NOTCH3 gene transcription is directly stimulated by the NOTCH1 coactivator complex and NOTCH1-mediated regulation of NOTCH3 is involved in differentiation of esophageal squamous cells (Ohashi et al. 2009).
NOTCH3 transcription is directly stimulated by transcription factor ELF3, activated by PRKCI (protein kinase C iota)-mediated phosphorylation downstream of KRAS signaling. The PRKCI-ELF3-NOTCH3 signaling controls the tumor-initiating cell phenotype in KRAS-mediated lung adenocarcinoma (Ali et al. 2016).",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-1911492"
],
"output_participant_list": [],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-1912415",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1912415"
}
]
},
{
"id": "R-HSA-1912416",
"name": "NOTCH1 gene transcription",
"equation": "",
"summary": "NOTCH1 was cloned as a chromosome 9 gene involved in translocation t(7;9)(q34;q34.3) in several T-cell acute lymphoblastic leukemia (T-ALL) patients. The gene was found to be highly homologous to the Drosophila gene Notch and was initially named TAN-1 (translocation-associated Notch homolog). Transcripts of NOTCH1 were detected in many fetal and adult human and mouse tissues, with the highest abundance in lymphoid tissues. The translocation t(7;9)(q34;q34.3) found in a small fraction of T-ALL patients puts NOTCH1 transcription under the control of the T-cell receptor-beta (TCRB) locus, which results in expression of truncated peptides that lack the extracellular ligand binding domain and are constitutively active (reviewed by Grabher et al. 2006). Activating NOTCH1 point mutations, mainly affecting the extracellular heterodimerization domain and/or the C-terminal PEST domain, are found in more than 50% of human T-ALLs (Weng et al. 2004).
Studies of mouse Rbpj knockout embryos and zebrafish Mib (mindbomb) mutants indicate that the NOTCH1 coactivator complex positively regulates NOTCH1 transcription. The RBPJ-binding site(s) that the NOTCH1 coactivator complex normally binds have not been found in the NOTCH1 promoter, however, so this effect may be indirect and its mechanism is unknown (Del Monte et al. 2007).
CCND1 (cyclin D1) forms a complex with CREBBP and binds to the NOTCH1 promoter, stimulating NOTCH1 transcription. The involvement of CCND1 in transcriptional regulation of NOTCH1 was established in mouse retinas and the rat retinal precursor cell line R28 (Bienvenu et al. 2010).
E2F1 and E2F3 are able to bind to the NOTCH1 promoter and activate NOTCH1 transcription (Viatour et al. 2011).
NOTCH1 promoter possesses two putative p53-binding sites. Chromatin immunoprecipitation (ChIP) assays of human primary keratinocytes showed binding of endogenous p53 protein to both sites. Experiments in which p53 was downregulated or overexpressed implicate p53 as a positive regulator of NOTCH1 expression in primary human keratinocytes. It is likely that p53-mediated regulation of NOTCH1 expression involves interplay with other cell-type specific determinants of gene expression (Lefort et al. 2007). In lymphoid cells, NOTCH1 expression may be negatively regulated by p53 (Laws and Osborne 2004). Other proteins implicated in the negative regulation of NOTCH1 transcription are KLF9 (Ying et al. 2011), JARID2 (Mysliwiec et al. 2011, Mysliwiec et al. 2012), KLF4 and SP3 (Lambertini et al. 2010), and p63 (Yugawa et al. 2010).",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-1911481"
],
"output_participant_list": [
"R-HSA-1606559"
],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-1912416",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1912416"
}
]
},
{
"id": "R-HSA-1980047",
"name": "NOTCH1 stimulates HES1 transcription",
"equation": "",
"summary": "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).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-1980047",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1980047"
}
]
},
{
"id": "R-HSA-1980065",
"name": "NOTCH1 stimulates HEY transcription",
"equation": "",
"summary": "RBPJ binding sites in the promoters of HEY1, HEY2 and HEYL genes are conserved between humans and mice (Maier and Gessler 2000), and expression of human NICD1 was directly shown to activate transcription from human HEY2 and HEYL promoters (Arnett et al. 2010). Based on the evolutionary conservation of RBPJ sites and the existing findings from human and mouse studies, NOTCH1 is expected to directly stimulate transcription of HEY1, HEY2 and HEYL (Fischer et al. 2004, Leimeister et al. 2000).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-1980065",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1980065"
}
]
},
{
"id": "R-HSA-1980067",
"name": "NOTCH1 stimulates MYC transcription",
"equation": "",
"summary": "Binding of the NOTCH1 Coactivator Complex to the MYC promoter stimulates MYC transcription (Palomero et al. 2006).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-1980067",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1980067"
}
]
},
{
"id": "R-HSA-1980078",
"name": "NOTCH1 stimulates HES5 transcription",
"equation": "",
"summary": "Binding of the NOTCH1 Coactivator Complex to the HES5 promoter stimulates HES5 transcription (Arnett et al. 2010).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-1980078",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1980078"
}
]
},
{
"id": "R-HSA-1989745",
"name": "Expression of ACADM",
"equation": "",
"summary": "The ACADM gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "mitochondrial matrix, nucleoplasm",
"input_participant_list": [
"R-HSA-5649946"
],
"output_participant_list": [
"R-HSA-49491"
],
"enzyme_list": [
"Q15788-1",
"P11310-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989745",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989745"
}
]
},
{
"id": "R-HSA-1989746",
"name": "Expression of CYP7A1",
"equation": "",
"summary": "The CYP7A1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "endoplasmic reticulum membrane, nucleoplasm",
"input_participant_list": [
"R-HSA-5649942"
],
"output_participant_list": [
"R-HSA-192169"
],
"enzyme_list": [
"P22680-1",
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989746",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989746"
}
]
},
{
"id": "R-HSA-1989747",
"name": "Expression of FHL2",
"equation": "",
"summary": "The FHL2 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-5649945"
],
"output_participant_list": [
"R-HSA-561161"
],
"enzyme_list": [
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989747",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989747"
}
]
},
{
"id": "R-HSA-1989748",
"name": "Expression of GRHL1",
"equation": "",
"summary": "The GRHL1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-5649951"
],
"output_participant_list": [
"R-HSA-561138"
],
"enzyme_list": [
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989748",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989748"
}
]
},
{
"id": "R-HSA-1989749",
"name": "Expression of ACOX1",
"equation": "",
"summary": "The ACOX1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "nucleoplasm, peroxisomal matrix",
"input_participant_list": [
"R-HSA-5649947"
],
"output_participant_list": [
"R-HSA-400212"
],
"enzyme_list": [
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989749",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989749"
}
]
},
{
"id": "R-HSA-1989750",
"name": "Expression of FATP1 (SLC27A1)",
"equation": "",
"summary": "The FATP1 (SLC27A1) gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "nucleoplasm, plasma membrane",
"input_participant_list": [
"R-HSA-5649954"
],
"output_participant_list": [
"R-HSA-400190"
],
"enzyme_list": [
"Q15788-1",
"Q92793-1",
"Q6PCB7-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989750",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989750"
}
]
},
{
"id": "R-HSA-1989751",
"name": "Expression of FABP1",
"equation": "",
"summary": "The FABP1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-5649943"
],
"output_participant_list": [
"R-HSA-1989743"
],
"enzyme_list": [
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989751",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989751"
}
]
},
{
"id": "R-HSA-1989752",
"name": "Expression of TXNRD1",
"equation": "",
"summary": "The TXNRD1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "cytosol, nucleoplasm",
"input_participant_list": [
"R-HSA-5649944"
],
"output_participant_list": [
"R-HSA-73531"
],
"enzyme_list": [
"Q16881-1",
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989752",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989752"
}
]
},
{
"id": "R-HSA-1989753",
"name": "Expression of PEX11A",
"equation": "",
"summary": "The PEX11A gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "nucleoplasm, peroxisomal membrane",
"input_participant_list": [
"R-HSA-5649952"
],
"output_participant_list": [
"R-HSA-400198"
],
"enzyme_list": [
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989753",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989753"
}
]
},
{
"id": "R-HSA-1989754",
"name": "Expression of APOA1",
"equation": "",
"summary": "The APOA1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "extracellular region, nucleoplasm",
"input_participant_list": [
"R-HSA-5649927"
],
"output_participant_list": [
"R-HSA-174720"
],
"enzyme_list": [
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989754",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989754"
}
]
},
{
"id": "R-HSA-1989755",
"name": "Expression of CYP4A11",
"equation": "",
"summary": "The CYP4A11 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "endoplasmic reticulum membrane, nucleoplasm",
"input_participant_list": [
"R-HSA-5649930"
],
"output_participant_list": [
"R-HSA-52649"
],
"enzyme_list": [
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q02928-1",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989755",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989755"
}
]
},
{
"id": "R-HSA-1989756",
"name": "Expression of ME1",
"equation": "",
"summary": "The ME1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "cytosol, nucleoplasm",
"input_participant_list": [
"R-HSA-5649931"
],
"output_participant_list": [],
"enzyme_list": [
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"P48163-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989756",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989756"
}
]
},
{
"id": "R-HSA-1989757",
"name": "Expression of FADS1",
"equation": "",
"summary": "The FADS1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "endoplasmic reticulum membrane, nucleoplasm",
"input_participant_list": [
"R-HSA-5649932"
],
"output_participant_list": [
"R-HSA-400122"
],
"enzyme_list": [
"Q15788-1",
"O60427-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989757",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989757"
}
]
},
{
"id": "R-HSA-1989758",
"name": "Expression of UGT1A9",
"equation": "",
"summary": "The UGT1A9 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "endoplasmic reticulum membrane, nucleoplasm",
"input_participant_list": [
"R-HSA-5649935"
],
"output_participant_list": [
"R-HSA-400210"
],
"enzyme_list": [
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1",
"O60656-1"
],
"evidence": [
{
"id": "R-HSA-1989758",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989758"
}
]
},
{
"id": "R-HSA-1989759",
"name": "Expression of G0S2",
"equation": "",
"summary": "The G0S2 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "lipid droplet, nucleoplasm",
"input_participant_list": [
"R-HSA-5649941"
],
"output_participant_list": [
"R-HSA-1989741"
],
"enzyme_list": [
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989759",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989759"
}
]
},
{
"id": "R-HSA-1989760",
"name": "Expression of HMGCS2",
"equation": "",
"summary": "The HMGCS2 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "mitochondrial matrix, nucleoplasm",
"input_participant_list": [
"R-HSA-5649934"
],
"output_participant_list": [
"R-HSA-56573"
],
"enzyme_list": [
"P54868-1",
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989760",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989760"
}
]
},
{
"id": "R-HSA-1989761",
"name": "Expression of APOA5",
"equation": "",
"summary": "The APOA5 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "extracellular region, nucleoplasm",
"input_participant_list": [
"R-HSA-5649925"
],
"output_participant_list": [
"R-HSA-174608"
],
"enzyme_list": [
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989761",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989761"
}
]
},
{
"id": "R-HSA-1989762",
"name": "Expression of ABCB4",
"equation": "",
"summary": "The ABCB4 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "nucleoplasm, plasma membrane",
"input_participant_list": [
"R-HSA-5649955"
],
"output_participant_list": [
"R-HSA-400167"
],
"enzyme_list": [
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"P21439-1",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989762",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989762"
}
]
},
{
"id": "R-HSA-1989764",
"name": "Expression of CYP1A1",
"equation": "",
"summary": "The CYP1A1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein (van der Meer et al. 2010, Rakhshandehroo et al. 2009). The aryl hydrocarbon receptor (AHR) is a ligand-activated transcription factor that controls the expression of a diverse set of genes. AHR acts as a sensor of polyaromatic chemicals, which upon activation, translocates to the nucleus and binds with the aryl hydrocarbon receptor nuclear translocator (ARNT) to transactivate target genes via binding to xenobiotic response elements (XREs) in their promoter regions. AHR targets genes of Phase I and Phase II metabolism, such as cytochrome P450 1A1 (CYP1A1) (Beischlag et al. 2008). AHR is regulated by the aryl hydrocarbon receptor repressor (AHRR, aka BHLHE77, KIAA1234) that inhibits both xenobiotic-induced and constitutively active AHR transcriptional activity in many species (Hahn et al. 2009, Haarmann-Stemmann & Abel 2006).
",
"cellular_location": "endoplasmic reticulum membrane, nucleoplasm",
"input_participant_list": [
"R-HSA-5649956"
],
"output_participant_list": [
"R-HSA-52623"
],
"enzyme_list": [
"Q15788-1",
"Q92793-1",
"P04798-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989764",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989764"
}
]
},
{
"id": "R-HSA-1989765",
"name": "Expression of ABCA1",
"equation": "",
"summary": "The ATP-binding cassette transporter A1 (ABCA1) gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "nucleoplasm, plasma membrane",
"input_participant_list": [
"R-HSA-5649950"
],
"output_participant_list": [],
"enzyme_list": [
"Q15788-1",
"O95477-1",
"O15379-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989765",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989765"
}
]
},
{
"id": "R-HSA-1989767",
"name": "Expression of TRIB3",
"equation": "",
"summary": "The TRIB3 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-5649928"
],
"output_participant_list": [
"R-HSA-9635877"
],
"enzyme_list": [
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989767",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989767"
}
]
},
{
"id": "R-HSA-1989768",
"name": "Expression of TIAM2",
"equation": "",
"summary": "The TIAM2 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "cytosol, nucleoplasm",
"input_participant_list": [
"R-HSA-5649926"
],
"output_participant_list": [
"R-HSA-561165"
],
"enzyme_list": [
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989768",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989768"
}
]
},
{
"id": "R-HSA-1989770",
"name": "Expression of PLIN2",
"equation": "",
"summary": "The Adipophilin (PLIN2) gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "nucleoplasm, plasma membrane",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-400160"
],
"enzyme_list": [
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989770",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989770"
}
]
},
{
"id": "R-HSA-1989771",
"name": "Expression of TNFRSF21",
"equation": "",
"summary": "The TNFRSF21 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "nucleoplasm, plasma membrane",
"input_participant_list": [
"R-HSA-4793840"
],
"output_participant_list": [
"R-HSA-561169"
],
"enzyme_list": [
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989771",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989771"
}
]
},
{
"id": "R-HSA-1989772",
"name": "Expression of GLIPR1",
"equation": "",
"summary": "The GLIPR1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "nucleoplasm, plasma membrane",
"input_participant_list": [
"R-HSA-5649933"
],
"output_participant_list": [
"R-HSA-561145"
],
"enzyme_list": [
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989772",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989772"
}
]
},
{
"id": "R-HSA-1989773",
"name": "Expression of CPT2",
"equation": "",
"summary": "The CPT2 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "mitochondrial inner membrane, nucleoplasm",
"input_participant_list": [
"R-HSA-5649936"
],
"output_participant_list": [
"R-HSA-200994"
],
"enzyme_list": [
"P23786-1",
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989773",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989773"
}
]
},
{
"id": "R-HSA-1989774",
"name": "Expression of AGT",
"equation": "",
"summary": "The AGT gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "extracellular region, nucleoplasm",
"input_participant_list": [
"R-HSA-5649924"
],
"output_participant_list": [],
"enzyme_list": [
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989774",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989774"
}
]
},
{
"id": "R-HSA-1989775",
"name": "Expression of SULT2A1",
"equation": "",
"summary": "The SULT2A1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "cytosol, nucleoplasm",
"input_participant_list": [
"R-HSA-5649940"
],
"output_participant_list": [
"R-HSA-176559"
],
"enzyme_list": [
"Q15788-1",
"Q06520-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989775",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989775"
}
]
},
{
"id": "R-HSA-1989776",
"name": "Expression of APOA2",
"equation": "",
"summary": "The APOA2 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "extracellular region, nucleoplasm",
"input_participant_list": [
"R-HSA-5649953"
],
"output_participant_list": [
"R-HSA-174775"
],
"enzyme_list": [
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989776",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989776"
}
]
},
{
"id": "R-HSA-1989777",
"name": "Expression of RGL1",
"equation": "",
"summary": "The RGL1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "cytosol, nucleoplasm",
"input_participant_list": [
"R-HSA-5649948"
],
"output_participant_list": [
"R-HSA-561160"
],
"enzyme_list": [
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989777",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989777"
}
]
},
{
"id": "R-HSA-1989778",
"name": "Expression of ACSL1",
"equation": "",
"summary": "The ACSL1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "mitochondrial outer membrane, nucleoplasm",
"input_participant_list": [
"R-HSA-5649949"
],
"output_participant_list": [
"R-HSA-400123"
],
"enzyme_list": [
"Q15788-1",
"P33121-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989778",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989778"
}
]
},
{
"id": "R-HSA-1989779",
"name": "Expression of ANKRD1",
"equation": "",
"summary": "The ANKRD1 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-5649939"
],
"output_participant_list": [
"R-HSA-561143"
],
"enzyme_list": [
"Q15788-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-1989779",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1989779"
}
]
},
{
"id": "R-HSA-212356",
"name": "Formation of CSL-NICD coactivator complex",
"equation": "",
"summary": "Mammalian CSL Coactivator Complexes: Upon activation of Notch signaling, cleavage of the transmembrane Notch receptor releases the Notch Intracellular Domain (NICD), which translocates to the nucleus, where it binds to CSL and displaces the corepressor complex from CSL (reviewed in Mumm, 2000 and Kovall, 2007). The resulting CSL-NICD \\binary complex\\ then recruits an additional coactivator, Mastermind (Mam), to form a ternary complex. The ternary complex then recruits additional, more general coactivators, such as CREB Binding Protein (CBP), or the related p300 coactivator, and a number of Histone Acetytransferase (HAT) proteins, including GCN5 and PCAF (Fryer, 2002). There is evidence that Mam also can subsequently recruit specific kinases that phosphorylate NICD, to downregulate its function and turn off Notch signaling (Fryer, 2004).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92830-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-212356",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-212356"
}
]
},
{
"id": "R-HSA-2220957",
"name": "NOTCH1 PEST domain mutants coactivator complex binds CDK8:CCNC",
"equation": "",
"summary": "MAML is expected to recruit CDK8 to NICD1 PEST domain mutants like it recruits CDK8 to wild-type NICD1 (Fryer et al. 2004).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1",
"P49336-1"
],
"evidence": [
{
"id": "R-HSA-2220957",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2220957"
}
]
},
{
"id": "R-HSA-2220964",
"name": "NICD1 PEST domain mutants in complex with RBPJ (CSL) bind MAML",
"equation": "",
"summary": "NICD1 PEST domain mutants in complex with RBPJ and SNW1 are expected, similar to the wild-type NICD1:RBPJ:SNW1 complex, to recruit MAML and histone acetylatransferases to form the NOTCH1 PEST domain mutants coactivator complex (Fryer et al. 2002, Wallberg et al. 2002, Nam et al. 2006).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-2220989"
],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-2220964",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2220964"
}
]
},
{
"id": "R-HSA-2220966",
"name": "NOTCH1 PEST domain mutants stimulate HES5 transcription",
"equation": "",
"summary": "NICD1 PEST domain mutants are expected to stimulate HES5 transcription in a similar manner to wild-type NICD1 (Arnett et al. 2010).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-2220966",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2220966"
}
]
},
{
"id": "R-HSA-2220971",
"name": "CDK8 phosphorylates NICD1 PEST domain mutants",
"equation": "",
"summary": "While CDK8 can probably phosphorylate the TAD domain of NICD1 PEST domain mutants, it cannot phosphorylate the PEST domain of these mutants as it is partially or completely truncated (Fryer et al. 2004).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-2220958"
],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1",
"P49336-1"
],
"evidence": [
{
"id": "R-HSA-2220971",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2220971"
}
]
},
{
"id": "R-HSA-2220979",
"name": "NOTCH1 PEST domain mutants stimulate HES1 transcription",
"equation": "",
"summary": "NICD1 PEST domain mutants are expected to stimulate HES1 transcription in a similar manner to wild-type NICD1 (Jarriault et al. 1995).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-2220979",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2220979"
}
]
},
{
"id": "R-HSA-2220981",
"name": "NOTCH1 PEST domain mutants stimulate HEY transcription",
"equation": "",
"summary": "NICD1 PEST domain mutants are expected to stimulate transcription of HEY genes (HEY1, HEY2 and HEYL) in a similar manner to wild-type NICD1 (Fischer et al. 2004, Leimeister et al. 2000, Maier et al. 2000, Arnett et al. 2010).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-2220981",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2220981"
}
]
},
{
"id": "R-HSA-2220985",
"name": "NOTCH1 PEST domain mutants stimulate MYC transcription",
"equation": "",
"summary": "NICD1 PEST domain mutants are expected to stimulate MYC transcription in a similar manner to wild-type NICD1 (Palomero et al. 2006).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-2220985",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2220985"
}
]
},
{
"id": "R-HSA-3134883",
"name": "Beta-catenin enhances association of IRF3 with CBP/p300",
"equation": "",
"summary": "Beta-catenin increases IFN-beta expression by binding to the C-terminal domain of the transcription factor IRF3 and recruiting the acetyltransferase p300 to the IFN-beta enhanceosome via IRF3.",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-3134883",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3134883"
}
]
},
{
"id": "R-HSA-3322427",
"name": "Beta-catenin recruits CBP/p300",
"equation": "",
"summary": "CBP (CREB-binding protein) and the closely related p300 are histone acetyltransferases that are recruited to WNT-responsive promoters through interactions with the C-terminal half of beta-catenin (Hecht et al, 2000; Takemura and Moon, 2000; Sun et al, 2000). Although recruitment is WNT-signaling dependent and results in activation of several WNT target genes, the precise role of CBP and p300 is not yet clear. In Drosophila, recruitment of CBP can affect the acetylation of histones H3 and H4 up to 30kb away from WREs, possibly aided by the DNA bending induced by TCFs (Parker et al, 2008); in other instances, the intrinsic HAT activity has been shown to acetylate beta-catenin (Levy et al, 2004; Wolf et al, 2002), or to be dispensable for the transcriptional activation activity of CBP/p300 at WREs (Hecht et al, 2000).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-3322427",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3322427"
}
]
},
{
"id": "R-HSA-3371554",
"name": "HSF1 acetylation at Lys80",
"equation": "",
"summary": "Acetylated HSF1 was detected in lysates of human embryonic kidney 293T cells which were transfected with vectors encoding a Flag-HSF1 fusion and p300 proteins and exposed to various stress conditions (Westerheide SD et al. 2012). No acetylation was found in lysates of unstressed cells. Acetylation of HSF1 may occurs on multiple lysines, such as Lys80 within the DNA binding domain. Mutation of Lys80 disrupted the DNA-binding ability of recombinant HSF1, indicating that the acetylation at Lys80 caused the regulated release of the HSF1 trimers from DNA and thus represents a regulatory step in the attenuation of the heat shock responce (Westerheide SD et al. 2009; Herbomel G et al 2013).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P11142-1",
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-3371554",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3371554"
}
]
},
{
"id": "R-HSA-3697008",
"name": "CREBBP acetylates histone H2B, H3, H4",
"equation": "",
"summary": "CREBBP (CBP) is named after its interaction with the CRE-binding protein CREB, though it interacts with many other proteins. It is thought to act as an integrator of signals from various pathways (Goodman & Smolik 2000), which compete for a limited amount of nuclear CREBBP. CREBBP and EP300 (p300) are closely related and have overlapping functions but also unique properties, particularly in vivo (Kalkhoven 2004). Both proteins form a physical bridge between DNA-binding transcription factors and the RNA polymerase II complex. Histones are believed to be the main acetylation targets of CREBBP and EP300, but their ability to acetylate and thereby regulate transcription factors such as p53 (Gu & Roeder 1997) is considered significant additional function (Kasper et al. 2006).
CREBBP has intrinsic histone acetyltransferase (HAT) activity on lysine-13 of H2B, lysine-15 of H3 and lysine-9 of H4 (Bannister & Kouzarides 1996, Rekowski & Giannis 2010, Barrett et al. 2011).
Homozygous knockout of CREBBP results in embryonic lethality (Tanaka et al. 1997). Focal deletion of CREBBP demonstrates that it is critical for the in vivo acetylation of lysines on histones H2B, H3 and H4, and cannot be compensated for by the p300 (Barrett et al. 2011).
Genomic aberrations in CREBBP are associated with Rubinstein-Taybi syndrome (Torress et al. 2013).
N.B. Coordinates of post-translational modifications described here follow UniProt standard practice whereby coordinates refer to the translated protein before any further processing. Histone literature typically refers to coordinates of the protein after the initiating methionine has been removed. Therefore the coordinates of post-translated residues in the Reactome database and described here are frequently +1 when compared with the literature.",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-3697008",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3697008"
}
]
},
{
"id": "R-HSA-381309",
"name": "PPARG:RXRA heterodimer binds to fatty acid-like ligands",
"equation": "",
"summary": "PPARG can be activated in cell cultures by adding ligands such as polyunsaturated fatty acids and certain prostanoids (prostaglandins). Endogenous fatty acids are relatively poor activators. Which ligands are most responsible for PPARG activation in the body has not yet been established. Generally, oxidized fatty acids such as 9(S')-hydroxyoctadeca-10,12-dienoic acid (9(S')-HODE) and 13(S')-HODE are more effective activators than are endogenous fatty acids. The thiazolidinedione (TZD) class of antidiabetic drugs are agonist ligands for PPARG (Lambe and Tugwood 1996).
FABP4 delivers ligands to PPARG directly. Binding of activator ligands to PPARG causes loss of corepressors such as SMRT/NCoR2, NCoR1, and HDAC3 and gain of interactions with the basal transcription machinery (Yoo et al. 2006). The TRAP220/MED1/DRIP205 subunit of the TRAP/Mediator (DRIP) complex binds directly to the LXXLL motif of PPARG and TRAP/Mediator is necessary for full transcriptional activation of target genes (Ge et al. 2008). PPARG also interacts with the MED14 subunit of the Mediator complex (Grontved et al. 2010).
Other coactivators, including NCOA1/SRC-1, NCOA2/TIF2/GRIP1, CBP, HAT/p300, and PRIP, interact with PPARG in a ligand-dependent way and enhance transcription (Gellman et al. 1999, Wallberg et al. 2003, Yang et al. 2000, Ge et al. 2002, Puigserver et al. 1999, Bugge et al. 2009, Steger et al. 2010).
The target genes of PPARG encode proteins involved in adipocyte differentiation (PGAR/ANGPTL4, PLIN, and aP2/FABP4), carbohydrate metabolism (PEPCK-C), and fatty acid transport (FAT/CD36, LPL).",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-376398",
"R-HSA-442499",
"R-HSA-8932115",
"R-HSA-8940294",
"R-HSA-442496"
],
"output_participant_list": [
"R-HSA-2026072",
"R-HSA-442469",
"R-HSA-442464",
"R-HSA-442501"
],
"enzyme_list": [
"Q15788-1",
"O15379-1",
"Q09472-1",
"Q92793-1",
"Q9Y6Q9-1",
"P49336-1",
"Q9BWU1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-381309",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-381309"
}
]
},
{
"id": "R-HSA-3927959",
"name": "SUMOylation of CREBBP with SUMO1",
"equation": "",
"summary": "As inferred from mouse homologs, CREBBP (CBP) is SUMOylated at lysine-998, lysine-1033, and lysine-1056 with SUMO1. SUMOylation recruits DAXX and HDAC2 to repress transcription.",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-3927877"
],
"enzyme_list": [
"P63279-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-3927959",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3927959"
}
]
},
{
"id": "R-HSA-400143",
"name": "Fatty acid ligands activate PPARA",
"equation": "",
"summary": "PPAR-alpha is activated by binding polyunsaturated fatty acids especially those having 18-22 carbon groups and 2-6 double bonds such as linoleiate, linolenate, arachidonate, and eicosapentaenoate. These ligands bind the C-terminal region of PPAR-alpha. The fibrate drugs are also agonists of PPAR-alpha.
Binding of a ligand causes a conformational change in PPAR-alpha so that it recruits coactivators. By analogy with the closely related receptor PPAR-gamma, PPAR-alpha probably binds TBL1 and TBLR1, which are responsible for recruiting the 19S proteasome to degrade corepressors during the exchange of corepressors for coactivators. The coactivators belong to the CBP-SRC-HAT complex (CBP/p300, SRC1, SRC2, SRC3, CARM1, SWI/SNF, BAF60C, PRIC320, and PRIC285), the ASC complex (PRIP/ASC2, PIMT), and the TRAP-DRIP-ARC-MEDIATOR complex (TRAP130, PBP/TRAP220). The coactivators contain LXXLL motifs (Nuclear Receptor Boxes) that interact with the AF-2 region in nuclear receptors such as PPAR-alpha. Additionally bilirubin binds to PPAR-alpha and acts as coactivator.",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q15788-1",
"O15379-1",
"Q92793-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-400143",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-400143"
}
]
},
{
"id": "R-HSA-4395227",
"name": "CCND1:CREBBP binds NOTCH1 promoter",
"equation": "",
"summary": "CCND1 (cyclin D1) forms a complex with CREBBP and binds to the NOTCH1 promoter, stimulating NOTCH1 transcription. The involvement of CCND1 in transcriptional regulation of NOTCH1 was established in mouse retinas and the rat retinal precursor cell line R28 (Bienvenu et al. 2010).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-4395227",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-4395227"
}
]
},
{
"id": "R-HSA-4396347",
"name": "NOTCH1 Coactivator Complex binds HES1 promoter",
"equation": "",
"summary": "NOTCH1 coactivator complex binds the promoter of HES1 gene and directly stimulates HES1 transcription (Jarriault et al. 1995).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-4396347",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-4396347"
}
]
},
{
"id": "R-HSA-4396371",
"name": "NOTCH1 Coactivator Complex binds MYC promoter",
"equation": "",
"summary": "NICD1, as a part of the NOTCH1 Coactivator Complex, binds to the MYC promoter (Palomero et al. 2006).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-4396371",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-4396371"
}
]
},
{
"id": "R-HSA-4396379",
"name": "NOTCH1 Coactivator Complex binds HES5 promoter",
"equation": "",
"summary": "NICD1, as a part of the NOTCH1 Coactivator Complex, binds to the HES5 promoter (Arnett et al. 2010).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-4396379",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-4396379"
}
]
},
{
"id": "R-HSA-4396382",
"name": "NOTCH1 Coactivator Complex binds promoters of HEY genes",
"equation": "",
"summary": "RBPJ binding sites in the promoters of HEY1, HEY2 and HEYL genes are conserved between humans and mice (Maier and Gessler 2000), and human NICD1 was directly shown to bind human HEY2 and HEYL promoters (Arnett et al. 2010).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-4396382",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-4396382"
}
]
},
{
"id": "R-HSA-4396392",
"name": "NOTCH1 PEST domain mutants bind HES1 promoter",
"equation": "",
"summary": "NICD1 PEST domain mutants-containing coactivator complexes are expected to bind HES1 promoter in a similar manner to the wild-type NOTCH1 Coactivator Complex (Jarriault et al. 1995).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-4396396"
],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-4396392",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-4396392"
}
]
},
{
"id": "R-HSA-4396393",
"name": "NOTCH1 PEST domain mutants bind MYC promoter",
"equation": "",
"summary": "NICD1 PEST domain mutant coactivator complexes are expected to bind MYC promoter in a similar manner to the wild-type NOTCH1 Coactivator Complex (Palomero et al. 2006).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-4396404"
],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-4396393",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-4396393"
}
]
},
{
"id": "R-HSA-4396401",
"name": "NOTCH1 PEST domain mutants bind HES5 promoter",
"equation": "",
"summary": "NICD1 PEST domain mutants coactivator complexes are expected to bind HES5 promoter in a similar manner to the wild-type NOTCH1 Coactivator Complex (Arnett et al. 2010).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-4396397"
],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-4396401",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-4396401"
}
]
},
{
"id": "R-HSA-4396402",
"name": "NOTCH1 PEST domain mutants bind promoters of HEY genes",
"equation": "",
"summary": "NICD1 PEST domain mutant coactivator complexes are expected to bind promoters of HEY genes (HEY1, HEY2 and HEYL) in a similar manner to the wild-type NOTCH1 Coactivator Complex (Maier and Gessler 2000, Arnett et al. 2010).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-4396391"
],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-4396402",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-4396402"
}
]
},
{
"id": "R-HSA-560472",
"name": "Expression of Phosphoenolpyruvate carboxykinase 1 (PEPCK-C)",
"equation": "",
"summary": "The PEPCK-C gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "cytosol, nucleoplasm",
"input_participant_list": [
"R-HSA-5640206"
],
"output_participant_list": [
"R-HSA-70495"
],
"enzyme_list": [
"P35558-1",
"Q15788-1",
"Q09472-1",
"Q92793-1",
"Q9Y6Q9-1",
"P49336-1",
"Q9BWU1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-560472",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-560472"
}
]
},
{
"id": "R-HSA-560473",
"name": "Expression of ANGPTL4",
"equation": "",
"summary": "The ANGPTL4 gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "extracellular region, nucleoplasm",
"input_participant_list": [
"R-HSA-5640194"
],
"output_participant_list": [
"R-HSA-381271"
],
"enzyme_list": [
"Q15788-1",
"Q09472-1",
"Q92793-1",
"Q9Y6Q9-1",
"Q96RS0-1",
"P49336-1",
"Q9BWU1-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-560473",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-560473"
}
]
},
{
"id": "R-HSA-560491",
"name": "Expression of CEBPA",
"equation": "",
"summary": "The CEBPA gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-5640210"
],
"output_participant_list": [
"R-HSA-381289"
],
"enzyme_list": [
"Q15788-1",
"Q09472-1",
"Q92793-1",
"Q9Y6Q9-1",
"P49336-1",
"Q9BWU1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-560491",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-560491"
}
]
},
{
"id": "R-HSA-560493",
"name": "Expression of Perilipin (PLIN)",
"equation": "",
"summary": "The Perilipin (PLIN) gene is transcribed to yield mRNA and the mRNA is translated to yield protein. Expression of Perilipin is upregulated during adipogenesis.",
"cellular_location": "lipid droplet, nucleoplasm",
"input_participant_list": [
"R-HSA-5640178"
],
"output_participant_list": [],
"enzyme_list": [
"Q15788-1",
"Q09472-1",
"Q92793-1",
"Q9Y6Q9-1",
"P49336-1",
"Q9BWU1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-560493",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-560493"
}
]
},
{
"id": "R-HSA-560498",
"name": "Expression of Lipoprotein lipase (LPL)",
"equation": "",
"summary": "The LPL gene is transcribed to yield mRNA and the mRNA is translated to yield protein.",
"cellular_location": "extracellular region, nucleoplasm",
"input_participant_list": [
"R-HSA-5640177"
],
"output_participant_list": [
"R-HSA-174605"
],
"enzyme_list": [
"Q15788-1",
"Q09472-1",
"Q92793-1",
"Q9Y6Q9-1",
"P49336-1",
"Q9BWU1-1",
"Q9BYK8-1",
"P06858-1"
],
"evidence": [
{
"id": "R-HSA-560498",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-560498"
}
]
},
{
"id": "R-HSA-560510",
"name": "Expression of FABP4 (aP2)",
"equation": "",
"summary": "The FABP4 gene is transcribed to yield mRNA and the mRNA is translated to yield protein. Expression of FABP4 is activated during adipogenesis.",
"cellular_location": "lipid droplet, nucleoplasm",
"input_participant_list": [
"R-HSA-5640172"
],
"output_participant_list": [
"R-HSA-163428"
],
"enzyme_list": [
"Q15788-1",
"Q09472-1",
"Q92793-1",
"Q9Y6Q9-1",
"P11802-1",
"P49336-1",
"Q9BWU1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-560510",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-560510"
}
]
},
{
"id": "R-HSA-560517",
"name": "Expression of CD36 (platelet glycoprotein IV, FAT)",
"equation": "",
"summary": "The Platelet glycoprotein IV gene (CD36, PAS IV, GPIV) is transcribed to yield mRNA and the mRNA is translated to yield proteind.",
"cellular_location": "nucleoplasm, plasma membrane",
"input_participant_list": [
"R-HSA-5640184"
],
"output_participant_list": [
"R-HSA-51645"
],
"enzyme_list": [
"Q15788-1",
"Q09472-1",
"Q92793-1",
"Q9Y6Q9-1",
"Q96RS0-1",
"P49336-1",
"Q9BWU1-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-560517",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-560517"
}
]
},
{
"id": "R-HSA-5617874",
"name": "HOXD4 gene is transcribed",
"equation": "",
"summary": "The HOXD4 gene is transcribed to yield mRNA (Moroni et al. 1993, Morrison et al. 1996, Morrison et al. 1997). In mouse embryos Hoxd4 mRNA is observed in rhombomere 7 and caudally in spinal cord and prevertebrae. The HOXD4 promoter region is a target of the microRNA miR-10a, which causes repression of transcription (Tan et al. 2009).",
"cellular_location": "cytosol, nucleoplasm",
"input_participant_list": [
"R-HSA-5617853"
],
"output_participant_list": [
"R-HSA-5617878"
],
"enzyme_list": [
"O15550-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"P24928-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"P30876-1"
],
"evidence": [
{
"id": "R-HSA-5617874",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5617874"
}
]
},
{
"id": "R-HSA-5617896",
"name": "Retinoic acid activates HOXD4 chromatin",
"equation": "",
"summary": "As inferred from mouse embryos, retinoic acid activates the HOXD4 gene in rhombomere 7 (r7) by binding RARB or RARA in RAR:RXR receptor dimers bound to a retinoic acid response element (RAREs) in the 5' flanking region of the gene. Ligand binding by retinoic acid receptors causes dismissal of corepressors such as NCOR1 and recruitment of coactivators such as NCOA3 (Klein et al. 2000). The response of HOXD4 to retinoic acid is also observed in human embryonal carcinoma cells (Moroni et al. 1993, Morrison et al. 1996, Morrison et al. 1997). PAX6 binds near the RARE and is required for maximal activation.
In human fibroblasts chromatin at HOXA genes is activated by loss of methylation at lysine-27 (H3K27me3), loss of Polycomb repressive complex 2 (PRC2), and gain of H3K4me3 (Lan et al. 2007). Similar changes occur at Hoxd4 in mouse embryos. The histone demethylase KDM6A (UTX) binds the HOXD4 gene in human lung fibroblasts and may participate in demethylating H3K27me3 (Lan et al. 2007). Other factors may also be involved in demethylation. KDM6A associates with the histone methyltransferases KMT2C,D (MLL2,3) which may participate in methylating H3K4 (Lee et al. 2007). As inferred from mouse homologs, PCGF2 (MEL18) dissociates from Hoxd4 during activation. After activation by retinoic acid, HOXD4 maintains its own expression by binding and activating its own promoter.",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-193545",
"R-HSA-381325",
"R-HSA-442488"
],
"output_participant_list": [
"R-HSA-389115"
],
"enzyme_list": [
"O15550-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"P24928-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"Q15910-1",
"P30876-1"
],
"evidence": [
{
"id": "R-HSA-5617896",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5617896"
}
]
},
{
"id": "R-HSA-5660660",
"name": "p300 acetylates RELA subunit",
"equation": "",
"summary": "Acetylation of RELA/p65 subunit differentially regulates distinct biological activities of the NF-kB transcription factor complex. The acetylation enables increased DNA binding and transcriptional activity by NF-kB, leading to up-regulated IL6 (interleukin 6), IL10, IL12p35, IL12p40 and IL23p19 production (Geijtenbeek and Gringhuis 2009). Acetyltransferases p300 and CBP are involved in the acetylation of RELA on multiple sites including lysines 122, 123, 218, 221 and 310. Acetylation of lysine 221 by p300/CBP increases the DNA binding affinity of RELA for the IkB enhancer and, together with acetylation of lysine 218, impairs assembly of RELA with newly synthesized IkBalpha, which shuttles in and out of the nucleus. Acetylation of lysine 310 does not modulate DNA binding or IkBalpha assembly but markedly enhances the transcriptional activity of NF-kB (Chen et al. 2002, 2005).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-5660660",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5660660"
}
]
},
{
"id": "R-HSA-5660666",
"name": "CBP and p300 binds NF-kB complex",
"equation": "",
"summary": "The phosphorylation of p65 subunit has been shown to be important for RELA transcriptional activity. Once phosphorylated RELA/p65 has been shown to recruit transcriptional coactivators CREB binding protein (CBP) and p300 (Chen at al. 2002). The association between CBP/p300 and NF-kB p65 occurs through RHD (Rel homology domain) and C-terminal transactivation domain (Zong et al. 1998). Both p300 and CBP contain a histone acetyltransferase (HAT) enzymatic activity that regulates gene expression through acetylation of RELA, and promoter proximal nucleosomal histones, resulting in increased accessibility of the DNA for other essential regulators (Kalkhoven 2004).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-5660666",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5660666"
}
]
},
{
"id": "R-HSA-6797993",
"name": "TP53 and CREBBP bind BNIP3L gene",
"equation": "",
"summary": "In hypoxic cells, TP53 (p53) binds p53 responsive elements in the BNIP3L gene. CREBBP (CBP) also localizes to the BNIP3L gene under hypoxic conditions, in vicinity to some of the p53 response elements, which is probably regulated by HIF1A (Fei et al. 2004).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-6797993",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6797993"
}
]
},
{
"id": "R-HSA-6798004",
"name": "TP53 stimulates BNIP3L expression",
"equation": "",
"summary": "TP53 (p53) and CREBBP (CBP) bound to the BNIP3L gene stimulate expression of the BNIP3L. BNIP3L is an outer mitochondrial membrane protein that belongs to the BCL2 family and promotes apoptosis of cells under hypoxic stress (Fei et al. 2004).",
"cellular_location": "mitochondrial outer membrane, nucleoplasm",
"input_participant_list": [
"R-HSA-6797990"
],
"output_participant_list": [
"R-HSA-6798001"
],
"enzyme_list": [
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-6798004",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6798004"
}
]
},
{
"id": "R-HSA-879724",
"name": "Expression of PPARA",
"equation": "",
"summary": "The PPARA gene is transcribed to yield mRNA and the mRNA is translated to yield protein. As inferred from mouse, BMAL1:CLOCK (ARNTL:CLOCK) heterodimers bind E-box elements in the second intron of the PPARA gene and activate transcription of PPARA.",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-5640195"
],
"output_participant_list": [
"R-HSA-400186"
],
"enzyme_list": [
"Q15788-1",
"Q92793-1",
"O15516-1",
"Q96RS0-1",
"Q86X55-3",
"Q3L8U1-1",
"Q9BYK8-1"
],
"evidence": [
{
"id": "R-HSA-879724",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-879724"
}
]
},
{
"id": "R-HSA-8864307",
"name": "TFAP2 homo- and heterodimers bind CITED and EP300/CREBBP",
"equation": "",
"summary": "Transcriptional co-factors from the CITED family interact with the helix-span-helix (HSH) domain of TFAP2 (AP-2) family of transcription factors and recruit transcription co-activators EP300 (p300) and CREBBP (CBP) to TFAP2-bound DNA elements. CITED2 shows the highest affinity for TFAP2 proteins, followed by CITED4, while CITED1 interacts with TFAP2s with a very low affinity. The interaction with CITED proteins was specifically demonstrated for TFAP2A (AP-2 alpha), TFAP2B (AP2-beta) and TFAP2C (AP-2 gamma), and is extrapolated to TFAP2D (AP2-delta) and TFAP2E (AP-2 epsilon) based on sequence similarity (Braganca et al. 2002, Braganca et al. 2003). Mouse embryos defective for CITED2 exhibit neural crest defects, cardiac malformations and adrenal agenesis, which can at least in part be attributed to defective Tfap2 transactivation (Bamforth et al. 2001).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-8864307",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8864307"
}
]
},
{
"id": "R-HSA-8878220",
"name": "RUNX3 binds the NOTCH1 coactivator complex",
"equation": "",
"summary": "RUNX3 binds the NOTCH1 coactivator complex by directly interacting with the NOTCH1 intracellular domain fragment (NICD1) (Gao et al. 2010).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-8878220",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8878220"
}
]
},
{
"id": "R-HSA-8878237",
"name": "RUNX3:NOTCH1 coactivator complex binds the HES1 gene promoter",
"equation": "",
"summary": "RUNX3, associated with the NOTCH1 coactivator complex, binds to the promoter of the HES1 gene (Gao et al. 2010).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-8878237",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8878237"
}
]
},
{
"id": "R-HSA-8878243",
"name": "HES1 gene transcription is inhibited by RUNX3",
"equation": "",
"summary": "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).",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-2197548"
],
"output_participant_list": [
"R-HSA-210825"
],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-8878243",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8878243"
}
]
},
{
"id": "R-HSA-8938228",
"name": "RUNX1:CBFB:CREBBP binds the CSF2 (GM-CSF) gene promoter",
"equation": "",
"summary": "The complex of the RUNX1:CBFB heterodimer and histone acetyltransferase CREBBP (CBP) binds the promoter of the CSF2 (GM-CSF) gene, encoding Granulocyte-macrophage colony-stimulating factor (Oakford et al. 2010). RUNX1 can also recruit the SWI/SNF complex to the CSF2 gene promoter (Bakshi et al. 2010).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-8938228",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8938228"
}
]
},
{
"id": "R-HSA-8938231",
"name": "RUNX1:CBFB binds CREBBP",
"equation": "",
"summary": "The RUNX1:CBFB complex binds CREBBP (CBP) histone acetyltransferase. The interaction involves the C-terminal domain of RUNX1 (Oakford et al. 2010).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-8938231",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8938231"
}
]
},
{
"id": "R-HSA-8938251",
"name": "CSF2 (GM-CSF) gene expression is stimulated by RUNX1 and CREBBP",
"equation": "",
"summary": "Binding of the RUNX1:CBFB complex associated with the histone acetyltransferase (HAT) CREBBP (CBP) to the promoter of the CSF2 gene, encoding Granulocyte-macrophage colony stimulating factor (GM-CSF), stimulates CSF2 transcription. HAT activity of CREBBP is required for RUNX1-mediated stimulation of CSF2 expression. GM-CSF is involved in myeloid cell differentiation (Oakford et al. 2010). It has not been fully elucidated how recruitment of the SWI/SNF complex to the CSF2 promoter by RUNX1 affects CSF2 transcription (Bakshi et al. 2010).",
"cellular_location": "extracellular region, nucleoplasm",
"input_participant_list": [
"R-HSA-8938235"
],
"output_participant_list": [
"R-HSA-517562"
],
"enzyme_list": [
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-8938251",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8938251"
}
]
},
{
"id": "R-HSA-9016751",
"name": "FABP7 gene expression is positively regulated by NOTCH1 and NOTCH3",
"equation": "",
"summary": "Based on studies in mice, expression of FABP7 (BLBP) in radial glia is positively regulated by NOTCH1 and NOTCH3 during neuronal migration (Anthony et al. 2005, Keilani and Sugaya 2008). The promoter of the mouse Fabp7 gene contains an Rbpj binding site needed for Fabp7 expression (Anthony et al. 2005). Several sites related to the consensus RBPJ binding sequence exist in the human FABP7 gene promoter.",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-9016777"
],
"output_participant_list": [
"R-HSA-5216158"
],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-9016751",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9016751"
}
]
},
{
"id": "R-HSA-9017835",
"name": "NOTCH1 coactivator complex binds NOTCH3 gene",
"equation": "",
"summary": "NOTCH1 and RBPJ (CSL), likely in the form of the NOTCH1 coactivator complex, bind to the RBPJ response elements in the second intron of the NOTCH3 gene (Ohashi et al. 2010).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-9017835",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9017835"
}
]
},
{
"id": "R-HSA-9021450",
"name": "PLXND1 gene expression is stimulated by NOTCH1,NOTCH3 coactivator complexes",
"equation": "",
"summary": "PLXND1 gene transcription is stimulated by NOTCH1 and NOTCH3 coactivator complexes. PLXND1 encodes the semaphorin receptor Plexin-D1, involved in neuronal migration as well as cancer cell invasiveness (Rehman et al. 2016).",
"cellular_location": "nucleoplasm, plasma membrane",
"input_participant_list": [
"R-HSA-9021445"
],
"output_participant_list": [
"R-HSA-209637"
],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-9021450",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9021450"
}
]
},
{
"id": "R-HSA-9021451",
"name": "NOTCH1,NOTCH3 coactivator complex binds PLXND1 gene promoter",
"equation": "",
"summary": "PLXND1 gene promoter possesses an RBPJ-binding site which is necessary for NOTCH1 and NOTCH3-mediated induction of PLXND1 transcription. It is therefore concluded that NOTCH1 and NOTCH3 co-activator complexes directly bind to the PLXND1 gene promoter (Rehman et al. 2016).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-9021451",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9021451"
}
]
},
{
"id": "R-HSA-9038052",
"name": "GREB1 binds ESR1:ESTG and co-activators",
"equation": "",
"summary": "In addition to being an estrogen-responsive target, GREB1 also interacts directly with ESR1 and functions as an coactivator at numerous estrogen-responsive promoters, as assessed in MCF7 cell lines, xenograft models and primary tumors (Mohammed et al, 2013). ESR1-binding coincides with ~95% of GREB1 binding events sites as assessed by ChIP-seq, and expression of up to half of ESR1- and estrogen-dependent genes is compromised when GREB1 expression is silenced, without affecting ESR1 binding. GREB1 may function to stabilize interactions with other coactivators such as EP300 and CREBBP (also known as p300 and CBP, respectively), as co-occupancy with these proteins is lost upon GREB1 silencing (Mohammed et al, 2013). GREB1 expression is high in ER+ cancers and is associated with positive prognosis (Mohammed et al, 2013; reviewed in Hodgkinson and Vanderhyden, 2014).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9038052",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9038052"
}
]
},
{
"id": "R-HSA-933536",
"name": "p-IRF7 dimer interacts with coactivator CBP/p300",
"equation": "",
"summary": "p-IRF7 dimers after translocation into nucleus interact with the coactivators p300 and CBP (CREB-binding protein) to form a stable complex. This interaction further increases the transcriptional activity of IRF7.",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-933536",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-933536"
}
]
},
{
"id": "R-HSA-9604499",
"name": "Expression of Interferon-alpha and beta mediated by VAF/pIRF7:CBP/p300",
"equation": "",
"summary": "The Interferon alpha and beta genes are transcribed and translated yielding IFNA and IFNB which are secreted. IRF7 and VAF transcription factors binds to IFN-alpha and IFN-beta promoter regions and induce the IFN-alpha and beta mRNA.",
"cellular_location": "extracellular region",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9604499",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9604499"
}
]
},
{
"id": "R-HSA-9604664",
"name": "ACTA2 gene expression is stimulated by NOTCH1, NOTCH2 and NOTCH4",
"equation": "",
"summary": "ACTA2 gene, encoding smooth muscle alpha actin, possesses several RBPJ (CSL) response elements in its promoter region. Transcription of ACTA2 is positively regulated by NOTCH1, NOTCH2 and NOTCH4 (Tang et al. 2008).",
"cellular_location": "cytosol, nucleoplasm",
"input_participant_list": [
"R-HSA-8957900"
],
"output_participant_list": [
"R-HSA-445792"
],
"enzyme_list": [
"Q92830-1",
"P62736-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-9604664",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9604664"
}
]
},
{
"id": "R-HSA-9617683",
"name": "EP300,CREBBP bind SOH-C481-FOXO4",
"equation": "",
"summary": "After oxidation of FOXO4 cysteine residues by reactive oxygen species (ROS), FOXO4 forms a complex with a protein acetyltransferase EP300 (p300) or CREBBP (CBP). A covalent disulfide bond between FOXO4 and EP300 or CREBBP facilitates complex formation (Dansen et al. 2009).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9617683",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9617683"
}
]
},
{
"id": "R-HSA-9617758",
"name": "EP300,CREBBP acetylate FOXO4",
"equation": "",
"summary": "EP300 and CREBBP histone acetyltransferases acetylate FOXO4 (Dansen et al. 2009).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-9617761"
],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9617758",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9617758"
}
]
},
{
"id": "R-HSA-9622572",
"name": "NF-Y and CREBBP,EP300 constitutively bind BCL2L11 gene promoter",
"equation": "",
"summary": "Based on studies in rat neurons, the NF-Y transcription factor complex (composed of NFYA, NFYB and NFYC) and histone acetyltransferases EP300 (p300) and/or CREBBP (CBP) constitutively bind to evolutionarily conserved sites in the promoter of the BCL2L11 (BIM) gene (Hughes et al. 2011).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9622572",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9622572"
}
]
},
{
"id": "R-HSA-9622579",
"name": "FOXO1,FOXO3,(FOXO4) bind BCL2L11 gene promoter",
"equation": "",
"summary": "Based on studies in rat neurons, in the absence of PI3K/AKT signaling, as happens under conditions of NGF withdrawal, for example, FOXO transcription factors, FOXO3, FOXO1 and probably also FOXO4 bind evolutionarily conserved forkhead box elements in the promoter of the BCL2L11 (BIM) gene (Gilley et al. 2003) and co-immunoprecipitate with the BCL2L11 promoter-bound NF-Y complex (Hughes et al. 2011).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9622579",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9622579"
}
]
},
{
"id": "R-HSA-9622604",
"name": "BCL2L11 gene expression is stimulated by FOXO1,FOXO3,(FOXO4) and NF-Y",
"equation": "",
"summary": "BCL2L11 (BIM) gene transcription is stimulated by FOXO transcription factors FOXO1 (Gilley et al. 2003), FOXO3 (Gilley et al. 2003, Hughes et al. 2011) and FOXO4 (Urbich et al. 2005, Chuang et al. 2007, Chen et al. 2013, Wang et al. 2016), the NF-Y transcription factor complex (Hughes et al. 2011), and histone acetyltransferases CREBBP and/or EP300 (Hughes et al. 2011). Direct transcriptional regulation of BCL2L11 gene has not been demonstrated for FOXO4. FOXO-mediated upregulation of the pro-apoptotic BCL2L11 plays an important role in NGF withdrawal-induced death of sympathetic neurons (Gilley et al. 2003, Hughes et al. 2011).
FOXO-mediated upregulation of BCL2L11 gene transcription is positively regulated by DDIT3 (CHOP) through an unknown mechanism that may involve binding of DDIT3 to FOXO3 (Ghosh et al. 2012).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9622604",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9622604"
}
]
},
{
"id": "R-HSA-9626928",
"name": "CREBBP binds FOXO1",
"equation": "",
"summary": "Endogenous human histone acetyltransferase CREBBP (CBP) binds to endogenous human FOXO1. The C-terminus of FOXO1 is needed for this interaction (Daitoku et al. 2004).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9626928",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9626928"
}
]
},
{
"id": "R-HSA-9626945",
"name": "CREBBP acetylates FOXO1",
"equation": "",
"summary": "Based on experiments using recombinant human CREBBP and recombinant mouse Foxo1, CREBBP phosphorylates FOXO1 on conserved lysine residues K245, K248 and K265 (these residues correspond to K242, K245 and K262, respectively, in mouse Foxo1) (Daitoku et al. 2004).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9626945",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9626945"
}
]
},
{
"id": "R-HSA-9644900",
"name": "BDNF gene expression is stimulated by NPAS4:ARNT2",
"equation": "",
"summary": "The complex of NPAS4 and ARNT2 directly stimulates transcription of the BDNF gene, based on in vitro studies (Pruunsild et al. 2011). In mouse brain (Lin et al. 2008; Ramamoorthi et al. 2011), Npas4 was also shown to positively regulate Bdnf gene expression. The NPAS4:ARNT2 complex is shown as a set member, while NPAS4:ARNT and NPAS4:ARNTL are shown as set candidates in the context of transcriptional activation of the BDNF gene.
Based on studies in mouse (Funahashi et al. 2019) and rat (Ooe et al. 2009) model systems, neuronal cell stimulation leads to MAPK1 (and probably MAPK3) mediated phosphorylation of NPAS4 on evolutionarily conserved amino acid residues, which increases transcriptional activity of NPAS4 on target gene promoters such as BDNF, possibly by enabling association of NPAS4 with histone acetyltransferase CREBBP (CBP).",
"cellular_location": "endoplasmic reticulum lumen, nucleoplasm",
"input_participant_list": [
"R-HSA-9006123"
],
"output_participant_list": [
"R-HSA-187041"
],
"enzyme_list": [
"P27361-1",
"Q92793-1",
"P28482-1"
],
"evidence": [
{
"id": "R-HSA-9644900",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9644900"
}
]
},
{
"id": "R-HSA-9756494",
"name": "CREBBP acetylates SARS-CoV-2 N at K375",
"equation": "",
"summary": "SARS-CoV-2 nucleocapsid protein (N) can undergo liquid-liquid phase separation (LLPS) with RNA (Wu Y et al. 2021; Wang S et al. 2021; Cubuk J et al. 2021; Lu S et al. 2021). The C-terminal dimerization domain (CTD) of viral N is essential for LLPS (Wu Y et al. 2021; Wang S et al. 2021). Acetylation of viral N at K375, a motif that is adjacent to the CTD, reduced LLPS and its ability to bind RNA (Wang S et al. 2021). Host CREB-binding protein (CREBBP, CBP) mediated acetylation of N at K375 upon co-expression of tagged proteins in human embryonic kidney 293T cells (HEK293T cells), while CREBBP deficiency caused by small interfering RNA (siRNA) inhibited N acetylation (Wang S et al. 2021). Further, SARS-CoV-2 N:RNA LLPS recruited mitochondrial antiviral-signaling protein (MAVS) (Wang S et al. 2021), TGF-beta-activated kinase 1 (TAK1) and I\u03baB kinase (IKK) complexes (Wu Y et al. 2021). The interaction with MAVS supressed MAVS downstream signaling, while N binding to TAK1 or IKBKB enhanced NB-kappaM activation. CTD of N was essential for these interactions (Wu Y et al. 2021; Wang S et al. 2021). The data suggest that acetylation of viral N at K375 abrogates its LLPS and the N-mediated modulation of host antiviral responses.",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [
"R-COV-9756485"
],
"enzyme_list": [
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9756494",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9756494"
}
]
},
{
"id": "R-HSA-9759141",
"name": "AcK-NFE2L2, CHD6 and MAFK bind NQO1 gene",
"equation": "",
"summary": "The NQO1 gene encodes an NAD(P)H dehydrogenase quinone 1 enzyme. NQO1 is one of a number of drug metabolism genes upregulated by the NFE2L2:KEAP1 pathway in response to oxidative stress and a chemically diverse group of compounds now known as \\phase II inducers\\ (Rangsamy et al, 2004; Malhotra et al, 2010; reviewed in Baird and Yamamoto, 2000). NFE2L2 binds to the anti-oxidant response element (ARE) as a heterodimer with small MAF proteins like MAFK and upregulates NQO1 expression (Itoh et al, 1997; McMahon et al, 2001; Rangasamy et al, 2004; Malhotra et al, 2010). Binding and transcriptional activation by NFE2L2 at the NQO1 promoter is enhanced by CREBBP or EP300-mediated acetylation of NFE2L2 at 18 sites in the N-terminal Neh1 domain (Sun et al, 2009). NEF2L2 additionally interacts with the ATP-dependent chromatin remodeller CHD6 through the NFE2L2 C-terminal Neh3 domain (Nioi et al, 2005). Whether CHD-mediated ATP hydrolysis contributes to NQO1 gene expression has not been explicitly determined, but RNAi-knockdown of CHD6 expression abrogates basal and induced NQO1 expression in HeLa cells (Nioi et al, 2005).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1",
"Q8TD26-1"
],
"evidence": [
{
"id": "R-HSA-9759141",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9759141"
}
]
},
{
"id": "R-HSA-9759186",
"name": "AcK-NFE2L2- dependent NQO1 gene expression",
"equation": "",
"summary": "NQO1 (NAD(P)H:Quinone acceptor oxidoreductase type1) catalyzes the two-electron reduction of quinones to hydroquinones (Faig et al, 2000). This reaction bypasses the one electron reduction of these substrates by P450 reductase, which generates reactive oxygen species (ROS) and consequent stress and damage (reviewed in Ross and Siegel, 2021). NQO1 expression is upregulated by NFE2L2, CHD6 and MAFK binding to the antioxidant response element (ARE) in the promoter in response to stimulus by phase II inducers (oxidative and electrophillic stressors) (Itoh et al, 1997; McMahon et al, 2001; Nioi et al, 2005). These inducers activate the NFE2L2-KEAP1 pathway, stabilizing NFE2L2 and allowing it to enter the nucleus to activate expression of target genes (reviewed in Baird and Yamamoto, 2000)",
"cellular_location": "cytosol, nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1",
"Q8TD26-1",
"P15559-1"
],
"evidence": [
{
"id": "R-HSA-9759186",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9759186"
}
]
},
{
"id": "R-HSA-9759332",
"name": "AcK-NFE2L2 binds the TXNRD1 promoter",
"equation": "",
"summary": "TXNRD1 expression is regulated downstream of the KEAP1-NFE2L2 pathway in response to oxidative and electrophilic stress (Kwak et al, 2003; Kim et al, 2001; Malhotra et al, 2010; reviewed in Baird and Yamamoto, 2020). NFE2L2 binds the antioxidant response element (ARE) as assessed by ChIP in mouse studies. Expression of TXNRD1 is significantly upregulated in the absence of KEAP1, marking it as an inducible NFE2L2 target gene (Malhotra et al, 2010). Binding and transcriptional activation by NFE2L2 at the TXNRD1 promoter is enhanced by CREBBP- or EP300-mediated acetylation of NFE2L2 at 18 residues in the N-terminal Neh1 domain (Sun et al, 2009).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9759332",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9759332"
}
]
},
{
"id": "R-HSA-9759364",
"name": "AcK-NFE2L2-dependent TXNRD1 gene expression",
"equation": "",
"summary": "TXNRD1 gene expression is upregulated in response to oxidative and electrophilic stressors in a way that depends on the KEAP1-NFE2L2 pathway (Kwak et al, 2003; Kim et al, 2001; Malhotra et al, 2010; reviewed in Baird and Yamamoto, 2020).",
"cellular_location": "cytosol, nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q16881-1",
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9759364",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9759364"
}
]
},
{
"id": "R-HSA-9760081",
"name": "CREBBP, EP300 acetylates NFE2L2",
"equation": "",
"summary": "NFE2L2 is acetylated by EP300 and CREBBP in vitro and in vivo. Acetylation occurs primarily at 18 residues in the N-terminal DNA-binding domain of Neh1, and increases (but is not absolutely required for) the transcriptional activity of NFE2L2 at some target promoters (Sun et al, 2009).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9760081",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9760081"
}
]
},
{
"id": "R-HSA-9760082",
"name": "NFE2L2 binds CREBBP,EP300",
"equation": "",
"summary": "NFE2L2 binds to CREBBP (also known as CBP, Creb-binding partner) and EP300 (p300) as assessed by co-immunoprecipitation and pulldown experiments. The interaction is mediated by the Neh5 domain of NFE2L2 and the C-terminal residues 1725-2414 of EP300. Both EP300 and CREBBP are able to acetylate NFE2L2 in vitro and in vivo leading to enhanced DNA-binding and transcriptional activation at some but not all NFE2L2-dependent promoters (Sun et al, 2009).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9760082",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9760082"
}
]
},
{
"id": "R-HSA-9760097",
"name": "AcK-NFE2L2 and MAFK bind the GSTA1 gene",
"equation": "",
"summary": "Phosphorylated, acetylated NFE2L2 binds to the antioxidant response element (ARE) in the promoter of the GSTA1 gene as assessed by electrophoretic mobility shift assay in mouse and stimulates GSTA1 expression (Itoh et al, 1997; Thimmulappa et al, 2002; Sun et al, 2009). GSTA1 protein expressed downstream of the KEAP1:NFE2L2 pathway contributes to the antioxidant response by catalyzing the nucleophilic attack of glutathione on endogenous and exogenous electrophilic compounds (reviewed in Baird and Yamamoto, 2020; Chatterjee et al, 2018).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9760097",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9760097"
}
]
},
{
"id": "R-HSA-9760099",
"name": "AcK-NFE2L2 binds the GCLC gene",
"equation": "",
"summary": "The GCLC gene encodes the catalytic heavy chain subunit of glutamine cysteine ligase. This enzyme contributes to the antioxidant response by synthesizing glutathione from glutamate and cysteine, and is a target gene of the KEAP1:NFE2L2 pathway (Sekhar et al, 2000; McMahon et al, 2001; Thimmulappa et al, 2002). Acetylation of NFE2L2 by CREBBP or EP300 increases the DNA-binding and transcription factor binding activity of NFE2L2 at the GCLC promoter (Sun et al, 2009).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9760099",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9760099"
}
]
},
{
"id": "R-HSA-9760103",
"name": "AcK-NFE2L2 binds the GCLM gene",
"equation": "",
"summary": "Phosphorylated, acetylated NFE2L2 binds to the antioxidant response element in the promoter of the GCLM gene as assessed by chromatin immunoprecipitation. Acetylation of NFE2L2 increases, but is not essential for, NFE2L2 DNA binding and transcription factor activity at the GCLM promoter (Sun et al, 2009). The GCLM gene encodes the regulatory subunit of glutamate-cysteine ligase, an enzyme responsible for one step in the synthesis of glutathione (reviewed in Lu, 2013). GCLM expression is downstream of the KEAP1-NFE2L2 pathway (Sekhat et al, 2000; McMahon et al, 2001; Thimmulappa et al, 2002; reviewed in Baird and Yamamoto, 2020; Lu, 2013).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9760103",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9760103"
}
]
},
{
"id": "R-HSA-9760122",
"name": "AcK-NFE2L2-dependent GCLC gene expression",
"equation": "",
"summary": "The GCLC gene encodes the catalytic subunit of glutamate-cysteine ligase, which produces glutathione from glutamate and cysteine. Glutathione contributes to the antioxidant response by reducing peroxides, detoxifying and exporting xenobiotic agents and acting as a redox buffer reviewed in Lu, 2013). GCLC expression is regulated in part by the binding of acetylated NFE2L2 to the anti-oxidant response element (ARE) in its promoter (Sun et al, 2009; Sekhar et al, 2000; McMahon 2001; Thimmulappa et al, 2002; reviewed in Lu, 2013).",
"cellular_location": "cytosol, nucleoplasm",
"input_participant_list": [
"R-HSA-5662569"
],
"output_participant_list": [
"R-HSA-174385"
],
"enzyme_list": [
"P48506-1",
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9760122",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9760122"
}
]
},
{
"id": "R-HSA-9760125",
"name": "AcK-NFE2L2-dependent GCLM gene expression",
"equation": "",
"summary": "The GCLM gene encodes the regulatory subunit of glutamate-cysteine ligase, an enzyme that ligates glutamate and cysteine as one step in the synthesis of glutathione. Glutathione contributes to the antioxidant response by reducing peroxides, neutralizing and promoting the export of xenobiotic agents and by acting as a redox buffer (reviewed in Lu, 2013). Expression of GCLM is dependent in part on the binding of NFE2L2 to the antioxidant response element (ARE) in the promoter (Sekhar et al, 2000; McMahon et al, 2001; Thimmulappa et al, 2002). Binding and transcription factor activity are enhanced by previous NFE2L2 acetylation mediated by CREBBP or EP300 (Sun et al, 2009).",
"cellular_location": "cytosol, nucleoplasm",
"input_participant_list": [
"R-HSA-9760036"
],
"output_participant_list": [
"R-HSA-174356"
],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9760125",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9760125"
}
]
},
{
"id": "R-HSA-9760128",
"name": "AcK-NFE2L2-dependent GSTA1 gene expression",
"equation": "",
"summary": "Gluthathione-S-transferase contributes to the antioxidant response by catalyzing the conjugation of glutathione to a range of endogenous and exogenous compounds, including peroxides and other oxidizing agents (reviewed in Chatterjee et al, 2018; Baird and Yamamoto, 2020). GSTA1 expression is driven in part by the binding of a heterodimer of MAFK and acetylated NFE2L2 to the antioxidant response element (ARE) in the promoter (Itoh et al, 1997; Thimmulappa et al, 2002; Sun et al, 2009).",
"cellular_location": "cytosol, nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1",
"P08263-1"
],
"evidence": [
{
"id": "R-HSA-9760128",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9760128"
}
]
},
{
"id": "R-HSA-9761812",
"name": "AcK- NFE2L2, MAFG and CREBBP, EP300 bind the G6PD",
"equation": "",
"summary": "Cytosolic glucose-6-phosphate dehydrogenase (G6PD) catalyzes the reaction of glucose 6-phosphate and NADP+ to form D-glucono-1,5-lactone 6-phosphate and NADPH + H+. This constitutes the first committed step of the pentose phosphate pathway and it is critical to the maintenance of NAPDH pool and redox homeostasis (reviewed in Hayes et al, 2020; Ge et al, 2020; Lin et al, 2016; Harris and DeNicola, 2020). G6PD expression is regulated downstream of the KEAP1-NFE2L2 pathway (Wu et al, 2011; Thimmulappa et al, 2002; reviewed in Baird and Yamamoto, 2020). Expression is mediated by the binding of the NFE2L2:MAFG heterodimer to the anti-oxidant response element in the G6PD promoter. CREBBP is likewise recruited upon stimulation with the NFE2L2-inducer diethyl malate (DEM), and DEM treatment increases the accumulation of histone modifications associated with a transcriptionally active state (Hirotsu et al, 2012; Mitsuishi et al, 2012; Tang et al, 2021; reviewed in Hayes et al, 2020).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9761812",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9761812"
}
]
},
{
"id": "R-HSA-9761815",
"name": "AcK-NFE2L2 and ATF4 bind the SLC7A11 gene",
"equation": "",
"summary": "SLC7A11 encodes one component of system xc-, a heterodimeric high affinity cystine-glutamate transporter that imports cystine in exchange for glutamate; the other protein component of the heterodimer is SLC3A2 (reviewed in Lewerenz et al, 2013). System xc- contributes to redox balance of the cell by increasing intracellular stores of cysteine, a limiting component in the synthesis of the key antioxidant glutathione (GSH). Depletion of GSH, for instance by inhibition of SLC7A11, causes lipid peroxidation and stimulates ferroptosis, a regulated form of cell death (reiewed in Chen et al, 2021; Kuang et al, 2020; Kajarabille and Latunde-Dada, 2019).; NFE2L2 is a major transcriptional regulator of genes involved in mitigating oxidative stress, and as such effectively acts as a negative regulator of the ferroptosis pathway (reviewed in Baird and Yamamoto, 2020; Kuang et al, 2020; Chen et al, 2021). SLC7A11 expression is upregulated in response to NFE2L2 inducers and has been shown to be a direct downstream target of NFE2L2 and ATF4 (Ye et al, 2014; Ishii et al, 2000; Sasaki et al, 2002; Chen et al, 2017; Dong et al, 2020; reviewed in Kuang et al, 2020; Kajarabille and Latunde-Dada, 2019). CREBBP also co-immunoprecipitates with NFE2L2 at the SLC7A11, and CREBBP-dependent acetylation of NFE2L2 is required for promoter binding and transcriptional activation (Chen et al, 2017; Sun et al, 2009). The acetylation activity of CREBBP is inhibited by interaction between p14ARF and NFE2L2 at the SLC7A11 promoter (Chen et al, 2017).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9761815",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9761815"
}
]
},
{
"id": "R-HSA-9761828",
"name": "NFE2L2 binds the PGD gene",
"equation": "",
"summary": "Phosphogluconate dehydrogenase (PGD, also known as 6PGDH) is an enzyme involved in the pentose phosphate pathway (PPP). The PPP is an alternative glucose metabolism pathway that branches off from glycolysis, consuming the shared metabolite glucose-6-phosphate to produce fructose-6-phosphate and glyceraldehyde-3-phosphate in the oxidative and non-oxidative branches, respectively. The PPP generates NADPH in place of ATP and is a source of biosynthetic intermediates required for nucleic acid, fatty acid and amino acid generation. Cells may switch to the PPP to support phases of highly proliferative growth, and also as a response to oxidative stress (reviewed in Ge et al, 2020; Hayes et al, 2020).
PGD catalyzes the third step of the oxidative branch of the PPP, the conversion of 6-phosphogluconate to ribulose-5-phosphate (Ru5P), and simultaneously generates NADPH. Ru5P is an intermediate on the synthetic pathway for nucleic acids and NADPH contributes reducing power needed for the synthesis of fatty acids, nucleotides and non-essential amino acids. PGD expression is regulated in part by the binding of NFE2L2 and MAFG to the antioxidant response element (ARE) in the promoter (Ong et al, 2020; Mitsuishi et al, 2012; Hirotsu et al, 2012). CREBBP is also recruited to the PDG promoter in response to treatment of mouse cells with the NFE2L2 inducer diethyl maleate (DEM), and is associated with acquistion of histone modifications indicative of transcriptional activation (Hirotsu et al, 2012). Although recruitment of CREBBP/EP300 with NFE2L2 has been associated with NFE2L2 acetylation at other target gene promoters, this has not been directly demonstrated in the case of the PGD gene (Sun et al, 2009).
Keap1-NFE2L2-dependent regulation of PGD contributes to metabolic reprogramming during initiation of cancer as well as to the response to oxidative stress (Thimmaluppa et al, 2002; Wu et al, 2011; reviewed in Baird and Yamamoto, 2020; Ge et al, 2020; Hayes et al, 2020).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9761828",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9761828"
}
]
},
{
"id": "R-HSA-9761836",
"name": "p14ARF binds NFE2L2:CREBBP, EP300",
"equation": "",
"summary": "p14ARF binds to NFE2L2 and inhibits its CREBBP/EP300-dependent acetylation (Chen et al, 2017). Acetylation has been shown to contribute to DNA-binding and therefore transcription factor activity at some NFE2L2 target genes (Sun et al, 2009). Consistent with this, binding of p14ARF to NFE2L2 inhibits the expression of SLC7A11, an NFE2L2 target with roles in suppressing ferroptosis (Chen et al, 2017; Ishii et al, 2000; reviewed in Baird and Yamamoto, 2020; Kuang et al, 2020; Kajarabille and Latunda-Dada, 2019).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9761836",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9761836"
}
]
},
{
"id": "R-HSA-9761841",
"name": "AcK-NFE2L2-dependent SLC7A11 expression",
"equation": "",
"summary": "SLC7A11 encodes one component of system xc-, a heterodimeric high affinity cystine-glutamate transporter that imports cystine in exchange for glutamate; the other protein component of the heterodimer is SLC3A2 (reviewed in Lewerenz et al, 2013). System xc- contributes to redox balance of the cell by increasing intracellular stores of cysteine, a limiting component in the synthesis of the key antioxidant glutathione (GSH). Depletion of GSH, for instance by inhibition of SLC7A11, causes lipid peroxidation and stimulates ferroptosis, a regulated form of cell death (reiewed in Chen et al, 2021; Kuang et al, 2020; Kajarabille and Latunde-Dada, 2019).; Expression of SLC7A11 is regulated downstream of the KEAP1:NFE2L2 pathway in response to oxidative stress. NFE2L2 and SLC7A11 are therefore both negative regulators of ferroptosis (Ye et al, 2014; Ishii et al, 2000; Sasaki et al, 2002; Chen et al, 2017; Dong et al, 2020; reviewed in Baird and Yamamoto, 2020; Kuang et al, 2020; Chen et al, 2021).",
"cellular_location": "nucleoplasm, plasma membrane",
"input_participant_list": [
"R-HSA-9761709"
],
"output_participant_list": [
"R-HSA-378515"
],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9761841",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9761841"
}
]
},
{
"id": "R-HSA-9761846",
"name": "NFE2L2-dependent PGD gene expression",
"equation": "",
"summary": "Phosphogluconate 6-dehydrogenase catalyzes the third step of the pentose phosphate pathway (PPP), an alternate glucose metabolic pathway that shares intermediates with glycolysis. PPP generates NADPH through its oxidative and non-oxidative branches, as well as biosynthetic intermediates required for the generation of nucleic acids, sterols, fatty acids and amino acids. Cells can switch to the PPP pathway in place of glycolysis and oxidative phosphorylation in times of high biosynthetic need, like proliferation, and also in response to oxidative stress, as the NADPH generated contributes to the redox potential of the cell (reviewed in Ge et al, 2020; Hayes et al, 2020; Baird and Yamamoto, 2020).
PGD expression is regulated downstream of NFE2L2 through binding of the transcription factor to anti-oxidant response elements in the promoter (Thimmulappa et al, 2002; Wu et al, 2011; Ong et al, 2020; Mitsuishi et al, 2012; reviewed in Baird and Yamamoto, 2020). Knockdown of PGD expression reduced the proliferation and colony formation of HepG2 cells and also downregulated expression of NFE2L2, suggesting the existence of a positive feedback loop (Ong et al, 2020).",
"cellular_location": "cytosol, nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P52209-1",
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9761846",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9761846"
}
]
},
{
"id": "R-HSA-9761849",
"name": "AcK-NFE2L2-dependent P6GD gene expression",
"equation": "",
"summary": "Glucose-6-phosphate dehydrogenase (G6PD) catalyzes the first, rate limiting step of the pentose phosphate pathway (PPP). The PPP is an alternate glucose metabolic pathway that shares intermediates with glycolysis. PPP generates NADPH through its oxidative and non-oxidative branches, as well as biosynthetic intermediates required for the generation of nucleic acids, sterols, fatty acids and amino acids. Cells can switch to the PPP pathway in place of glycolysis and oxidative phosphorylation in times of high biosynthetic need, like proliferation, and also in response to oxidative stress, as the NADPH generated contributes to the redox potential of the cell (reviewed in Ge et al, 2020; Hayes et al, 2020; Baird and Yamamoto, 2020).
G6PD expression is regulated downstream of the KEAP1-NFE2L2 pathway and depends on the binding of an NFE2L2:MAFG heterodimer to the antioxidant response element in the promoter (Hirotsu et al, 2012; Mitsuishi et al, 2012; Thimmulappa et al, 2002; Wu et al, 2011; reviewed in Baird and Yamamoto, 2020; Ge et al, 2020).",
"cellular_location": "cytosol, nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1",
"P11413-1"
],
"evidence": [
{
"id": "R-HSA-9761849",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9761849"
}
]
},
{
"id": "R-HSA-9793383",
"name": "Expression of TBX6 in paraxial mesoderm",
"equation": "",
"summary": "TBX6 is expressed in the primitive streak and then continues in the paraxial mesoderm (Xi et al. 2017 and inferred from the mouse homolog). NOTCH signaling acting through RBPJ directly activates expression of TBX6 in paraxial mesoderm (inferred from mouse homologs). WNT signaling and FGF signaling also directly or indirectly activate expression of TBX6 in paraxial mesoderm (inferred from mouse homologs). TBXT is not required for initial activation of TBX6 expression, but is required for maintenance of TBX6 expression (inferred from mouse homologs). Mesogenin1 (MSGN1), which is itself activated by TBX6, activates TBX6 in a reinforcing loop (inferred from mouse homologs).",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-9793371"
],
"output_participant_list": [
"R-HSA-9793377"
],
"enzyme_list": [
"Q92830-1",
"P11362-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-9793383",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9793383"
}
]
},
{
"id": "R-HSA-9793400",
"name": "NOTCH1 coactivator complex binds the TBX6 gene",
"equation": "",
"summary": "NOTCH signaling activates TBX6 expression in paraxial mesoderm via RBPJ, which binds a site in the promoter of the TBX6 gene (inferred from mouse and Drosophila homologs). RBPJ is inferred to bind other members of the NOTCH1 coactivator complex in order to activate transcription of TBX6.",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-9793400",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9793400"
}
]
},
{
"id": "R-HSA-9796039",
"name": "AcK-NFE2L2 binds the ABCF2 gene",
"equation": "",
"summary": "ABCF2 is an NFE2L2 target gene that contains a functional ARE sequence in the promoter which is confirmed through ChIP assay in Human Ovarian cancer cell-lines (Bao et al, 2017).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796039",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796039"
}
]
},
{
"id": "R-HSA-9796040",
"name": "NFE2L2 dependent KEAP1 expression",
"equation": "",
"summary": "NFE2L2 (NRF2) controls its own degradation by regulating the expression and induction of the INrf2 (KEAP1) gene. The antioxidant treatment of cells led to nuclear localization and stabilization of Nrf2 and induction of INrf2 gene expression (PMID: 17925401)",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-8962726"
],
"output_participant_list": [
"R-HSA-976038"
],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796040",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796040"
}
]
},
{
"id": "R-HSA-9796042",
"name": "NFE2L2 dependent ABCF2 expression",
"equation": "",
"summary": "ABCF2 is an NFE2L2 target gene that contains a functional ARE sequence in the promoter which is confirmed through ChIP assay in Human Ovarian cancer cell lines. It has role in Cisplatin resistance (Bao et al, 2017)",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-9795737"
],
"output_participant_list": [
"R-HSA-5215945"
],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796042",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796042"
}
]
},
{
"id": "R-HSA-9796043",
"name": "NFE2L2 dependent BCL2L1 expression",
"equation": "",
"summary": "NFE2L2 in control of BCL2L1 expression and apoptotic cell death with implications in antioxidant protection, survival of cancer cells, and drug resistance. (Niture et al, 2013)",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796043",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796043"
}
]
},
{
"id": "R-HSA-9796044",
"name": "NFE2L2 dependent EGF expression",
"equation": "",
"summary": "NFE2L2 regulating EGFR signalling in Melanoma cells by inducing EGF expression (Kreb et al, 2021)",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-9795740"
],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796044",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796044"
}
]
},
{
"id": "R-HSA-9796045",
"name": "NFE2L2 dependent TXN expression",
"equation": "",
"summary": "NFE2L2 regulates the expression of TXN (Thioredoxin) by binding to ARE element present on TXN promoter and regulating anti-oxidant response (Hawkes et al, 2014; Tanito et al, 2005; Kim et al, 2001).",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-9795738"
],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796045",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796045"
}
]
},
{
"id": "R-HSA-9796048",
"name": "AcK-NFE2L2 binds the ABCG2 gene",
"equation": "",
"summary": "A detailed promoter analysis using luciferase reporter assays showed that ARE at -431 to -420 bp is critical for the NFE2L2-mediated expression in lung cancer cells. Electrophoretic mobility shift assays and chromatin immunoprecipitation assays revealed that NFE2L2 interacts with the ABCG2 ARE element at -431 to -420 bp in vitro and in vivo (Singh et al, 2010)
",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796048",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796048"
}
]
},
{
"id": "R-HSA-9796049",
"name": "AcK-NFE2L2 binds the SOD3 gene",
"equation": "",
"summary": "SOD3 is under transcriptional control of NFE2L2 and contains a functional antioxidant response element confirmed by ChIP assay in MCF-10A Cells (Singh et al, 2012, Folz et al, 1994)",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796049",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796049"
}
]
},
{
"id": "R-HSA-9796050",
"name": "AcK-NFE2L2 binds the KEAP1 gene",
"equation": "",
"summary": "NFE2L2 (NRF2) controls its own degradation by regulating the expression and induction of the INrf2 (KEAP1) gene. The antioxidant treatment of cells led to nuclear localization and stabilization of Nrf2 and induction of INrf2 gene expression (PMID: 17925401)",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796050",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796050"
}
]
},
{
"id": "R-HSA-9796051",
"name": "AcK-NFE2L2 binds the AREG gene",
"equation": "",
"summary": "The knockdown of NFE2L2 and KEAP1 via short hairpin RNA in BEAS-2B cells and an EMSA with lung tissue revealed that AREG is regulated by NFE2L2 (Reiss et al, 2014).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796051",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796051"
}
]
},
{
"id": "R-HSA-9796054",
"name": "NFE2L2 negatively regulates IL8 mRNA degradation",
"equation": "",
"summary": "The dominant mechanism of NFE2L2-mediated IL8 induction is through mRNA stabilization (Zhang et al, 2005)
",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796054",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796054"
}
]
},
{
"id": "R-HSA-9796055",
"name": "NFE2L2 dependent BCL2 expression",
"equation": "",
"summary": "NFE2L2 upregulates BCL2 expression and apoptotic cell death with implications in antioxidant protection, survival of cancer cells, and drug resistance. (Niture et al 2012)",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796055",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796055"
}
]
},
{
"id": "R-HSA-9796057",
"name": "NFE2L2 dependent AREG expression",
"equation": "",
"summary": "The knockdown of NFE2L2 and KEAP1 via short hairpin RNA in BEAS-2B cells and an EMSA with lung tissue revealed that AREG is regulated by NFE2L2. AREG (Amphiregulin) plays role in EGFR signalling (Reiss et al, 2014)",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-9795733"
],
"output_participant_list": [
"R-HSA-5689438"
],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796057",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796057"
}
]
},
{
"id": "R-HSA-9796058",
"name": "AcK-NFE2L2 binds the TXN gene",
"equation": "",
"summary": "NFE2L2 regulates the expression of TXN (Thioredoxin) by binding to ARE element present on TXN promoter confirmed through ChIP and EMSA assay in K562 cells (Hawkes et al, 2014; Tanito et al, 2005; Kim et al, 2001).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796058",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796058"
}
]
},
{
"id": "R-HSA-9796059",
"name": "AcK-NFE2L2 binds the BCL2 gene",
"equation": "",
"summary": "NFE2L2 upregulates BCL2 expression and apoptotic cell death with implications in antioxidant protection, survival of cancer cells, and drug resistance. Mutagenesis and transfection assays identified an antioxidant response element between nucleotides -3148 and -3140 on the reverse strand of the Bcl-2 gene promoter that was essential for the activation of Bcl-2 gene expression (Niture et al 2012)",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796059",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796059"
}
]
},
{
"id": "R-HSA-9796060",
"name": "NFE2L2 dependent NFE2L2 expression",
"equation": "",
"summary": "NFE2L2 regulates its own expression thus forming a self-regulatory loop that helps to build up the NFE2L2 response in stress conditions and provides protective support (Kwak et al, 2002)",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796060",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796060"
}
]
},
{
"id": "R-HSA-9796061",
"name": "NFE2L2 dependent ATF4 expression",
"equation": "",
"summary": "Stress induction of ATF4 is significantly regulated transcriptionally through an NFE2L2-dependent mechanism. This helps in regulating the oxidative stress impact (Miyamoto et al, 2011, DeNicola et al, 2015)",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-9795746"
],
"output_participant_list": [
"R-HSA-381084"
],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796061",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796061"
}
]
},
{
"id": "R-HSA-9796064",
"name": "AcK-NFE2L2 binds the NOTCH1 gene",
"equation": "",
"summary": "NFE2L2 appears to directly affect Notch1 expression in MEFs and this is likely mediated by the binding of NFE2L2 to a regulatory domain(s) in the \u22121640 proximal promoter of Notch1 (Wakabayashi et al, 2010; Kim et al, 2014).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796064",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796064"
}
]
},
{
"id": "R-HSA-9796065",
"name": "AcK-NFE2L2 binds the ABCC3 gene",
"equation": "",
"summary": "ABCC3 is under transcriptional control of NFE2L2 and contains a functional antioxidant response element within the eighth intron of the human ABCC3 gene. The same has been confirmed through ChIP and Pull-down assay (Canet et al, 2015; Pellegatta et al, 2019)
",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796065",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796065"
}
]
},
{
"id": "R-HSA-9796066",
"name": "AcK-NFE2L2 binds the CCL2 gene",
"equation": "",
"summary": "CCL2 expression is regulated by NFE2L2 and the same has been validated through ChIP assay and ELISA. (Huang et al, 2021)",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796066",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796066"
}
]
},
{
"id": "R-HSA-9796068",
"name": "AcK-NFE2L2 binds the ATF4 gene",
"equation": "",
"summary": "Stress induction of ATF4 is significantly regulated transcriptionally through an NFE2L2-dependent mechanism. NFE2L2 binding to ATF4 promoter is confirmed by ChIP assay. (Miyamoto et al, 2011, DeNicola et al, 2015)
",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796068",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796068"
}
]
},
{
"id": "R-HSA-9796069",
"name": "AcK-NFE2L2 binds the PDGFA gene",
"equation": "",
"summary": "NFE2L2 binding to the PDGFA promoter and recruits SP1 on it to facilitate PDGFA expression. (Liu et al, 2016))",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796069",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796069"
}
]
},
{
"id": "R-HSA-9796070",
"name": "NFE2L2 dependent CCL2 expression",
"equation": "",
"summary": "CCL2 expression is regulated by NFE2L2 and it plays role in M2 macrophage recruitment (Huang et al, 2021)",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-443967"
],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796070",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796070"
}
]
},
{
"id": "R-HSA-9796071",
"name": "NFE2L2 dependent NOTCH1 expression",
"equation": "",
"summary": "NFE2L2 appears to directly affect Notch1 expression in MEFs and this is likely mediated by the binding of NFE2L2 to a regulatory domain(s) in the \u22121640 proximal promoter of NOTCH1. NOTCH1 plays role in tissue regeneration and hematopoietic reconstitution following myelosuppressive radiation (Wakabayashi et al, 2010; Kim et al, 2014).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-9793912"
],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796071",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796071"
}
]
},
{
"id": "R-HSA-9796074",
"name": "NFE2L2 dependent ABCC1 expression",
"equation": "",
"summary": "NFE2L2 regulated ABCC1 (MRP1) in small cell lung cancer which plays role in multidrug resistance (Ji et al, 2013)",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-9795735"
],
"output_participant_list": [
"R-HSA-266068"
],
"enzyme_list": [
"Q09472-1",
"Q92793-1",
"P33527-1"
],
"evidence": [
{
"id": "R-HSA-9796074",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796074"
}
]
},
{
"id": "R-HSA-9796075",
"name": "NFE2L2 dependent SOD3 expression",
"equation": "",
"summary": "SOD3 is under transcriptional control of NFE2L2 and plays role in antioxidant response in extracellular space (Singh et al, 2012, Folz et al, 1994)",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-9795749"
],
"output_participant_list": [
"R-HSA-3299690"
],
"enzyme_list": [
"Q09472-1",
"Q92793-1",
"P08294-1"
],
"evidence": [
{
"id": "R-HSA-9796075",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796075"
}
]
},
{
"id": "R-HSA-9796076",
"name": "NFE2L2 dependent ABCG2 expression",
"equation": "",
"summary": "Expression of ABCG2 (BCRP) is regulated by NFE2L2 in cancer cells that confer side population and chemoresistance phenotype (Singh et al, 2010)",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-9795742"
],
"output_participant_list": [
"R-HSA-917929"
],
"enzyme_list": [
"Q9UNQ0-1",
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796076",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796076"
}
]
},
{
"id": "R-HSA-9796077",
"name": "AcK-NFE2L2 binds the ABCC1 gene",
"equation": "",
"summary": "The promoter of ABCC1 (MRP1) contains two ARE sites occupied by NFE2L2 which is confirmed through ChIP and induced its expression under oxidative stress conditions (Ji et al, 2013)
",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796077",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796077"
}
]
},
{
"id": "R-HSA-9796079",
"name": "NFE2L2 dependent ABCC3 expression",
"equation": "",
"summary": "ABCC3 is under transcriptional control of NFE2L2 and contains a functional antioxidant response element within the eighth intron of the human ABCC3 gene (Canet et al, 2015; Pellegatta et al, 2019). It plays a significant role in multidrug resistance.",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-9795747"
],
"output_participant_list": [
"R-HSA-194172"
],
"enzyme_list": [
"Q09472-1",
"Q92793-1",
"O15438-1"
],
"evidence": [
{
"id": "R-HSA-9796079",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796079"
}
]
},
{
"id": "R-HSA-9796080",
"name": "AcK-NFE2L2 binds the NFE2L2 gene",
"equation": "",
"summary": "NFE2L2 regulates its own expression by interacting with its own promoter which contains ARE elements. ChIP and EMSA assay is conducted to validate the same (Kwak et al, 2002). This self-regulatory loop helps to build up the NFE2L2 response in stress conditions and provides protective support.",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796080",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796080"
}
]
},
{
"id": "R-HSA-9796082",
"name": "AcK-NFE2L2 binds the EGF gene",
"equation": "",
"summary": "ChIP-sequencing data show that NFE2L2 directly binds to the promoter of EGF, which contains a canonical antioxidant response element (Kreb et al, 2021)",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796082",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796082"
}
]
},
{
"id": "R-HSA-9796084",
"name": "AcK-NFE2L2 binds the BCL2L1 gene",
"equation": "",
"summary": "NFE2L2 in control of BCL2L1 expression and apoptotic cell death with implications in antioxidant protection, survival of cancer cells, and drug resistance. Promoter mutagenesis, transfection, and chromatin immunoprecipitation assays identified an ARE between nucleotides -608 and -600 in the forward strand of the proximal BCL2L1 promoter that bound to NFE2L2 and led to increased BCL2L1 gene expression (Niture et al, 2013)",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9796084",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9796084"
}
]
},
{
"id": "R-HSA-9816396",
"name": "DUX4, TPRXL, TPRX1, TPRX2, EP300, and CREBBP bind the ZSCAN4 gene",
"equation": "",
"summary": "DUX4 binds four sites in the upstream promoter and enhancer region of ZSCAN4 (Geng et al. 2012, De Iaco et al. 2017) and a site in the second exon of the ZSCAN4 gene (Choi et al. 2016) and recruits EP300 (p300) and CREBBP (CBP) (Choi et al. 2016, Vuoristo et al. 2022). DUX4 activates bidirectional transcription of an ERVL-MaLR retrotransposon element 20 kb upstream of the ZSCAN4 transcription start site that upregulates expression of ZSCAN4 (Vuoristo et al. 2022). TPRXL, TPRX1, and TPRX2 are translated at the time of zygotic genome activation and TPRX1 and TPRX2 bind and activate the ZSCAN4 gene (Zou et al. 2022). In mouse, Obox genes appear to be orthologous to human TPRX2 (Maeso et al. 2016) and bind and activate mouse Zscan4 genes (Ji et al. 2023).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9816396",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9816396"
}
]
},
{
"id": "R-HSA-9818523",
"name": "Expression of ZSCAN4 in the embryo",
"equation": "",
"summary": "The ZSCAN4 gene, the single human homolog of the Zscan4 gene family in mouse, is transcribed to yield mRNA (Petropoulos et al. 2016) which is translated to yield protein. ZSCAN4 is expressed initially in 2-cell embryos (Yan et al. 2013), increases in 4-cell embryos (Yan et al. 2013), and continues in blastocysts (Petropoulos et al. 2016). DUX4 (Hendrickson et al. 2017) and TPRXL, TPRX1, and TPRX2 (Zou et al. 2022) directly activate ZSCAN4 during minor (initial) zygotic genome activation. ZSCAN4 binds nucleosomes of microsatellites and protects against DNA damage (inferred from the mouse homolog in Srinivasan et al. 2020).",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-9816413"
],
"output_participant_list": [
"R-HSA-9816447"
],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9818523",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9818523"
}
]
},
{
"id": "R-HSA-9825747",
"name": "CREBBP acetylates HINT1 dimer",
"equation": "",
"summary": "Histidine Triad Nucleotide-binding protein 1 (HINT1) is a tumor suppressor protein that exerts its function in part by binding to and repressing transcription factors such as MITF and CTNNB1 (beta-catenin) (Razin et al, 1999; Lee et al, 2004; Weiske and Huber, 2005; Genovese et al, 2009). Activity of HINT1 is regulated by post-translational modifications, notably acetylation. CREBBP-dependent acetylation of HINT1 at K21 and K30 disrupts the interaction of HINT1 and MITF, liberating MITF to bind and activate its transcriptional targets (Choudhary et al, 2009; Motzik et al, 2017; Jung et al, 2020; reviewed in Goding and Arnheiter 2019).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P49773-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9825747",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9825747"
}
]
},
{
"id": "R-HSA-9825751",
"name": "HINT1 binds MITF-M",
"equation": "",
"summary": "Deacetylation of HINT1 by SIRT1 promotes the interaction of MITF and HINT1, consequently restricting the transcription factor activity of MITF (Jung et al, 2020).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P49773-1",
"Q96EB6-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9825751",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9825751"
}
]
},
{
"id": "R-HSA-9833446",
"name": "NS1 (1C) binds to CREBBP",
"equation": "",
"summary": "After hRSV nonstructural protein 1C (NS1) localizes to the nucleus, it binds to both phosphorylated IRF3 dimer and CREB-binding protein (CREBBP), preventing association of these two proteins and the subsequent stimulation of expression of interferon-beta (Ren et al, 2011).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-9833449"
],
"enzyme_list": [
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9833446",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9833446"
}
]
},
{
"id": "R-HSA-9843116",
"name": "PPARG2 transcription is stimulated by PPARG2:RXRA:MLL4,(MLL3)-ASCOM complex",
"equation": "",
"summary": "Based on mouse studies, expression of the PPARG2 isoform of the PPARG gene, encoding Peroxisome proliferator-activated receptor gamma, a nuclear receptor transcription factor that is one of the master regulators of adipogenesis, is positively regulated in fat tissue by the PPARG:RXRA heterodimer, creating a positive feedback loop, and KMT2C (MLL3)/KMT2D (MLL4) histone methyltransferase complexes. Deletion of Paxip1 (also known as Ptip) gene, encoding one of the mandatory accessory subunits of Mll3/Mll4 complexes, in mouse embryonic fibroblasts (MEFs) leads to over 10-fold decrease of expression of Pparg gene. Pparg1 is the only Pparg isoform expressed in MEFs. Pparg expression can be rescued by ectopic expression of Paxip1 (Cho et al. 2009). Deletion of Paxip1 in mouse brown preadipocytes almost completely prevents the induction of Pparg1, Pparg2, and Cebpa, but has little effect on the induction of their upstream transcription regulator Cebpb (Cho et al. 2009). In differentiating mouse brown preadipocytes, Paxip1 promotes recruitment of RNA Pol II to promoters of Pparg1 and Pparg2 isoforms (Cho et al. 2009). The expression of Pparg2 but not Pparg1 is induced by high fat diet in mouse liver in an Mll4-dependent manner (Kim et al. 2016). The overlapping Pparg, Kmt2d, and H3K4me1 ChIP-seq peaks are found around the Pparg2 promoter region, with each peak containing a conserved PPRE (peroxisome proliferator response element) (Kim et al. 2016). In a mouse hepatocyte cell line, transactivation of expression of Scd1, Cd36, and Cidec genes by Pparg2 but not Pparg1, in response to synthetic PPARG agonist rosiglitazone, is dependent on Kmt2d (Kim et al. 2016).
In mouse brown preadipocytes expressing histone 3 mutant H3.3 K4M the expression of Pparg is severely reduced (Jang et al. 2019). Deletion of SET domains of Kmt2c and Kmt2d in mouse brown preadipocytes prevents induction of Pparg during adipogenesis (Jang et al. 2019).",
"cellular_location": "nucleoplasm",
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"id": "R-HSA-9843116",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9843116"
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},
{
"id": "R-HSA-9843119",
"name": "MLL4-ASCOM,(MLL3-ASCOM) complex is recruited to ligand- and coactivator-bound PPARG:RXRA heterodimer",
"equation": "",
"summary": "The MLL4-ASCOM complex (an MLL4 complex, composed of the core MLL4 complex, consisting of KMT2D and the WRAD subcomplex of WDR5, RBBP5, ASH2L, and DPY30, and accessory subunits PAXIP1, PAGR1, NCOA6, and KDM6A) and/or the MLL3-ASCOM complex (same composition as the MLL4-ASCOM except for the catalytic subunit KMT2C) are recruited to ligand- and coactivator-bound PPARG:RXRA heterodimer to PPARG target gene loci. While most of the functional studies were done in mouse, as described below, the physical interaction between KMT2D and PPARG was confirmed by co-immunoprecipitation of the endogenous complex from human prostate cancer cell lines (Zhai et al. 2022).
In differentiating mouse brown adipocytes, KMT2D (MLL4) mainly binds to active enhancers that are prevalently bound by both CEBP and PPARG, or at least by one of the two adipogenic transcription factors - the experiment did not distinguish between CEBPA and CEBPB (Lee et al. 2013). In mouse differentiating adipocytes, the non-catalytic subunits of KMT2C (MLL3)- and MLL4-ASCOM complexes were shown to co-immunoprecipitate with the complex of PPARG and RXRA (Lee et al. 2008). The MLL4 complex physically interacts with PPARG in mouse differentiating brown adipocytes (Lee et al. 2013). A flavonoid, kaempferol, is a PPARG antagonist that prevents rosiglitazone-induced association of Mll4 with Pparg at Pparg target loci in mouse adipocytes (Park et al. 2022).
By ChIP, at day 2 of mouse brown adipocyte differentiation, more than half of MLL4 binding sites overlap with binding sites for CEBPB, CEBPA, and PPARG (Lee et al. 2013). Association of PPARG1 and PPARG2 with KMT2D requires a PPARG agonist such as rosiglitazone (Kim et al. 2016). KMT2D binds to PPARG2 more robustly than to PPARG1 (Kim et al. 2016). The interaction between PPARG2 and KMT2D is diminished in the presence of the ABL1 inhibitor imatinib (Kim et al. 2016). ABL1-dependent phosphorylation of PPARG2 enhances association of PPARG with KMT2D in mouse liver carcinoma cells. Imatinib, an inhibitor of ABL1 kinase, decreases association between PPARG2 and RBBP5, a component of the MLL4 complex and other KMT2 complexes (Kim et al. 2016). Imatinib significantly decreases the recruitment of KMT2D to PPREs (peroxisome proliferator response elements) in the PPARG, CD36, CIDEC and SCD gene loci (Kim et al. 2016).
The MLL4-ASCOM and MLL3-ASCOM complexes or their components were shown to bind to regulatory elements of the following adipogenesis genes regulated by PPARG in adipocytes and/or steatotic hepatocytes:
ACSS3 gene (Kim et al. 2016: based on ChIP-seq for KMT2D and PPARG in mouse hepatocytes)
AGPAT2 gene (Kim et al. 2016: based on ChIP-seq for KMT2D and PPARG in mouse hepatocytes)
CD36 gene (Kim et al. 2016: based on ChIP-seq for KMT2D and PPARG in mouse hepatocytes)
CEBPA gene (Cho et al. 2009: by ChIP assay in mouse embryonic fibroblasts - MEFs, endogenous PAXIP1 - PTIP, an accessory subunit of MLL3 and MLL4 complexes, associates with the CEBPA gene promoter with a signal peak around the transcription start site; in mouse white preadipocyte line 3T3-L1, PAXIP1 is enriched around the transcription start sites of CEBPA before and after the onset of differentiation; in differentiating mouse brown preadipocytes, KMT2D is enriched around the transcription start site of CEBPA in a PAXIP1-dependent manner; Lee et al. 2013: KMT2D binds the CEBPA gene locus in differentiating mouse brown adipocytes)
CIDEC gene (Kim et al. 2016: based on ChIP-seq for KMT2D and PPARG in mouse hepatocytes)
ELOVL5 gene (Kim et al. 2016: based on ChIP-seq for KMT2D and PPARG in mouse hepatocytes)
FABP4 gene (Qi et al. 2003: by ChIP, NCOA6 binds to the FABP4 gene locus in a PPARG-dependent manner in mouse embryonic fibroblasts - MEFs - stimulated to differentiate into adipocytes; Lee et al. 2008: by ChIP, KMT2C and KMT2D, as well as NCOA6, bind the FABP4 gene locus in mouse fibroblasts induced to differentiate into adipocytes; the recruitment of components of MLL3/4-ASCOM complexes - KMT2C, KMT2D, WDR5, RBBP5, ASH2L, DPY30, NCOA6, PAXIP1, and KDM6A - is dependent on direct interaction of MLL3-ASCOM and MLL4-ASCOM with the PPARG:RXRA heterodimer; Lee et al. 2013: MLL4 binds the FABP4 gene locus in differentiating mouse brown adipocytes)
GPAM gene (Kim et al. 2016: based on ChIP-seq for KMT2D and PPARG in mouse hepatocytes)
LPL gene (Lee et al. 2013: mouse Mll4 complex was shown to bind to Lpl gene locus in differentiating mouse brown adipocytes)
PLIN2 gene (Kim et al. 2016: based on ChIP-seq for KMT2D and PPARG in mouse hepatocytes)
PPARG gene (Cho et al. 2009: by ChIP in mouse embryonic fibroblasts (MEFs), PAXIP1 (PTIP) and PAGR1 (PA1), accessory subunits of the MLL3 and MLL4 complexes, as well as the obligatory subunit RBBP5 and the catalytic subunit KMT2D are found associated with the PPARG1 but not PPARG2 promoter; PPARG1 is the only isoform of PPARG expressed in MEFs; in mouse white preadipocyte line 3T3-L1, PAXIP1 is enriched around the transcription start sites of PPARG1 and PPARG2 before and after the onset of differentiation; in differentiating mouse brown preadipocytes, KMT2D is enriched around the transcription start sites of PPARG1 and PPARG2 in a PAXIP1-dependent manner; Lee et al. 2013: KMT2D binds the PPARG gene locus in differentiating mouse brown adipocytes)
SCD gene (also known as SCD1, Kim et al. 2016: based on ChIP-seq for KMT2D and PPARG in mouse hepatocytes)
SCD5 gene (also known as SCD2 or SCD4, Scd4 in mouse; Kim et al. 2016: based on ChIP-seq for KMT2D and PPARG in mouse hepatocytes)
THRSP gene (Kim et al. 2016: based on ChIP-seq for KMT2D and PPARG in mouse hepatocytes).
While PPARG-mediated recruitment of MLL3/MLL4 complexes to PPARG target genes ACSL1, ADIPOQ, ANGPTL4, DGAT2, LIPE, LPIN1, MGLL, PDK4, PEX11A, PLIN1, PLIN4, PNPLA2 has not been reported, the expression of these genes, as well as the genes for which more direct evidence was available (ACSS3, AGPAT2, CD36, CEBPA, CIDEC, ELOVL5, FABP4, GPAM, LPL, PLIN2, PPARG, SCD, SCD5, and THRSP), is severely reduced in differentiating mouse brown preadipocytes expressing histone H3.3 K4M mutant or Kmt2c (Mll3) and Kmt2d (Mll4) with deleted SET domains (Jang et al. 2019: RNA-seq, supplementary information). Therefore, these genes are also annotated as direct MLL3/MLL4 targets.
UCP1 gene (Lee et al. 2013: KMT2D binds the UCP1 gene locus in differentiating mouse brown adipocytes).
KMT2D was also shown to bind the UCP1 and KLF15 gene loci in differentiating mouse brown adipocytes, while it was largely absent from the CEBPB gene locus (Lee et al. 2013). KLF15 has not been reported as a PPARG target gene, while UCP1 gene was reported to be co-regulated by EBF2 and PPARG (Stine et al. 2016).",
"cellular_location": "nucleoplasm",
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{
"id": "R-HSA-9843119",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9843119"
}
]
},
{
"id": "R-HSA-9843120",
"name": "Coactivators are recruited to liganded PPARG:RXRA heterodimer",
"equation": "",
"summary": "Transcriptional coactivators recruited to the ligand binding domain (LBD) of the ligand-bound heterodimer of PPARG and RXRA include histone acetyltransferases, such as NCOA1, NCOA3, CREBBP, and EP300, components of the MED1 complex (also known as DRIP or TRAP complex), and PPAR-specific (PPARGC1A, PPARGC1B) and non-specific (NCOA2, NCOA4, NCOA6) coactivators.
NCOA1 (SRC1) binding to PPARG is supported by multiple studies (Zhu et al. 1996: mouse Ncoa1 shown to bind to mouse Pparg1 and act as its coactivator; DiRenzo et al. 1997: NCOA1 from African green monkey cell line CV-1 shown to bind both mouse Pparg and human RXRA; Oberfield et al. 1999: binding to human PPARG2 shown; Yang et al. 2000: ligand-dependent binding of PPARG to NCOA1, and ligand-dependent binding of NCOA1 to the DNA-bound PPARG:RXRA heterodimer, species unspecified - presumably human; Mueller et al. 2002: comparable binding of mouse Ncoa1 to both Pparg1 and Pparg2 mouse isoforms; Fujimura et al. 2005: human recombinant NCOA1 associates with recombinant human PPARG2 in the presence of PPARG agonists; Allen et al. 2006: a mammalian two-hybrid assay using recombinant mouse proteins showed that PPARG agonists induce association of Ncoa1, to Pparg). NCOA1 possesses a single LXXLL motif that binds to LBDs of nuclear receptors so that one molecule of NCOA1 is bound to PPARG and one is bound to RXRA (Gampe et al. 2000). The structural study showed that the LXXLL motif of human NCOA1 interacts with the LBD of human PPARG bound to synthetic agonist rosiglitazone, similarly to previously established interactions between NCOA1 and other nuclear receptors (Nolte et al. 1998). NCOA1 also binds to RXRA in a ligand-dependent manner (Yang et al. 2000: species unspecified).
NCOA3 (ACTR) binding to PPARG is supported by multiple studies (Yang et al. 2000: ligand-dependent binding of PPARG to NCOA3, and ligand-dependent binding of NCOA3 to the DNA-bound PPARG:RXRA heterodimer, species unspecified - presumably human; Hartig et al. 2011: fluorescence resonance energy transfer \u2013 FRET \u2013 using human NCOA3 and PPARG). NCOA3 also binds to RXRA in a ligand-dependent manner (Yang et al. 2000: species unspecified).
CREBBP (CBP) binding to PPARG is supported by multiple studies (Mizukami and Taniguchi 1997: binding of mouse Crebbp to human PPARG2 in the presence of synthetic PPARG agonist; Oberfield et al. 1999: binding to human PPARG2 shown; Gelman et al. 1999: binding of the N-terminal region of CREBBP to human PPARG2 in the presence of synthetic PPARG agonists; Fujimura et al. 2005: human recombinant CREBBP associates with recombinant human PPARG2 in the presence of PPARG agonists; Allen et al. 2006: a mammalian two-hybrid assay using recombinant mouse proteins showed that PPARG agonists induce association of Crebbp to Pparg; Xie et al. 2015: binding of human CREBBP to PPARG2 in response to synthetic PPARG agonist; Park et al. 2022: a flavonoid, kaempferol, is a PPARG antagonist that prevents rosiglitazone-induced association of Crebbp with Pparg at Pparg target loci in mouse adipocytes).
EP300 (p300) binding to PPARG is supported by multiple studies (Gelman et al. 1999: EP300 stimulates transcription from PPAR response elements - PPREs - in the presence of synthetic PPARG ligands, and the N-terminus of EP300 binds to human PPARG2; Jang and Jung 2015: binding of Pparg to Ep300 in mouse white preadipocyte line 3T3-L1 is negatively regulated by Atf3). EP300 was reported to acetylate PPARG, which increases PPARG transcriptional activity (Han et al. 2010). Levels of acetylated PPARG are significantly lower in young than in senescent human embryonic lung diploid fibroblast cell lines (Han et al. 2010). EP300 was reported to directly bind to RXRA in a ligand-dependent manner and acetylate it on lysine residue K145, which increases RXRA transcriptional activity (Zhao et al. 2007: recombinant and endogenous human RXRA and EP300 were used). The interaction between EP300 and RXRA is negatively regulated by NR4A1 (also known as TR3), an orphan nuclear receptor, which can sequester RXRA to mitochondria, triggering apoptosis (Zhao et al. 2007).
The A/B domain of PPARG (residues 1-136 in mouse Pparg2) is needed for recruitment of CREBBP and EP300 to PPARG target genes (Bugge et al. 2009).
PCAF is another histone acetyltransferase that may associate with PPARG (Puigserver et al. 1999).
The entire MED1 complex (also known as DRIP or TRAP complex) co-immunoprecipitates (coIPs) with the ligand-bound PPARG (Yang et al. 2000: ligand-dependent coIP of the MED1 complex associated with PPARG, ligand-dependent association of MED1 with the DNA-bound PPARG:RXRA heterodimer, species unspecified; Ge et al. 2002: recombinant mouse Pparg2 was used to coIP proteins from mouse embryonic fibroblasts; Allen et al. 2006: a mammalian two-hybrid assay using recombinant mouse proteins showed that PPARG agonists induce association of Med1, also known as TRAP220, to Pparg (Allen et al. 2006). Ge et al. 2008: recombinant mouse Pparg was used to coIP proteins from HeLa cell nuclear extracts). The interaction between MED1 and PPARG involves the LXXLL motifs in MED1 that are known to associate with nuclear receptors (Ge et al. 2008: mouse Pparg2 and human MED1 were used). Mouse Med1 binds with similar affinity to mouse Pparg1 and Pparg2 isoforms (Mueller et al. 2002). Epigenetic readers, such as BRD4, which can bind to epigenetic marks deposited at the PPARG target genes, may enable recruitment of the MED1 complex during adipogenesis (Lee et al. 2017). Mouse Med1 knockout fibroblasts were reported to be refractory to Pparg2-stimulated adipogenesis but not to Myod-stimulated myogenesis (Ge et al. 2002), but this does not depend on direct interaction between MED1 and PPARG (Ge et al. 2008). Knockout of another Mediator complex subunit, Med24, also impairs the adipogenic program in mouse fibroblasts (Ge et al. 2008). In mouse 3T3-L1 preadipocyte line, it was shown that the Mediator complex component Med14 directly interacts with the N-terminus of Pparg2 and facilitates the recruitment of the Mediator complex to PPARG targets (Grontved et al. 2010). Med14 knockdown impairs adipogenesis in 3T3-L1 cells (Grontved et al. 2010). Mouse Med14 binds with similar affinity to mouse Pparg1 and Pparg2 isoforms (Mueller et al. 2002). A structural study of the RXRA heterodimer with VDR (Vitamin D3 receptor) found that a single molecule of MED1 was bound to the heterodimer, interacting with both RXRA and VDR (Belorusova et al. 2020: human proteins were used), which implies that a single MED1 complex associates with one PPARG:RXRA heterodimer. In an earlier study, RXRA was shown to have a lower affinity for MED1 compared to PPARG2 (Yang et al. 2000: species unspecified).
PPARGC1A (PGC-1alpha) possesses largely independent PPARG, EP300, and MED1 interaction domains (Wallberg et al. 2003). Mouse Ppargc1a binds with equal affinity to mouse Pparg1 and Pparg2 isoforms (Mueller et al. 2002). Human recombinant PPARGC1A associates with recombinant human PPARG2 in the presence of PPARG agonists (Fujimura et al. 2005). Direct interaction between PPARGC1A and MED1 may explain recruitment of MED1 to PPARG even in the absence of LXXLL motifs in MED1 (Ge et al. 2008). Recombinant mouse Ppargc1a coIPs Mediator complex subunits besides MED1 from nuclear extracts of HeLa cells and wild-type, but not Med1 knockout MEFs (Wallberg et al. 2003). In a luciferase reporter assay, transcription from a PPRE is enhanced when PPARGC1A and MED1 are both present in addition to the PPARG:RXRA heterodimer and PPARG natural agonist 15dJ2, and all four proteins form a complex on target DNA based on electrophoretic mobility shift assay (EMSA) (Wallberg et al. 2003). When template DNA is histone-coated, prior EP300-mediated histone acetylation is required for PPARGC1A-stimulated transcription of PPARG:RXRA targets (Wallberg et al. 2003). Besides direct binding to PPARG, the histone acetyltransferases CREBBP, EP300, and NCOA1 also interact directly with PPARGC1A and PPARGC1A, which may aid in recruiting them to PPARG (Puigserver et al. 1999). The more N-terminal of the two PPARGC1A LXXLL motifs is necessary for its interaction with the coactivator-binding domain of PPARG (Li et al. 2008: human recombinant PPARGC1A and PPARG fragments were used for the crystallographic structural study). In mouse, it was shown that Naa10, an N-acetyltransferase, acetylates Ppargc1a, preventing its association with Pparg, and inhibiting beige adipocyte-mediated thermogenesis (Lee et al. 2019). NAA10 is overexpressed in cancer and in white adipose tissue of obese mice and humans (Lee et al. 2019). PPARGC1A was shown to directly associate with RXRA in a ligand-dependent manner and act as an RXRA co-activator, that may, in addition, facilitate recruitment of NCOA2 to RXRA (Delrive et al. 2002: human PPARGC1A and mouse Rxra were used).
PPARGC1B (also known as PGC1beta) can also bind PPARG and act as a transcriptional coactivator (Parham et al. 2015: human PPARG and human PPARGC1B co-immunoprecipitate in human endothelial cells treated with sphingosine 1-phosphate, also known as S1P, a putative PPARG ligand). Ppargc1b is strongly induced during differentiation of mouse brown adipocytes in a Ppargc1a-independent manner (Uldry et al. 2006). The presence of either Ppargc1a or Ppargc1b is needed for the development of mouse brown adipocytes and to increase mitochondrial density in differentiated mouse brown adipocytes in response to cold-induced adrenergic signaling (Uldry et al. 2006). Based on studies in mice, PPARGC1B is likely itself a PPARG target gene, with the PPARG:RXRA heterodimer shown to bind PPREs in the first intron of the PPARGC1B gene to induce PPARGC1B expression (Deng et al. 2011: Pparg-mediated induction of Ppargc1b was shown in mouse white preadipocyte cell line 3T3-L1 and in the white adipose tissue of obese mice). PPARGC1B and PPARGC1A likely bind to PPARG in a mutually exclusive manner.
NCOA2 was reported to bind to PPARG in a ligand-dependent manner (Yang et al. 2000: ligand-dependent binding of NCOA2 to the DNA-bound PPARG:RXRA heterodimer, species unspecified, presumably human; Hartig et al. 2011: interaction between human PPARG and NCOA2 by FRET). While NCOA2 was reported to bind to RXRA in a ligand-dependent manner (Yang et al. 2000: species unspecified), in a structural study in which recombinant human proteins were used, the ligand-bound PPARG:RXRA heterodimer was reported to contain only one molecule of NCOA2, bound to PPARG (Osz et al. 2012). Another study, also using recombinant human proteins confirmed the 1:1 stoichiometry of the ligand-bound PPARX:RXRA heterodimer and NCOA2, showing that a single molecule of NCOA2 interacts with both RXRA (more weakly) and PPARG (more strongly), and this interaction is facilitated by both RXRA and PPARG binding to their respective ligands and to target DNA (de Vera et al. 2017).
NCOA4 (ARA70) was shown to bind directly to both PPARG and RXRA and activate transcription of PPARG target genes (Heinlein et al. 1999: human NCOA4, human RXRA, and mouse Pparg1 were used; binding to RXRA was dependent on the presence of RXRA ligand 9-cis-retinoic acid; binding to Pparg1 was enhanced in the presence of PPARG natural ligand 15dJ2 - 5-deoxy-delta12,14-prostaglandin J2).
Based on a study using mouse proteins, NCOA6 directly binds to both PPARG and RXRA in a ligand-dependent manner and stimulates PPARG:RXRA-mediated transcription (Zhu et al. 2000).
Based on studies in mouse white preadipocyte cell line 3T3-L1, AJUBA was reported to act both as a coactivator of PPARG, aiding in recruitment of EP300 and CREBBP to PPARG (Li et al. 2016), and to act upstream of PPARG, as a coactivator of CEBPB, aiding in recruitment of CREBBP and EP300 to CEBPB at PPARG and CEBPA gene promoters (Yan et al. 2022).
Combinations of coactivators that simultaneously bind to ligand-activated PPARG:RXRA dimers have not been fully elucidated, but can be regulated by cell type- and/or developmental stage-specific gene expression and posttranslational modifications. Also, different coactivators were reported to bind with different affinities to the PPARG:RXRA heterodimer in response to different PPARG and RXRA agonists (Yang et al. 2000: species unspecified). During human adipocyte differentiation, mRNA and protein levels of NCOA2 and NCOA3 were reported to remain constant, while levels of NCOA1 increase; siRNA-mediated knockdown of NCOA1, however, does not affect lipogenesis significantly, while siRNA-mediated knockdown of NCOA2 and NCOA3 does (Hartig et al. 2011). Inhibitory phosphorylation of PPARG on serine residue S112, known to diminish PPARG ligand affinity, interaction with NCOAs, transcriptional activity and adipogenic capacity, was shown to be increased upon NCOA2 and NCOA3 knockdown and decreased after NCOA1 knockdown (Hartig et al. 2011). CDK5-mediated phosphorylation of PPARG2 on serine residue S273 (corresponds to S245 in PPARG1) was reported to decrease the affinity of PPARG2 for the coactivator proteins MED1 (TRAP220), PPARGC1A (PGC 1alpha), and NCOA2 (TIF2) (Dias et al. 2020: human recombinant PPARG2 was used with human recombinant NCOA2, human recombinant MED1, and mouse recombinant PPARGC1A). Binding of NCOA1 and MED1 does not appear to occur simultaneously on each subunit of the PPARG:RXRA heterodimer (Yang et al. 2000). Relative level of NCOA1 to NCOA2 can modulate energy metabolism (Picard et al. 2002). Ncoa2 knockout mice are protected against obesity and exhibit enhanced adaptive thermogenesis, while Ncoa1 knockout mice are prone to obesity due to reduced energy expenditure (Picard et al. 2002). In brown adipose tissue of mice, the lack of NCOA2 facilitates the interaction of PPARGC1A with NCOA1, which promotes transcription of thermogenic genes (Picard et al. 2002). As the roles of individual NCOAs have not been clarified, NCOA1, NCOA2, and NCOA3 are annotated as candidates in this reaction.",
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},
{
"id": "R-HSA-9843121",
"name": "MLL4-ASCOM, (MLL3-ASCOM) complex monomethylates nucleosomes at PPARG:RXRA-bound enhancers",
"equation": "",
"summary": "The KMT2D (MLL4)-ASCOM and KMT2C (MLL3)-ASCOM complexes methylate H3K4 at nucleosomes of PPARG target genes during adipogenesis, thus creating an active chromatin mark. A flavonoid, kaempferol, is a PPARG antagonist that prevents rosiglitazone-induced association of Mll4 with Pparg at Pparg target loci and H3K4 methylation of nucleosomes associated with Pparg targets in mouse adipocytes (Park et al. 2022). As MLL3 and MLL4 mostly function as H3K4 monomethyl transferases, histone modifications at all target gene loci are shown as monomethylation (H3K4me1). At some target loci other types of H3K4 methylation (di- and trimethylation) have been reported, as indicated below. KMT2C/KMT2D-dependent H3K4 methylation has been shown at the following PPARG target genes:
CD36 gene (Kim et al. 2016: MLL4-dependent increase in H3K4me1 levels coincident with PPARG and KMT2D recruitment to regulatory gene elements was detected in steatotic mouse hepatocytes)
CEBPA gene (Cho et al. 2009: H3K4me3 signal at the CEBPA proximal promoter is reduced upon deletion of PAXIP1 - PTIP - in mouse embryonic fibroblasts - MEFs; in mouse white preadipocyte line 3T3-L1; H3K4me3 is enriched around the transcription start sites of CEBPA before and after the onset of differentiation; in differentiating mouse brown preadipocytes, H3K4me3 is enriched around the transcription start site of CEBPA in a PAXIP1-dependent manner)
CIDEC gene (Kim et al. 2016: KMT2D-dependent increase in H3K4me1 levels coincident with PPARG and KMT2D recruitment to regulatory gene elements was detected in steatotic mouse hepatocytes)
FABP4 gene (Lee et al. 2008: the kinetics of H3K4 trimethylation at the mouse FABP4 gene locus corresponds to the kinetics of KMT2C/KMT2D recruitment, and is followed by H3 and H4 acetylation; PPARG ligand rosiglitazone induced H3K4 trimethylation in MEFs which was abolished in NCOA6 null cells and significantly attenuated in Kmt2c delta/delta MEFs that express catalytically inactive KMT2C)
PPARG (Cho et al. 2009: in MEFs, which only express PPARG1 but not PPARG2 isoform of PPARG, increased trimethylation of the PPARG1 proximal promoter at H3K4 - H3K4me3 mark of active chromatin - was dependent on the presence of PAXIP1 (PTIP), an accessory subunit of MLL3 and MLL4 complexes; in mouse white preadipocyte line 3T3-L1, H3K4me3 is enriched around the transcription start sites of PPARG1 and PPARG2 before and after the onset of differentiation; in differentiating mouse brown preadipocytes, H3K4me3 is enriched around the transcription start sites of PPARG1 and PPARG2 in a PAXIP1-dependent manner)
SCD gene (Kim et al. 2016: KMT2D-dependent increase in H3K4me1 levels coincident with PPARG and KMT2D recruitment to regulatory gene elements was detected in steatotic mouse hepatocytes)
Targeted knock-in of Kmt2d (Mll4) mutant with deleted SET domain in somatic precursor cells of brown adipose tissue and skeletal muscle leads to death immediately after birth due to breathing malfunction, with affected mice showing similar brown adipose tissue mass but altered morphology and reduced muscle mass compared to wild type mice (Jang et al. 2019). When targeted knock-in involves both Kmt2c (Mll3) and Kmt2d mutants with deleted SET domains, affected mice also die immediately after birth, but show a profound reduction in brown adipose tissue and muscle mass (Jang et al. 2019). Deletion of SET domains in Kmt2c and Kmt2d decreases global levels of H3K4me1 and H3K4me2 but not H3K4me3 in mouse brown preadipocytes (Jang et al. 2019). Deletion of Kmt2c and Kmt2d SET domains reduces protein levels of Kmt2c, Kmt2d, and the accessory protein of Mll3/Mll4 complexes Utx (Kdm6a), but not Rbbp5 - an obligatory subunit of all KMT2 (MLL) complexes (Jang et al. 2019).
While KMT2C/KMT2D-mediated H3K4 methylation of the nucleosomes at regulatory elements of PPARG target genes ACSL1, ACSS3, ADIPOQ, AGPAT2, ANGPTL4, DGAT2, ELOVL5, GPAM, LIPE, LPIN1, LPL, MGLL, PDK4, PEX11A, PLIN1, PLIN2, PLIN4, PNPLA2, SCD5, THRSP has not been reported, the expression of these genes, as well as the genes for which more direct evidence was available (CD36, CEBPA, CIDEC, FABP4, PPARG, and SCD), is severely reduced in differentiating mouse brown preadipocytes expressing histone H3.3 K4M mutant or Kmt2c and Kmt2d with deleted SET domains (Jang et al. 2019: RNA seq, supplementary information).",
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"Q15788-1",
"O15550-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"P49336-1"
],
"evidence": [
{
"id": "R-HSA-9843121",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9843121"
}
]
},
{
"id": "R-HSA-9843900",
"name": "FABP4 gene expression is stimulated by PPARG:RXRA:MLL4,(MLL3)-ASCOM complex",
"equation": "",
"summary": "Expression of the FABP4 gene, encoding Fatty acid-binding protein 4, also known as aP2, is positively regulated in fat tissue by the PPARG:RXRA heterodimer and KMT2C (MLL3)/KMT2D (MLL4) histone methyltransferase complexes. Based on a mouse study, the heterodimer of PPARG and RXRA directly stimulates transcription of the FABP4 (aP2) gene by binding to an adipocyte-specific enhancer (Tontonoz et al. 1994). Expression of FABP4 is significantly down-regulated in white adipose tissue (WAT) of Kmt2c (Mll3) delta/delta mice that express H3K4 methyltransferase inactive Kmt2c mutant (Lee et al. 2008). Expression of Fabp4 is completely ablated in Ncoa6 (also known as Prip)-null cells (Qi et al. 2003). Mouse embryonic fibroblasts (MEFs) deficient for Paxip1 (Ptip), an accessory subunit of MLL3 and MLL4 complexes, do not show a defect in Pparg- and ligand-stimulated expression of endogenous Fabp4 (Cho et al. 2009).
Based on a study in MEFs in which Pparg was ectopically expressed, Pparg positively regulates Fabp4 transcription in a ligand-dependent manner (Ge et a. 2008).
Treatment of mouse white preadipocyte cell line 3T3-L1 with PPARG agonists results in increased Fabp4 mRNA levels (Allen et al. 2006, Bhalla et al. 2011).
By microarray-based gene expression analysis in primary human white adipocytes undergoing browning, the mRNA level of FABP4 is significantly increased upon treatment with the PPARG synthetic agonist rosiglitazone (Barquissau et al. 2016: supplementary information, Table S3). In human monocytes, mRNA level of FABP4 is significantly increased upon treatment with the natural PPARG ligand 15d-PGJ2 (Pelton et al. 1999).
In mouse brown preadipocytes expressing histone 3 mutant H3.3 K4M, the expression of Fabp4 is severely reduced (Jang et al. 2019). Deletion of SET domains of Kmt2c and Kmt2d in mouse brown preadipocytes prevents induction of Fabp4 during adipogenesis (Jang et al. 2019).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q15788-1",
"O15550-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"P49336-1"
],
"evidence": [
{
"id": "R-HSA-9843900",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9843900"
}
]
},
{
"id": "R-HSA-9851530",
"name": "CD36 gene expression is stimulated by PPARG:RXRA:MLL4,(MLL3)-ASCOM complex",
"equation": "",
"summary": "Expression of the CD36 gene, encoding Platelet glycoprotein 4, also known as Fatty acid translocase (FAT), responsible for binding of long-chain fatty acids at the cell surface and facilitating their transport into cells, is positively regulated by the PPARG:RXRA heterodimer and KMT2C (MLL3)/KMT2D (MLL4) histone methyltransferases. In differentiating primary human adipocytes, CD36 mRNA levels are significantly reduced upon antisense-mediated knockdown of PPARG mRNA (Perera et al. 2006, Supplementary materials Table 2). In mouse 3T3-L1 cell line-derived adipocytes, Cd36 mRNA level is increased upon treatment with the PAPRG agonist rosiglitazone (Allen et al. 2006). Expression of the Cd36 gene is severely reduced in differentiating mouse brown preadipocytes expressing histone H3.3 K4M mutant or Kmt2c (Mll3) and Kmt2d (Mll4) with deleted SET domains (Jang et al. 2019: RNA-seq, supplementary information).
Based on a mouse model of hepatic steatosis, expression of the Cd36 gene is directly stimulated by Pparg2 and the Mll4 complex, but negatively regulated by imatinib, an Abl1 kinase inhibitor that disrupts the Abl1-mediated association between Pparg2 and the Mll4 complex (Kim et al. 2016).",
"cellular_location": "nucleoplasm, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q15788-1",
"O15550-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"P49336-1"
],
"evidence": [
{
"id": "R-HSA-9851530",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9851530"
}
]
},
{
"id": "R-HSA-9851534",
"name": "CIDEC gene expression is stimulated by PPARG:RXRA:MLL4,(MLL3)-ASCOM complex",
"equation": "",
"summary": "Expression of the CIDEC gene, encoding Lipid transferase CIDEC (also known as Fat-specific protein FSP27 homolog) that is specifically expressed in white adipocytes where it mediates fusion of lipid droplets into a single lipid droplet, is positively regulated in fat tissue by the PPARG:RXRA heterodimer and KMT2C (MLL3)/KMT2D (MLL4) histone methyltransferase complexes. After the differentiation of mouse adipocytes, the expression pattern of Cidec is similar to that of Pparg2 (Kim et al. 2008). The level of Cidec mRNA in mouse adipocytes increases in the presence of PPARG agonists (Kim et al. 2008). By reporter assay, Pparg2 activates transcription from the mouse Cidec gene promoter (Kim et al. 2008). Expression of human CIDEC gene reporter construct is positively regulated by exogenously expressed mouse Pparg and Rxra (Sharma et al. 2018). In contrast, growth hormone (GH)-induced phosphorylation of Pparg and its translocation from the nucleus in mouse white preadipocyte line 3T3-L1 lead to reduced Cidec expression (Sharma et al. 2018). Expression of the Cidec gene is severely reduced in differentiating mouse brown preadipocytes expressing histone H3.3 K4M mutant or Kmt2c (Mll3) and Kmt2d (Mll4) with deleted SET domains (Jang et al. 2019: RNA-seq, supplementary information). RNA Pol II occupancy at the mouse Cidec gene promoter is increased in response to PPARG agonists (Nielsen et al. 2008).
Based on a mouse model of hepatic steatosis, expression of the Cidec gene is directly stimulated by Pparg2 and the Mll4 complex, but negatively regulated by imatinib, an Abl1 kinase inhibitor that disrupts the Abl1-mediated association between Pparg2 and the Mll4 complex (Kim et al. 2016).",
"cellular_location": "cytosol, nucleoplasm",
"input_participant_list": [
"R-HSA-6784665"
],
"output_participant_list": [
"R-HSA-8856627"
],
"enzyme_list": [
"Q15788-1",
"O15550-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"P49336-1"
],
"evidence": [
{
"id": "R-HSA-9851534",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9851534"
}
]
},
{
"id": "R-HSA-9851539",
"name": "SCD gene expression is stimulated by PPARG:RXRA:MLL4,(MLL3)-ASCOM complex",
"equation": "",
"summary": "Expression of the SCD gene, encoding Stearoyl-coenzyme A desaturase (SCD, also known as SCD1), responsible for conversion of palmitoyl- and stearoyl-coenzyme A to palmitoleoyl- and oleoyl-coenzyme A, is positively regulated by PPARG:RXRA heterodimers and KMT2C (MLL3)/KMT2D (MLL4) histone methyltransferase complexes. Expression of SCD mRNA is increased in fat tissue of human subjects treated with PPARG agonist pioglitazone, and correlates with increased mRNA levels of other PPARG-responsive genes, such as LPIN1 (Yao-Borengasser et al. 2008). Expression of the Scd1 gene, a mouse SCD ortholog, is severely reduced in differentiating mouse brown preadipocytes expressing histone H3.3 K4M mutant or Kmt2c (Mll3) and Kmt2d (Mll4) with deleted SET domains (Jang et al. 2019: RNA-seq, supplementary information).
Based on a mouse model of hepatic steatosis, expression of the Scd gene is directly stimulated by Pparg2 and the Mll4 complex but negatively regulated by imatinib, an Abl1 kinase inhibitor that disrupts Abl1-mediated association between Pparg2 and the Mll4 complex (Kim et al. 2016).",
"cellular_location": "endoplasmic reticulum membrane, nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q15788-1",
"O15550-1",
"O00767-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"P49336-1"
],
"evidence": [
{
"id": "R-HSA-9851539",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9851539"
}
]
},
{
"id": "R-HSA-9854128",
"name": "ACSS3 gene expression is stimulated by PPARG2:RXRA:MLL4(MLL3)-ASCOM complex",
"equation": "",
"summary": "Based on a mouse model of hepatic steatosis, expression of the ACSS3 gene, encoding Acyl-CoA synthetase short-chain family member 3 that localizes to the mitochondrial matrix, is directly stimulated by PPARG2 and the MLL4 complex (Kim et al. 2016).",
"cellular_location": "mitochondrial matrix, nucleoplasm",
"input_participant_list": [
"R-HSA-9851810"
],
"output_participant_list": [
"R-HSA-5696385"
],
"enzyme_list": [
"Q15788-1",
"O15550-1",
"Q9H6R3-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"P49336-1"
],
"evidence": [
{
"id": "R-HSA-9854128",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9854128"
}
]
},
{
"id": "R-HSA-9854130",
"name": "THRSP gene expression is stimulated by PPARG2:RXRA:MLL4,(MLL3)-ASCOM complex",
"equation": "",
"summary": "Based on a mouse model of hepatic steatosis, expression of the THRSP gene, encoding Thyroid hormone inducible hepatic protein, is directly stimulated by PPARG2 and the KMT2D (MLL4) complex (Kim et al. 2016). Expression of the Thrsp gene is severely reduced in differentiating mouse brown preadipocytes expressing histone H3.3 K4M mutant or Kmt2c (Mll3) and Kmt2d (Mll4) with deleted SET domains (Jang et al. 2019: RNA seq, supplementary information).",
"cellular_location": "cytosol, nucleoplasm",
"input_participant_list": [
"R-HSA-9851801"
],
"output_participant_list": [
"R-HSA-8867326"
],
"enzyme_list": [
"Q15788-1",
"O15550-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"P49336-1"
],
"evidence": [
{
"id": "R-HSA-9854130",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9854130"
}
]
},
{
"id": "R-HSA-9854141",
"name": "GPAM gene expression is stimulated by PPARG2:RXRA:MLL4,(MLL3)-ASCOM complex",
"equation": "",
"summary": "Based on a mouse model of hepatic steatosis, expression of the GPAM gene, encoding Glycerol-3-phosphate acyltransferase that localizes to the mitochondrial outer membrane, is directly stimulated by PPARG2 and the KMT2D (MLL4) complex (Kim et al. 2016). Gpam gene expression is reduced in differentiating mouse brown preadipocytes expressing histone H3.3 K4M mutant or Kmt2c (Mll3) and Kmt2d (Mll4) with deleted SET domains (Jang et al. 2019: RNA seq, supplementary information).",
"cellular_location": "mitochondrial outer membrane, nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q15788-1",
"O15550-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"Q9HCL2-1",
"P49336-1"
],
"evidence": [
{
"id": "R-HSA-9854141",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9854141"
}
]
},
{
"id": "R-HSA-9854142",
"name": "ELOVL5 gene expression is stimulated by PPARG2:RXRA:MLL4(MLL3)-ASCOM complex",
"equation": "",
"summary": "Based on a mouse model of hepatic steatosis, expression of the ELOVL5 gene, encoding Elongation of very long chain fatty acids protein 5 that localizes to the endoplasmic reticulum membrane, is directly stimulated by PPARG2 and the KMT2D (MLL4) complex (Kim et al. 2016). Elovl5 gene expression is reduced in differentiating mouse brown preadipocytes expressing histone H3.3 K4M mutant or Kmt2c (Mll3) and Kmt2d (Mll4) with deleted SET domains (Jang et al. 2019: RNA seq, supplementary information).",
"cellular_location": "endoplasmic reticulum membrane, nucleoplasm",
"input_participant_list": [
"R-HSA-8962699"
],
"output_participant_list": [
"R-HSA-548679"
],
"enzyme_list": [
"Q15788-1",
"O15550-1",
"Q9NYP7-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"P49336-1"
],
"evidence": [
{
"id": "R-HSA-9854142",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9854142"
}
]
},
{
"id": "R-HSA-9856211",
"name": "ADIPOQ gene expression is stimulated by PPARG:RXRA:MLL4,(MLL3)-ASCOM complex",
"equation": "",
"summary": "Transcription of the ADIPOQ gene, encoding a fat-derived hormone with antidiabetic and anti-atherogenic properties, is positively regulated by the PPARG:RXRA heterodimer and KMT2C (MLL3)/KMT2D (MLL4) histone methyltransferase complexes. Administration of synthetic agonists of PPARG increases plasma ADIPOQ protein levels in both insulin resistant humans and mice (Maeda et al. 2001). In cultured mouse 3T3-L1 white preadipocytes, PPARG synthetic agonists enhance mRNA transcription and secretion of Adipoq protein (Maeda et al. 2001). In 3T3-L1 cells, PPARG synthetic agonists stimulate activation of the luciferase reporter containing the human ADIPOQ gene promoter (Maeda et al. 2001). In obese diabetic mice chronically treated with PPARG synthetic agonists (11-day treatment window), mean plasma Adipoq protein levels increase (Combs et al. 2002). A two-week treatment of normal human subjects with the PPARG synthetic agonist rosiglitazone leads to increased circulating ADIPOQ protein (Combs et al. 2002). ADIPOQ serum levels are 5-fold suppressed in patients with severe insulin resistance caused by dominant-negative mutations in the PPARG gene (Combs et al. 2002). The human PPARG:RXRA heterodimer was shown by EMSA to directly bind to peroxisome proliferator response element (PPRE) in the promoter of the human ADIPOQ gene to increase its transcription (Iwaki et al. 2003). The human ADIPOQ gene promoter contains a responsive element for the liver receptor homolog-1 (LRH1, officially known as NR5A2) in the vicinity of the PPRE and direct NR5A2 binding to the ADIPOQ gene promoter facilitates PPARG:RXRA-mediated induction of the ADIPOQ gene transcription (Iwaki et al. 2003). Expression of ADIPOQ is significantly down-regulated in WAT of Kmt2c delta/delta mice that express a H3K4 methyltransferase-inactive Kmt2c mutant (Lee et al. 2008). Treatment of mouse white preadipocyte cell line 3T3-L1 with PPARG agonists results in increased Adipoq mRNA levels (Bhalla et al. 2011). Expression of the ADIPOQ gene is severely reduced in differentiating mouse brown preadipocytes expressing histone H3.3 K4M mutant or Kmt2c and Kmt2d with deleted SET domains (Jang et al. 2019: RNA-seq, supplementary information).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q15788-1",
"O15550-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"P49336-1"
],
"evidence": [
{
"id": "R-HSA-9856211",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9856211"
}
]
},
{
"id": "R-HSA-9856486",
"name": "CEBPA gene expression is stimulated by PPARG:RXRA:MLL4,(MLL3)-ASCOM complex",
"equation": "",
"summary": "Expression of CEBPA gene, encoding CCAAT/enhancer-binding protein alpha which functions as one of the master transcriptional regulators of adipocyte differentiation, is positively regulated in fat tissue by PPARG:RXRA heterodimer and KMT2C (MLL3)/KMT2D (MLL4) histone methyltransferases. In differentiating primary human adipocytes, CEBPA mRNA levels are reduced upon antisense-mediated knockdown of PPARG mRNA (Perera et al. 2006, Supplementary materials Table 2). Based on a study in mouse embryonic fibroblasts (MEFs) in which Pparg was ectopically expressed, PPARG positively regulates CEBPA transcription in a ligand-dependent manner (Ge et a. 2008).
MEFs deficient for Paxip1 (Ptip), an accessory subunit of Mll3 and Mll4 complexes, show a severe defect in Pparg- and ligand-stimulated expression of endogenous Cebpa (Cho et al. 2009). In differentiating mouse brown preadipocytes, Paxip1 promotes recruitment of RNA Pol II to Cebpa gene promoter (Cho et al. 2009).
In mouse brown preadipocytes expressing histone 3 mutant H3.3 K4M, the expression of the Cebpa gene is severely reduced (Jang et al. 2019). Deletion of SET domains of Kmt2c (Mll3) and Kmt2d (Mll4) in mouse brown preadipocytes prevents induction of Cebpa during adipogenesis (Jang et al. 2019).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q15788-1",
"O15550-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"P49336-1"
],
"evidence": [
{
"id": "R-HSA-9856486",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9856486"
}
]
},
{
"id": "R-HSA-9859005",
"name": "PEX11A gene expression is stimulated by PPARG:RXRA:MLL4,(MLL3)-ASCOM complex",
"equation": "",
"summary": "Expression of the PEX11A gene, encoding Peroxisomal membrane protein 11A, is positively regulated in fat tissue by the PPARG:RXRA heterodimer and KMT2C (MLL3)/KMT2D (MLL4) histone methyltransferase complexes. Mouse Pex11a gene is clustered together with the Plin1 gene on chromosome 7. A peroxisome proliferator response element (PPRE) is found in between the Pex11a gene and the downstream Plin1 gene, at ~8 kb downstream of Pex11a transcription start site (TSS), and ~2 kb upstream of the Plin1 TSS. The Pparg:Rxra heterodimer specifically binds this PPRE to stimulate transcription of both Pex11a and Plin1 (Shimizu et al. 2004, Shimizu et al. 2006). The arrangement of the PEX11A and PLIN1 genes and their shared regulatory elements are conserved in rats and humans (Shimizu et al. 2006). Expression of the Pex11a gene is severely reduced in differentiating mouse brown preadipocytes expressing histone H3.3 K4M mutant or Kmt2c (Mll3) and Kmt2d (Mll4) with deleted SET domains (Jang et al. 2019: RNA-seq, supplementary information).",
"cellular_location": "nucleoplasm, peroxisomal membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q15788-1",
"O15550-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"P49336-1"
],
"evidence": [
{
"id": "R-HSA-9859005",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9859005"
}
]
},
{
"id": "R-HSA-9859007",
"name": "PLIN1 gene expression is stimulated by PPARG:RXRA:MLL4,(MLL3)-ASCOM complex",
"equation": "",
"summary": "Expression of the PLIN1 gene, encoding Perilipin-1, involved in the formation and maintenance of lipid droplets, is positively regulated in fat tissue by the PPARG:RXRA heterodimer and KMT2C (MLL3)/KMT2D (MLL4) histone methyltransferase complexes. In differentiating primary human adipocytes, PLIN1 mRNA levels are reduced upon antisense-mediated knockdown of PPARG mRNA (Perera et al. 2006, Supplementary materials Table 2). Mouse Plin1 gene in clustered together with the Pex11a gene on chromosome 7. A peroxisome proliferator response element (PPRE) is found in between the Pex11a gene and the downstream Plin1 gene, at ~8 kb downstream of Pex11a transcription start site (TSS), and ~2 kb upstream of the Plin1 TSS. The Pparg:Rxra heterodimer specifically binds this PPRE to stimulate transcription of both Pex11a and Plin1 (Shimizu et al. 2004, Shimizu et al. 2006). The arrangement of the PEX11A and PLIN1 genes and their shared regulatory elements are conserved in rats and humans (Shimizu et al. 2006). Expression of the Plin1 gene is severely reduced in differentiating mouse brown preadipocytes expressing histone H3.3 K4M mutant or Kmt2c (Mll3) and Kmt2d (Mll4) with deleted SET domains (Jang et al. 2019: RNA-seq, supplementary information).",
"cellular_location": "lipid droplet, nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q15788-1",
"O15550-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"P49336-1"
],
"evidence": [
{
"id": "R-HSA-9859007",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9859007"
}
]
},
{
"id": "R-HSA-9859082",
"name": "PNPLA2 gene expression is stimulated by PPARG:RXRA:MLL4,(MLL3)-ASCOM complex",
"equation": "",
"summary": "Expression of the PNPLA2 gene, encoding Patatin-like phospholipase domain-containing protein 2, also known as Adipose triglyceride lipase (ATGL), is positively regulated in fat tissue by the PPARG:RXRA heterodimer and KMT2C (MLL3)/KMT2D (MLL4) histone methyltransferase complexes. By qRT-PCR in primary human white adipocytes undergoing browning, the mRNA level of PNPLA2 is significantly increased upon treatment with the PPARG agonist rosiglitazone (Barquissau et al. 2016: supplementary information, Figure S3). Expression of the Pnpla2 gene is severely reduced in differentiating mouse brown preadipocytes expressing histone H3.3 K4M mutant or Kmt2c (Mll3) and Kmt2d (Mll4) with deleted SET domains (Jang et al. 2019: RNA-seq, supplementary information).",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-9859076"
],
"output_participant_list": [
"R-HSA-9859603"
],
"enzyme_list": [
"Q15788-1",
"O15550-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"Q96AD5-1",
"P49336-1"
],
"evidence": [
{
"id": "R-HSA-9859082",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9859082"
}
]
},
{
"id": "R-HSA-9859084",
"name": "AGPAT2 gene expression is stimulated by PPARG:RXRA:MLL4,(MLL3)-ASCOM complex",
"equation": "",
"summary": "Expression of the AGPAT2 gene, encoding 1-acyl-sn-glycerol-3-phosphate acyltransferase beta that localizes to the endoplasmic reticulum membrane and is responsible for conversion of lysophosphatidic acid (LPA) into phosphatidic acid (PA) is positively regulated by PPARG:RXRA heterodimers and KMT2C (MLL3)/KMT2D (MLL4) histone methyltransferases. Expression of AGPAT2 mRNA is increased in fat tissue of human subjects treated with PPARG agonist pioglitazone, and correlates with increased mRNA levels of other PPARG responsive genes, such as SCD (Yao-Borengasser et al. 2008). Expression of the AGPAT2 gene is severely reduced in differentiating mouse brown preadipocytes expressing histone H3.3 K4M mutant or Kmt2c (Mll3) and Kmt2d (Mll4) with deleted SET domains (Jang et al. 2019: RNA-seq, supplementary information). Based on a mouse model of hepatic steatosis, expression of the AGPAT2 gene is directly stimulated by PPARG2 and the MLL4 complex (Kim et al. 2016).",
"cellular_location": "endoplasmic reticulum membrane, nucleoplasm",
"input_participant_list": [
"R-HSA-9851811"
],
"output_participant_list": [
"R-HSA-61805"
],
"enzyme_list": [
"Q15788-1",
"O15550-1",
"O15120-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"P49336-1"
],
"evidence": [
{
"id": "R-HSA-9859084",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9859084"
}
]
},
{
"id": "R-HSA-9859119",
"name": "PDK4 gene expression is stimulated by PPARG:RXRA:MLL4,(MLL3)-ASCOM complex",
"equation": "",
"summary": "Expression of the PDK4 gene, encoding mitochondrial Pyruvate dehydrogenase acetyl-transferring kinase isozyme 4, also known as PDHK4, which regulates the TCA cycle, is positively regulated in fat tissue by the PPARG:RXRA heterodimer and KMT2C (MLL3)/KMT2D (MLL4) histone methyltransferase complexes. In primary human white adipocytes undergoing browning, the PDK4 expression is significantly increased upon treatment with the PPARG agonist rosiglitazone (Barquissau et al. 2016). In mouse 3T3-L1 cell line-derived adipocytes, Pdk4 (also known as Pdhk4) mRNA level is increased upon treatment with the PAPRG agonist rosiglitazone (Allen et al. 2006). Expression of the Pdk4 gene is severely reduced in differentiating mouse brown preadipocytes expressing histone H3.3 K4M mutant or Kmt2c (Mll3) and Kmt2d (Mll4) with deleted SET domains (Jang et al. 2019: RNA-seq, supplementary information).",
"cellular_location": "mitochondrial matrix, nucleoplasm",
"input_participant_list": [
"R-HSA-9859113"
],
"output_participant_list": [
"R-HSA-203941"
],
"enzyme_list": [
"Q15788-1",
"O15550-1",
"Q16654-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"P49336-1"
],
"evidence": [
{
"id": "R-HSA-9859119",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9859119"
}
]
},
{
"id": "R-HSA-9859121",
"name": "ANGPTL4 gene expression is stimulated by PPARG:RXRA:MLL4,(MLL3)-ASCOM complex",
"equation": "",
"summary": "Expression of the ANGPTL4 gene, encoding Angiopoietin-related protein 4, also known as PPARG angiopoietin related (PGAR), is positively regulated by the PPARG:RXRA heterodimer and MLL3/MLL4 histone methyltransferases. Based on studies in mouse preadipocyte cell line 3T3-L1, ANGTPL4 expression is rapidly induced upon treatment with PPARG agonists (Yoon et al. 2000, Allen et al. 2006, Bhalla et al. 2011) in the absence of protein synthesis (Yoon et al. 2000). ANGTPL4 mRNA is highly expressed in human white fat and placenta (Yoon et al. 2000). Angptl4 expression in mouse white fat upon treatment with the PPARG agonist rosiglitazone leads to enhanced angiogenesis, which is likely required for adipose tissue growth (Gealekman et al. 2008). By microarray-based gene expression analysis in primary human white adipocytes undergoing browning, the mRNA level of ANGPTL4 is significantly increased upon treatment with the PPARG agonist rosiglitazone (Barquissau et al. 2016: supplementary information, Table S3). Expression of the Angptl4 gene is severely reduced in differentiating mouse brown preadipocytes expressing histone H3.3 K4M mutant or Kmt2c (Mll3) and Kmt2d (Mll4) with deleted SET domains (Jang et al. 2019: RNA-seq, supplementary information). RNA Pol II occupancy at the Angptl4 gene promoter is increased in response to PPARG agonists (Nielsen et al. 2008). Pparg-mediated upregulation of Angptl4 secretion from mouse white fat tissue was shown to specifically promote proliferation of glucagon-secreting alpha-cells of the endocrine pancreas (Ben-Zvi et al. 2015). In mice, it was shown that ANGPTL4 is involved in regulation of lipid metabolism by inhibiting lipoprotein lipase (LPL) responsible for the clearance of lipids from the bloodstream, therefore leading to increased blood levels of plasma triglycerides (TG) and fatty acids (Yoshida et al. 2002).",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-9859116"
],
"output_participant_list": [],
"enzyme_list": [
"Q15788-1",
"O15550-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"P49336-1"
],
"evidence": [
{
"id": "R-HSA-9859121",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9859121"
}
]
},
{
"id": "R-HSA-9859182",
"name": "LPL gene expression is stimulated by PPARG:RXRA:MLL4,(MLL3)-ASCOM complex",
"equation": "",
"summary": "Expression of the LPL gene, encoding Lipoprotein lipase responsible for hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby lipid clearance from the bloodstream, lipid utilization and storage, is positively regulated in fat tissue by the PPARG:RXRA heterodimer and KMT2C (MLL3)/KMT2D (MLL4) histone methyltransferase complexes. In differentiating primary human adipocytes, LPIN1 mRNA levels are significantly reduced upon antisense-mediated knockdown of PPARG mRNA (Perera et al. 2006, Supplementary materials Table 2). By microarray-based gene expression analysis in primary human white adipocytes undergoing browning, the mRNA level of LPL is significantly increased upon treatment with the PPARG agonist rosiglitazone (Barquissau et al. 2016: supplementary information, Table S3). Expression of the Lpl gene is severely reduced in differentiating mouse brown preadipocytes expressing histone H3.3 K4M mutant or Kmt2c (Mll3) and Kmt2d (Mll4) with deleted SET domains (Jang et al. 2019: RNA-seq, supplementary information).",
"cellular_location": "extracellular region, nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q15788-1",
"O15550-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"P49336-1",
"P06858-1"
],
"evidence": [
{
"id": "R-HSA-9859182",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9859182"
}
]
},
{
"id": "R-HSA-9859188",
"name": "ACSL1 gene expression is stimulated by PPARG:RXRA:MLL4,(MLL3)-ASCOM complex",
"equation": "",
"summary": "Expression of the ACSL1 gene, encoding Long-chain-fatty-acid-CoA ligase 1, is positively regulated in fat tissue by the PPARG:RXRA heterodimer and KMT2C (MLL3)/KMT2D (MLL4) histone methyltransferase complexes. In differentiating primary human adipocytes, ACSL1 (FACL1) mRNA level is significantly reduced upon antisense-mediated knockdown of PPARG mRNA (Perera et al. 2006, Supplementary materials Table 2). Expression of the ACSL1 gene is severely reduced in differentiating mouse brown preadipocytes expressing histone H3.3 K4M mutant or Kmt2c (Mll3) and Kmt2d (Mll4) with deleted SET domains (Jang et al. 2019: RNA-seq, supplementary information).",
"cellular_location": "mitochondrial outer membrane, nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q15788-1",
"O15550-1",
"P33121-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"P49336-1"
],
"evidence": [
{
"id": "R-HSA-9859188",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9859188"
}
]
},
{
"id": "R-HSA-9859196",
"name": "PLIN2 gene expression is stimulated by PPARG:RXRA:MLL4,(MLL3)-ASCOM complex",
"equation": "",
"summary": "Expression of the PLIN2 gene, encoding Perilipin-2, also known as Adipophilin or ADFP or Adipose differentiation-related protein (ADRP), which localizes to lipid droplets, is positively regulated in fat tissue by the PPARG:RXRA heterodimer and KMT2C (MLL3)/KMT2D (MLL4) histone methyltransferase complexes. Treatment of mouse white preadipocyte cell line 3T3-L1 with PPARG agonists results in increased Plin2 mRNA levels (Bhalla et al. 2011). Ligand-activated PPARG:RXRA heterodimer (i.e. PPARG ligand, troglitazone or RXR ligand LG268) was shown to stimulate PLIN2 gene transcription in human trophoblasts (Bildirici et al. 2003). Expression of the PLIN2 gene is severely reduced in differentiating mouse brown preadipocytes expressing histone H3.3 K4M mutant or Kmt2c (Mll3) and Kmt2d (Mll4) with deleted SET domains (Jang et al. 2019: RNA-seq, supplementary information).
Based on a mouse model of hepatic steatosis, expression of the Plin2 gene is directly stimulated by Pparg2 and the MLL4 complex but negatively regulated by imatinib, an Abl1 kinase inhibitor that disrupts Abl1-mediated association between Pparg2 and the Mll4 complex (Kim et al. 2016).",
"cellular_location": "lipid droplet, nucleoplasm",
"input_participant_list": [
"R-HSA-5649938"
],
"output_participant_list": [
"R-HSA-9613345"
],
"enzyme_list": [
"Q15788-1",
"O15550-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"P49336-1"
],
"evidence": [
{
"id": "R-HSA-9859196",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9859196"
}
]
},
{
"id": "R-HSA-9859206",
"name": "PLIN4 gene expression is stimulated by PPARG:RXRA:MLL4,(MLL3)-ASCOM complex",
"equation": "",
"summary": "Expression of the PLIN4 gene, encoding Perilipin-4, also known as adipocyte protein S3-12, is positively regulated in fat tissue by the PPARG:RXRA heterodimer and KMT2C (MLL3)/KMT2D (MLL4) histone methyltransferase complexes. In human adipocyte cell line SGBS, the expression level of PLIN4 gene correlates with PPARG gene expression (Dalen et al. 2004). In mouse white preadipocyte line 3T3-L1, treatment with PPARG agonists induces Plin4 gene expression (Dalen et al. 2004). peroxisome proliferator response elements (PPREs) are conserved between human and mouse PLIN4 gene loci, and mouse Plin4 gene reporter construct is activated by exogenously expressed ligand-activated PPARG:RXRA heterodimer (Dalen et al. 2004). Expression of the Plin4 gene is severely reduced in differentiating mouse brown preadipocytes expressing histone H3.3 K4M mutant or Kmt2c (Mll3) and Kmt2d (Mll4) with deleted SET domains (Jang et al. 2019: RNA-seq, supplementary information).",
"cellular_location": "lipid droplet, nucleoplasm",
"input_participant_list": [
"R-HSA-9859208"
],
"output_participant_list": [
"R-HSA-9859207"
],
"enzyme_list": [
"Q15788-1",
"O15550-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"P49336-1"
],
"evidence": [
{
"id": "R-HSA-9859206",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9859206"
}
]
},
{
"id": "R-HSA-9859223",
"name": "LIPE gene expression is stimulated by PPARG:RXRA:MLL4,(MLL3)-ASCOM complex",
"equation": "",
"summary": "Expression of the LIPE gene, encoding a hormone sensitive lipase primarily responsible for hydrolysis of stored triglycerides to free fatty acids (reviewed in Althaher 2022), is positively regulated in fat tissue by the PPARG:RXRA heterodimer and KMT2C (MLL3)/KMT2D (MLL4) histone methyltransferase complexes. In differentiating primary human adipocytes, LIPE mRNA levels are reduced upon antisense-mediated knockdown of PPARG mRNA (Perera et al. 2006, Supplementary materials Table 2). Expression of the Lipe gene is severely reduced in differentiating mouse brown preadipocytes expressing histone H3.3 K4M mutant or Kmt2c (Mll3) and Kmt2d (Mll4) with deleted SET domains (Jang et al. 2019: RNA-seq, supplementary information).",
"cellular_location": "lipid droplet, nucleoplasm",
"input_participant_list": [
"R-HSA-9859224"
],
"output_participant_list": [
"R-HSA-9859222"
],
"enzyme_list": [
"Q15788-1",
"O15550-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"P49336-1",
"Q05469-1"
],
"evidence": [
{
"id": "R-HSA-9859223",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9859223"
}
]
},
{
"id": "R-HSA-9859273",
"name": "MGLL gene expression is stimulated by PPARG:RXRA:MLL4,(MLL3)-ASCOM complex",
"equation": "",
"summary": "Expression of the MGLL gene, encoding Monoglyceride lipase responsible for conversion of monoacylglycerides to free fatty acids and glycerol, is positively regulated in fat tissue by the PPARG:RXRA heterodimer and KMT2C (MLL3)/KMT2D (MLL4) histone methyltransferase complexes. Treatment of rats with PPARG agonist rosiglitazone increases mRNA levels of MGLL (also known as MGL) and other lipolysis enzymes in subcutaneous and visceral white adipose tissue (Festuccia et al. 2006). Expression of the Mgll gene is severely reduced in differentiating mouse brown preadipocytes expressing histone H3.3 K4M mutant or Kmt2c (Mll3) and Kmt2d (Mll4) with deleted SET domains (Jang et al. 2019: RNA-seq, supplementary information).",
"cellular_location": "lipid droplet, nucleoplasm",
"input_participant_list": [
"R-HSA-8962802"
],
"output_participant_list": [
"R-HSA-163567"
],
"enzyme_list": [
"Q15788-1",
"O15550-1",
"Q99685-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"P49336-1"
],
"evidence": [
{
"id": "R-HSA-9859273",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9859273"
}
]
},
{
"id": "R-HSA-9859291",
"name": "DGAT2 gene expression is stimulated by PPARG:RXRA:MLL4,(MLL3)-ASCOM complex",
"equation": "",
"summary": "Expression of the DGAT2 gene, encoding Diacylglycerol O-acyltransferase 2, an essential acyltransferase required for synthesis and storage of intracellular triglycerides, is positively regulated in fat tissue by the PPARG:RXRA heterodimer and KMT2C (MLL3)/KMT2D (MLL4) histone methyltransferase complexes. In the adipose tissue of Fgf21 knockout mice, the activity of Pparg is decreased due to SUMOylation, which correlates with a lower expression of Dgat2 gene that can be restored by Fgf21 administration or expression of a SUMOylation-resistant Pparg mutant (Dutchak et al. 2012). Twist1-mediated direct repression of Pparg transcription in mouse white adipocytes correlates with reduced Dgat2 mRNA levels (Sun et al. 2023). Expression of the Dgat2 gene is severely reduced in differentiating mouse brown preadipocytes expressing histone H3.3 K4M mutant or Kmt2c (Mll3) and Kmt2d (Mll4) with deleted SET domains (Jang et al. 2019: RNA-seq, supplementary information).",
"cellular_location": "endoplasmic reticulum membrane, nucleoplasm",
"input_participant_list": [
"R-HSA-9859276"
],
"output_participant_list": [
"R-HSA-549188"
],
"enzyme_list": [
"Q15788-1",
"O15550-1",
"Q96PD7-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"P49336-1"
],
"evidence": [
{
"id": "R-HSA-9859291",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9859291"
}
]
},
{
"id": "R-HSA-9859334",
"name": "LPIN1 gene expression is stimulated by PPARG:RXRA:MLL4,(MLL3)-ASCOM complex",
"equation": "",
"summary": "Expression of the LPIN1 (LPN, also known as Lipin) gene, encoding magnesium-dependent phosphatidate phosphatase enzyme responsible for conversion of phosphatidic acid (PA) to diacylglycerol (DAG) during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis (reviewed in Welcome et al. 2025), is positively regulated by PPARG:RXRA heterodimers and KMT2C (MLL3)/KMT2D (MLL4) histone methyltransferase complexes. In differentiating primary human adipocytes, LPIN1 mRNA levels are reduced upon antisense-mediated knockdown of PPARG mRNA (Perera et al. 2006, Supplementary materials Table 2). Expression of LPIN1 splicing isoform beta (Lipin-beta) mRNA is increased in fat tissue of human subjects treated with PPARG agonist pioglitazone, and correlates with increased mRNA levels of other PPARG-responsive genes, such as SCD, but this correlation is not seen for LPIN1 splicing isoform alpha (Lipin-alpha) (Yao-Borengasser et al. 2008). This implies that alpha and beta splicing isoforms of LPIN1 may be differentially regulated by PPARG (Yao-Borengasser et al. 2008). Expression of the Lpin1 gene is severely reduced in differentiating mouse brown preadipocytes expressing histone H3.3 K4M mutant or Kmt2c (Mll3) and Kmt2d (Mll4) with deleted SET domains (Jang et al. 2019: RNA-seq, supplementary information).",
"cellular_location": "endoplasmic reticulum membrane, nucleoplasm",
"input_participant_list": [
"R-HSA-8962866"
],
"output_participant_list": [
"R-HSA-549157"
],
"enzyme_list": [
"Q15788-1",
"O15550-1",
"Q09472-1",
"O14686-1",
"Q92793-1",
"Q8NEZ4-1",
"Q9Y6Q9-1",
"P49336-1",
"Q14693-1"
],
"evidence": [
{
"id": "R-HSA-9859334",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9859334"
}
]
},
{
"id": "R-HSA-9909374",
"name": "Phosphorylated BMAL1:CLOCK and coactivators positively regulate expression of Period-3 (PER3)",
"equation": "",
"summary": "Phosphorylated BMAL1:CLOCK bound to the promoter of PER3 activates transcription (Matsumura and Akashi 2017). Expression of PER3 oscillates in a circadian rhythm in the suprachiasmatic nucleus, but, unlike PER1 and PER2, expression is not induced by light during the night (Li et al. 2013, and inferred from mouse homologs). Expression of PER3 peaks around mid-day, after the peak of PER1 expression and before the peak of PER2 expression (Li et al. 2013).",
"cellular_location": "cytosol, nucleoplasm",
"input_participant_list": [
"R-HSA-9909379"
],
"output_participant_list": [
"R-HSA-400323"
],
"enzyme_list": [
"Q03164-1",
"Q92793-1",
"O15516-1"
],
"evidence": [
{
"id": "R-HSA-9909374",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9909374"
}
]
},
{
"id": "R-HSA-9909400",
"name": "p-S90-BMAL1:p-T451,T461-CLOCK and coactivators bind the PER3 gene",
"equation": "",
"summary": "A dimer of phosphorylated BMAL1:CLOCK heterodimers binds adjacent E-boxes in the PER3 promoter (Matsumura and Akashi 2017, and inferred from mouse homologs). Phosphorylated BMAL1:CLOCK also binds one additional site in the promoter (Matsumura and Akashi 2017). Phosphorylated BMAL1:CLOCK recruits the histone acetyltransferase CREBBP (CBP) and the histone methyltransferase KMT2A (MLL1) (inferred from mouse homologs), and activates transcription.",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q03164-1",
"Q92793-1",
"O15516-1"
],
"evidence": [
{
"id": "R-HSA-9909400",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9909400"
}
]
},
{
"id": "R-HSA-9909561",
"name": "Phosphorylated BMAL1:CLOCK,NPAS2 and coactivators positively regulate expression of Period-1 (PER1)",
"equation": "",
"summary": "As inferred from mouse homologs, RBM4 (hLARK) binds the 3' UTR of PER1 mRNA and increases production of PER1 protein probably by enhancing translation (Kojima et al. 2007).",
"cellular_location": "cytosol, nucleoplasm",
"input_participant_list": [
"R-HSA-5641209"
],
"output_participant_list": [
"R-HSA-400373"
],
"enzyme_list": [
"P57059-1",
"Q03164-1",
"Q92793-1",
"O15516-1"
],
"evidence": [
{
"id": "R-HSA-9909561",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9909561"
}
]
},
{
"id": "R-HSA-9909623",
"name": "CD274 Transcription",
"equation": "",
"summary": "The transcriptional regulation of CD274 (PD-L1/programmed death-ligand 1) is crucial in cancer biology, enabling tumor cells to evade immune detection. PD-L1 expression is tightly controlled by various transcription factors and signalling pathways responding to both intrinsic cellular signals and extrinsic environmental perturbations. It is regulated transcriptionally by multiple mechanisms, including epigenetic modifications (EZH2, DNMTs, MLLs) and transcription factors (STAT3, STAT1, IRF1, MYC, HIF, and others) activated by various upstream signalling pathways. The regulation of PD-L1 is a complex interplay of oncogenic signalling pathways, cytokine responses, epigenetic modifications, specific transcription factors, the tumor microenvironment, and non-coding RNAs. This multifaceted regulation finely tunes PD-L1 expression to promote immune evasion in cancer, making it a critical target for cancer immunotherapy (Zhou et al., 2023, Cha et al.,2019, Yamaguchi et al.,2022, Ju et al., 2020).",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-9701419"
],
"output_participant_list": [
"R-HSA-9909617"
],
"enzyme_list": [
"Q09472-1",
"Q03164-1",
"Q92793-1",
"Q8NEZ4-1",
"Q15910-1"
],
"evidence": [
{
"id": "R-HSA-9909623",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9909623"
}
]
},
{
"id": "R-HSA-9909652",
"name": "NFE2L2 binding to CD274 gene",
"equation": "",
"summary": "NFE2L2 (NRF2/(Nuclear Factor Erythroid 2\u2013Related Factor 2) regulates CD274 (PD-L1) transcription by binding to antioxidant response elements (AREs) in the PD-L1 promoter region. Upon activation by oxidative stress or electrophilic compounds, NFE2L2 translocates to the nucleus and binds to AREs, recruiting transcriptional co-activators (CEBP/p300) and machinery to initiate PD-L1 gene transcription. (Duan et al., 2023, Payandeh et al., 2021, Zhu et al., 2018)",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9909652",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9909652"
}
]
},
{
"id": "R-HSA-9920716",
"name": "CLOCK acetylates BMAL1 on lysine-538",
"equation": "",
"summary": "CLOCK in the BMAL1:CLOCK heterodimer acetylates lysine-538 of BMAL1 (inferred from mouse homologs). The acetylation reaction occurs in the evening at the time when transactivation by BMAL1:CLOCK declines (inferred from mouse homologs). The acetylation is required for efficient interaction with the CRY:PER:kinase complex that represses BMAL1:CLOCK activity (inferred from mouse homologs).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q03164-1",
"Q92793-1",
"O15516-1"
],
"evidence": [
{
"id": "R-HSA-9920716",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9920716"
}
]
},
{
"id": "R-HSA-9920724",
"name": "p-T451,T461-CLOCK is phosphorylated on serines-440,441,446",
"equation": "",
"summary": "An unidentified kinase or kinases phosphorylates three serine residues (S440, S441, S446) of CLOCK (inferred from the mouse homolog).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q03164-1",
"Q92793-1",
"O15516-1"
],
"evidence": [
{
"id": "R-HSA-9920724",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9920724"
}
]
},
{
"id": "R-HSA-9922269",
"name": "p-S-CRY:p-S-PER:CSNK1D,E binds p-S90,Ac-K538-BMAL1:p-2T,3S-CLOCK:target gene",
"equation": "",
"summary": "The phosphorylated CRY:PER:kinase complex, containing CRY1, CRY2, PER1, PER2, PER3, and CSNK1D and/or CSNK1E (inferred from mouse homologs), enters the nucleus and binds BMAL1:CLOCK heterodimers bound to E-boxes in circadian regulated target genes (inferred from mouse homologs). Acetylation of BMAL1 enhances the interaction (inferred from mouse homologs). The kinase CSNK1D (and likely CSNK1E), in a complex with CRY and PER proteins, is brought to phosphorylated BMAL1:CLOCK where it further phosphorylates CLOCK, causing dissociation of BMAL1:CLOCK from DNA (inferred from mouse homologs). CRY1, CRY2, and PER2 interact with BMAL1 and PER2 binds CLOCK (inferred from mouse homologs). CRY1 alone is capable of binding BMAL1:CLOCK and repressing transactivation of target genes by BMAL1:CLOCK (inferred from homologs). CRY1 together with PER2 is able to dissociate BMAL1:CLOCK from DNA (inferred from mouse homologs).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P48730-1",
"P49674-1",
"Q03164-1",
"Q92793-1",
"O15516-1"
],
"evidence": [
{
"id": "R-HSA-9922269",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9922269"
}
]
},
{
"id": "R-HSA-9922273",
"name": "CSNK1D,E phosphorylates CLOCK in p-S-CRY:p-S-PER:CSNK1D,E:p-S90,Ac-538-BMAL:p-2T,3S-CLOCK:target gene",
"equation": "",
"summary": "Cryptochrome (CRY) and Period (PER) proteins form complexes with the kinase CSNK1D (CK1delta) and/or CSNK1E (CK1epsilon) and bind the BMAL1:CLOCK heterodimer at promoters of target genes. The CRY:PER:kinase complex thereby brings CSNK1D and/or CSNK1E into proximity with CLOCK, resulting in the phosphorylation of CLOCK (inferred from mouse homologs).The residues phosphorylated by CSNK1D,E may be serine-38 and serine-42, which are located in the DNA-binding region of CLOCK and are observed to undergo cyclic phosphorylation that causes weakened transactivation and DNA-binding activity of BMAL1:CLOCK (inferred from mouse homologs in Yoshitane et al. 2009).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P48730-1",
"P49674-1",
"Q03164-1",
"Q92793-1",
"O15516-1"
],
"evidence": [
{
"id": "R-HSA-9922273",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9922273"
}
]
},
{
"id": "R-HSA-9922982",
"name": "p-S90-BMAL1:p-T451,T461-CLOCK,p-NPAS2 and coactivators bind the PER1 gene",
"equation": "",
"summary": "A dimer of the phosphorylated BMAL1:CLOCK heterodimer binds adjacent E-boxes (EE element, E1E2 element) in the promoter of the PER1 gene (inferred from mouse homologs). Phosphorylated BMAL1:CLOCK also binds three or four other sites in the PER1 promoter (inferred from mouse homologs). Phosphorylated BMAL1:CLOCK recruits the histone acetyltransferase CREBBP and the histone methyltransferase KMT2A (MLL1) (inferred from the Bmal1:Clock complex at the Per2 promoter in Katada and Sassone-Corsi 2010). CREBBP interacts with BMAL1 and KMT2A interacts with CLOCK (inferred from mouse homologs). KMT2A forms MLL1 complexes with other factors but it is unknown which of these factors are present in the complex with BMAL1:CLOCK. NPAS2 can dimerize with BMAL1 in place of CLOCK and the BMAL1:NPAS2 heterodimer binds E-boxes and regulates expression of PER1 (inferred from mouse homologs).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q03164-1",
"Q92793-1",
"O15516-1"
],
"evidence": [
{
"id": "R-HSA-9922982",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9922982"
}
]
},
{
"id": "R-HSA-9922990",
"name": "Phosphorylated BMAL1:CLOCK,NPAS2 and coactivators positively regulate expression of Period-2 (PER2)",
"equation": "",
"summary": "Phosphorylated BMAL1:CLOCK (ARNTL:CLOCK) heterodimers bound to E-box sequences in the promoter of PER2 drive transcription (inferred from mouse homologs). Accumulation of PER2 mRNA begins about 4 hours after phosphorylated BMAL1:CLOCK binds and peaks in the late afternoon of the circadian cycle, significantly later than the peak of PER1 expression (Li et al. 2013, and inferred from mouse homologs). NPAS2 can heterodimerize with BMAL1 and the BMAL1:NPAS2 heterodimer binds E-boxes and regulates PER2 expression (inferred from mouse homologs).",
"cellular_location": "cytosol, nucleoplasm",
"input_participant_list": [
"R-HSA-5641227"
],
"output_participant_list": [
"R-HSA-400399"
],
"enzyme_list": [
"Q03164-1",
"Q92793-1",
"O15516-1"
],
"evidence": [
{
"id": "R-HSA-9922990",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9922990"
}
]
},
{
"id": "R-HSA-9922998",
"name": "p-S90-BMAL1:p-T451,T461-CLOCK,p-NPAS2 and coactivators bind the PER2 gene",
"equation": "",
"summary": "A dimer of phosphorylated BMAL1:CLOCK (ARNTL:CLOCK) heterodimers bind adjacent E-boxes (EE element, E1E2 element) in the promoter of the PER2 gene (inferred from mouse homologs) and recruit the histone acetyltransferase CREBBP (CBP) and the histone methyltransferase KMT2A (MLL1) to activate transcription (inferred from mouse homologs). Large scale chromatin immunoprecipitation also indicates that BMAL:CLOCK binds additional sites in the PER2 promoter (inferred from mouse homologs). NPAS2 can heterodimerize with BMAL1 in place of CLOCK, and the BMAL1:NPAS2 heterodimer binds E-boxes and regulates PER2 expression (inferred from mouse homologs).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q03164-1",
"Q92793-1",
"O15516-1"
],
"evidence": [
{
"id": "R-HSA-9922998",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9922998"
}
]
},
{
"id": "R-HSA-9923005",
"name": "p-S-CRY:p-S-PER:CSNK1D,E:p-S90,Ac-538-BMAL1:p-4S,2T-CLOCK dissociates from target gene",
"equation": "",
"summary": "After phosphorylation of CLOCK by the kinase CSNK1D, the BMAL1:CLOCK heterodimer dissociates from DNA (inferred from mouse homologs). CRY and PER proteins form a complex with CSNK1D, shuttle CSNK1D into the nucleus, and bring CSNK1D into proximity with CLOCK (inferred from mouse homologs). CSNK1E appears to act redundantly with CSNK1D. Notably, after BMAL1:CLOCK dissociates from promoters, some promoters are negatively regulated and some promoters, such as the CRY1 promoter, are positively regulated by residual PER proteins (inferred from mouse homologs in Chiou et al. 2016).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P48730-1",
"P49674-1",
"Q03164-1",
"Q92793-1",
"O15516-1"
],
"evidence": [
{
"id": "R-HSA-9923005",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9923005"
}
]
},
{
"id": "R-HSA-9923010",
"name": "p-S90-BMAL1:p-T451,T461-CLOCK and coactivators bind the NR1D1 (REV-ERBA) gene",
"equation": "",
"summary": "Phosphorylated BMAL1:CLOCK heterodimers bind multiple E-boxes in the promoter of the NR1D1 (REV-ERBA) gene (inferred from mouse homologs, also inferred from rat homologs in Triqueneaux et al. 2004). The BMAL1:CLOCK heterodimers recruit the histone methyltransferase KMT2A and the histone acetyltransferase CREBBP (inferred from mouse homologs).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q03164-1",
"Q92793-1",
"O15516-1"
],
"evidence": [
{
"id": "R-HSA-9923010",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9923010"
}
]
},
{
"id": "R-HSA-9923018",
"name": "Phosphorylated BMAL1:CLOCK positively regulates expression of NR1D1 (REV-ERBA)",
"equation": "",
"summary": "Phosphorylated BMAL1:CLOCK heterodimers bound to the promoter of the NR1D1 (REV-ERBA) gene and coactivated by PPARGC1A (PGC-1alpha) activate transcription, resulting in a circadian rhythm of expression in suprachiasmatic nucleus, liver, and kidney that peaks at mid-day in mice (inferred from mouse homologs, and inferred from rat in Triqueneaux et al. 2004). Transcription of the NR1D1 gene occurs on the opposite strand of the ERBA gene (Lazar et al.1990).
Oscillation of NR1D1 expression is also observed in cultured cells in response to serum shock (inferred from mouse cells). In the human brain, expression of NR1D1 peaks in the early morning, before the peak of PER1 expression (Li et al. 2013) and earlier than the peak of expression of mouse Nr1d1.
NR1D1 acts as a heme sensor that represses transcription of genes in response to heme and time of day (reviewed in Yin et al. 2010). Notably NR1D1:heme represses transcription of PPARG1CA, a positive regulator of heme biosynthesis, thus maintaining heme homeostasis (Wu et al. 2009). NR1D1:heme also regulates transcription of INSIG1 and INSIG2 (inferred from mouse homologs in Martelot et al. 2009), sterol sensors that interact with SREBF1 (SREBP1), an activator of sterol biosynthesis. NR1D1 is a component of the secondary loop of the circadian clock which regulates expression of BMAL1, CLOCK, and NPAS2 (reviewed in Cox and Takahashi 2019).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q03164-1",
"Q92793-1",
"O15516-1"
],
"evidence": [
{
"id": "R-HSA-9923018",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9923018"
}
]
},
{
"id": "R-HSA-9925647",
"name": "Phosphorylated BMAL1:CLOCK and coactivators positively regulate expression of Cryptochrome-2 (CRY2)",
"equation": "",
"summary": "Phosphorylated BMAL1:CLOCK and the histone acetyltransferase CREBBP (CBP) bind the promoter of the CRY2 gene (inferred from mouse homologs) and activate transcription. CRY2 is expressed rhythmically in some tissues but without periodicity in other tissues and shows some cell-type specificity (inferred from mouse homologs). Expression of CRY2 is weak in the suprachiasmatic nucleus and is rhythmic in liver and kidney, but not in spleen, thymus, testis, or blood (inferred from mouse homologs).",
"cellular_location": "cytosol, nucleoplasm",
"input_participant_list": [
"R-HSA-5641201"
],
"output_participant_list": [
"R-HSA-400255"
],
"enzyme_list": [
"Q03164-1",
"Q92793-1",
"O15516-1"
],
"evidence": [
{
"id": "R-HSA-9925647",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9925647"
}
]
},
{
"id": "R-HSA-9925650",
"name": "p-S90-BMAL1:p-T451,T461-CLOCK and coactivators bind the CRY2 gene",
"equation": "",
"summary": "Phosphoryated BMAL1:CLOCK heterodimers bind two E-boxes in the CRY2 promoter and recruit the histone methyltransferase KMT2A (MLL1) and the histone acetyltransferase CREBBP (CBP) (inferred from mouse homologs). KMT2A interacts with CLOCK and CREBBP interacts with BMAL1 (inferred from mouse homologs). KMT2A is part of larger MLL1 complexes, however the binding of other components of the MLL1 complexes has not been demonstrated.",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q03164-1",
"Q92793-1",
"O15516-1"
],
"evidence": [
{
"id": "R-HSA-9925650",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9925650"
}
]
},
{
"id": "R-HSA-9925861",
"name": "Phosphorylated BMAL1:CLOCK and coactivators positively regulate expression of RORC",
"equation": "",
"summary": "BMAL1:CLOCK binds one site in the RORC gene and enhances expression of RORC (inferred from mouse homologs). Binding of BMAL1:CLOCK precedes accumulation of pre-mRNA by several hours, therefore additional levels of regulation may exist (inferred from mouse homologs). In mice, expression of the Rorgamma isoform shows circadian oscillation while expression of the Rorgammat isoform is independent of the circadian clock (Mongrain et al. 2008).",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-8948433"
],
"output_participant_list": [
"R-HSA-446177"
],
"enzyme_list": [
"Q03164-1",
"Q92793-1",
"O15516-1"
],
"evidence": [
{
"id": "R-HSA-9925861",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9925861"
}
]
},
{
"id": "R-HSA-9925862",
"name": "p-S90-BMAL1:p-T451,T461-CLOCK and coactivators bind the RORC gene",
"equation": "",
"summary": "A phosphorylated BMAL1:CLOCK heterodimer binds a site near the RORC gene and recruits the histone acetyltransferase CREBBP and the histone methyltransferase KMT2A (inferred from mouse homologs).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q03164-1",
"Q92793-1",
"O15516-1"
],
"evidence": [
{
"id": "R-HSA-9925862",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9925862"
}
]
},
{
"id": "R-HSA-9926478",
"name": "MITF-M binds CREBBP,EP300",
"equation": "",
"summary": "MITF-M interacts with CREBBP and EP300 to activate expression at target genes (Sato et al, 1997; Brown et al, 2023 a,b). Interaction is mediated by two transactivation domains (TAD) in MITF-M, one at the N-terminal and one in the disordered C-terminal region ((Sato et al, 1997; Brown et al, 2023 a,b). Both regions of MITF-M interact with the TAZ1 and TAZ2 domains of the histone acetyltransferases (Brown et al, 2023 a,b). Some studies have shown that the interaction between MITF and CREBBP and EP300 is enhanced by MAPK1-dependent phosphorylation of MITF-M at serine 73, however other studies have not reproduced this effect (Price et al, 1998; Xu et al, 2000; Sato et al, 1997)",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9926478",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9926478"
}
]
},
{
"id": "R-HSA-9926482",
"name": "CREBBP, EP300 acetylate MITF-M",
"equation": "",
"summary": "MITF-M is acteylated on lysine 206 by CREBBP or EP300. Acetylation decreases the DNA-binding affinity at MITF-M target sites genome-wide, with a more pronounced decrease at differentiation-specific CATGTG motifs relative to canonical CACGTG elements. In this way, acetylation may contribute to the regulation of differentiation by titrating MITF-M away from differentiation-specific target genes (Louphrasitthiphol et al, 2023).
MAPK-dependent phosphorylation of MITF has been shown to promote the recruitment of CREBBP/EP300 (Price et al, 1998). In a study unrelated to MITF, MAPK signaling was shown to promote the phosphorylation of CREBBP/EP300, increasing its histone acetyltransferase activity (Chen et al, 2007). These studies suggest a possible link between proliferative MAPK signaling and a decrease in MITF-dependent differentiation-specific gene expression. Consistent with this, the acetylation mimetic mutation K206Q has been identified in families with Waardenburg syndrome Type 2, displaying defects in pigmentation and hearing (Leger et al, 2012).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q09472-1",
"Q92793-1"
],
"evidence": [
{
"id": "R-HSA-9926482",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9926482"
}
]
},
{
"id": "R-HSA-9929319",
"name": "p-90-BMAL1:p-T451,T461-CLOCK and coactivators bind the DBP gene",
"equation": "",
"summary": "Phosphorylated BMAL1:CLOCK binds an E-box located in the promoter and two E-boxes located in introns of the DBP gene (inferred from mouse homologs). BMAL1:CLOCK at the DBP promoter is highly unstable and inhibition of its proteolysis causes inhibition of its transcription activation activity, suggesting that BMAL1:CLOCK may be a \\kamikaze\\ transcription factor (inferred from mouse homologs). Phosphorylated BMAL1:CLOCK recruits the histone methyltransferase KMT2A (MLL1) and the histone acetyltransferase CREBBP through an interaction between KMT2A and CLOCK (inferred from mouse homologs in Katada and Sassone-Corsi 2010) and an interaction between BMAL1 and CREBBP (inferred from mouse homologs Garg et al. 2019).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q03164-1",
"Q92793-1",
"O15516-1"
],
"evidence": [
{
"id": "R-HSA-9929319",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9929319"
}
]
},
{
"id": "R-HSA-9929321",
"name": "Phosphorylated BMAL1:CLOCK and coactivators positively regulate expression of DBP",
"equation": "",
"summary": "Phosphorylated BMAL1:CLOCK binds E-boxes in the promoter of the DBP gene and activates transcription (inferred from mouse homologs). DBP protein then binds D-boxes in promoters of circadian genes such as PER1 and enhances transcription (inferred from mouse homologs). DBP is expressed in a circadian rhythm in the suprachiasmatic nucleus (inferred from mouse homologs). Levels of DBP mRNA are highest in the morning (inferred from mouse homologs).",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-5641228"
],
"output_participant_list": [
"R-HSA-879796"
],
"enzyme_list": [
"Q03164-1",
"Q92793-1",
"O15516-1"
],
"evidence": [
{
"id": "R-HSA-9929321",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9929321"
}
]
},
{
"id": "R-HSA-9976117",
"name": "STAT6, NFATC2 (NFAT1), and NICD1,2 bind the GATA3 gene and cause displacement of repressor complexes (PRC1, RBPJ:NCOR) by activator complexes (MLL1, RBPJ:NICD1,2)",
"equation": "",
"summary": "IL4 signaling via IL4RA produces phosphorylated STAT6 dimers (reviewed in Keegan et al. 2021), which enter the nucleus and bind intronic regions within the the GATA3 gene (inferred from mouse homologs in Wei et al. 2010, Onodera et al. 2010) and in the proximal and distal promoters of GATA3 (inferred from mouse homologs in Scheinman and Avni 2009). Binding of phosphorylated STAT6 causes displacement of repressive PRC1 complexes and recruitment of MLL1 complexes (inferred from mouse homologs in Onodera et al. 2010).
Signaling by the T cell receptor results in increased cytosolic Ca2+, which activates calcineurin to dephosphorylate NFATC2 (NFAT1)(inferred from mouse homologs in Scheinman and Avni 2009), enabling it to translocate to the nucleus and to bind 3 conserved noncoding sequences, the distal promoter, and the proximal promoter of the GATA3 gene (inferred from mouse homologs in Scheinman and Avni 2009).
In mice, Notch1 and Notch2 (present in T cells) can get activated by their ligands Jagged1/Jagged2 (present in Antigen Presenting Cells), leading to an enhanced expression of Gata3 (Amsen et al. 2004, 2007, Fang et al. 2007).
In more detail, after Notch1/2 activation, the protein undergoes a proteolytic cleavage, which results in the release of the intracellular domain (NICD) from the membrane. NICD translocates to the nucleus where it associates with the DNA-binding factor RBP-J, which is already bound to the upstream (distal) promoter of the GATA3 gene, about 10 kb upstream of the proximal promoter (inferred from mouse homologs in Amsen et al. 2007, Fang et al. 2007). NICD1,2 causes displacement of RBPJ-bound NCOR corepressors by MAML and coactivators.",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92830-1",
"O00257-1",
"P56524-1",
"O15379-1",
"Q8WUI4-1",
"Q9UQL6-1",
"Q09472-1",
"Q03164-1",
"Q92793-1",
"Q13547-1",
"Q9UBN7-1",
"Q96DB2-1",
"Q9UKV0-1",
"Q92769-1",
"Q06587-1",
"Q99496-1",
"Q92831-1",
"Q9BY41-1",
"Q969S8-1"
],
"evidence": [
{
"id": "R-HSA-9976117",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9976117"
}
]
},
{
"id": "R-HSA-9976143",
"name": "STAT6, NFATC2 (NFAT1), and NICD1,2 positively regulate expression of GATA3",
"equation": "",
"summary": "IL4 signaling produces phosphorylated STAT6 dimers and T cell receptor signaling produces dephosphorylated NFATC2 (NFAT1), both of which bind to the GATA3 gene and activate its expression (inferred from mouse homologs in Scheinman and Avni 2009, Wei et al. 2010, Onodera et al. 2010). Phosphorylated STAT6 dimers recruit MLL1 complexes to positively regulate transcription (inferred from mouse homologs in Onodera et al. 2010). Activation of NOTCH1,2 signaling by JAGGED1 or JAGGED2 located on antigen presenting cells results in generation of NICD1,2, the intracellular cleavage product of NOTCH1,2, which binds to RBPJ at the upstream promoter of the GATA3 gene and recruits coactivators to enhance its transcription (inferred from mouse homologs in Amsen et al. 2004, 2007, Fang et al. 2007).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92830-1",
"Q09472-1",
"Q03164-1",
"Q92793-1",
"Q92831-1"
],
"evidence": [
{
"id": "R-HSA-9976143",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9976143"
}
]
}
],
"reaction_participants": [
{
"participant_id": "R-COV-9756485",
"participant_name": "SUMO1-K62,ADPr-,p-11S,2T,met-2R,Ac-K375-N dimer [cytosol]",
"crossref": [
{
"id": "0100096",
"database": "Mondo",
"url": ""
}
]
},
{
"participant_id": "R-HSA-1183052",
"participant_name": "ADIPOQ [extracellular region]",
"crossref": [
{
"id": "Q15848",
"database": "Pharos - Targets",
"url": ""
},
{
"id": "ADIPOQ",
"database": "GeneCards",
"url": ""
},
{
"id": "ENSP00000389814",
"database": "ENSEMBL",
"url": ""
},
{
"id": "4DOU",
"database": "PDB",
"url": ""
},
{
"id": "NP_001171271.1",
"database": "RefSeq",
"url": ""
},
{
"id": "ENSG00000181092-ADIPOQ",
"database": "HPA",
"url": ""
},
{
"id": "ENST00000444204",
"database": "ENSEMBL",
"url": ""
},
{
"id": "6U66",
"database": "PDB",
"url": ""
},
{
"id": "Q15848",
"database": "UniProt",
"url": ""
},
{
"id": "6U6N",
"database": "PDB",
"url": ""
},
{
"id": "ENSP00000320709",
"database": "ENSEMBL",
"url": ""
},
{
"id": "NP_004788.1",
"database": "RefSeq",
"url": ""
},
{
"id": "HMDBP02512",
"database": "HMDB Protein",
"url": ""
},
{
"id": "ENSG00000181092",
"database": "ENSEMBL",
"url": ""
},
{
"id": "ENSG00000181092",
"database": "OpenTargets",
"url": ""
},
{
"id": "ENST00000320741",
"database": "ENSEMBL",
"url": ""
},
{
"id": "Q15848",
"database": "PRO",
"url": ""
}
]
},
{
"participant_id": "R-HSA-1235065",
"participant_name": "CA9 [plasma membrane]",
"crossref": [
{
"id": "6RQU",
"database": "PDB",
"url": ""
},
{
"id": "6RQQ",
"database": "PDB",
"url": ""
},
{
"id": "Q16790",
"database": "PRO",
"url": ""
},
{
"id": "CAH9_HUMAN",
"database": "ZINC - Substances",
"url": ""
},
{
"id": "6FE2",
"database": "PDB",
"url": ""
},
{
"id": "CA9",
"database": "GeneCards",
"url": ""
},
{
"id": "6G9U",
"database": "PDB",
"url": ""
},
{
"id": "ENSG00000107159",
"database": "ENSEMBL",
"url": ""
},
{
"id": "8CO0",
"database": "PDB",
"url": ""
},
{
"id": "CAH9_HUMAN",
"database": "ZINC - FDA approved",
"url": ""
},
{
"id": "8Q18",
"database": "PDB",
"url": ""
},
{
"id": "4.2.1.1",
"database": "IntEnz",
"url": ""
},
{
"id": "Q16790",
"database": "UniProt",
"url": ""
},
{
"id": "3IAI",
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{
"id": "ENSG00000177666-PNPLA2",
"database": "HPA",
"url": ""
},
{
"id": "Q96AD5",
"database": "Pharos - Targets",
"url": ""
},
{
"id": "3253",
"database": "Guide to Pharmacology - Targets",
"url": ""
},
{
"id": "Q96AD5",
"database": "UniProt",
"url": ""
},
{
"id": "Q96AD5",
"database": "GlyGen",
"url": ""
},
{
"id": "PNPLA2",
"database": "Orphanet",
"url": ""
},
{
"id": "ENSP00000337701",
"database": "ENSEMBL",
"url": ""
},
{
"id": "NP_065109.1",
"database": "RefSeq",
"url": ""
},
{
"id": "HMDBP07347",
"database": "HMDB Protein",
"url": ""
},
{
"id": "ENST00000336615",
"database": "ENSEMBL",
"url": ""
},
{
"id": "Q96AD5",
"database": "PRO",
"url": ""
},
{
"id": "ENSG00000177666",
"database": "ENSEMBL",
"url": ""
},
{
"id": "ENSG00000177666",
"database": "OpenTargets",
"url": ""
},
{
"id": "PNPLA2",
"database": "GeneCards",
"url": ""
}
]
},
{
"participant_id": "R-HSA-9909379",
"participant_name": "PER3 gene [nucleoplasm]",
"crossref": [
{
"id": "ENSG00000049246",
"database": "ENSEMBL",
"url": ""
}
]
},
{
"participant_id": "R-HSA-9909617",
"participant_name": "CD274 mRNA [cytosol]",
"crossref": [
{
"id": "ENST00000381573.3",
"database": "ENSEMBL",
"url": ""
}
]
}
],
"reaction_enzymes": [
{
"uniprot_ac": "O00257",
"gene_name": "CBX4",
"activity": [
{
"ec_number": "2.3.2.-",
"activity": "",
"evidence": [
{
"id": "O00257",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O00257"
}
]
}
]
},
{
"uniprot_ac": "O00767",
"gene_name": "SCD",
"activity": [
{
"ec_number": "1.14.19.1",
"activity": "octadecanoyl-CoA + 2 Fe(II)-[cytochrome b5] + O2 + 2 H(+) = (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O.",
"evidence": [
{
"id": "O00767",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O00767"
}
]
},
{
"ec_number": "1.14.19.1",
"activity": "",
"evidence": [
{
"id": "O00767",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O00767"
}
]
}
]
},
{
"uniprot_ac": "O14686",
"gene_name": "KMT2D",
"activity": [
{
"ec_number": "2.1.1.364",
"activity": "L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine + H(+).",
"evidence": [
{
"id": "O14686",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O14686"
}
]
},
{
"ec_number": "2.1.1.364",
"activity": "",
"evidence": [
{
"id": "O14686",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O14686"
}
]
}
]
},
{
"uniprot_ac": "O14929",
"gene_name": "HAT1",
"activity": [
{
"ec_number": "2.3.1.48",
"activity": "L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+).",
"evidence": [
{
"id": "O14929",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O14929"
}
]
},
{
"ec_number": "2.3.1.-",
"activity": "",
"evidence": [
{
"id": "O14929",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O14929"
}
]
},
{
"ec_number": "2.3.1.48",
"activity": "",
"evidence": [
{
"id": "O14929",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O14929"
}
]
}
]
},
{
"uniprot_ac": "O15120",
"gene_name": "AGPAT2",
"activity": [
{
"ec_number": "2.3.1.51",
"activity": "a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA.",
"evidence": [
{
"id": "O15120",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O15120"
}
]
},
{
"ec_number": "2.3.1.51",
"activity": "",
"evidence": [
{
"id": "O15120",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O15120"
}
]
}
]
},
{
"uniprot_ac": "O15379",
"gene_name": "HDAC3",
"activity": [
{
"ec_number": "3.5.1.-",
"activity": "",
"evidence": [
{
"id": "O15379",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O15379"
}
]
},
{
"ec_number": "3.5.1.98",
"activity": "N(6)-acetyl-L-lysyl-[histone] + H2O = L-lysyl-[histone] + acetate.",
"evidence": [
{
"id": "O15379",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O15379"
}
]
},
{
"ec_number": "3.5.1.98",
"activity": "",
"evidence": [
{
"id": "O15379",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O15379"
}
]
}
]
},
{
"uniprot_ac": "O15438",
"gene_name": "ABCC3",
"activity": [
{
"ec_number": "7.6.2.2",
"activity": "daunorubicin(in) + ATP + H2O = daunorubicin(out) + ADP + phosphate + H(+).",
"evidence": [
{
"id": "O15438",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O15438"
}
]
},
{
"ec_number": "7.6.2.-",
"activity": "",
"evidence": [
{
"id": "O15438",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O15438"
}
]
},
{
"ec_number": "7.6.2.3",
"activity": "an S-substituted glutathione(in) + ATP + H2O = an S-substituted glutathione(out) + ADP + phosphate + H(+).",
"evidence": [
{
"id": "O15438",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O15438"
}
]
},
{
"ec_number": "7.6.2.2",
"activity": "",
"evidence": [
{
"id": "O15438",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O15438"
}
]
},
{
"ec_number": "7.6.2.3",
"activity": "",
"evidence": [
{
"id": "O15438",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O15438"
}
]
}
]
},
{
"uniprot_ac": "O15516",
"gene_name": "CLOCK",
"activity": [
{
"ec_number": "2.3.1.48",
"activity": "L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+).",
"evidence": [
{
"id": "O15516",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O15516"
}
]
},
{
"ec_number": "2.3.1.48",
"activity": "",
"evidence": [
{
"id": "O15516",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O15516"
}
]
}
]
},
{
"uniprot_ac": "O15550",
"gene_name": "KDM6A",
"activity": [
{
"ec_number": "1.14.11.68",
"activity": "N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 2 2-oxoglutarate + 2 O2 = N(6)-methyl-L-lysyl(27)-[histone H3] + 2 formaldehyde + 2 succinate + 2 CO2.",
"evidence": [
{
"id": "O15550",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O15550"
}
]
},
{
"ec_number": "1.14.11.68",
"activity": "",
"evidence": [
{
"id": "O15550",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O15550"
}
]
}
]
},
{
"uniprot_ac": "O60318",
"gene_name": "MCM3AP",
"activity": [
{
"ec_number": "2.3.1.48",
"activity": "L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+).",
"evidence": [
{
"id": "O60318",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O60318"
}
]
},
{
"ec_number": "2.3.1.-",
"activity": "",
"evidence": [
{
"id": "O60318",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O60318"
}
]
},
{
"ec_number": "2.3.1.48",
"activity": "",
"evidence": [
{
"id": "O60318",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O60318"
}
]
}
]
},
{
"uniprot_ac": "O60427",
"gene_name": "FADS1",
"activity": [
{
"ec_number": "1.14.19.44",
"activity": "(8Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA + 2 Fe(II)-[cytochrome b5] + O2 + 2 H(+) = (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O.",
"evidence": [
{
"id": "O60427",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O60427"
}
]
},
{
"ec_number": "1.14.19.44",
"activity": "",
"evidence": [
{
"id": "O60427",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O60427"
}
]
}
]
},
{
"uniprot_ac": "O60656",
"gene_name": "UGT1A9",
"activity": [
{
"ec_number": "2.4.1.17",
"activity": "glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + UDP + H(+).",
"evidence": [
{
"id": "O60656",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O60656"
}
]
},
{
"ec_number": "2.4.1.17",
"activity": "",
"evidence": [
{
"id": "O60656",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O60656"
}
]
}
]
},
{
"uniprot_ac": "O95251",
"gene_name": "KAT7",
"activity": [
{
"ec_number": "2.3.1.48",
"activity": "L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+).",
"evidence": [
{
"id": "O95251",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O95251"
}
]
},
{
"ec_number": "2.3.1.48",
"activity": "",
"evidence": [
{
"id": "O95251",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O95251"
}
]
}
]
},
{
"uniprot_ac": "O95477",
"gene_name": "ABCA1",
"activity": [
{
"ec_number": "7.6.2.1",
"activity": "ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.",
"evidence": [
{
"id": "O95477",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O95477"
}
]
},
{
"ec_number": "7.6.2.1",
"activity": "",
"evidence": [
{
"id": "O95477",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O95477"
}
]
}
]
},
{
"uniprot_ac": "P04798",
"gene_name": "CYP1A1",
"activity": [
{
"ec_number": "1.14.14.1",
"activity": "an organic molecule + reduced [NADPH--hemoprotein reductase] + O2 = an alcohol + oxidized [NADPH--hemoprotein reductase] + H2O + H(+).",
"evidence": [
{
"id": "P04798",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P04798"
}
]
},
{
"ec_number": "1.14.14.1",
"activity": "",
"evidence": [
{
"id": "P04798",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P04798"
}
]
},
{
"ec_number": "4.2.1.152",
"activity": "(12R)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-oxo-(5Z,8Z,10E,14Z)-eicosatetraenoate + H2O.",
"evidence": [
{
"id": "P04798",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P04798"
}
]
}
]
},
{
"uniprot_ac": "P06858",
"gene_name": "LPL",
"activity": [
{
"ec_number": "3.1.1.32",
"activity": "a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+).",
"evidence": [
{
"id": "P06858",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P06858"
}
]
},
{
"ec_number": "3.1.1.34",
"activity": "a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+).",
"evidence": [
{
"id": "P06858",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P06858"
}
]
},
{
"ec_number": "3.1.1.34",
"activity": "",
"evidence": [
{
"id": "P06858",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P06858"
}
]
}
]
},
{
"uniprot_ac": "P08263",
"gene_name": "GSTA1",
"activity": [
{
"ec_number": "1.11.1.-",
"activity": "",
"evidence": [
{
"id": "P08263",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P08263"
}
]
},
{
"ec_number": "5.3.3.-",
"activity": "",
"evidence": [
{
"id": "P08263",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P08263"
}
]
},
{
"ec_number": "2.5.1.18",
"activity": "RX + glutathione = an S-substituted glutathione + a halide anion + H(+).",
"evidence": [
{
"id": "P08263",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P08263"
}
]
},
{
"ec_number": "2.5.1.18",
"activity": "",
"evidence": [
{
"id": "P08263",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P08263"
}
]
}
]
},
{
"uniprot_ac": "P08294",
"gene_name": "SOD3",
"activity": [
{
"ec_number": "1.15.1.1",
"activity": "2 superoxide + 2 H(+) = H2O2 + O2.",
"evidence": [
{
"id": "P08294",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P08294"
}
]
},
{
"ec_number": "1.15.1.1",
"activity": "",
"evidence": [
{
"id": "P08294",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P08294"
}
]
}
]
},
{
"uniprot_ac": "P11142",
"gene_name": "HSPA8",
"activity": [
{
"ec_number": "3.6.4.10",
"activity": "ATP + H2O = ADP + phosphate + H(+).",
"evidence": [
{
"id": "P11142",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P11142"
}
]
},
{
"ec_number": "3.6.4.10",
"activity": "",
"evidence": [
{
"id": "P11142",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P11142"
}
]
}
]
},
{
"uniprot_ac": "P11310",
"gene_name": "ACADM",
"activity": [
{
"ec_number": "1.3.8.7",
"activity": "a medium-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = a medium-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein].",
"evidence": [
{
"id": "P11310",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P11310"
}
]
},
{
"ec_number": "1.3.8.7",
"activity": "",
"evidence": [
{
"id": "P11310",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P11310"
}
]
}
]
},
{
"uniprot_ac": "P11362",
"gene_name": "FGFR1",
"activity": [
{
"ec_number": "2.7.10.1",
"activity": "L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P11362",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P11362"
}
]
},
{
"ec_number": "2.7.10.1",
"activity": "",
"evidence": [
{
"id": "P11362",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P11362"
}
]
}
]
},
{
"uniprot_ac": "P11413",
"gene_name": "G6PD",
"activity": [
{
"ec_number": "1.-.-.-",
"activity": "",
"evidence": [
{
"id": "P11413",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P11413"
}
]
},
{
"ec_number": "1.1.1.49",
"activity": "D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + NADPH + H(+).",
"evidence": [
{
"id": "P11413",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P11413"
}
]
},
{
"ec_number": "1.1.1.49",
"activity": "",
"evidence": [
{
"id": "P11413",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P11413"
}
]
}
]
},
{
"uniprot_ac": "P11802",
"gene_name": "CDK4",
"activity": [
{
"ec_number": "2.7.11.22",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P11802",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P11802"
}
]
},
{
"ec_number": "2.7.11.22",
"activity": "",
"evidence": [
{
"id": "P11802",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P11802"
}
]
}
]
},
{
"uniprot_ac": "P13196",
"gene_name": "ALAS1",
"activity": [
{
"ec_number": "2.3.1.37",
"activity": "succinyl-CoA + glycine + H(+) = 5-aminolevulinate + CO2 + CoA.",
"evidence": [
{
"id": "P13196",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P13196"
}
]
},
{
"ec_number": "2.3.1.37",
"activity": "",
"evidence": [
{
"id": "P13196",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P13196"
}
]
}
]
},
{
"uniprot_ac": "P15559",
"gene_name": "NQO1",
"activity": [
{
"ec_number": "1.6.5.2",
"activity": "a quinone + NADPH + H(+) = a quinol + NADP(+).",
"evidence": [
{
"id": "P15559",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P15559"
}
]
},
{
"ec_number": "1.6.5.2",
"activity": "",
"evidence": [
{
"id": "P15559",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P15559"
}
]
}
]
},
{
"uniprot_ac": "P21439",
"gene_name": "ABCB4",
"activity": [
{
"ec_number": "7.6.2.1",
"activity": "ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.",
"evidence": [
{
"id": "P21439",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P21439"
}
]
},
{
"ec_number": "7.6.2.1",
"activity": "",
"evidence": [
{
"id": "P21439",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P21439"
}
]
}
]
},
{
"uniprot_ac": "P21675",
"gene_name": "TAF1",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P21675",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P21675"
}
]
},
{
"ec_number": "2.3.1.48",
"activity": "L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+).",
"evidence": [
{
"id": "P21675",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P21675"
}
]
},
{
"ec_number": "2.3.1.48",
"activity": "",
"evidence": [
{
"id": "P21675",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P21675"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "P21675",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P21675"
}
]
}
]
},
{
"uniprot_ac": "P22680",
"gene_name": "CYP7A1",
"activity": [
{
"ec_number": "1.14.14.23",
"activity": "cholesterol + reduced [NADPH--hemoprotein reductase] + O2 = 7alpha-hydroxycholesterol + oxidized [NADPH--hemoprotein reductase] + H2O + H(+).",
"evidence": [
{
"id": "P22680",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P22680"
}
]
},
{
"ec_number": "1.14.14.26",
"activity": "(24S)-hydroxycholesterol + reduced [NADPH--hemoprotein reductase] + O2 = (24S)-7alpha-dihydroxycholesterol + oxidized [NADPH--hemoprotein reductase] + H2O + H(+).",
"evidence": [
{
"id": "P22680",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P22680"
}
]
}
]
},
{
"uniprot_ac": "P23786",
"gene_name": "CPT2",
"activity": [
{
"ec_number": "2.3.1.21",
"activity": "(R)-carnitine + hexadecanoyl-CoA = O-hexadecanoyl-(R)-carnitine + CoA.",
"evidence": [
{
"id": "P23786",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P23786"
}
]
},
{
"ec_number": "2.3.1.21",
"activity": "",
"evidence": [
{
"id": "P23786",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P23786"
}
]
}
]
},
{
"uniprot_ac": "P24928",
"gene_name": "POLR2A",
"activity": [
{
"ec_number": "3.1.13.-",
"activity": "",
"evidence": [
{
"id": "P24928",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P24928"
}
]
},
{
"ec_number": "2.7.7.48",
"activity": "RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate.",
"evidence": [
{
"id": "P24928",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P24928"
}
]
},
{
"ec_number": "2.7.7.6",
"activity": "RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate.",
"evidence": [
{
"id": "P24928",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P24928"
}
]
},
{
"ec_number": "2.7.7.6",
"activity": "",
"evidence": [
{
"id": "P24928",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P24928"
}
]
}
]
},
{
"uniprot_ac": "P27361",
"gene_name": "MAPK3",
"activity": [
{
"ec_number": "2.7.11.24",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P27361",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P27361"
}
]
},
{
"ec_number": "2.7.11.24",
"activity": "",
"evidence": [
{
"id": "P27361",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P27361"
}
]
}
]
},
{
"uniprot_ac": "P28482",
"gene_name": "MAPK1",
"activity": [
{
"ec_number": "2.7.11.24",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P28482",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P28482"
}
]
},
{
"ec_number": "2.7.11.24",
"activity": "",
"evidence": [
{
"id": "P28482",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P28482"
}
]
}
]
},
{
"uniprot_ac": "P30876",
"gene_name": "POLR2B",
"activity": [
{
"ec_number": "3.1.13.-",
"activity": "",
"evidence": [
{
"id": "P30876",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P30876"
}
]
},
{
"ec_number": "2.7.7.48",
"activity": "RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate.",
"evidence": [
{
"id": "P30876",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P30876"
}
]
},
{
"ec_number": "2.7.7.6",
"activity": "RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate.",
"evidence": [
{
"id": "P30876",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P30876"
}
]
},
{
"ec_number": "2.7.7.6",
"activity": "",
"evidence": [
{
"id": "P30876",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P30876"
}
]
}
]
},
{
"uniprot_ac": "P33121",
"gene_name": "ACSL1",
"activity": [
{
"ec_number": "6.2.1.3",
"activity": "a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate.",
"evidence": [
{
"id": "P33121",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P33121"
}
]
},
{
"ec_number": "6.2.1.3",
"activity": "",
"evidence": [
{
"id": "P33121",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P33121"
}
]
},
{
"ec_number": "6.2.1.24",
"activity": "3,7,11,15-tetramethylhexadecanoate + ATP + CoA = phytanoyl-CoA + AMP + diphosphate.",
"evidence": [
{
"id": "P33121",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P33121"
}
]
},
{
"ec_number": "6.2.1.15",
"activity": "(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate.",
"evidence": [
{
"id": "P33121",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P33121"
}
]
},
{
"ec_number": "6.2.1.15",
"activity": "",
"evidence": [
{
"id": "P33121",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P33121"
}
]
}
]
},
{
"uniprot_ac": "P33527",
"gene_name": "ABCC1",
"activity": [
{
"ec_number": "7.6.2.2",
"activity": "daunorubicin(in) + ATP + H2O = daunorubicin(out) + ADP + phosphate + H(+).",
"evidence": [
{
"id": "P33527",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P33527"
}
]
},
{
"ec_number": "7.6.2.3",
"activity": "an S-substituted glutathione(in) + ATP + H2O = an S-substituted glutathione(out) + ADP + phosphate + H(+).",
"evidence": [
{
"id": "P33527",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P33527"
}
]
},
{
"ec_number": "7.6.2.3",
"activity": "",
"evidence": [
{
"id": "P33527",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P33527"
}
]
},
{
"ec_number": "7.6.2.2",
"activity": "",
"evidence": [
{
"id": "P33527",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P33527"
}
]
}
]
},
{
"uniprot_ac": "P35558",
"gene_name": "PCK1",
"activity": [
{
"ec_number": "4.1.1.32",
"activity": "ITP + oxaloacetate = IDP + phosphoenolpyruvate + CO2.",
"evidence": [
{
"id": "P35558",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P35558"
}
]
},
{
"ec_number": "2.7.11.-",
"activity": "",
"evidence": [
{
"id": "P35558",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P35558"
}
]
},
{
"ec_number": "4.1.1.32",
"activity": "",
"evidence": [
{
"id": "P35558",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P35558"
}
]
}
]
},
{
"uniprot_ac": "P37268",
"gene_name": "FDFT1",
"activity": [
{
"ec_number": "2.5.1.21",
"activity": "2 (2E,6E)-farnesyl diphosphate + NADH + H(+) = squalene + 2 diphosphate + NAD(+).",
"evidence": [
{
"id": "P37268",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P37268"
}
]
},
{
"ec_number": "2.5.1.21",
"activity": "",
"evidence": [
{
"id": "P37268",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P37268"
}
]
}
]
},
{
"uniprot_ac": "P48163",
"gene_name": "ME1",
"activity": [
{
"ec_number": "1.1.1.40",
"activity": "(S)-malate + NADP(+) = pyruvate + CO2 + NADPH.",
"evidence": [
{
"id": "P48163",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P48163"
}
]
},
{
"ec_number": "1.1.1.40",
"activity": "",
"evidence": [
{
"id": "P48163",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P48163"
}
]
}
]
},
{
"uniprot_ac": "P48506",
"gene_name": "GCLC",
"activity": [
{
"ec_number": "6.3.2.2",
"activity": "L-cysteine + L-glutamate + ATP = gamma-L-glutamyl-L-cysteine + ADP + phosphate + H(+).",
"evidence": [
{
"id": "P48506",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P48506"
}
]
},
{
"ec_number": "6.3.2.2",
"activity": "",
"evidence": [
{
"id": "P48506",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P48506"
}
]
}
]
},
{
"uniprot_ac": "P48730",
"gene_name": "CSNK1D",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P48730",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P48730"
}
]
},
{
"ec_number": "2.7.11.26",
"activity": "L-seryl-[tau protein] + ATP = O-phospho-L-seryl-[tau protein] + ADP + H(+).",
"evidence": [
{
"id": "P48730",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P48730"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "P48730",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P48730"
}
]
}
]
},
{
"uniprot_ac": "P49336",
"gene_name": "CDK8",
"activity": [
{
"ec_number": "2.7.11.22",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P49336",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P49336"
}
]
},
{
"ec_number": "2.7.11.23",
"activity": "[DNA-directed RNA polymerase] + ATP = phospho-[DNA-directed RNA polymerase] + ADP + H(+).",
"evidence": [
{
"id": "P49336",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P49336"
}
]
},
{
"ec_number": "2.7.11.23",
"activity": "",
"evidence": [
{
"id": "P49336",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P49336"
}
]
},
{
"ec_number": "2.7.11.22",
"activity": "",
"evidence": [
{
"id": "P49336",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P49336"
}
]
}
]
},
{
"uniprot_ac": "P49674",
"gene_name": "CSNK1E",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P49674",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P49674"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "P49674",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P49674"
}
]
}
]
},
{
"uniprot_ac": "P49773",
"gene_name": "HINT1",
"activity": [
{
"ec_number": "3.4.22.-",
"activity": "",
"evidence": [
{
"id": "P49773",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P49773"
}
]
},
{
"ec_number": "3.9.1.-",
"activity": "",
"evidence": [
{
"id": "P49773",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P49773"
}
]
}
]
},
{
"uniprot_ac": "P50416",
"gene_name": "CPT1A",
"activity": [
{
"ec_number": "2.3.1.21",
"activity": "(R)-carnitine + hexadecanoyl-CoA = O-hexadecanoyl-(R)-carnitine + CoA.",
"evidence": [
{
"id": "P50416",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P50416"
}
]
},
{
"ec_number": "2.3.1.-",
"activity": "",
"evidence": [
{
"id": "P50416",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P50416"
}
]
},
{
"ec_number": "2.3.1.21",
"activity": "",
"evidence": [
{
"id": "P50416",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P50416"
}
]
}
]
},
{
"uniprot_ac": "P52209",
"gene_name": "PGD",
"activity": [
{
"ec_number": "1.1.1.44",
"activity": "6-phospho-D-gluconate + NADP(+) = D-ribulose 5-phosphate + CO2 + NADPH.",
"evidence": [
{
"id": "P52209",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P52209"
}
]
},
{
"ec_number": "1.1.1.44",
"activity": "",
"evidence": [
{
"id": "P52209",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P52209"
}
]
}
]
},
{
"uniprot_ac": "P54868",
"gene_name": "HMGCS2",
"activity": [
{
"ec_number": "2.3.3.10",
"activity": "acetoacetyl-CoA + acetyl-CoA + H2O = (3S)-3-hydroxy-3-methylglutaryl-CoA + CoA + H(+).",
"evidence": [
{
"id": "P54868",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P54868"
}
]
},
{
"ec_number": "2.3.3.10",
"activity": "",
"evidence": [
{
"id": "P54868",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P54868"
}
]
}
]
},
{
"uniprot_ac": "P56524",
"gene_name": "HDAC4",
"activity": [
{
"ec_number": "3.5.1.98",
"activity": "N(6)-acetyl-L-lysyl-[histone] + H2O = L-lysyl-[histone] + acetate.",
"evidence": [
{
"id": "P56524",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P56524"
}
]
},
{
"ec_number": "3.5.1.98",
"activity": "",
"evidence": [
{
"id": "P56524",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P56524"
}
]
}
]
},
{
"uniprot_ac": "P57059",
"gene_name": "SIK1",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P57059",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P57059"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "P57059",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P57059"
}
]
}
]
},
{
"uniprot_ac": "P62736",
"gene_name": "ACTA2",
"activity": [
{
"ec_number": "3.6.4.-",
"activity": "",
"evidence": [
{
"id": "P62736",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P62736"
}
]
}
]
},
{
"uniprot_ac": "P63279",
"gene_name": "UBE2I",
"activity": [
{
"ec_number": "2.3.2.-",
"activity": "",
"evidence": [
{
"id": "P63279",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P63279"
}
]
}
]
},
{
"uniprot_ac": "P78537",
"gene_name": "BLOC1S1",
"activity": [
{
"ec_number": "2.3.1.-",
"activity": "",
"evidence": [
{
"id": "P78537",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P78537"
}
]
}
]
},
{
"uniprot_ac": "Q00403",
"gene_name": "GTF2B",
"activity": [
{
"ec_number": "2.3.1.48",
"activity": "L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+).",
"evidence": [
{
"id": "Q00403",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q00403"
}
]
},
{
"ec_number": "2.3.1.48",
"activity": "",
"evidence": [
{
"id": "Q00403",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q00403"
}
]
}
]
},
{
"uniprot_ac": "Q00535",
"gene_name": "CDK5",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q00535",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q00535"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "Q00535",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q00535"
}
]
}
]
},
{
"uniprot_ac": "Q01581",
"gene_name": "HMGCS1",
"activity": [
{
"ec_number": "2.3.3.10",
"activity": "acetoacetyl-CoA + acetyl-CoA + H2O = (3S)-3-hydroxy-3-methylglutaryl-CoA + CoA + H(+).",
"evidence": [
{
"id": "Q01581",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q01581"
}
]
},
{
"ec_number": "2.3.3.10",
"activity": "",
"evidence": [
{
"id": "Q01581",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q01581"
}
]
}
]
},
{
"uniprot_ac": "Q02928",
"gene_name": "CYP4A11",
"activity": [
{
"ec_number": "1.14.14.1",
"activity": "an organic molecule + reduced [NADPH--hemoprotein reductase] + O2 = an alcohol + oxidized [NADPH--hemoprotein reductase] + H2O + H(+).",
"evidence": [
{
"id": "Q02928",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q02928"
}
]
},
{
"ec_number": "1.14.14.80",
"activity": "hexadecanoate + reduced [NADPH--hemoprotein reductase] + O2 = 16-hydroxyhexadecanoate + oxidized [NADPH--hemoprotein reductase] + H2O + H(+).",
"evidence": [
{
"id": "Q02928",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q02928"
}
]
},
{
"ec_number": "1.14.14.1",
"activity": "",
"evidence": [
{
"id": "Q02928",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q02928"
}
]
}
]
},
{
"uniprot_ac": "Q03164",
"gene_name": "KMT2A",
"activity": [
{
"ec_number": "2.1.1.-",
"activity": "",
"evidence": [
{
"id": "Q03164",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q03164"
}
]
},
{
"ec_number": "2.1.1.364",
"activity": "L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine + H(+).",
"evidence": [
{
"id": "Q03164",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q03164"
}
]
},
{
"ec_number": "2.1.1.364",
"activity": "",
"evidence": [
{
"id": "Q03164",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q03164"
}
]
}
]
},
{
"uniprot_ac": "Q05469",
"gene_name": "LIPE",
"activity": [
{
"ec_number": "3.1.1.23",
"activity": "Hydrolyzes glycerol monoesters of long-chain fatty acids.",
"evidence": [
{
"id": "Q05469",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q05469"
}
]
},
{
"ec_number": "3.1.1.79",
"activity": "a monoacylglycerol + H2O = glycerol + a fatty acid + H(+).",
"evidence": [
{
"id": "Q05469",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q05469"
}
]
},
{
"ec_number": "3.1.1.23",
"activity": "",
"evidence": [
{
"id": "Q05469",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q05469"
}
]
},
{
"ec_number": "3.1.1.79",
"activity": "",
"evidence": [
{
"id": "Q05469",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q05469"
}
]
}
]
},
{
"uniprot_ac": "Q06520",
"gene_name": "SULT2A1",
"activity": [
{
"ec_number": "2.8.2.14",
"activity": "glycolithocholate + 3'-phosphoadenylyl sulfate = glycolithocholate 3-sulfate + adenosine 3',5'-bisphosphate + H(+).",
"evidence": [
{
"id": "Q06520",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q06520"
}
]
},
{
"ec_number": "2.8.2.2",
"activity": "an alcohol + 3'-phosphoadenylyl sulfate = an alkyl sulfate + adenosine 3',5'-bisphosphate + H(+).",
"evidence": [
{
"id": "Q06520",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q06520"
}
]
},
{
"ec_number": "2.8.2.2",
"activity": "",
"evidence": [
{
"id": "Q06520",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q06520"
}
]
}
]
},
{
"uniprot_ac": "Q06587",
"gene_name": "RING1",
"activity": [
{
"ec_number": "2.3.2.27",
"activity": "S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.",
"evidence": [
{
"id": "Q06587",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q06587"
}
]
},
{
"ec_number": "2.3.2.27",
"activity": "",
"evidence": [
{
"id": "Q06587",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q06587"
}
]
}
]
},
{
"uniprot_ac": "Q09472",
"gene_name": "EP300",
"activity": [
{
"ec_number": "2.3.1.48",
"activity": "L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+).",
"evidence": [
{
"id": "Q09472",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q09472"
}
]
},
{
"ec_number": "2.3.1.-",
"activity": "",
"evidence": [
{
"id": "Q09472",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q09472"
}
]
},
{
"ec_number": "2.3.1.48",
"activity": "",
"evidence": [
{
"id": "Q09472",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q09472"
}
]
}
]
},
{
"uniprot_ac": "Q13547",
"gene_name": "HDAC1",
"activity": [
{
"ec_number": "3.5.1.-",
"activity": "",
"evidence": [
{
"id": "Q13547",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13547"
}
]
},
{
"ec_number": "3.5.1.98",
"activity": "N(6)-acetyl-L-lysyl-[histone] + H2O = L-lysyl-[histone] + acetate.",
"evidence": [
{
"id": "Q13547",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13547"
}
]
},
{
"ec_number": "3.5.1.98",
"activity": "",
"evidence": [
{
"id": "Q13547",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13547"
}
]
}
]
},
{
"uniprot_ac": "Q14693",
"gene_name": "LPIN1",
"activity": [
{
"ec_number": "3.1.3.4",
"activity": "1-O-alkyl-2-acyl-sn-glycero-3-phosphate + H2O = 1-O-alkyl-2-acyl-sn-glycerol + phosphate.",
"evidence": [
{
"id": "Q14693",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q14693"
}
]
},
{
"ec_number": "3.1.3.4",
"activity": "",
"evidence": [
{
"id": "Q14693",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q14693"
}
]
}
]
},
{
"uniprot_ac": "Q15788",
"gene_name": "NCOA1",
"activity": [
{
"ec_number": "2.3.1.48",
"activity": "L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+).",
"evidence": [
{
"id": "Q15788",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q15788"
}
]
},
{
"ec_number": "2.3.1.48",
"activity": "",
"evidence": [
{
"id": "Q15788",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q15788"
}
]
}
]
},
{
"uniprot_ac": "Q15910",
"gene_name": "EZH2",
"activity": [
{
"ec_number": "2.1.1.356",
"activity": "L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-methionine = N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-homocysteine + 3 H(+).",
"evidence": [
{
"id": "Q15910",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q15910"
}
]
},
{
"ec_number": "2.1.1.356",
"activity": "",
"evidence": [
{
"id": "Q15910",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q15910"
}
]
}
]
},
{
"uniprot_ac": "Q16654",
"gene_name": "PDK4",
"activity": [
{
"ec_number": "2.7.11.2",
"activity": "L-seryl-[pyruvate dehydrogenase E1 alpha subunit] + ATP = O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit] + ADP + H(+).",
"evidence": [
{
"id": "Q16654",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q16654"
}
]
},
{
"ec_number": "2.7.11.2",
"activity": "",
"evidence": [
{
"id": "Q16654",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q16654"
}
]
}
]
},
{
"uniprot_ac": "Q16790",
"gene_name": "CA9",
"activity": [
{
"ec_number": "4.2.1.1",
"activity": "hydrogencarbonate + H(+) = CO2 + H2O.",
"evidence": [
{
"id": "Q16790",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q16790"
}
]
},
{
"ec_number": "4.2.1.1",
"activity": "",
"evidence": [
{
"id": "Q16790",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q16790"
}
]
}
]
},
{
"uniprot_ac": "Q16881",
"gene_name": "TXNRD1",
"activity": [
{
"ec_number": "1.8.1.9",
"activity": "[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + NADPH + H(+).",
"evidence": [
{
"id": "Q16881",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q16881"
}
]
},
{
"ec_number": "1.11.1.2",
"activity": "H2O2 + NADPH + H(+) = NADP(+) + 2 H2O.",
"evidence": [
{
"id": "Q16881",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q16881"
}
]
},
{
"ec_number": "1.8.1.9",
"activity": "",
"evidence": [
{
"id": "Q16881",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q16881"
}
]
},
{
"ec_number": "1.11.1.2",
"activity": "",
"evidence": [
{
"id": "Q16881",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q16881"
}
]
}
]
},
{
"uniprot_ac": "Q3L8U1",
"gene_name": "CHD9",
"activity": [
{
"ec_number": "3.6.4.-",
"activity": "",
"evidence": [
{
"id": "Q3L8U1",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q3L8U1"
}
]
}
]
},
{
"uniprot_ac": "Q56NI9",
"gene_name": "ESCO2",
"activity": [
{
"ec_number": "2.3.1.-",
"activity": "",
"evidence": [
{
"id": "Q56NI9",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q56NI9"
}
]
}
]
},
{
"uniprot_ac": "Q5FWF5",
"gene_name": "ESCO1",
"activity": [
{
"ec_number": "2.3.1.-",
"activity": "",
"evidence": [
{
"id": "Q5FWF5",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q5FWF5"
}
]
}
]
},
{
"uniprot_ac": "Q6PCB7",
"gene_name": "SLC27A1",
"activity": [
{
"ec_number": "6.2.1.3",
"activity": "a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate.",
"evidence": [
{
"id": "Q6PCB7",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q6PCB7"
}
]
},
{
"ec_number": "6.2.1.-",
"activity": "",
"evidence": [
{
"id": "Q6PCB7",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q6PCB7"
}
]
},
{
"ec_number": "6.2.1.15",
"activity": "(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate.",
"evidence": [
{
"id": "Q6PCB7",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q6PCB7"
}
]
}
]
},
{
"uniprot_ac": "Q86X55",
"gene_name": "CARM1",
"activity": [
{
"ec_number": "2.1.1.319",
"activity": "L-arginyl-[protein] + 2 S-adenosyl-L-methionine = N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine + 2 H(+).",
"evidence": [
{
"id": "Q86X55",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q86X55"
}
]
},
{
"ec_number": "2.1.1.319",
"activity": "",
"evidence": [
{
"id": "Q86X55",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q86X55"
}
]
}
]
},
{
"uniprot_ac": "Q8NEZ4",
"gene_name": "KMT2C",
"activity": [
{
"ec_number": "2.1.1.364",
"activity": "L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine + H(+).",
"evidence": [
{
"id": "Q8NEZ4",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q8NEZ4"
}
]
},
{
"ec_number": "2.1.1.364",
"activity": "",
"evidence": [
{
"id": "Q8NEZ4",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q8NEZ4"
}
]
}
]
},
{
"uniprot_ac": "Q8TD26",
"gene_name": "CHD6",
"activity": [
{
"ec_number": "3.6.4.-",
"activity": "",
"evidence": [
{
"id": "Q8TD26",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q8TD26"
}
]
}
]
},
{
"uniprot_ac": "Q8WUI4",
"gene_name": "HDAC7",
"activity": [
{
"ec_number": "3.5.1.-",
"activity": "",
"evidence": [
{
"id": "Q8WUI4",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q8WUI4"
}
]
},
{
"ec_number": "3.5.1.98",
"activity": "N(6)-acetyl-L-lysyl-[histone] + H2O = L-lysyl-[histone] + acetate.",
"evidence": [
{
"id": "Q8WUI4",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q8WUI4"
}
]
},
{
"ec_number": "3.5.1.98",
"activity": "",
"evidence": [
{
"id": "Q8WUI4",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q8WUI4"
}
]
}
]
},
{
"uniprot_ac": "Q8WYB5",
"gene_name": "KAT6B",
"activity": [
{
"ec_number": "2.3.1.48",
"activity": "L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+).",
"evidence": [
{
"id": "Q8WYB5",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q8WYB5"
}
]
},
{
"ec_number": "2.3.1.48",
"activity": "",
"evidence": [
{
"id": "Q8WYB5",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q8WYB5"
}
]
}
]
},
{
"uniprot_ac": "Q92769",
"gene_name": "HDAC2",
"activity": [
{
"ec_number": "3.5.1.-",
"activity": "",
"evidence": [
{
"id": "Q92769",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q92769"
}
]
},
{
"ec_number": "3.5.1.98",
"activity": "N(6)-acetyl-L-lysyl-[histone] + H2O = L-lysyl-[histone] + acetate.",
"evidence": [
{
"id": "Q92769",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q92769"
}
]
},
{
"ec_number": "3.5.1.98",
"activity": "",
"evidence": [
{
"id": "Q92769",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q92769"
}
]
}
]
},
{
"uniprot_ac": "Q92793",
"gene_name": "CREBBP",
"activity": [
{
"ec_number": "2.3.1.48",
"activity": "L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+).",
"evidence": [
{
"id": "Q92793",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q92793"
}
]
},
{
"ec_number": "2.3.1.-",
"activity": "",
"evidence": [
{
"id": "Q92793",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q92793"
}
]
},
{
"ec_number": "2.3.1.48",
"activity": "",
"evidence": [
{
"id": "Q92793",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q92793"
}
]
}
]
},
{
"uniprot_ac": "Q92794",
"gene_name": "KAT6A",
"activity": [
{
"ec_number": "2.3.1.48",
"activity": "L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+).",
"evidence": [
{
"id": "Q92794",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q92794"
}
]
},
{
"ec_number": "2.3.1.48",
"activity": "",
"evidence": [
{
"id": "Q92794",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q92794"
}
]
}
]
},
{
"uniprot_ac": "Q92830",
"gene_name": "KAT2A",
"activity": [
{
"ec_number": "2.3.1.48",
"activity": "L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+).",
"evidence": [
{
"id": "Q92830",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q92830"
}
]
},
{
"ec_number": "2.3.1.-",
"activity": "",
"evidence": [
{
"id": "Q92830",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q92830"
}
]
},
{
"ec_number": "2.3.1.48",
"activity": "",
"evidence": [
{
"id": "Q92830",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q92830"
}
]
}
]
},
{
"uniprot_ac": "Q92831",
"gene_name": "KAT2B",
"activity": [
{
"ec_number": "2.3.1.48",
"activity": "L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+).",
"evidence": [
{
"id": "Q92831",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q92831"
}
]
},
{
"ec_number": "2.3.1.57",
"activity": "an alkane-alpha,omega-diamine + acetyl-CoA = an N-acetylalkane-alpha,omega-diamine + CoA + H(+).",
"evidence": [
{
"id": "Q92831",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q92831"
}
]
},
{
"ec_number": "2.3.1.48",
"activity": "",
"evidence": [
{
"id": "Q92831",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q92831"
}
]
}
]
},
{
"uniprot_ac": "Q92993",
"gene_name": "KAT5",
"activity": [
{
"ec_number": "2.3.1.48",
"activity": "L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+).",
"evidence": [
{
"id": "Q92993",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q92993"
}
]
},
{
"ec_number": "2.3.1.-",
"activity": "",
"evidence": [
{
"id": "Q92993",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q92993"
}
]
},
{
"ec_number": "2.3.1.48",
"activity": "",
"evidence": [
{
"id": "Q92993",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q92993"
}
]
}
]
},
{
"uniprot_ac": "Q969S8",
"gene_name": "HDAC10",
"activity": [
{
"ec_number": "3.5.1.48",
"activity": "N(8)-acetylspermidine + H2O = spermidine + acetate.",
"evidence": [
{
"id": "Q969S8",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q969S8"
}
]
},
{
"ec_number": "3.5.1.62",
"activity": "N-acetylputrescine + H2O = putrescine + acetate.",
"evidence": [
{
"id": "Q969S8",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q969S8"
}
]
},
{
"ec_number": "3.5.1.62",
"activity": "",
"evidence": [
{
"id": "Q969S8",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q969S8"
}
]
},
{
"ec_number": "3.5.1.48",
"activity": "",
"evidence": [
{
"id": "Q969S8",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q969S8"
}
]
}
]
},
{
"uniprot_ac": "Q96AD5",
"gene_name": "PNPLA2",
"activity": [
{
"ec_number": "3.1.1.4",
"activity": "a 1-O-alkyl-2-acyl-sn-glycero-3-phosphocholine + H2O = a 1-O-alkyl-sn-glycero-3-phosphocholine + a fatty acid + H(+).",
"evidence": [
{
"id": "Q96AD5",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q96AD5"
}
]
},
{
"ec_number": "3.1.1.3",
"activity": "a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+).",
"evidence": [
{
"id": "Q96AD5",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q96AD5"
}
]
},
{
"ec_number": "3.1.1.3",
"activity": "",
"evidence": [
{
"id": "Q96AD5",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q96AD5"
}
]
}
]
},
{
"uniprot_ac": "Q96DB2",
"gene_name": "HDAC11",
"activity": [
{
"ec_number": "3.5.1.98",
"activity": "N(6)-acetyl-L-lysyl-[histone] + H2O = L-lysyl-[histone] + acetate.",
"evidence": [
{
"id": "Q96DB2",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q96DB2"
}
]
},
{
"ec_number": "3.5.1.98",
"activity": "",
"evidence": [
{
"id": "Q96DB2",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q96DB2"
}
]
}
]
},
{
"uniprot_ac": "Q96EB6",
"gene_name": "SIRT1",
"activity": [
{
"ec_number": "2.3.1.-",
"activity": "",
"evidence": [
{
"id": "Q96EB6",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q96EB6"
}
]
},
{
"ec_number": "2.3.1.286",
"activity": "N(6)-acetyl-L-lysyl-[protein] + NAD(+) + H2O = 2''-O-acetyl-ADP-D-ribose + nicotinamide + L-lysyl-[protein].",
"evidence": [
{
"id": "Q96EB6",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q96EB6"
}
]
},
{
"ec_number": "2.3.1.286",
"activity": "",
"evidence": [
{
"id": "Q96EB6",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q96EB6"
}
]
}
]
},
{
"uniprot_ac": "Q96IU4",
"gene_name": "ABHD14B",
"activity": [
{
"ec_number": "2.3.1.-",
"activity": "",
"evidence": [
{
"id": "Q96IU4",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q96IU4"
}
]
}
]
},
{
"uniprot_ac": "Q96PD7",
"gene_name": "DGAT2",
"activity": [
{
"ec_number": "2.3.1.20",
"activity": "an acyl-CoA + a 1,2-diacyl-sn-glycerol = a triacyl-sn-glycerol + CoA.",
"evidence": [
{
"id": "Q96PD7",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q96PD7"
}
]
},
{
"ec_number": "2.3.1.76",
"activity": "all-trans-retinol + an acyl-CoA = an all-trans-retinyl ester + CoA.",
"evidence": [
{
"id": "Q96PD7",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q96PD7"
}
]
},
{
"ec_number": "2.3.1.76",
"activity": "",
"evidence": [
{
"id": "Q96PD7",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q96PD7"
}
]
},
{
"ec_number": "2.3.1.20",
"activity": "",
"evidence": [
{
"id": "Q96PD7",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q96PD7"
}
]
}
]
},
{
"uniprot_ac": "Q96RS0",
"gene_name": "TGS1",
"activity": [
{
"ec_number": "2.1.1.-",
"activity": "",
"evidence": [
{
"id": "Q96RS0",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q96RS0"
}
]
}
]
},
{
"uniprot_ac": "Q99496",
"gene_name": "RNF2",
"activity": [
{
"ec_number": "2.3.2.27",
"activity": "S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.",
"evidence": [
{
"id": "Q99496",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q99496"
}
]
},
{
"ec_number": "2.3.2.27",
"activity": "",
"evidence": [
{
"id": "Q99496",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q99496"
}
]
}
]
},
{
"uniprot_ac": "Q99685",
"gene_name": "MGLL",
"activity": [
{
"ec_number": "3.1.1.23",
"activity": "Hydrolyzes glycerol monoesters of long-chain fatty acids.",
"evidence": [
{
"id": "Q99685",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q99685"
}
]
},
{
"ec_number": "3.1.1.23",
"activity": "",
"evidence": [
{
"id": "Q99685",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q99685"
}
]
}
]
},
{
"uniprot_ac": "Q9BWU1",
"gene_name": "CDK19",
"activity": [
{
"ec_number": "2.7.11.22",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q9BWU1",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9BWU1"
}
]
},
{
"ec_number": "2.7.11.22",
"activity": "",
"evidence": [
{
"id": "Q9BWU1",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9BWU1"
}
]
}
]
},
{
"uniprot_ac": "Q9BY41",
"gene_name": "HDAC8",
"activity": [
{
"ec_number": "3.5.1.-",
"activity": "",
"evidence": [
{
"id": "Q9BY41",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9BY41"
}
]
},
{
"ec_number": "3.5.1.98",
"activity": "N(6)-acetyl-L-lysyl-[histone] + H2O = L-lysyl-[histone] + acetate.",
"evidence": [
{
"id": "Q9BY41",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9BY41"
}
]
},
{
"ec_number": "3.5.1.98",
"activity": "",
"evidence": [
{
"id": "Q9BY41",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9BY41"
}
]
}
]
},
{
"uniprot_ac": "Q9BYK8",
"gene_name": "HELZ2",
"activity": [
{
"ec_number": "3.1.13.1",
"activity": "Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.",
"evidence": [
{
"id": "Q9BYK8",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9BYK8"
}
]
},
{
"ec_number": "5.6.2.6",
"activity": "n ATP + n H2O + wound RNA = n ADP + n phosphate + unwound RNA.",
"evidence": [
{
"id": "Q9BYK8",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9BYK8"
}
]
},
{
"ec_number": "3.1.13.1",
"activity": "",
"evidence": [
{
"id": "Q9BYK8",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9BYK8"
}
]
},
{
"ec_number": "3.6.4.13",
"activity": "ATP + H2O = ADP + phosphate + H(+).",
"evidence": [
{
"id": "Q9BYK8",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9BYK8"
}
]
},
{
"ec_number": "3.6.4.13",
"activity": "",
"evidence": [
{
"id": "Q9BYK8",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9BYK8"
}
]
}
]
},
{
"uniprot_ac": "Q9H6R3",
"gene_name": "ACSS3",
"activity": [
{
"ec_number": "6.2.1.1",
"activity": "acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate.",
"evidence": [
{
"id": "Q9H6R3",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9H6R3"
}
]
},
{
"ec_number": "6.2.1.17",
"activity": "propanoate + ATP + CoA = propanoyl-CoA + AMP + diphosphate.",
"evidence": [
{
"id": "Q9H6R3",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9H6R3"
}
]
},
{
"ec_number": "6.2.1.1",
"activity": "",
"evidence": [
{
"id": "Q9H6R3",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9H6R3"
}
]
},
{
"ec_number": "6.2.1.17",
"activity": "",
"evidence": [
{
"id": "Q9H6R3",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9H6R3"
}
]
}
]
},
{
"uniprot_ac": "Q9H7X0",
"gene_name": "NAA60",
"activity": [
{
"ec_number": "2.3.1.48",
"activity": "L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+).",
"evidence": [
{
"id": "Q9H7X0",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9H7X0"
}
]
},
{
"ec_number": "2.3.1.48",
"activity": "",
"evidence": [
{
"id": "Q9H7X0",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9H7X0"
}
]
},
{
"ec_number": "2.3.1.259",
"activity": "N-terminal L-methionyl-[transmembrane protein] + acetyl-CoA = N-terminal N(alpha)-acetyl-L-methionyl-[transmembrane protein] + CoA + H(+).",
"evidence": [
{
"id": "Q9H7X0",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9H7X0"
}
]
},
{
"ec_number": "2.3.1.259",
"activity": "",
"evidence": [
{
"id": "Q9H7X0",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9H7X0"
}
]
}
]
},
{
"uniprot_ac": "Q9H7Z6",
"gene_name": "KAT8",
"activity": [
{
"ec_number": "2.3.1.48",
"activity": "L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+).",
"evidence": [
{
"id": "Q9H7Z6",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9H7Z6"
}
]
},
{
"ec_number": "2.3.1.48",
"activity": "",
"evidence": [
{
"id": "Q9H7Z6",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9H7Z6"
}
]
},
{
"ec_number": "2.3.1.-",
"activity": "",
"evidence": [
{
"id": "Q9H7Z6",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9H7Z6"
}
]
}
]
},
{
"uniprot_ac": "Q9HCL2",
"gene_name": "GPAM",
"activity": [
{
"ec_number": "2.3.1.15",
"activity": "sn-glycerol 3-phosphate + an acyl-CoA = a 1-acyl-sn-glycero-3-phosphate + CoA.",
"evidence": [
{
"id": "Q9HCL2",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9HCL2"
}
]
},
{
"ec_number": "2.3.1.15",
"activity": "",
"evidence": [
{
"id": "Q9HCL2",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9HCL2"
}
]
}
]
},
{
"uniprot_ac": "Q9NYP7",
"gene_name": "ELOVL5",
"activity": [
{
"ec_number": "2.3.1.199",
"activity": "a very-long-chain acyl-CoA + malonyl-CoA + H(+) = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA.",
"evidence": [
{
"id": "Q9NYP7",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9NYP7"
}
]
},
{
"ec_number": "2.3.1.199",
"activity": "",
"evidence": [
{
"id": "Q9NYP7",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9NYP7"
}
]
}
]
},
{
"uniprot_ac": "Q9UBN7",
"gene_name": "HDAC6",
"activity": [
{
"ec_number": "3.5.1.-",
"activity": "",
"evidence": [
{
"id": "Q9UBN7",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9UBN7"
}
]
},
{
"ec_number": "2.3.2.-",
"activity": "",
"evidence": [
{
"id": "Q9UBN7",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9UBN7"
}
]
}
]
},
{
"uniprot_ac": "Q9UHE5",
"gene_name": "NAT8",
"activity": [
{
"ec_number": "2.3.1.-",
"activity": "",
"evidence": [
{
"id": "Q9UHE5",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9UHE5"
}
]
},
{
"ec_number": "2.3.1.80",
"activity": "an S-substituted L-cysteine + acetyl-CoA = an N-acetyl-L-cysteine-S-conjugate + CoA + H(+).",
"evidence": [
{
"id": "Q9UHE5",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9UHE5"
}
]
}
]
},
{
"uniprot_ac": "Q9UHF3",
"gene_name": "NAT8B",
"activity": [
{
"ec_number": "2.3.1.-",
"activity": "",
"evidence": [
{
"id": "Q9UHF3",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9UHF3"
}
]
}
]
},
{
"uniprot_ac": "Q9UKN8",
"gene_name": "GTF3C4",
"activity": [
{
"ec_number": "2.3.1.48",
"activity": "L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+).",
"evidence": [
{
"id": "Q9UKN8",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9UKN8"
}
]
},
{
"ec_number": "2.3.1.48",
"activity": "",
"evidence": [
{
"id": "Q9UKN8",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9UKN8"
}
]
}
]
},
{
"uniprot_ac": "Q9UKV0",
"gene_name": "HDAC9",
"activity": [
{
"ec_number": "3.5.1.98",
"activity": "N(6)-acetyl-L-lysyl-[histone] + H2O = L-lysyl-[histone] + acetate.",
"evidence": [
{
"id": "Q9UKV0",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9UKV0"
}
]
},
{
"ec_number": "3.5.1.98",
"activity": "",
"evidence": [
{
"id": "Q9UKV0",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9UKV0"
}
]
}
]
},
{
"uniprot_ac": "Q9UNQ0",
"gene_name": "ABCG2",
"activity": [
{
"ec_number": "7.6.2.2",
"activity": "daunorubicin(in) + ATP + H2O = daunorubicin(out) + ADP + phosphate + H(+).",
"evidence": [
{
"id": "Q9UNQ0",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9UNQ0"
}
]
},
{
"ec_number": "7.6.2.2",
"activity": "",
"evidence": [
{
"id": "Q9UNQ0",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9UNQ0"
}
]
}
]
},
{
"uniprot_ac": "Q9UQL6",
"gene_name": "HDAC5",
"activity": [
{
"ec_number": "3.5.1.98",
"activity": "N(6)-acetyl-L-lysyl-[histone] + H2O = L-lysyl-[histone] + acetate.",
"evidence": [
{
"id": "Q9UQL6",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9UQL6"
}
]
},
{
"ec_number": "3.5.1.98",
"activity": "",
"evidence": [
{
"id": "Q9UQL6",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9UQL6"
}
]
}
]
},
{
"uniprot_ac": "Q9Y6F7",
"gene_name": "CDY2A",
"activity": [
{
"ec_number": "2.3.1.48",
"activity": "L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+).",
"evidence": [
{
"id": "Q9Y6F7",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9Y6F7"
}
]
},
{
"ec_number": "2.3.1.48",
"activity": "",
"evidence": [
{
"id": "Q9Y6F7",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9Y6F7"
}
]
}
]
},
{
"uniprot_ac": "Q9Y6F8",
"gene_name": "CDY1B",
"activity": [
{
"ec_number": "2.3.1.48",
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