P02828 · HSP83_DROME
- ProteinHeat shock protein 83
- GeneHsp83
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids717 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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.
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHeat shock protein 83
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP02828
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
RNAi-mediated knockdown is lethal at third instar larva stage and shows decreased levels of sicily, ND-42, and ND-30.
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 234 | in strain: MA-10.2, DPF-13, DPF-82.1, EM-10, 178.7, 709.6 and MA-4.4 | ||||
Sequence: Missing | ||||||
Natural variant | 368 | in strain: DPF-2, DPF-30, DPF-62, MA-10.2, DPF-82.1, 178.7, DPF-13, MA-4.4, EM-10, VC-805, MA-4.2, DPF-46, DPF-77, VC-815 and 709.6 | ||||
Sequence: N → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000062930 | 1-717 | Heat shock protein 83 | |||
Sequence: MPEEAETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELYIKLIPNKTAGTLTIIDTGIGMTKSDLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVADKVTVTSKNNDDEQYVWESSAGGSFTVRADNSEPLGRGTKIVLYIKEDQTDYLEESKIKEIVNKHSQFIGYPIKLLVEKEREKEVSDDEADDEKKEGDEKKEMETDEPKIEDVGEDEDADKKDKDAKKKKTIKEKYTEDEELNKTKPIWTRNPDDISQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRTPFDLFENQKKRNNIKLYVRRVFIMDNCEDLIPEYLNFMKGVVDSEDLPLNISREMLQQNKVLKVIRKNLVKKTMELIEELTEDKENYKKFYDQFSKNLKLGVHEDSNNRAKLADFLRFHTSASGDDFCSLADYVSRMKDNQKHVYFITGESKDQVSNSAFVERVKARGFEVVYMTEPIDEYVIQHLKEYKGKQLVSVTKEGLELPEDESEKKKREEDKAKFESLCKLMKSILDNKVEKVVVSNRLVDSPCCIVTSQFGWSANMERIMKAQALRDTATMGYMAGKKQLEINPDHPIVETLRQKADADKNDKAVKDLVILLFETSLLSSGFSLDSPQVHASRIYRMIKLGLGIDEDEPMTTDDAQSAGDAPSLVEDTEDASHMEEVD | ||||||
Modified residue | 219 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 294 | Phosphotyrosine | ||||
Sequence: Y |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
In contrast to other major heat shock proteins, this one is also expressed at normal growth temperatures. It is also developmentally expressed during oogenesis.
Gene expression databases
Interaction
Subunit
Homodimer (By similarity).
Forms a complex with Hop and piwi; probably Hop mediates the interaction between piwi and Hsp83 (PubMed:21186352).
Forms a complex including sicily, ND-42 and Hsp83; the complex is necessary to chaperone ND-42 in the cytoplasm before mitochondrial import; the interaction with sicily is direct and is dependent on its ATPase activity (PubMed:23509070).
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).
Interacts with mora (PubMed:31907206).
Forms a complex with Hop and piwi; probably Hop mediates the interaction between piwi and Hsp83 (PubMed:21186352).
Forms a complex including sicily, ND-42 and Hsp83; the complex is necessary to chaperone ND-42 in the cytoplasm before mitochondrial import; the interaction with sicily is direct and is dependent on its ATPase activity (PubMed:23509070).
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).
Interacts with mora (PubMed:31907206).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P02828 | Nelf-E P92204 | 2 | EBI-136814, EBI-194490 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 213-241 | Basic and acidic residues | ||||
Sequence: EREKEVSDDEADDEKKEGDEKKEMETDEP | ||||||
Region | 213-263 | Disordered | ||||
Sequence: EREKEVSDDEADDEKKEGDEKKEMETDEPKIEDVGEDEDADKKDKDAKKKK | ||||||
Compositional bias | 248-263 | Basic and acidic residues | ||||
Sequence: EDEDADKKDKDAKKKK | ||||||
Region | 685-717 | Disordered | ||||
Sequence: EDEPMTTDDAQSAGDAPSLVEDTEDASHMEEVD | ||||||
Motif | 713-717 | TPR repeat-binding | ||||
Sequence: MEEVD |
Domain
The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.
Sequence similarities
Belongs to the heat shock protein 90 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length717
- Mass (Da)81,865
- Last updated1987-08-13 v1
- ChecksumA71B96B2FE1684E6
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
M9PBL3 | M9PBL3_DROME | Hsp83 | 717 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 213-241 | Basic and acidic residues | ||||
Sequence: EREKEVSDDEADDEKKEGDEKKEMETDEP | ||||||
Compositional bias | 248-263 | Basic and acidic residues | ||||
Sequence: EDEDADKKDKDAKKKK |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X03810 EMBL· GenBank· DDBJ | CAA27435.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X00065 EMBL· GenBank· DDBJ | CAA24938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014296 EMBL· GenBank· DDBJ | AAF47734.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY122080 EMBL· GenBank· DDBJ | AAM52592.1 EMBL· GenBank· DDBJ | mRNA | ||
U57459 EMBL· GenBank· DDBJ | AAB46677.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U57460 EMBL· GenBank· DDBJ | AAB46678.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U57461 EMBL· GenBank· DDBJ | AAB46679.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U57462 EMBL· GenBank· DDBJ | AAB46680.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U57463 EMBL· GenBank· DDBJ | AAB46681.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U57464 EMBL· GenBank· DDBJ | AAB46682.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U57465 EMBL· GenBank· DDBJ | AAB46683.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U57466 EMBL· GenBank· DDBJ | AAB46684.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U57467 EMBL· GenBank· DDBJ | AAB46685.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U57468 EMBL· GenBank· DDBJ | AAB46686.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U57469 EMBL· GenBank· DDBJ | AAB46687.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U57470 EMBL· GenBank· DDBJ | AAB46688.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U57471 EMBL· GenBank· DDBJ | AAB46689.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U57472 EMBL· GenBank· DDBJ | AAB46690.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U57473 EMBL· GenBank· DDBJ | AAB46691.1 EMBL· GenBank· DDBJ | Genomic DNA |