Q9WTZ9 · BEX3_MOUSE

  • Protein
    Protein BEX3
  • Gene
    Bex3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

May be a signaling adapter molecule involved in NGFR/p75NTR-mediated apoptosis induced by NGF (PubMed:10764727).
Plays a role in zinc-triggered neuronal death (PubMed:10764727).
In absence of reductive stress, acts as a pseudosubstrate for the CRL2(FEM1B) complex: associates with FEM1B via zinc, thereby preventing association between FEM1B and its substrates (PubMed:34562363).

Features

Showing features for binding site.

1124102030405060708090100110120
TypeIDPosition(s)Description
Binding site121Zn2+ (UniProtKB | ChEBI); ligand shared with FEM1B

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 Componentnucleus
Molecular Functiondeath receptor binding
Molecular Functionidentical protein binding
Molecular Functionmetal ion binding
Molecular Functionmolecular function inhibitor activity
Molecular Functionnerve growth factor receptor binding
Biological Processextrinsic apoptotic signaling pathway via death domain receptors
Biological Processnegative regulation of protein ubiquitination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein BEX3
  • Alternative names
    • Brain-expressed X-linked protein 3 homolog
    • Nerve growth factor receptor-associated protein 1
    • p75NTR-associated cell death executor

Gene names

    • Name
      Bex3
    • Synonyms
      Nade
      , Ngfrap1

Organism names

  • Taxonomic identifier
  • Strains
    • FVB/N
    • BALB/cJ
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9WTZ9
  • Secondary accessions
    • A3KGA0
    • A3KGA1
    • Q9CWN9
    • Q9D0S2
    • Q9D1N5

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Cytoplasm, cytosol
Note: Shuttles between the cytoplasm and the nucleus (PubMed:11830582).
Associates with replicating mitochondria (PubMed:15563833).

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis94Abolishes nuclear export and interactions with itself and p75NTR/NGFR; when associated with A-97 and A-99.
Mutagenesis97Abolishes nuclear export and interactions with itself and p75NTR/NGFR; when associated with A-97 and A-99.
Mutagenesis99Abolishes nuclear export and interactions with itself and p75NTR/NGFR; when associated with A-94 and A-97.
Mutagenesis113-117Abolished zinc-binding and association with FEM1B.
Mutagenesis121Abolishes localization with replicating mitochondria.
Mutagenesis121Abolished zinc-binding and association with FEM1B.

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.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002297811-124Protein BEX3

Post-translational modification

Ubiquitinated (PubMed:10764727).
Degraded by the proteasome (PubMed:10764727).

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Widely expressed.

Gene expression databases

Interaction

Subunit

Self-associates (PubMed:11830582).
Binds to the DEATH domain of p75NTR/NGFR (PubMed:11830582).
Interacts with 14-3-3 epsilon (YWHAE) (PubMed:11278287).
Interacts with DIABLO/SMAC (PubMed:15178455).

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, motif.

Type
IDPosition(s)Description
Region1-56Disordered
Region81-106Interaction with p75NTR/NGFR
Region81-124Interaction with 14-3-3 epsilon
Motif90-100Nuclear export signal
Region113-117His cluster

Domain

The nuclear export signal is required for export from the nucleus and the interactions with itself and NGFR/p75NTR.
The histidine cluster (His cluster) and Cys-121 mediate zinc-binding.

Sequence similarities

Belongs to the BEX family.

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q9WTZ9-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    124
  • Mass (Da)
    14,542
  • Last updated
    1999-11-01 v1
  • Checksum
    3CCCD4F05E66F461
MANVHQENEEMEQPLQNGQEDRPVGGGEGHQPAANNNNNNHNHNHNHHRRGQARRLAPNFRWAIPNRQMNDGLGGDGDDMEMFMEEMREIRRKLRELQLRNCLRILMGELSNHHDHHDEFCLMP

Q9WTZ9-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Sequence caution

The sequence BAB23350.1 differs from that shown. Reason: Erroneous termination Extended C-terminus.

Features

Showing features for alternative sequence, sequence conflict.

Type
IDPosition(s)Description
Alternative sequenceVSP_0177441-10in isoform 2
Sequence conflict17in Ref. 4; BAB26986
Sequence conflict82in Ref. 4; BAB22697

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF097440
EMBL· GenBank· DDBJ
AAD24431.1
EMBL· GenBank· DDBJ
mRNA
AF187066
EMBL· GenBank· DDBJ
AAF75131.1
EMBL· GenBank· DDBJ
mRNA
AK003294
EMBL· GenBank· DDBJ
BAB22697.1
EMBL· GenBank· DDBJ
mRNA
AK004531
EMBL· GenBank· DDBJ
BAB23350.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
AK010500
EMBL· GenBank· DDBJ
BAB26986.1
EMBL· GenBank· DDBJ
mRNA
AL671493
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC027815
EMBL· GenBank· DDBJ
AAH27815.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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