Q5SXA9 · KIBRA_MOUSE
- ProteinProtein KIBRA
- GeneWwc1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1104 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Regulator of the Hippo signaling pathway, also known as the Salvador-Warts-Hippo (SWH) pathway. Enhances phosphorylation of LATS1 and YAP1 and negatively regulates cell proliferation and organ growth due to a suppression of the transcriptional activity of YAP1, the major effector of the Hippo pathway. Along with NF2 can synergistically induce the phosphorylation of LATS1 and LATS2 and function in the regulation of Hippo signaling pathway. Acts as a transcriptional coactivator of ESR1 which plays an essential role in DYNLL1-mediated ESR1 transactivation. Modulates directional migration of podocytes. May be associated with memory performance (By similarity).
Regulates collagen-stimulated activation of the ERK/MAPK cascade (PubMed:18190796).
Plays an important role in regulating AMPA-selective glutamate receptors (AMPARs) trafficking (PubMed:21943600, PubMed:31730661).
Regulates collagen-stimulated activation of the ERK/MAPK cascade (PubMed:18190796).
Plays an important role in regulating AMPA-selective glutamate receptors (AMPARs) trafficking (PubMed:21943600, PubMed:31730661).
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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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | protein-containing complex | |
Cellular Component | ruffle membrane | |
Molecular Function | kinase binding | |
Molecular Function | molecular adaptor activity | |
Molecular Function | protein-macromolecule adaptor activity | |
Molecular Function | transcription coactivator activity | |
Biological Process | cell migration | |
Biological Process | negative regulation of cell population proliferation | |
Biological Process | negative regulation of hippo signaling | |
Biological Process | negative regulation of organ growth | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | positive regulation of MAPK cascade | |
Biological Process | regulation of DNA-templated transcription | |
Biological Process | regulation of hippo signaling |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein KIBRA
- 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 accessionQ5SXA9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with PRKCZ in the perinuclear region.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Deficient mice have significant deficits in hippocampal long-term potentiation (LTP) and long-term depression (LTD)vcand have profound learning and memory defects.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 52 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000242154 | 1-1104 | Protein KIBRA | |||
Sequence: MPRPELPLPEGWEEARDFDGKVYYIDHRNRTTSWIDPRDRYTKPLTFADCISDELPLGWEEAYDPQVGDYFIDHNTKTTQIEDPRVQWRREQEHMLKDYLVVAQEALSAQKEIYQVKQQRLELAQQEYQQLHAVWEHKLGSQVSLVSGSSSSSKYDPEILKAEIATAKSRVNKLKREMVHLQHELQFKERGFQTLKKIDERMSDAQGGYKLDEAQAVLRETKAIKKAITCGEKEKQDLIKSLAMLKDGFRTDRGSHSDLWSSSSSLESSSFPMPKQFLDVSSQTDISGSFSTSSNNQLAEKVRLRLRYEEAKRRIANLKIQLAKLDSEAWPGVLDSERDRLILINEKEELLKEMRFISPRKWTQGEVEQLEMARRRLEKDLQAARDTQSKALTERLKLNSKRNQLVRELEEATRQVATLHSQLKSLSSSMQSLSSGSSPGSLTSSRGSLAASSLDSSTSASFTDLYYDPFEQLDSELQSKVELLFLEGATGFRPSGCITTIHEDEVAKTQKAEGGSRLQALRSLSGTPRSMTSLSPRSSLSSPSPPCSPLITDPLLTGDAFLAPLEFEDTELSTTLCELNLGGSGTQERYRLEEPGPEGKPLGQAASVAPGCGLKVACVSAAVSDESVAGDSGVYEASAQRPGTSEAAAFDSDESEAVGATRVQIALKYDEKNKQFAILIIQLSHLSALSLQQDQKVNIRVAILPCSESSTCLFRTRPLDSANTLVFNEAFWVSISYPALHQKTLRVDVCTTDRSHTEECLGGAQISLAEVCRSGERSTRWYNLLSYKYLKKQCREPQPTEAPGPDHVDAVSALLEQTAVELEKRQEGRSSSQTLEGSWTYEEEASENEAVAEEEEEGEEDVFTEKVSPEAEECPALKVDRETNTDSVAPSPTVVRPKDRRVGAPSTGPFLRGNTIIRSKTFSPGPQSQYVCRLNRSDSDSSTLSKKPPFVRNSLERRSVRMKRPSSVKSLRTERLIRTSLDLELDLQATRTWHSQLTQEISVLKELKEHLEQAKNHGEKELPQWLREDERFRLLLRMLEKKVDRGEHKSELQADKMMRAAAKDVHRLRGQSCKEPPEVQSFREKMAFFTRPRMNIPALSADDV | ||||||
Modified residue | 141 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 535 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 542 | Phosphoserine; by CDK1 | ||||
Sequence: S | ||||||
Modified residue | 887 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 891 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 919 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 921 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 923 | Phosphoserine; by CDK1 | ||||
Sequence: S | ||||||
Modified residue | 939 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 967 | Phosphoserine; by PKC/PRKCZ | ||||
Sequence: S | ||||||
Modified residue | 970 | Phosphoserine; by PKC/PRKCZ | ||||
Sequence: S |
Post-translational modification
Phosphorylation at Ser-542 and Ser-923 by CDK1 in response to spindle damage stress regulates mitotic exit, these two sites are dephosphorylated by CDC14B.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Mammary epithelium.
Developmental stage
Expressed in mammary tissue throughout development (at protein level). Strongly up-regulated during pregnancy, falls during lactation and is again up-regulated during involution of the gland at weaning.
Gene expression databases
Interaction
Subunit
Homodimer. Forms heterodimers with WWC2 and WWC3. Interacts with DDN. Interacts with DYNLL1 and histone H3. The interaction with DYNLL1 is mandatory for the recruitment and transactivation functions of ESR1 or DYNLL1 to the target chromatin and the interaction with histone H3 ensures proper regulatory interaction of WWC1-DYNLL1-ESR1 complexes with target chromatin. Interacts (via WW domains) with DDR1 (via PPxY motif) in a collagen-regulated manner. Interacts with PRKCZ (via the protein kinase domain). Forms a tripartite complex with DDR1 and PRKCZ, but predominantly in the absence of collagen. Interacts (via the ADDV motif) with PATJ (via PDZ domain 8). Interacts (via WW domains) with SYNPO (via PPxY motifs). Interacts with NF2 and SNX4 (By similarity).
Interacts with CCDC141; retains AMPAR in the cytosol after internalization (PubMed:31730661).
Interacts with DLC1 and PRKCZ (By similarity).
Interacts (via WW domains) with LATS1 and LATS2 (By similarity).
Interacts with CCDC141; retains AMPAR in the cytosol after internalization (PubMed:31730661).
Interacts with DLC1 and PRKCZ (By similarity).
Interacts (via WW domains) with LATS1 and LATS2 (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, coiled coil, region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 6-39 | WW 1 | ||||
Sequence: LPLPEGWEEARDFDGKVYYIDHRNRTTSWIDPRD | ||||||
Domain | 53-86 | WW 2 | ||||
Sequence: DELPLGWEEAYDPQVGDYFIDHNTKTTQIEDPRV | ||||||
Coiled coil | 107-193 | |||||
Sequence: LSAQKEIYQVKQQRLELAQQEYQQLHAVWEHKLGSQVSLVSGSSSSSKYDPEILKAEIATAKSRVNKLKREMVHLQHELQFKERGFQ | ||||||
Region | 429-449 | Disordered | ||||
Sequence: SMQSLSSGSSPGSLTSSRGSL | ||||||
Region | 509-547 | Disordered | ||||
Sequence: TQKAEGGSRLQALRSLSGTPRSMTSLSPRSSLSSPSPPC | ||||||
Compositional bias | 520-546 | Polar residues | ||||
Sequence: ALRSLSGTPRSMTSLSPRSSLSSPSPP | ||||||
Domain | 659-782 | C2 | ||||
Sequence: GATRVQIALKYDEKNKQFAILIIQLSHLSALSLQQDQKVNIRVAILPCSESSTCLFRTRPLDSANTLVFNEAFWVSISYPALHQKTLRVDVCTTDRSHTEECLGGAQISLAEVCRSGERSTRWY | ||||||
Region | 822-949 | Disordered | ||||
Sequence: LEKRQEGRSSSQTLEGSWTYEEEASENEAVAEEEEEGEEDVFTEKVSPEAEECPALKVDRETNTDSVAPSPTVVRPKDRRVGAPSTGPFLRGNTIIRSKTFSPGPQSQYVCRLNRSDSDSSTLSKKPP | ||||||
Region | 836-1104 | Interaction with histone H3 | ||||
Sequence: EGSWTYEEEASENEAVAEEEEEGEEDVFTEKVSPEAEECPALKVDRETNTDSVAPSPTVVRPKDRRVGAPSTGPFLRGNTIIRSKTFSPGPQSQYVCRLNRSDSDSSTLSKKPPFVRNSLERRSVRMKRPSSVKSLRTERLIRTSLDLELDLQATRTWHSQLTQEISVLKELKEHLEQAKNHGEKELPQWLREDERFRLLLRMLEKKVDRGEHKSELQADKMMRAAAKDVHRLRGQSCKEPPEVQSFREKMAFFTRPRMNIPALSADDV | ||||||
Compositional bias | 842-863 | Acidic residues | ||||
Sequence: EEEASENEAVAEEEEEGEEDVF | ||||||
Compositional bias | 864-880 | Basic and acidic residues | ||||
Sequence: TEKVSPEAEECPALKVD | ||||||
Compositional bias | 912-949 | Polar residues | ||||
Sequence: RGNTIIRSKTFSPGPQSQYVCRLNRSDSDSSTLSKKPP | ||||||
Region | 945-988 | Interaction with PRKCZ | ||||
Sequence: SKKPPFVRNSLERRSVRMKRPSSVKSLRTERLIRTSLDLELDLQ | ||||||
Region | 948-967 | Interaction with PRKCZ | ||||
Sequence: PPFVRNSLERRSVRMKRPSS | ||||||
Coiled coil | 994-1024 | |||||
Sequence: HSQLTQEISVLKELKEHLEQAKNHGEKELPQ | ||||||
Motif | 1102-1104 | ADDV motif | ||||
Sequence: DDV |
Domain
The C2-domain mediates homodimerization.
Sequence similarities
Belongs to the WWC family. KIBRA subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,104
- Mass (Da)124,110
- Last updated2004-12-21 v1
- ChecksumD827EFD9AAB19FBA
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 141-145 | in Ref. 3; BAD90184 | ||||
Sequence: SQVSL → AGLPV | ||||||
Sequence conflict | 348 | in Ref. 4; AAH06733 | ||||
Sequence: E → K | ||||||
Compositional bias | 520-546 | Polar residues | ||||
Sequence: ALRSLSGTPRSMTSLSPRSSLSSPSPP | ||||||
Compositional bias | 842-863 | Acidic residues | ||||
Sequence: EEEASENEAVAEEEEEGEEDVF | ||||||
Compositional bias | 864-880 | Basic and acidic residues | ||||
Sequence: TEKVSPEAEECPALKVD | ||||||
Compositional bias | 912-949 | Polar residues | ||||
Sequence: RGNTIIRSKTFSPGPQSQYVCRLNRSDSDSSTLSKKPP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DQ256090 EMBL· GenBank· DDBJ | ABB51169.1 EMBL· GenBank· DDBJ | mRNA | ||
AL596084 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL645912 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AK220259 EMBL· GenBank· DDBJ | BAD90184.1 EMBL· GenBank· DDBJ | mRNA | ||
BC006733 EMBL· GenBank· DDBJ | AAH06733.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC017638 EMBL· GenBank· DDBJ | AAH17638.1 EMBL· GenBank· DDBJ | mRNA | ||
BC037006 EMBL· GenBank· DDBJ | AAH37006.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |