The severe acute respiratory syndrome coronavirus type 1 (SARS-CoV-1) nucleocapsid (N) protein was found to inhibit TRIM25-mediated DDX58 ubiquitination upon coexpression in HEK293T cells in a dose-dependent manner (Hu Y et al. 2017). Similar results were reported for the SARS-CoV-2 N protein (Gori Savellini G et al. 2021).", "cellular_location": "cytosol", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q8IUD6-1", "Q14258-1", "O95786-1", "Q9C037-1" ], "evidence": [ { "id": "R-HSA-918224", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-918224" } ] }, { "id": "R-HSA-918225", "name": "TBK1/IKK epsilon complex interacts with MAVS bound TRAF3", "equation": "", "summary": "TRAF3 binds both IPS\u20111 and downstream interferon regulatory factor 3/7 (IRF3/7) kinases TBK1 and IKK\u2011epsilon (IKKi, IKBKE) and thus serves as a critical link between RIG\u2011I/MDA5 adaptors and downstream regulatory kinases important for interferon regulatory factor (IRF) activation (Oganesyan et al. 2006).
SIKE (Suppressor of IKK-epsilon) interacts with IKBKE and TBK1. SIKE is associated with TBK1 under physiological conditions and dissociated from TBK1 upon viral infection. Overexpression of SIKE disrupted the interactions of IKBKE or TBK1 with RIG\u2011I (DDX58).
SARS-CoV-1 M protein prevents the formation of the TRAF3:TANK:TBK1/IKBKE complex and thereby inhibits TBK1/IKBKE-dependent activation of IRF3/IRF7 transcription factors (Siu KL et al. 2009).",
"cellular_location": "cytosol, mitochondrial outer membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q14164-1",
"Q9UHD2-1",
"Q8IUD6-1",
"Q9BYX4-1",
"Q14258-1",
"Q13114-1",
"O95786-1",
"Q9C037-1"
],
"evidence": [
{
"id": "R-HSA-918225",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-918225"
}
]
},
{
"id": "R-HSA-918227",
"name": "Recruitment of TRAF3 to MAVS",
"equation": "",
"summary": "TRAF3 a E3 ligase for K63-linked polyubiquitination, is one of the critical molecules required for mediating IPS-1 dependent type I IFN production. TRAF3 interacts directly with IPS-1 through the TRAF domain of TRAF3 and a TRAF-interaction motif (TIM) with in IPS-1.",
"cellular_location": "cytosol, mitochondrial outer membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q8IUD6-1",
"Q9BYX4-1",
"Q14258-1",
"Q13114-1",
"O95786-1",
"Q9C037-1"
],
"evidence": [
{
"id": "R-HSA-918227",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-918227"
}
]
},
{
"id": "R-HSA-918229",
"name": "Phosphorylation and release of IRF3/IRF7",
"equation": "",
"summary": "Human IRF3 is activated through a two-step phosphorylation in the C-terminal domain mediated by TBK1 and/or IKKi, requiring Ser386 and/or Ser385- site 1; and a cluster of serine/threonine residues between Ser396 and Ser405- site 2 [Panne et al 2007]. Phosphorylated residues at site 2 (Ser396\u2014Ser405) alleviate autoinhibition to allow interaction with CBP (CREB-binding protein) and facilitate phosphorylation at site 1 (Ser385 or Ser386). Phosphorylation at site 1 is required for IRF3 dimerization.
IRF3 and IRF7 transcription factors possess distinct structural characteristics; IRF7 is phosphorylated on Ser477 and Ser479 residues [Lin R et al 2000].
Since the number of serine residues involved into IRF activation remains unclear this reaction represents a minimum stoichiometry to achieve the phosphorylation of at least 3 Ser residues per each IRF transcription factor. [Lin et al 2000, Ning et al 2008]",
"cellular_location": "cytosol, mitochondrial outer membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q14164-1",
"Q9UHD2-1",
"Q8IUD6-1",
"Q9BYX4-1",
"Q14258-1",
"Q13114-1",
"O95786-1",
"Q9C037-1"
],
"evidence": [
{
"id": "R-HSA-918229",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-918229"
}
]
},
{
"id": "R-HSA-918230",
"name": "Recruitment of TRAF6/TRAF2 to IPS-1",
"equation": "",
"summary": "IPS-1 interacts with TRAF2 and TRAF6 through its consensus TRAF-interaction motif (TIM) (TRAF2 143-PVGET-147 and TRAF6 153-PGENSE-158 & 455-PEENEY-460). Although IPS-1 can bind to both TRAF6 and TRAF2, TRAF2 binding is not required for IPS-1 activation of NF-kB.",
"cellular_location": "cytosol, mitochondrial outer membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q12933-1",
"Q9Y4K3-1",
"Q8IUD6-1",
"Q9BYX4-1",
"Q14258-1",
"O95786-1",
"Q9C037-1"
],
"evidence": [
{
"id": "R-HSA-918230",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-918230"
}
]
},
{
"id": "R-HSA-918232",
"name": "Recruitment of IRF3,IRF7",
"equation": "",
"summary": "IRF3 and IRF7 (IRF3/IRF7) are the two major members of the interferon regulatory factor (IRF) family, involved in modulating the IFN gene expression. However, their roles are different in these processes. In the early phase of viral infection, preexisting IRF-3 is activated and induces expression of IFN beta and IFN alpha4. These early produced IFNs transcriptionally induce IRF-7, and upon viral infection, the induced high-level IRF-7 is activated and transactivates multiple IFN genes, leading to robust production of IFNs in response to viral infection. IPS-1 interacts with both IRF3 and IRF7 and recruits them to RIG-1. TBK1/IKKi kinases phosphorylate and activate IRF3/IRF7.",
"cellular_location": "cytosol, mitochondrial outer membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q14164-1",
"Q9UHD2-1",
"Q8IUD6-1",
"Q9BYX4-1",
"Q14258-1",
"Q13114-1",
"O95786-1",
"Q9C037-1"
],
"evidence": [
{
"id": "R-HSA-918232",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-918232"
}
]
},
{
"id": "R-HSA-933523",
"name": "Dimerzation of procaspase-8, procaspase-10",
"equation": "",
"summary": "Procaspase-8/10 undergo dimerization and the subsequent conformational changes at the receptor complex results in the formation of catalytic active caspase dimers.",
"cellular_location": "cytosol, mitochondrial outer membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q14790-1",
"Q13546-1",
"Q92851-1",
"Q8IUD6-1",
"Q9BYX4-1",
"Q14258-1",
"O95786-1",
"Q9C037-1"
],
"evidence": [
{
"id": "R-HSA-933523",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-933523"
}
]
},
{
"id": "R-HSA-933525",
"name": "Phosphorylation and release of IRF7",
"equation": "",
"summary": "IRF7 is activated through phosphorylation of residues Ser477 and Ser479 by TBK1/IKKi kinase complex.",
"cellular_location": "cytosol, mitochondrial outer membrane",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-450318"
],
"enzyme_list": [
"Q12933-1",
"Q14164-1",
"Q9UHD2-1",
"Q9Y4K3-1",
"Q8IUD6-1",
"Q9BYX4-1",
"Q14258-1",
"O95786-1",
"Q9C037-1"
],
"evidence": [
{
"id": "R-HSA-933525",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-933525"
}
]
},
{
"id": "R-HSA-933526",
"name": "Recruitment of caspase-8 and -10 to FADD complex",
"equation": "",
"summary": "Caspase-8 (CASP8) and caspase-10 (CASP10) are involved in RIG-I/MDA5-dependent antiviral immune responses. Caspase-8/10 activation contributes to NF-kB activation in response to viral dsRNA.
Caspase-8/10 are synthesized as zymogens (procaspases), containing a large N-terminal prodomain with two death effector domains (DED), and a C-terminal catalytic subunit composed of small and a large domain separated by a smaller linker region. FADD plays a crucial role in the recruitment and activation of procaspase-8/10. The two DED domains of procaspase-8/10 interacts with DED domain of FADD.",
"cellular_location": "cytosol, mitochondrial outer membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q14790-1",
"Q13546-1",
"Q92851-1",
"Q8IUD6-1",
"Q9BYX4-1",
"Q14258-1",
"O95786-1",
"Q9C037-1"
],
"evidence": [
{
"id": "R-HSA-933526",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-933526"
}
]
},
{
"id": "R-HSA-933527",
"name": "Recruitment of TBK1/IKK epsilon complex to TANK:TRAF6",
"equation": "",
"summary": "TANK acts as an adapter protein and regulates the assembly of TBK1/IKK epsilon complex with upstream signaling molecules. SIKE (for Suppressor of IKKepsilon) interacts with IKKepsilon and TBK1. SIKE is associated with TBK1 under physiological condition and dissociated from TBK1 upon viral infection. Overexpression of SIKE disrupted the interactions of IKKepsilon or TBK1 with RIG-1.",
"cellular_location": "cytosol, mitochondrial outer membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q12933-1",
"Q14164-1",
"Q9UHD2-1",
"Q9Y4K3-1",
"Q8IUD6-1",
"Q9BYX4-1",
"Q14258-1",
"O95786-1",
"Q9C037-1"
],
"evidence": [
{
"id": "R-HSA-933527",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-933527"
}
]
},
{
"id": "R-HSA-933528",
"name": "Interaction of MEKK1 with TRAF6",
"equation": "",
"summary": "TRAF6 requires MEKK1 (MAP3K1) to activate NF-kB and MEKK1 may interact with TRAF6, which in turn contributes to the activation of IKK and MAPKK, leading to the activation of NF-kB and AP-1. (Yoshida et al)",
"cellular_location": "cytosol, mitochondrial outer membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q12933-1",
"Q13233-1",
"Q9Y4K3-1",
"Q8IUD6-1",
"Q9BYX4-1",
"Q14258-1",
"O95786-1",
"Q9C037-1"
],
"evidence": [
{
"id": "R-HSA-933528",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-933528"
}
]
},
{
"id": "R-HSA-933530",
"name": "Activation of IKK by MEKK1",
"equation": "",
"summary": "In Human, IKKs - IkB kinase (IKK) complex serves as the master regulator for the activation of NF-kB by various stimuli. It contains two catalytic subunits, IKK alpha and IKK beta, and a regulatory subunit, IKKgamma/NEMO. The activation of IKK complex and NFkB mediated antiviral responce are dependent on the phosphorylation of IKK alpha/beta at its activation loop and the ubiquitination of NEMO.[Solt et al 2009]; [Li et al 2002]. NEMO ubiquitination by TRAF6 is required for optimal activation of IKKalpha/beta; it's remained unclear if NEMO subunit undergoes K63-linked or linear ubiquitination.
This basic trimolecular complex is referred to as the IKK complex. Each catalytic IKK subunit has a N-term kinase domain a leucine zipper (LZ) motifs, a helix-loop-helix (HLH) and a C-ter NEMO binding domain (NBD). IKK catalytic subunits are dimerized through their LZ motifs.
IKK beta is the major IKK catalytic subunit for NF-kB activation. MEKK1 can activate both IKK-alpha (IKKA) and IKK-beta (IKKB) in vivo. MEKK1 phosphorylates Ser-176 and Ser-180 in IKKA and Ser-177 and Ser-181 in IKKB activation loop and thus activate the IKK kinase activity, leading to the IkB alpha phosphorylation and NF-kB activation.",
"cellular_location": "cytosol, mitochondrial outer membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q12933-1",
"O15111-1",
"Q13233-1",
"Q9Y4K3-1",
"Q8IUD6-1",
"Q9BYX4-1",
"O14920-1",
"Q14258-1",
"O95786-1",
"Q9C037-1"
],
"evidence": [
{
"id": "R-HSA-933530",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-933530"
}
]
},
{
"id": "R-HSA-933532",
"name": "Processing of caspases",
"equation": "",
"summary": "Processing of caspases is required for activation of downstream signaling and dsRNA stimulation inducese the processing of these caspases. The nonapoptotic caspase function of both caspase-8 and -10 does not require the protease activity and the DED-containing prodomains are sufficient for NF-kB activation.",
"cellular_location": "cytosol, mitochondrial outer membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q14790-1",
"Q13546-1",
"Q92851-1",
"Q8IUD6-1",
"Q9BYX4-1",
"Q14258-1",
"O95786-1",
"Q9C037-1"
],
"evidence": [
{
"id": "R-HSA-933532",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-933532"
}
]
},
{
"id": "R-HSA-933537",
"name": "Recruitment of TANK to TRAF6",
"equation": "",
"summary": "TRAF family member-associated NF-kB activator (TANK, also known as I-TRAF) plays an important role in IFN induction through both RIG-I and Toll-like receptor-dependent pathways. TANK has been identified as a TRAF6 binding protein. Transient transfection experiments in 293T cells revealed that TRAF6 associates with IPS-1, TBK1, IKKi, and TANK (Konno et al. 2009).",
"cellular_location": "cytosol, mitochondrial outer membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q12933-1",
"Q9Y4K3-1",
"Q8IUD6-1",
"Q9BYX4-1",
"Q14258-1",
"O95786-1",
"Q9C037-1"
],
"evidence": [
{
"id": "R-HSA-933537",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-933537"
}
]
},
{
"id": "R-HSA-933538",
"name": "Recruitment of IRF7 to TRAF6",
"equation": "",
"summary": "TRAF6 associates with and activates IRF7 but not IRF3.",
"cellular_location": "cytosol, mitochondrial outer membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q12933-1",
"Q14164-1",
"Q9UHD2-1",
"Q9Y4K3-1",
"Q8IUD6-1",
"Q9BYX4-1",
"Q14258-1",
"O95786-1",
"Q9C037-1"
],
"evidence": [
{
"id": "R-HSA-933538",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-933538"
}
]
},
{
"id": "R-HSA-933539",
"name": "Recruitment of IKK complex",
"equation": "",
"summary": "The molecular mechanisms by which caspase-8/10 attribute to NF-kB signaling is unclear. Caspase-8 might act as a scaffolding protein by bringing the IKK-complex in close proximity to its activator TAK1. The prodomain of Caspase-8 could interact with IKK2 in the IKK complex whereas the protease homology domain failed to do so. These results indicate that the interaction of the DEDs-containing prodomain of caspase-8 with the IKKs may be crucial for the NF-kB induction by caspase-8.",
"cellular_location": "cytosol, mitochondrial outer membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q14790-1",
"O15111-1",
"Q13546-1",
"Q92851-1",
"Q8IUD6-1",
"Q9BYX4-1",
"O14920-1",
"Q14258-1",
"O95786-1",
"Q9C037-1"
],
"evidence": [
{
"id": "R-HSA-933539",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-933539"
}
]
},
{
"id": "R-HSA-936378",
"name": "Inhibition of DDX58/IFIH1 signaling by ATG5:ATG12:MAVS",
"equation": "",
"summary": "Autophagy protein 5 (ATG5) and autophagy-related protein 12 (ATG12) conjugate negatively regulates the type I IFN production pathway by directly associating with DDX58/IFIH1 and MAVS through the caspase recruitment domains (CARDs). The ATG5-ATG12 conjugate intercalates between the CARDs of DDX58/IFIH1 and MAVS and inhibits signal transmission, resulting in suppression of type I IFN production and innate antiviral immune responses.",
"cellular_location": "cytosol, mitochondrial outer membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q8IUD6-1",
"Q9BYX4-1",
"Q14258-1",
"O95786-1",
"Q9C037-1"
],
"evidence": [
{
"id": "R-HSA-936378",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-936378"
}
]
},
{
"id": "R-HSA-936381",
"name": "OTUD5 deubiquitinates TRAF3",
"equation": "",
"summary": "OTUD5 (Deubiquitinating enzyme A (DUBA)) is a negative regulator of type I interferon (IFN-) production. TRAF3, an E3 ubiquitin ligase that preferentially assembles lysine-63-linked polyubiquitin chains, is one of the targets of OTUD5. Expression of DUBA increases the cleavage of K63-linked ubiquitin chains from TRAF3, resulting in its dissociation from the downstream signaling complex that contains TANK-binding kinase 1 (TBK1) (Kayagaki et al. 2007), which leads to blockade of IRF3 and IRF7 phosphorylation.",
"cellular_location": "cytosol, mitochondrial outer membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q8IUD6-1",
"Q9BYX4-1",
"Q14258-1",
"Q13114-1",
"O95786-1",
"Q96G74-1",
"Q9C037-1"
],
"evidence": [
{
"id": "R-HSA-936381",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-936381"
}
]
},
{
"id": "R-HSA-936390",
"name": "CYLD mediated deubiquitination of DDX58 (RIG-I)",
"equation": "",
"summary": "CYLD is an ovarian tumor (OTU) domain-containing deubiquitinating enzyme (DUB) and has been identified as a negative regulator of DDX58 (RIG-I) mediated antiviral signaling. CYLD associates with the CARD domain of DDX58 and removes K63-linked ubiquitin from the DDX58 CARDs that are conjugated by the E3 ubiquitin ligase, TRIM25 and RNF135.",
"cellular_location": "cytosol",
"input_participant_list": [
"R-HSA-918191"
],
"output_participant_list": [
"R-HSA-168917"
],
"enzyme_list": [
"O95786-1",
"Q9NQC7-1"
],
"evidence": [
{
"id": "R-HSA-936390",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-936390"
}
]
},
{
"id": "R-HSA-936412",
"name": "RNF125 mediated ubiquitination of DDX58, IFIH1 and MAVS",
"equation": "",
"summary": "RNF125 acts as an E3-ubiquitin ligase that conjugates with RIG-I (DDX58), MDA5 (IFIH1) and IPS-1 (MAVS) and mediate their proteosomal degradation. UbcH1, UbcH5a, UbcH5b, and UbcH5c function as an E2 enzyme and conjugate ubiquitin to RNF125 and DDX58 via K48. Among these enzymes UbcH5c is the major E2 enzyme showing enhanced ubiquitin conjugation to DDX58. RNF125 mediated ubiquitination of RIG-I, MDA5 and MAVS (IPS-1) inhibits DDX58/IFIH1 signaling by shunting these proteins toward proteasomal degradation.",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O14933-1",
"Q9BYX4-1",
"P51668-1",
"P61077-1",
"Q96EQ8-1",
"P62837-1",
"O95786-1",
"P61086-1"
],
"evidence": [
{
"id": "R-HSA-936412",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-936412"
}
]
},
{
"id": "R-HSA-936475",
"name": "Negative regulation of DDX58/IFIH1 signaling by RNF216",
"equation": "",
"summary": "TRAF3 is dual regulated by DUBA (OTUD5) and TRIAD3A (RNF216). TRAF3 K63-polyubiquitin is removed by DUBA to disrupt TRAF3-TBK1/IKKi interactions. TRAF3 then undergoes a late phase K48-linked polyubiquitination by TRIAD3A, leading to TRAF3 proteasomal degradation. Thus TRIAD3A acts as a E3- ubiquitin ligase that negatively regulates RLR pathway.",
"cellular_location": "mitochondrial outer membrane",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-936556"
],
"enzyme_list": [
"Q8IUD6-1",
"Q9BYX4-1",
"Q14258-1",
"Q13114-1",
"O95786-1",
"Q9C037-1",
"Q9NWF9-2"
],
"evidence": [
{
"id": "R-HSA-936475",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-936475"
}
]
},
{
"id": "R-HSA-936563",
"name": "ISGylation of DDX58",
"equation": "",
"summary": "ISG15 is an ubiquitin (Ub)-like protein which is conjugated to intracellular proteins via an isopeptide bond. Similar to ubiquitination, the conjugation of ISG15 (ISGylation) requires a three-step process, involving an E1 activating enzyme (UBE1L), an E2 conjugating enzyme (UbcM8/H8), and HERC5/Ceb1 an IFN-inducible ISG15-specific E3 ligase. ISG15 conjugation may play an important regulatory role in IFN-mediated antiviral responses. IFN induces ISG15 conjugation to DDX58 negatively regulating DDX58-mediated antiviral signaling. ISGylated DDX58 becomes subject to an irreversible biochemical process, such as proteolysis or proteasomeal degradation.",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O14933-1",
"Q9UII4-1",
"O95786-1",
"P41226-1"
],
"evidence": [
{
"id": "R-HSA-936563",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-936563"
}
]
},
{
"id": "R-HSA-937343",
"name": "NLRC5 interacts with DDX58/IFIH1",
"equation": "",
"summary": "NLRC5 competes with IPS-1 for binding to the CARD domain of RIG-I/MDA5. NLRC5 specifically recognize the CARD domains of RIG-I/MDA5 when the CARD domains become accessible after viral infection, leading to dampened activation of IRF3.",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q8IUD6-1",
"Q9BYX4-1",
"Q14258-1",
"O95786-1",
"Q9C037-1"
],
"evidence": [
{
"id": "R-HSA-937343",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-937343"
}
]
},
{
"id": "R-HSA-9693589",
"name": "SARS-CoV-1 dsRNA intermediates bind DDX58",
"equation": "",
"summary": "Double\u2011stranded RNA (dsRNA), synthesized during the course of infection by RNA viruses as a byproduct of replication and transcription, acts as a potent trigger of the host innate antiviral response. In the cytoplasm of the infected cell, the presence of viral dsRNA is recognized by retinoic\u2011acid inducible gene I (RIG\u2011I)\u2011like receptors (RLR), such as antiviral innate immune response receptor RIG-I (RIG\u2011I, also known as DEAD box protein 58, DDX58). DDX58 recognizes short dsRNAs. The dsRNA length must be 19 bp or longer to induce DDX58\u2011mediated type I interferon (IFN)\u2011mediated response (Schlee M et al. 2009; Marq JB et al. 2010). Viral RNAs activates DDX58 by binding to its RNA helicase domain. This provokes a change in DDX58 conformation exposing the caspase activation and recruitment domain (CARD) leading to DDX58 oligomerization, allowing it to interact with mitochondrial antiviral\u2011signaling protein (MAVS, IPS\u20111). Host mRNAs are 5'\u2011capped and 2'\u2011O\u2011methylated. These mRNA characteristics enable host mRNAs to escape from self\u2011recognition by DDX58 (Schlee M et al. 2009; Schmidt A et al. 2009; Schuberth\u2011Wagner C et al. 2015). Severe acute respiratory syndrome coronavirus type 1 (SARS\u2011CoV\u20111) has developed a strategy to avoid recognition by DDX58. Viral dsRNA replication intermediates derived from SARS\u2011CoV\u20111 were shown to associate with the replicase\u2011transcriptase complex (RTC) bound to double membrane vesicles, which protected viral RNA from host sensors (Stertz S et al. 2007; Knoops K et al. 2008). In addition, nonstructural protein 14 (nsp14) of SARS\u2011CoV\u20111 possesses guanine\u2011N7\u2011methyltransferase activity that can mimic host 5'\u2011cap structure on the viral RNA (Chen Y et al. 2009). Nsp16 of SARS\u2011CoV-1 further modifies this cap with its 2\u2019\u2011O\u2011methyl\u2011transferase activity, allowing the virus to efficiently evade recognition by DDX58 (RIG\u2011I) and MDA5 (Chen Y et al. 2011; Menachery VD et al. 2014; Daffis S et al. 2010). SARS\u2011CoV\u20111 with a mutated nsp16 displays reduced virulence that is dependent on MDA5 sensing (Menachery VD et al. 2014). Mutating nsp16 also attenuates virulence in Middle East respiratory syndrome (MERS)\u2011CoV and reduces disease severity in infected mice (Menachery VD et al. 2017). Thus, nsp16 is critical to alter the type I IFN\u2011mediated innate antiviral response in SARS and MERS infections.
The amino acid sequence alignment of nsp14 and nsp16 from SARS-CoV-2 and of SARS-CoV-1 showed 95 and 93% of sequence identity respectively (Yoshimoto FK 2020). Structural studies suggest that properties and biological functions of SARS-CoV-2 nsp14 and nsp16 could be very similar to these of SARS-CoV-1 (Decroly E et al. 2011; Chen Y et al. 2011; Rosas-Lemus M et al. 2020; Lin S et al. 2020; Viswanathan T et al. 2020).; ;",
"cellular_location": "cytosol, double membrane vesicle viral factory outer membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O95786-1"
],
"evidence": [
{
"id": "R-HSA-9693589",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9693589"
}
]
},
{
"id": "R-HSA-9705137",
"name": "TBK1 or IKBKE forms homodimers",
"equation": "",
"summary": "RIG\u2011I\u2011like receptors (RLRs) recognize RNAs from various RNA viruses and activate the mitochondrial antiviral\u2011signaling protein (MAVS) adaptor protein. MAVS recruits the serine/threonine protein kinase TBK1 (tumor necrosis factor (TNF) receptor\u2011associated factor (TRAF) family member\u2011associated NF\u2011\u03baB activator (TANK)\u2011binding kinase 1) and/or its close homolog inhibitor\u2011kappa\u2011B kinase (IKK) epsilon (IKK\u03b5 or IKBKE) via TRAFs. Imunoprecipitation combined with mass spectrometry (MS)-based proteomic assays identified interactors of endogenous TBK1, such as TANK and NAP1, in SeV or HHV-1 (HSV-1)-infected human acute monocytic leukemia cells (THP\u20101) cells (Shang L et al. 2018). TBK1 and IKBKE trigger phosphorylation of interferon regulatory factor 3 (IRF3) and IRF7 and subsequent expression of type I interferons (IFNs; IFN\u2011\u03b1/\u03b2). Both TBK1 and IKBKE directly phosphorylate IRF3 and IRF7 targeting identical residues within the C-terminal signal-responsive domain (McWhirter SM et al. 2004; tenOever BR et al. 2004). Type I IFNs can induce the expression of numerous antiviral genes called interferon\u2011stimulated genes (ISGs). Structural studies revealed a dimeric assembly of TBK1 that is stabilized by an extensive network of interactions among the kinase, ubiquitin\u2011like (ULD) and scaffold/dimerization (SDD) domains of TBK1 (Larabi A et al. 2013; Tu D et al. 2013). IKBKE was also reported to form dimers (Nakatsu Y et al. 2014). Even though the contacts that stabilize the TBK1 dimer are largely conserved in IKK\u03b5 (IKBKE), studies reported differences in activation mechanisms between TBK1 and IKBKE (Larabi A et al. 2013; Tu D et al. 2013; Nakatsu Y et al. 2014). While the C\u2011terminal region was required for dimerization of IKBKE and downstream signaling, a C\u2011terminally truncated fragment of TBK1 formed a homodimer both in vitro and in vivo and was able to induce IRF3 phosphorylation (Nakatsu Y et al. 2014). Mutants that interfere with TBK1 dimerization showed significantly reduced trans\u2011autophosphorylation upon expression in human embryonic kidney 293 (HEK293) cells (Larabi A et al. 2013). An intact TBK1 dimer was modified by K63\u2011linked polyubiquitination on lysine 30 and lysine 401, and these modifications were required for TBK1 activation in HEK293 cells (Tu D et al. 2013). Similar findings were reported for IKBKE (Zhou AY et al. 2013). Further, interferon\u2011\u03b2 expression was ablated in TBK1\u2011/\u2011 mouse embryo fibroblasts (MEFs) cells reconstituted with dimerization defective TBK1 mutants (Tu D et al. 2013). Structural studies suggest that TBK1 dimerization is required for activation via transautophosphorylation at Ser172 of dimeric TBK1 (Larabi A et al. 2013; Tu D et al. 2013; Ma X et al. 2012). However, familial amyotrophic lateral sclerosis (ALS)\u2011associated TBK1 mutations in ULD or SDD displayed defects in dimerization of TBK1 without losing kinase activity (Ye J et al. 2019). These observations suggest that TBK1 dimerization is not required for kinase activation. Rather, dimerization seems to increase protein stability and enables efficient kinase\u2011substrate interactions (Ye J et al. 2019).",
"cellular_location": "mitochondrial outer membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q14164-1",
"Q9UHD2-1",
"Q8IUD6-1",
"Q9BYX4-1",
"Q14258-1",
"Q13114-1",
"O95786-1",
"Q9C037-1"
],
"evidence": [
{
"id": "R-HSA-9705137",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9705137"
}
]
},
{
"id": "R-HSA-9705145",
"name": "TBK1, IKBKE form homodimers",
"equation": "",
"summary": "TBK1 (tumor necrosis factor (TNF) receptor-associated factor (TRAF) family member-associated NF-\u03baB activator (TANK)-binding kinase 1) and its close homolog inhibitor-kappa-B kinase (IKK) epsilon (IKK\u03b5 or IKBKE) are serine/threonine-protein kinases that trigger phosphorylation of interferon regulatory factor 3 (IRF3) and IRF7 and subsequent expression of type I interferons (IFNs; IFN-\u03b1/\u03b2). Type I IFNs can induce the expression of numerous antiviral genes called interferon-stimulated genes (ISGs). Structural studies revealed a dimeric assembly of TBK1 stabilized by an extensive network of interactions among its kinase, ubiquitin-like (ULD) and scaffold/dimerization (SDD) domains (Larabi A et al. 2013; Tu D et al. 2013). IKBKE was also reported to form dimers (Nakatsu Y et al. 2014). Even though the contacts that stabilize the TBK1 dimer are largely conserved in IKK\u03b5 (IKBKE), studies reported differences in activation mechanisms between TBK1 and IKBKE (Larabi A et al. 2013; Tu D et al. 2013; Nakatsu Y et al. 2014). While the C-terminal region was required for dimerization of IKBKE and downstream signaling, a C-terminally truncated fragment of TBK1 formed a dimer both in vitro and in vivo and was able to induce IRF3 phosphorylation (Nakatsu Y et al. 2014). Mutants that interfere with TBK1 dimerization showed significantly reduced trans-autophosphorylation upon expression in human embryonic kidney 293 (HEK293) cells (Larabi A et al. 2013). An intact TBK1 dimer was modified by K63-linked polyubiquitination on lysine 30 and lysine 401, and these modifications were required for TBK1 activation in HEK293 cells (Tu D et al. 2013). Similar findings were reported for IKBKE (Zhou AY et al. 2013). Further, interferon-\u03b2 expression was ablated in TBK1-/- mouse embryo fibroblasts (MEFs) cells reconstituted with dimerization defective TBK1 mutants (Tu D et al. 2013). Structural studies suggest that TBK1 dimerization is required for kinase activation via transautophosphorylation at Ser172 of dimeric TBK1 (Larabi A et al. 2013; Tu D et al. 2013; Ma X et al. 2012). However, dimerization of TBK1 was not required for TBK1 downstream activity once the activation loop was phosphorylated (Ma X et al. 2012; Larabi A et al. 2013). These observations are supported by findings that amyotrophic lateral sclerosis (ALS)-associated TBK1 mutations in ULD or SDD displayed defects in dimerization of TBK1 without losing kinase activity (Ye J et al. 2019). The Reactome event shows homodimer formation of TBK1 and/or IKBKE in the RIG-I-like receptors (RLRs):mitochondrial antiviral-signaling protein (MAVS) signaling pathway.
",
"cellular_location": "mitochondrial outer membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q12933-1",
"Q14164-1",
"Q9UHD2-1",
"Q9Y4K3-1",
"Q8IUD6-1",
"Q9BYX4-1",
"Q14258-1",
"O95786-1",
"Q9C037-1"
],
"evidence": [
{
"id": "R-HSA-9705145",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9705145"
}
]
},
{
"id": "R-HSA-9705320",
"name": "TBK1, IKBKE are autophosphorylated at Ser172",
"equation": "",
"summary": "Viral nucleic acids are sensed by cellular pattern-recognition receptors (PRRs), such as RIG-I-like receptors (RLR). RLRs activate the adaptor protein called mitochondrial antiviral-signaling protein (MAVS). MAVS recruits TBK1 (tumor necrosis factor (TNF) receptor-associated factor (TRAF) family member-associated NF-\u03baB activator (TANK)-binding kinase 1) and/or its close homolog inhibitor-kappa-B kinase (IKK) epsilon (IKK\u03b5 or IKBKE) via TRAFs (Fitzgerald KA et al. 2003; Fang R et al. 2017). The enzymatic activity of TBK1/IKBKE is initiated by phosphorylation at Ser172 located in the T loop of the TBK1 and IKK\u03b5 kinase domains, which is essential for the enhancement of kinase activity (Shimada T et al. 1999; Kishore N et al. 2002; Ma X et al. 2012; Gu L et al. 2013). TBK1 forms a homodimer (Larabi A et al. 2013; Tu D et al. 2013) and structural studies suggest that dimerization of TBK1 precludes autophosphorylation and activation in cis (Larabi A et al. 2013). IKBKE is also a dimer (Nakatsu Y et al. 2014). Other kinases such as IKKs were also implicated in TBK1/IKBKE activation (Fang R et al. 2017). Further, K63-linked polyubiquitination on Lys30 and Lys401 enhanced TBK1/IKBKe activation in HEK293 cells (Tu D et al. 2013; Zhou AY et al. 2013).
Activated TBK1 and IKBKE (IKK\u03b5) in turn trigger phosphorylation of interferon regulatory factor 3 (IRF3) and IRF7 and subsequent expression of type I interferons (IFNs; IFN-\u03b1/\u03b2). Type I IFNs can induce the expression of numerous antiviral genes called interferon-stimulated genes (ISGs).
Many viruses have evolved numerous mechanisms to evade antiviral action of type I IFNs by acting at the level of the TBK1/IKBKE kinases. For example, nonstructural protein 13 (nsp13) of severe acute respiratory syndrome coronavirus type 2 (SARS-CoV-2) binds and blocks TBK1 phosphorylation, while nsp6 binds TBK1 to suppress TBK1-mediated phosphorylation of IRF3 (Xia H et al. 2020). SARS-CoV-2 membrane protein M interacts with MAVS and TBK1 thus preventing the formation of MAVS signalosome (Zheng Y et al. 2020).", "cellular_location": "mitochondrial outer membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q14164-1", "Q9UHD2-1", "Q8IUD6-1", "Q9BYX4-1", "Q14258-1", "Q13114-1", "O95786-1", "Q9C037-1" ], "evidence": [ { "id": "R-HSA-9705320", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9705320" } ] }, { "id": "R-HSA-9705323", "name": "Phosphorylation of TBK1/IKBKE", "equation": "", "summary": "Viral nucleic acids are sensed by cellular pattern-recognition receptors (PRRs), such as RIG-I-like receptors (RLR). RLRs activate the adaptor protein called mitochondrial antiviral-signaling protein (MAVS). MAVS recruits TBK1 (tumor necrosis factor (TNF) receptor-associated factor (TRAF) family member-associated NF-\u03baB activator (TANK)-binding kinase 1) and/or its close homolog inhibitor-kappa-B kinase (IKK) epsilon (IKK\u03b5 or IKBKE) via TRAFs (Fitzgerald KA et al. 2003; Fang R et al. 2017). The enzymatic activity of TBK1/IKBKE is initiated by phosphorylation at Ser172 located in the T loop of the TBK1 and IKK\u03b5 kinase domains, which is essential for the enhancement of kinase activity (Shimada T et al. 1999; Kishore N et al. 2002; Ma X et al. 2012; Gu L et al. 2013). TBK1 forms a homodimer (Larabi A et al. 2013; Tu D et al. 2013) and structural studies suggest that dimerization of TBK1 precludes autophosphorylation and activation in cis (Larabi A et al. 2013). IKBKE is also a dimer (Nakatsu Y et al. 2014). Other kinases such as IKKs were also implicated in TBK1/IKBKE activation (Fang R et al. 2017). Further, K63-linked polyubiquitination on Lys30 and Lys401 enhanced TBK1/IKBKE activation in HEK293 cells (Tu D et al. 2013; Zhou AY et al. 2013).
Activated TBK1 and IKBKE in turn trigger phosphorylation of interferon regulatory factor 3 (IRF3) and IRF7 and subsequent expression of type I interferons (IFNs; IFN-\u03b1/\u03b2). Type I IFNs can induce the expression of numerous antiviral genes called interferon-stimulated genes (ISGs).
Many viruses have evolved numerous mechanisms to evade antiviral action of type I IFNs by acting at the level of the TBK1/IKBKE kinases. For example, nonstructural protein 13 (nsp13) of severe acute respiratory syndrome coronavirus type 2 (SARS-CoV-2) binds and blocks TBK1 phosphorylation, while nsp6 binds TBK1 to suppress TBK1-mediated phosphorylation of IRF3 (Xia H et al. 2020). SARS-CoV-2 membrane protein M interacts with MAVS and TBK1 thus preventing the formation of MAVS signalosome (Zheng Y et al. 2020).", "cellular_location": "mitochondrial outer membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q12933-1", "Q14164-1", "Q9UHD2-1", "Q9Y4K3-1", "Q8IUD6-1", "Q9BYX4-1", "Q14258-1", "O95786-1", "Q9C037-1" ], "evidence": [ { "id": "R-HSA-9705323", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9705323" } ] }, { "id": "R-HSA-9717469", "name": "NS2 (1B) binds DDX58", "equation": "", "summary": "Human respiratory syncytial virus (RSV) nonstructural protein (NS2 or 1B) interacts with the N-terminal caspase activation recruitment domain (CARD) of DDX58 (RIG-I) upon co-expression in human embryonic kidney 293T (HEK293T) cells (Ling Z et al. 2009). Viral 1B also co-precipitates with endogenous DDX58 during RSV infection in human lung carcinoma (A549) cells. The binding of viral 1B (NS2) is believed to prevent CARD-CARD interactions between DDX58 and MAVS, thereby inhibiting DDX58 (RIG-I)-mediated induction of IFN. In summary, hRSV 1B acts as a multifunctional IFN antagonist, helping the virus to evade host innate immunity (Ling Z et al. 2009; Pei et al, 2021).", "cellular_location": "cytosol", "input_participant_list": [], "output_participant_list": [ "R-RSY-9717498" ], "enzyme_list": [ "O95786-1" ], "evidence": [ { "id": "R-HSA-9717469", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9717469" } ] }, { "id": "R-HSA-9717658", "name": "SARS-CoV-2 N binds DDX58", "equation": "", "summary": "Antiviral innate immune response receptor RIG-I (also known as retinoic acid-inducible gene I protein RIG-1 or DExD/H-box helicase 58, DDX58) directly recognizes and binds to viral 5\u2032-PPP RNA and short dsRNA through its helicase and repressor domain (Kato H et al. 2006). DDX58 activates downstream signaling cascade leading to the production of type I interferons (IFN) and proinflammatory cytokines. Type I IFN immune signaling has been found to be dampened upon infection with the severe acute respiratory syndrome coronavirus type 2 (SARS-CoV-2) and SARS-CoV-2 nucleocapsid (N) protein was shown to produce this effect (Li et al, 2020; Oh SJ & Shin OK 2021). SARS-CoV-2 N suppressed type I interferon (IFN) production in Sendai virus (SeV)-infected or poly(I:C)-stimulated human embryonic kidney 293T (HEK293T) cells by targeting the DDX58 signaling pathway (Chen K et al. 2020). Similar results were obtained using human alveolar basal epithelial (A549) cells. The viral N protein was found to bind DDX58 in HEK293T cells expressing Flag-DDX58 and pHA-N protein (Chen K et al. 2020). \\Moreover, N protein was co-immunoprecipitated with endogenous RIG-I in Hela cells transfected with pHA-N, and the interaction was significantly enhanced upon SeV infection\\- Chen K et al. 2020. The viral N protein interacts with the DExD/H domain of DDX58, which has ATPase activity (Chen K et al. 2020). RNA-dependent ATP hydrolysis by DDX58 (RIG-1) is thought to control the ability of DDX58 to discriminate non-self RNA from the cellular self RNA (Louber J et al. 2015; Dickey TH et al. 2019). These data suggest that SARS-CoV-2 N protein suppresses type I IFN production by targeting the ATP-dependent DDX58 signaling pathway (Chen K et al. 2020). In addition, N suppresses DDX58-mediated IFN-production via binding to RING-finger E3 ubiquitin ligase TRIM25 (Oh SJ & Shin OK 2021).", "cellular_location": "cytosol", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O95786-1" ], "evidence": [ { "id": "R-HSA-9717658", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9717658" } ] }, { "id": "R-HSA-9755258", "name": "DDX58 binds SARS-CoV-2 dsRNA intermediates", "equation": "", "summary": "The replication strategy of SARS-CoV-2 can generate double-stranded RNA (dsRNA) intermediates, that may act as pathogen-associated molecular patterns (PAMPs) recognized by cytoplasmic pattern recognition receptor (PRR) such as antiviral innate immune response receptor RIG-I (also known as DEAD box protein 58, DDX58). DDX58 recognizes short dsRNAs. Viral RNA binding provokes a change in DDX58 conformation exposing the caspase activation and recruitment domain (CARD) leading to DDX58 oligomerization, allowing it to interact with mitochondrial antiviral\u2011signaling protein (MAVS, IPS\u20111).
Gene ablation using CRISPR/Cas9 showed that both DDX58 and IFIH1 sense severe acute respiratory syndrome coronavirus type 2 (SARS-CoV-2) infection in human embryonic kidney HEK293T cells (Kouwaki T et al. 2021). Similar findings were reported for SARS-CoV-2-infected human adenocarcinoma-derived lung epithelial Calu-3 cells (Thorne LG et al. 2021). On the contrary, several studies showed that depletion of DDX58 had no effect in infected Calu-3 cells (Sampaio NG et al. 2021; Yin X et al. 2021; Rebendenne A et al. 2021). Another group reported that the helicase domain of DDX58 interacts with the 3\u2032 UTR of the SARS-CoV-2 RNA in human lung epithelial cells, though this interaction failed to activate the ATPase activity of DDX58 and binding to MAVS (Yamada T et al. 2021). DDX58 (RIG-I), along with other proteins associated to virus infection (MAVS, TRAFs), were differentially expressed in COVID-19 patients vs healthy controls (Leng L et al. 2020). This Reactome event describes binding of DDX58 (RIG-I) to SARS-CoV-2 dsRNA intermediates, however the role of DDX58 in the antiviral innate immune response to SARS-CoV-2 remains elusive.", "cellular_location": "cytosol", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O95786-1" ], "evidence": [ { "id": "R-HSA-9755258", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9755258" } ] }, { "id": "R-HSA-9833388", "name": "MAVS and DDX58 interact", "equation": "", "summary": "Mitochondrial antiviral signaling protein (MAVS, IPS-1) acts as an adaptor linking RIG-I (also known as retinoic acid-inducible gene I protein RIG-1 or DExD/H-box helicase 58, DDX58) and MDA5 (IFIH1) to downstream molecules that activate TBK1 and IKKi (Kawai et al, 2005; Seth et al, 2005).", "cellular_location": "cytosol, mitochondrial matrix, mitochondrial outer membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q14258-1", "O95786-1" ], "evidence": [ { "id": "R-HSA-9833388", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9833388" } ] }, { "id": "R-HSA-9836769", "name": "RSV dsRNA binds DDX58", "equation": "", "summary": "Retinoic acid-inducible gene I (RIG-I)-like receptors (RIG-I and MDA5), encoded by the DDX58 and IFIH1 genes, respectively, detect the presence of double-stranded RNA\u00a0within the cell cytosol (reviewed by Chow KT et al. 2018; Rehwinkel J & Gack MU 2020).\u00a0DDX58 (RIG-I) is activated by short 5' triphosphorylated dsRNA, while IFIH1 (MDA5) is triggered by long double-stranded RNA molecules regardless of their 5' phosphorylation status. Upon detection, both RIG-I and MDA5 transmit signals through the adaptor protein mitochondrial antiviral-signaling protein (MAVS) to induce the activation of transcription factors interferon receptor factor 3 (IRF-3) and nuclear factor kappa B (NF-kappa-B), which ultimately results in the induction of type I interferons.
Respiratory syncytial virus\u00a0(RSV) induces DDX58 (RIG-I) activity to mediate production of inflammatory cytokines and chemokines (Liu P et al. 2007; Okabayashi T et al. 2011; Guo X et al. 2015; Mart\u00edn-Vicente M et al. 2019). Immunoprecipitation assay showed that DDX58 (RIG-I) binds to RSV RNA (Liu P et al. 2007). Upregulation of DDX58 expression was observed following RSV infection in human bronchiolar carcinoma cell line A549 (Liu P et al. 2007; Guo X et al. 2015) and in human primary peripheral blood mononuclear cells (PBMCs) (Vissers M et al. 2012). Both type I IFN-\u03b1/\u03b2 and type III IFN-\u03bb were induced by RSV infection in A549 cells in a DDX58 (RIG-I)-dependent manner (Okabayashi T et al. 2011). Suppression of DDX58 in RSV-infected human primary nasal epithelial cells (hTERT-NECs) reduced the production of IFN-\u03bb, but not type I IFNs, indicating that DDX58 (RIG-I) plays a prominent role in inducing type III IFN in NECs (Okabayashi T et al. 2011). RSV-induced phosphorylation of NF-kappa B p65 at serine 536 in A549 cells was shown to be dependent upon the presence of RIG-I, MAVS, TRAF6, and IKK beta (Yoboua F et al. 2010). Silencing DDX58(RIG-I) in A549 cells using siRNA inhibits the activation of both NF-\u03baB and IRF3 transcription factors, as well as the expression of IFN-\u03b2, CXCL10, CCL5, ISG15, TNF-\u03b1, and IL-6, during early stages of RSV infection (Liu P et al. 2007; Yamamoto K et al. 2016; Mart\u00edn-Vicente M et al. 2019). Additionally, siRNA-mediated suppression of RIG-I expression in A549 or Vero cells blocks DDX58 (RIG-I) induction by RSV infection, preventing the upregulation of NLRC5, MHC-I, and the phosphorylation of IRF3, all of which are essential for an effective IFN response (Guo X et al. 2015). Further, immunofluorescence assay showed that DDX58 (RIG-I), IFIH1 (MDA5) and MAVS co-localized with RSV genomic RNA (RSV A2 strain) in the small inclusion bodies in A549 cells (Lifland AW et al. 2012). Pretreatment of human, mouse, or ferret airway cell lines with a synthetic DDX58 (RIG-I) agonist (3pRNA) before RSV infection reduces susceptibility to the virus and inhibits its replication (Schwab LSU et al. 2022). A single intravenous injection of mice or ferrets with 3pRNA prior to RSV infection significantly restricts virus growth in the lungs (Schwab LSU et al. 2022). Clinical studies have shown a positive correlation between RSV viral load and the expression of RIG-1 mRNA in infants with RSV-induced bronchiolitis (Scagnolari C et al. 2009). The significance of the DDX58-signaling pathway was also demonstrated in an in vivo infectious model using MAVS-deficient mice, which exhibited reduced IFN-I production and pro-inflammatory cytokine expression in response to RSV (Demoor T et al. 2012; Kirsebom FCM et al. 2019; Paulsen M et al. 2020). These findings suggest a crucial role for DDX58 (RIG-I) in host defense against RSV infection.
The replication/transcription process of RSV,\u00a0a (\u2212)-sense ssRNA virus, is coordinated by nucleoprotein (N), large protein (L), phosphoprotein (P), and M2-1 protein. Viral N, L, P , M2-1 and RSV RNA form the RNA synthesis ribonucleoprotein (RNP) complex (reviewed by Cao D et al. 2021). This complex serves as a template for RNA replication, generating the (+) RNA antigenome and the (-) RNA genome, as well as for RNA transcription, producing capped and poly-adenylated mRNAs. Within this complex, the catalytic core L polypeptide performs various enzymatic activities including RNA-dependent RNA polymerase (RdRp) activity, polyribonucleotidyl transferase activity, which is essential for mRNA 5' cap addition, and methyltransferase activity to catalyze the cap methylation at both N7- and 2\u2032-O-positions (reviewed by Sutto-Ortiz P et al. 2023).\u00a0The interaction of the cofactor P\u00a0with multiple proteins, including L and M2-1, enables conformational changes necessary to perform various enzymatic activities during the viral replication/transcription process. The M2-1 protein is required for RSV transcription to prevent premature transcription termination by increasing the processivity of the RdRp complex. Further, during RNA replication, the viral RNA polymerase activity can generate both standard (such as genomic) viral RNA and nonstandard viral RNA (reviewed by Vignuzzi M\u00a0 &\u00a0L\u00f3pez\u00a0CB 2019;\u00a0Gonz\u00e1lez Aparicio LJ et al. 2022). One type of nonstandard viral genome is known as copy-back viral genomes (cbVGs). These cbVGs are produced when the polymerase enzyme dissociates from the template strand at a specific breakpoint and then resumes elongation at a downstream rejoin point (reviewed by Vignuzzi M\u00a0 &\u00a0L\u00f3pez\u00a0CB 2019;\u00a0Gonz\u00e1lez Aparicio LJ et al. 2022). This process creates a complementary end to the 5' end of the nascent genomic RNA, resulting in the formation of double-stranded cbVG structures. RSV infection has been shown to generate\u00a0cbVGs in vitro and in vivo (Sun Y et al. 2015; 2019; Felt SA et al. 2022). The accumulation of cbVGs is thought to modulate the viral replication and stimulate host immune responses via PRRs including TLR3, DDX58 and IFIH1 (reviewed by Vignuzzi M\u00a0 &\u00a0L\u00f3pez\u00a0CB 2019;\u00a0Gonz\u00e1lez Aparicio LJ et al. 2022).
This Reactome event shows binding of RSV dsRNA species to RIG-I (DDX58).", "cellular_location": "cytosol", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O95786-1" ], "evidence": [ { "id": "R-HSA-9836769", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9836769" } ] }, { "id": "R-HSA-990526", "name": "Recruitment of ITCH and K48 ubiquitination of MAVS", "equation": "", "summary": "On viral infection PCB2 binds MAVS/IPS-1 and recruits the HECT domain-containing E3 ligase AIP4/ITCHY. AIP4 catalyses K48-polyubiquitination and degradation of MAVS. PCBP2 overexpression enhanced the interaction between MAVS and AIP4 and led to more degradation of MAVS. MAVS/IPS-1 regulation is very important in preventing excessive harmful immune responses.", "cellular_location": "cytosol, mitochondrial outer membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q96J02-1", "Q8IUD6-1", "Q9BYX4-1", "Q14258-1", "O95786-1", "Q9C037-1" ], "evidence": [ { "id": "R-HSA-990526", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-990526" } ] }, { "id": "R-HSA-990528", "name": "Interaction of PCBP2 with MAVS", "equation": "", "summary": "Poly(rC) binding protein 2 (PCB2), is one of the negative regulators of RIG-I/MDA5 signaling. 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"ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "A8MPP1", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/A8MPP1" } ] } ] }, { "uniprot_ac": "A8MUK1", "gene_name": "USP17L5", "activity": [ { "ec_number": "3.4.19.12", "activity": "Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).", "evidence": [ { "id": "A8MUK1", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/A8MUK1" } ] }, { "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "A8MUK1", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/A8MUK1" } ] } ] }, { "uniprot_ac": "B0G0Y4", "gene_name": "wrn", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "B0G0Y4", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/B0G0Y4" } ] }, { 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{ "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "C9JLJ4", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/C9JLJ4" } ] } ] }, { "uniprot_ac": "C9JPN9", "gene_name": "USP17L12", "activity": [ { "ec_number": "3.4.19.12", "activity": "Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).", "evidence": [ { "id": "C9JPN9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/C9JPN9" } ] }, { "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "C9JPN9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/C9JPN9" } ] } ] }, { "uniprot_ac": "C9JVI0", "gene_name": "USP17L11", "activity": [ { "ec_number": "3.4.19.12", "activity": "Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).", "evidence": [ { "id": "C9JVI0", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/C9JVI0" } ] }, { "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "C9JVI0", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/C9JVI0" } ] } ] }, { "uniprot_ac": "D3Z0M9", "gene_name": "Ddx23", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D3Z0M9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3Z0M9" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "D3Z0M9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3Z0M9" } ] } ] }, { "uniprot_ac": "D3Z4R1", "gene_name": "Hfm1", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D3Z4R1", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3Z4R1" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "D3Z4R1", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3Z4R1" } ] } ] }, { "uniprot_ac": "D3Z9Z9", "gene_name": "Smarcad1", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D3Z9Z9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3Z9Z9" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "D3Z9Z9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3Z9Z9" } ] } ] }, { "uniprot_ac": "D3ZA12", "gene_name": "Chd6", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D3ZA12", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZA12" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "D3ZA12", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZA12" } ] } ] }, { "uniprot_ac": "D3ZAP7", "gene_name": "Chd7", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D3ZAP7", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZAP7" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "D3ZAP7", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZAP7" } ] } ] }, { "uniprot_ac": "D3ZBY5", "gene_name": "Ddx10", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D3ZBY5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZBY5" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "D3ZBY5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZBY5" } ] } ] }, { "uniprot_ac": "D3ZD32", "gene_name": "Chd5", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D3ZD32", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZD32" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "D3ZD32", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZD32" } ] } ] }, { "uniprot_ac": "D3ZD46", "gene_name": "Dhx58", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D3ZD46", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZD46" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "D3ZD46", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZD46" } ] } ] }, { "uniprot_ac": "D3ZD97", "gene_name": "Dhx15", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D3ZD97", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZD97" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "D3ZD97", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZD97" } ] } ] }, { "uniprot_ac": "D3ZEG9", "gene_name": "Ercc2", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D3ZEG9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZEG9" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "D3ZEG9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZEG9" } ] } ] }, { "uniprot_ac": "D3ZFP4", "gene_name": "Mcm3", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D3ZFP4", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZFP4" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "D3ZFP4", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZFP4" } ] } ] }, { "uniprot_ac": "D3ZG52", "gene_name": "Dna2", "activity": [ { "ec_number": "3.1.-.-", "activity": "", "evidence": [ { "id": "D3ZG52", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZG52" } ] }, { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D3ZG52", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZG52" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "D3ZG52", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZG52" } ] } ] }, { "uniprot_ac": "D3ZH42", "gene_name": "Mov10l1", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D3ZH42", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZH42" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "D3ZH42", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZH42" } ] } ] }, { "uniprot_ac": "D3ZHW0", "gene_name": "Dhx29", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D3ZHW0", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZHW0" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "D3ZHW0", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZHW0" } ] } ] }, { "uniprot_ac": "D3ZP96", "gene_name": "Mcm2", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D3ZP96", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZP96" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "D3ZP96", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZP96" } ] } ] }, { "uniprot_ac": "D3ZQW1", "gene_name": "Blm", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D3ZQW1", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZQW1" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "D3ZQW1", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZQW1" } ] } ] }, { "uniprot_ac": "D3ZSV6", "gene_name": "Dhx33", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D3ZSV6", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZSV6" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "D3ZSV6", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZSV6" } ] } ] }, { "uniprot_ac": "D3ZUC2", "gene_name": "Mov10", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D3ZUC2", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZUC2" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "D3ZUC2", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZUC2" } ] } ] }, { "uniprot_ac": "D3ZVK1", "gene_name": "Mcm8", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D3ZVK1", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZVK1" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "D3ZVK1", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZVK1" } ] } ] }, { "uniprot_ac": "D3ZX56", "gene_name": "Ddx55", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D3ZX56", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZX56" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "D3ZX56", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D3ZX56" } ] } ] }, { "uniprot_ac": "D4A1R0", "gene_name": "Dhx37", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D4A1R0", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D4A1R0" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "D4A1R0", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D4A1R0" } ] } ] }, { "uniprot_ac": "D4A2B7", "gene_name": "Afg2b", "activity": [ { "ec_number": "3.6.4.10", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D4A2B7", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D4A2B7" } ] }, { "ec_number": "3.6.4.10", "activity": "", "evidence": [ { "id": "D4A2B7", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D4A2B7" } ] } ] }, { "uniprot_ac": "D4A2Z8", "gene_name": "Dhx36", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D4A2Z8", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D4A2Z8" } ] }, { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D4A2Z8", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D4A2Z8" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "D4A2Z8", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D4A2Z8" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "D4A2Z8", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D4A2Z8" } ] } ] }, { "uniprot_ac": "D4A321", "gene_name": "Dhx38", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D4A321", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D4A321" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "D4A321", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D4A321" } ] } ] }, { "uniprot_ac": "D4A523", "gene_name": "Nlrp3", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "D4A523", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D4A523" } ] } ] }, { "uniprot_ac": "D4A6Q6", "gene_name": "Ino80", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "D4A6Q6", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D4A6Q6" } ] } ] }, { "uniprot_ac": "D4A7Q5", "gene_name": "Ddx28", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D4A7Q5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D4A7Q5" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "D4A7Q5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D4A7Q5" } ] } ] }, { "uniprot_ac": "D4AAG9", "gene_name": "Chd1", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D4AAG9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D4AAG9" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "D4AAG9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D4AAG9" } ] } ] }, { "uniprot_ac": "D4ACP5", "gene_name": "Recql5", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D4ACP5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D4ACP5" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "D4ACP5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D4ACP5" } ] } ] }, { "uniprot_ac": "D4ADT5", "gene_name": "Rig1", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "D4ADT5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D4ADT5" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "D4ADT5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D4ADT5" } ] } ] }, { "uniprot_ac": "D6R901", "gene_name": "USP17L21", "activity": [ { "ec_number": "3.4.19.12", "activity": "Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).", "evidence": [ { "id": "D6R901", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D6R901" } ] }, { "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "D6R901", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D6R901" } ] } ] }, { "uniprot_ac": "D6R9N7", "gene_name": "USP17L18", "activity": [ { "ec_number": "3.4.19.12", "activity": "Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).", "evidence": [ { "id": "D6R9N7", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D6R9N7" } ] }, { "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "D6R9N7", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D6R9N7" } ] } ] }, { "uniprot_ac": "D6RA61", "gene_name": "USP17L22", "activity": [ { "ec_number": "3.4.19.12", "activity": "Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).", "evidence": [ { "id": "D6RA61", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D6RA61" } ] }, { "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "D6RA61", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D6RA61" } ] } ] }, { "uniprot_ac": "D6RBQ6", "gene_name": "USP17L17", "activity": [ { "ec_number": "3.4.19.12", "activity": "Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).", "evidence": [ { "id": "D6RBQ6", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D6RBQ6" } ] }, { "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "D6RBQ6", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D6RBQ6" } ] } ] }, { "uniprot_ac": "D6RCP7", "gene_name": "USP17L19", "activity": [ { "ec_number": "3.4.19.12", "activity": "Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).", "evidence": [ { "id": "D6RCP7", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D6RCP7" } ] }, { "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "D6RCP7", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D6RCP7" } ] } ] }, { "uniprot_ac": "D6RJB6", "gene_name": "USP17L20", "activity": [ { "ec_number": "3.4.19.12", "activity": "Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).", "evidence": [ { "id": "D6RJB6", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D6RJB6" } ] }, { "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "D6RJB6", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/D6RJB6" } ] } ] }, { "uniprot_ac": "E9PU01", "gene_name": "Chd4", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "E9PU01", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/E9PU01" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "E9PU01", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/E9PU01" } ] } ] }, { "uniprot_ac": "E9PZJ8", "gene_name": "Ascc3", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "E9PZJ8", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/E9PZJ8" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "E9PZJ8", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/E9PZJ8" } ] } ] }, { "uniprot_ac": "E9PZM4", "gene_name": "Chd2", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "E9PZM4", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/E9PZM4" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "E9PZM4", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/E9PZM4" } ] } ] }, { "uniprot_ac": "E9Q555", "gene_name": "Rnf213", "activity": [ { "ec_number": "2.3.2.-", "activity": "", "evidence": [ { "id": "E9Q555", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/E9Q555" } ] }, { "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": "E9Q555", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/E9Q555" } ] }, { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "E9Q555", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/E9Q555" } ] }, { "ec_number": "2.3.2.27", "activity": "", "evidence": [ { "id": "E9Q555", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/E9Q555" } ] } ] }, { "uniprot_ac": "E9QAM5", "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": "E9QAM5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/E9QAM5" } ] }, { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "E9QAM5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/E9QAM5" } ] }, { "ec_number": "3.1.13.1", "activity": "", "evidence": [ { "id": "E9QAM5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/E9QAM5" } ] } ] }, { "uniprot_ac": "F1LNJ2", "gene_name": "Snrnp200", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "F1LNJ2", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/F1LNJ2" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "F1LNJ2", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/F1LNJ2" } ] } ] }, { "uniprot_ac": "F1LPQ2", "gene_name": "Ascc3", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "F1LPQ2", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/F1LPQ2" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "F1LPQ2", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/F1LPQ2" } ] } ] }, { "uniprot_ac": "F1LTH9", "gene_name": "Wrn", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "F1LTH9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/F1LTH9" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "F1LTH9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/F1LTH9" } ] } ] }, { "uniprot_ac": "F1LTR3", "gene_name": "Tdrd12", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "F1LTR3", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/F1LTR3" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "F1LTR3", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/F1LTR3" } ] } ] }, { "uniprot_ac": "F1LWY1", "gene_name": "Hfm1", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "F1LWY1", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/F1LWY1" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "F1LWY1", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/F1LWY1" } ] } ] }, { "uniprot_ac": "F1M298", "gene_name": "Fbh1", "activity": [ { "ec_number": "5.6.2.4", "activity": "Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.", "evidence": [ { "id": "F1M298", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/F1M298" } ] }, { "ec_number": "5.6.2.4", "activity": "", "evidence": [ { "id": "F1M298", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/F1M298" } ] } ] }, { "uniprot_ac": "F1M5F3", "gene_name": "Mcm9", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "F1M5F3", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/F1M5F3" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "F1M5F3", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/F1M5F3" } ] } ] }, { "uniprot_ac": "F1M9L4", "gene_name": "Atp13a4", "activity": [ { "ec_number": "7.2.2.-", "activity": "", "evidence": [ { "id": "F1M9L4", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/F1M9L4" } ] } ] }, { "uniprot_ac": "F1MA70", "gene_name": "Atp13a5", "activity": [ { "ec_number": "7.2.2.-", "activity": "", "evidence": [ { "id": "F1MA70", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/F1MA70" } ] } ] }, { "uniprot_ac": "F8VPZ5", "gene_name": "Ercc6", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "F8VPZ5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/F8VPZ5" } ] } ] }, { "uniprot_ac": "G3V681", "gene_name": "Mcm4", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "G3V681", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/G3V681" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "G3V681", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/G3V681" } ] } ] }, { "uniprot_ac": "G3V6W5", "gene_name": "Ifih1", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "G3V6W5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/G3V6W5" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "G3V6W5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/G3V6W5" } ] } ] }, { "uniprot_ac": "G3V8T5", "gene_name": "Ruvbl2", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "G3V8T5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/G3V8T5" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "G3V8T5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/G3V8T5" } ] } ] }, { "uniprot_ac": "G3V9M1", "gene_name": "Ddx23", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "G3V9M1", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/G3V9M1" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "G3V9M1", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/G3V9M1" } ] } ] }, { "uniprot_ac": "G3X8X0", "gene_name": "Dhx16", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "G3X8X0", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/G3X8X0" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "G3X8X0", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/G3X8X0" } ] } ] }, { "uniprot_ac": "O00148", "gene_name": "DDX39A", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O00148", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O00148" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "O00148", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O00148" } ] } ] }, { "uniprot_ac": "O00571", "gene_name": "DDX3X", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O00571", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O00571" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "O00571", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O00571" } ] } ] }, { "uniprot_ac": "O00835", "gene_name": "repB", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O00835", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O00835" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "O00835", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O00835" } ] } ] }, { "uniprot_ac": "O08811", "gene_name": "Ercc2", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O08811", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O08811" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "O08811", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O08811" } ] } ] }, { "uniprot_ac": "O09053", "gene_name": "Wrn", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O09053", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O09053" } ] }, { "ec_number": "3.1.-.-", "activity": "", "evidence": [ { "id": "O09053", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O09053" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "O09053", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O09053" } ] } ] }, { "uniprot_ac": "O13559", "gene_name": "YRF1-4", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O13559", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O13559" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "O13559", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O13559" } ] } ] }, { "uniprot_ac": "O14646", "gene_name": "CHD1", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O14646", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O14646" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "O14646", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O14646" } ] } ] }, { "uniprot_ac": "O14647", "gene_name": "CHD2", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O14647", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O14647" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "O14647", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O14647" } ] } ] }, { "uniprot_ac": "O14656", "gene_name": "TOR1A", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "O14656", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O14656" } ] } ] }, { "uniprot_ac": "O14657", "gene_name": "TOR1B", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "O14657", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O14657" } ] } ] }, { "uniprot_ac": "O14920", "gene_name": "IKBKB", "activity": [ { "ec_number": "2.7.11.10", "activity": "ATP + L-seryl-[I-kappa-B protein] = ADP + H(+) + O-phospho-L-seryl-[I-kappa-B protein].", "evidence": [ { "id": "O14920", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O14920" } ] }, { "ec_number": "2.7.11.10", "activity": "", "evidence": [ { "id": "O14920", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O14920" } ] }, { "ec_number": "2.7.11.1", "activity": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].", "evidence": [ { "id": "O14920", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O14920" } ] } ] }, { "uniprot_ac": "O14933", "gene_name": "UBE2L6", "activity": [ { "ec_number": "2.3.2.23", "activity": "S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.", "evidence": [ { "id": "O14933", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O14933" } ] }, { "ec_number": "2.3.2.23", "activity": "", "evidence": [ { "id": "O14933", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O14933" } ] } ] }, { "uniprot_ac": "O15111", "gene_name": "CHUK", "activity": [ { "ec_number": "2.7.11.10", "activity": "ATP + L-seryl-[I-kappa-B protein] = ADP + H(+) + O-phospho-L-seryl-[I-kappa-B protein].", "evidence": [ { "id": "O15111", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O15111" } ] }, { "ec_number": "2.7.11.10", "activity": "", "evidence": [ { "id": "O15111", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O15111" } ] } ] }, { "uniprot_ac": "O15523", "gene_name": "DDX3Y", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O15523", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O15523" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "O15523", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O15523" } ] } ] }, { "uniprot_ac": "O16102", "gene_name": "Chd3", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O16102", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O16102" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "O16102", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O16102" } ] } ] }, { "uniprot_ac": "O35286", "gene_name": "Dhx15", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O35286", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O35286" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "O35286", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O35286" } ] } ] }, { "uniprot_ac": "O43143", "gene_name": "DHX15", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O43143", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O43143" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "O43143", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O43143" } ] } ] }, { "uniprot_ac": "O43933", "gene_name": "PEX1", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "O43933", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O43933" } ] } ] }, { "uniprot_ac": "O46072", "gene_name": "kz", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O46072", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O46072" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "O46072", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O46072" } ] } ] }, { "uniprot_ac": "O60231", "gene_name": "DHX16", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O60231", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O60231" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "O60231", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O60231" } ] } ] }, { "uniprot_ac": "O60282", "gene_name": "KIF5C", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "O60282", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O60282" } ] } ] }, { "uniprot_ac": "O60306", "gene_name": "AQR", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O60306", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O60306" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "O60306", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O60306" } ] } ] }, { "uniprot_ac": "O61305", "gene_name": "Dbp80", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O61305", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O61305" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "O61305", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O61305" } ] } ] }, { "uniprot_ac": "O70133", "gene_name": "Dhx9", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O70133", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O70133" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "O70133", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O70133" } ] } ] }, { "uniprot_ac": "O75351", "gene_name": "VPS4B", "activity": [ { "ec_number": "3.6.4.6", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O75351", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O75351" } ] }, { "ec_number": "3.6.4.6", "activity": "", "evidence": [ { "id": "O75351", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O75351" } ] } ] }, { "uniprot_ac": "O75417", "gene_name": "POLQ", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O75417", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O75417" } ] }, { "ec_number": "2.7.7.7", "activity": "a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1).", "evidence": [ { "id": "O75417", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O75417" } ] }, { "ec_number": "2.7.7.49", "activity": "a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1).", "evidence": [ { "id": "O75417", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O75417" } ] } ] }, { "uniprot_ac": "O75643", "gene_name": "SNRNP200", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O75643", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O75643" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "O75643", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O75643" } ] } ] }, { "uniprot_ac": "O88700", "gene_name": "Blm", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O88700", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O88700" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "O88700", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O88700" } ] } ] }, { "uniprot_ac": "O94761", "gene_name": "RECQL4", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O94761", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O94761" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "O94761", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O94761" } ] } ] }, { "uniprot_ac": "O94762", "gene_name": "RECQL5", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O94762", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O94762" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "O94762", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O94762" } ] } ] }, { "uniprot_ac": "O95786", "gene_name": "RIGI", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O95786", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O95786" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "O95786", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O95786" } ] } ] }, { "uniprot_ac": "O97159", "gene_name": "Mi-2", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "O97159", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O97159" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "O97159", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O97159" } ] } ] }, { "uniprot_ac": "P02572", "gene_name": "Act42A", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "P02572", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P02572" } ] } ] }, { "uniprot_ac": "P02574", "gene_name": "Act79B", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "P02574", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P02574" } ] } ] }, { "uniprot_ac": "P05186", "gene_name": "ALPL", "activity": [ { "ec_number": "3.1.3.1", "activity": "a phosphate monoester + H2O = an alcohol + phosphate.", "evidence": [ { "id": "P05186", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P05186" } ] }, { "ec_number": "3.9.1.1", "activity": "H2O + N-phosphocreatine = creatine + phosphate.", "evidence": [ { "id": "P05186", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P05186" } ] }, { "ec_number": "3.1.3.1", "activity": "", "evidence": [ { "id": "P05186", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P05186" } ] }, { "ec_number": "3.9.1.1", "activity": "", "evidence": [ { "id": "P05186", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P05186" } ] } ] }, { "uniprot_ac": "P06634", "gene_name": "DED1", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P06634", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P06634" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P06634", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P06634" } ] } ] }, { "uniprot_ac": "P06761", "gene_name": "Hspa5", "activity": [ { "ec_number": "3.6.4.10", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P06761", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P06761" } ] }, { "ec_number": "3.6.4.10", "activity": "", "evidence": [ { "id": "P06761", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P06761" } ] } ] }, { "uniprot_ac": "P06839", "gene_name": "RAD3", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P06839", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P06839" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "P06839", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P06839" } ] } ] }, { "uniprot_ac": "P07271", "gene_name": "PIF1", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P07271", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P07271" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "P07271", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P07271" } ] } ] }, { "uniprot_ac": "P07828", "gene_name": "act18", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "P07828", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P07828" } ] } ] }, { "uniprot_ac": "P07829", "gene_name": "act3", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "P07829", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P07829" } ] } ] }, { "uniprot_ac": "P07830", "gene_name": "act19", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "P07830", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P07830" } ] } ] }, { "uniprot_ac": "P07900", "gene_name": "HSP90AA1", "activity": [ { "ec_number": "3.6.4.10", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P07900", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P07900" } ] }, { "ec_number": "3.6.4.10", "activity": "", "evidence": [ { "id": "P07900", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P07900" } ] } ] }, { "uniprot_ac": "P07901", "gene_name": "Hsp90aa1", "activity": [ { "ec_number": "3.6.4.10", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P07901", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P07901" } ] }, { "ec_number": "3.6.4.10", "activity": "", "evidence": [ { "id": "P07901", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P07901" } ] } ] }, { "uniprot_ac": "P08289", "gene_name": "Alpl", "activity": [ { "ec_number": "3.1.3.1", "activity": "a phosphate monoester + H2O = an alcohol + phosphate.", "evidence": [ { "id": "P08289", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08289" } ] }, { "ec_number": "3.9.1.1", "activity": "H2O + N-phosphocreatine = creatine + phosphate.", "evidence": [ { "id": "P08289", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08289" } ] }, { "ec_number": "3.1.3.1", "activity": "", "evidence": [ { "id": "P08289", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08289" } ] } ] }, { "uniprot_ac": "P09052", "gene_name": "vas", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P09052", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P09052" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P09052", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P09052" } ] } ] }, { "uniprot_ac": "P09242", "gene_name": "Alpl", "activity": [ { "ec_number": "3.1.3.1", "activity": "a phosphate monoester + H2O = an alcohol + phosphate.", "evidence": [ { "id": "P09242", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P09242" } ] }, { "ec_number": "3.9.1.1", "activity": "H2O + N-phosphocreatine = creatine + phosphate.", "evidence": [ { "id": "P09242", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P09242" } ] }, { "ec_number": "3.1.3.1", "activity": "", "evidence": [ { "id": "P09242", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P09242" } ] }, { "ec_number": "3.9.1.1", "activity": "", "evidence": [ { "id": "P09242", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P09242" } ] } ] }, { "uniprot_ac": "P0CS90", "gene_name": "SSC1", "activity": [ { "ec_number": "3.6.4.10", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P0CS90", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P0CS90" } ] }, { "ec_number": "3.6.4.10", "activity": "", "evidence": [ { "id": "P0CS90", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P0CS90" } ] } ] }, { "uniprot_ac": "P0CX14", "gene_name": "YRF1-3", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P0CX14", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P0CX14" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "P0CX14", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P0CX14" } ] } ] }, { "uniprot_ac": "P0CX15", "gene_name": "YRF1-7", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P0CX15", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P0CX15" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "P0CX15", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P0CX15" } ] } ] }, { "uniprot_ac": "P0CX20", "gene_name": "YRF1-1", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P0CX20", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P0CX20" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "P0CX20", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P0CX20" } ] } ] }, { "uniprot_ac": "P0CX21", "gene_name": "YRF1-5", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P0CX21", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P0CX21" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "P0CX21", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P0CX21" } ] } ] }, { "uniprot_ac": "P0CX22", "gene_name": "YRF1-8", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P0CX22", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P0CX22" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "P0CX22", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P0CX22" } ] } ] }, { "uniprot_ac": "P10081", "gene_name": "TIF1", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P10081", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P10081" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P10081", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P10081" } ] } ] }, { "uniprot_ac": "P10630", "gene_name": "Eif4a2", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P10630", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P10630" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P10630", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P10630" } ] } ] }, { "uniprot_ac": "P10981", "gene_name": "Act87E", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "P10981", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P10981" } ] } ] }, { "uniprot_ac": "P10987", "gene_name": "Act5C", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "P10987", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P10987" } ] } ] }, { "uniprot_ac": "P11021", "gene_name": "HSPA5", "activity": [ { "ec_number": "3.6.4.10", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P11021", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P11021" } ] }, { "ec_number": "3.6.4.10", "activity": "", "evidence": [ { "id": "P11021", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P11021" } ] } ] }, { "uniprot_ac": "P11142", "gene_name": "HSPA8", "activity": [ { "ec_number": "3.6.4.10", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P11142", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P11142" } ] }, { "ec_number": "3.6.4.10", "activity": "", "evidence": [ { "id": "P11142", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P11142" } ] } ] }, { "uniprot_ac": "P11484", "gene_name": "SSB1", "activity": [ { "ec_number": "3.6.4.10", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P11484", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P11484" } ] }, { "ec_number": "3.6.4.10", "activity": "", "evidence": [ { "id": "P11484", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P11484" } ] } ] }, { "uniprot_ac": "P12954", "gene_name": "SRS2", "activity": [ { "ec_number": "5.6.2.4", "activity": "Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.", "evidence": [ { "id": "P12954", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P12954" } ] }, { "ec_number": "5.6.2.4", "activity": "", "evidence": [ { "id": "P12954", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P12954" } ] } ] }, { "uniprot_ac": "P15424", "gene_name": "MSS116", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P15424", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P15424" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P15424", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P15424" } ] } ] }, { "uniprot_ac": "P15938", "gene_name": "PRP16", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P15938", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P15938" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P15938", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P15938" } ] } ] }, { "uniprot_ac": "P16381", "gene_name": "D1Pas1", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P16381", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P16381" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P16381", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P16381" } ] } ] }, { "uniprot_ac": "P16474", "gene_name": "KAR2", "activity": [ { "ec_number": "3.6.4.10", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P16474", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P16474" } ] }, { "ec_number": "3.6.4.10", "activity": "", "evidence": [ { "id": "P16474", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P16474" } ] } ] }, { "uniprot_ac": "P16521", "gene_name": "YEF3", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "P16521", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P16521" } ] } ] }, { "uniprot_ac": "P17119", "gene_name": "KAR3", "activity": [ { "ec_number": "5.6.1.4", "activity": "ATP + H2O + a kinesin associated with a microtubule at position (n) = ADP + phosphate + a kinesin associated with a microtubule at position (n-1, toward the minus end).", "evidence": [ { "id": "P17119", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P17119" } ] }, { "ec_number": "5.6.1.4", "activity": "", "evidence": [ { "id": "P17119", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P17119" } ] } ] }, { "uniprot_ac": "P17844", "gene_name": "DDX5", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P17844", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P17844" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P17844", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P17844" } ] } ] }, { "uniprot_ac": "P18074", "gene_name": "ERCC2", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P18074", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P18074" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "P18074", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P18074" } ] } ] }, { "uniprot_ac": "P19109", "gene_name": "Rm62", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P19109", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P19109" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P19109", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P19109" } ] } ] }, { "uniprot_ac": "P19174", "gene_name": "PLCG1", "activity": [ { "ec_number": "3.1.4.11", "activity": "a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+).", "evidence": [ { "id": "P19174", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P19174" } ] }, { "ec_number": "3.1.4.11", "activity": "", "evidence": [ { "id": "P19174", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P19174" } ] } ] }, { "uniprot_ac": "P19447", "gene_name": "ERCC3", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P19447", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P19447" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "P19447", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P19447" } ] } ] }, { "uniprot_ac": "P19525", "gene_name": "EIF2AK2", "activity": [ { "ec_number": "2.7.10.2", "activity": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].", "evidence": [ { "id": "P19525", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P19525" } ] }, { "ec_number": "2.7.11.1", "activity": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].", "evidence": [ { "id": "P19525", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P19525" } ] }, { "ec_number": "2.7.11.1", "activity": "", "evidence": [ { "id": "P19525", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P19525" } ] } ] }, { "uniprot_ac": "P20029", "gene_name": "Hspa5", "activity": [ { "ec_number": "3.6.4.10", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P20029", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P20029" } ] }, { "ec_number": "3.6.4.10", "activity": "", "evidence": [ { "id": "P20029", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P20029" } ] } ] }, { "uniprot_ac": "P20095", "gene_name": "PRP2", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P20095", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P20095" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P20095", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P20095" } ] } ] }, { "uniprot_ac": "P20447", "gene_name": "DBP3", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P20447", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P20447" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P20447", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P20447" } ] } ] }, { "uniprot_ac": "P20448", "gene_name": "HCA4", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P20448", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P20448" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P20448", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P20448" } ] } ] }, { "uniprot_ac": "P20449", "gene_name": "DBP5", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P20449", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P20449" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P20449", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P20449" } ] } ] }, { "uniprot_ac": "P20480", "gene_name": "ncd", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "P20480", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P20480" } ] } ] }, { "uniprot_ac": "P21372", "gene_name": "PRP5", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P21372", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P21372" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P21372", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P21372" } ] } ] }, { "uniprot_ac": "P22516", "gene_name": "CHL1", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P22516", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P22516" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "P22516", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P22516" } ] } ] }, { "uniprot_ac": "P23128", "gene_name": "me31B", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P23128", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P23128" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P23128", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P23128" } ] } ] }, { "uniprot_ac": "P23249", "gene_name": "Mov10", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P23249", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P23249" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P23249", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P23249" } ] } ] }, { "uniprot_ac": "P23394", "gene_name": "PRP28", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P23394", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P23394" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P23394", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P23394" } ] } ] }, { "uniprot_ac": "P23458", "gene_name": "JAK1", "activity": [ { "ec_number": "2.7.10.2", "activity": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].", "evidence": [ { "id": "P23458", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P23458" } ] }, { "ec_number": "2.7.10.2", "activity": "", "evidence": [ { "id": "P23458", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P23458" } ] } ] }, { "uniprot_ac": "P24004", "gene_name": "PEX1", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "P24004", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P24004" } ] } ] }, { "uniprot_ac": "P24279", "gene_name": "MCM3", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P24279", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P24279" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "P24279", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P24279" } ] } ] }, { "uniprot_ac": "P24384", "gene_name": "PRP22", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P24384", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P24384" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P24384", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P24384" } ] } ] }, { "uniprot_ac": "P24783", "gene_name": "DBP2", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P24783", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P24783" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P24783", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P24783" } ] } ] }, { "uniprot_ac": "P24784", "gene_name": "DBP1", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P24784", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P24784" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P24784", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P24784" } ] } ] }, { "uniprot_ac": "P24785", "gene_name": "mle", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P24785", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P24785" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P24785", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P24785" } ] } ] }, { "uniprot_ac": "P25205", "gene_name": "MCM3", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P25205", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P25205" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "P25205", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P25205" } ] } ] }, { "uniprot_ac": "P25206", "gene_name": "Mcm3", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P25206", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P25206" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "P25206", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P25206" } ] } ] }, { "uniprot_ac": "P25439", "gene_name": "brm", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P25439", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P25439" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "P25439", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P25439" } ] } ] }, { "uniprot_ac": "P25694", "gene_name": "CDC48", "activity": [ { "ec_number": "3.6.4.6", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P25694", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P25694" } ] }, { "ec_number": "3.6.4.6", "activity": "", "evidence": [ { "id": "P25694", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P25694" } ] } ] }, { "uniprot_ac": "P25808", "gene_name": "SPB4", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P25808", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P25808" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P25808", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P25808" } ] } ] }, { "uniprot_ac": "P26196", "gene_name": "DDX6", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P26196", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P26196" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P26196", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P26196" } ] } ] }, { "uniprot_ac": "P26802", "gene_name": "Dbp73D", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P26802", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P26802" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P26802", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P26802" } ] } ] }, { "uniprot_ac": "P27361", "gene_name": "MAPK3", "activity": [ { "ec_number": "2.7.11.24", "activity": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].", "evidence": [ { "id": "P27361", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P27361" } ] }, { "ec_number": "2.7.11.24", "activity": "", "evidence": [ { "id": "P27361", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P27361" } ] } ] }, { "uniprot_ac": "P28738", "gene_name": "Kif5c", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "P28738", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P28738" } ] } ] }, { "uniprot_ac": "P29469", "gene_name": "MCM2", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P29469", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P29469" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "P29469", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P29469" } ] } ] }, { "uniprot_ac": "P29496", "gene_name": "MCM5", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P29496", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P29496" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "P29496", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P29496" } ] } ] }, { "uniprot_ac": "P29844", "gene_name": "Hsc70-3", "activity": [ { "ec_number": "3.6.1.3", "activity": "", "evidence": [ { "id": "P29844", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P29844" } ] }, { "ec_number": "3.6.4.10", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P29844", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P29844" } ] }, { "ec_number": "3.6.4.10", "activity": "", "evidence": [ { "id": "P29844", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P29844" } ] } ] }, { "uniprot_ac": "P30304", "gene_name": "CDC25A", "activity": [ { "ec_number": "3.1.3.48", "activity": "H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate.", "evidence": [ { "id": "P30304", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P30304" } ] }, { "ec_number": "3.1.3.48", "activity": "", "evidence": [ { "id": "P30304", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P30304" } ] } ] }, { "uniprot_ac": "P30665", "gene_name": "MCM4", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P30665", "database": "UniProtKB", "url": 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"database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P45818" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P45818", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P45818" } ] } ] }, { "uniprot_ac": "P46063", "gene_name": "RECQL", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P46063", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P46063" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "P46063", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P46063" } ] } ] }, { "uniprot_ac": "P46100", "gene_name": "ATRX", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P46100", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P46100" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "P46100", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P46100" } ] } ] }, { "uniprot_ac": "P46459", "gene_name": "NSF", "activity": [ { "ec_number": "3.6.4.6", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P46459", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P46459" } ] }, { "ec_number": "3.6.4.6", "activity": "", "evidence": [ { "id": "P46459", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P46459" } ] } ] }, { "uniprot_ac": "P46460", "gene_name": "Nsf", "activity": [ { "ec_number": "3.6.4.6", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P46460", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P46460" } ] }, { "ec_number": "3.6.4.6", "activity": "", "evidence": [ { "id": "P46460", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P46460" } ] } ] }, { "uniprot_ac": "P46461", "gene_name": "comt", "activity": [ { "ec_number": "3.6.4.6", "activity": "ATP + H2O = ADP + H(+) + 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"id": "P56536", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P56536" } ] } ] }, { "uniprot_ac": "P60010", "gene_name": "ACT1", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "P60010", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P60010" } ] } ] }, { "uniprot_ac": "P60122", "gene_name": "Ruvbl1", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P60122", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P60122" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "P60122", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P60122" } ] } ] }, { "uniprot_ac": "P60123", "gene_name": "Ruvbl1", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P60123", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P60123" } ] }, { "ec_number": 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"url": "https://www.uniprot.org/uniprot/P60842" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P60842", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P60842" } ] } ] }, { "uniprot_ac": "P60843", "gene_name": "Eif4a1", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P60843", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P60843" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P60843", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P60843" } ] } ] }, { "uniprot_ac": "P61077", "gene_name": "UBE2D3", "activity": [ { "ec_number": "2.3.2.24", "activity": "S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N(6)-monoubiquitinyl-[acceptor protein]-L-lysine.", "evidence": [ { "id": "P61077", "database": "UniProtKB", "url": 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ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.", "evidence": [ { "id": "P62837", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P62837" } ] }, { "ec_number": "2.3.2.23", "activity": "", "evidence": [ { "id": "P62837", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P62837" } ] } ] }, { "uniprot_ac": "P63017", "gene_name": "Hspa8", "activity": [ { "ec_number": "3.6.4.10", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P63017", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P63017" } ] }, { "ec_number": "3.6.4.10", "activity": "", "evidence": [ { "id": "P63017", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P63017" } ] } ] }, { "uniprot_ac": "P63018", "gene_name": "Hspa8", "activity": [ { "ec_number": "3.6.4.10", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P63018", "database": "UniProtKB", "url": 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"gene_name": "Actc1", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "P68035", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P68035" } ] } ] }, { "uniprot_ac": "P68133", "gene_name": "ACTA1", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "P68133", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P68133" } ] } ] }, { "uniprot_ac": "P68134", "gene_name": "Acta1", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "P68134", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P68134" } ] } ] }, { "uniprot_ac": "P68136", "gene_name": "Acta1", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "P68136", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P68136" } ] } ] }, { "uniprot_ac": "P70270", "gene_name": "Rad54l", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P70270", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P70270" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "P70270", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P70270" } ] } ] }, { "uniprot_ac": "P70486", "gene_name": "Atrx", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P70486", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P70486" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "P70486", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P70486" } ] } ] }, { "uniprot_ac": "P82995", "gene_name": "Hsp90aa1", "activity": [ { "ec_number": "3.6.4.10", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P82995", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P82995" } ] }, { "ec_number": "3.6.4.10", "activity": "", "evidence": [ { "id": "P82995", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P82995" } ] } ] }, { "uniprot_ac": "P83967", "gene_name": "Act88F", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "P83967", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P83967" } ] } ] }, { "uniprot_ac": "P90529", "gene_name": "ifdA", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P90529", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P90529" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "P90529", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P90529" } ] } ] }, { "uniprot_ac": "P97310", "gene_name": "Mcm2", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "P97310", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P97310" } ] }, { "ec_number": 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"3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q04217", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q04217" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q04217", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q04217" } ] } ] }, { "uniprot_ac": "Q04437", "gene_name": "YKU80", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q04437", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q04437" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "Q04437", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q04437" } ] } ] }, { "uniprot_ac": "Q04692", "gene_name": "Smarcad1", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q04692", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q04692" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "Q04692", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q04692" } ] } ] }, { "uniprot_ac": "Q05471", "gene_name": "SWR1", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q05471", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q05471" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "Q05471", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q05471" } ] } ] }, { "uniprot_ac": "Q05549", "gene_name": "HRQ1", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q05549", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q05549" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "Q05549", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q05549" } ] } ] }, { "uniprot_ac": "Q05931", "gene_name": "SSQ1", "activity": [ { "ec_number": "3.6.4.10", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q05931", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q05931" } ] }, { "ec_number": "3.6.4.10", "activity": "", "evidence": [ { "id": "Q05931", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q05931" } ] } ] }, { "uniprot_ac": "Q06218", "gene_name": "DBP9", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q06218", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q06218" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q06218", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q06218" } ] } ] }, { "uniprot_ac": "Q06698", "gene_name": "", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q06698", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q06698" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q06698", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q06698" } ] } ] }, { "uniprot_ac": "Q07478", "gene_name": "SUB2", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q07478", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q07478" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q07478", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q07478" } ] } ] }, { "uniprot_ac": "Q07886", "gene_name": "Dbp45A", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q07886", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q07886" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q07886", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q07886" } ] } ] }, { "uniprot_ac": "Q07888", "gene_name": "", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q07888", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q07888" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "Q07888", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q07888" } ] } ] }, { "uniprot_ac": "Q08211", "gene_name": "DHX9", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q08211", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q08211" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q08211", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q08211" } ] } ] }, { "uniprot_ac": "Q08995", "gene_name": "", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q08995", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q08995" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "Q08995", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q08995" } ] } ] }, { "uniprot_ac": "Q09XV5", "gene_name": "Chd8", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q09XV5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q09XV5" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "Q09XV5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q09XV5" } ] } ] }, { "uniprot_ac": "Q0VGM9", "gene_name": "Rtel1", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q0VGM9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q0VGM9" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "Q0VGM9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q0VGM9" } ] } ] }, { "uniprot_ac": "Q0VGT4", "gene_name": "Zgrf1", "activity": [ { "ec_number": "5.6.2.3", "activity": "Couples ATP hydrolysis with the unwinding of duplex DNA at the replication fork by translocating in the 5'-3' direction. This creates two antiparallel DNA single strands (ssDNA). The leading ssDNA polymer is the template for DNA polymerase III holoenzyme which synthesizes a continuous strand.", "evidence": [ { "id": "Q0VGT4", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q0VGT4" } ] }, { "ec_number": "5.6.2.3", "activity": "", "evidence": [ { "id": "Q0VGT4", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q0VGT4" } ] } ] }, { "uniprot_ac": "Q0WX57", "gene_name": "USP17L30", "activity": [ { "ec_number": "3.4.19.12", "activity": "Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).", "evidence": [ { "id": "Q0WX57", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q0WX57" } ] }, { "ec_number": "3.4.19.12", "activity": "", "evidence": [ { "id": "Q0WX57", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q0WX57" } ] } ] }, { "uniprot_ac": "Q12039", "gene_name": "HMI1", "activity": [ { "ec_number": "5.6.2.4", "activity": "Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.", "evidence": [ { "id": "Q12039", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q12039" } ] }, { "ec_number": "5.6.2.4", "activity": "", "evidence": [ { "id": "Q12039", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q12039" } ] } ] }, { "uniprot_ac": "Q12099", "gene_name": "FAL1", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q12099", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q12099" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q12099", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q12099" } ] } ] }, { "uniprot_ac": "Q12389", "gene_name": "DBP10", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q12389", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q12389" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q12389", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q12389" } ] } ] }, { "uniprot_ac": "Q12464", "gene_name": "RVB2", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q12464", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q12464" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "Q12464", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q12464" } ] } ] }, { "uniprot_ac": "Q12697", "gene_name": "YPK9", "activity": [ { "ec_number": "7.2.2.-", "activity": "", "evidence": [ { "id": "Q12697", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q12697" } ] } ] }, { "uniprot_ac": "Q12873", "gene_name": "CHD3", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q12873", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q12873" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "Q12873", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q12873" } ] } ] }, { "uniprot_ac": "Q12933", "gene_name": "TRAF2", "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": "Q12933", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q12933" } ] }, { "ec_number": "2.3.2.27", "activity": "", "evidence": [ { "id": "Q12933", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q12933" } ] } ] }, { "uniprot_ac": "Q13114", "gene_name": "TRAF3", "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": "Q13114", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q13114" } ] }, { "ec_number": "2.3.2.27", "activity": "", "evidence": [ { "id": "Q13114", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q13114" } ] } ] }, { "uniprot_ac": "Q13206", "gene_name": "DDX10", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q13206", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q13206" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q13206", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q13206" } ] } ] }, { "uniprot_ac": "Q13233", "gene_name": "MAP3K1", "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": "Q13233", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q13233" } ] }, { "ec_number": "2.7.11.25", "activity": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].", "evidence": [ { "id": "Q13233", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q13233" } ] }, { "ec_number": "2.7.11.25", "activity": "", "evidence": [ { "id": "Q13233", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q13233" } ] } ] }, { "uniprot_ac": "Q13283", "gene_name": "G3BP1", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q13283", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q13283" } ] }, { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q13283", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q13283" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q13283", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q13283" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "Q13283", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q13283" } ] } ] }, { "uniprot_ac": "Q13546", "gene_name": "RIPK1", "activity": [ { "ec_number": "2.7.11.1", "activity": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].", "evidence": [ { "id": "Q13546", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q13546" } ] }, { "ec_number": "2.7.11.1", "activity": "", "evidence": [ { "id": "Q13546", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q13546" } ] } ] }, { "uniprot_ac": "Q13608", "gene_name": "PEX6", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "Q13608", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q13608" } ] } ] }, { "uniprot_ac": "Q13838", "gene_name": "DDX39B", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q13838", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q13838" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q13838", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q13838" } ] } ] }, { "uniprot_ac": "Q14147", "gene_name": "DHX34", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q14147", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q14147" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q14147", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q14147" } ] } ] }, { "uniprot_ac": "Q14164", "gene_name": "IKBKE", "activity": [ { "ec_number": "2.7.11.10", "activity": "ATP + L-seryl-[I-kappa-B protein] = ADP + H(+) + O-phospho-L-seryl-[I-kappa-B protein].", "evidence": [ { "id": "Q14164", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q14164" } ] }, { "ec_number": "2.7.11.10", "activity": "", "evidence": [ { "id": "Q14164", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q14164" } ] } ] }, { "uniprot_ac": "Q14191", "gene_name": "WRN", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q14191", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q14191" } ] }, { "ec_number": "3.1.-.-", "activity": "", "evidence": [ { "id": "Q14191", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q14191" } ] } ] }, { "uniprot_ac": "Q14240", "gene_name": "EIF4A2", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q14240", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q14240" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q14240", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q14240" } ] } ] }, { "uniprot_ac": "Q14258", "gene_name": "TRIM25", "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": "Q14258", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q14258" } ] }, { "ec_number": "6.3.2.n3", "activity": "ATP + [ISG15] + [protein]-lysine = AMP + diphosphate + [protein]-N-ISGyllysine.", "evidence": [ { "id": "Q14258", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q14258" } ] }, { "ec_number": "6.3.2.n3", "activity": "", "evidence": [ { "id": "Q14258", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q14258" } ] } ] }, { "uniprot_ac": "Q14562", "gene_name": "DHX8", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q14562", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q14562" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q14562", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q14562" } ] } ] }, { "uniprot_ac": "Q14566", "gene_name": "MCM6", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q14566", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q14566" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "Q14566", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q14566" } ] } ] }, { "uniprot_ac": "Q14790", "gene_name": "CASP8", "activity": [ { "ec_number": "3.4.22.61", "activity": "Strict requirement for Asp at position P1 and has a preferred cleavage 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"3.6.4.12", "activity": "", "evidence": [ { "id": "Q9V3K3", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9V3K3" } ] } ] }, { "uniprot_ac": "Q9V433", "gene_name": "RecQ5", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9V433", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9V433" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "Q9V433", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9V433" } ] } ] }, { "uniprot_ac": "Q9V461", "gene_name": "Mcm6", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9V461", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9V461" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "Q9V461", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9V461" } ] } ] }, { "uniprot_ac": "Q9VD51", "gene_name": "pit", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VD51", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VD51" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q9VD51", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VD51" } ] } ] }, { "uniprot_ac": "Q9VDA0", "gene_name": "Fancm", "activity": [ { "ec_number": "5.6.2.4", "activity": "Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.", "evidence": [ { "id": "Q9VDA0", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VDA0" } ] }, { "ec_number": "5.6.2.4", "activity": "", "evidence": [ { "id": "Q9VDA0", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VDA0" } ] } ] }, { "uniprot_ac": "Q9VDY1", "gene_name": "Ino80", "activity": [ { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "Q9VDY1", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VDY1" } ] } ] }, { "uniprot_ac": "Q9VF26", "gene_name": "spn-E", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VF26", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VF26" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q9VF26", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VF26" } ] } ] }, { "uniprot_ac": "Q9VGI8", "gene_name": "Blm", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VGI8", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VGI8" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "Q9VGI8", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VGI8" } ] } ] }, { "uniprot_ac": "Q9VGW6", "gene_name": "Mcm5", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VGW6", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VGW6" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "Q9VGW6", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VGW6" } ] } ] }, { "uniprot_ac": "Q9VH07", "gene_name": "pont", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VH07", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VH07" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "Q9VH07", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VH07" } ] } ] }, { "uniprot_ac": "Q9VHP0", "gene_name": "bel", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VHP0", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VHP0" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q9VHP0", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VHP0" } ] } ] }, { "uniprot_ac": "Q9VHS8", "gene_name": "", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VHS8", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VHS8" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q9VHS8", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VHS8" } ] } ] }, { "uniprot_ac": "Q9VHU1", "gene_name": "", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VHU1", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VHU1" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q9VHU1", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VHU1" } ] } ] }, { "uniprot_ac": "Q9VIF6", "gene_name": "pths", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VIF6", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VIF6" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q9VIF6", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VIF6" } ] } ] }, { "uniprot_ac": "Q9VIZ3", "gene_name": "l(2)37Cb", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VIZ3", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VIZ3" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q9VIZ3", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VIZ3" } ] } ] }, { "uniprot_ac": "Q9VJ74", "gene_name": "Dmel\\CG10333", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VJ74", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VJ74" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q9VJ74", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VJ74" } ] } ] }, { "uniprot_ac": "Q9VL25", "gene_name": "ath", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VL25", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VL25" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q9VL25", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VL25" } ] } ] }, { "uniprot_ac": "Q9VL52", "gene_name": "SoYb", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VL52", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VL52" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q9VL52", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VL52" } ] } ] }, { "uniprot_ac": "Q9VL72", "gene_name": "Etl1", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VL72", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VL72" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "Q9VL72", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VL72" } ] } ] }, { "uniprot_ac": "Q9VL76", "gene_name": "mtDNA-helicase", "activity": [ { "ec_number": "5.6.2.3", "activity": "Couples ATP hydrolysis with the unwinding of duplex DNA at the replication fork by translocating in the 5'-3' direction. This creates two antiparallel DNA single strands (ssDNA). The leading ssDNA polymer is the template for DNA polymerase III holoenzyme which synthesizes a continuous strand.", "evidence": [ { "id": "Q9VL76", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VL76" } ] }, { "ec_number": "5.6.2.3", "activity": "", "evidence": [ { "id": "Q9VL76", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VL76" } ] } ] }, { "uniprot_ac": "Q9VN03", "gene_name": "Suv3", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VN03", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VN03" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q9VN03", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VN03" } ] } ] }, { "uniprot_ac": "Q9VNP5", "gene_name": "BoYb", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VNP5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VNP5" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q9VNP5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VNP5" } ] } ] }, { "uniprot_ac": "Q9VNV3", "gene_name": "Ddx1", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VNV3", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VNV3" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q9VNV3", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VNV3" } ] } ] }, { "uniprot_ac": "Q9VPT3", "gene_name": "Dbp21E2", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VPT3", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VPT3" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q9VPT3", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VPT3" } ] } ] }, { "uniprot_ac": "Q9VQN8", "gene_name": "Fign", "activity": [ { "ec_number": "3.-.-.-", "activity": "", "evidence": [ { "id": "Q9VQN8", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VQN8" } ] }, { "ec_number": "5.6.1.1", "activity": "n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.", "evidence": [ { "id": "Q9VQN8", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VQN8" } ] }, { "ec_number": "3.6.4.-", "activity": "", "evidence": [ { "id": "Q9VQN8", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VQN8" } ] } ] }, { "uniprot_ac": "Q9VQR3", "gene_name": "Pif1", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VQR3", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VQR3" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "Q9VQR3", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VQR3" } ] } ] }, { "uniprot_ac": "Q9VRI0", "gene_name": "Ddx56", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VRI0", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VRI0" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q9VRI0", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VRI0" } ] } ] }, { "uniprot_ac": "Q9VSE2", "gene_name": "mus301", "activity": [ { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VSE2", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VSE2" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "Q9VSE2", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VSE2" } ] } ] }, { "uniprot_ac": "Q9VUV9", "gene_name": "Brr2", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VUV9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VUV9" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q9VUV9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VUV9" } ] } ] }, { "uniprot_ac": "Q9VVK8", "gene_name": "ais", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VVK8", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VVK8" } ] } ] }, { "uniprot_ac": "Q9VX34", "gene_name": "cg5800", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VX34", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VX34" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q9VX34", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VX34" } ] } ] }, { "uniprot_ac": "Q9VY54", "gene_name": "Prp16", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VY54", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VY54" } ] } ] }, { "uniprot_ac": "Q9VYS3", "gene_name": "Upf1", "activity": [ { "ec_number": "3.6.4.13", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VYS3", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VYS3" } ] }, { "ec_number": "3.6.4.12", "activity": "ATP + H2O = ADP + H(+) + phosphate.", "evidence": [ { "id": "Q9VYS3", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VYS3" } ] }, { "ec_number": "3.6.4.13", "activity": "", "evidence": [ { "id": "Q9VYS3", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VYS3" } ] }, { "ec_number": "3.6.4.12", "activity": "", "evidence": [ { "id": "Q9VYS3", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VYS3" } 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