Q925B0 · PAWR_MOUSE
- ProteinPRKC apoptosis WT1 regulator protein
- GenePawr
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids333 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended namePRKC apoptosis WT1 regulator protein
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ925B0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000058237 | 1-333 | PRKC apoptosis WT1 regulator protein | |||
Sequence: MATGGYRSGGSTTTDFLEEWKAKREKMRAKQNPAGPGSSGGDPAAKSPAGSLTPTAVAGTSELNHGPAGAAAPAAPAPGALNCAHGSSTLPRAAPGSRRAEDECPSAAAASGAPGSRGDEEEPDSAREKGRSSGPSARKGKGQIEKRKLREKRRSTGVVNIPAAECLDEYEDDEAGQKERKREDAITQQNTIQNEAATLPDPGTSYLPQDPSRTVPGRYKSTTSAPEDEISNRYPRTDRSGFSRHNRDANAPASFSSSSTLEKRIEDLEKEVVRERQENLRLVRLMQDKEEMIGKLKEEIDLLNRDLDDMEDENEQLKQENKTLLKVVGQLTR | ||||||
Modified residue | 156 | Phosphothreonine; by PKA | ||||
Sequence: T | ||||||
Modified residue | 224 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Preferentially phosphorylated at the Thr-156 by PKC in cancer cells.
Keywords
- PTM
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).
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q925B0 | Dapk3 O54784 | 2 | EBI-77397, EBI-77359 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, motif, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Polar residues | ||||
Sequence: MATGGYRSGGSTTTD | ||||||
Region | 1-262 | Disordered | ||||
Sequence: MATGGYRSGGSTTTDFLEEWKAKREKMRAKQNPAGPGSSGGDPAAKSPAGSLTPTAVAGTSELNHGPAGAAAPAAPAPGALNCAHGSSTLPRAAPGSRRAEDECPSAAAASGAPGSRGDEEEPDSAREKGRSSGPSARKGKGQIEKRKLREKRRSTGVVNIPAAECLDEYEDDEAGQKERKREDAITQQNTIQNEAATLPDPGTSYLPQDPSRTVPGRYKSTTSAPEDEISNRYPRTDRSGFSRHNRDANAPASFSSSSTLE | ||||||
Motif | 62-66 | B30.2/SPRY domain-binding motif | ||||
Sequence: ELNHG | ||||||
Compositional bias | 117-155 | Basic and acidic residues | ||||
Sequence: RGDEEEPDSAREKGRSSGPSARKGKGQIEKRKLREKRRS | ||||||
Motif | 138-154 | Nuclear localization signal | ||||
Sequence: RKGKGQIEKRKLREKRR | ||||||
Region | 138-196 | Selective for apoptosis induction in cancer cells (SAC) | ||||
Sequence: RKGKGQIEKRKLREKRRSTGVVNIPAAECLDEYEDDEAGQKERKREDAITQQNTIQNEA | ||||||
Compositional bias | 187-230 | Polar residues | ||||
Sequence: TQQNTIQNEAATLPDPGTSYLPQDPSRTVPGRYKSTTSAPEDEI | ||||||
Compositional bias | 231-245 | Basic and acidic residues | ||||
Sequence: SNRYPRTDRSGFSRH | ||||||
Compositional bias | 247-261 | Polar residues | ||||
Sequence: RDANAPASFSSSSTL | ||||||
Coiled coil | 255-333 | |||||
Sequence: FSSSSTLEKRIEDLEKEVVRERQENLRLVRLMQDKEEMIGKLKEEIDLLNRDLDDMEDENEQLKQENKTLLKVVGQLTR | ||||||
Region | 293-333 | Leucine-zipper | ||||
Sequence: IGKLKEEIDLLNRDLDDMEDENEQLKQENKTLLKVVGQLTR |
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
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.
- Name1
- Length333
- Mass (Da)35,908
- Last updated2006-12-12 v2
- Checksum80CD3DBA586C01F7
Q925B0-2
- Name2
- SynonymsP33
- Differences from canonical
- 166-209: Missing
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Polar residues | ||||
Sequence: MATGGYRSGGSTTTD | ||||||
Compositional bias | 117-155 | Basic and acidic residues | ||||
Sequence: RGDEEEPDSAREKGRSSGPSARKGKGQIEKRKLREKRRS | ||||||
Alternative sequence | VSP_022018 | 166-209 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 187-230 | Polar residues | ||||
Sequence: TQQNTIQNEAATLPDPGTSYLPQDPSRTVPGRYKSTTSAPEDEI | ||||||
Compositional bias | 231-245 | Basic and acidic residues | ||||
Sequence: SNRYPRTDRSGFSRH | ||||||
Compositional bias | 247-261 | Polar residues | ||||
Sequence: RDANAPASFSSSSTL |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |