Q925B0 · PAWR_MOUSE

  • Protein
    PRKC apoptosis WT1 regulator protein
  • Gene
    Pawr
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Pro-apoptotic protein capable of selectively inducing apoptosis in cancer cells, sensitizing the cells to diverse apoptotic stimuli and causing regression of tumors in animal models. Induces apoptosis in certain cancer cells by activation of the Fas prodeath pathway and coparallel inhibition of NF-kappa-B transcriptional activity. Inhibits the transcriptional activation and augments the transcriptional repression mediated by WT1. Down-regulates the anti-apoptotic protein BCL2 via its interaction with WT1. Seems also to be a transcriptional repressor by itself. May be directly involved in regulating the amyloid precursor protein (APP) cleavage activity of BACE1 (By similarity).

Miscellaneous

The synapses are crucial cellular sites for the cell death promoting actions of PAWR in motor neurons. Targeted inhibition of PAWR by RNAi is neuroprotective.

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 Componentactin cytoskeleton
Cellular Componentaxon
Cellular Componentchromatin
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentneuronal cell body
Cellular Componentnucleus
Cellular Componentplasma membrane
Molecular Functionactin binding
Molecular Functionleucine zipper domain binding
Molecular Functionprotein kinase C binding
Molecular Functionprotein phosphatase 1 binding
Biological Processactin filament bundle assembly
Biological Processapoptotic process
Biological Processapoptotic signaling pathway
Biological Processcalcium ion import across plasma membrane
Biological Processdetection of mechanical stimulus involved in sensory perception of pain
Biological Processdetection of temperature stimulus involved in sensory perception of pain
Biological Processnegative regulation of B cell proliferation
Biological Processnegative regulation of calcium ion import
Biological Processnegative regulation of epithelial to mesenchymal transition
Biological Processnegative regulation of fibroblast proliferation
Biological Processnegative regulation of gene expression
Biological Processnegative regulation of T cell proliferation
Biological Processnegative regulation of T cell receptor signaling pathway
Biological Processnegative regulation of transcription by RNA polymerase II
Biological Processpositive regulation of action potential
Biological Processpositive regulation of amyloid precursor protein biosynthetic process
Biological Processpositive regulation of apoptotic process
Biological Processpositive regulation of cellular senescence
Biological Processpositive regulation of gene expression
Biological Processpositive regulation of hindgut contraction
Biological Processpositive regulation of hydrogen peroxide-mediated programmed cell death
Biological Processpositive regulation of leukocyte tethering or rolling
Biological Processpositive regulation of neuron apoptotic process
Biological Processpositive regulation of neuronal action potential
Biological Processpositive regulation of neutrophil extravasation
Biological Processpositive regulation of relaxation of smooth muscle

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    PRKC apoptosis WT1 regulator protein
  • Alternative names
    • Prostate apoptosis response 4 protein (Par-4)

Gene names

    • Name
      Pawr
    • Synonyms
      Par4

Organism names

  • Taxonomic identifier
  • Strains
    • 129S4/SvJae
    • C57BL/6J
    • Swiss Webster / NIH
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q925B0
  • Secondary accessions
    • Q0ZHI4
    • Q2HYJ1

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Nucleus
Note: Mainly cytoplasmic in absence of apoptosis signal and in normal cells. Nuclear in most cancer cell lines. Nuclear entry seems to be essential but not sufficient for apoptosis. Nuclear localization includes nucleoplasm and PML nuclear bodies (By similarity).

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000582371-333PRKC apoptosis WT1 regulator protein
Modified residue156Phosphothreonine; by PKA
Modified residue224Phosphoserine

Post-translational modification

Preferentially phosphorylated at the Thr-156 by PKC in cancer cells.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Homooligomer. Interacts (via the C-terminal region) with WT1. Interacts with THAP1. Interacts with AATF. Interacts with BACE1. Interacts with SPSB1 (via B30.2/SPRY domain); this interaction is direct and occurs in association with the Elongin BC complex (PubMed:16369487, PubMed:20561531).
Interacts with SPSB2 (via B30.2/SPRY domain); this interaction occurs in association with the Elongin BC complex (PubMed:16369487, PubMed:20561531).
Interacts with SPSB4 (via B30.2/SPRY domain); this interaction occurs in association with the Elongin BC complex (PubMed:16369487, PubMed:20561531).
Component of a ternary complex composed of SQSTM1 and PRKCZ (By similarity).
Interacts with actin (By similarity).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q925B0Dapk3 O547842EBI-77397, EBI-77359

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for compositional bias, region, motif, coiled coil.

TypeIDPosition(s)Description
Compositional bias1-15Polar residues
Region1-262Disordered
Motif62-66B30.2/SPRY domain-binding motif
Compositional bias117-155Basic and acidic residues
Motif138-154Nuclear localization signal
Region138-196Selective for apoptosis induction in cancer cells (SAC)
Compositional bias187-230Polar residues
Compositional bias231-245Basic and acidic residues
Compositional bias247-261Polar residues
Coiled coil255-333
Region293-333Leucine-zipper

Domain

The leucine-zipper domain is not essential for apoptosis, but is required for sensitization of cells to exogenous apoptotic insults and for interaction with its partners.
The SAC domain is a death-inducing domain selective for apoptosis induction in cancer cells. This domain is essential for nuclear entry, Fas activation, inhibition of NF-kappa-B activity and induction of apoptosis in cancer cells (By similarity).
The B30.2/SPRY domain-binding motif mediates recognition by proteins containing a B30.2/SPRY domain.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q925B0-1

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
    333
  • Mass (Da)
    35,908
  • Last updated
    2006-12-12 v2
  • Checksum
    80CD3DBA586C01F7
MATGGYRSGGSTTTDFLEEWKAKREKMRAKQNPAGPGSSGGDPAAKSPAGSLTPTAVAGTSELNHGPAGAAAPAAPAPGALNCAHGSSTLPRAAPGSRRAEDECPSAAAASGAPGSRGDEEEPDSAREKGRSSGPSARKGKGQIEKRKLREKRRSTGVVNIPAAECLDEYEDDEAGQKERKREDAITQQNTIQNEAATLPDPGTSYLPQDPSRTVPGRYKSTTSAPEDEISNRYPRTDRSGFSRHNRDANAPASFSSSSTLEKRIEDLEKEVVRERQENLRLVRLMQDKEEMIGKLKEEIDLLNRDLDDMEDENEQLKQENKTLLKVVGQLTR

Q925B0-2

  • Name
    2
  • Synonyms
    P33
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Features

Showing features for compositional bias, alternative sequence.

TypeIDPosition(s)Description
Compositional bias1-15Polar residues
Compositional bias117-155Basic and acidic residues
Alternative sequenceVSP_022018166-209in isoform 2
Compositional bias187-230Polar residues
Compositional bias231-245Basic and acidic residues
Compositional bias247-261Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQ449073
EMBL· GenBank· DDBJ
ABE27591.1
EMBL· GenBank· DDBJ
mRNA
DQ449074
EMBL· GenBank· DDBJ
ABE27592.1
EMBL· GenBank· DDBJ
mRNA
DQ363525
EMBL· GenBank· DDBJ
ABC96645.1
EMBL· GenBank· DDBJ
mRNA
AF377871
EMBL· GenBank· DDBJ
AAK55414.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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