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General Information
Symbol
Dmel\Hsp83
Species
D. melanogaster
Name
Heat shock protein 83
Annotation Symbol
CG1242
Feature Type
FlyBase ID
FBgn0001233
Gene Model Status
Stock Availability
Gene Snapshot
In progress.Contributions welcome.
Also Known As
Hsp90, hsp82, l(3)j5C2, E(sev)3A, E(sina)2
Key Links
Genomic Location
Cytogenetic map
Sequence location
3L:3,192,969..3,197,059 [+]
Recombination map
3-6
Sequence
Other Genome Views
The following external sites may use different assemblies or annotations than FlyBase.
Function
GO Summary Ribbons
Protein Family (UniProt)
Belongs to the heat shock protein 90 family. (P02828)
Summaries
Gene Group (FlyBase)
HEAT SHOCK PROTEIN 90 CHAPERONES -
The Heat Shock Protein 90 (Hsp90) family of chaperones are homodimers that catalyse the ATP-dependent refolding proteins which are in a near native state, at the later stages of folding. (Adapted from PMID:16756493 and FBrf0232269).
Protein Function (UniProtKB)
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Together with Hop and piwi, mediates canalization, also known as developmental robustness, likely via epigenetic silencing of existing genetic variants and suppression of transposon-induced new genetic variation. Required for piRNA biogenesis by facilitating loading of piRNAs into PIWI proteins.
(UniProt, P02828)
Phenotypic Description (Red Book; Lindsley and Zimm 1992)
Hsp83
The structural gene for the 83,000 dalton heat-shock protein (HSP83). During development, the gene is expressed at high levels in the absence of heat shock in many tissues, especially ovaries where it apparently originates in nurse cells (Zimmerman, Petri, and Meselson, 1983, Cell 32: 1161-70). During heat shock, however, the expression level is only raised several fold (Xiao and Lis, 1989, Mol. Cell Biol. 9: 1746-53). Deletion of sequences upstream from the coding region eliminates normal developmental expression and results in regulation of Hsp83 in a manner similar to that of Hsp70 which is activated only in response to heat shock.
Summary (Interactive Fly)
a molecular chaperones that promotes the maturation of several important proteins - maintains and optimizes RNA polymerase II pausingvia stabilization of the negative elongation factor complex - promotes anaphase-promoting complex/cyclosome function during cell cycle exit - acts to generate neuroblast cortical polarity - acts to prevent phenotypic variation
Gene Model and Products
Number of Transcripts
2
Number of Unique Polypeptides
1

Please see the GBrowse view of Dmel\Hsp83 or the JBrowse view of Dmel\Hsp83 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 5.46
Sequence Ontology: Class of Gene
Transcript Data
Annotated Transcripts
Name
FlyBase ID
RefSeq ID
Length (nt)
Assoc. CDS (aa)
FBtr0073040
2713
717
FBtr0332873
2960
717
Additional Transcript Data and Comments
Reported size (kB)
3.05 (northern blot)
Comments
External Data
Crossreferences
Polypeptide Data
Annotated Polypeptides
Name
FlyBase ID
Predicted MW (kDa)
Length (aa)
Theoretical pI
RefSeq ID
GenBank
FBpp0072904
81.9
717
4.64
FBpp0305095
81.9
717
4.64
Polypeptides with Identical Sequences

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

717 aa isoforms: Hsp83-PA, Hsp83-PB
Additional Polypeptide Data and Comments
Reported size (kDa)
Comments
External Data
Subunit Structure (UniProtKB)
Homodimer (By similarity). Forms a complex with Hop and piwi; probably Hop mediates the interaction between piwi and Hsp83 (PubMed:21186352). Interacts with shu (PubMed:22902557). Interacts with Nup358 (via TPR repeats); the interaction is required for the nuclear import of the sesquiterpenoid juvenile hormone receptor Met (PubMed:27979731). Forms a complex with Dpit47 and Hsp70aa (PubMed:11493638).
(UniProt, P02828)
Domain
The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.
(UniProt, P02828)
Linkouts
Sequences Consistent with the Gene Model
Nucleotide / Polypeptide Records
 
Mapped Features

Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Hsp83 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 (25 terms)
Molecular Function (4 terms)
Terms Based on Experimental Evidence (2 terms)
CV Term
Evidence
References
inferred from physical interaction with UniProtKB:A0A0B4K7J2
(assigned by UniProt )
inferred from direct assay
Terms Based on Predictions or Assertions (3 terms)
CV Term
Evidence
References
inferred from biological aspect of ancestor with PANTHER:PTN000163632
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN000163632
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN000163527
(assigned by GO_Central )
Biological Process (13 terms)
Terms Based on Experimental Evidence (10 terms)
CV Term
Evidence
References
Terms Based on Predictions or Assertions (4 terms)
CV Term
Evidence
References
inferred from sequence or structural similarity with UniProtKB:P15108
inferred from biological aspect of ancestor with PANTHER:PTN000163629
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN000163527
(assigned by GO_Central )
inferred from sequence or structural similarity with UniProtKB:P15108
traceable author statement
inferred from biological aspect of ancestor with PANTHER:PTN000163629
(assigned by GO_Central )
Cellular Component (8 terms)
Terms Based on Experimental Evidence (5 terms)
CV Term
Evidence
References
inferred from direct assay
inferred from direct assay
inferred from high throughput direct assay
inferred from high throughput direct assay
Terms Based on Predictions or Assertions (6 terms)
CV Term
Evidence
References
inferred from biological aspect of ancestor with PANTHER:PTN000163629
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN000163629
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN000163629
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN000163629
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN000163629
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN000163629
(assigned by GO_Central )
Expression Data
Expression Summary Ribbons
Colored tiles in ribbon indicate that expression data has been curated by FlyBase for that anatomical location. Colorless tiles indicate that there is no curated data for that location.
For complete stage-specific expression data, view the modENCODE Development RNA-Seq section under High-Throughput Expression below.
Transcript Expression
in situ
Stage
Tissue/Position (including subcellular localization)
Reference
organism

Comment: maternally deposited

organism | ubiquitous

Comment: maternally-supplied transcript

organism | anterior

Comment: embryonically expressed transcript

organism | posterior

Comment: maternally-supplied transcript

anterior endoderm anlage

Comment: anlage in statu nascendi

antennal anlage in statu nascendi

Comment: reported as procephalic ectoderm anlage in statu nascendi

dorsal head epidermis anlage in statu nascendi

Comment: reported as procephalic ectoderm anlage in statu nascendi

visual anlage in statu nascendi

Comment: reported as procephalic ectoderm anlage in statu nascendi

antennal anlage

Comment: reported as procephalic ectoderm anlage

central brain anlage

Comment: reported as procephalic ectoderm anlage

dorsal head epidermis anlage

Comment: reported as procephalic ectoderm anlage

visual anlage

Comment: reported as procephalic ectoderm anlage

ventral nerve cord primordium

Comment: reported as ventral nerve cord anlage

antennal primordium

Comment: reported as procephalic ectoderm primordium

central brain primordium

Comment: reported as procephalic ectoderm primordium

visual primordium

Comment: reported as procephalic ectoderm primordium

dorsal head epidermis primordium

Comment: reported as procephalic ectoderm primordium

lateral head epidermis primordium

Comment: reported as procephalic ectoderm primordium

ventral head epidermis primordium

Comment: reported as procephalic ectoderm primordium

northern blot
Stage
Tissue/Position (including subcellular localization)
Reference
organism | posterior

Comment: Transcript level substantially decreased between 2 hr AEL and 3 hr AEL

Additional Descriptive Data
Maternally-supplied Hsp83 transcript is ubiquitous at embryonic stage 1. By embryonic stage 2 (embryonic cycle 2-3), embryonically transcribed Hsp83 is localized at the anterior pole of the embryo, while the maternally-supplied transcript is localized to the posterior pole plasm.
Marker for
 
Subcellular Localization
CV Term
Polypeptide Expression
immunolocalization
Stage
Tissue/Position (including subcellular localization)
Reference
mass spectroscopy
Stage
Tissue/Position (including subcellular localization)
Reference
Additional Descriptive Data
Hsp83 protein colocalizes with cup protein in the cytoplasm of germline stem cells in region 1, is nearly absent in the anterior of region 2 (cystoblast cleavage stage), but rises to high levels in the posterior part of region 2, and in the maturing germline cysts of region 3. Hsp83 protein is distributed in the cytoplasm of both somatic and germline derived cells throughout oogenesis.
Marker for
 
Subcellular Localization
CV Term
Evidence
References
inferred from direct assay
inferred from direct assay
inferred from high throughput direct assay
inferred from high throughput direct assay
Expression Deduced from Reporters
Reporter: P{Hsp83-GAL4}
Stage
Tissue/Position (including subcellular localization)
Reference
High-Throughput Expression Data
Associated Tools

GBrowse - Visual display of RNA-Seq signals

View Dmel\Hsp83 in GBrowse 2
RNA-Seq by Region - Search RNA-Seq expression levels by exon or genomic region
Reference
See Gelbart and Emmert, 2013 for analysis details and data files for all genes.
Developmental Proteome: Life Cycle
Developmental Proteome: Embryogenesis
External Data and Images
Linkouts
BDGP expression data - Patterns of gene expression in Drosophila embryogenesis
FLIGHT - Cell culture data for RNAi and other high-throughput technologies
FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
Fly-FISH - A database of Drosophila embryo and larvae mRNA localization patterns
Flygut - An atlas of the Drosophila adult midgut
Images
FlyExpress - Embryonic expression images (BDGP data)
  • Stages(s) 1-3
  • Stages(s) 4-6
  • Stages(s) 7-8
  • Stages(s) 9-10
  • Stages(s) 11-12
  • Stages(s) 13-16
Alleles, Insertions, and Transgenic Constructs
Classical and Insertion Alleles ( 23 )
For All Classical and Insertion Alleles Show
 
Other relevant insertions
Transgenic Constructs ( 39 )
For All Alleles Carried on Transgenic Constructs Show
Transgenic constructs containing/affecting coding region of Hsp83
Transgenic constructs containing regulatory region of Hsp83
Deletions and Duplications ( 7 )
Phenotypes
For more details about a specific phenotype click on the relevant allele symbol.
Lethality
Allele
Sterility
Allele
Other Phenotypes
Allele
Phenotype manifest in
Allele
Orthologs
Human Orthologs (via DIOPT v7.1)
Homo sapiens (Human) (3)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Alignment
Complementation?
Transgene?
13 of 15
Yes
Yes
13 of 15
Yes
Yes
3 of 15
No
No
Model Organism Orthologs (via DIOPT v7.1)
Mus musculus (laboratory mouse) (3)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Alignment
Complementation?
Transgene?
13 of 15
Yes
Yes
13 of 15
Yes
Yes
2 of 15
No
No
Rattus norvegicus (Norway rat) (4)
12 of 13
Yes
Yes
11 of 13
No
Yes
5 of 13
No
Yes
2 of 13
No
No
Xenopus tropicalis (Western clawed frog) (4)
12 of 12
Yes
Yes
11 of 12
No
Yes
2 of 12
No
Yes
2 of 12
No
No
Danio rerio (Zebrafish) (4)
13 of 15
Yes
Yes
13 of 15
Yes
Yes
12 of 15
No
Yes
3 of 15
No
No
Caenorhabditis elegans (Nematode, roundworm) (2)
13 of 15
Yes
Yes
2 of 15
No
No
Arabidopsis thaliana (thale-cress) (7)
9 of 9
Yes
Yes
8 of 9
No
Yes
8 of 9
No
Yes
8 of 9
No
Yes
2 of 9
No
No
2 of 9
No
No
2 of 9
No
No
Saccharomyces cerevisiae (Brewer's yeast) (2)
15 of 15
Yes
Yes
14 of 15
No
Yes
Schizosaccharomyces pombe (Fission yeast) (1)
12 of 12
Yes
Yes
Orthologs in Drosophila Species (via OrthoDB v9.1) ( EOG091904BZ )
Organism
Common Name
Gene
AAA Syntenic Ortholog
Multiple Dmel Genes in this Orthologous Group
Drosophila melanogaster
fruit fly
Drosophila suzukii
Spotted wing Drosophila
Drosophila simulans
Drosophila sechellia
Drosophila erecta
Drosophila yakuba
Drosophila ananassae
Drosophila pseudoobscura pseudoobscura
Drosophila persimilis
Drosophila willistoni
Drosophila willistoni
Drosophila virilis
Drosophila mojavensis
Drosophila grimshawi
Orthologs in non-Drosophila Dipterans (via OrthoDB v9.1) ( EOG091502FC )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Musca domestica
House fly
Glossina morsitans
Tsetse fly
Lucilia cuprina
Australian sheep blowfly
Mayetiola destructor
Hessian fly
Aedes aegypti
Yellow fever mosquito
Aedes aegypti
Yellow fever mosquito
Aedes aegypti
Yellow fever mosquito
Aedes aegypti
Yellow fever mosquito
Anopheles darlingi
American malaria mosquito
Anopheles darlingi
American malaria mosquito
Anopheles gambiae
Malaria mosquito
Anopheles gambiae
Malaria mosquito
Anopheles gambiae
Malaria mosquito
Culex quinquefasciatus
Southern house mosquito
Culex quinquefasciatus
Southern house mosquito
Culex quinquefasciatus
Southern house mosquito
Orthologs in non-Dipteran Insects (via OrthoDB v9.1) ( EOG090W024R )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Bombyx mori
Silkmoth
Danaus plexippus
Monarch butterfly
Heliconius melpomene
Postman butterfly
Apis florea
Little honeybee
Apis florea
Little honeybee
Apis mellifera
Western honey bee
Apis mellifera
Western honey bee
Bombus impatiens
Common eastern bumble bee
Bombus impatiens
Common eastern bumble bee
Bombus terrestris
Buff-tailed bumblebee
Bombus terrestris
Buff-tailed bumblebee
Linepithema humile
Argentine ant
Linepithema humile
Argentine ant
Megachile rotundata
Alfalfa leafcutting bee
Megachile rotundata
Alfalfa leafcutting bee
Nasonia vitripennis
Parasitic wasp
Nasonia vitripennis
Parasitic wasp
Dendroctonus ponderosae
Mountain pine beetle
Tribolium castaneum
Red flour beetle
Pediculus humanus
Human body louse
Rhodnius prolixus
Kissing bug
Rhodnius prolixus
Kissing bug
Cimex lectularius
Bed bug
Acyrthosiphon pisum
Pea aphid
Acyrthosiphon pisum
Pea aphid
Zootermopsis nevadensis
Nevada dampwood termite
Orthologs in non-Insect Arthropods (via OrthoDB v9.1) ( EOG090X0221 )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Strigamia maritima
European centipede
Ixodes scapularis
Black-legged tick
Stegodyphus mimosarum
African social velvet spider
Tetranychus urticae
Two-spotted spider mite
Daphnia pulex
Water flea
Daphnia pulex
Water flea
Daphnia pulex
Water flea
Daphnia pulex
Water flea
Daphnia pulex
Water flea
Daphnia pulex
Water flea
Daphnia pulex
Water flea
Daphnia pulex
Water flea
Orthologs in non-Arthropod Metazoa (via OrthoDB v9.1) ( EOG091G0270 )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Strongylocentrotus purpuratus
Purple sea urchin
Strongylocentrotus purpuratus
Purple sea urchin
Strongylocentrotus purpuratus
Purple sea urchin
Ciona intestinalis
Vase tunicate
Ciona intestinalis
Vase tunicate
Gallus gallus
Domestic chicken
Gallus gallus
Domestic chicken
Gallus gallus
Domestic chicken
Paralogs
Paralogs (via DIOPT v7.1)
Drosophila melanogaster (Fruit fly) (2)
5 of 10
2 of 10
Human Disease Associations
FlyBase Human Disease Model Reports
    Disease Model Summary Ribbon
    Disease Ontology (DO) Annotations
    Models Based on Experimental Evidence ( 0 )
    Allele
    Disease
    Evidence
    References
    Potential Models Based on Orthology ( 0 )
    Human Ortholog
    Disease
    Evidence
    References
    Modifiers Based on Experimental Evidence ( 1 )
    Allele
    Disease
    Interaction
    References
    Comments on Models/Modifiers Based on Experimental Evidence ( 0 )
     
    Disease Associations of Human Orthologs (via DIOPT v7.1 and OMIM)
    Note that ortholog calls supported by only 1 or 2 algorithms (DIOPT score < 3) are not shown.
    Functional Complementation Data
    Functional complementation data is computed by FlyBase using a combination of the orthology data obtained from DIOPT and OrthoDB and the allele-level genetic interaction data curated from the literature.
    Interactions
    Summary of Physical Interactions
    esyN Network Diagram
    Show neighbor-neighbor interactions:
    Select Layout:
    Legend:
    Protein
    RNA
    Selected Interactor(s)
    Interactions Browser

    Please see the Physical Interaction reports below for full details
    protein-protein
    Physical Interaction
    Assay
    References
    RNA-protein
    Physical Interaction
    Assay
    References
    Summary of Genetic Interactions
    esyN Network Diagram
    esyN Network Key:
    Suppression
    Enhancement

    Please look at the allele data for full details of the genetic interactions
    Starting gene(s)
    Interaction type
    Interacting gene(s)
    Reference
    Starting gene(s)
    Interaction type
    Interacting gene(s)
    Reference
    External Data
    Subunit Structure (UniProtKB)
    Homodimer (By similarity). Forms a complex with Hop and piwi; probably Hop mediates the interaction between piwi and Hsp83 (PubMed:21186352). Interacts with shu (PubMed:22902557). Interacts with Nup358 (via TPR repeats); the interaction is required for the nuclear import of the sesquiterpenoid juvenile hormone receptor Met (PubMed:27979731). Forms a complex with Dpit47 and Hsp70aa (PubMed:11493638).
    (UniProt, P02828 )
    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 (genetic) - An integrated Molecular Interaction Database
    MIST (protein-protein) - An integrated Molecular Interaction Database
    Pathways
    Gene Group - Pathway Membership (FlyBase)
    External Data
    Linkouts
    KEGG Pathways - Wiring diagrams of molecular interactions, reactions and relations.
    Genomic Location and Detailed Mapping Data
    Chromosome (arm)
    3L
    Recombination map
    3-6
    Cytogenetic map
    Sequence location
    3L:3,192,969..3,197,059 [+]
    FlyBase Computed Cytological Location
    Cytogenetic map
    Evidence for location
    63B11-63B11
    Limits computationally determined from genome sequence between P{PZ}l(3)0680306803 and P{PZ}kst01318
    Experimentally Determined Cytological Location
    Cytogenetic map
    Notes
    References
    63B7-63B8
    (determined by in situ hybridisation)
    63B9-63B9
    (determined by in situ hybridisation)
    63B5-63B11
    (determined by in situ hybridisation)
    88A-88A
    (determined by in situ hybridisation)
    63A1-63B12
    (determined by in situ hybridisation)
    63B-63B
    (determined by in situ hybridisation)
    Experimentally Determined Recombination Data
    Notes
    Stocks and Reagents
    Stocks (23)
    Genomic Clones (14)
     

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

    cDNA Clones (591)
     

    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
       
      Cell Signaling Technology - Commercial vendor for primary antibodies and antibody conjugates.
      Other Information
      Relationship to Other Genes
      Source for database identify of
      Source for identity of: Hsp83 CG1242
      Source for database merge of
      Source for merge of: Hsp83 ms(3)08445
      Source for merge of: Hsp83 l(3)j5C2
      Source for merge of: Hsp83 anon-WO0140519.209
      Additional comments
      Source for merge of Hsp83 anon-WO0140519.209 was sequence comparison ( date:051113 ).
      Other Comments
      Hsp83 is a potent capacitor of behavioral variation.
      RNAi screen using dsRNA made from templates generated with primers directed against this gene results in chromosome misalignment on the metaphase spindle and spindles that are aberrantly long when assayed in S2 cells. This phenotype can be observed when the screen is performed with or without Cdc27 dsRNA.
      Hsp83 is required for localisation of the nos and pgc mRNAs in the posterior pole.
      dsRNA made from templates generated with primers directed against this gene results in a change in cell proliferation and cell size.
      Expression is enriched in embryonic gonads.
      When Hsp83 alleles are combined in transheterozygotes, there are both cumulative and complementary effects on thoracic and variable bristle trait numbers, depending on the allelic combination.
      dsRNA made from templates generated with primers directed against this gene tested in RNAi screen for effects on Kc167 and S2R+ cell morphology.
      RNAi screen using dsRNA made from templates generated with primers directed against this gene causes a phenotype when assayed in Kc167 cells: change from round to spindle-shaped, with the formation of F-actin puncta and microtubule extensions. S2R+ cells are unaffected.
      The gene products of Hsp83 and the Hsc70 genes are present in a chaperone complex required for activation of DNA binding by the EcR/usp complex. The gene products of Hsp83 and the Hsc70 genes are also required in vivo for EcR activity and EcR is the primary target of the chaperone complex.
      Hsp83 may have a role in ensuring proper centrosome function.
      The joint action of two RNA degradation pathways (a maternally encoded and a zygotic pathway) controls maternal transcript degradation and its timing in the early embryo. Hsp83 transcripts (relatively high in abundance) require the action of both pathways in order to be eliminated prior to the midblastula transition.
      Hsp83 is required for normal spermatogenesis.
      Homologous genetic loci in D.subobscura and D.melanogaster tend to show a similar ultrastructure in the two species.
      In a sample of 79 genes with multiple introns, 33 showed significant heterogeneity in G+C content among introns of the same gene and significant positive correspondence between the intron and the third codon position G+C content within genes. These results are consistent with selection adding against preferred codons at the start of genes.
      Identification: Enhancer trap screen designed to discover genes involved in the cellular aspects of defense mechanisms, as well as in melanotic tumor formation processes linked to blood cell disregulation.
      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.
      Su(Raf)3A encodes Hsp83 as demonstrated by phenotypic rescue and nucleotide sequence of the mutations.
      Wild-type and mutant forms of Hsp83 bind to activated phl but the mutant Hsp83 protein causes a reduction in the kinase activity of phl. Results indicate Hsp83 is essential for phl function in vivo. Location of the E(sev) and Su(Raf) mutations of Hsp83 indicates a weak correlation between the site of mutation and its genetic nature: all but one of the hypomorphs and none of the antimorphs map to the C-terminal domain known to be involved in dimerisation.
      Identified in a genetic screen for modifiers of the phl::tor12D.sev rough eye mutant phenotype. Clonal analysis failed to recover any Hsp83 mutant clones suggesting that is required for cell proliferation.
      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.
      The in vitro binding of Hsf protein to the promoter region of a number of heat shock genes has been analysed.
      Germline clone analysis demonstrates that Hsp83 plays an essential role in germline development.
      An allele of Hsp83 was isolated in a screen for suppressors of the rough eye phenotype caused by an activated phl kinase.
      Hsp83 gene product may be required for normal sina activity.
      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.
      Splicing of Hsp83 RNA has been studied in B5228 mutant embryos.
      The transcription of heat shock proteins, except Hsp83, is independent of the p200 subunit of initiation factor eIF-4F, eIF-4G.
      Growth phase defect locus.
      Maternal mRNA localises to the pole region of the embryo.
      Hsp83 RNA is expressed in a dynamic fashion during oogenesis. Maternally synthesised Hsp83 transcripts are protected from degradation at the posterior pole of the early embryo and is a component of the posterior pole plasm. Zygotic transcription is restricted to the anterior third of the embryo, expression is controlled by bcd.
      Mutants of Hsp83 display weak suppression of tor mutant embryos, embryos display 2 to 3 abdominal denticle belts.
      The product of Hsp83 and its homologs shows a specific nuclear localization in different species of Drosophila and Chironomus. Besides being abundant in the cytoplasm, the Hsp83 product is associated with specific chromosomal loci, such as Hsrω and Dhyd\Hsrω, the telomeric Balbiani rings in Chironomus thummi and the heat-induced puff I-1C in C.tentans.
      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.
      Studies of splicing thermotolerance in Schneider cells with Hsp83 show that Hsp83 transcript is made during heat shock but not processed until the heat shock is over. As little as 10 mins of pretreatment can induce thermotolerance. In the absence of thermotolerant factors, premRNA-containing complexes leave the splicing pathway and exit to the cytoplasm. Induced thermotolerance lasts for approximately 8 hours.
      Probes from D.melanogaster were used in chromosome in situ hybridisation to study response to heat shock in D.guanche, D.madeirensis and D.subobscura. Results suggest that the 18C, 94A, 89A and 27A loci of the three obscura group species are homologous to the D.melanogaster loci Hsp83, Hsp70A, Hsp68 and the small Hsp group Hsp22, Hsp23, Hsp26 and Hsp27 respectively.
      Hsp83 is required for cell growth and viability.
      Translation of the majority of non-heat shock mRNAs and Hsp83 mRNA is very dependent on eIF-4E.
      The subcellular distribution of Hsp83 protein under normal temperature conditions and after heat shock has been determined.
      Sequence analysis of the Hsp83 gene in several species reveals a conserved 5' 34 base pair imperfect dyad made up of three overlapping copies of the consensus heat shock regulatory sequence. The heat inducible Hsp83 gene is flanked on both sides by transcription units not induced by heat shock, CG14965 and anon-63BC-T2.
      Even though Hsp83 and anon-63BC-T2 are separated by only one thousand base pairs they display strikingly different regulatory properties. anon-63BC-T2 is not heat inducible, whereas Hsp83 is.
      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. 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 et al., 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 et al., 1979; Peterson and Mitchell, 1981). For reviews of the heat-shock response see Ashburner and Bonner (1978).
      The structural gene for the 83,000 dalton heat-shock protein (HSP83). During development, the gene is expressed at high levels in the absence of heat shock in many tissues, especially ovaries where it apparently originates in nurse cells (Zimmerman, Petri, and Meselson, 1983). During heat shock, however, the expression level is only raised several fold (Xiao and Lis, 1989). Deletion of sequences upstream from the coding region eliminates normal developmental expression and results in regulation of Hsp83 in a manner similar to that of Hsp70 which is activated only in response to heat shock.
      Origin and Etymology
      Discoverer
      Etymology
      Identification
      External Crossreferences and Linkouts ( 92 )
      Sequence Crossreferences
      NCBI Gene - Gene integrates information from a wide range of species. A record may include nomenclature, Reference Sequences (RefSeqs), maps, pathways, variations, phenotypes, and links to genome-, phenotype-, and locus-specific resources worldwide.
      GenBank Protein - A collection of sequences from several sources, including translations from annotated coding regions in GenBank, RefSeq and TPA, as well as records from SwissProt, PIR, PRF, and PDB.
      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
      UniProt/TrEMBL - Automatically annotated and unreviewed records of protein sequence and functional information
      Other crossreferences
      BDGP expression data - Patterns of gene expression in Drosophila embryogenesis
      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.
      Fly-FISH - A database of Drosophila embryo and larvae mRNA localization patterns
      Flygut - An atlas of the Drosophila adult midgut
      GenomeRNAi - A database for cell-based and in vivo RNAi phenotypes and reagents
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      ApoDroso - Functional genomic database for photoreceptor development, survival and function
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      FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
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      Synonyms and Secondary IDs (36)
      Reported As
      Symbol Synonym
      Hsp83
      (Ji et al., 2019, Singh and Tapadia, 2019, Sinigaglia et al., 2019, Specchia et al., 2019, Bischof et al., 2018, Burow et al., 2018, Chung et al., 2018, Demir and Marcos, 2018, de Paula et al., 2018, Hall et al., 2018, Lefebvre and Lécuyer, 2018, Tsuboyama et al., 2018, Ashton-Beaucage and Therrien, 2017, Berson et al., 2017, Choutka et al., 2017, Galluzzi et al., 2017, Götze et al., 2017, He et al., 2017, Lakhotia, 2017, Sekiya et al., 2017, Transgenic RNAi Project members, 2017-, Yan et al., 2017, Lefebvre et al., 2016, Lycette et al., 2016, Sarov et al., 2016, Tan et al., 2016, Vourekas et al., 2016, Barckmann et al., 2015, Chen et al., 2015, Dent et al., 2015, Hull et al., 2015, Iwasaki et al., 2015, Štětina et al., 2015, Zang et al., 2015, Ashwal-Fluss et al., 2014, Benbahouche et al., 2014, Chen et al., 2014, Deivasigamani et al., 2014, He et al., 2014, Lee et al., 2014, Luck et al., 2014, McClure et al., 2014, Temme et al., 2014, White-Grindley et al., 2014, Bandura et al., 2013, Colinet et al., 2013, Kwon et al., 2013, Potdar and Sheeba, 2013, Telonis-Scott et al., 2013, Awofala et al., 2012, Chen and Wagner, 2012, Gonsalvez and Long, 2012, Haskel-Ittah et al., 2012, Howell et al., 2012, Japanese National Institute of Genetics, 2012.5.21, Olivieri et al., 2012, Reinhardt et al., 2012, Shirasaki et al., 2012, White-Cooper, 2012, Franco et al., 2011, Friedman et al., 2011, Gangaraju et al., 2011, Gonsalves et al., 2011, Morettini et al., 2011, Rees et al., 2011, Salamanca et al., 2011, Takahashi et al., 2011, Weake et al., 2011, Colinet et al., 2010, Guertin and Lis, 2010, Iwasaki et al., 2010, Kallappagoudar et al., 2010, Kwon et al., 2010, Müller et al., 2010, Sawatsubashi et al., 2010, Specchia et al., 2010, Tian et al., 2010, Wasbrough et al., 2010, Wasbrough et al., 2010, Ardehali et al., 2009, Baker and Russell, 2009, Benoit et al., 2009, Lipardi and Paterson, 2009, Lu et al., 2009, Moskalev et al., 2009, Nie et al., 2009, Pisa et al., 2009, Takemori and Yamamoto, 2009, Tan et al., 2009, Bettencourt et al., 2008, Christensen et al., 2008.12.28, Duncan, 2008, Golombieski et al., 2008, Liebl and Featherstone, 2008, Linder et al., 2008, Semotok et al., 2008, Zhai et al., 2008, Basto et al., 2007, Castorena et al., 2007, Curtis et al., 2007, Dietzl et al., 2007, Gibert et al., 2007, Goldman et al., 2007, Goshima et al., 2007, Nelson et al., 2007, Quinones-Coello, 2007, Schlötterer et al., 2007, Stuart et al., 2007, Tadros et al., 2007, Bartolome and Charlesworth, 2006, Beller et al., 2006, Braendle and Flatt, 2006, Chartier et al., 2006, Guertin et al., 2006, Korol et al., 2006, Oishi et al., 2006, Shigenobu et al., 2006, Walser et al., 2006, Yano et al., 2006, Birch-Machin et al., 2005, Kampmueller and Miller, 2005, Qin et al., 2005, Williams and Thompson, 2005, Wheeler et al., 2004, Powell et al., 2003)
      Hsp90
      (Anyagaligbo et al., 2019, Bayliak et al., 2019, Ray et al., 2019, Takahashi et al., 2018, Tsuboyama et al., 2018, Hirakata and Siomi, 2016, Hull et al., 2015, Iwasaki et al., 2015, Morgante et al., 2015, Benbahouche et al., 2014, Comoglio and Paro, 2014, Goda et al., 2014, Maheshwari et al., 2014, Zhang et al., 2014, Zhang et al., 2013, Andersen et al., 2012, Chen and Wagner, 2012, Ratzke et al., 2012, Gangaraju et al., 2011, Rosenbaum et al., 2011, Demontis and Perrimon, 2010, Hrizo and Palladino, 2010, Miyoshi et al., 2010, Sgrò et al., 2010, Specchia et al., 2010, Zhang et al., 2010, Hung et al., 2009, Pare et al., 2009, Pisa et al., 2009, Tariq et al., 2009, Duncan, 2008, Fujikake et al., 2008, Martins et al., 2008, Sgrò et al., 2008, Ahrens et al., 2007, Basto et al., 2007, Song et al., 2007, Carey et al., 2006, Milton et al., 2006, Debat et al., 2005, Duncan, 2005, Ahmed and Duncan, 2004, Chong and Whitelaw, 2004, Sangster et al., 2004, Auluck and Bonini, 2003, Baxter, 2003, Blagden and Glover, 2003, Milton et al., 2003, Ruden, 2003, Rutherford, 2003, Rutherford and Henikoff, 2003, Tatar et al., 2003, Auluck and Bonini, 2002, Ohta, 2002, Ruden et al., 2002, Rutherford, 2002, Crevel et al., 2001, Csermely, 2001, de Carcer et al., 2001, Milton et al., 2001, Young et al., 2001, Arbeitman and Hogness, 2000, Gonzalez et al., 2000, Lange et al., 2000, Metzgar and Wills, 2000, Rutherford, 2000, Rutherford et al., 2000, Caplan, 1999, Holland, 1999, Jones, 1999, McLaren, 1999, Yue et al., 1999, Cossins, 1998, Csermely et al., 1998, Rutherford and Lindquist, 1998)
      Su(Raf)3A
      anon-EST:Liang-2.53
      anon-WO0068693
      anon-WO0140519.209
      hsp83
      (Ray et al., 2019, Specchia et al., 2017, Alaraby et al., 2016, Elgart et al., 2016, Astakhova et al., 2015, Jevtov et al., 2015, Onorati et al., 2015, Uytterhoeven et al., 2015, Astakhova et al., 2014, Huang et al., 2014, Pandey et al., 2014, Brianti et al., 2013, Colinet et al., 2013, Costa et al., 2013, Malmendal et al., 2013, Riveron et al., 2013, Andersen et al., 2012, Awofala et al., 2012, Bozzetti et al., 2012, Sharma et al., 2012, Vecchio et al., 2012, Wang et al., 2012, White-Cooper, 2012, Ardehali et al., 2011, Murawska et al., 2011, Schiemann et al., 2010, Singh et al., 2010, Specchia et al., 2010, Zhang et al., 2010, Hung et al., 2009, Singh et al., 2009, Bönisch et al., 2007, De Renzis et al., 2007, Yao et al., 2007, Buszczak and Spradling, 2006, Jolly and Lakhotia, 2006, Kiebler and Bassell, 2006, Neal et al., 2006, Thompson et al., 2006, Yagi and Ip, 2005, Rehwinkel et al., 2004, Santos and Lehmann, 2004, Faucheux et al., 2003, Lakhotia, 2003, Schwartz et al., 2003, Tritto et al., 2003, Badenhorst et al., 2002, Tekotte and Davis, 2002, Gatfield et al., 2001, Herold et al., 2001, Kaminker et al., 2001, Li et al., 2001, Mahowald, 2001, Raushenbakh et al., 2001, Comeron and Kreitman, 2000, Leach et al., 2000, Lakhotia et al., 1999, Mayer and Bukau, 1999, Liang and Biggin, 1998, Rommel and Hafen, 1998, Leibovitch et al., 1997, Otsuka et al., 1997, Yiangou et al., 1997, Segarra et al., 1996, Eickbush et al., 1995, Fernandes et al., 1995, Lozovskaya et al., 1995, Munks and Turner, 1994, O'Brien et al., 1994, Ring and Lis, 1994, Zapata et al., 1994, Heikkila, 1993, Papaceit and Juan, 1993, Pauli et al., 1992, Zapata et al., 1991, Carbajal et al., 1990, O'Connor and Lis, 1981)
      stc
      Secondary FlyBase IDs
      • FBgn0004639
      • FBgn0010233
      • FBgn0011792
      • FBgn0016742
      • FBgn0024852
      • FBgn0044664
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      References (634)