O46067 · O46067_DROME

Function

function

Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. May play a role as a molecular chaperone and participate in protein folding.

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 Componentendomembrane system
Cellular Componentendoplasmic reticulum chaperone complex
Cellular Componentendoplasmic reticulum lumen
Cellular Componentextracellular space
Molecular Functionadenyl-nucleotide exchange factor activity
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent protein folding chaperone
Molecular Functionunfolded protein binding
Biological Processcellular response to hypoxia

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Hypoxia up-regulated protein 1

Gene names

    • Name
      Grp170
    • Synonyms
      CT9894
      , Dmel\CG2918
      , EG:25E8.1
      , GRP170
    • ORF names
      CG2918
      , Dmel_CG2918

Organism names

  • Taxonomic identifier
  • Strain
    • Berkeley
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    O46067

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-19
ChainPRO_501509677620-923Hypoxia up-regulated protein 1

Proteomic databases

Expression

Gene expression databases

    • FBgn0023529Expressed in spermatid in male reproductive gland and 257 other cell types or tissues

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region572-623Disordered
Compositional bias859-902Basic and acidic residues
Region859-923Disordered

Sequence similarities

Belongs to the heat shock protein 70 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    923
  • Mass (Da)
    103,445
  • Last updated
    1998-06-01 v1
  • Checksum
    28196A51FE21BBC8
MKLVLLLSALLAGIALSQGAAVMSVDLGSEWMKVGVVSPGVPMEIALNRESKRKTPAILAFRDGTRTIGEDAQTIGIKDPNSAYGYLLDLLGKTIDNPIVDLYRKRFPYYNIVGDPERNTVVFRKSDTDEFSVEELVAQLLVKAKQFAQESVQQPITECVLTVPGYFGQAEREALLSAAQLANLKVLQLINDYAAVALNYGVFHRGEINETAQYFLFYDMGAYKTSAAVVSYQLVKDKQTREINPVVQVLGVGYDRTLGGLEIQLRLRDYLAQEFNALKKTKTDVTTSPRALAKLFKEAGRLKNVLSANTEFFAQIENLIEDIDFKLPVTREKLEQLCEDLWPRATKPLEEALASSHLSLDVINQVILFGGGTRVPRVQETIKAVIKQELGKNLNADESATMGAVYKAADLSAGFKVKKFVVKDATLFPLQVSFERDPGDGAAVKQVKRALFALMNPYPQKKVITFNKHTDDFEFYVNYADLDRYSKEEIAALGSLNVTKVQLKQVKELLEKSKKELVDNKGIKAYFYLDDSGIFRCTGVEYVYEKQKPEDDADEDSTLSKFGSTLSKLFTKEGEEKKDNSEQEEAANAGEEPSKSEDNEKAKEEDASKEQKSEESTKQDTEAKNETIKLVTVKSPVTYESQTQFVVPLVGSAYDQSVAKLAAINKAEEQRVRLESAFNALEAHIIEVQQKLDEESYAKCATAEEKEKLLAECSTLGEWLYEDLEDPKAEIYEEKLAQLKKLSNVFLARHWEHEERPEAIKALKGMIDGAEKFLVTGRNLTKDTNPEKDVFTQVEIDTLDKVITETNAWLKTETAAQKKLAKNADIRLTVKDITDKMSLLDREVKYLVNKIKIWKPKVKPAAEKEKKKEEEVVASGSGDDTKSEDAEQQQEQATKEEQQEQEPVDEITPTPAEEETKTPHSEL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias859-902Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE014298
EMBL· GenBank· DDBJ
AAF45769.1
EMBL· GenBank· DDBJ
Genomic DNA
AY094705
EMBL· GenBank· DDBJ
AAM11058.1
EMBL· GenBank· DDBJ
mRNA
AE014298
EMBL· GenBank· DDBJ
ACZ95182.1
EMBL· GenBank· DDBJ
Genomic DNA
AL009196
EMBL· GenBank· DDBJ
CAA15711.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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