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CTNNB1 — SOX9
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
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Gene Ontology Complexes protein complex:
protein complex complex (HSF1-TRMT112-HIST1H4A-UBQLN1-CDX2-USP28-HDAC5-CAV3-CANX-LHX1-TUBA3C-TUBA3E-PI4K2A-NR0B2-RYR2-NTRK1-MPP5-N6AMT1-STAP1-ZFP42-FADD-ATP6V0D1-PRKCDBP-AQP2-FNTB-PRPSAP2-WIPI2-CRB3-CRB2-PEX11A-LDB1-RBP4-TMEM102-GATA2-ADCY2-DZIP1-SYK-TUBB4B-PTPN11-KAT5-CEP290-SYP-ASF1B-PLEKHA2-KIF24-MYO5B-RGP1-CFTR-SPTBN5-VPS72-ACTA2-PRKCI-CNST-SNX4-GNAO1-NFKBIA-UBE2D2-EPB41-RAB5A-GLUL-BSND-GSK3B-SKI-XRCC6-PPM1E-TTR-TUBA1A-SUCLG1-TRIAP1-AKT1S1-MYD88-NPPB-GDF11-INCENP-PLCB3-BECN1-PRKAB1-SOD1-TUBB1-NPHS2-NPHS1-EPS8L1-GDI1-TUBB2A-TUBB2B-SUCLG2-PEX3-TUBAL3-ERLIN1-MAGED1-GCH1-TUBB-CPS1-MEF2C-ZNF703-SLC22A6-CPLX1-EIF4EBP1-TUBE1-FLNA-CD19-STX1A-HDAC2-TOMM40L-HDAC6-SMAD6-SMAD7-TLE6-SMAD2-PARD6B-STXBP1-ACR-TRPC1-PARD6A-TRPC4-PANX1-DCTN1-SOX9-PXMP2-BCR-SET-MALT1-BHMT-RILP-TRADD-HIST1H3A-MAPK1-PVALB-NFKB1-NUFIP1-ACVR2B-TAL1-FOXP3-SSX2IP-GNB2-SLC27A5-GOPC-PAX2-CXADR-AIF1L-APBA1-MYL12A-LMO2-ID2-CCDC113-DDOST-SPP2-GATAD2B-PLN-ERCC8-BIRC8-ASF1A-CAB39-BIRC3-BIRC2-CTNNB1-CORO1A-PRELID1-HAND2-CHAF1B-SCAP-GNAT3-CDC20-SMARCA4-IQGAP1-YWHAZ-CEBPA-PRPS2-AXIN1-XRCC5-YWHAQ-UVRAG-SLC51B-RGS4-RGS6-HTT-YWHAB-APCS-CDCA8-RIPK1-MTA2-SIN3A-ANXA1-NOS1-SNTA1-TRAF6-KPNB1-VCL-VCP-PTRF-PRKCZ-SKIL-RAB3A-KRIT1-SSBP3-PRPSAP1-PPP1CC-TAB1-MYO6-ACTL7A-TUBG2-MBD2-COL6A1-COL6A2-BCL3)
Helps et al., Biochem J 2000, Lauderdale et al., Proc Natl Acad Sci U S A 2000, Didichenko et al., FEBS Lett 2000, Koh et al., Curr Biol 2002, Fan et al., Mol Cell Biol 2002, Groisman et al., Cell 2003, Offenhäuser et al., Mol Biol Cell 2004, Tagami et al., Cell 2004, Doyon et al., Mol Cell Biol 2004, Moore et al., Genomics 2004, Sun et al., Mol Cell 2004, Zang et al., J Cell Biochem 2004, Tian et al., Cancer Res 2005, An et al., Biochemistry 2005, Mahajan et al., Proc Natl Acad Sci U S A 2005, Vader et al., EMBO Rep 2006, Yeh et al., J Biol Chem 2006, Li et al., Immunol Rev 2006, Agbas et al., Biochem J 2007, Swiatecka-Urban et al., J Biol Chem 2007, McKeegan et al., Mol Cell Biol 2007, Shono et al., J Am Soc Nephrol 2007, Popov et al., Cell cycle (Georgetown, Tex.) 2007, Sato et al., J Biol Chem 2008, Fitzgerald et al., J Biol Chem 2008, Lyssand et al., J Biol Chem 2008, Figaro et al., FEBS Lett 2008, Ueda et al., Proc Natl Acad Sci U S A 2008, Shimojo et al., J Biol Chem 2008, Costantini et al., Blood 2009, Mitsuishi et al., J Biol Chem 2010, Masuda et al., J Biol Chem 2010, Koch et al., J Cell Sci 2010, Boëda et al., J Biol Chem 2011, Sircoulomb et al., EMBO Mol Med 2011, Hoxhaj et al., J Cell Sci 2012, Uckun et al., Proc Natl Acad Sci U S A 2012, Pusapati et al., J Biol Chem 2012, Ghai et al., Proc Natl Acad Sci U S A 2013, Kelly et al., PLoS Biol 2013, Chiang et al., PloS one 2013, Dauphinee et al., J Immunol 2013, Potting et al., Cell Metab 2013, Ludwig et al., PLoS Biol 2013, Lee et al., Proc Natl Acad Sci U S A 2013, Kobayashi et al., J Cell Biol 2014, Zheng et al., Am J Physiol 1994, Kumar et al., Biochem Biophys Res Commun 1998, Watabe-Uchida et al., J Cell Biol 1998, Haft et al., Mol Cell Biol 1998
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Gene Ontology Complexes transcription factor complex:
transcription factor complex complex (ATF7IP-GSC-GCM1-MAFB-NKX2-1-NKX2-5-RARG-KLF4-FOXF1-FOXF2-FOXE3-LDB1-ZFHX3-GATA6-SNAI3-FOXH1-KAT5-AHR-EYA3-NFATC2-CRX-MED27-HES6-SKI-XRCC6-ARNTL-SUB1-JUN-SOX17-SCX-DMBX1-TCF4-TCF7-PDLIM1-TFEB-LBX1-TRRAP-NAA16-EPAS1-MGA-PTF1A-HOXD12-MEF2B-TFDP3-TFDP1-HDAC2-YY1-SMAD9-CLOCK-ONECUT3-SMAD5-SMAD6-SMAD7-SMAD1-SMAD2-PRKDC-RCOR2-NHLH2-REL-TBX5-ARNTL2-BSX-HOXA10-HOXB13-MED23-PUS1-TAL1-RBL1-RBL2-MINA-HMGA1-BARX2-LEF1-EP300-PMF1-ARID5A-WWTR1-LMO2-LMO4-TP73-ABT1-CDK2-DKFZp686M216-CREG1-CTNNB1-SOX9-HAND2-SOX2-TEAD2-MYOG-TEAD4-CEBPA-GFI1B-MYOD1-ALX1-NPAS4-TFAP2D-FIGLA-ALX4-ETS1-PROP1-ASCL3-HCLS1-MSX1-MSX2-SRA1-AJUBA-MTA2-SIN3A-POU3F2-POU3F1-BEX1-MLXIPL-NR2E3-PBX2-ANKRD1-E2F6-E2F5-E2F4-E2F3-E2F2-E2F1-E2F8-CREBBP-ATF5-ATF4-POU2F3)
Kaspar et al., J Biol Chem 1999, Wang et al., J Biol Chem 1999, Nagpal et al., J Biol Chem 1999, Blixt et al., Genes Dev 2000, Carlberg et al., Mol Cell Biol Res Commun 2000, Bae et al., Development 2000, Cairo et al., Hum Mol Genet 2001, Tutter et al., Genes Dev 2001, Willis et al., J Biol Chem 2002, Bayne et al., Mol Hum Reprod 2004, Schubert et al., J Biol Chem 2004, Han et al., J Mol Biol 2005, Rodriguez et al., EMBO J 2005, Han et al., Nucleic Acids Res 2005, Zhang et al., Mol Cell Biol 2007, Wong et al., Cell 2009, Stevens et al., Immunology 2009, Stefanovic et al., J Cell Biol 2009, Skokowa et al., Nat Med 2012, Ge et al., Cell 1994, Durocher et al., EMBO J 1997, Hogenesch et al., Proc Natl Acad Sci U S A 1998, Hellqvist et al., J Biol Chem 1998, Ryu et al., Nature 1999
Text-mined interactions from Literome
Akiyama et al., Genes Dev 2004
:
Sox9 markedly inhibits activation of beta-catenin dependent promoters and
stimulates degradation of
beta-catenin by the ubiquitination/proteasome pathway
Blache et al., J Cell Biol 2004
(Carcinoma...) :
We provide in vitro and in vivo evidence that a bipartite
beta-catenin/TCF4 transcription factor, the effector of the Wnt signaling pathway, is
required for
SOX9 expression in epithelial cells
Wang et al., Cancer Res 2007
(Neoplasm Recurrence, Local...) :
SOX9 message and protein levels in prostate cancer cells were increased by treatment with glycogen synthase kinase 3beta inhibitor ( SB415286 ), and SOX9 was reduced when beta-catenin was down-regulated by small interfering RNA ( siRNA ), indicating that
SOX9 expression in prostate cancer is
regulated by
Wnt/beta-catenin signaling
Bastide et al., J Cell Biol 2007
:
Sox9 expression
requires an active
beta-catenin-Tcf complex, the transcriptional effector of the Wnt pathway
Wang et al., Cancer Res 2008
(Neoplasm Invasiveness...) :
Moreover,
SOX9 expression in PCa cell lines enhanced tumor cell proliferation and was
beta-catenin regulated
Topol et al., J Biol Chem 2009
:
Chondrocyte fate determination and maintenance requires
Sox9 , an intrinsic transcription factor, but is
inhibited by
Wnt/beta-catenin signaling activated by extrinsic Wnt ligands ... We found that
Sox9 employed two distinct mechanisms to inhibit Wnt/beta-catenin signaling : the Sox9 N terminus is necessary and
sufficient to promote
beta-catenin degradation, whereas the C terminus is required to inhibit beta-catenin transcriptional activity without affecting its stability ... Independent of its DNA binding ability, nuclear localization of
Sox9 is both necessary and
sufficient to enhance
beta-catenin phosphorylation and its subsequent degradation