Q9VS83 · Q9VS83_DROME

Function

function

Involved in DNA damage-induced apoptosis: following DNA damage, accumulates in the nucleus and forms a complex with p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation leading to increase p53/TP53 transcriptional activity. When nuclear, may also act as a component of some chromatin regulator complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2).
Released extracellularly via exosomes, it is a ligand of the natural killer/NK cells receptor NCR3 and stimulates NK cells cytotoxicity. It may thereby trigger NK cells cytotoxicity against neighboring tumor cells and immature myeloid dendritic cells (DC).

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 ComponentBAT3 complex
Cellular Componentcytosol
Cellular Componentextracellular region
Cellular Componentnucleus
Molecular Functionmisfolded protein binding
Molecular Functionpolyubiquitin modification-dependent protein binding
Biological Processapoptotic process
Biological Processcell differentiation
Biological Processchromatin organization
Biological ProcessERAD pathway
Biological Processimmune system process
Biological Processnegative regulation of apoptotic process
Biological Processspermatogenesis

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Large proline-rich protein BAG6
  • Alternative names
    • BCL2-associated athanogene 6
    • HLA-B-associated transcript 3

Gene names

    • Name
      clone 2.45
    • Synonyms
      anon-EST:Liang-2.45
      , Dmel\CG7546
    • ORF names
      CG7546
      , Dmel_CG7546

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
    Q9VS83
  • Secondary accessions
    • Q95TP8

Proteomes

Organism-specific databases

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Keywords

Expression

Gene expression databases

Interaction

Subunit

Component of the BAG6/BAT3 complex, also named BAT3 complex, at least composed of BAG6, UBL4A and GET4/TRC35. Interacts with GET4; the interaction is direct and localizes BAG6 in the cytosol. Interacts with UBL4A; the interaction is direct and required for UBL4A protein stability. Interacts with AIFM1. Interacts with HSPA2. Interacts with CTCFL. Interacts with p300/EP300. Interacts (via ubiquitin-like domain) with RNF126; required for BAG6-dependent ubiquitination of proteins mislocalized to the cytosol. Interacts (via ubiquitin-like domain) with SGTA; SGTA competes with RNF126 by binding the same region of BAG6, thereby promoting deubiquitination of BAG6-target proteins and rescuing them from degradation. Interacts with ricin A chain. Interacts with VCP and AMFR; both form the VCP/p97-AMFR/gp78 complex. Interacts with SYVN1. Interacts with USP13; the interaction is direct and may mediate UBL4A deubiquitination. Interacts with ZFAND2B. Interacts with KPNA2. Interacts with UBQLN4.

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain3-64Ubiquitin-like
Region77-103Disordered
Region241-272Disordered
Region286-344Disordered
Compositional bias315-334Polar residues
Region462-503Disordered
Compositional bias470-503Polar residues
Region633-707Disordered
Compositional bias736-752Polar residues
Region736-757Disordered
Region782-815Disordered
Compositional bias785-815Polar residues

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,166
  • Mass (Da)
    124,341
  • Last updated
    2004-07-05 v3
  • Checksum
    9624A11AAC1512AE
MLINLKVKTLDARIHEFSIDNELTIRQFKDQIAEKTNIAAENQRIIYQGRVLVDDKQVKEYDVDGKVLHVAERPPFSQRGANARNNDEPMRTFRNVARPPPPGMRTSPYFRALDGMLVGTMAIPVNNGPVAGTRPPPNRYPNSSSFCINRITVALHMIDCADNIAAYLENPAVGLNNQSLDILQRGRWSMESTVVEVGVSSTDLPRNNNIIDMVQDAVTAALSHTGARNYTVVQLPTVYTNENGETSQQRTAEAITSEGAASGAASNASGETTAATVIIEDVIETDDEVADGASDRSVTPTPEPEAEGAVGGQQVTAAETPTSSVGSANDAAAEGGNNSGPRRRTRPQVLAQVIQHYRGVQARLAPFVDRYYEILQNDPTFEESDTDGRENAQRIFDRVSEAFHYLSHAQHAISDLMLDLSQPGPRVLTCRPILVEQSGYIRSNNIFTPNFLAPPSGIINEPFRNRAPGSASAAGTQTATTAGTQTPTSAGTPTAVAPSQAANLQAATDASRSAAAMAEIASRAAGAAAEMAAGAASAAAGAANAAAAAARDLSSDQVEDPIDEPMVGPNAAGAETLAQEQQRLEMDPQLEMARIIQAMVNGQRPNDIHVEFNAPNVMSINLPVHVMTTVRQAPAAGSNETADQSASESSSPESAPASGNGESPNAASTSSGTRSGDQRANTLPTTATQTRSTSRPQIQIGGNNNWGGRIAPTHTAFDRFLPCNSHHIREPEQLLQNNSTSRSTSTAPAGGATVVPPTSAAVTRPASVGSAVAAVGDTAASPSGEAAPIASTTPAAPLQTVLPTSTPTPRGDSNNLRSQLRTFLNDSLFVGVPINEQTIPGAIGRALDWFGESLVYLPQYERPEYNSRDSVCNILRVSLRLIIELCNGAPAGVDSAQFEQSLKQICDQFRKRLYSVLFLCLGSANAELYWRQLMRLLCAPMRSNFRNEALQFLCIYIDPTIPAQTDTVDAQQFLVLRSIQAAPPTAADEQQLQEQTLDTDVEMSEVTASGSNSSPADELPAVIVGSEPWHMSFPNDWLPVITRDLQTQAEQSNRPQPPFSDAYISGMSAKRRKIIQSEKPTASVECLIANGVQRAIQSVGLGGSNGGSALNASISMDTVIGSIAHDSTIQAAYTDAVRNSLKERTERDVDFKTSKYPQIAKFTEQK

Computationally mapped potential isoform sequences

There are 7 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
B7Z0D3B7Z0D3_DROMEclone 2.451346
M9PBU3M9PBU3_DROMEclone 2.451179
M9PEE7M9PEE7_DROMEclone 2.451332
Q9VS82Q9VS82_DROMEclone 2.451332
M9ND57M9ND57_DROMEclone 2.451298
M9PHN9M9PHN9_DROMEclone 2.451167
B7Z0D4B7Z0D4_DROMEclone 2.451199

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias315-334Polar residues
Compositional bias470-503Polar residues
Compositional bias736-752Polar residues
Compositional bias785-815Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE014296
EMBL· GenBank· DDBJ
AAF50545.3
EMBL· GenBank· DDBJ
Genomic DNA
BT030991
EMBL· GenBank· DDBJ
ABV82373.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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