Transcriptional regulation by RUNX3 (Homo sapiens)

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8, 11, 12, 14, 18...66594, 16, 2938912, 9553, 101, 1032811138482865, 106129354, 10881312351, 53, 69, 71, 82...87, 8987, 892, 10838910, 36, 41, 5489, 938965, 10619, 28814838621111113715, 17, 5189665115, 1789, 9337604, 16, 29nucleoplasmcytosolYAP1 p-S166,S188-MDM2dimerCDKN1A gene RUNX3 CCND1UBB(77-152) CBFB RUNX3 UBC(229-304) UBC(1-76) SMURFEP300 CDKN2A geneEP300 PSMD5 RUNX3 PSMB1 RUNX3ITGA4 TEAD4 ADPLEF1 YAP1:TEAD1,TEAD4,(TEAD2,TEAD3)RUNX3:CBFB:EP300UBC(229-304) TEAD3 CBFB Ac-K94,K171-RUNX3:CBFB:EP300:BRD2CBFBHDAC4 BRD2 PPARA RUNX1 mRNAPSMD1 TEADs:YAP1PolyUb-RUNX3RUNX3 RUNX1:CBFB,(Ac-K94,K171-RUNX3:CBFB:EP300:BRD2):CDKN2A geneUBB(153-228) PSMC2 Ac-K94,K171-RUNX3 TCF7L1/TCF7L2/LEF1:CTNNB1:MYC geneAc-K94,K171-RUNX3 UBC(305-380) ITGAL,(ITGA4)RBPJ CTNNB1 CHD9 PSMA3 RUNX3 GTP MAML2 TEAD4 PSMD13 UBC(381-456) RUNX3:CBFB:CCND1:HDAC4PSMB8 RUNX3 Ac-K94,K171-RUNX3 CBFB TBL1XR1 CCND1 gene MAMLD1 Ac-K94,K171-RUNX3 p-S166,S188-MDM2 TEAD4 KAT2B TGFB1 TEAD4 CTNNB1 LEF1 TEADs:YAP1:CTGF geneUBC(381-456) JAG1PSMB3 RUNX1 genePSMD4 NCOA6 NOTCH1 CoactivatorComplexCARM1 PSMA5 TCF7L1/TCF7L2/LEF1:CTNNB1LEF1 KAT2A H2OMAMLD1 CBFB PSMC5 MAML3 CBFB Ac-K94,K171-RUNX3:CBFB:BRD2:CCND1MYC geneHDAC4TEAD1 UBC(1-76) TCF7L2 CTNNB1 UBC(153-228) EPA RUNX3 CTGFp14-ARF mRNAPSMB5 RUNX3 CCND1 CBFB RUNX1 gene NICD1 CBFB UBC(153-228) UBA52(1-76) ATPNCOA1 UBC(77-152) RUNX3YAP1 CREBBP PSMD7 TCF7L2 RUNX3 MyrG-p-Y419-SRCPSMA1 ITGAL TEAD1 RBPJ Ac-K94,K171-RUNX3 26S proteasomeEP300 TCF7L2 PSMC6 RUNX1:CBFB,(Ac-K94,K171-RUNX3:CBFB:EP300:BRD2)PSMB9 NICD1 RUNX3:CBFB:ITGALgene,(ITGA4 gene)KAT2A CCND1 RUNX3:p-2S-SMAD3:p-2S-SMAD3:SMAD4:CDKN1A geneCBFB CBFB RUNX3:p-2S-SMAD3:p-2S-SMAD3:SMAD4:FOXO3:BCL2L11 geneRUNX3 WWTR1 NICD1 PPARA:RXRACoactivator complexSPP1 genePolyUb-K94,K148-RUNX3TCF7L2 MAML1 CoA-SHRUNX3 BRD2 CBFB EP300 PSMD12 ITGA4 gene MyrG-p-Y419-SRC KAT2B TCF7L2 MAML3 PSMD11 BRD2 UBB(1-76) LINA ZFHX3 TCF7L1 RUNX3 EP300 RUNX3 TCF7 CDKN1A geneTEAD1 CCND1PSMA4 UBC(609-684) MAML2 SMAD4 TEAD1 TP53 TetramerAc-K94,K171-RUNX3:CBFB:BRD2:CCND1:HDAC4JAG1 gene BRD2 p14-ARFSNW1 MAMLD1 FOXO3RBPJ MAMLD1 TEAD:WWTR1(TAZ)p-S423,S425-SMAD3 RXRA KRAS TEAD2 SMAD4 CDKN1ATGS1 RUNX3:JAG1 genep-Y-RUNX3UbBCL2L11 gene BCL2L11 genePSMD14 HES1 gene p-2S-SMAD3:p-2S-SMAD3:SMAD4BRD2 MAML1 Dimeric TGFB1SMURF2 PSMA2 SPP1RUNX3:TCF7L2,(LEF1,TCF7L1)LEF1 CTNNB1 TCF7L1 RUNX3:ZFHX3PSMB6 FOXO3 p-S423,S425-SMAD3 p-S166,S188-MDM2 ITGAL gene MAML2 p-S423,S425-SMAD3 TCF7L2 ALA CTGF gene Ac-K94,K171-RUNX3 ITGA4 gene SNW1 RUNX3:p-S166,S188-MDM2 dimerPSMC3 TCF7L1 TCF7 BRD2 UBB(77-152) RUNX1 RUNX3 UBA52(1-76) RORC geneEP300 TEAD3 UBC(533-608) TEAD1 RUNX3:CBFB:RUNX1geneRPS27A(1-76) PSMB4 Signaling byTGF-beta ReceptorComplexRUNX3:CTNNB1:TCF7L2,(LEF1,TCF7L1,TCF1)PSME3 PSMC1 CDKN2A gene HES1 gene RUNX3 RPS27A(1-76) KAT2A Ac-CoASMAD4 UBB(1-76) CTNNB1 TCF7L1 LEF1 MAML1 CREBBP RUNX3:NOTCH1Coactivator ComplexCTGF geneRUNX3 EP300PSMD3 TEAD2 RUNX3 MYCTEAD2 SMURF1 PSMF1 HELZ2 TEAD3 CTNNB1:TCF7L2,LEF1:CCND1 GeneRUNX3:NOTCH1coactivatorcomplex:HES1 geneSHFM1 UBB(153-228) RUNX3:CBFB:RORC geneRUNX3 CREBBP TEAD2 PolyUb-K94,K148-RUNX3LEF1 NOTCH1 CoactivatorComplex:HES1 GeneTP53 UBC(457-532) RUNX1 SNW1 RUNX3:CBFBITGAL gene PSMD6 HES1KAT2A RUNX3:TP53 tetramerCCND1 SNW1 TBL1X RBPJ TEAD4 PSMA6 SMAD4 LEF1 RUNX3:CBFB:CTNNB1:TCF7L2,(LEF1)PSMB10 CTNNB1:TCF7L2,(LEF1,TCF7L1,TCF7)CTNNB1 Peroxisome Proliferator Receptor Element (PPRE) TEAD3 RORC-2MAML2 PSMC4 KAT2B PSME1 UBC(533-608) YAP1 UBC(457-532) PSMB7 CBFB MyrG-p-Y419-SRC:RUNX3SMARCD3 CBFB HDAC4 CTNNB1:TCF7L2,LEF1TEAD2 EP300 Signaling by NOTCH1RORC gene UBC(305-380) AA ITGAL gene,(ITGA4gene)TCF7L2 MAML3 HES1 geneCH3COO-MYC gene ZFHX3TEAD3 Ac-K94,K171-RUNX3:CBFB:EP300RUNX3:p-2S-SMAD3:p-2S-SMAD3:SMAD4RUNX3 JAG1 genePSMD8 YAP1 LEF1 PSME2 EP300 PSMD9 PSMD2 MED1 UbBCL2L11NCOA2 KAT2B EP300MAML1 PSMA7 BRD2 homodimerPSMB2 RUNX3 p-S423,S425-SMAD3 UBC(609-684) CBFB TCF7L2 CREBBP MAML3 RUNX3:YAP1:TEAD1,TEAD4,(TEAD2,TEAD3)KRAS:GTPPalm TP53 NICD1 CREBBP TCF7L1 UBC(77-152) CCND1 geneEP300 PSMD10 15, 1779, 10978910789608111111187, 892837512, 1081215, 1710663109892789312385136, 41665989481, 5, 6, 9, 13...


Description

The transcription factor RUNX3 is a RUNX family member. All RUNX family members, RUNX1, RUNX2 and RUNX3, possess a highly conserved Runt domain, involved in DNA binding. For a more detailed description of the structure of RUNX proteins, please refer to the pathway 'Transcriptional regulation by RUNX1'. Similar to RUNX1 and RUNX2, RUNX3 forms a transcriptionally active heterodimer with CBFB (CBF-beta). Studies in mice have shown that RUNX3 plays a role in neurogenesis and development of T lymphocytes. RUNX3 is implicated as a tumor suppressor gene in various human malignancies.
During nervous system formation, the Cbfb:Runx3 complex is involved in development of mouse proprioceptive dorsal root ganglion neurons by regulating expression of Ntrk3 (Neurotrophic tyrosine kinase receptor type 3) and possibly other genes (Inoue et al. 2002, Kramer et al. 2006, Nakamura et al. 2008, Dykes et al. 2011, Ogihara et al. 2016). It is not yet known whether RUNX3 is involved in human neuronal development and neuronal disorders.
RUNX3 plays a major role in immune response. RUNX3 regulates development of T lymphocytes. In mouse hematopoietic stem cells, expression of Runx3 is regulated by the transcription factor TAL1 (Landry et al. 2008). RUNX3 promotes the CD8+ lineage fate in developing thymocytes. In the CD4+ thymocyte lineage in mice, the transcription factor ThPOK induces transcription of SOCS family members, which repress Runx3 expression (Luckey et al. 2014). RUNX3, along with RUNX1 and ETS1, is implicated in regulation of transcription of the CD6 gene, encoding a lymphocyte surface receptor expressed on developing and mature T cells (Arman et al. 2009). RUNX3 and ThPOK regulate intestinal CD4+ T cell immunity in a TGF-beta and retinoic acid-dependent manner, which is important for cellular defense against intestinal pathogens (Reis et al. 2013). Besides T lymphocytes, RUNX3 is a key transcription factor in the commitment of innate lymphoid cells ILC1 and ILC3 (Ebihara et al. 2015). RUNX3 regulates expression of CD11A and CD49D integrin genes, involved in immune and inflammatory responses (Dominguez-Soto et al. 2005). RUNX3 is involved in mouse TGF-beta-mediated dendritic cell function and its deficiency is linked to airway inflammation (Fainaru et al. 2004).
In addition to its developmental role, RUNX3 is implicated as a tumor suppressor. The loss of RUNX3 expression and function was first causally linked to the genesis and progression of human gastric cancer (Li et al. 2002). Expression of RUNX3 increases in human pancreatic islet of Langerhans cells but not in pancreatic adenocarcinoma cells in response to differentiation stimulus (serum withdrawal) (Levkovitz et al. 2010). Hypermethylation of the RUNX3 gene is associated with an increased risk for progression of Barrett's esophagus to esophageal adenocarcinoma (Schulmann et al. 2005). Hypermethylation-mediated silencing of the RUNX3 gene expression is also frequent in granulosa cell tumors (Dhillon et al. 2004) and has also been reported in colon cancer (Weisenberger et al. 2006), breast cancer (Lau et al. 2006, Huang et al. 2012), bladder cancer (Wolff et al. 2008) and gastric cancer (Li et al. 2002). In colorectal cancer, RUNX3 is one of the five markers in a gene panel used to classify CpG island methylator phenotype (CIMP+) (Weisenberger et al. 2006).
RUNX3 and CBFB are frequently downregulated in gastric cancer. RUNX3 cooperates with TGF-beta to maintain homeostasis in the stomach and is involved in TGF-beta-induced cell cycle arrest of stomach epithelial cells. Runx3 knockout mice exhibit decreased sensitivity to TGF-beta and develop gastric epithelial hyperplasia (Li et al. 2002, Chi et al. 2005). RUNX3-mediated inhibition of binding of TEADs:YAP1 complexes to target promoters is also implicated in gastric cancer suppression (Qiao et al. 2016).
RUNX3 is a negative regulator of NOTCH signaling and RUNX3-mediated inhibition of NOTCH activity may play a tumor suppressor role in hepatocellular carcinoma (Gao et al. 2010, Nishina et al. 2011).
In addition to RUNX3 silencing through promoter hypermethylation in breast cancer (Lau et al. 2006), Runx3+/- mice are predisposed to breast cancer development. RUNX3 downregulates estrogen receptor alpha (ESR1) protein levels in a proteasome-dependent manner (Huang et al. 2012).
Besides its tumor suppressor role, mainly manifested through its negative effect on cell proliferation, RUNX3 can promote cancer cell invasion by stimulating expression of genes involved in metastasis, such as osteopontin (SPP1) (Whittle et al. 2015). View original pathway at:Reactome.

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Reactome-Converter 
Pathway is converted from Reactome ID: 8878159
Reactome-version 
Reactome version: 62
Reactome Author 
Reactome Author: Orlic-Milacic, Marija

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  63. Cordle J, Redfieldz C, Stacey M, van der Merwe PA, Willis AC, Champion BR, Hambleton S, Handford PA.; ''Localization of the delta-like-1-binding site in human Notch-1 and its modulation by calcium affinity.''; PubMed Europe PMC Scholia
  64. Benedito R, Roca C, Sörensen I, Adams S, Gossler A, Fruttiger M, Adams RH.; ''The notch ligands Dll4 and Jagged1 have opposing effects on angiogenesis.''; PubMed Europe PMC Scholia
  65. Song R, Koo BK, Yoon KJ, Yoon MJ, Yoo KW, Kim HT, Oh HJ, Kim YY, Han JK, Kim CH, Kong YY.; ''Neuralized-2 regulates a Notch ligand in cooperation with Mind bomb-1.''; PubMed Europe PMC Scholia
  66. Wildey GM, Patil S, Howe PH.; ''Smad3 potentiates transforming growth factor beta (TGFbeta )-induced apoptosis and expression of the BH3-only protein Bim in WEHI 231 B lymphocytes.''; PubMed Europe PMC Scholia
  67. Tetsu O, McCormick F.; ''Beta-catenin regulates expression of cyclin D1 in colon carcinoma cells.''; PubMed Europe PMC Scholia
  68. Reis BS, Rogoz A, Costa-Pinto FA, Taniuchi I, Mucida D.; ''Mutual expression of the transcription factors Runx3 and ThPOK regulates intestinal CD4⁺ T cell immunity.''; PubMed Europe PMC Scholia
  69. Maier MM, Gessler M.; ''Comparative analysis of the human and mouse Hey1 promoter: Hey genes are new Notch target genes.''; PubMed Europe PMC Scholia
  70. Spender LC, Whiteman HJ, Karstegl CE, Farrell PJ.; ''Transcriptional cross-regulation of RUNX1 by RUNX3 in human B cells.''; PubMed Europe PMC Scholia
  71. Gao J, Chen Y, Wu KC, Liu J, Zhao YQ, Pan YL, Du R, Zheng GR, Xiong YM, Xu HL, Fan DM.; ''RUNX3 directly interacts with intracellular domain of Notch1 and suppresses Notch signaling in hepatocellular carcinoma cells.''; PubMed Europe PMC Scholia
  72. Gustafsson MV, Zheng X, Pereira T, Gradin K, Jin S, Lundkvist J, Ruas JL, Poellinger L, Lendahl U, Bondesson M.; ''Hypoxia requires notch signaling to maintain the undifferentiated cell state.''; PubMed Europe PMC Scholia
  73. Fainaru O, Woolf E, Lotem J, Yarmus M, Brenner O, Goldenberg D, Negreanu V, Bernstein Y, Levanon D, Jung S, Groner Y.; ''Runx3 regulates mouse TGF-beta-mediated dendritic cell function and its absence results in airway inflammation.''; PubMed Europe PMC Scholia
  74. Wu G, Lyapina S, Das I, Li J, Gurney M, Pauley A, Chui I, Deshaies RJ, Kitajewski J.; ''SEL-10 is an inhibitor of notch signaling that targets notch for ubiquitin-mediated protein degradation.''; PubMed Europe PMC Scholia
  75. Koo BK, Yoon MJ, Yoon KJ, Im SK, Kim YY, Kim CH, Suh PG, Jan YN, Kong YY.; ''An obligatory role of mind bomb-1 in notch signaling of mammalian development.''; PubMed Europe PMC Scholia
  76. Fisher AL, Ohsako S, Caudy M.; ''The WRPW motif of the hairy-related basic helix-loop-helix repressor proteins acts as a 4-amino-acid transcription repression and protein-protein interaction domain.''; PubMed Europe PMC Scholia
  77. Bray SJ, Takada S, Harrison E, Shen SC, Ferguson-Smith AC.; ''The atypical mammalian ligand Delta-like homologue 1 (Dlk1) can regulate Notch signalling in Drosophila.''; PubMed Europe PMC Scholia
  78. Wilkins JA, Sansom OJ.; ''C-Myc is a critical mediator of the phenotypes of Apc loss in the intestine.''; PubMed Europe PMC Scholia
  79. Jin YH, Jeon EJ, Li QL, Lee YH, Choi JK, Kim WJ, Lee KY, Bae SC.; ''Transforming growth factor-beta stimulates p300-dependent RUNX3 acetylation, which inhibits ubiquitination-mediated degradation.''; PubMed Europe PMC Scholia
  80. Yamamura Y, Lee WL, Inoue K, Ida H, Ito Y.; ''RUNX3 cooperates with FoxO3a to induce apoptosis in gastric cancer cells.''; PubMed Europe PMC Scholia
  81. Perissi V, Aggarwal A, Glass CK, Rose DW, Rosenfeld MG.; ''A corepressor/coactivator exchange complex required for transcriptional activation by nuclear receptors and other regulated transcription factors.''; PubMed Europe PMC Scholia
  82. Yano T, Ito K, Fukamachi H, Chi XZ, Wee HJ, Inoue K, Ida H, Bouillet P, Strasser A, Bae SC, Ito Y.; ''The RUNX3 tumor suppressor upregulates Bim in gastric epithelial cells undergoing transforming growth factor beta-induced apoptosis.''; PubMed Europe PMC Scholia
  83. Park JI, Venteicher AS, Hong JY, Choi J, Jun S, Shkreli M, Chang W, Meng Z, Cheung P, Ji H, McLaughlin M, Veenstra TD, Nusse R, McCrea PD, Artandi SE.; ''Telomerase modulates Wnt signalling by association with target gene chromatin.''; PubMed Europe PMC Scholia
  84. Wei SJ, Williams JG, Dang H, Darden TA, Betz BL, Humble MM, Chang FM, Trempus CS, Johnson K, Cannon RE, Tennant RW.; ''Identification of a specific motif of the DSS1 protein required for proteasome interaction and p53 protein degradation.''; PubMed Europe PMC Scholia
  85. Moumen M, Chiche A, Decraene C, Petit V, Gandarillas A, Deugnier MA, Glukhova MA, Faraldo MM.; ''Myc is required for β-catenin-mediated mammary stem cell amplification and tumorigenesis.''; PubMed Europe PMC Scholia
  86. Kishi N, Tang Z, Maeda Y, Hirai A, Mo R, Ito M, Suzuki S, Nakao K, Kinoshita T, Kadesch T, Hui C, Artavanis-Tsakonas S, Okano H, Matsuno K.; ''Murine homologs of deltex define a novel gene family involved in vertebrate Notch signaling and neurogenesis.''; PubMed Europe PMC Scholia
  87. Shimizu K, Chiba S, Saito T, Kumano K, Hirai H.; ''Physical interaction of Delta1, Jagged1, and Jagged2 with Notch1 and Notch3 receptors.''; PubMed Europe PMC Scholia
  88. Oberg C, Li J, Pauley A, Wolf E, Gurney M, Lendahl U.; ''The Notch intracellular domain is ubiquitinated and negatively regulated by the mammalian Sel-10 homolog.''; PubMed Europe PMC Scholia
  89. Zhao B, Ye X, Yu J, Li L, Li W, Li S, Yu J, Lin JD, Wang CY, Chinnaiyan AM, Lai ZC, Guan KL.; ''TEAD mediates YAP-dependent gene induction and growth control.''; PubMed Europe PMC Scholia
  90. Nakamura Y, Umehara T, Nakano K, Jang MK, Shirouzu M, Morita S, Uda-Tochio H, Hamana H, Terada T, Adachi N, Matsumoto T, Tanaka A, Horikoshi M, Ozato K, Padmanabhan B, Yokoyama S.; ''Crystal structure of the human BRD2 bromodomain: insights into dimerization and recognition of acetylated histone H4.''; PubMed Europe PMC Scholia
  91. Welcker M, Clurman BE.; ''FBW7 ubiquitin ligase: a tumour suppressor at the crossroads of cell division, growth and differentiation.''; PubMed Europe PMC Scholia
  92. Chan SW, Lim CJ, Loo LS, Chong YF, Huang C, Hong W.; ''TEADs mediate nuclear retention of TAZ to promote oncogenic transformation.''; PubMed Europe PMC Scholia
  93. Matsuno K, Eastman D, Mitsiades T, Quinn AM, Carcanciu ML, Ordentlich P, Kadesch T, Artavanis-Tsakonas S.; ''Human deltex is a conserved regulator of Notch signalling.''; PubMed Europe PMC Scholia
  94. Cairo S, Armengol C, Buendia MA.; ''Activation of Wnt and Myc signaling in hepatoblastoma.''; PubMed Europe PMC Scholia
  95. Qiao Y, Lin SJ, Chen Y, Voon DC, Zhu F, Chuang LS, Wang T, Tan P, Lee SC, Yeoh KG, Sudol M, Ito Y.; ''RUNX3 is a novel negative regulator of oncogenic TEAD-YAP complex in gastric cancer.''; PubMed Europe PMC Scholia
  96. Kao HY, Ordentlich P, Koyano-Nakagawa N, Tang Z, Downes M, Kintner CR, Evans RM, Kadesch T.; ''A histone deacetylase corepressor complex regulates the Notch signal transduction pathway.''; PubMed Europe PMC Scholia
  97. Voges D, Zwickl P, Baumeister W.; ''The 26S proteasome: a molecular machine designed for controlled proteolysis.''; PubMed Europe PMC Scholia
  98. Jarriault S, Brou C, Logeat F, Schroeter EH, Kopan R, Israel A.; ''Signalling downstream of activated mammalian Notch.''; PubMed Europe PMC Scholia
  99. Shtutman M, Zhurinsky J, Simcha I, Albanese C, D'Amico M, Pestell R, Ben-Ze'ev A.; ''The cyclin D1 gene is a target of the beta-catenin/LEF-1 pathway.''; PubMed Europe PMC Scholia
  100. Yamada C, Ozaki T, Ando K, Suenaga Y, Inoue K, Ito Y, Okoshi R, Kageyama H, Kimura H, Miyazaki M, Nakagawara A.; ''RUNX3 modulates DNA damage-mediated phosphorylation of tumor suppressor p53 at Ser-15 and acts as a co-activator for p53.''; PubMed Europe PMC Scholia
  101. Ito K, Liu Q, Salto-Tellez M, Yano T, Tada K, Ida H, Huang C, Shah N, Inoue M, Rajnakova A, Hiong KC, Peh BK, Han HC, Ito T, Teh M, Yeoh KG, Ito Y.; ''RUNX3, a novel tumor suppressor, is frequently inactivated in gastric cancer by protein mislocalization.''; PubMed Europe PMC Scholia
  102. Levkovitz L, Yosef N, Gershengorn MC, Ruppin E, Sharan R, Oron Y.; ''A novel HMM-based method for detecting enriched transcription factor binding sites reveals RUNX3 as a potential target in pancreatic cancer biology.''; PubMed Europe PMC Scholia
  103. Domínguez-Soto A, Relloso M, Vega MA, Corbí AL, Puig-Kröger A.; ''RUNX3 regulates the activity of the CD11a and CD49d integrin gene promoters.''; PubMed Europe PMC Scholia
  104. Yang LT, Nichols JT, Yao C, Manilay JO, Robey EA, Weinmaster G.; ''Fringe glycosyltransferases differentially modulate Notch1 proteolysis induced by Delta1 and Jagged1.''; PubMed Europe PMC Scholia
  105. Linggi B, Müller-Tidow C, van de Locht L, Hu M, Nip J, Serve H, Berdel WE, van der Reijden B, Quelle DE, Rowley JD, Cleveland J, Jansen JH, Pandolfi PP, Hiebert SW.; ''The t(8;21) fusion protein, AML1 ETO, specifically represses the transcription of the p14(ARF) tumor suppressor in acute myeloid leukemia.''; PubMed Europe PMC Scholia
  106. Nam Y, Sliz P, Song L, Aster JC, Blacklow SC.; ''Structural basis for cooperativity in recruitment of MAML coactivators to Notch transcription complexes.''; PubMed Europe PMC Scholia
  107. Mukherjee A, Veraksa A, Bauer A, Rosse C, Camonis J, Artavanis-Tsakonas S.; ''Regulation of Notch signalling by non-visual beta-arrestin.''; PubMed Europe PMC Scholia
  108. Fischer A, Schumacher N, Maier M, Sendtner M, Gessler M.; ''The Notch target genes Hey1 and Hey2 are required for embryonic vascular development.''; PubMed Europe PMC Scholia
  109. Sansom OJ, Meniel VS, Muncan V, Phesse TJ, Wilkins JA, Reed KR, Vass JK, Athineos D, Clevers H, Clarke AR.; ''Myc deletion rescues Apc deficiency in the small intestine.''; PubMed Europe PMC Scholia
  110. Luckey MA, Kimura MY, Waickman AT, Feigenbaum L, Singer A, Park JH.; ''The transcription factor ThPOK suppresses Runx3 and imposes CD4(+) lineage fate by inducing the SOCS suppressors of cytokine signaling.''; PubMed Europe PMC Scholia
  111. Dhillon VS, Shahid M, Husain SA.; ''CpG methylation of the FHIT, FANCF, cyclin-D2, BRCA2 and RUNX3 genes in Granulosa cell tumors (GCTs) of ovarian origin.''; PubMed Europe PMC Scholia
  112. Kang JS, Liu C, Derynck R.; ''New regulatory mechanisms of TGF-beta receptor function.''; PubMed Europe PMC Scholia
  113. Puig-Kröger A, Sanchez-Elsner T, Ruiz N, Andreu EJ, Prosper F, Jensen UB, Gil J, Erickson P, Drabkin H, Groner Y, Corbi AL.; ''RUNX/AML and C/EBP factors regulate CD11a integrin expression in myeloid cells through overlapping regulatory elements.''; PubMed Europe PMC Scholia
  114. Goh YM, Cinghu S, Hong ET, Lee YS, Kim JH, Jang JW, Li YH, Chi XZ, Lee KS, Wee H, Ito Y, Oh BC, Bae SC.; ''Src kinase phosphorylates RUNX3 at tyrosine residues and localizes the protein in the cytoplasm.''; PubMed Europe PMC Scholia

History

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CompareRevisionActionTimeUserComment
114631view16:09, 25 January 2021ReactomeTeamReactome version 75
113079view11:14, 2 November 2020ReactomeTeamReactome version 74
112313view15:23, 9 October 2020ReactomeTeamReactome version 73
101212view11:10, 1 November 2018ReactomeTeamreactome version 66
100750view20:35, 31 October 2018ReactomeTeamreactome version 65
100294view19:13, 31 October 2018ReactomeTeamreactome version 64
99840view15:56, 31 October 2018ReactomeTeamreactome version 63
99397view14:34, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
93569view11:27, 9 August 2017ReactomeTeamNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
26S proteasomeComplexR-HSA-177750 (Reactome)
AA MetaboliteCHEBI:15843 (ChEBI)
ADPMetaboliteCHEBI:16761 (ChEBI)
ALA MetaboliteCHEBI:27432 (ChEBI)
ATPMetaboliteCHEBI:15422 (ChEBI)
Ac-CoAMetaboliteCHEBI:15351 (ChEBI)
Ac-K94,K171-RUNX3 ProteinQ13761 (Uniprot-TrEMBL)
Ac-K94,K171-RUNX3:CBFB:BRD2:CCND1:HDAC4ComplexR-HSA-8952063 (Reactome)
Ac-K94,K171-RUNX3:CBFB:BRD2:CCND1ComplexR-HSA-8952057 (Reactome)
Ac-K94,K171-RUNX3:CBFB:EP300:BRD2ComplexR-HSA-8951976 (Reactome)
Ac-K94,K171-RUNX3:CBFB:EP300ComplexR-HSA-8951959 (Reactome)
BCL2L11 gene ProteinENSG00000153094 (Ensembl)
BCL2L11 geneGeneProductENSG00000153094 (Ensembl)
BCL2L11ProteinO43521 (Uniprot-TrEMBL)
BRD2 ProteinP25440 (Uniprot-TrEMBL)
BRD2 homodimerComplexR-HSA-8951995 (Reactome)
CARM1 ProteinQ86X55 (Uniprot-TrEMBL)
CBFB ProteinQ13951 (Uniprot-TrEMBL)
CBFBProteinQ13951 (Uniprot-TrEMBL)
CCND1 ProteinP24385 (Uniprot-TrEMBL)
CCND1 gene ProteinENSG00000110092 (Ensembl)
CCND1 geneGeneProductENSG00000110092 (Ensembl)
CCND1ProteinP24385 (Uniprot-TrEMBL)
CDKN1A gene ProteinENSG00000124762 (Ensembl)
CDKN1A geneGeneProductENSG00000124762 (Ensembl)
CDKN1AProteinP38936 (Uniprot-TrEMBL)
CDKN2A gene ProteinENSG00000147889 (Ensembl)
CDKN2A geneGeneProductENSG00000147889 (Ensembl)
CH3COO-MetaboliteCHEBI:15366 (ChEBI)
CHD9 ProteinQ3L8U1 (Uniprot-TrEMBL)
CREBBP ProteinQ92793 (Uniprot-TrEMBL)
CTGF gene ProteinENSG00000118523 (Ensembl)
CTGF geneGeneProductENSG00000118523 (Ensembl)
CTGFProteinP29279 (Uniprot-TrEMBL)
CTNNB1 ProteinP35222 (Uniprot-TrEMBL)
CTNNB1:TCF7L2,(LEF1,TCF7L1,TCF7)ComplexR-HSA-8951429 (Reactome)
CTNNB1:TCF7L2,LEF1:CCND1 GeneComplexR-HSA-8853944 (Reactome)
CTNNB1:TCF7L2,LEF1ComplexR-HSA-8951439 (Reactome)
CoA-SHMetaboliteCHEBI:15346 (ChEBI)
Dimeric TGFB1ComplexR-HSA-170852 (Reactome)
EP300 ProteinQ09472 (Uniprot-TrEMBL)
EP300ProteinQ09472 (Uniprot-TrEMBL)
EPA MetaboliteCHEBI:28364 (ChEBI)
FOXO3 ProteinO43524 (Uniprot-TrEMBL)
FOXO3ProteinO43524 (Uniprot-TrEMBL)
GTP MetaboliteCHEBI:15996 (ChEBI)
H2OMetaboliteCHEBI:15377 (ChEBI)
HDAC4 ProteinP56524 (Uniprot-TrEMBL)
HDAC4ProteinP56524 (Uniprot-TrEMBL)
HELZ2 ProteinQ9BYK8 (Uniprot-TrEMBL)
HES1 gene ProteinENSG00000114315 (Ensembl)
HES1 geneGeneProductENSG00000114315 (Ensembl)
HES1ProteinQ14469 (Uniprot-TrEMBL)
ITGA4 ProteinP13612 (Uniprot-TrEMBL)
ITGA4 gene ProteinENSG00000115232 (Ensembl)
ITGAL ProteinP20701 (Uniprot-TrEMBL)
ITGAL gene ProteinENSG00000005844 (Ensembl)
ITGAL gene,(ITGA4 gene)ComplexR-HSA-8949354 (Reactome)
ITGAL,(ITGA4)ComplexR-HSA-8949353 (Reactome)
JAG1 gene ProteinENSG00000101384 (Ensembl)
JAG1 geneGeneProductENSG00000101384 (Ensembl)
JAG1ProteinP78504 (Uniprot-TrEMBL)
KAT2A ProteinQ92830 (Uniprot-TrEMBL)
KAT2B ProteinQ92831 (Uniprot-TrEMBL)
KRAS ProteinP01116 (Uniprot-TrEMBL)
KRAS:GTPComplexR-HSA-8951978 (Reactome)
LEF1 ProteinQ9UJU2 (Uniprot-TrEMBL)
LINA MetaboliteCHEBI:17351 (ChEBI)
MAML1 ProteinQ92585 (Uniprot-TrEMBL)
MAML2 ProteinQ8IZL2 (Uniprot-TrEMBL)
MAML3 ProteinQ96JK9 (Uniprot-TrEMBL)
MAMLD1 ProteinQ13495 (Uniprot-TrEMBL)
MED1 ProteinQ15648 (Uniprot-TrEMBL) MED1 is a component of each of the various Mediator complexes, that function as transcription co-activators. The MED1-containing compolexes include the DRIP, ARC, TRIP and CRSP compllexes.
MYC gene ProteinENSG00000136997 (Ensembl)
MYC geneGeneProductENSG00000136997 (Ensembl)
MYCProteinP01106 (Uniprot-TrEMBL)
MyrG-p-Y419-SRC ProteinP12931 (Uniprot-TrEMBL)
MyrG-p-Y419-SRC:RUNX3ComplexR-HSA-8937795 (Reactome)
MyrG-p-Y419-SRCProteinP12931 (Uniprot-TrEMBL)
NCOA1 ProteinQ15788 (Uniprot-TrEMBL)
NCOA2 ProteinQ15596 (Uniprot-TrEMBL)
NCOA6 ProteinQ14686 (Uniprot-TrEMBL)
NICD1 ProteinP46531 (Uniprot-TrEMBL)
NOTCH1 Coactivator Complex:HES1 GeneComplexR-HSA-4396364 (Reactome)
NOTCH1 Coactivator ComplexComplexR-HSA-1604462 (Reactome)
PPARA ProteinQ07869 (Uniprot-TrEMBL)
PPARA:RXRA Coactivator complexComplexR-HSA-400154 (Reactome)
PSMA1 ProteinP25786 (Uniprot-TrEMBL)
PSMA2 ProteinP25787 (Uniprot-TrEMBL)
PSMA3 ProteinP25788 (Uniprot-TrEMBL)
PSMA4 ProteinP25789 (Uniprot-TrEMBL)
PSMA5 ProteinP28066 (Uniprot-TrEMBL)
PSMA6 ProteinP60900 (Uniprot-TrEMBL)
PSMA7 ProteinO14818 (Uniprot-TrEMBL)
PSMB1 ProteinP20618 (Uniprot-TrEMBL)
PSMB10 ProteinP40306 (Uniprot-TrEMBL)
PSMB2 ProteinP49721 (Uniprot-TrEMBL)
PSMB3 ProteinP49720 (Uniprot-TrEMBL)
PSMB4 ProteinP28070 (Uniprot-TrEMBL)
PSMB5 ProteinP28074 (Uniprot-TrEMBL)
PSMB6 ProteinP28072 (Uniprot-TrEMBL)
PSMB7 ProteinQ99436 (Uniprot-TrEMBL)
PSMB8 ProteinP28062 (Uniprot-TrEMBL)
PSMB9 ProteinP28065 (Uniprot-TrEMBL)
PSMC1 ProteinP62191 (Uniprot-TrEMBL)
PSMC2 ProteinP35998 (Uniprot-TrEMBL)
PSMC3 ProteinP17980 (Uniprot-TrEMBL)
PSMC4 ProteinP43686 (Uniprot-TrEMBL)
PSMC5 ProteinP62195 (Uniprot-TrEMBL)
PSMC6 ProteinP62333 (Uniprot-TrEMBL)
PSMD1 ProteinQ99460 (Uniprot-TrEMBL)
PSMD10 ProteinO75832 (Uniprot-TrEMBL)
PSMD11 ProteinO00231 (Uniprot-TrEMBL)
PSMD12 ProteinO00232 (Uniprot-TrEMBL)
PSMD13 ProteinQ9UNM6 (Uniprot-TrEMBL)
PSMD14 ProteinO00487 (Uniprot-TrEMBL)
PSMD2 ProteinQ13200 (Uniprot-TrEMBL)
PSMD3 ProteinO43242 (Uniprot-TrEMBL)
PSMD4 ProteinP55036 (Uniprot-TrEMBL)
PSMD5 ProteinQ16401 (Uniprot-TrEMBL)
PSMD6 ProteinQ15008 (Uniprot-TrEMBL)
PSMD7 ProteinP51665 (Uniprot-TrEMBL)
PSMD8 ProteinP48556 (Uniprot-TrEMBL)
PSMD9 ProteinO00233 (Uniprot-TrEMBL)
PSME1 ProteinQ06323 (Uniprot-TrEMBL)
PSME2 ProteinQ9UL46 (Uniprot-TrEMBL)
PSME3 ProteinP61289 (Uniprot-TrEMBL)
PSMF1 ProteinQ92530 (Uniprot-TrEMBL)
Palm MetaboliteCHEBI:15756 (ChEBI)
Peroxisome Proliferator Receptor Element (PPRE) R-ALL-422139 (Reactome) Peroxisome proliferator receptor elements bind heterodimers containing a peroxisome proliferator receptor and a retinoic acid receptor. The consensus sequence is TGAMCTTTGNCCTAGWTYYG.
PolyUb-K94,K148-RUNX3ProteinQ13761 (Uniprot-TrEMBL)
PolyUb-RUNX3ProteinQ13761 (Uniprot-TrEMBL)
RBPJ ProteinQ06330 (Uniprot-TrEMBL)
RORC gene ProteinENSG00000143365 (Ensembl)
RORC geneGeneProductENSG00000143365 (Ensembl)
RORC-2ProteinP51449-2 (Uniprot-TrEMBL)
RPS27A(1-76) ProteinP62979 (Uniprot-TrEMBL)
RUNX1 ProteinQ01196 (Uniprot-TrEMBL)
RUNX1 gene ProteinENSG00000159216 (Ensembl)
RUNX1 geneGeneProductENSG00000159216 (Ensembl)
RUNX1 mRNARnaENST00000344691 (Ensembl)
RUNX1:CBFB,(Ac-K94,K171-RUNX3:CBFB:EP300:BRD2):CDKN2A geneComplexR-HSA-8952078 (Reactome)
RUNX1:CBFB,(Ac-K94,K171-RUNX3:CBFB:EP300:BRD2)ComplexR-HSA-8952092 (Reactome)
RUNX3 ProteinQ13761 (Uniprot-TrEMBL)
RUNX3:CBFB:CCND1:HDAC4ComplexR-HSA-8952072 (Reactome)
RUNX3:CBFB:CTNNB1:TCF7L2,(LEF1)ComplexR-HSA-8951514 (Reactome)
RUNX3:CBFB:EP300ComplexR-HSA-8951952 (Reactome)
RUNX3:CBFB:ITGAL gene,(ITGA4 gene)ComplexR-HSA-8949328 (Reactome)
RUNX3:CBFB:RORC geneComplexR-HSA-8949278 (Reactome)
RUNX3:CBFB:RUNX1 geneComplexR-HSA-8951907 (Reactome)
RUNX3:CBFBComplexR-HSA-8865463 (Reactome)
RUNX3:CTNNB1:TCF7L2,(LEF1,TCF7L1,TCF1)ComplexR-HSA-8951432 (Reactome)
RUNX3:JAG1 geneComplexR-HSA-8878200 (Reactome)
RUNX3:NOTCH1 Coactivator ComplexComplexR-HSA-8878230 (Reactome)
RUNX3:NOTCH1

coactivator

complex:HES1 gene
ComplexR-HSA-8878239 (Reactome)
RUNX3:TCF7L2,(LEF1,TCF7L1)ComplexR-HSA-8951528 (Reactome)
RUNX3:TP53 tetramerComplexR-HSA-8952123 (Reactome)
RUNX3:YAP1:TEAD1,TEAD4,(TEAD2,TEAD3)ComplexR-HSA-8951679 (Reactome)
RUNX3:ZFHX3ComplexR-HSA-8878120 (Reactome)
RUNX3:p-2S-SMAD3:p-2S-SMAD3:SMAD4:CDKN1A geneComplexR-HSA-8878180 (Reactome)
RUNX3:p-2S-SMAD3:p-2S-SMAD3:SMAD4:FOXO3:BCL2L11 geneComplexR-HSA-8952225 (Reactome)
RUNX3:p-2S-SMAD3:p-2S-SMAD3:SMAD4ComplexR-HSA-8878146 (Reactome)
RUNX3:p-S166,S188-MDM2 dimerComplexR-HSA-8952373 (Reactome)
RUNX3ProteinQ13761 (Uniprot-TrEMBL)
RXRA ProteinP19793 (Uniprot-TrEMBL)
SHFM1 ProteinP60896 (Uniprot-TrEMBL)
SMAD4 ProteinQ13485 (Uniprot-TrEMBL)
SMARCD3 ProteinQ6STE5 (Uniprot-TrEMBL)
SMURF1 ProteinQ9HCE7 (Uniprot-TrEMBL)
SMURF2 ProteinQ9HAU4 (Uniprot-TrEMBL)
SMURFComplexR-HSA-178205 (Reactome)
SNW1 ProteinQ13573 (Uniprot-TrEMBL)
SPP1 geneGeneProductENSG00000118785 (Ensembl)
SPP1ProteinP10451 (Uniprot-TrEMBL)
Signaling by

TGF-beta Receptor

Complex
PathwayR-HSA-170834 (Reactome) The TGF-beta/BMP pathway incorporates several signaling pathways that share most, but not all, components of a central signal transduction engine. The general signaling scheme is rather simple: upon binding of a ligand, an activated plasma membrane receptor complex is formed, which passes on the signal towards the nucleus through a phosphorylated receptor SMAD (R-SMAD). In the nucleus, the activated R-SMAD promotes transcription in complex with a closely related helper molecule termed Co-SMAD (SMAD4). However, this simple linear pathway expands into a network when various regulatory components and mechanisms are taken into account. The signaling pathway includes a great variety of different TGF-beta/BMP superfamily ligands and receptors, several types of the R-SMADs, and functionally critical negative feedback loops. The R-SMAD:Co-SMAD complex can interact with a great number of transcriptional co-activators/co-repressors to regulate positively or negatively effector genes, so that the interpretation of a signal depends on the cell-type and cross talk with other signaling pathways such as Notch, MAPK and Wnt. The pathway plays a number of different biological roles in the control of embryonic and adult cell proliferation and differentiation, and it is implicated in a great number of human diseases.
TGF beta (TGFB1) is secreted as a homodimer, and as such it binds to TGF beta receptor II (TGFBR2), inducing its dimerization. Binding of TGF beta enables TGFBR2 to form a stable hetero-tetrameric complex with TGF beta receptor I homodimer (TGFBR1). TGFBR2 acts as a serine/threonine kinase and phosphorylates serine and threonine residues within the short GS domain (glycine-serine rich domain) of TGFBR1.
The phosphorylated heterotetrameric TGF beta receptor complex (TGFBR) internalizes into clathrin coated endocytic vesicles where it associates with the endosomal membrane protein SARA. SARA facilitates the recruitment of cytosolic SMAD2 and SMAD3, which act as R-SMADs for TGF beta receptor complex. TGFBR1 phosphorylates recruited SMAD2 and SMAD3, inducing a conformational change that promotes formation of R-SMAD trimers and dissociation of R-SMADs from the TGF beta receptor complex.
In the cytosol, phosphorylated SMAD2 and SMAD3 associate with SMAD4 (known as Co-SMAD), forming a heterotrimer which is more stable than the R-SMAD homotrimers. R-SMAD:Co-SMAD heterotrimer translocates to the nucleus where it directly binds DNA and, in cooperation with other transcription factors, regulates expression of genes involved in cell differentiation, in a context-dependent manner.
The intracellular level of SMAD2 and SMAD3 is regulated by SMURF ubiquitin ligases, which target R-SMADs for degradation. In addition, nuclear R-SMAD:Co-SMAD heterotrimer stimulates transcription of inhibitory SMADs (I-SMADs), forming a negative feedback loop. I-SMADs bind the phosphorylated TGF beta receptor complexes on caveolin coated vesicles, derived from the lipid rafts, and recruit SMURF ubiquitin ligases to TGF beta receptors, leading to ubiquitination and degradation of TGFBR1. Nuclear R-SMAD:Co-SMAD heterotrimers are targets of nuclear ubiquitin ligases which ubiquitinate SMAD2/3 and SMAD4, causing heterotrimer dissociation, translocation of ubiquitinated SMADs to the cytosol and their proteasome-mediated degradation. For a recent review of TGF-beta receptor signaling, please refer to Kang et al. 2009.
Signaling by NOTCH1PathwayR-HSA-1980143 (Reactome) NOTCH1 functions as both a transmembrane receptor presented on the cell surface and as a transcriptional regulator in the nucleus.

NOTCH1 receptor presented on the plasma membrane is activated by a membrane bound ligand expressed in trans on the surface of a neighboring cell. In trans, ligand binding triggers proteolytic cleavage of NOTCH1 and results in release of the NOTCH1 intracellular domain, NICD1, into the cytosol.

NICD1 translocates to the nucleus where it associates with RBPJ (also known as CSL or CBF) and mastermind-like (MAML) proteins (MAML1, MAML2 or MAML3; possibly also MAMLD1) to form NOTCH1 coactivator complex. NOTCH1 coactivator complex activates transcription of genes that possess RBPJ binding sites in their promoters.

TBL1X ProteinO60907 (Uniprot-TrEMBL)
TBL1XR1 ProteinQ9BZK7 (Uniprot-TrEMBL)
TCF7 ProteinP36402 (Uniprot-TrEMBL)
TCF7L1 ProteinQ9HCS4 (Uniprot-TrEMBL)
TCF7L1/TCF7L2/LEF1:CTNNB1:MYC geneComplexR-HSA-4411387 (Reactome)
TCF7L1/TCF7L2/LEF1:CTNNB1ComplexR-HSA-4411378 (Reactome)
TCF7L2 ProteinQ9NQB0 (Uniprot-TrEMBL)
TEAD1 ProteinP28347 (Uniprot-TrEMBL)
TEAD2 ProteinQ15562 (Uniprot-TrEMBL)
TEAD3 ProteinQ99594 (Uniprot-TrEMBL)
TEAD4 ProteinQ15561 (Uniprot-TrEMBL)
TEAD:WWTR1(TAZ)ComplexR-HSA-2032762 (Reactome)
TEADs:YAP1:CTGF geneComplexR-HSA-8951697 (Reactome)
TEADs:YAP1ComplexR-HSA-8869639 (Reactome)
TGFB1 ProteinP01137 (Uniprot-TrEMBL)
TGS1 ProteinQ96RS0 (Uniprot-TrEMBL)
TP53 ProteinP04637 (Uniprot-TrEMBL)
TP53 TetramerComplexR-HSA-3209194 (Reactome)
UBA52(1-76) ProteinP62987 (Uniprot-TrEMBL)
UBB(1-76) ProteinP0CG47 (Uniprot-TrEMBL)
UBB(153-228) ProteinP0CG47 (Uniprot-TrEMBL)
UBB(77-152) ProteinP0CG47 (Uniprot-TrEMBL)
UBC(1-76) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(153-228) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(229-304) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(305-380) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(381-456) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(457-532) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(533-608) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(609-684) ProteinP0CG48 (Uniprot-TrEMBL)
UBC(77-152) ProteinP0CG48 (Uniprot-TrEMBL)
UbComplexR-HSA-113595 (Reactome)
UbComplexR-HSA-6782667 (Reactome)
WWTR1 ProteinQ9GZV5 (Uniprot-TrEMBL)
YAP1 ProteinP46937 (Uniprot-TrEMBL)
YAP1:TEAD1,TEAD4,(TEAD2,TEAD3)ComplexR-HSA-8951678 (Reactome)
ZFHX3 ProteinQ15911 (Uniprot-TrEMBL)
ZFHX3ProteinQ15911 (Uniprot-TrEMBL)
p-2S-SMAD3:p-2S-SMAD3:SMAD4ComplexR-HSA-8878153 (Reactome)
p-S166,S188-MDM2 dimerComplexR-HSA-6804933 (Reactome)
p-S166,S188-MDM2 ProteinQ00987 (Uniprot-TrEMBL)
p-S423,S425-SMAD3 ProteinP84022 (Uniprot-TrEMBL)
p-Y-RUNX3ProteinQ13761 (Uniprot-TrEMBL)
p14-ARF mRNARnaENST00000579755 (Ensembl)
p14-ARFProteinQ8N726 (Uniprot-TrEMBL)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
26S proteasomemim-catalysisR-HSA-8952408 (Reactome)
ADPArrowR-HSA-8937807 (Reactome)
ATPR-HSA-8937807 (Reactome)
Ac-CoAR-HSA-8951966 (Reactome)
Ac-K94,K171-RUNX3:CBFB:BRD2:CCND1:HDAC4ArrowR-HSA-8952062 (Reactome)
Ac-K94,K171-RUNX3:CBFB:BRD2:CCND1:HDAC4R-HSA-8952069 (Reactome)
Ac-K94,K171-RUNX3:CBFB:BRD2:CCND1:HDAC4mim-catalysisR-HSA-8952069 (Reactome)
Ac-K94,K171-RUNX3:CBFB:BRD2:CCND1ArrowR-HSA-8952058 (Reactome)
Ac-K94,K171-RUNX3:CBFB:BRD2:CCND1R-HSA-8952062 (Reactome)
Ac-K94,K171-RUNX3:CBFB:EP300:BRD2ArrowR-HSA-8951977 (Reactome)
Ac-K94,K171-RUNX3:CBFB:EP300:BRD2R-HSA-8952058 (Reactome)
Ac-K94,K171-RUNX3:CBFB:EP300ArrowR-HSA-8951966 (Reactome)
Ac-K94,K171-RUNX3:CBFB:EP300R-HSA-8951977 (Reactome)
BCL2L11 geneR-HSA-8952226 (Reactome)
BCL2L11 geneR-HSA-8952232 (Reactome)
BCL2L11ArrowR-HSA-8952232 (Reactome)
BRD2 homodimerArrowR-HSA-8952069 (Reactome)
BRD2 homodimerR-HSA-8951977 (Reactome)
CBFBR-HSA-8865454 (Reactome)
CCND1 geneR-HSA-8951442 (Reactome)
CCND1 geneR-HSA-8951443 (Reactome)
CCND1ArrowR-HSA-8951443 (Reactome)
CCND1R-HSA-8952058 (Reactome)
CDKN1A geneR-HSA-8878130 (Reactome)
CDKN1A geneR-HSA-8878178 (Reactome)
CDKN1A geneR-HSA-8878186 (Reactome)
CDKN1AArrowR-HSA-8878130 (Reactome)
CDKN1AArrowR-HSA-8878186 (Reactome)
CDKN2A geneR-HSA-8952081 (Reactome)
CDKN2A geneR-HSA-8952101 (Reactome)
CH3COO-ArrowR-HSA-8952069 (Reactome)
CTGF geneR-HSA-1989766 (Reactome)
CTGF geneR-HSA-8951695 (Reactome)
CTGFArrowR-HSA-1989766 (Reactome)
CTNNB1:TCF7L2,(LEF1,TCF7L1,TCF7)R-HSA-8951428 (Reactome)
CTNNB1:TCF7L2,LEF1:CCND1 GeneArrowR-HSA-8951442 (Reactome)
CTNNB1:TCF7L2,LEF1:CCND1 GeneArrowR-HSA-8951443 (Reactome)
CTNNB1:TCF7L2,LEF1R-HSA-8951442 (Reactome)
CoA-SHArrowR-HSA-8951966 (Reactome)
Dimeric TGFB1ArrowR-HSA-8878117 (Reactome)
Dimeric TGFB1ArrowR-HSA-8937814 (Reactome)
Dimeric TGFB1ArrowR-HSA-8951966 (Reactome)
EP300ArrowR-HSA-8952058 (Reactome)
EP300R-HSA-8951951 (Reactome)
EP300TBarR-HSA-8952419 (Reactome)
FOXO3R-HSA-8952226 (Reactome)
H2OR-HSA-8952069 (Reactome)
HDAC4R-HSA-8952062 (Reactome)
HES1 geneR-HSA-1980047 (Reactome)
HES1 geneR-HSA-4396347 (Reactome)
HES1 geneR-HSA-8878237 (Reactome)
HES1 geneR-HSA-8878243 (Reactome)
HES1ArrowR-HSA-1980047 (Reactome)
HES1ArrowR-HSA-8878243 (Reactome)
ITGAL gene,(ITGA4 gene)R-HSA-8949335 (Reactome)
ITGAL gene,(ITGA4 gene)R-HSA-8949343 (Reactome)
ITGAL,(ITGA4)ArrowR-HSA-8949343 (Reactome)
JAG1 geneR-HSA-8878193 (Reactome)
JAG1 geneR-HSA-8878212 (Reactome)
JAG1ArrowR-HSA-8878212 (Reactome)
KRAS:GTPArrowR-HSA-8951977 (Reactome)
MYC geneR-HSA-4411357 (Reactome)
MYC geneR-HSA-4411367 (Reactome)
MYCArrowR-HSA-4411357 (Reactome)
MyrG-p-Y419-SRC:RUNX3ArrowR-HSA-8937792 (Reactome)
MyrG-p-Y419-SRC:RUNX3R-HSA-8937807 (Reactome)
MyrG-p-Y419-SRC:RUNX3mim-catalysisR-HSA-8937807 (Reactome)
MyrG-p-Y419-SRCArrowR-HSA-8937807 (Reactome)
MyrG-p-Y419-SRCR-HSA-8937792 (Reactome)
MyrG-p-Y419-SRCTBarR-HSA-8937814 (Reactome)
NOTCH1 Coactivator Complex:HES1 GeneArrowR-HSA-1980047 (Reactome)
NOTCH1 Coactivator Complex:HES1 GeneArrowR-HSA-4396347 (Reactome)
NOTCH1 Coactivator ComplexR-HSA-4396347 (Reactome)
NOTCH1 Coactivator ComplexR-HSA-8878220 (Reactome)
PPARA:RXRA Coactivator complexArrowR-HSA-1989766 (Reactome)
PolyUb-K94,K148-RUNX3ArrowR-HSA-8952382 (Reactome)
PolyUb-K94,K148-RUNX3ArrowR-HSA-8952399 (Reactome)
PolyUb-K94,K148-RUNX3R-HSA-8952399 (Reactome)
PolyUb-K94,K148-RUNX3R-HSA-8952408 (Reactome)
PolyUb-RUNX3ArrowR-HSA-8952419 (Reactome)
R-HSA-1980047 (Reactome) NOTCH1 coactivator complex binds the promoter of HES1 gene and directly stimulates HES1 transcription. HES1 belongs to the bHLH family of transcription factors (Jarriault et al. 1995).
R-HSA-1989766 (Reactome) The CTGF gene is transcribed to yield mRNA and the mRNA is translated to yield protein. Transcription of the CTGF gene is increased by both YAP1:TEAD and WWTR1(TAZ):TEAD transcriptional coactivator:transcription factor complexes, so that CTGF is one of the many genes whose expression is downregulated by the action of the hippo cascade (Zhang et al. 2009; Zhao et al. 2008).
R-HSA-4396347 (Reactome) NOTCH1 coactivator complex binds the promoter of HES1 gene and directly stimulates HES1 transcription (Jarriault et al. 1995).
R-HSA-4411357 (Reactome) TCF7L1 (also known as TCF3), TCF7L3 (also known as LEF1) and TCF7L2 (also known as TCF4) have been demonstrated to bind to the MYC gene in vivo and in vitro and to mediate beta-catenin dependent transcription (Park et al, 2009; He et al, 1998; Sierra et al, 2006). Aberrant beta-catenin dependent activation of the MYC gene contributes to oncogenic signaling and cellular proliferation in colorectal and other cancers (see for instance Sansom et al, 2007; Moumen et al, 2013; reviewed in Wilkins and Sansom, 2008; Cairo et al, 2012).
Binding of RUNX3 to the CTNNB1:TCF7L2 and possibly to the CTNNB1:LEF1 and TCF7L1 complexes, prevents binding of CTNNB1 complexes to the MYC promoter, thus negatively regulating MYC transcription (Ito et al. 2008).
R-HSA-4411367 (Reactome) TCF7L1 (also known as TCF3), TCF7L3 (also known as LEF1) and TCF7L2 (also known as TCF4) have been demonstrated to bind to the MYC gene in vivo and in vitro and to mediate beta-catenin dependent transcription (Park et al, 2009; He et al, 1998; Sierra et al, 2006). Aberrant beta-catenin dependent activation of the MYC gene contributes to oncogenic signaling and cellular proliferation in colorectal and other cancers (see for instance Sansom et al, 2007; Moumen et al, 2013; reviewed in Wilkins and Sansom, 2008; Cairo et al, 2012).
Binding of RUNX3 to the CTNNB1:TCF7L2 and possibly to the CTNNB1:LEF1 and TCF7L1 complexes, prevents binding of CTNNB1 complexes to the MYC promoter, thus negatively regulating MYC transcription (Ito et al. 2008).
R-HSA-8865454 (Reactome) CBFB binds the transcription factor RUNX3, interacting with its Runt domain, which is highly similar to Runt domains of RUNX1 and RUNX2 (Kim et al. 2013). RUNX3 is implicated in neurogenesis, thymopoiesis and stomach development (Inoue et al. 2002, Levanon et al. 2002, Levanon et al. 2003). RUNX3 and CBFB are frequently downregulated in gastric cancer (Sakakura et al. 2005).
R-HSA-8878117 (Reactome) In response to TGF-beta (TGFB1) signaling, RUNX3 binds to the homeobox transcription factor and tumor suppressor ZFHX3 (ATBF1). The exact mechanism and regulation of RUNX3 and ATBF1 binding is not known (Mabuchi et al. 2010).
R-HSA-8878130 (Reactome) Transcription of the CDKN1A (p21) gene is synergistically stimulated by RUNX3 and ZFHX3 (ATBF1), presumably through formation of the complex between RUNX3 and ZFHX3. RUNX3 and ZFHX3 can also stimulate CDKN1A transcription independently of one another, albeit to a lower level than when they act in tandem (Mabuchi et al. 2010).
R-HSA-8878143 (Reactome) RUNX3 binds the complex of SMAD3 and SMAD4, formed in response to TGF-beta (TGFB1) signaling (Hanai et al. 1999, Chi et al. 2005).
R-HSA-8878178 (Reactome) The CDKN1A (p21) gene promoter contains five putative RUNX3 binding sites. RUNX3 binds the CDKN1A promoter. The complex of SMAD4 and activated SMAD3, a known CDKN1A transcriptional activator, can bind to RUNX3 to cooperatively activate the CDKN1A gene transcription (Chi et al. 2005).
R-HSA-8878186 (Reactome) RUNX3 binds the complex of SMAD4 and SMAD3, generated in response to TGF-beta (TGFB1) signaling. While the individual action of the SMAD3:SMAD4 complex or RUNX3 can induce 2-3-fold activation of CDKN1A transcription, the synergistic action of SMAD3, SMAD4 and RUNX3 induces 10-fold activation of CDKN1A transcription. Runx3 knockout mice exhibit decreased sensitivity to TGF-beta and develop gastric epithelial hyperplasia (Chi et al. 2005).
R-HSA-8878193 (Reactome) RUNX3 binds the promoter of the JAG1 gene, which encodes a ligand for NOTCH receptors (Nishina et al. 2011).
R-HSA-8878212 (Reactome) Binding of RUNX3 to the JAG1 gene promoter inhibits transcription of JAG1, which correlates with reduced amount of cleaved JAG1 receptor, NOTCH1. There is an inverse correlation between the expression levels of RUNX3 and JAG1 in hepatocellular carcinoma (HCC) cell lines and tumor samples. HCC cell lines with higher RUNX3 levels have reduced tumorigenic capacity (Nishina et al. 2011).
R-HSA-8878220 (Reactome) RUNX3 binds the NOTCH1 coactivator complex by directly interacting with the NOTCH1 intracellular domain fragment (NICD1) (Gao et al. 2010).
R-HSA-8878237 (Reactome) RUNX3, associated with the NOTCH1 coactivator complex, binds to the promoter of the HES1 gene (Gao et al. 2010).
R-HSA-8878243 (Reactome) Binding of RUNX3 to the NOTCH1 coactivator complex at the HES1 gene promoter results in repression of HES1 transcription downstream of NOTCH1 signaling (Gao et al. 2010).
R-HSA-8937792 (Reactome) Activated SRC binds to RUNX3 in the cytosol. The interaction involves the Runt domain of RUNX3 (Goh et al. 2010).
R-HSA-8937807 (Reactome) Activated SRC phosphorylates RUNX3 in the cytosol, on multiple tyrosine residues. There are eleven tyrosine residues in RUNX3, but SRC target sites have not been determined. SRC-mediated phosphorylation of RUNX3 inhibits translocation of RUNX3 to the nucleus and is the underlying cause of cytosolic localization of RUNX3 in gastric and breast cancer (Goh et al. 2010).
R-HSA-8937814 (Reactome) Translocation of RUNX3 from the cytosol to the nucleus is stimulated by TGF-beta (TGFB1) treatment (Ito et al. 2005) and inhibited by SRC-mediated phosphorylation of RUNX3 on multiple tyrosine residues (Goh et al. 2010).
R-HSA-8949276 (Reactome) Based on studies in mice, the complex of RUNX3 and CBFB binds the promoter of the RORC (RORgamma) gene, encoding nuclear retinoid-related orphan receptor-gamma. The RUNX binding site TGTGGT is conserved between mouse and human RORC promoters. Mouse Runx3 is expressed in innate lymphoid cell lineages ILC1 and ILC3, but not ILC2 (Ebihara et al. 2015).
R-HSA-8949301 (Reactome) Based on mouse studies, binding of the RUNX3:CBFB heterodimer to the RUNX binding motif TGTGGT conserved between the mouse and human promoters of the RORC (RORgamma) gene, stimulates transcription of the RORC transcript variant 2 (RORC-2), also known as RORgT (RORgamma-t). In the ILC3 lineage of innate lymphoid cells in mice, expression of the Ahr transcription factor is positively indirectly regulated by Runx3, most likely through RORgT (Ebihara et al. 2015).
R-HSA-8949335 (Reactome) RUNX3, presumably in complex with CBFB, binds the RUNX response element in the promoter of the ITGAL (CD11a) gene, encoding leukocyte integrin involved in transendothelial migration of leukocytes during immune and inflammatory responses as well as co-stimulation of T cells (Puig-Kroger et al. 2003, Dominguez-Soto et al. 2005). RUNX3, as well as RUNX1, may also be involved in regulation of integrin alpha 4 (ITGA4, also known as CD49d) expression. A RUNX binding site exists in the ITGA4 promoter, but the direct binding of RUNX transcription factors has not been demonstrated (Domniguez-Soto et al. 2005).
R-HSA-8949343 (Reactome) Transcription of the ITGAL (CD11a) gene, is stimulated by binding of RUNX3, presumably in complex with CBFB, to the ITGAL promoter. ITGAL is a leukocyte integrin involved in transendothelial migration of leukocytes during immune and inflammatory responses as well as co-stimulation of T cells. RUNX3, as well as RUNX1, positively regulate integrin alpha 4 (ITGA4, also known as CD49d) expression. A RUNX binding site exists in the ITGA4 promoter, but the direct regulation by RUNX transcription factors has not been demonstrated (Domniguez-Soto et al. 2005).
R-HSA-8951428 (Reactome) RUNX3 forms a ternary complex with beta-catenin (CTNNB1) and its binding partner TCF7L2 (TCF4). In addition to TCF7L2, RUNX3 is also able to interact with LEF1, TCF7L1 (TCF3) and TCF7 (also known as TCF1). The interaction involves the Runt domain of RUNX3 and the HMG box of TCF7L2 (Ito et al. 2008).
R-HSA-8951442 (Reactome) Beta-catenin (CTNNB1), in complex with TCF7L2 (TCF4) or LEF1, binds to TCF/LEF binding sites in the promoter of the cyclin D1 (CCND1) gene (Tetsu and McCormick 1999, Shtutman et al. 1999). Binding of RUNX3 to the CTNNB1:TCF7L2 and possibly to the CTNNB1:LEF1 complex, prevents binding of CTNNB1 complexes to the CCND1 promoter, thus negatively regulating CCND1 transcription (Ito et al. 2008).
R-HSA-8951443 (Reactome) Binding of the complex of beta-catenin (CTNNB1) and TCF7L2 (TCF4) or LEF1 transcription factors to TCF/LEF binding sites in the promoter of the cyclin D1 (CCND1) gene stimulates CCND1 transcription (Tetsu and McCormick 1999, Shtutman et al. 1999).
R-HSA-8951676 (Reactome) RUNX3 interacts with both YAP1 and TEAD proteins. The interaction with YAP1 involves the PY motif of RUNX3 and the WW domain of YAP1. The interaction with TEADs involves the Runt domain of RUNX3 and the DNA recognition helix of TEADs. RUNX3 was shown to directly interact with TEAD1 and TEAD4. Based on sequence similarity, it is highly probable that RUNX3 also interacts with TEAD2 and TEAD3. The interaction of RUNX3 with YAP1 and/or TEADs does not prevent formation of the YAP1:TEADs complex (Yagi et al. 1999, Qiao et al. 2015).
R-HSA-8951695 (Reactome) The complex of YAP1 and one TEAD proteins (TEAD1, TEAD2, TEAD3 or TEAD4) binds to TEAD-binding sites in the promoter of the CTGF gene (Zhao et al. 2008). Association of RUNX3 with the TEADs:YAP1 complex inhibits loading of the TEADs:YAP1 to the CTGF promoter (Qiao et al. 2016).
R-HSA-8951910 (Reactome) RUNX3, presumably associated with CBFB, binds Runx response elements in the distal (P1) promoter of the RUNX1 gene (Spender et al. 2005). All RUNX family members contain Runx response elements in their promoters (Levanon and Groner 2004).
R-HSA-8951926 (Reactome) Transcription of the RUNX1 gene is repressed by binding of RUNX3 to Runx response elements in the distal (P1) promoter of RUNX1. Expression of RUNX3 is therefore mutually exclusive with expression of RUNX1 in human B cells (Spender et al. 2005).
R-HSA-8951951 (Reactome) The histone acetyltransferase EP300 (p300) forms a complex with RUNX3, presumably bound to CBFB (Jin et al. 2004, Lee et al. 2013). EP300 can also form a complex with other RUNX family members, RUNX1 and RUNX2 (Jin et al. 2004).
R-HSA-8951966 (Reactome) EP300 (p300) histone acetyltransferase acetylates RUNX3 on lysine residues K94 and K171 (Lee et al. 2013), and probably other lysines (Jin et al. 2004). EP300-mediated acetylation of RUNX3 is positively regulated by TGF-beta treatment. Besides increasing the transcriptional activity of RUNX3, EP300-mediated acetylation also increases the half-life of RUNX3, as it interferes with SMURF-mediated ubiquitination and subsequent degradation of RUNX3 (Jin et al. 2004).
R-HSA-8951977 (Reactome) RUNX3 acetylated on lysine residues K94 and K171 binds to BRD2 (bromodomain-containing protein 2). Formation of the RUNX3 complex with BRD2 is stimulated by activated KRAS (Lee et al. 2013).
R-HSA-8952058 (Reactome) CCND1 (cyclin D1) can bind to RUNX3 and displace EP300 (p300) histone acetyltransferase (Lee et al. 2013).
R-HSA-8952062 (Reactome) CCND1 (cyclin D1) recruits histone deacetylase HDAC4 to acetylated RUNX3 (Lee et al. 2013).
R-HSA-8952069 (Reactome) Histone deacetylase HDAC4, recruited to RUNX3 by CCND1 (cyclin D1), deacetylates RUNX3, leading to BRD2 dissociation (Lee et al. 2013).
R-HSA-8952081 (Reactome) The CDKN2A gene promoter that regulates transcription of p14-ARF contains Runx response elements that are known to be recognized by the RUNX1:CBFB complex (Linggi et al. 2002). Based on sequence similarity between RUNX1 and RUNX3 and the fact that the complex of acetylated RUNX3 and BRD2 positively regulate p14-ARF transcription, it is possible that RUNX3 can also bind to the Runx response elements at the p14-ARF promoter (Lee et al. 2013).
R-HSA-8952101 (Reactome) Binding of the RUNX1:CBFB complex to the p14-ARF promoter at the CDKN2A locus promotes p14-ARF transcription (Linggi et al. 2002). The complex of acetylated RUNX3 and BRD2 positively regulates p14-ARF transcription, leading to activation of TP53 (p53) in response to oncogenic KRAS signaling. It is possible that RUNX3 directly binds to Runx response elements in the p14-ARF promoter that are recognized by RUNX1, although the direct association of RUNX3 with the CDKN2A gene has not been examined (Lee et al. 2013).
R-HSA-8952128 (Reactome) RUNX3 can bind to TP53 (p53). The interaction involves the C-termini of both RUNX3 and TP53. RUNX3 may act as a TP53 co-factor, stimulating TP53-mediated transcription of target genes, including CDKN1A (p21). RUNX3 may also interact with phosphorylated ATM kinase in response to DNA damage and facilitate ATM-mediated phosphorylation and stabilization of TP53 (Yamada et al. 2010).
R-HSA-8952226 (Reactome) In response to TGF-beta treatment, RUNX3 binds to Runx response elements in the promoter of the BCL2L11 (BIM) gene. The BCL2L11 promoter contains three Runx response elements, one SMAD-binding site, and a binding site for FOXO3 (FOXO3A). The SMAD binding site is needed for RUNX3-mediated upregulation of BCL2L11 transcription and was shown to bind SMAD3 (Wildey et al. 2003). FOXO3 can bind to the BCL2L11 promoter synergistically with RUNX3 and contribute to BCL2L11 stimulation (Yamamura et al. 2006).
R-HSA-8952232 (Reactome) In response to TGF-beta treatment, transcription factors RUNX3 (presumably in complex with CBFB), SMAD3 (presumably in complex with SMAD4) and FOXO3 (FOXO3A) bind to their corresponding response elements in the promoter of the pro-apoptotic BCL2L11 (BIM) gene, synergistically stimulating BCL2L11 transcription (Wildey et al. 2003, Yano et al. 2006, Yamamura et al. 2006).
R-HSA-8952371 (Reactome) MDM2 and RUNX3 form a complex in the nucleus. Association of RUNX3 with CBFB does not interfere with binding of MDM2 to RUNX3. The interaction involves the acidic domain of MDM2 and the Runt domain of RUNX3 (Chi et al. 2009).
R-HSA-8952382 (Reactome) MDM2 polyubiquitinates RUNX3 on lysine residues K94 and K148. MDM-mediated ubiquitination of RUNX3 is inhibited by p14-ARF (Chi et al. 2009).
R-HSA-8952399 (Reactome) Polyubiquitination of RUNX3 by MDM2 promotes translocation of RUNX3 from the nucleus to the cytosol (Chi et al. 2009).
R-HSA-8952408 (Reactome) Polyubiquitinated RUNX3 is degraded by the proteasome (Chi et al. 2009).
R-HSA-8952419 (Reactome) SMURF1 and SMURF2 polyubiquitinate RUNX3 on unknown lysine residues, possibly K148, K186 and K192, targeting it for degradation. The interaction between SMURFs and RUNX3 involves the PY motif of RUNX3 and the WW domain of SMURFs. Acetylation of RUNX3 by EP300 (p300) prevents SMURF-mediated ubiquitination of RUNX3, thus increasing RUNX3 protein stability (Jin et al. 2004).
R-HSA-8952442 (Reactome) Both human and mouse SPP1 (osteopontin) gene promoters contain Runx and SMAD response elements. Transcription of SPP1 increases in response to increased RUNX3 levels, which contributes to invasiveness of pancreatic cancer cells. Direct binding of RUNX3 to the SPP1 promoter has not been examined (Whittle et al. 2015).
RORC geneR-HSA-8949276 (Reactome)
RORC geneR-HSA-8949301 (Reactome)
RORC-2ArrowR-HSA-8949301 (Reactome)
RUNX1 geneR-HSA-8951910 (Reactome)
RUNX1 geneR-HSA-8951926 (Reactome)
RUNX1 mRNAArrowR-HSA-8951926 (Reactome)
RUNX1:CBFB,(Ac-K94,K171-RUNX3:CBFB:EP300:BRD2):CDKN2A geneArrowR-HSA-8952081 (Reactome)
RUNX1:CBFB,(Ac-K94,K171-RUNX3:CBFB:EP300:BRD2):CDKN2A geneArrowR-HSA-8952101 (Reactome)
RUNX1:CBFB,(Ac-K94,K171-RUNX3:CBFB:EP300:BRD2)R-HSA-8952081 (Reactome)
RUNX3:CBFB:CCND1:HDAC4ArrowR-HSA-8952069 (Reactome)
RUNX3:CBFB:CTNNB1:TCF7L2,(LEF1)TBarR-HSA-8951442 (Reactome)
RUNX3:CBFB:EP300ArrowR-HSA-8951951 (Reactome)
RUNX3:CBFB:EP300R-HSA-8951966 (Reactome)
RUNX3:CBFB:EP300mim-catalysisR-HSA-8951966 (Reactome)
RUNX3:CBFB:ITGAL gene,(ITGA4 gene)ArrowR-HSA-8949335 (Reactome)
RUNX3:CBFB:ITGAL gene,(ITGA4 gene)ArrowR-HSA-8949343 (Reactome)
RUNX3:CBFB:RORC geneArrowR-HSA-8949276 (Reactome)
RUNX3:CBFB:RORC geneArrowR-HSA-8949301 (Reactome)
RUNX3:CBFB:RUNX1 geneArrowR-HSA-8951910 (Reactome)
RUNX3:CBFB:RUNX1 geneTBarR-HSA-8951926 (Reactome)
RUNX3:CBFBArrowR-HSA-8865454 (Reactome)
RUNX3:CBFBArrowR-HSA-8952442 (Reactome)
RUNX3:CBFBR-HSA-8949276 (Reactome)
RUNX3:CBFBR-HSA-8949335 (Reactome)
RUNX3:CBFBR-HSA-8951910 (Reactome)
RUNX3:CBFBR-HSA-8951951 (Reactome)
RUNX3:CTNNB1:TCF7L2,(LEF1,TCF7L1,TCF1)ArrowR-HSA-8951428 (Reactome)
RUNX3:JAG1 geneArrowR-HSA-8878193 (Reactome)
RUNX3:JAG1 geneTBarR-HSA-8878212 (Reactome)
RUNX3:NOTCH1 Coactivator ComplexArrowR-HSA-8878220 (Reactome)
RUNX3:NOTCH1 Coactivator ComplexR-HSA-8878237 (Reactome)
RUNX3:NOTCH1

coactivator

complex:HES1 gene
ArrowR-HSA-8878237 (Reactome)
RUNX3:NOTCH1

coactivator

complex:HES1 gene
TBarR-HSA-8878243 (Reactome)
RUNX3:TCF7L2,(LEF1,TCF7L1)TBarR-HSA-4411367 (Reactome)
RUNX3:TP53 tetramerArrowR-HSA-8952128 (Reactome)
RUNX3:YAP1:TEAD1,TEAD4,(TEAD2,TEAD3)ArrowR-HSA-8951676 (Reactome)
RUNX3:YAP1:TEAD1,TEAD4,(TEAD2,TEAD3)TBarR-HSA-8951695 (Reactome)
RUNX3:ZFHX3ArrowR-HSA-8878117 (Reactome)
RUNX3:ZFHX3ArrowR-HSA-8878130 (Reactome)
RUNX3:p-2S-SMAD3:p-2S-SMAD3:SMAD4:CDKN1A geneArrowR-HSA-8878178 (Reactome)
RUNX3:p-2S-SMAD3:p-2S-SMAD3:SMAD4:CDKN1A geneArrowR-HSA-8878186 (Reactome)
RUNX3:p-2S-SMAD3:p-2S-SMAD3:SMAD4:FOXO3:BCL2L11 geneArrowR-HSA-8952226 (Reactome)
RUNX3:p-2S-SMAD3:p-2S-SMAD3:SMAD4:FOXO3:BCL2L11 geneArrowR-HSA-8952232 (Reactome)
RUNX3:p-2S-SMAD3:p-2S-SMAD3:SMAD4ArrowR-HSA-8878143 (Reactome)
RUNX3:p-2S-SMAD3:p-2S-SMAD3:SMAD4R-HSA-8878178 (Reactome)
RUNX3:p-2S-SMAD3:p-2S-SMAD3:SMAD4R-HSA-8952226 (Reactome)
RUNX3:p-S166,S188-MDM2 dimerArrowR-HSA-8952371 (Reactome)
RUNX3:p-S166,S188-MDM2 dimerR-HSA-8952382 (Reactome)
RUNX3:p-S166,S188-MDM2 dimermim-catalysisR-HSA-8952382 (Reactome)
RUNX3ArrowR-HSA-8937814 (Reactome)
RUNX3R-HSA-8865454 (Reactome)
RUNX3R-HSA-8878117 (Reactome)
RUNX3R-HSA-8878143 (Reactome)
RUNX3R-HSA-8878193 (Reactome)
RUNX3R-HSA-8878220 (Reactome)
RUNX3R-HSA-8937792 (Reactome)
RUNX3R-HSA-8937814 (Reactome)
RUNX3R-HSA-8951428 (Reactome)
RUNX3R-HSA-8951676 (Reactome)
RUNX3R-HSA-8952128 (Reactome)
RUNX3R-HSA-8952371 (Reactome)
RUNX3R-HSA-8952419 (Reactome)
SMURFmim-catalysisR-HSA-8952419 (Reactome)
SPP1 geneR-HSA-8952442 (Reactome)
SPP1ArrowR-HSA-8952442 (Reactome)
TCF7L1/TCF7L2/LEF1:CTNNB1:MYC geneArrowR-HSA-4411357 (Reactome)
TCF7L1/TCF7L2/LEF1:CTNNB1:MYC geneArrowR-HSA-4411367 (Reactome)
TCF7L1/TCF7L2/LEF1:CTNNB1R-HSA-4411367 (Reactome)
TEAD:WWTR1(TAZ)ArrowR-HSA-1989766 (Reactome)
TEADs:YAP1:CTGF geneArrowR-HSA-8951695 (Reactome)
TEADs:YAP1ArrowR-HSA-1989766 (Reactome)
TEADs:YAP1R-HSA-8951695 (Reactome)
TP53 TetramerR-HSA-8952128 (Reactome)
UbArrowR-HSA-8952408 (Reactome)
UbR-HSA-8952382 (Reactome)
UbR-HSA-8952419 (Reactome)
YAP1:TEAD1,TEAD4,(TEAD2,TEAD3)R-HSA-8951676 (Reactome)
ZFHX3R-HSA-8878117 (Reactome)
p-2S-SMAD3:p-2S-SMAD3:SMAD4R-HSA-8878143 (Reactome)
p-S166,S188-MDM2 dimerArrowR-HSA-8952382 (Reactome)
p-S166,S188-MDM2 dimerR-HSA-8952371 (Reactome)
p-Y-RUNX3ArrowR-HSA-8937807 (Reactome)
p14-ARF mRNAArrowR-HSA-8952101 (Reactome)
p14-ARFTBarR-HSA-8952382 (Reactome)
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