2015, Bernardo et al., 2014, Blanchard et al., 2014, Pandey et al., 2014, Brianti et al., 2013, Soh et al., 2013, Pakula et al., 2012, Zoglowek et al., 2012, He et al., 2011, Johnston et al., 2011, Kugler et al., 2011, Sala et al., 2011, Schauer et al., 2011, Tower, 2011, Frydenberg et al., 2010, Krusiński et al., 2010, Beatty et al., 2009, Lee et al., 2008, Liao et al., 2008, Sudi et al., 2008, Hao et al., 2007, Dobryszycki et al., 2006, Tsuda et al., 2006, Kurapati et al., 2004, Poels et al., 2004, Sawatsubashi et al., 2004, Wang et al., 2004, Ringrose et al., 2003, Rymarczyk et al., 2003, Chen et al., 2002, Seo et al., 2002, Wang and Benzer, 2002, Burns et al., 2001, Grad et al., 2001, Mouillet et al., 2001, Fivaz et al., 2000, Henrich et al., 2000, Jiang et al., 2000, Kurapati et al., 2000, Niedziela-Majka et al., 2000, King and Tower, 1999, Lezzi et al., 1999, Perera et al., 1999, Crispi et al., 1998, Niedziela-Majka et al., 1998, Rorth et al., 1998, Wang et al., 1998, Elke et al., 1997, Lehmann et al., 1997, Otsuka et al., 1997, Strutt et al., 1997, Wilkins and Lis, 1997, Huet et al., 1996, Mehlen et al., 1996, Mikitani, 1996.9.4, Quivy and Becker, 1996, Shopland and Lis, 1996, Antoniewski et al., 1995, Fernandes et al., 1995, Mikitani, 1995, Rasmussen and Lis, 1995, Wheeler et al., 1995, Champlin and Lis, 1994, Dubrovsky et al., 1994, Jindra, 1994, Quivy and Becker, 1994, Southgate, 1994.2.17, Antoniewski et al., 1993, Ayme-Southgate, 1993.2.23, Cherbas, 1993, Heikkila, 1993, Mehlen et al., 1993, O'Brien and Lis, 1993, Vazquez et al., 1993, Andres and Thummel, 1992, Berger et al., 1992, Pauli et al., 1992, Amin et al., 1991, Cherbas et al., 1991, Dobens et al., 1991, Koelle et al., 1991, Luo et al., 1991, Ozyhar et al., 1991, Vazquez, 1991, Zapata et al., 1991, Berger and Dobens, 1990, Galceran et al., 1990, Haass et al., 1990, Maschat et al., 1990, Ornelles and Penman, 1990, Pauli et al., 1990, Thummel, 1990, Pauli et al., 1989, Pauli et al., 1988, Pauli and Tonka, 1987, Ayme-Southgate and Tissieres, 1985, Southgate et al., 1983, Ingolia and Craig, 1981)
                        hsp27/26
                        (Munks and Turner, 1994)
                        hsp28
                        (Segarra et al., 1996, Heino et al., 1995, Molto et al., 1993, Papaceit and Juan, 1993, Yost et al., 1990, Hoffman and Corces, 1984)
                        small hsp locus 67B
                        (Yao et al., 2007)
                        Name Synonyms
                        Heat shock protein 237
                        (Manh et al., 2005)
                        Heat shock protein 27
                        (Hull et al., 2015, Toshima et al., 2014, Davis et al., 2011, Lim et al., 2011, Gim et al., 2001)
                        Hsp 27
                        (Takemori and Yamamoto, 2009)
                        Protein 27
                        (Bournias-Vardiabasis et al., 1990)
                        heat shock protein 27
                        (Chen et al., 2012)
                        heat shock protein hsp27
                        (Ingolia, 1994.2.16)
                        heatshock protein 27
                        (Faisal et al., 2014)
                        hsp27
                        (Chetverina et al., 2021)
                        Secondary FlyBase IDs
                        • FBgn0001226
                        • FBgn0010232
                        • FBgn0044559
                        • FBgn0265486
                        Datasets (0)
                        Study focus (0)
                        Experimental Role
                        Project
                        Project Type
                        Title
                        Study result (0)
                        Result
                        Result Type
                        Title
                        External Crossreferences and Linkouts ( 49 )
                        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/GCRP - The gene-centric reference proteome (GCRP) provides a 1:1 mapping between genes and UniProt accessions in which a single 'canonical' isoform represents the product(s) of each protein-coding gene.
                        UniProt/Swiss-Prot - Manually annotated and reviewed records of protein sequence and functional information
                        UniProt/TrEMBL - Automatically annotated and unreviewed records of protein sequence and functional information
                        Other crossreferences
                        AlphaFold DB - AlphaFold provides open access to protein structure predictions for the human proteome and other key proteins of interest, to accelerate scientific research.
                        DRscDB - A single-cell RNA-seq resource for data mining and data comparison across species
                        EMBL-EBI Single Cell Expression Atlas - Single cell expression across species
                        FlyAtlas2 - A Drosophila melanogaster expression atlas with RNA-Seq, miRNA-Seq and sex-specific data
                        InterPro - A database of protein families, domains and functional sites
                        KEGG Genes - Molecular building blocks of life in the genomic space.
                        MARRVEL_MODEL - MARRVEL (model organism gene)
                        Linkouts
                        FlyCyc Genes - Genes from a BioCyc PGDB for Dmel
                        Fly-FISH - A database of Drosophila embryo and larvae mRNA localization patterns
                        References (386)