C4NYP8 · F10A1_DROME

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 annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentprotein-containing complex
Molecular Functionheat shock protein binding
Molecular FunctionHsp70 protein binding
Molecular Functionprotein dimerization activity
Molecular Functionprotein-folding chaperone binding
Biological Processchaperone cofactor-dependent protein refolding

Names & Taxonomy

Protein names

  • Recommended name
    Hsc70-interacting protein 1

Gene names

    • Name
      HIP
    • ORF names
      CG32789

Organism names

  • Taxonomic identifier
  • Strains
    • XCPA112
    • XCPA126
    • XCPA25
    • XCPA77
    • XCPA93
    • Berkeley
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    C4NYP8
  • Secondary accessions
    • C0L9I4
    • C0L9I8
    • C9QP24
    • Q8IRT4

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variant105in strain: XCPA112
Natural variant227in strain: XCPA25
Natural variant290in strain: XCPA77, XCPA93 and XCPA126

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.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00003935841-377Hsc70-interacting protein 1
Modified residue80Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Homotetramer. Interacts with Hsc70 as well as DNAJ homologs and Hsp90 (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, repeat, coiled coil, domain.

TypeIDPosition(s)Description
Region68-123Disordered
Compositional bias83-101Acidic residues
Repeat126-159TPR 1
Repeat161-193TPR 2
Repeat195-227TPR 3
Coiled coil239-276
Compositional bias243-277Basic and acidic residues
Region243-302Disordered
Compositional bias278-295Polar residues
Domain294-336STI1
Region344-377Disordered
Compositional bias358-377Basic and acidic residues

Sequence similarities

Belongs to the FAM10 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    377
  • Mass (Da)
    41,037
  • Last updated
    2010-04-20 v2
  • Checksum
    D62D41198348A786
MAFTMQTGDLKKLKYFIDFALENPTFLNMPQLQFVKDFVEKFGGTVPPGQFNGGSAGGKCPFGGVAGAKANEPANAPEDSEDEKSLSDPESDVELDMEGVIEADSDPAQPMGNYSKKATEEEVEQASELRAQAASAYGQQKFDEAIALYTKAIELSPGNALFHAKRGQAFLKLKKPNACIRDCDVALELNSDLAAGYKFRGRARRLLGDFELAAHDLRQACKLDFDEETDEWLKEVTPNAKKIEQHRLKQERRQAERKIKERQRDQRRARKEQEKHNASSGGSSGEFSGGNPGNGNMSDILGAMSDPEVSAAIQDILSNPGNITKYASNPKIYNLIKKIVPGGDVGAAFGQAGEKAGKPSEPKPKKDSADFVDDGLD

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
E2QD63E2QD63_DROMEHIP-R377

Sequence caution

The sequence ACX32977.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias83-101Acidic residues
Compositional bias243-277Basic and acidic residues
Compositional bias278-295Polar residues
Compositional bias358-377Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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