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Q5SXA9 (KIBRA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein KIBRA
Alternative name(s):
Kidney and brain protein
Short name=KIBRA
WW domain-containing protein 1
Gene names
Name:Wwc1
Synonyms:Kiaa0869
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1104 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with NF2 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. Acts as a transcriptional coactivator of ESR1 which plays an essential role in DYNLL1-mediated ESR1 transactivation. Regulates collagen-stimulated activation of the ERK/MAPK cascade. Modulates directional migration of podocytes. Acts as a substrate for PRKCZ and may be associated with memory performance By similarity. Regulates collagen-stimulated activation of the ERK/MAPK cascade. Ref.6

Subunit structure

Homodimer. 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 INADL (via PDZ domain 8). Interacts (via WW domains) with SYNPO (via PPxY motifs). Interacts with NF2 and SNX4 By similarity.

Subcellular location

Cytoplasm. Cytoplasmperinuclear region By similarity. Nucleus By similarity. Cell projectionruffle membrane By similarity. Note: Colocalizes with PRKCZ in the perinuclear region By similarity. Ref.6

Tissue specificity

Mammary epithelium. Ref.6

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. Ref.6

Domain

The C2-domain mediates homodimerization By similarity.

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 By similarity.

Sequence similarities

Belongs to the WWC family. KIBRA subfamily.

Contains 1 C2 domain.

Contains 2 WW domains.

Sequence caution

The sequence AAH06733.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH37006.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11041104Protein KIBRA
PRO_0000242154

Regions

Domain6 – 3934WW 1
Domain53 – 8634WW 2
Domain656 – 784129C2
Region836 – 1104269Interaction with histone H3 By similarity
Region945 – 98844Interaction with PRKCZ By similarity
Coiled coil107 – 19387 Potential
Coiled coil994 – 102431 Potential
Motif1102 – 11043ADDV motif
Compositional bias255 – 29440Ser-rich
Compositional bias421 – 46141Ser-rich
Compositional bias816 – 87358Glu-rich

Amino acid modifications

Modified residue5421Phosphoserine; by CDK1 By similarity
Modified residue8871Phosphoserine Ref.5
Modified residue8911Phosphoserine Ref.5
Modified residue9211Phosphothreonine By similarity
Modified residue9231Phosphoserine; by CDK1 By similarity
Modified residue9391Phosphoserine By similarity
Modified residue9671Phosphoserine; by PKC/PRKCZ By similarity
Modified residue9701Phosphoserine; by PKC/PRKCZ By similarity

Experimental info

Sequence conflict141 – 1455SQVSL → AGLPV in BAD90184. Ref.3
Sequence conflict3481E → K in AAH06733. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q5SXA9 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: D827EFD9AAB19FBA

FASTA1,104124,110
        10         20         30         40         50         60 
MPRPELPLPE GWEEARDFDG KVYYIDHRNR TTSWIDPRDR YTKPLTFADC ISDELPLGWE 

        70         80         90        100        110        120 
EAYDPQVGDY FIDHNTKTTQ IEDPRVQWRR EQEHMLKDYL VVAQEALSAQ KEIYQVKQQR 

       130        140        150        160        170        180 
LELAQQEYQQ LHAVWEHKLG SQVSLVSGSS SSSKYDPEIL KAEIATAKSR VNKLKREMVH 

       190        200        210        220        230        240 
LQHELQFKER GFQTLKKIDE RMSDAQGGYK LDEAQAVLRE TKAIKKAITC GEKEKQDLIK 

       250        260        270        280        290        300 
SLAMLKDGFR TDRGSHSDLW SSSSSLESSS FPMPKQFLDV SSQTDISGSF STSSNNQLAE 

       310        320        330        340        350        360 
KVRLRLRYEE AKRRIANLKI QLAKLDSEAW PGVLDSERDR LILINEKEEL LKEMRFISPR 

       370        380        390        400        410        420 
KWTQGEVEQL EMARRRLEKD LQAARDTQSK ALTERLKLNS KRNQLVRELE EATRQVATLH 

       430        440        450        460        470        480 
SQLKSLSSSM QSLSSGSSPG SLTSSRGSLA ASSLDSSTSA SFTDLYYDPF EQLDSELQSK 

       490        500        510        520        530        540 
VELLFLEGAT GFRPSGCITT IHEDEVAKTQ KAEGGSRLQA LRSLSGTPRS MTSLSPRSSL 

       550        560        570        580        590        600 
SSPSPPCSPL ITDPLLTGDA FLAPLEFEDT ELSTTLCELN LGGSGTQERY RLEEPGPEGK 

       610        620        630        640        650        660 
PLGQAASVAP GCGLKVACVS AAVSDESVAG DSGVYEASAQ RPGTSEAAAF DSDESEAVGA 

       670        680        690        700        710        720 
TRVQIALKYD EKNKQFAILI IQLSHLSALS LQQDQKVNIR VAILPCSESS TCLFRTRPLD 

       730        740        750        760        770        780 
SANTLVFNEA FWVSISYPAL HQKTLRVDVC TTDRSHTEEC LGGAQISLAE VCRSGERSTR 

       790        800        810        820        830        840 
WYNLLSYKYL KKQCREPQPT EAPGPDHVDA VSALLEQTAV ELEKRQEGRS SSQTLEGSWT 

       850        860        870        880        890        900 
YEEEASENEA VAEEEEEGEE DVFTEKVSPE AEECPALKVD RETNTDSVAP SPTVVRPKDR 

       910        920        930        940        950        960 
RVGAPSTGPF LRGNTIIRSK TFSPGPQSQY VCRLNRSDSD SSTLSKKPPF VRNSLERRSV 

       970        980        990       1000       1010       1020 
RMKRPSSVKS LRTERLIRTS LDLELDLQAT RTWHSQLTQE ISVLKELKEH LEQAKNHGEK 

      1030       1040       1050       1060       1070       1080 
ELPQWLREDE RFRLLLRMLE KKVDRGEHKS ELQADKMMRA AAKDVHRLRG QSCKEPPEVQ 

      1090       1100 
SFREKMAFFT RPRMNIPALS ADDV 

« Hide

References

« Hide 'large scale' references
[1]"Protein-coding sequence of KIBRA from Mus musculus."
Kremerskothen J.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 129/SvEv.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Seino S., Nishimura M., Nagase T., Ohara O., Koga H.
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 141-1104.
Tissue: Pancreatic islet.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 146-1104.
Strain: FVB/N.
Tissue: Mammary gland, Mammary tumor and Salivary gland.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-887 AND SER-891, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"KIBRA interacts with discoidin domain receptor 1 to modulate collagen-induced signalling."
Hilton H.N., Stanford P.M., Harris J., Oakes S.R., Kaplan W., Daly R.J., Ormandy C.J.
Biochim. Biophys. Acta 1783:383-393(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ256090 mRNA. Translation: ABB51169.1.
AL596084, AL645912 Genomic DNA. Translation: CAI24387.1.
AL645912, AL596084 Genomic DNA. Translation: CAI35081.1.
AK220259 mRNA. Translation: BAD90184.1.
BC006733 mRNA. Translation: AAH06733.1. Different initiation.
BC017638 mRNA. Translation: AAH17638.1.
BC037006 mRNA. Translation: AAH37006.1. Different initiation.
CCDSCCDS24545.1.
RefSeqNP_740749.1. NM_170779.1.
UniGeneMm.31267.

3D structure databases

ProteinModelPortalQ5SXA9.
SMRQ5SXA9. Positions 7-86, 659-786.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ5SXA9.

Proteomic databases

MaxQBQ5SXA9.
PaxDbQ5SXA9.
PRIDEQ5SXA9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000018993; ENSMUSP00000018993; ENSMUSG00000018849.
GeneID211652.
KEGGmmu:211652.
UCSCuc007ili.1. mouse.

Organism-specific databases

CTD23286.
MGIMGI:2388637. Wwc1.
RougeSearch...

Phylogenomic databases

eggNOGCOG5021.
GeneTreeENSGT00410000025556.
HOGENOMHOG000013211.
HOVERGENHBG058082.
InParanoidQ5SXA9.
KOK16685.
OMADPQVGDY.
OrthoDBEOG7DJSNR.
PhylomeDBQ5SXA9.
TreeFamTF324040.

Gene expression databases

ArrayExpressQ5SXA9.
BgeeQ5SXA9.
CleanExMM_WWC1.
GenevestigatorQ5SXA9.

Family and domain databases

Gene3D2.60.40.150. 1 hit.
InterProIPR000008. C2_dom.
IPR001202. WW_dom.
[Graphical view]
PfamPF00397. WW. 2 hits.
[Graphical view]
SMARTSM00456. WW. 2 hits.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF51045. SSF51045. 2 hits.
PROSITEPS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio373320.
PROQ5SXA9.
SOURCESearch...

Entry information

Entry nameKIBRA_MOUSE
AccessionPrimary (citable) accession number: Q5SXA9
Secondary accession number(s): Q571D0 expand/collapse secondary AC list , Q8K1Y3, Q8VD17, Q922W3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: December 21, 2004
Last modified: July 9, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot