C4NYP8 · F10A1_DROME
- ProteinHsc70-interacting protein 1
- GeneHIP
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids377 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
One HIP oligomer binds the ATPase domains of at least two Hsc70 molecules dependent on activation of the Hsc70 ATPase by Hsp40. Stabilizes the ADP state of Hsc70 that has a high affinity for substrate protein. Through its own chaperone activity, it may contribute to the interaction of Hsc70 with various target proteins (By similarity).
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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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | protein-containing complex | |
Molecular Function | heat shock protein binding | |
Molecular Function | Hsp70 protein binding | |
Molecular Function | protein dimerization activity | |
Molecular Function | protein-folding chaperone binding | |
Biological Process | chaperone cofactor-dependent protein refolding |
Names & Taxonomy
Protein names
- Recommended nameHsc70-interacting protein 1
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionC4NYP8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 105 | in strain: XCPA112 | ||||
Sequence: S → N | ||||||
Natural variant | 227 | in strain: XCPA25 | ||||
Sequence: E → D | ||||||
Natural variant | 290 | in strain: XCPA77, XCPA93 and XCPA126 | ||||
Sequence: G → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 3 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_0000393584 | 1-377 | Hsc70-interacting protein 1 | |||
Sequence: MAFTMQTGDLKKLKYFIDFALENPTFLNMPQLQFVKDFVEKFGGTVPPGQFNGGSAGGKCPFGGVAGAKANEPANAPEDSEDEKSLSDPESDVELDMEGVIEADSDPAQPMGNYSKKATEEEVEQASELRAQAASAYGQQKFDEAIALYTKAIELSPGNALFHAKRGQAFLKLKKPNACIRDCDVALELNSDLAAGYKFRGRARRLLGDFELAAHDLRQACKLDFDEETDEWLKEVTPNAKKIEQHRLKQERRQAERKIKERQRDQRRARKEQEKHNASSGGSSGEFSGGNPGNGNMSDILGAMSDPEVSAAIQDILSNPGNITKYASNPKIYNLIKKIVPGGDVGAAFGQAGEKAGKPSEPKPKKDSADFVDDGLD | ||||||
Modified residue | 80 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, repeat, coiled coil, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 68-123 | Disordered | ||||
Sequence: AKANEPANAPEDSEDEKSLSDPESDVELDMEGVIEADSDPAQPMGNYSKKATEEEV | ||||||
Compositional bias | 83-101 | Acidic residues | ||||
Sequence: EKSLSDPESDVELDMEGVI | ||||||
Repeat | 126-159 | TPR 1 | ||||
Sequence: ASELRAQAASAYGQQKFDEAIALYTKAIELSPGN | ||||||
Repeat | 161-193 | TPR 2 | ||||
Sequence: LFHAKRGQAFLKLKKPNACIRDCDVALELNSDL | ||||||
Repeat | 195-227 | TPR 3 | ||||
Sequence: AGYKFRGRARRLLGDFELAAHDLRQACKLDFDE | ||||||
Coiled coil | 239-276 | |||||
Sequence: NAKKIEQHRLKQERRQAERKIKERQRDQRRARKEQEKH | ||||||
Compositional bias | 243-277 | Basic and acidic residues | ||||
Sequence: IEQHRLKQERRQAERKIKERQRDQRRARKEQEKHN | ||||||
Region | 243-302 | Disordered | ||||
Sequence: IEQHRLKQERRQAERKIKERQRDQRRARKEQEKHNASSGGSSGEFSGGNPGNGNMSDILG | ||||||
Compositional bias | 278-295 | Polar residues | ||||
Sequence: ASSGGSSGEFSGGNPGNG | ||||||
Domain | 294-336 | STI1 | ||||
Sequence: NGNMSDILGAMSDPEVSAAIQDILSNPGNITKYASNPKIYNLI | ||||||
Region | 344-377 | Disordered | ||||
Sequence: DVGAAFGQAGEKAGKPSEPKPKKDSADFVDDGLD | ||||||
Compositional bias | 358-377 | Basic and acidic residues | ||||
Sequence: KPSEPKPKKDSADFVDDGLD |
Sequence similarities
Belongs to the FAM10 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length377
- Mass (Da)41,037
- Last updated2010-04-20 v2
- ChecksumD62D41198348A786
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E2QD63 | E2QD63_DROME | HIP-R | 377 |
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 83-101 | Acidic residues | ||||
Sequence: EKSLSDPESDVELDMEGVI | ||||||
Compositional bias | 243-277 | Basic and acidic residues | ||||
Sequence: IEQHRLKQERRQAERKIKERQRDQRRARKEQEKHN | ||||||
Compositional bias | 278-295 | Polar residues | ||||
Sequence: ASSGGSSGEFSGGNPGNG | ||||||
Compositional bias | 358-377 | Basic and acidic residues | ||||
Sequence: KPSEPKPKKDSADFVDDGLD |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FJ686088 EMBL· GenBank· DDBJ | ACQ66626.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ686092 EMBL· GenBank· DDBJ | ACQ66627.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ686093 EMBL· GenBank· DDBJ | ACQ66628.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ686094 EMBL· GenBank· DDBJ | ACQ66629.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FJ686095 EMBL· GenBank· DDBJ | ACQ66630.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014298 EMBL· GenBank· DDBJ | AAN09108.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT099906 EMBL· GenBank· DDBJ | ACX32977.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |