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Protein KIBRA (HBeAg-binding protein 3) (Kidney and brain protein) (KIBRA) (WW domain-containing protein 1)

 KIBRA_HUMAN             Reviewed;        1113 AA.
Q8IX03; B4DK05; O94946; Q6MZX4; Q6Y2F8; Q7Z4G8; Q8WVM4; Q9BT29;
27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
25-OCT-2017, entry version 122.
RecName: Full=Protein KIBRA;
AltName: Full=HBeAg-binding protein 3;
AltName: Full=Kidney and brain protein;
Short=KIBRA;
AltName: Full=WW domain-containing protein 1;
Name=WWC1; Synonyms=KIAA0869;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DDN,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=12559952; DOI=10.1016/S0006-291X(02)02945-5;
Kremerskothen J., Plaas C., Buether K., Finger I., Veltel S.,
Matanis T., Liedtke T., Barnekow A.;
"Characterization of KIBRA, a novel WW domain-containing protein.";
Biochem. Biophys. Res. Commun. 300:862-867(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-1113 (ISOFORM 2).
TISSUE=Fetal brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 225-1113 (ISOFORM 2).
TISSUE=Brain;
PubMed=10048485; DOI=10.1093/dnares/5.6.355;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 5:355-364(1998).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 202-1113 (ISOFORM 1).
TISSUE=Liver;
Lu Y., Liu Y., Cheng J.;
"Screening and cloning of interaction protein 3 of HBeAg.";
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 782-1113 (ISOFORM 1).
TISSUE=Liver, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, SUBUNIT, INTERACTION WITH PRKCZ, AND PHOSPHORYLATION AT
SER-975 AND SER-978.
PubMed=15081397; DOI=10.1016/j.bbrc.2004.03.107;
Buether K., Plaas C., Barnekow A., Kremerskothen J.;
"KIBRA is a novel substrate for protein kinase Czeta.";
Biochem. Biophys. Res. Commun. 317:703-707(2004).
[9]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH
DYNLL1 AND HISTONE H3.
PubMed=16684779; DOI=10.1074/jbc.M600021200;
Rayala S.K., den Hollander P., Manavathi B., Talukder A.H., Song C.,
Peng S., Barnekow A., Kremerskothen J., Kumar R.;
"Essential role of KIBRA in co-activator function of dynein light
chain 1 in mammalian cells.";
J. Biol. Chem. 281:19092-19099(2006).
[10]
POLYMORPHISM, AND INVOLVEMENT IN MEMRYQTL.
PubMed=17053149; DOI=10.1126/science.1129837;
Papassotiropoulos A., Stephan D.A., Huentelman M.J., Hoerndli F.J.,
Craig D.W., Pearson J.V., Huynh K.D., Brunner F., Corneveaux J.,
Osborne D., Wollmer M.A., Aerni A., Coluccia D., Hanggi J.,
Mondadori C.R., Buchmann A., Reiman E.M., Caselli R.J., Henke K.,
de Quervain D.J.;
"Common Kibra alleles are associated with human memory performance.";
Science 314:475-478(2006).
[11]
INTERACTION WITH SNX4.
PubMed=17994011; DOI=10.1038/ncb1656;
Traer C.J., Rutherford A.C., Palmer K.J., Wassmer T., Oakley J.,
Attar N., Carlton J.G., Kremerskothen J., Stephens D.J., Cullen P.J.;
"SNX4 coordinates endosomal sorting of TfnR with dynein-mediated
transport into the endocytic recycling compartment.";
Nat. Cell Biol. 9:1370-1380(2007).
[12]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SYNPO AND PATJ, AND
TISSUE SPECIFICITY.
PubMed=18596123; DOI=10.1681/ASN.2007080916;
Duning K., Schurek E.M., Schlueter M., Bayer M., Reinhardt H.C.,
Schwab A., Schaefer L., Benzing T., Schermer B., Saleem M.A.,
Huber T.B., Bachmann S., Kremerskothen J., Weide T., Pavenstaedt H.;
"KIBRA modulates directional migration of podocytes.";
J. Am. Soc. Nephrol. 19:1891-1903(2008).
[13]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INDUCTION,
INTERACTION WITH DDR1 AND PRKCZ, AND TISSUE SPECIFICITY.
PubMed=18190796; DOI=10.1016/j.bbamcr.2007.12.007;
Hilton H.N., Stanford P.M., Harris J., Oakes S.R., Kaplan W.,
Daly R.J., Ormandy C.J.;
"KIBRA interacts with discoidin domain receptor 1 to modulate
collagen-induced signalling.";
Biochim. Biophys. Acta 1783:383-393(2008).
[14]
FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND DOMAIN C2.
PubMed=18672031; DOI=10.1016/j.neuroscience.2008.06.054;
Johannsen S., Duning K., Pavenstaedt H., Kremerskothen J.,
Boeckers T.M.;
"Temporal-spatial expression and novel biochemical properties of the
memory-related protein KIBRA.";
Neuroscience 155:1165-1173(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-912; THR-929 AND
SER-931, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
FUNCTION.
PubMed=20159598; DOI=10.1016/j.devcel.2009.12.012;
Yu J., Zheng Y., Dong J., Klusza S., Deng W.-M., Pan D.;
"Kibra functions as a tumor suppressor protein that regulates Hippo
signaling in conjunction with Merlin and Expanded.";
Dev. Cell 18:288-299(2010).
[17]
INTERACTION WITH NF2.
PubMed=20159599; DOI=10.1016/j.devcel.2009.12.011;
Genevet A., Wehr M.C., Brain R., Thompson B.J., Tapon N.;
"Kibra Is a regulator of the Salvador/Warts/Hippo signaling network.";
Dev. Cell 18:300-308(2010).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-947, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
POLYMORPHISM, AND INVOLVEMENT IN MEMRYQTL.
PubMed=23065961; DOI=10.1002/ajmg.b.32101;
Milnik A., Heck A., Vogler C., Heinze H.J., de Quervain D.J.,
Papassotiropoulos A.;
"Association of KIBRA with episodic and working memory: a meta-
analysis.";
Am. J. Med. Genet. B Neuropsychiatr. Genet. 159B:958-969(2012).
[20]
PHOSPHORYLATION AT SER-542 AND SER-931 BY CDK1, AND DEPHOSPHORYLATION
BY CDC14B.
PubMed=22784093; DOI=10.1042/BJ20120751;
Ji M., Yang S., Chen Y., Xiao L., Zhang L., Dong J.;
"Phospho-regulation of KIBRA by CDK1 and CDC14 phosphatase controls
cell-cycle progression.";
Biochem. J. 447:93-102(2012).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535 AND THR-929, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
FUNCTION OF C2 DOMAIN, VARIANTS ILE-734 AND ALA-735, AND
CHARACTERIZATION OF VARIANTS ILE-734 AND ALA-735.
PubMed=23778582; DOI=10.1038/tp.2013.49;
Duning K., Wennmann D.O., Bokemeyer A., Reissner C., Wersching H.,
Thomas C., Buschert J., Guske K., Franzke V., Floel A., Lohmann H.,
Knecht S., Brand S.M., Poter M., Rescher U., Missler M., Seelheim P.,
Propper C., Boeckers T.M., Makuch L., Huganir R., Weide T., Brand E.,
Pavenstadt H., Kremerskothen J.;
"Common exonic missense variants in the C2 domain of the human KIBRA
protein modify lipid binding and cognitive performance.";
Transl. Psychiatry 3:E272-E272(2013).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-899, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[24]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 638-785.
RIKEN structural genomics initiative (RSGI);
"Crystal structure of C2 domain of KIBRA protein.";
Submitted (FEB-2009) to the PDB data bank.
-!- 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.
Plays a role in cognition and memory performance.
{ECO:0000269|PubMed:15081397, ECO:0000269|PubMed:16684779,
ECO:0000269|PubMed:18190796, ECO:0000269|PubMed:18596123,
ECO:0000269|PubMed:18672031, ECO:0000269|PubMed:20159598,
ECO:0000269|PubMed:23778582}.
-!- SUBUNIT: 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 PATJ (via PDZ domain 8). Interacts (via
WW domains) with SYNPO (via PPxY motifs). Interacts with NF2 and
SNX4. {ECO:0000269|PubMed:12559952, ECO:0000269|PubMed:15081397,
ECO:0000269|PubMed:16684779, ECO:0000269|PubMed:17994011,
ECO:0000269|PubMed:18190796, ECO:0000269|PubMed:18596123,
ECO:0000269|PubMed:18672031, ECO:0000269|PubMed:20159599}.
-!- INTERACTION:
Q62824:Exoc4 (xeno); NbExp=3; IntAct=EBI-15812469, EBI-6959516;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
Nucleus. Cell projection, ruffle membrane. Note=Colocalizes with
PRKCZ in the perinuclear region.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8IX03-1; Sequence=Displayed;
Name=2;
IsoId=Q8IX03-2; Sequence=VSP_019448;
-!- TISSUE SPECIFICITY: Expressed in mammary epithelial cells and
breast cancer cell lines. Found in the luminal epithelium
surrounding the ducts in the normal breast. In the brain,
expressed in somatodendritic compartment of neurons in the cortex
and hippocampus and in the cerebellum it is found in the Purkinje
cells and some granule cells (at protein level). Detected in
brain, heart, colon and kidney. In the kidney, expressed in
glomerular podocytes, in some tubules and in the collecting duct.
{ECO:0000269|PubMed:12559952, ECO:0000269|PubMed:18190796,
ECO:0000269|PubMed:18596123, ECO:0000269|PubMed:18672031}.
-!- INDUCTION: Strongly up-regulated by progestin treatment.
{ECO:0000269|PubMed:18190796}.
-!- DOMAIN: The C2-domain mediates homodimerization. It is a calcium-
sensitive lipid-binding domain with preference for PI(3)P.
{ECO:0000269|PubMed:18672031}.
-!- PTM: Phosphorylation at Ser-542 and Ser-931 by CDK1 in response to
spindle damage stress regulates mitotic exit, these two sites are
dephosphorylated by CDC14B. {ECO:0000269|PubMed:15081397,
ECO:0000269|PubMed:16684779, ECO:0000269|PubMed:18190796,
ECO:0000269|PubMed:22784093}.
-!- POLYMORPHISM: Genetic variations in WWC1 define the memory
quantitative trait locus (MEMRYQTL) [MIM:615602].
{ECO:0000269|PubMed:17053149, ECO:0000269|PubMed:23065961}.
-!- SIMILARITY: Belongs to the WWC family. KIBRA subfamily.
{ECO:0000305}.
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EMBL; AF506799; AAO15881.1; -; mRNA.
EMBL; AK296323; BAG59017.1; -; mRNA.
EMBL; AC020894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC026689; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX640827; CAE45903.1; -; mRNA.
EMBL; AB020676; BAA74892.1; -; mRNA.
EMBL; AF530058; AAQ09942.1; -; mRNA.
EMBL; AY189820; AAO73817.1; -; mRNA.
EMBL; BC004394; AAH04394.1; -; mRNA.
EMBL; BC017746; AAH17746.1; -; mRNA.
CCDS; CCDS4366.1; -. [Q8IX03-1]
CCDS; CCDS54945.1; -. [Q8IX03-2]
RefSeq; NP_001155133.1; NM_001161661.1. [Q8IX03-2]
RefSeq; NP_001155134.1; NM_001161662.1.
RefSeq; NP_056053.1; NM_015238.2. [Q8IX03-1]
UniGene; Hs.484047; -.
PDB; 2Z0U; X-ray; 2.20 A; A/B=638-785.
PDBsum; 2Z0U; -.
ProteinModelPortal; Q8IX03; -.
SMR; Q8IX03; -.
BioGrid; 116884; 42.
CORUM; Q8IX03; -.
DIP; DIP-35287N; -.
IntAct; Q8IX03; 29.
MINT; MINT-1405937; -.
STRING; 9606.ENSP00000427772; -.
iPTMnet; Q8IX03; -.
PhosphoSitePlus; Q8IX03; -.
BioMuta; WWC1; -.
DMDM; 74714457; -.
EPD; Q8IX03; -.
MaxQB; Q8IX03; -.
PaxDb; Q8IX03; -.
PeptideAtlas; Q8IX03; -.
PRIDE; Q8IX03; -.
DNASU; 23286; -.
Ensembl; ENST00000265293; ENSP00000265293; ENSG00000113645. [Q8IX03-1]
Ensembl; ENST00000521089; ENSP00000427772; ENSG00000113645. [Q8IX03-2]
GeneID; 23286; -.
KEGG; hsa:23286; -.
UCSC; uc003lzu.4; human. [Q8IX03-1]
CTD; 23286; -.
DisGeNET; 23286; -.
EuPathDB; HostDB:ENSG00000113645.13; -.
GeneCards; WWC1; -.
HGNC; HGNC:29435; WWC1.
HPA; HPA038016; -.
HPA; HPA038017; -.
MIM; 610533; gene.
MIM; 615602; phenotype.
neXtProt; NX_Q8IX03; -.
OpenTargets; ENSG00000113645; -.
PharmGKB; PA143485670; -.
eggNOG; KOG3209; Eukaryota.
eggNOG; COG5021; LUCA.
GeneTree; ENSGT00410000025556; -.
HOGENOM; HOG000013211; -.
HOVERGEN; HBG058082; -.
InParanoid; Q8IX03; -.
KO; K16685; -.
OMA; HHTHIPR; -.
OrthoDB; EOG091G0UU4; -.
PhylomeDB; Q8IX03; -.
TreeFam; TF324040; -.
Reactome; R-HSA-2028269; Signaling by Hippo.
SignaLink; Q8IX03; -.
SIGNOR; Q8IX03; -.
ChiTaRS; WWC1; human.
EvolutionaryTrace; Q8IX03; -.
GeneWiki; WWC1; -.
GenomeRNAi; 23286; -.
PRO; PR:Q8IX03; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113645; -.
CleanEx; HS_WWC1; -.
ExpressionAtlas; Q8IX03; baseline and differential.
Genevisible; Q8IX03; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
GO; GO:0019900; F:kinase binding; IPI:BHF-UCL.
GO; GO:0030674; F:protein binding, bridging; IEA:Ensembl.
GO; GO:0032947; F:protein complex scaffold activity; IDA:BHF-UCL.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0016477; P:cell migration; IDA:UniProtKB.
GO; GO:0030010; P:establishment of cell polarity; TAS:BHF-UCL.
GO; GO:0035329; P:hippo signaling; TAS:Reactome.
GO; GO:0035331; P:negative regulation of hippo signaling; IDA:BHF-UCL.
GO; GO:0046621; P:negative regulation of organ growth; IMP:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB.
GO; GO:0035330; P:regulation of hippo signaling; IMP:UniProtKB.
GO; GO:0032386; P:regulation of intracellular transport; TAS:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00201; WW; 2.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR001202; WW_dom.
InterPro; IPR036020; WW_dom_sf.
Pfam; PF00397; WW; 2.
SMART; SM00456; WW; 2.
SUPFAM; SSF49562; SSF49562; 1.
SUPFAM; SSF51045; SSF51045; 2.
PROSITE; PS01159; WW_DOMAIN_1; 1.
PROSITE; PS50020; WW_DOMAIN_2; 2.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Cell membrane;
Cell projection; Coiled coil; Complete proteome; Cytoplasm; Membrane;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Transcription; Transcription regulation.
CHAIN 1 1113 Protein KIBRA.
/FTId=PRO_0000242153.
DOMAIN 6 39 WW 1. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 53 86 WW 2. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 655 783 C2.
REGION 839 1113 Interaction with histone H3.
REGION 953 996 Interaction with PRKCZ.
COILED 107 193 {ECO:0000255}.
COILED 293 431 {ECO:0000255}.
COILED 1001 1032 {ECO:0000255}.
MOTIF 1111 1113 ADDV motif.
COMPBIAS 261 265 Poly-Ser.
COMPBIAS 819 873 Glu-rich.
MOD_RES 141 141 Phosphoserine.
{ECO:0000250|UniProtKB:Q5SXA9}.
MOD_RES 535 535 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 542 542 Phosphoserine; by CDK1.
{ECO:0000269|PubMed:22784093}.
MOD_RES 899 899 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 912 912 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 927 927 Phosphoserine.
{ECO:0000250|UniProtKB:Q5SXA9}.
MOD_RES 929 929 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 931 931 Phosphoserine; by CDK1.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:22784093}.
MOD_RES 947 947 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 975 975 Phosphoserine; by PKC/PRKCZ.
{ECO:0000269|PubMed:15081397}.
MOD_RES 978 978 Phosphoserine; by PKC/PRKCZ.
{ECO:0000269|PubMed:15081397}.
VAR_SEQ 974 974 S -> SPPPQPS (in isoform 2).
{ECO:0000303|PubMed:10048485,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_019448.
VARIANT 250 250 R -> C (in dbSNP:rs17551608).
/FTId=VAR_026844.
VARIANT 734 734 M -> I (polymorphism; associated with
Ala-735; affects KIBRA lipid-binding
specificity showing stronger interactions
with PI(4)P and PI(5)P; dbSNP:rs3822660).
{ECO:0000269|PubMed:23778582}.
/FTId=VAR_053449.
VARIANT 735 735 S -> A (polymorphism; associated with
Ile-734; affects KIBRA lipid-binding
specificity showing stronger interactions
with PI(4)P and PI(5)P; dbSNP:rs3822659).
{ECO:0000269|PubMed:23778582}.
/FTId=VAR_053450.
CONFLICT 561 561 F -> L (in Ref. 4; CAE45903).
{ECO:0000305}.
CONFLICT 759 759 C -> R (in Ref. 4; CAE45903).
{ECO:0000305}.
CONFLICT 811 811 T -> TVSWDQ (in Ref. 6; AAO73817).
{ECO:0000305}.
CONFLICT 834 834 S -> N (in Ref. 4; CAE45903).
{ECO:0000305}.
CONFLICT 865 865 Missing (in Ref. 6; AAO73817).
{ECO:0000305}.
CONFLICT 1051 1051 Missing (in Ref. 4; CAE45903 and 5;
BAA74892). {ECO:0000305}.
CONFLICT 1064 1065 DK -> AR (in Ref. 6; AAO73817).
{ECO:0000305}.
STRAND 660 669 {ECO:0000244|PDB:2Z0U}.
TURN 670 673 {ECO:0000244|PDB:2Z0U}.
STRAND 674 683 {ECO:0000244|PDB:2Z0U}.
HELIX 685 687 {ECO:0000244|PDB:2Z0U}.
STRAND 694 704 {ECO:0000244|PDB:2Z0U}.
HELIX 708 711 {ECO:0000244|PDB:2Z0U}.
STRAND 712 714 {ECO:0000244|PDB:2Z0U}.
STRAND 722 733 {ECO:0000244|PDB:2Z0U}.
HELIX 736 741 {ECO:0000244|PDB:2Z0U}.
STRAND 743 751 {ECO:0000244|PDB:2Z0U}.
STRAND 757 766 {ECO:0000244|PDB:2Z0U}.
STRAND 777 784 {ECO:0000244|PDB:2Z0U}.
SEQUENCE 1113 AA; 125301 MW; 9010B9C127129165 CRC64;
MPRPELPLPE GWEEARDFDG KVYYIDHTNR TTSWIDPRDR YTKPLTFADC ISDELPLGWE
EAYDPQVGDY FIDHNTKTTQ IEDPRVQWRR EQEHMLKDYL VVAQEALSAQ KEIYQVKQQR
LELAQQEYQQ LHAVWEHKLG SQVSLVSGSS SSSKYDPEIL KAEIATAKSR VNKLKREMVH
LQHELQFKER GFQTLKKIDK KMSDAQGSYK LDEAQAVLRE TKAIKKAITC GEKEKQDLIK
SLAMLKDGFR TDRGSHSDLW SSSSSLESSS FPLPKQYLDV SSQTDISGSF GINSNNQLAE
KVRLRLRYEE AKRRIANLKI QLAKLDSEAW PGVLDSERDR LILINEKEEL LKEMRFISPR
KWTQGEVEQL EMARKRLEKD LQAARDTQSK ALTERLKLNS KRNQLVRELE EATRQVATLH
SQLKSLSSSM QSLSSGSSPG SLTSSRGSLV ASSLDSSTSA SFTDLYYDPF EQLDSELQSK
VEFLLLEGAT GFRPSGCITT IHEDEVAKTQ KAEGGGRLQA LRSLSGTPKS MTSLSPRSSL
SSPSPPCSPL MADPLLAGDA FLNSLEFEDP ELSATLCELS LGNSAQERYR LEEPGTEGKQ
LGQAVNTAQG CGLKVACVSA AVSDESVAGD SGVYEASVQR LGASEAAAFD SDESEAVGAT
RIQIALKYDE KNKQFAILII QLSNLSALLQ QQDQKVNIRV AVLPCSESTT CLFRTRPLDA
SDTLVFNEVF WVSMSYPALH QKTLRVDVCT TDRSHLEECL GGAQISLAEV CRSGERSTRW
YNLLSYKYLK KQSRELKPVG VMAPASGPAS TDAVSALLEQ TAVELEKRQE GRSSTQTLED
SWRYEETSEN EAVAEEEEEE VEEEEGEEDV FTEKASPDMD GYPALKVDKE TNTETPAPSP
TVVRPKDRRV GTPSQGPFLR GSTIIRSKTF SPGPQSQYVC RLNRSDSDSS TLSKKPPFVR
NSLERRSVRM KRPSSVKSLR SERLIRTSLD LELDLQATRT WHSQLTQEIS VLKELKEQLE
QAKSHGEKEL PQWLREDERF RLLLRMLEKR QMDRAEHKGE LQTDKMMRAA AKDVHRLRGQ
SCKEPPEVQS FREKMAFFTR PRMNIPALSA DDV


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