Q5SXA9 · KIBRA_MOUSE

  • Protein
    Protein KIBRA
  • Gene
    Wwc1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

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
Cellular Componentperinuclear region of cytoplasm
Cellular Componentprotein-containing complex
Cellular Componentruffle membrane
Molecular Functionkinase binding
Molecular Functionmolecular adaptor activity
Molecular Functionprotein-macromolecule adaptor activity
Molecular Functiontranscription coactivator activity
Biological Processcell migration
Biological Processnegative regulation of cell population proliferation
Biological Processnegative regulation of hippo signaling
Biological Processnegative regulation of organ growth
Biological Processnegative regulation of transcription by RNA polymerase II
Biological Processpositive regulation of MAPK cascade
Biological Processregulation of DNA-templated transcription
Biological Processregulation of hippo signaling

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein KIBRA
  • Alternative names
    • Kidney and brain protein (KIBRA)
    • WW domain-containing protein 1

Gene names

    • Name
      Wwc1
    • Synonyms
      Kiaa0869

Organism names

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

Accessions

  • Primary accession
    Q5SXA9
  • Secondary accessions
    • Q571D0
    • Q8K1Y3
    • Q8VD17
    • Q922W3

Proteomes

Organism-specific databases

Subcellular Location

Keywords

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.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002421541-1104Protein KIBRA
Modified residue141Phosphoserine
Modified residue535Phosphoserine
Modified residue542Phosphoserine; by CDK1
Modified residue887Phosphoserine
Modified residue891Phosphoserine
Modified residue919Phosphoserine
Modified residue921Phosphothreonine
Modified residue923Phosphoserine; by CDK1
Modified residue939Phosphoserine
Modified residue967Phosphoserine; by PKC/PRKCZ
Modified residue970Phosphoserine; by PKC/PRKCZ

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

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).

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

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

TypeIDPosition(s)Description
Domain6-39WW 1
Domain53-86WW 2
Coiled coil107-193
Region429-449Disordered
Region509-547Disordered
Compositional bias520-546Polar residues
Domain659-782C2
Region822-949Disordered
Region836-1104Interaction with histone H3
Compositional bias842-863Acidic residues
Compositional bias864-880Basic and acidic residues
Compositional bias912-949Polar residues
Region945-988Interaction with PRKCZ
Region948-967Interaction with PRKCZ
Coiled coil994-1024
Motif1102-1104ADDV motif

Domain

The C2-domain mediates homodimerization.

Sequence similarities

Belongs to the WWC family. KIBRA subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,104
  • Mass (Da)
    124,110
  • Last updated
    2004-12-21 v1
  • Checksum
    D827EFD9AAB19FBA
MPRPELPLPEGWEEARDFDGKVYYIDHRNRTTSWIDPRDRYTKPLTFADCISDELPLGWEEAYDPQVGDYFIDHNTKTTQIEDPRVQWRREQEHMLKDYLVVAQEALSAQKEIYQVKQQRLELAQQEYQQLHAVWEHKLGSQVSLVSGSSSSSKYDPEILKAEIATAKSRVNKLKREMVHLQHELQFKERGFQTLKKIDERMSDAQGGYKLDEAQAVLRETKAIKKAITCGEKEKQDLIKSLAMLKDGFRTDRGSHSDLWSSSSSLESSSFPMPKQFLDVSSQTDISGSFSTSSNNQLAEKVRLRLRYEEAKRRIANLKIQLAKLDSEAWPGVLDSERDRLILINEKEELLKEMRFISPRKWTQGEVEQLEMARRRLEKDLQAARDTQSKALTERLKLNSKRNQLVRELEEATRQVATLHSQLKSLSSSMQSLSSGSSPGSLTSSRGSLAASSLDSSTSASFTDLYYDPFEQLDSELQSKVELLFLEGATGFRPSGCITTIHEDEVAKTQKAEGGSRLQALRSLSGTPRSMTSLSPRSSLSSPSPPCSPLITDPLLTGDAFLAPLEFEDTELSTTLCELNLGGSGTQERYRLEEPGPEGKPLGQAASVAPGCGLKVACVSAAVSDESVAGDSGVYEASAQRPGTSEAAAFDSDESEAVGATRVQIALKYDEKNKQFAILIIQLSHLSALSLQQDQKVNIRVAILPCSESSTCLFRTRPLDSANTLVFNEAFWVSISYPALHQKTLRVDVCTTDRSHTEECLGGAQISLAEVCRSGERSTRWYNLLSYKYLKKQCREPQPTEAPGPDHVDAVSALLEQTAVELEKRQEGRSSSQTLEGSWTYEEEASENEAVAEEEEEGEEDVFTEKVSPEAEECPALKVDRETNTDSVAPSPTVVRPKDRRVGAPSTGPFLRGNTIIRSKTFSPGPQSQYVCRLNRSDSDSSTLSKKPPFVRNSLERRSVRMKRPSSVKSLRTERLIRTSLDLELDLQATRTWHSQLTQEISVLKELKEHLEQAKNHGEKELPQWLREDERFRLLLRMLEKKVDRGEHKSELQADKMMRAAAKDVHRLRGQSCKEPPEVQSFREKMAFFTRPRMNIPALSADDV

Sequence caution

The sequence AAH06733.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence AAH37006.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict141-145in Ref. 3; BAD90184
Sequence conflict348in Ref. 4; AAH06733
Compositional bias520-546Polar residues
Compositional bias842-863Acidic residues
Compositional bias864-880Basic and acidic residues
Compositional bias912-949Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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