{
"bcoid": "GLY_000320",
"title": "Human Protein Reactions (Reactome)",
"description": "The Human Protein Reactions (Reactome) dataset contains reactions information for pathways for human ...",
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Expression of EGR genes depends on binding of phosphorylated ternary complex factor (TCF) protein ELK1 and its transcriptional coactivator SRF (serum response factor) to their cognate DNA binding sequences in the promoters (Hooker et al, 2017; De Franco et al, 1993; Harada et al, 2001; reviewed in Herdegen and Leah, 1998). NGF-stimulated expression of EGR1 and 2 occurs downstream of sustained MAPK signaling (Millbrandt et al, 1987; Sukhatme et al, 1988; de Franco et al, 1998; Mullenbrock et al, 2011; Crosby et al, 1991; L\u00f6nn et al, 2005). In addition to SRF and TCF binding sites, the EGR1 promoter also contain consensus binding sequences for AP-1 and CREB, as well as binding sites for EGR1 protein itself (Schwachtgen et al, 2000; Thiel et al, 2000; Svaren et al, 1996; reviewed in Page; and Deindl, 2001). Expression of EGR1 is limited by a negative feedback loop mediated by the binding of a complex of EGR1 with a repressor protein of the NAB family (NGF1A binding protein) to the EGR1 binding site (Cao et al, 1990; Thiel et al, 2000; Svaren et al, 1996)."
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Expression of EGR genes depends on binding of phosphorylated ternary complex factor (TCF) protein ELK1 and its transcriptional coactivator SRF (serum response factor) to their cognate DNA binding sequences in the promoters (Hooker et al, 2017; De Franco et al, 1993; Harada et al, 2001; reviewed in Herdegen and Leah, 1998). NGF-stimulated expression of EGR1 and 2 occurs downstream of sustained MAPK signaling (Millbrandt et al, 1987; Sukhatme et al, 1988; de Franco et al, 1998; Mullenbrock et al, 2011; Crosby et al, 1991; L\u00f6nn et al, 2005). In addition to SRF and TCF binding sites, the EGR1 promoter also contain consensus binding sequences for AP-1 and CREB, as well as binding sites for EGR1 protein itself (Schwachtgen et al, 2000; Thiel et al, 2000; Svaren et al, 1996; reviewed in Page; and Deindl, 2001). Expression of EGR1 is limited by a negative feedback loop mediated by the binding of a complex of EGR1 with a repressor protein of the NAB family (NGF1A binding protein) to the EGR1 binding site (Cao et al, 1990; Thiel et al, 2000; Svaren et al, 1996)."
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Expression of EGR genes depends on binding of phosphorylated ternary complex factor (TCF) protein ELK1 and its transcriptional coactivator SRF (serum response factor) to their cognate DNA binding sequences in the promoters (Hooker et al, 2017; De Franco et al, 1993; Harada et al, 2001; reviewed in Herdegen and Leah, 1998). NGF-stimulated expression of EGR1 and 2 occurs downstream of sustained MAPK signaling (Millbrandt et al, 1987; Sukhatme et al, 1988; de Franco et al, 1998; Mullenbrock et al, 2011; Crosby et al, 1991; L\u00f6nn et al, 2005). In addition to SRF and TCF binding sites, the EGR1 promoter also contain consensus binding sequences for AP-1 and CREB, as well as binding sites for EGR1 protein itself (Schwachtgen et al, 2000; Thiel et al, 2000; Svaren et al, 1996; reviewed in Page; and Deindl, 2001). Expression of EGR1 is limited by a negative feedback loop mediated by the binding of a complex of EGR1 with a repressor protein of the NAB family (NGF1A binding protein) to the EGR1 binding site (Cao et al, 1990; Thiel et al, 2000; Svaren et al, 1996)."
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Expression of EGR genes depends on binding of phosphorylated ternary complex factor (TCF) protein ELK1 and its transcriptional coactivator SRF (serum response factor) to their cognate DNA binding sequences in the promoters (Hooker et al, 2017; De Franco et al, 1993; Harada et al, 2001; reviewed in Herdegen and Leah, 1998). NGF-stimulated expression of EGR1 and 2 occurs downstream of sustained MAPK signaling (Millbrandt et al, 1987; Sukhatme et al, 1988; de Franco et al, 1998; Mullenbrock et al, 2011; Crosby et al, 1991; L\u00f6nn et al, 2005). In addition to SRF and TCF binding sites, the EGR1 promoter also contain consensus binding sequences for AP-1 and CREB, as well as binding sites for EGR1 protein itself (Schwachtgen et al, 2000; Thiel et al, 2000; Svaren et al, 1996; reviewed in Page; and Deindl, 2001). Expression of EGR1 is limited by a negative feedback loop mediated by the binding of a complex of EGR1 with a repressor protein of the NAB family (NGF1A binding protein) to the EGR1 binding site (Cao et al, 1990; Thiel et al, 2000; Svaren et al, 1996)."
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Expression of EGR genes depends on binding of phosphorylated ternary complex factor (TCF) protein ELK1 and its transcriptional coactivator SRF (serum response factor) to their cognate DNA binding sequences in the promoters (Hooker et al, 2017; De Franco et al, 1993; Harada et al, 2001; reviewed in Herdegen and Leah, 1998). NGF-stimulated expression of EGR1 and 2 occurs downstream of sustained MAPK signaling (Millbrandt et al, 1987; Sukhatme et al, 1988; de Franco et al, 1998; Mullenbrock et al, 2011; Crosby et al, 1991; L\u00f6nn et al, 2005). In addition to SRF and TCF binding sites, the EGR1 promoter also contain consensus binding sequences for AP-1 and CREB, as well as binding sites for EGR1 protein itself (Schwachtgen et al, 2000; Thiel et al, 2000; Svaren et al, 1996; reviewed in Page; and Deindl, 2001). Expression of EGR1 is limited by a negative feedback loop mediated by the binding of a complex of EGR1 with a repressor protein of the NAB family (NGF1A binding protein) to the EGR1 binding site (Cao et al, 1990; Thiel et al, 2000; Svaren et al, 1996)."
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Expression of EGR genes depends on binding of phosphorylated ternary complex factor (TCF) protein ELK1 and its transcriptional coactivator SRF (serum response factor) to their cognate DNA binding sequences in the promoters (Hooker et al, 2017; De Franco et al, 1993; Harada et al, 2001; reviewed in Herdegen and Leah, 1998). NGF-stimulated expression of EGR1 and 2 occurs downstream of sustained MAPK signaling (Millbrandt et al, 1987; Sukhatme et al, 1988; de Franco et al, 1998; Mullenbrock et al, 2011; Crosby et al, 1991; L\u00f6nn et al, 2005). In addition to SRF and TCF binding sites, the EGR1 promoter also contain consensus binding sequences for AP-1 and CREB, as well as binding sites for EGR1 protein itself (Schwachtgen et al, 2000; Thiel et al, 2000; Svaren et al, 1996; reviewed in Page; and Deindl, 2001). Expression of EGR1 is limited by a negative feedback loop mediated by the binding of a complex of EGR1 with a repressor protein of the NAB family (NGF1A binding protein) to the EGR1 binding site (Cao et al, 1990; Thiel et al, 2000; Svaren et al, 1996)."
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Expression of EGR genes depends on binding of phosphorylated ternary complex factor (TCF) protein ELK1 and its transcriptional coactivator SRF (serum response factor) to their cognate DNA binding sequences in the promoters (Hooker et al, 2017; De Franco et al, 1993; Harada et al, 2001; reviewed in Herdegen and Leah, 1998). NGF-stimulated expression of EGR1 and 2 occurs downstream of sustained MAPK signaling (Millbrandt et al, 1987; Sukhatme et al, 1988; de Franco et al, 1998; Mullenbrock et al, 2011; Crosby et al, 1991; L\u00f6nn et al, 2005). In addition to SRF and TCF binding sites, the EGR1 promoter also contain consensus binding sequences for AP-1 and CREB, as well as binding sites for EGR1 protein itself (Schwachtgen et al, 2000; Thiel et al, 2000; Svaren et al, 1996; reviewed in Page; and Deindl, 2001). Expression of EGR1 is limited by a negative feedback loop mediated by the binding of a complex of EGR1 with a repressor protein of the NAB family (NGF1A binding protein) to the EGR1 binding site (Cao et al, 1990; Thiel et al, 2000; Svaren et al, 1996)."
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Expression of EGR genes depends on binding of phosphorylated ternary complex factor (TCF) protein ELK1 and its transcriptional coactivator SRF (serum response factor) to their cognate DNA binding sequences in the promoters (Hooker et al, 2017; De Franco et al, 1993; Harada et al, 2001; reviewed in Herdegen and Leah, 1998). NGF-stimulated expression of EGR1 and 2 occurs downstream of sustained MAPK signaling (Millbrandt et al, 1987; Sukhatme et al, 1988; de Franco et al, 1998; Mullenbrock et al, 2011; Crosby et al, 1991; L\u00f6nn et al, 2005). In addition to SRF and TCF binding sites, the EGR1 promoter also contain consensus binding sequences for AP-1 and CREB, as well as binding sites for EGR1 protein itself (Schwachtgen et al, 2000; Thiel et al, 2000; Svaren et al, 1996; reviewed in Page; and Deindl, 2001). Expression of EGR1 is limited by a negative feedback loop mediated by the binding of a complex of EGR1 with a repressor protein of the NAB family (NGF1A binding protein) to the EGR1 binding site (Cao et al, 1990; Thiel et al, 2000; Svaren et al, 1996)."
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Expression of EGR genes depends on binding of phosphorylated ternary complex factor (TCF) protein ELK1 and its transcriptional coactivator SRF (serum response factor) to their cognate DNA binding sequences in the promoters (Hooker et al, 2017; De Franco et al, 1993; Harada et al, 2001; reviewed in Herdegen and Leah, 1998). NGF-stimulated expression of EGR1 and 2 occurs downstream of sustained MAPK signaling (Millbrandt et al, 1987; Sukhatme et al, 1988; de Franco et al, 1998; Mullenbrock et al, 2011; Crosby et al, 1991; L\u00f6nn et al, 2005). In addition to SRF and TCF binding sites, the EGR1 promoter also contain consensus binding sequences for AP-1 and CREB, as well as binding sites for EGR1 protein itself (Schwachtgen et al, 2000; Thiel et al, 2000; Svaren et al, 1996; reviewed in Page; and Deindl, 2001). Expression of EGR1 is limited by a negative feedback loop mediated by the binding of a complex of EGR1 with a repressor protein of the NAB family (NGF1A binding protein) to the EGR1 binding site (Cao et al, 1990; Thiel et al, 2000; Svaren et al, 1996)."
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Expression of EGR genes depends on binding of phosphorylated ternary complex factor (TCF) protein ELK1 and its transcriptional coactivator SRF (serum response factor) to their cognate DNA binding sequences in the promoters (Hooker et al, 2017; De Franco et al, 1993; Harada et al, 2001; reviewed in Herdegen and Leah, 1998). NGF-stimulated expression of EGR1 and 2 occurs downstream of sustained MAPK signaling (Millbrandt et al, 1987; Sukhatme et al, 1988; de Franco et al, 1998; Mullenbrock et al, 2011; Crosby et al, 1991; L\u00f6nn et al, 2005). In addition to SRF and TCF binding sites, the EGR1 promoter also contain consensus binding sequences for AP-1 and CREB, as well as binding sites for EGR1 protein itself (Schwachtgen et al, 2000; Thiel et al, 2000; Svaren et al, 1996; reviewed in Page; and Deindl, 2001). Expression of EGR1 is limited by a negative feedback loop mediated by the binding of a complex of EGR1 with a repressor protein of the NAB family (NGF1A binding protein) to the EGR1 binding site (Cao et al, 1990; Thiel et al, 2000; Svaren et al, 1996)."
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"The Early Growth Response (EGR) gene family includes EGR1-4 and WT1. These Cys2-His2 zinc finger transcription factors are immediate early genes (IEG) that are rapidly turned on downstream of a number of stimuli and regulate expression of genes involved in stress response and differentiation (reviewed in Pagel and Deindl, 2001; Bahrami and Drabl\u00f8s, 2016). Roles for EGR proteins are well established in the nervous system, with EGR target genes contributing to synaptic plasticity, long-term potentiation, peripheral nerve myelination and NGF-induced neurite outgrowth (reviewed in Perez-Cadahia et al, 2011; Herdegen and Leah, 1998; O'Donovan et al, 1999).
Expression of EGR genes depends on binding of phosphorylated ternary complex factor (TCF) protein ELK1 and its transcriptional coactivator SRF (serum response factor) to their cognate DNA binding sequences in the promoters (Hooker et al, 2017; De Franco et al, 1993; Harada et al, 2001; reviewed in Herdegen and Leah, 1998). NGF-stimulated expression of EGR1 and 2 occurs downstream of sustained MAPK signaling (Millbrandt et al, 1987; Sukhatme et al, 1988; de Franco et al, 1998; Mullenbrock et al, 2011; Crosby et al, 1991; L\u00f6nn et al, 2005). In addition to SRF and TCF binding sites, the EGR1 promoter also contain consensus binding sequences for AP-1 and CREB, as well as binding sites for EGR1 protein itself (Schwachtgen et al, 2000; Thiel et al, 2000; Svaren et al, 1996; reviewed in Page; and Deindl, 2001). Expression of EGR1 is limited by a negative feedback loop mediated by the binding of a complex of EGR1 with a repressor protein of the NAB family (NGF1A binding protein) to the EGR1 binding site (Cao et al, 1990; Thiel et al, 2000; Svaren et al, 1996)."
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"The Early Growth Response (EGR) gene family includes EGR1-4 and WT1. These Cys2-His2 zinc finger transcription factors are immediate early genes (IEG) that are rapidly turned on downstream of a number of stimuli and regulate expression of genes involved in stress response and differentiation (reviewed in Pagel and Deindl, 2001; Bahrami and Drabl\u00f8s, 2016). Roles for EGR proteins are well established in the nervous system, with EGR target genes contributing to synaptic plasticity, long-term potentiation, peripheral nerve myelination and NGF-induced neurite outgrowth (reviewed in Perez-Cadahia et al, 2011; Herdegen and Leah, 1998; O'Donovan et al, 1999).
Expression of EGR genes depends on binding of phosphorylated ternary complex factor (TCF) protein ELK1 and its transcriptional coactivator SRF (serum response factor) to their cognate DNA binding sequences in the promoters (Hooker et al, 2017; De Franco et al, 1993; Harada et al, 2001; reviewed in Herdegen and Leah, 1998). NGF-stimulated expression of EGR1 and 2 occurs downstream of sustained MAPK signaling (Millbrandt et al, 1987; Sukhatme et al, 1988; de Franco et al, 1998; Mullenbrock et al, 2011; Crosby et al, 1991; L\u00f6nn et al, 2005). In addition to SRF and TCF binding sites, the EGR1 promoter also contain consensus binding sequences for AP-1 and CREB, as well as binding sites for EGR1 protein itself (Schwachtgen et al, 2000; Thiel et al, 2000; Svaren et al, 1996; reviewed in Page; and Deindl, 2001). Expression of EGR1 is limited by a negative feedback loop mediated by the binding of a complex of EGR1 with a repressor protein of the NAB family (NGF1A binding protein) to the EGR1 binding site (Cao et al, 1990; Thiel et al, 2000; Svaren et al, 1996)."
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"The Early Growth Response (EGR) gene family includes EGR1-4 and WT1. These Cys2-His2 zinc finger transcription factors are immediate early genes (IEG) that are rapidly turned on downstream of a number of stimuli and regulate expression of genes involved in stress response and differentiation (reviewed in Pagel and Deindl, 2001; Bahrami and Drabl\u00f8s, 2016). Roles for EGR proteins are well established in the nervous system, with EGR target genes contributing to synaptic plasticity, long-term potentiation, peripheral nerve myelination and NGF-induced neurite outgrowth (reviewed in Perez-Cadahia et al, 2011; Herdegen and Leah, 1998; O'Donovan et al, 1999).
Expression of EGR genes depends on binding of phosphorylated ternary complex factor (TCF) protein ELK1 and its transcriptional coactivator SRF (serum response factor) to their cognate DNA binding sequences in the promoters (Hooker et al, 2017; De Franco et al, 1993; Harada et al, 2001; reviewed in Herdegen and Leah, 1998). NGF-stimulated expression of EGR1 and 2 occurs downstream of sustained MAPK signaling (Millbrandt et al, 1987; Sukhatme et al, 1988; de Franco et al, 1998; Mullenbrock et al, 2011; Crosby et al, 1991; L\u00f6nn et al, 2005). In addition to SRF and TCF binding sites, the EGR1 promoter also contain consensus binding sequences for AP-1 and CREB, as well as binding sites for EGR1 protein itself (Schwachtgen et al, 2000; Thiel et al, 2000; Svaren et al, 1996; reviewed in Page; and Deindl, 2001). Expression of EGR1 is limited by a negative feedback loop mediated by the binding of a complex of EGR1 with a repressor protein of the NAB family (NGF1A binding protein) to the EGR1 binding site (Cao et al, 1990; Thiel et al, 2000; Svaren et al, 1996)."
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"The Early Growth Response (EGR) gene family includes EGR1-4 and WT1. These Cys2-His2 zinc finger transcription factors are immediate early genes (IEG) that are rapidly turned on downstream of a number of stimuli and regulate expression of genes involved in stress response and differentiation (reviewed in Pagel and Deindl, 2001; Bahrami and Drabl\u00f8s, 2016). Roles for EGR proteins are well established in the nervous system, with EGR target genes contributing to synaptic plasticity, long-term potentiation, peripheral nerve myelination and NGF-induced neurite outgrowth (reviewed in Perez-Cadahia et al, 2011; Herdegen and Leah, 1998; O'Donovan et al, 1999).
Expression of EGR genes depends on binding of phosphorylated ternary complex factor (TCF) protein ELK1 and its transcriptional coactivator SRF (serum response factor) to their cognate DNA binding sequences in the promoters (Hooker et al, 2017; De Franco et al, 1993; Harada et al, 2001; reviewed in Herdegen and Leah, 1998). NGF-stimulated expression of EGR1 and 2 occurs downstream of sustained MAPK signaling (Millbrandt et al, 1987; Sukhatme et al, 1988; de Franco et al, 1998; Mullenbrock et al, 2011; Crosby et al, 1991; L\u00f6nn et al, 2005). In addition to SRF and TCF binding sites, the EGR1 promoter also contain consensus binding sequences for AP-1 and CREB, as well as binding sites for EGR1 protein itself (Schwachtgen et al, 2000; Thiel et al, 2000; Svaren et al, 1996; reviewed in Page; and Deindl, 2001). Expression of EGR1 is limited by a negative feedback loop mediated by the binding of a complex of EGR1 with a repressor protein of the NAB family (NGF1A binding protein) to the EGR1 binding site (Cao et al, 1990; Thiel et al, 2000; Svaren et al, 1996)."
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"The Early Growth Response (EGR) gene family includes EGR1-4 and WT1. These Cys2-His2 zinc finger transcription factors are immediate early genes (IEG) that are rapidly turned on downstream of a number of stimuli and regulate expression of genes involved in stress response and differentiation (reviewed in Pagel and Deindl, 2001; Bahrami and Drabl\u00f8s, 2016). Roles for EGR proteins are well established in the nervous system, with EGR target genes contributing to synaptic plasticity, long-term potentiation, peripheral nerve myelination and NGF-induced neurite outgrowth (reviewed in Perez-Cadahia et al, 2011; Herdegen and Leah, 1998; O'Donovan et al, 1999).
Expression of EGR genes depends on binding of phosphorylated ternary complex factor (TCF) protein ELK1 and its transcriptional coactivator SRF (serum response factor) to their cognate DNA binding sequences in the promoters (Hooker et al, 2017; De Franco et al, 1993; Harada et al, 2001; reviewed in Herdegen and Leah, 1998). NGF-stimulated expression of EGR1 and 2 occurs downstream of sustained MAPK signaling (Millbrandt et al, 1987; Sukhatme et al, 1988; de Franco et al, 1998; Mullenbrock et al, 2011; Crosby et al, 1991; L\u00f6nn et al, 2005). In addition to SRF and TCF binding sites, the EGR1 promoter also contain consensus binding sequences for AP-1 and CREB, as well as binding sites for EGR1 protein itself (Schwachtgen et al, 2000; Thiel et al, 2000; Svaren et al, 1996; reviewed in Page; and Deindl, 2001). Expression of EGR1 is limited by a negative feedback loop mediated by the binding of a complex of EGR1 with a repressor protein of the NAB family (NGF1A binding protein) to the EGR1 binding site (Cao et al, 1990; Thiel et al, 2000; Svaren et al, 1996)."
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"The Early Growth Response (EGR) gene family includes EGR1-4 and WT1. These Cys2-His2 zinc finger transcription factors are immediate early genes (IEG) that are rapidly turned on downstream of a number of stimuli and regulate expression of genes involved in stress response and differentiation (reviewed in Pagel and Deindl, 2001; Bahrami and Drabl\u00f8s, 2016). Roles for EGR proteins are well established in the nervous system, with EGR target genes contributing to synaptic plasticity, long-term potentiation, peripheral nerve myelination and NGF-induced neurite outgrowth (reviewed in Perez-Cadahia et al, 2011; Herdegen and Leah, 1998; O'Donovan et al, 1999).
Expression of EGR genes depends on binding of phosphorylated ternary complex factor (TCF) protein ELK1 and its transcriptional coactivator SRF (serum response factor) to their cognate DNA binding sequences in the promoters (Hooker et al, 2017; De Franco et al, 1993; Harada et al, 2001; reviewed in Herdegen and Leah, 1998). NGF-stimulated expression of EGR1 and 2 occurs downstream of sustained MAPK signaling (Millbrandt et al, 1987; Sukhatme et al, 1988; de Franco et al, 1998; Mullenbrock et al, 2011; Crosby et al, 1991; L\u00f6nn et al, 2005). In addition to SRF and TCF binding sites, the EGR1 promoter also contain consensus binding sequences for AP-1 and CREB, as well as binding sites for EGR1 protein itself (Schwachtgen et al, 2000; Thiel et al, 2000; Svaren et al, 1996; reviewed in Page; and Deindl, 2001). Expression of EGR1 is limited by a negative feedback loop mediated by the binding of a complex of EGR1 with a repressor protein of the NAB family (NGF1A binding protein) to the EGR1 binding site (Cao et al, 1990; Thiel et al, 2000; Svaren et al, 1996)."
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"The Early Growth Response (EGR) gene family includes EGR1-4 and WT1. These Cys2-His2 zinc finger transcription factors are immediate early genes (IEG) that are rapidly turned on downstream of a number of stimuli and regulate expression of genes involved in stress response and differentiation (reviewed in Pagel and Deindl, 2001; Bahrami and Drabl\u00f8s, 2016). Roles for EGR proteins are well established in the nervous system, with EGR target genes contributing to synaptic plasticity, long-term potentiation, peripheral nerve myelination and NGF-induced neurite outgrowth (reviewed in Perez-Cadahia et al, 2011; Herdegen and Leah, 1998; O'Donovan et al, 1999).
Expression of EGR genes depends on binding of phosphorylated ternary complex factor (TCF) protein ELK1 and its transcriptional coactivator SRF (serum response factor) to their cognate DNA binding sequences in the promoters (Hooker et al, 2017; De Franco et al, 1993; Harada et al, 2001; reviewed in Herdegen and Leah, 1998). NGF-stimulated expression of EGR1 and 2 occurs downstream of sustained MAPK signaling (Millbrandt et al, 1987; Sukhatme et al, 1988; de Franco et al, 1998; Mullenbrock et al, 2011; Crosby et al, 1991; L\u00f6nn et al, 2005). In addition to SRF and TCF binding sites, the EGR1 promoter also contain consensus binding sequences for AP-1 and CREB, as well as binding sites for EGR1 protein itself (Schwachtgen et al, 2000; Thiel et al, 2000; Svaren et al, 1996; reviewed in Page; and Deindl, 2001). Expression of EGR1 is limited by a negative feedback loop mediated by the binding of a complex of EGR1 with a repressor protein of the NAB family (NGF1A binding protein) to the EGR1 binding site (Cao et al, 1990; Thiel et al, 2000; Svaren et al, 1996)."
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"Expression of Early Growth Response (EGR) genes is dependent in part on the presence of upstream serum response elements (SREs) that bind SRF (serum response factor) and its co-activator ELK1 in response to mutiptle stimuli (Quereshi et al, 1991; Alexandre et al, 1991; de Franco et al, 1993; McMahon and Monroe, 1995;Chen et al, 2004; Vickers et al, 2004; Adams et al, 2017; Esnault et al, 2017; reviewed in O'Donovan et al, 1999; P\u00e9rez-Cadah\u00eda et al, 2011; Pagel and Deindl, 2011)."
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"Expression of Early Growth Response (EGR) genes is dependent in part on the presence of upstream serum response elements (SREs) that bind SRF (serum response factor) and its co-activator ELK1 in response to mutiptle stimuli (Quereshi et al, 1991; Alexandre et al, 1991; de Franco et al, 1993; McMahon and Monroe, 1995;Chen et al, 2004; Vickers et al, 2004; Adams et al, 2017; Esnault et al, 2017; reviewed in O'Donovan et al, 1999; P\u00e9rez-Cadah\u00eda et al, 2011; Pagel and Deindl, 2011)."
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"Expression of Early Growth Response (EGR) genes is dependent in part on the presence of upstream serum response elements (SREs) that bind SRF (serum response factor) and its co-activator ELK1 in response to mutiptle stimuli (Quereshi et al, 1991; Alexandre et al, 1991; de Franco et al, 1993; McMahon and Monroe, 1995;Chen et al, 2004; Vickers et al, 2004; Adams et al, 2017; Esnault et al, 2017; reviewed in O'Donovan et al, 1999; P\u00e9rez-Cadah\u00eda et al, 2011; Pagel and Deindl, 2011)."
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"Expression of Early Growth Response (EGR) genes is dependent in part on the presence of upstream serum response elements (SREs) that bind SRF (serum response factor) and its co-activator ELK1 in response to mutiptle stimuli (Quereshi et al, 1991; Alexandre et al, 1991; de Franco et al, 1993; McMahon and Monroe, 1995;Chen et al, 2004; Vickers et al, 2004; Adams et al, 2017; Esnault et al, 2017; reviewed in O'Donovan et al, 1999; P\u00e9rez-Cadah\u00eda et al, 2011; Pagel and Deindl, 2011)."
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"Expression of Early Growth Response (EGR) genes is dependent in part on the presence of upstream serum response elements (SREs) that bind SRF (serum response factor) and its co-activator ELK1 in response to mutiptle stimuli (Quereshi et al, 1991; Alexandre et al, 1991; de Franco et al, 1993; McMahon and Monroe, 1995;Chen et al, 2004; Vickers et al, 2004; Adams et al, 2017; Esnault et al, 2017; reviewed in O'Donovan et al, 1999; P\u00e9rez-Cadah\u00eda et al, 2011; Pagel and Deindl, 2011)."
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"Expression of Early Growth Response (EGR) genes is dependent in part on the presence of upstream serum response elements (SREs) that bind SRF (serum response factor) and its co-activator ELK1 in response to mutiptle stimuli (Quereshi et al, 1991; Alexandre et al, 1991; de Franco et al, 1993; McMahon and Monroe, 1995;Chen et al, 2004; Vickers et al, 2004; Adams et al, 2017; Esnault et al, 2017; reviewed in O'Donovan et al, 1999; P\u00e9rez-Cadah\u00eda et al, 2011; Pagel and Deindl, 2011)."
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"Serum/glucticocorticoid kinase (SGK) phosphorylates SRF at serine residue 103 in response to multiple upstream stimuli (Tyan et al, 2008). Phosphorylation of SRF and CREB1 by SGK contributes to the SGK-dependent expression of EGR1, an immediate early gene with roles in neuronal development, (David et al, 2005; Tyan et al, 2008; reviewed in Pagel and Deindl, 2011)."
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"Serum/glucticocorticoid kinase (SGK) phosphorylates SRF at serine residue 103 in response to multiple upstream stimuli (Tyan et al, 2008). Phosphorylation of SRF and CREB1 by SGK contributes to the SGK-dependent expression of EGR1, an immediate early gene with roles in neuronal development, (David et al, 2005; Tyan et al, 2008; reviewed in Pagel and Deindl, 2011)."
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"Serum/glucticocorticoid kinase (SGK) phosphorylates SRF at serine residue 103 in response to multiple upstream stimuli (Tyan et al, 2008). Phosphorylation of SRF and CREB1 by SGK contributes to the SGK-dependent expression of EGR1, an immediate early gene with roles in neuronal development, (David et al, 2005; Tyan et al, 2008; reviewed in Pagel and Deindl, 2011)."
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"Expression of EGR1 depends in part on the binding of phosphorylated CREB and SRF factors to their cognate sites in the promoter (Quereshi et al, 1991; Alexandre et al, 1991; McMahon et al, 1995; Chen et al, 2004; Vickers et al, 2004; Tyan et al, 2008; David et al, 2005; Esnault et al, 2017). Phosphorylation of CREB can be mediated by RSK proteins, MAPKAPK2 or by SGK (de Cesare et al, 1998; Bonni et al, 1995; David et al, 2005; Tyan et al, 2008). SGK-mediated phosphorylation of SRF has also been implicated in the activation of EGR1 gene expression (Tyan et al, 2008).; "
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"Expression of EGR1 depends in part on the binding of phosphorylated CREB and SRF factors to their cognate sites in the promoter (Quereshi et al, 1991; Alexandre et al, 1991; McMahon et al, 1995; Chen et al, 2004; Vickers et al, 2004; Tyan et al, 2008; David et al, 2005; Esnault et al, 2017). Phosphorylation of CREB can be mediated by RSK proteins, MAPKAPK2 or by SGK (de Cesare et al, 1998; Bonni et al, 1995; David et al, 2005; Tyan et al, 2008). SGK-mediated phosphorylation of SRF has also been implicated in the activation of EGR1 gene expression (Tyan et al, 2008).; "
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"Expression of EGR1 depends in part on the binding of phosphorylated CREB and SRF factors to their cognate sites in the promoter (Quereshi et al, 1991; Alexandre et al, 1991; McMahon et al, 1995; Chen et al, 2004; Vickers et al, 2004; Tyan et al, 2008; David et al, 2005; Esnault et al, 2017). Phosphorylation of CREB can be mediated by RSK proteins, MAPKAPK2 or by SGK (de Cesare et al, 1998; Bonni et al, 1995; David et al, 2005; Tyan et al, 2008). SGK-mediated phosphorylation of SRF has also been implicated in the activation of EGR1 gene expression (Tyan et al, 2008).; "
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"Expression of EGR1 depends in part on the binding of phosphorylated CREB and SRF factors to their cognate sites in the promoter (Quereshi et al, 1991; Alexandre et al, 1991; McMahon et al, 1995; Chen et al, 2004; Vickers et al, 2004; Tyan et al, 2008; David et al, 2005; Esnault et al, 2017). Phosphorylation of CREB can be mediated by RSK proteins, MAPKAPK2 or by SGK (de Cesare et al, 1998; Bonni et al, 1995; David et al, 2005; Tyan et al, 2008). SGK-mediated phosphorylation of SRF has also been implicated in the activation of EGR1 gene expression (Tyan et al, 2008).; "
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"Expression of EGR1 depends in part on the binding of phosphorylated CREB and SRF factors to their cognate sites in the promoter (Quereshi et al, 1991; Alexandre et al, 1991; McMahon et al, 1995; Chen et al, 2004; Vickers et al, 2004; Tyan et al, 2008; David et al, 2005; Esnault et al, 2017). Phosphorylation of CREB can be mediated by RSK proteins, MAPKAPK2 or by SGK (de Cesare et al, 1998; Bonni et al, 1995; David et al, 2005; Tyan et al, 2008). SGK-mediated phosphorylation of SRF has also been implicated in the activation of EGR1 gene expression (Tyan et al, 2008).; "
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"Expression of EGR1 depends in part on the binding of phosphorylated CREB and SRF factors to their cognate sites in the promoter (Quereshi et al, 1991; Alexandre et al, 1991; McMahon et al, 1995; Chen et al, 2004; Vickers et al, 2004; Tyan et al, 2008; David et al, 2005; Esnault et al, 2017). Phosphorylation of CREB can be mediated by RSK proteins, MAPKAPK2 or by SGK (de Cesare et al, 1998; Bonni et al, 1995; David et al, 2005; Tyan et al, 2008). SGK-mediated phosphorylation of SRF has also been implicated in the activation of EGR1 gene expression (Tyan et al, 2008).; "
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"nucleoplasm",
" 1833716",
"R-HSA-9031628",
"",
"Expression of EGR1 depends in part on the binding of phosphorylated CREB and SRF factors to their cognate sites in the promoter (Quereshi et al, 1991; Alexandre et al, 1991; McMahon et al, 1995; Chen et al, 2004; Vickers et al, 2004; Tyan et al, 2008; David et al, 2005; Esnault et al, 2017). Phosphorylation of CREB can be mediated by RSK proteins, MAPKAPK2 or by SGK (de Cesare et al, 1998; Bonni et al, 1995; David et al, 2005; Tyan et al, 2008). SGK-mediated phosphorylation of SRF has also been implicated in the activation of EGR1 gene expression (Tyan et al, 2008).; "
],
[
"R-HSA-9612514",
"p-S133 CREB and p-S103 SRF bind the EGR1 promoter",
"nucleoplasm",
" 2040600",
"R-HSA-9031628",
"",
"Expression of EGR1 depends in part on the binding of phosphorylated CREB and SRF factors to their cognate sites in the promoter (Quereshi et al, 1991; Alexandre et al, 1991; McMahon et al, 1995; Chen et al, 2004; Vickers et al, 2004; Tyan et al, 2008; David et al, 2005; Esnault et al, 2017). Phosphorylation of CREB can be mediated by RSK proteins, MAPKAPK2 or by SGK (de Cesare et al, 1998; Bonni et al, 1995; David et al, 2005; Tyan et al, 2008). SGK-mediated phosphorylation of SRF has also been implicated in the activation of EGR1 gene expression (Tyan et al, 2008).; "
],
[
"R-HSA-9612514",
"p-S133 CREB and p-S103 SRF bind the EGR1 promoter",
"nucleoplasm",
" 28286024",
"R-HSA-9031628",
"",
"Expression of EGR1 depends in part on the binding of phosphorylated CREB and SRF factors to their cognate sites in the promoter (Quereshi et al, 1991; Alexandre et al, 1991; McMahon et al, 1995; Chen et al, 2004; Vickers et al, 2004; Tyan et al, 2008; David et al, 2005; Esnault et al, 2017). Phosphorylation of CREB can be mediated by RSK proteins, MAPKAPK2 or by SGK (de Cesare et al, 1998; Bonni et al, 1995; David et al, 2005; Tyan et al, 2008). SGK-mediated phosphorylation of SRF has also been implicated in the activation of EGR1 gene expression (Tyan et al, 2008).; "
],
[
"R-HSA-9612514",
"p-S133 CREB and p-S103 SRF bind the EGR1 promoter",
"nucleoplasm",
" 7823924",
"R-HSA-9031628",
"",
"Expression of EGR1 depends in part on the binding of phosphorylated CREB and SRF factors to their cognate sites in the promoter (Quereshi et al, 1991; Alexandre et al, 1991; McMahon et al, 1995; Chen et al, 2004; Vickers et al, 2004; Tyan et al, 2008; David et al, 2005; Esnault et al, 2017). Phosphorylation of CREB can be mediated by RSK proteins, MAPKAPK2 or by SGK (de Cesare et al, 1998; Bonni et al, 1995; David et al, 2005; Tyan et al, 2008). SGK-mediated phosphorylation of SRF has also been implicated in the activation of EGR1 gene expression (Tyan et al, 2008).; "
],
[
"R-HSA-9647977",
"ICMT methylates S-Farn RAS proteins",
"endoplasmic reticulum membrane",
"27791178",
"R-HSA-9648002",
"",
"RAS proteins undergo C-terminal carboxymethylation by isoprenylcysteine methyltransferase (ICMT) (Yang et al, 2011; Dharmaiah et al, 2016; reviewed in Gysin et al, 2011; Ahearn et al, 2018). LIke prenylation, methylation is required for plasma membrane localization and function of RAS proteins, and disruption of ICMT or interference with the methylation reaction inhibits cell growth and KRAS-dependent transformation (Chiu et al, 2004; Michaelson et al, 2005; Bergo et al, 2004; Wahlstrom et al, 2008; Winter-Vann et al, 2003). Consistent with this, a number of small molecule inhibitors of ICMT have been shown to decrease tumor proliferation (Wang et al, 2009; Manu et al, 2017; Sun et al, 2016)."
],
[
"R-HSA-9647977",
"ICMT methylates S-Farn RAS proteins",
"endoplasmic reticulum membrane",
" 14966563",
"R-HSA-9648002",
"",
"RAS proteins undergo C-terminal carboxymethylation by isoprenylcysteine methyltransferase (ICMT) (Yang et al, 2011; Dharmaiah et al, 2016; reviewed in Gysin et al, 2011; Ahearn et al, 2018). LIke prenylation, methylation is required for plasma membrane localization and function of RAS proteins, and disruption of ICMT or interference with the methylation reaction inhibits cell growth and KRAS-dependent transformation (Chiu et al, 2004; Michaelson et al, 2005; Bergo et al, 2004; Wahlstrom et al, 2008; Winter-Vann et al, 2003). Consistent with this, a number of small molecule inhibitors of ICMT have been shown to decrease tumor proliferation (Wang et al, 2009; Manu et al, 2017; Sun et al, 2016)."
],
[
"R-HSA-9647977",
"ICMT methylates S-Farn RAS proteins",
"endoplasmic reticulum membrane",
" 22195972",
"R-HSA-9648002",
"",
"RAS proteins undergo C-terminal carboxymethylation by isoprenylcysteine methyltransferase (ICMT) (Yang et al, 2011; Dharmaiah et al, 2016; reviewed in Gysin et al, 2011; Ahearn et al, 2018). LIke prenylation, methylation is required for plasma membrane localization and function of RAS proteins, and disruption of ICMT or interference with the methylation reaction inhibits cell growth and KRAS-dependent transformation (Chiu et al, 2004; Michaelson et al, 2005; Bergo et al, 2004; Wahlstrom et al, 2008; Winter-Vann et al, 2003). Consistent with this, a number of small molecule inhibitors of ICMT have been shown to decrease tumor proliferation (Wang et al, 2009; Manu et al, 2017; Sun et al, 2016)."
],
[
"R-HSA-9647977",
"ICMT methylates S-Farn RAS proteins",
"endoplasmic reticulum membrane",
" 12750467",
"R-HSA-9648002",
"",
"RAS proteins undergo C-terminal carboxymethylation by isoprenylcysteine methyltransferase (ICMT) (Yang et al, 2011; Dharmaiah et al, 2016; reviewed in Gysin et al, 2011; Ahearn et al, 2018). LIke prenylation, methylation is required for plasma membrane localization and function of RAS proteins, and disruption of ICMT or interference with the methylation reaction inhibits cell growth and KRAS-dependent transformation (Chiu et al, 2004; Michaelson et al, 2005; Bergo et al, 2004; Wahlstrom et al, 2008; Winter-Vann et al, 2003). Consistent with this, a number of small molecule inhibitors of ICMT have been shown to decrease tumor proliferation (Wang et al, 2009; Manu et al, 2017; Sun et al, 2016)."
],
[
"R-HSA-9647977",
"ICMT methylates S-Farn RAS proteins",
"endoplasmic reticulum membrane",
" 14660603",
"R-HSA-9648002",
"",
"RAS proteins undergo C-terminal carboxymethylation by isoprenylcysteine methyltransferase (ICMT) (Yang et al, 2011; Dharmaiah et al, 2016; reviewed in Gysin et al, 2011; Ahearn et al, 2018). LIke prenylation, methylation is required for plasma membrane localization and function of RAS proteins, and disruption of ICMT or interference with the methylation reaction inhibits cell growth and KRAS-dependent transformation (Chiu et al, 2004; Michaelson et al, 2005; Bergo et al, 2004; Wahlstrom et al, 2008; Winter-Vann et al, 2003). Consistent with this, a number of small molecule inhibitors of ICMT have been shown to decrease tumor proliferation (Wang et al, 2009; Manu et al, 2017; Sun et al, 2016)."
],
[
"R-HSA-9647977",
"ICMT methylates S-Farn RAS proteins",
"endoplasmic reticulum membrane",
" 15659645",
"R-HSA-9648002",
"",
"RAS proteins undergo C-terminal carboxymethylation by isoprenylcysteine methyltransferase (ICMT) (Yang et al, 2011; Dharmaiah et al, 2016; reviewed in Gysin et al, 2011; Ahearn et al, 2018). LIke prenylation, methylation is required for plasma membrane localization and function of RAS proteins, and disruption of ICMT or interference with the methylation reaction inhibits cell growth and KRAS-dependent transformation (Chiu et al, 2004; Michaelson et al, 2005; Bergo et al, 2004; Wahlstrom et al, 2008; Winter-Vann et al, 2003). Consistent with this, a number of small molecule inhibitors of ICMT have been shown to decrease tumor proliferation (Wang et al, 2009; Manu et al, 2017; Sun et al, 2016)."
],
[
"R-HSA-9647977",
"ICMT methylates S-Farn RAS proteins",
"endoplasmic reticulum membrane",
" 18502828",
"R-HSA-9648002",
"",
"RAS proteins undergo C-terminal carboxymethylation by isoprenylcysteine methyltransferase (ICMT) (Yang et al, 2011; Dharmaiah et al, 2016; reviewed in Gysin et al, 2011; Ahearn et al, 2018). LIke prenylation, methylation is required for plasma membrane localization and function of RAS proteins, and disruption of ICMT or interference with the methylation reaction inhibits cell growth and KRAS-dependent transformation (Chiu et al, 2004; Michaelson et al, 2005; Bergo et al, 2004; Wahlstrom et al, 2008; Winter-Vann et al, 2003). Consistent with this, a number of small molecule inhibitors of ICMT have been shown to decrease tumor proliferation (Wang et al, 2009; Manu et al, 2017; Sun et al, 2016)."
],
[
"R-HSA-9647977",
"ICMT methylates S-Farn RAS proteins",
"endoplasmic reticulum membrane",
" 20622895",
"R-HSA-9648002",
"",
"RAS proteins undergo C-terminal carboxymethylation by isoprenylcysteine methyltransferase (ICMT) (Yang et al, 2011; Dharmaiah et al, 2016; reviewed in Gysin et al, 2011; Ahearn et al, 2018). LIke prenylation, methylation is required for plasma membrane localization and function of RAS proteins, and disruption of ICMT or interference with the methylation reaction inhibits cell growth and KRAS-dependent transformation (Chiu et al, 2004; Michaelson et al, 2005; Bergo et al, 2004; Wahlstrom et al, 2008; Winter-Vann et al, 2003). Consistent with this, a number of small molecule inhibitors of ICMT have been shown to decrease tumor proliferation (Wang et al, 2009; Manu et al, 2017; Sun et al, 2016)."
],
[
"R-HSA-9647977",
"ICMT methylates S-Farn RAS proteins",
"endoplasmic reticulum membrane",
" 26706195",
"R-HSA-9648002",
"",
"RAS proteins undergo C-terminal carboxymethylation by isoprenylcysteine methyltransferase (ICMT) (Yang et al, 2011; Dharmaiah et al, 2016; reviewed in Gysin et al, 2011; Ahearn et al, 2018). LIke prenylation, methylation is required for plasma membrane localization and function of RAS proteins, and disruption of ICMT or interference with the methylation reaction inhibits cell growth and KRAS-dependent transformation (Chiu et al, 2004; Michaelson et al, 2005; Bergo et al, 2004; Wahlstrom et al, 2008; Winter-Vann et al, 2003). Consistent with this, a number of small molecule inhibitors of ICMT have been shown to decrease tumor proliferation (Wang et al, 2009; Manu et al, 2017; Sun et al, 2016)."
],
[
"R-HSA-9647977",
"ICMT methylates S-Farn RAS proteins",
"endoplasmic reticulum membrane",
" 28167504",
"R-HSA-9648002",
"",
"RAS proteins undergo C-terminal carboxymethylation by isoprenylcysteine methyltransferase (ICMT) (Yang et al, 2011; Dharmaiah et al, 2016; reviewed in Gysin et al, 2011; Ahearn et al, 2018). LIke prenylation, methylation is required for plasma membrane localization and function of RAS proteins, and disruption of ICMT or interference with the methylation reaction inhibits cell growth and KRAS-dependent transformation (Chiu et al, 2004; Michaelson et al, 2005; Bergo et al, 2004; Wahlstrom et al, 2008; Winter-Vann et al, 2003). Consistent with this, a number of small molecule inhibitors of ICMT have been shown to decrease tumor proliferation (Wang et al, 2009; Manu et al, 2017; Sun et al, 2016)."
],
[
"R-HSA-9647977",
"ICMT methylates S-Farn RAS proteins",
"endoplasmic reticulum membrane",
" 29311131",
"R-HSA-9648002",
"",
"RAS proteins undergo C-terminal carboxymethylation by isoprenylcysteine methyltransferase (ICMT) (Yang et al, 2011; Dharmaiah et al, 2016; reviewed in Gysin et al, 2011; Ahearn et al, 2018). LIke prenylation, methylation is required for plasma membrane localization and function of RAS proteins, and disruption of ICMT or interference with the methylation reaction inhibits cell growth and KRAS-dependent transformation (Chiu et al, 2004; Michaelson et al, 2005; Bergo et al, 2004; Wahlstrom et al, 2008; Winter-Vann et al, 2003). Consistent with this, a number of small molecule inhibitors of ICMT have been shown to decrease tumor proliferation (Wang et al, 2009; Manu et al, 2017; Sun et al, 2016)."
],
[
"R-HSA-9647977",
"ICMT methylates S-Farn RAS proteins",
"endoplasmic reticulum membrane",
" 21779505",
"R-HSA-9648002",
"",
"RAS proteins undergo C-terminal carboxymethylation by isoprenylcysteine methyltransferase (ICMT) (Yang et al, 2011; Dharmaiah et al, 2016; reviewed in Gysin et al, 2011; Ahearn et al, 2018). LIke prenylation, methylation is required for plasma membrane localization and function of RAS proteins, and disruption of ICMT or interference with the methylation reaction inhibits cell growth and KRAS-dependent transformation (Chiu et al, 2004; Michaelson et al, 2005; Bergo et al, 2004; Wahlstrom et al, 2008; Winter-Vann et al, 2003). Consistent with this, a number of small molecule inhibitors of ICMT have been shown to decrease tumor proliferation (Wang et al, 2009; Manu et al, 2017; Sun et al, 2016)."
],
[
"R-HSA-9647978",
"pro-RAS proteins are farnesylated",
"cytosol, endoplasmic reticulum membrane",
"15451670",
"R-HSA-9648002",
"",
"RAS proteins are isoprenylated at a CaaX motif in the hypervariable region, where a is an aliphatic amino acid and X is any amino acid (Casey et al, 1989; Dharmaiah et al, 2016; reviewed in Ahean et al, 2018). Geranylgeranylation is favoured when X is leucine, while all other amino acids at this position favour farnesylation by farnesyltransferase (Casey et al, 1989; Reid et al, 2004)."
],
[
"R-HSA-9647978",
"pro-RAS proteins are farnesylated",
"cytosol, endoplasmic reticulum membrane",
" 27791178",
"R-HSA-9648002",
"",
"RAS proteins are isoprenylated at a CaaX motif in the hypervariable region, where a is an aliphatic amino acid and X is any amino acid (Casey et al, 1989; Dharmaiah et al, 2016; reviewed in Ahean et al, 2018). Geranylgeranylation is favoured when X is leucine, while all other amino acids at this position favour farnesylation by farnesyltransferase (Casey et al, 1989; Reid et al, 2004)."
],
[
"R-HSA-9647978",
"pro-RAS proteins are farnesylated",
"cytosol, endoplasmic reticulum membrane",
" 2682646",
"R-HSA-9648002",
"",
"RAS proteins are isoprenylated at a CaaX motif in the hypervariable region, where a is an aliphatic amino acid and X is any amino acid (Casey et al, 1989; Dharmaiah et al, 2016; reviewed in Ahean et al, 2018). Geranylgeranylation is favoured when X is leucine, while all other amino acids at this position favour farnesylation by farnesyltransferase (Casey et al, 1989; Reid et al, 2004)."
],
[
"R-HSA-9647978",
"pro-RAS proteins are farnesylated",
"cytosol, endoplasmic reticulum membrane",
" 29311131",
"R-HSA-9648002",
"",
"RAS proteins are isoprenylated at a CaaX motif in the hypervariable region, where a is an aliphatic amino acid and X is any amino acid (Casey et al, 1989; Dharmaiah et al, 2016; reviewed in Ahean et al, 2018). Geranylgeranylation is favoured when X is leucine, while all other amino acids at this position favour farnesylation by farnesyltransferase (Casey et al, 1989; Reid et al, 2004)."
],
[
"R-HSA-9647980",
"mature RAS proteins translocate to plasma membrane",
"Golgi membrane, plasma membrane",
"21779505",
"R-HSA-9648002",
"",
"After farnesylation, C-terminal proteolysis, carboxymethylation and palmitoylation, RAS proteins translocate to the plasma membrane (reviewed in Gysin et al, 2011)."
],
[
"R-HSA-9647994",
"RAS proteins are depalmitoylated",
"plasma membrane",
"16000296",
"R-HSA-9648002",
"",
"RAS proteins undergo a dynamic palmitoylation and depalmitoylation cycle that regulates their association with membranes and thus their localization and function (Hancock et al, 1989; Swarthout et al, 2005; reviewed in Gysin et al, 2011; Lin et al, 2017; Ahearn et al, 2018). Depalmitoylation is catalyzed by the acyl-protein thioesterase LYPLA1, also known as APT1, or by members of the ABHD17 family (Dekker et al, 2010; Lin and Conibear, 2015; reviewed in Lin et al, 2017). "
],
[
"R-HSA-9647994",
"RAS proteins are depalmitoylated",
"plasma membrane",
" 2661017",
"R-HSA-9648002",
"",
"RAS proteins undergo a dynamic palmitoylation and depalmitoylation cycle that regulates their association with membranes and thus their localization and function (Hancock et al, 1989; Swarthout et al, 2005; reviewed in Gysin et al, 2011; Lin et al, 2017; Ahearn et al, 2018). Depalmitoylation is catalyzed by the acyl-protein thioesterase LYPLA1, also known as APT1, or by members of the ABHD17 family (Dekker et al, 2010; Lin and Conibear, 2015; reviewed in Lin et al, 2017). "
],
[
"R-HSA-9647994",
"RAS proteins are depalmitoylated",
"plasma membrane",
" 20418879",
"R-HSA-9648002",
"",
"RAS proteins undergo a dynamic palmitoylation and depalmitoylation cycle that regulates their association with membranes and thus their localization and function (Hancock et al, 1989; Swarthout et al, 2005; reviewed in Gysin et al, 2011; Lin et al, 2017; Ahearn et al, 2018). Depalmitoylation is catalyzed by the acyl-protein thioesterase LYPLA1, also known as APT1, or by members of the ABHD17 family (Dekker et al, 2010; Lin and Conibear, 2015; reviewed in Lin et al, 2017). "
],
[
"R-HSA-9647994",
"RAS proteins are depalmitoylated",
"plasma membrane",
" 26701913",
"R-HSA-9648002",
"",
"RAS proteins undergo a dynamic palmitoylation and depalmitoylation cycle that regulates their association with membranes and thus their localization and function (Hancock et al, 1989; Swarthout et al, 2005; reviewed in Gysin et al, 2011; Lin et al, 2017; Ahearn et al, 2018). Depalmitoylation is catalyzed by the acyl-protein thioesterase LYPLA1, also known as APT1, or by members of the ABHD17 family (Dekker et al, 2010; Lin and Conibear, 2015; reviewed in Lin et al, 2017). "
],
[
"R-HSA-9647994",
"RAS proteins are depalmitoylated",
"plasma membrane",
" 28630138",
"R-HSA-9648002",
"",
"RAS proteins undergo a dynamic palmitoylation and depalmitoylation cycle that regulates their association with membranes and thus their localization and function (Hancock et al, 1989; Swarthout et al, 2005; reviewed in Gysin et al, 2011; Lin et al, 2017; Ahearn et al, 2018). Depalmitoylation is catalyzed by the acyl-protein thioesterase LYPLA1, also known as APT1, or by members of the ABHD17 family (Dekker et al, 2010; Lin and Conibear, 2015; reviewed in Lin et al, 2017). "
],
[
"R-HSA-9647994",
"RAS proteins are depalmitoylated",
"plasma membrane",
" 29311131",
"R-HSA-9648002",
"",
"RAS proteins undergo a dynamic palmitoylation and depalmitoylation cycle that regulates their association with membranes and thus their localization and function (Hancock et al, 1989; Swarthout et al, 2005; reviewed in Gysin et al, 2011; Lin et al, 2017; Ahearn et al, 2018). Depalmitoylation is catalyzed by the acyl-protein thioesterase LYPLA1, also known as APT1, or by members of the ABHD17 family (Dekker et al, 2010; Lin and Conibear, 2015; reviewed in Lin et al, 2017). "
],
[
"R-HSA-9647994",
"RAS proteins are depalmitoylated",
"plasma membrane",
" 21779505",
"R-HSA-9648002",
"",
"RAS proteins undergo a dynamic palmitoylation and depalmitoylation cycle that regulates their association with membranes and thus their localization and function (Hancock et al, 1989; Swarthout et al, 2005; reviewed in Gysin et al, 2011; Lin et al, 2017; Ahearn et al, 2018). Depalmitoylation is catalyzed by the acyl-protein thioesterase LYPLA1, also known as APT1, or by members of the ABHD17 family (Dekker et al, 2010; Lin and Conibear, 2015; reviewed in Lin et al, 2017). "
],
[
"R-HSA-9647999",
"RCE1 cleaves S-Farn proRAS proteins",
"endoplasmic reticulum membrane",
"10085068",
"R-HSA-9648002",
"",
"After prenylation, RAS proteins undergo C-terminal endoproteolysis by RAS-converting enzyme I (RCE1), which removes the aaX residues of the CaaX motif (Otto et al, 1999; Hollander et al, 2000; reviewed in Hampton et al, 2018; Ahearn et al, 2018). RCE1-mediated cleavage is required for RAS plasma membrane localization and function (Michaelson et al, 2005). RCE1 is ubiquitinated in its active form, and deubiquitination by USP17L2 abrogates its catalytic activity and inhibits signaling through the RAS-RAF MAP kinase pathway (Burrows et al, 2009). RCE1 has thus been investigated as a potential therapeutic target in RAS driven disease. Despite some promising studies, the effects of RCE1 inactivation appear unpredictable and can lead to unexpected activation of RAS signaling through mechanisms that are not fully understood (Bergo et al, 2002; Aiyagari et al, 2003; Kim et al, 1999; Chen et al, 1998; Chen et al, 1999; Wahlstrom et al, 2007)."
],
[
"R-HSA-9647999",
"RCE1 cleaves S-Farn proRAS proteins",
"endoplasmic reticulum membrane",
" 11038283",
"R-HSA-9648002",
"",
"After prenylation, RAS proteins undergo C-terminal endoproteolysis by RAS-converting enzyme I (RCE1), which removes the aaX residues of the CaaX motif (Otto et al, 1999; Hollander et al, 2000; reviewed in Hampton et al, 2018; Ahearn et al, 2018). RCE1-mediated cleavage is required for RAS plasma membrane localization and function (Michaelson et al, 2005). RCE1 is ubiquitinated in its active form, and deubiquitination by USP17L2 abrogates its catalytic activity and inhibits signaling through the RAS-RAF MAP kinase pathway (Burrows et al, 2009). RCE1 has thus been investigated as a potential therapeutic target in RAS driven disease. Despite some promising studies, the effects of RCE1 inactivation appear unpredictable and can lead to unexpected activation of RAS signaling through mechanisms that are not fully understood (Bergo et al, 2002; Aiyagari et al, 2003; Kim et al, 1999; Chen et al, 1998; Chen et al, 1999; Wahlstrom et al, 2007)."
],
[
"R-HSA-9647999",
"RCE1 cleaves S-Farn proRAS proteins",
"endoplasmic reticulum membrane",
" 19188362",
"R-HSA-9648002",
"",
"After prenylation, RAS proteins undergo C-terminal endoproteolysis by RAS-converting enzyme I (RCE1), which removes the aaX residues of the CaaX motif (Otto et al, 1999; Hollander et al, 2000; reviewed in Hampton et al, 2018; Ahearn et al, 2018). RCE1-mediated cleavage is required for RAS plasma membrane localization and function (Michaelson et al, 2005). RCE1 is ubiquitinated in its active form, and deubiquitination by USP17L2 abrogates its catalytic activity and inhibits signaling through the RAS-RAF MAP kinase pathway (Burrows et al, 2009). RCE1 has thus been investigated as a potential therapeutic target in RAS driven disease. Despite some promising studies, the effects of RCE1 inactivation appear unpredictable and can lead to unexpected activation of RAS signaling through mechanisms that are not fully understood (Bergo et al, 2002; Aiyagari et al, 2003; Kim et al, 1999; Chen et al, 1998; Chen et al, 1999; Wahlstrom et al, 2007)."
],
[
"R-HSA-9647999",
"RCE1 cleaves S-Farn proRAS proteins",
"endoplasmic reticulum membrane",
" 10085069",
"R-HSA-9648002",
"",
"After prenylation, RAS proteins undergo C-terminal endoproteolysis by RAS-converting enzyme I (RCE1), which removes the aaX residues of the CaaX motif (Otto et al, 1999; Hollander et al, 2000; reviewed in Hampton et al, 2018; Ahearn et al, 2018). RCE1-mediated cleavage is required for RAS plasma membrane localization and function (Michaelson et al, 2005). RCE1 is ubiquitinated in its active form, and deubiquitination by USP17L2 abrogates its catalytic activity and inhibits signaling through the RAS-RAF MAP kinase pathway (Burrows et al, 2009). RCE1 has thus been investigated as a potential therapeutic target in RAS driven disease. Despite some promising studies, the effects of RCE1 inactivation appear unpredictable and can lead to unexpected activation of RAS signaling through mechanisms that are not fully understood (Bergo et al, 2002; Aiyagari et al, 2003; Kim et al, 1999; Chen et al, 1998; Chen et al, 1999; Wahlstrom et al, 2007)."
],
[
"R-HSA-9647999",
"RCE1 cleaves S-Farn proRAS proteins",
"endoplasmic reticulum membrane",
" 10667208",
"R-HSA-9648002",
"",
"After prenylation, RAS proteins undergo C-terminal endoproteolysis by RAS-converting enzyme I (RCE1), which removes the aaX residues of the CaaX motif (Otto et al, 1999; Hollander et al, 2000; reviewed in Hampton et al, 2018; Ahearn et al, 2018). RCE1-mediated cleavage is required for RAS plasma membrane localization and function (Michaelson et al, 2005). RCE1 is ubiquitinated in its active form, and deubiquitination by USP17L2 abrogates its catalytic activity and inhibits signaling through the RAS-RAF MAP kinase pathway (Burrows et al, 2009). RCE1 has thus been investigated as a potential therapeutic target in RAS driven disease. Despite some promising studies, the effects of RCE1 inactivation appear unpredictable and can lead to unexpected activation of RAS signaling through mechanisms that are not fully understood (Bergo et al, 2002; Aiyagari et al, 2003; Kim et al, 1999; Chen et al, 1998; Chen et al, 1999; Wahlstrom et al, 2007)."
],
[
"R-HSA-9647999",
"RCE1 cleaves S-Farn proRAS proteins",
"endoplasmic reticulum membrane",
" 11739732",
"R-HSA-9648002",
"",
"After prenylation, RAS proteins undergo C-terminal endoproteolysis by RAS-converting enzyme I (RCE1), which removes the aaX residues of the CaaX motif (Otto et al, 1999; Hollander et al, 2000; reviewed in Hampton et al, 2018; Ahearn et al, 2018). RCE1-mediated cleavage is required for RAS plasma membrane localization and function (Michaelson et al, 2005). RCE1 is ubiquitinated in its active form, and deubiquitination by USP17L2 abrogates its catalytic activity and inhibits signaling through the RAS-RAF MAP kinase pathway (Burrows et al, 2009). RCE1 has thus been investigated as a potential therapeutic target in RAS driven disease. Despite some promising studies, the effects of RCE1 inactivation appear unpredictable and can lead to unexpected activation of RAS signaling through mechanisms that are not fully understood (Bergo et al, 2002; Aiyagari et al, 2003; Kim et al, 1999; Chen et al, 1998; Chen et al, 1999; Wahlstrom et al, 2007)."
],
[
"R-HSA-9647999",
"RCE1 cleaves S-Farn proRAS proteins",
"endoplasmic reticulum membrane",
" 12433685",
"R-HSA-9648002",
"",
"After prenylation, RAS proteins undergo C-terminal endoproteolysis by RAS-converting enzyme I (RCE1), which removes the aaX residues of the CaaX motif (Otto et al, 1999; Hollander et al, 2000; reviewed in Hampton et al, 2018; Ahearn et al, 2018). RCE1-mediated cleavage is required for RAS plasma membrane localization and function (Michaelson et al, 2005). RCE1 is ubiquitinated in its active form, and deubiquitination by USP17L2 abrogates its catalytic activity and inhibits signaling through the RAS-RAF MAP kinase pathway (Burrows et al, 2009). RCE1 has thus been investigated as a potential therapeutic target in RAS driven disease. Despite some promising studies, the effects of RCE1 inactivation appear unpredictable and can lead to unexpected activation of RAS signaling through mechanisms that are not fully understood (Bergo et al, 2002; Aiyagari et al, 2003; Kim et al, 1999; Chen et al, 1998; Chen et al, 1999; Wahlstrom et al, 2007)."
],
[
"R-HSA-9647999",
"RCE1 cleaves S-Farn proRAS proteins",
"endoplasmic reticulum membrane",
" 15659645",
"R-HSA-9648002",
"",
"After prenylation, RAS proteins undergo C-terminal endoproteolysis by RAS-converting enzyme I (RCE1), which removes the aaX residues of the CaaX motif (Otto et al, 1999; Hollander et al, 2000; reviewed in Hampton et al, 2018; Ahearn et al, 2018). RCE1-mediated cleavage is required for RAS plasma membrane localization and function (Michaelson et al, 2005). RCE1 is ubiquitinated in its active form, and deubiquitination by USP17L2 abrogates its catalytic activity and inhibits signaling through the RAS-RAF MAP kinase pathway (Burrows et al, 2009). RCE1 has thus been investigated as a potential therapeutic target in RAS driven disease. Despite some promising studies, the effects of RCE1 inactivation appear unpredictable and can lead to unexpected activation of RAS signaling through mechanisms that are not fully understood (Bergo et al, 2002; Aiyagari et al, 2003; Kim et al, 1999; Chen et al, 1998; Chen et al, 1999; Wahlstrom et al, 2007)."
],
[
"R-HSA-9647999",
"RCE1 cleaves S-Farn proRAS proteins",
"endoplasmic reticulum membrane",
" 29311131",
"R-HSA-9648002",
"",
"After prenylation, RAS proteins undergo C-terminal endoproteolysis by RAS-converting enzyme I (RCE1), which removes the aaX residues of the CaaX motif (Otto et al, 1999; Hollander et al, 2000; reviewed in Hampton et al, 2018; Ahearn et al, 2018). RCE1-mediated cleavage is required for RAS plasma membrane localization and function (Michaelson et al, 2005). RCE1 is ubiquitinated in its active form, and deubiquitination by USP17L2 abrogates its catalytic activity and inhibits signaling through the RAS-RAF MAP kinase pathway (Burrows et al, 2009). RCE1 has thus been investigated as a potential therapeutic target in RAS driven disease. Despite some promising studies, the effects of RCE1 inactivation appear unpredictable and can lead to unexpected activation of RAS signaling through mechanisms that are not fully understood (Bergo et al, 2002; Aiyagari et al, 2003; Kim et al, 1999; Chen et al, 1998; Chen et al, 1999; Wahlstrom et al, 2007)."
],
[
"R-HSA-9647999",
"RCE1 cleaves S-Farn proRAS proteins",
"endoplasmic reticulum membrane",
" 29424242",
"R-HSA-9648002",
"",
"After prenylation, RAS proteins undergo C-terminal endoproteolysis by RAS-converting enzyme I (RCE1), which removes the aaX residues of the CaaX motif (Otto et al, 1999; Hollander et al, 2000; reviewed in Hampton et al, 2018; Ahearn et al, 2018). RCE1-mediated cleavage is required for RAS plasma membrane localization and function (Michaelson et al, 2005). RCE1 is ubiquitinated in its active form, and deubiquitination by USP17L2 abrogates its catalytic activity and inhibits signaling through the RAS-RAF MAP kinase pathway (Burrows et al, 2009). RCE1 has thus been investigated as a potential therapeutic target in RAS driven disease. Despite some promising studies, the effects of RCE1 inactivation appear unpredictable and can lead to unexpected activation of RAS signaling through mechanisms that are not fully understood (Bergo et al, 2002; Aiyagari et al, 2003; Kim et al, 1999; Chen et al, 1998; Chen et al, 1999; Wahlstrom et al, 2007)."
],
[
"R-HSA-9647999",
"RCE1 cleaves S-Farn proRAS proteins",
"endoplasmic reticulum membrane",
" 9851253",
"R-HSA-9648002",
"",
"After prenylation, RAS proteins undergo C-terminal endoproteolysis by RAS-converting enzyme I (RCE1), which removes the aaX residues of the CaaX motif (Otto et al, 1999; Hollander et al, 2000; reviewed in Hampton et al, 2018; Ahearn et al, 2018). RCE1-mediated cleavage is required for RAS plasma membrane localization and function (Michaelson et al, 2005). RCE1 is ubiquitinated in its active form, and deubiquitination by USP17L2 abrogates its catalytic activity and inhibits signaling through the RAS-RAF MAP kinase pathway (Burrows et al, 2009). RCE1 has thus been investigated as a potential therapeutic target in RAS driven disease. Despite some promising studies, the effects of RCE1 inactivation appear unpredictable and can lead to unexpected activation of RAS signaling through mechanisms that are not fully understood (Bergo et al, 2002; Aiyagari et al, 2003; Kim et al, 1999; Chen et al, 1998; Chen et al, 1999; Wahlstrom et al, 2007)."
]
]
},
"readme": "Name\n - Human Protein Reactions (Reactome)\n\nVersion\n - v-2.2.1\n\nCreated on\n - 2019-11-30T15:06:36.890527\n\nModified on\n - 2022-09-26T09:05:27.602135\n\nCreated by\n - Jeet Vora [jeetvora@gwu.edu], Robel Kahsay [rykahsay@gwu.edu], Karina Martinez [karinamartinez@gwu.edu], Jingyue Wu [jingyue.wu@email.gwu.edu]\n\nAuthors\n - Maria Martin [martin@ebi.ac.uk], Preethi Vasudev [pvasudev@ebi.ac.uk]\n\nChecksum\n - \n\nUsability Domain\n - The Human Protein Reactions (Reactome) dataset contains reactions information for pathways for human [taxid:9606] UniProtKB accessions that includes reaction participants, pathway ID, reaction ID, PMID etc from Reactome database. The dataset is derived from 2019-09 UniProtKB release. If you use this dataset please provide proper attribution to EMBL-EBI-UniProtKB and GlyGen\n\nDescription Domain\n Keywords\n - Reactome\n - Pathway\n - Reactions\n - PMID\n\n Pipeline Steps\n - Step-1: The script loads the Reactome reaction data from the triplestore containing triples from nt file to retrieve the information associated with the Reactome IDs and maps it to the UniProtKB canonical accessions and extracts the dataset in the csv format\n\nExecution Domain\n Scripts - https://github.com/glygener/glygen-backend-integration/blob/master/dataset-maker/make-protein-dataset.py\n\n\n Software Prerequisites\n Name: Python\n Version: 2.7.5\n URI: https://www.python.org/download/releases/2.7.5/\n\nI/O Domain\n Input Subdomain\n Name: uniprot-proteome-homo-sapiens.nt\n URI: https:/data.glygen.org/ln2downloads/ebi/2023_10_30/uniprot-proteome-homo-sapiens.nt\n Output Subdomain\n Name: human_protein_reactions_reactome.csv\n URI: https:/data.glygen.org/ln2releases/data/v-2.2.1/reviewed/human_protein_reactions_reactome.csv\n Name: human_protein_reactions_reactome.stat.csv\n URI: https:/data.glygen.org/ln2releases/data/v-2.2.1/reviewed/human_protein_reactions_reactome.stat.csv\n\nFields\n Name: \"reaction_id\"\n Description: \"The identifier assigned to a reaction in Reactome database\"\n Unique Values: \"13711\"\n Name: \"reaction_name\"\n Description: \"The name assigned to a reaction in Reactome database\"\n Unique Values: \"13609\"\n Name: \"cellular_location\"\n Description: \"The loaction in the cell where reaction occurs\"\n Unique Values: \"365\"\n Name: \"pmid\"\n Description: \"NCBI PubMed database Identifier\"\n Unique Values: \"20589\"\n Name: \"pathway_id\"\n Description: \"Pathway Identifier\"\n Unique Values: \"2057\"\n Name: \"equation\"\n Description: \"\"\n Unique Values: \"1\"\n Name: \"reaction_summary\"\n Description: \"\"\n Unique Values: \"13142\"",
"downloadurl": "/ln2data/releases/data/v-2.2.1/reviewed/human_protein_reactions_reactome.csv"
}