MCPH1 recognizes and binds diphosphorylated H2AFX, but the exact biological role of this interaction has not been elucidated (Singh et al. 2012).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O95677-1", "Q99502-1", "Q13315-1", "Q92993-1", "P49959-1", "O00167-1", "Q99504-1", "Q92878-1" ], "evidence": [ { "id": "R-HSA-5683967", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5683967" } ] }, { "id": "R-HSA-5683986", "name": "APBB1 and MAPK8 bind diphosphorylated H2AFX", "equation": "", "summary": "In the absence of sufficient EYA1-4 activity, APBB1 (FE65) binds diphosphorylated H2AFX and recruits MAPK8 (JNK1) to H2AFX. This triggers pro-apoptotic signaling and targets the affected cell for apoptosis instead of DNA repair (Cook et al. 2009).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q13315-1", "Q92993-1", "P49959-1", "P45983-1", "Q92878-1" ], "evidence": [ { "id": "R-HSA-5683986", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5683986" } ] }, { "id": "R-HSA-5684052", "name": "PIAS4 SUMOylates MDC1", "equation": "", "summary": "PIAS4 SUMOylates MDC1 at lysine residue K1840. The exact timing and regulation of this modification is not known (Luo et al. 2012, Yin et al. 2012).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P38398-1", "Q13315-1", "P46736-1", "P63279-1", "O96028-1", "Q92993-1", "O76064-1", "P49959-1", "Q8IYW5-1", "Q99728-1", "P61088-1", "Q92878-1", "O95714-1", "Q8N2W9-1" ], "evidence": [ { "id": "R-HSA-5684052", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5684052" } ] }, { "id": "R-HSA-5684071", "name": "RNF4 ubiquitinates MDC1", "equation": "", "summary": "SUMOylation of MDC1 by PIAS4 creates a docking site for RNF4, an E3 ubiquitin ligase. RNF4 binds to MDC1 specifically when SUMO2 is attached to lysine K1840 of MDC1. RNF4 polyubiquitinates MDC1 through ubiquitin lysine residue K48 cross-linking. RNF4-mediated ubiquitination targets MDC1 for degradation and causes dissociation of MDC1-bound proteins from DNA double-strand breaks (DSBs). While additional regulation steps may be involved, the activity of RNF4 is necessary for the initiation of resection of DNA ends at DSBs and progression of homologous recombination (Luo et al. 2012, Yin et al. 2012, Galanty et al. 2012).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P38398-1", "Q13315-1", "P46736-1", "O96028-1", "Q92993-1", "O76064-1", "P49959-1", "Q8IYW5-1", "P78317-1", "Q99728-1", "P61088-1", "Q92878-1", "O95714-1", "Q8N2W9-1" ], "evidence": [ { "id": "R-HSA-5684071", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5684071" } ] }, { "id": "R-HSA-5684081", "name": "MRN complex binds CDK2 and RBBP8", "equation": "", "summary": "In the S/G2 phase of the cell cycle, CDK2:CCNA (CDK2:cyclin A) complex and CtIP (RBBP8) are recruited to DNA double-strand breaks (DSBs) by the MRN complex. RBBP8 interacts with NBN (NBS1) and RAD50 subunits, while CDK2:CCNA interacts with the MRE11A subunit of the complex (Buis et al. 2012). RBBP8 functions as a homotetramer (Davies et al. 2015).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q13315-1", "Q92993-1", "P49959-1", "Q99708-1", "Q92878-1", "P24941-1" ], "evidence": [ { "id": "R-HSA-5684081", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5684081" } ] }, { "id": "R-HSA-5684096", "name": "CDK2 phosphorylates RBBP8", "equation": "", "summary": "CDK2, in complex with cyclin A (CCNA), phosphorylates RBBP8 (CtIP) on serine residue S327 and threonine residue T847. Residue T847 is conserved in the yeast ortholog of CtIP, Sae2, and phosphorylation of T847 increases CtIP activity in DNA end resection. Serine S327 phosphorylation enables CtIP to bind BRCA1 (Buis et al. 2012).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q13315-1", "Q92993-1", "P49959-1", "Q99708-1", "Q92878-1", "P24941-1" ], "evidence": [ { "id": "R-HSA-5684096", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5684096" } ] }, { "id": "R-HSA-5684108", "name": "BRCA1 binds phosphorylated RBBP8", "equation": "", "summary": "BRCA1:BARD1 complex binds RBBP8 (CtIP) phosphorylated by CDK2 at DNA double-strand breaks (DSBs), thus forming the so-called BRCA1-C complex. As active CDK2 in complex with CCNA (cyclin A) exists only in the S and G2 phases of the cell cycle, this limits the formation of BRCA1 complex with RBBP8 and the consequent initiation of homologous recombination to S and G2 phases, when the genome is duplicated and sister chromatids are available (Chen et al. 2008, Yun and Hiom 2009). Dissociation of the BRCA1-A complex is necessary for BRCA1 to be able to bind RBBP8 (Coleman and Greenberg 2011). Phosphorylation of BRCA1 by CHEK2 also contributes to the initiation of homologous recombination, with this phosphorylation similarly serving as a molecular clock (Parameswaran et al. 2015).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P38398-1", "Q13315-1", "Q92993-1", "P49959-1", "Q99728-1", "Q99708-1", "Q92878-1" ], "evidence": [ { "id": "R-HSA-5684108", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5684108" } ] }, { "id": "R-HSA-5684140", "name": "ATM phosphorylates RBBP8", "equation": "", "summary": "CDK2-mediated phosphorylation of RBBP8 (CtIP) triggers ATM-mediated phosphorylation of RBBP8 on several ATM consensus SQ/TQ sites. The ATM phosphorylation site at threonine residue T859 of RBBP8 is evolutionarily conserved and seems to be particularly important for the RBBP8-promoted resection of DNA double-strand break (DSB) ends (Wang et al. 2013).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q13315-1", "Q92993-1", "P49959-1", "Q99708-1", "Q92878-1" ], "evidence": [ { "id": "R-HSA-5684140", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5684140" } ] }, { "id": "R-HSA-5684875", "name": "Binding of ATR:ATRIP to RPA at resected DNA DSBs", "equation": "", "summary": "ATR (ATM- and rad3-related) kinase is an essential checkpoint factor in human cells constitutively associated with ATRIP (ATR-interacting protein). The ATR:ATRIP complex binds RPA complex (RPA1:RPA2:RPA3) associated with ssDNA at resected DNA double-strand breaks (DSBs). Complex formation is primarily mediated by physical interaction between ATRIP and RPA1 (Zou and Elledge 2003, Jazayeri et al. 2006).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P38398-1", "Q13315-1", "Q92993-1", "Q13535-1", "P54132-1", "P49959-1", "Q9UQ84-1", "Q13472-1", "Q99728-1", "Q99708-1", "Q9BX63-1", "Q92878-1" ], "evidence": [ { "id": "R-HSA-5684875", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5684875" } ] }, { "id": "R-HSA-5684882", "name": "CHEK1 is recruited to resected DNA DSBs", "equation": "", "summary": "The recruitment of CHEK1 (CHK1) to resected DNA double-strand breaks (DSBs) and activation by ATR-mediated phosphorylation requires the presence of CLSPN (claspin) and TIMELESS:TIPIN protein complex. TIPIN simultaneously interacts with the RPA2 subunit of the RPA complex and CLSPN, allowing CLSPN to stably associate with resected DNA DSBs (Kemp et al. 2010). Phosphorylation of CLSPN at threonine T916 and serine S945 is needed for CHEK1 binding (Kumagai et al. 2003, Clarke and Clarke 2005). CLSPN phosphorylation at these sites is independent of CHEK1 (Bennett et al. 2008). Casein kinase 1 (CK1) was proposed as a kinase responsible for CLSPN phosphorylation (Meng et al. 2011) but the exact mechanism of this modification has not been established.
ATR-mediated phosphorylation of RAD17 on serine residues S635 and S645 is implicated in CLSPN recruitment to resected DNA DSBs and CLSPN phosphorylation (Wang et al. 2006). Also, phosphorylation of the RPA2 subunit of the RPA complex positively contributes to CHEK1 activation (Liu et al. 2012).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P38398-1", "Q13315-1", "O14757-1", "Q92993-1", "Q13535-1", "P54132-1", "P49959-1", "Q9UQ84-1", "Q13472-1", "Q99728-1", "Q99708-1", "Q9BX63-1", "Q92878-1", "Q99638-1" ], "evidence": [ { "id": "R-HSA-5684882", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5684882" } ] }, { "id": "R-HSA-5684887", "name": "Activation of CHEK1 at resected DNA DSBs", "equation": "", "summary": "CHEK1 (Chk1) is a checkpoint kinase activated during genotoxic stress. CHEK1 activation at resected DNA double-strand breaks (DSBs) involves ATR-mediated phosphorylation of CHEK1 serine residues S317 and S345 in the presence of claspin (CLSPN), TOPBP1, RAD17:RFC complex, RAD9:HUS1:RAD1 complex, TIMELESS:TIPIN complex, RPA complex and RHNO1 (Liu et al. 2000, Zhao and Piwnica-Worms 2001, Kumagai and Dunphy 2003, Sorensen et al. 2004, Wang et al. 2006, Kemp et al. 2010, Cotta-Ramusino et al. 2011, Liu et al. 2012). Following phosphorylation, CHEK1 dissociates from chromatin and phosphorylates target proteins involved in S/G2 checkpoint activation and/or homologous recombination repair (Smits et al. 2006). CLSPN needs to interact with chromatin only transiently in order to facilitate CHEK1 activation (Lee et al. 2005).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [ "R-HSA-176296" ], "enzyme_list": [ "P38398-1", "Q13315-1", "O14757-1", "Q92993-1", "Q13535-1", "P54132-1", "P49959-1", "Q9UQ84-1", "Q13472-1", "Q99728-1", "Q99708-1", "Q9BX63-1", "Q92878-1", "Q99638-1" ], "evidence": [ { "id": "R-HSA-5684887", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5684887" } ] }, { "id": "R-HSA-5685011", "name": "ATR activation at DNA DSBs", "equation": "", "summary": "ATR:ATRIP complex is recruited to resected DNA double-strand breaks (DSBs) via interaction with the RPA complex that coats single strand DNA (ssDNA) 3'-overhangs, but this is not sufficient for ATR to become catalytically active. ATR kinase activity requires the presence of the RAD17:RFC complex, RAD9:HUS1:RAD1 (9-1-1) complex and TOPBP1. RAD17:RFC loads RAD9:HUS1:RAD1 onto junctions of single strand and double-strand DNA (ssDNA-dsDNA junctions), present at resected DNA DSBs (Bermudez et al. 2003, reviewed by Sancar et al. 2004). TOPBP1 binds the C-terminal tail of RAD9, and is thus brought in the proximity of ATR, where it can activate it (Kumagai et al. 2006, Delacroix et al. 2007). The interaction of TOPBP1 and RBBP8 (CtIP) also contributes to TOPBP1 loading (Ramirez-Lugo et al. 2011). Phosphorylation of ATR at threonine residue T1989 may create a binding site for the BRCT domains of TOPBP1 (Liu et al. 2011). It is not clear whether T1989 of ATR is phosphorylated through autophosphorylation (Liu et al. 2011), as it does not conform to the SQ/TQ consensus, or by another kinase (Liu et al. 2013). RHNO1 (RHINO) protein simultaneously binds RAD9:HUS1:RAD1 complex and TOPBP1 and is required for the full catalytic activation of ATR (Cotta-Ramusino et al. 2011).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P38398-1", "Q13315-1", "Q92993-1", "Q13535-1", "P54132-1", "P49959-1", "Q9UQ84-1", "Q13472-1", "Q99728-1", "Q99708-1", "Q9BX63-1", "Q92878-1", "Q99638-1" ], "evidence": [ { "id": "R-HSA-5685011", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5685011" } ] }, { "id": "R-HSA-5685156", "name": "ATR phosphorylates RPA2", "equation": "", "summary": "Activated ATR phosphorylates the RPA2 subunit of the RPA complex on serine residue S33. Phosphorylation of RPA2 at S33 likely stimulates additional RPA2 phosphorylation on CDK sites (S23 and S29) and DNA-PKcs (PRKDC) sites (S4, S8 and S21). DNA damage-regulated phosphorylation of RPA2 plays an important role in the progression of homologous recombination-directed repair of DNA double-strand breaks (DSBs) (Anantha et al. 2007, Liu et al. 2012, Murphy et al. 2014)", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P38398-1", "Q13315-1", "Q92993-1", "Q13535-1", "P54132-1", "P49959-1", "Q9UQ84-1", "Q13472-1", "Q99728-1", "Q99708-1", "Q9BX63-1", "Q92878-1", "Q99638-1" ], "evidence": [ { "id": "R-HSA-5685156", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5685156" } ] }, { "id": "R-HSA-5685341", "name": "BCDX2 complex stabilizes RAD51 filament", "equation": "", "summary": "The BCDX2 complex, composed of RAD51 paralogs RAD51B, RAD51C, RAD51D and XRCC2, preferentially binds at the ends of 3' overhanging ssDNA created by resection of DNA double-strand breaks (DSBs). The BCDX2 complex stabilizes nucleoprotein filaments formed by BRCA2-mediated RAD51 loading onto ssDNA (Masson et al. 2001, Chun et al. 2013). The BCDX2 complex may act by inhibiting displacement of RAD51 by BLM helicase (Amunugama et al. 2013).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P38398-1", "Q13315-1", "Q92993-1", "Q06609-1", "P54132-1", "P49959-1", "Q9UQ84-1", "Q13472-1", "Q99728-1", "Q99708-1", "Q9BX63-1", "Q92878-1" ], "evidence": [ { "id": "R-HSA-5685341", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5685341" } ] }, { "id": "R-HSA-5685838", "name": "CX3 complex binds D-loop structures", "equation": "", "summary": "The CX3 complex, composed of RAD51 paralogs RAD51C and XRCC3 (Masson, Tarsounas et al. 2001), binds homologous recombination repair sites at a later time point than the BCDX2 complex (Chun et al. 2013). Both RAD51C and XRCC3 can directly interact with PALB2 (Park et al. 2014). CX3 complexes, as well as BCDX2 complexes, multimerize into ring like structures with a central cavity (Masson, Stasiak et al. 2001, Compton et al. 2010). The CX3 complex may be involved in the resolution of Holliday junctions (Liu et al. 2004, Liu et al. 2007).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P38398-1", "Q13315-1", "Q92993-1", "Q06609-1", "P54132-1", "P49959-1", "Q9UQ84-1", "Q13472-1", "Q99728-1", "Q99708-1", "Q9BX63-1", "Q92878-1" ], "evidence": [ { "id": "R-HSA-5685838", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5685838" } ] }, { "id": "R-HSA-5685985", "name": "EXO1 or DNA2 in complex with BLM or WRN binds initially resected DNA DSBs along with BRIP1 recruitment", "equation": "", "summary": "After the initial resection of DNA double-strand breaks (DSBs) by MRE11A and RBBP8 (CtIP), which creates short 3' ssDNA overhangs, a DNA exonuclease EXO1 or a DNA endonuclease DNA2 is recruited to perform long-range resection of DNA DSBs. The redundant function of EXO1 and DNA2 in resection of DNA DSBs is conserved in yeast (Zhu et al. 2008). BLM, the Bloom syndrome helicase, acts as an activator of DNA2 catalytic activity (Nimonkar et al. 2011) and increases affinity of EXO1 for DNA ends (Nimonkar et al. 2008). BLM directly interacts with the MRN complex, which can assist recruitment of either DNA2 or EXO1 to DNA DSBs (Nimonkar et al. 2011). EXO1 can also be recruited to DNA DSBs through its interaction with RBBP8 (CtIP) (Eid et al. 2010, Nimonkar et al. 2011). Another DNA helicase, WRN (Werner syndrome helicase) can function redundantly with BLM to facilitate/activate EXO1- or DNA2-mediated long range resection of DNA DSBs (Sturzenegger et al. 2014).
A DNA helicase BRIP1 (also known as BACH1 or FANCJ) is recruited to DNA DSBs through its interaction with BRCA1 (Cantor et al. 2001) and BLM (Suhasini et al. 2011, Suhasini and Brosh 2012). BRIP1 promotes DNA end processing events that stimulate recruitment of the RPA complex and RAD51 (Xie et al. 2012). The interaction with BRCA1 requires BRIP1 to be phosphorylated on serine residue S990 in a cell cycle-dependent manner (Yu et al. 2003). BRIP1 also has to be acetylated on lysine residue K1249 to be functional (Xie et al. 2012).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P38398-1", "Q13315-1", "Q92993-1", "P54132-1", "P49959-1", "Q9UQ84-1", "Q13472-1", "Q99728-1", "Q99708-1", "Q9BX63-1", "Q92878-1" ], "evidence": [ { "id": "R-HSA-5685985", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5685985" } ] }, { "id": "R-HSA-5685994", "name": "Long-range resection of DNA DSBs by EXO1 or DNA2", "equation": "", "summary": "DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). Both DNA nucleases act after short 3' ssDNA overhangs are created by the initial resection of DNA DSBs mediated by MRE11A and RBBP8 (CtIP). The roles of BLM (Bloom syndrome helicase) and WRN (Werner syndrome helicase) in facilitation of EXO1- or DNA2-mediated resection of DNA DSBs are also redundant.
EXO1 possesses an intrinsic 5'->3' exonuclease activity. The ATPase activity of BLM DNA helicase is not required for EXO1 catalytic activity, but BLM increases the affinity of EXO1 for DNA ends (Nimonkar et al. 2008). WRN can also positively affect EXO1 exonuclease activity, although the mechanism is not clear (Sturzenegger et al. 2014).
The DNA endonuclease DNA2 has to form a complex with either BLM (Nimonkar et al. 2011) or WRN (Sturzenegger et al. 2014) in order to perform a 5'->3' directed resection of DNA DSBs. BLM forms an evolutionarily conserved complex with TOP3A, RMI1 and RMI2, known as the STR complex in yeast (Zhu et al. 2008) and the BTB or BTRR complex in humans. The entire BTRR complex participates in the activation of DNA2-mediated resection of DNA DSBs (Sturzenegger et al. 2014).
While ATR signaling may be detectable in the absence of long-range resection of DNA DSBs by EXO1 or DNA2 (Eid et al. 2010), EXO1 or DNA2 activity may be necessary to achieve biologically meaningful level of ATR activation (Gravel et al. 2008).
BRIP1 (BACH1, FANCJ) is a DNA helicase recruited to DNA DSBs by interaction with BRCA1 (Cantor et al. 2001) and BLM (Suhasini et al. 2011). BRIP1 is necessary for BRCA1-mediated homology-directed repair of DNA DSBs, and BRIP1 loss-of-function mutations are found in familial breast cancer (Cantor et al. 2001, Litman et al. 2005). The exact role of BRIP1 in DNA repair is not completely clear. BRIP1 is needed for the successful formation of RPA foci and, subsequently, RAD51 foci (Xie et al. 2012). The available evidence suggest that it cooperates with BLM in unwinding of DNA DSBs during resection (Suhasini et al. 2011, Sarkies et al. 2012), and may be especially important for unwinding of DNA that contains oxidative damage (Suhasini et al. 2009).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P38398-1", "Q13315-1", "Q92993-1", "P54132-1", "P49959-1", "Q9UQ84-1", "Q13472-1", "Q99728-1", "Q99708-1", "Q9BX63-1", "Q92878-1" ], "evidence": [ { "id": "R-HSA-5685994", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5685994" } ] }, { "id": "R-HSA-5686410", "name": "BLM mediates dissolution of double Holliday junction", "equation": "", "summary": "The BTRR complex, composed of BLM, TOP3A, RMI1 and RMI2, dissolves double Holliday junctions by disentangling hemicatenane intermediates (Bocquet et al. 2014). This results in non-crossover products, where no exchange of genetic material happens between the sister chromatid that served as a template for the DNA repair synthesis and the repaired DNA duplex. SPIDR serves as a scaffold that connects the BTRR complex with the double Holliday junction through its simultaneous interaction with RAD51-coated DNA strands of the Holliday junction and BLM. SPIDR is needed for BTRR-mediated prevention of cross-over between sister chromatids (Wan et al. 2013). The complex of FIGNL1 and FIRRM is recruited to DNA damage foci through interaction of FIGNL1 with RAD51 (Yan and Chen 2013, Fernandes et al. 2018) and SPIDR (Yuan and Chen 2013). FIGNL1 and FIRRM inhibit formation of cross-overs during repair of DNA double strand breaks, which is consistent with the role of SPIDR (Fernandes et al. 2013).", "cellular_location": "chromosome, nucleoplasm", "input_participant_list": [], "output_participant_list": [ "R-HSA-5693527", "R-ALL-1638790", "R-HSA-3321979", "R-HSA-419548", "R-HSA-5649637", "R-HSA-5685301", "R-HSA-5687710" ], "enzyme_list": [ "Q6PIW4-1", "P38398-1", "Q13315-1", "Q92993-1", "Q06609-1", "P54132-1", "P49959-1", "Q9UQ84-1", "Q13472-1", "Q99728-1", "Q99708-1", "Q9BX63-1", "Q92878-1" ], "evidence": [ { "id": "R-HSA-5686410", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5686410" } ] }, { "id": "R-HSA-5686440", "name": "MUS81:EME1,EME2 cleaves D-loop", "equation": "", "summary": "The complex of MUS81 and EME1 or EME2 acts as an endonuclease and processes D-loops by cleaving the sister chromatid strand complementary to the invading strand at the junction point. MUS81:EME2 complex has a higher catalytic activity than MUS81:EME1 complex and, in vitro, cleaves D-loops at several other sites in addition to the junction point (Osman et al. 2003, Pepe and West 2014). The yeast Mus81:Eme1 (Mus81:Mms4) complex also acts on D-loops (Schwartz et al. 2012).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P38398-1", "Q13315-1", "Q92993-1", "Q06609-1", "P54132-1", "P49959-1", "Q9UQ84-1", "Q13472-1", "Q96NY9-1", "Q99728-1", "Q99708-1", "Q9BX63-1", "Q92878-1" ], "evidence": [ { "id": "R-HSA-5686440", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5686440" } ] }, { "id": "R-HSA-5686469", "name": "Resolution of D-loops cleaved by MUS81:EME1 or MUS81:EME2", "equation": "", "summary": "Based on studies in yeast, D-loop cleavage by MUS81 in complex with EME1 or EME2 always produces crossovers between sister chromatids (Osman et al. 2003). The identity of the DNA polymerase(s) and ligase(s) that complete DNA repair synthesis and ligation after MUS81:EME1 or MUS81:EME2 cleavage of D-loops has not been determined.", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P38398-1", "Q13315-1", "Q92993-1", "Q06609-1", "P54132-1", "P49959-1", "Q9UQ84-1", "Q13472-1", "Q99728-1", "Q99708-1", "Q9BX63-1", "Q92878-1" ], "evidence": [ { "id": "R-HSA-5686469", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5686469" } ] }, { "id": "R-HSA-5686483", "name": "Resolution of Holliday junctions cleaved by GEN1 or SLX1A:SLX4:MUS81:EME1,(MUS81:EME2)", "equation": "", "summary": "The identity of DNA ligases that ligate DNA strands generated during cleavage of Holliday junctions by GEN1 or the SLX-MUS complex (composed of SLX1A:SLX4 heterodimer and MUS81:EME1 or possibly MUS81:EME2 heterodimer) is not known. The resolvase activity of GEN1 or SLX-MUS predominantly results in the generation of crossover products, with exchange of genetic material between sister chromatids (Wyatt et al. 2013).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P38398-1", "Q13315-1", "Q92993-1", "Q06609-1", "P54132-1", "P49959-1", "Q9UQ84-1", "Q13472-1", "Q99728-1", "Q99708-1", "Q9BX63-1", "Q92878-1" ], "evidence": [ { "id": "R-HSA-5686483", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5686483" } ] }, { "id": "R-HSA-5686578", "name": "Activated ATM phosphorylates ABL1", "equation": "", "summary": "ATM, activated in response to DNA damage in the form of double-strand breaks, phosphorylates ABL1 (c-ABL) on serine residue S456, resulting in the activation of kinase activity of ABL1 (Baskaran et al. 1997).", "cellular_location": "nucleoplasm", "input_participant_list": [ "R-HSA-5686579" ], "output_participant_list": [ "R-HSA-5686576" ], "enzyme_list": [ "P00519-1", "Q13315-1" ], "evidence": [ { "id": "R-HSA-5686578", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5686578" } ] }, { "id": "R-HSA-5686642", "name": "RAD52 promotes single strand annealing at resected DNA DSBs", "equation": "", "summary": "RAD52 promotes annealing of 3' ssDNA overhangs at resected DNA double-strand breaks (DSBs) through complementary regions. The complementarity between the two 3' ssDNA overhangs at resected DNA DSBs exists if 3' ssDNA overhangs contain direct repeats. While single strand annealing (SSA) requires significant homology between the annealed sequences it is nonetheless mutagenic. The parts of two 3' overhanging DNA single strands at resected DSBs that lie 3' to the annealed regions become displaced as flaps and subsequently excised. This results in the deletion (loss) of the DNA sequence lying between the two regions of homology used for SSA, as well as the deletion of one of the repeats used for annealing (Parsons et al. 2000, Van Dyck et al. 2001, Singleton et al. 2002, Stark et al. 2004, Mansour et al. 2008).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P38398-1", "Q13315-1", "Q92993-1", "Q06609-1", "Q13535-1", "P54132-1", "P49959-1", "Q9UQ84-1", "Q13472-1", "Q99728-1", "Q99708-1", "Q9BX63-1", "Q92878-1", "Q99638-1" ], "evidence": [ { "id": "R-HSA-5686642", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5686642" } ] }, { "id": "R-HSA-5686657", "name": "ERCC1:XPF cleaves flaps generated by SSA", "equation": "", "summary": "The endonuclease complex ERCC1:XPF (ERCC1:ERCC4) is recruited to single strand annealing (SSA) sites of DNA double-strand break (DSB) repair through direct interaction between XPF (ERCC4) and RAD52 (Motycka et al. 2004). ERCC1:XPF cleaves the ssDNA flaps generated by displacement of non-complementary 3' parts of 3' ssDNA overhangs during RAD52-mediated annealing. The enzymatic activity of ERCC1:XPF is necessary for the completion of SSA (Motycka et al. 2004, Al-Minawi et al. 2008, Ahmad et al. 2008).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q92889-1", "P38398-1", "Q13315-1", "Q92993-1", "Q06609-1", "Q13535-1", "P54132-1", "P49959-1", "Q9UQ84-1", "Q13472-1", "Q99728-1", "Q99708-1", "Q9BX63-1", "Q92878-1", "Q99638-1" ], "evidence": [ { "id": "R-HSA-5686657", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5686657" } ] }, { "id": "R-HSA-5686663", "name": "Completion of SSA", "equation": "", "summary": "A DNA ligase, most likely LIG1 (DNA ligase I), ligates single strand breaks (SSBs) remaining after RAD52-mediated single strand annealing (SSA) of resected DNA double-strand breaks (DSBs) and cleavage of displaced flaps by ERCC1:XPF (ERCC1:ERCC4). LIG4 is not involved in SSA (Maruta et al. 2024), and the activity of LIG3 is inhibited in the presence of RAD51 (Batenburg et al. 2023). Therefore, the only remaining candidate DNA ligase is LIG1. While LIG1 does not require RPA to bind to single-strand breaks in DNA, the RPA complex, which coats long reseced ends created during SSA and homologous recombination repair (HRR), greatly stimulates the catalytic activity of LIG1 (Ranalli et al. 2002). The product of SSA is a double-strand DNA with a deletion of one complementary region (repeat) and the sequence lying between the two complementary regions used for SSA (inter-SSA deletion) (reviewed by Ciccia and Elledge 2010).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q92889-1", "P38398-1", "Q13315-1", "Q92993-1", "Q06609-1", "Q13535-1", "P54132-1", "P49959-1", "Q9UQ84-1", "Q13472-1", "P18858-1", "Q99728-1", "Q99708-1", "Q9BX63-1", "Q92878-1", "Q99638-1" ], "evidence": [ { "id": "R-HSA-5686663", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5686663" } ] }, { "id": "R-HSA-5686685", "name": "RIF1 and PAX1IP bind TP53BP1 at DNA DSBs", "equation": "", "summary": "RIF1 binds TP53BP1 phosphorylated by ATM at DNA double strand breaks (DSBs). RIF1 binding interferes with the accumulation of BRCA1:BARD1 heterodimers and associated proteins at DNA DSBs. Therefore, TP53BP1-mediated recruitment of RIF1 prevents RBBP8 (CtIP) binding to BRCA1:BARD1 and the subsequent resection of DNA DSBs. The action of RIF1 and TP53BP1 promotes non-homologous end joining (NHEJ) of DNA DSBs during G1 phase of the cell cycle, when sister chromatids are not available for homologous recombination-mediated repair (Zimmermann et al. 2013, Escribano-Diaz et al. 2013).
Similar to RIF1, PAX1IP (PTIP) is also recruited to DNA DSBs through interaction with ATM-phosphorylated TP53BP1. Since RIF1 and PAX1IP interact with different phosphorylated sites on TP53BP1, they can simultaneously bind TP53BP1 and colocalize in the majority of TP53BP1 foci. PAX1IP contributes to inhibition of DNA DSB resection mediated by BRCA1-recruited RBBP8 (CtIP) (Callen et al. 2013).", "cellular_location": "nucleoplasm", "input_participant_list": [ "R-HSA-480742", "R-HSA-5619395" ], "output_participant_list": [ "R-HSA-5682574", "R-HSA-5682575", "R-HSA-5682577", "R-HSA-5682579", "R-HSA-5682582" ], "enzyme_list": [ "P38398-1", "Q13315-1", "P46736-1", "O96028-1", "Q92993-1", "O76064-1", "P49959-1", "Q8IYW5-1", "Q99728-1", "P61088-1", "Q92878-1", "O95714-1", "Q8N2W9-1" ], "evidence": [ { "id": "R-HSA-5686685", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5686685" } ] }, { "id": "R-HSA-5686704", "name": "Activated ATM phosphorylates DCLRE1C", "equation": "", "summary": "Activated ATM phosphorylates DCLRE1C (ARTEMIS) at serine residue S645. S645 phosphorylation is necessary for the function of DCLRE1C in non-homologous end joining (NHEJ) (Riballo et al. 2004, Poinsignon et al. 2004, Chen et al. 2005).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [ "R-HSA-5686708" ], "enzyme_list": [ "Q96SD1-1", "Q13315-1", "O96028-1", "Q92993-1", "O76064-1", "P49959-1", "Q8IYW5-1", "P61088-1", "Q92878-1", "O95714-1", "Q8N2W9-1" ], "evidence": [ { "id": "R-HSA-5686704", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5686704" } ] }, { "id": "R-HSA-5686900", "name": "TP53BP1 recruits DCLRE1C to ATM", "equation": "", "summary": "TP53BP1 is required for the recruitment of DCLRE1C (ARTEMIS) to DNA double strand breaks (DSBs) and ATM-mediated phosphorylation of DCLRE1C (Riballo et al. 2004). DCRLE1C directly interacts with the TP53BP1-binding protein PAX1IP (PTIP) (Wang et al. 2014).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q96SD1-1", "Q13315-1", "O96028-1", "Q92993-1", "O76064-1", "P49959-1", "Q8IYW5-1", "P61088-1", "Q92878-1", "O95714-1", "Q8N2W9-1" ], "evidence": [ { "id": "R-HSA-5686900", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5686900" } ] }, { "id": "R-HSA-5693536", "name": "ATM phosphorylates MDC1", "equation": "", "summary": "The function of MDC1 in recruiting and retaining DNA repair proteins at the sites of DNA damage (Xu and Stern 2003, Stewart et al. 2003) is promoted by the ATM-mediated phosphorylation of MDC1 (Liu et al. 2012). Phosphorylation of MDC1 (NFBD1) by ATM at threonine residue T4 stabilizes otherwise unstable MDC1 homodimers by enabling in trans interaction of MDC1 FHA domains with phosphorylated N-terminal threonine residues (Goldberg et al. 2003, Liu et al. 2012). ATM also phosphorylates MDC1 on at least four threonine residues that match the consensus RNF8-binding sequence T-Q-X-F: T699, T719, T752, T765 (Kolas et al. 2007). Binding of the ubiquitin ligase RNF8 to ATM phosphorylated MDC1 is necessary for the recruitment of TP53BP1 and BRCA1 to DNA double-strand break (DSB) sites.", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q13315-1", "Q92993-1", "P49959-1", "Q92878-1" ], "evidence": [ { "id": "R-HSA-5693536", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5693536" } ] }, { "id": "R-HSA-5693539", "name": "Ligation of DNA and formation of Holliday structures following repair synthesis", "equation": "", "summary": "Ligation of the crossed-strand intermediate results in the formation of double Holliday junctions with two crossovers. In humans, the identity of the ligase activity involved in this process is not known (reviewed by Ciccia and Elledge 2010).", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P38398-1", "Q13315-1", "Q92993-1", "Q06609-1", "P54132-1", "P49959-1", "Q9UQ84-1", "Q13472-1", "Q99728-1", "Q99708-1", "Q9BX63-1", "Q92878-1" ], "evidence": [ { "id": "R-HSA-5693539", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5693539" } ] }, { "id": "R-HSA-5693540", "name": "MRN activates ATM", "equation": "", "summary": "MRN promotes dissociation of ATM dimers to ATM monomers which is accompanied by ATM trans-autophosphorylation on serine residue S1981 (Bakkenist et al. 2003, Du et al. 2014). ATM autophosphorylation at serine residues S367 and S1893 is also implicated in ATM activation (Kozlov et al. 2006). Dissociation of ATM dimers requires the ATP-dependent DNA-helicase activity of the MRN subunit RAD50 (Lee and Paull 2005). KAT5 (Tip60)-mediated acetylation of ATM dimers at lysine K3016 is a prerequisite for ATM kinase activity (Sun et al. 2007). Upon the dissociation of ATM dimers induced by DNA double-strand breaks (DSBs), a fraction of activated ATM is retained at DSB sites, co-localizing with the MRN complex (Andegeko et al. 2001, Uziel et al. 2003) at ionizing radiation-induced foci (IRIF). MRN facilitates the binding of a portion of ATM substrates to ATM (Lee and Paull 2004).
After DSBs are repaired, ATM is dephosphorylated by an unidentified PP2A phosphatase complex, leading to dimer reformation (Goodarzi et al. 2004).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13315-1",
"Q92993-1",
"P49959-1",
"Q92878-1"
],
"evidence": [
{
"id": "R-HSA-5693540",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5693540"
}
]
},
{
"id": "R-HSA-5693542",
"name": "Association of RPA complexes with ssDNA at resected DNA DSBs",
"equation": "",
"summary": "Human replication protein A (RPA) is a single-stranded DNA (ssDNA) binding protein complex required for DNA replication, recombination, and repair. RPA is a stable heterotrimer consisting of subunits with molecular masses of 14, 32 and 70 kDa (p14, p32 and p70, respectively). Association of RPA with ssDNA is thought to contribute to both the protection and removal of secondary structure from single-stranded DNA (ssDNA) (McIlwraith et al. 2000). The RPA complexes coat 3'-ssDNA overhangs generated by RBBP8 (CtIP)-initiated long-range resection of DNA double-strand breaks (DSBs) (Sartori et al. 2007, Chen et al. 2008).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P38398-1",
"Q13315-1",
"Q92993-1",
"P54132-1",
"P49959-1",
"Q9UQ84-1",
"Q13472-1",
"Q99728-1",
"Q99708-1",
"Q9BX63-1",
"Q92878-1"
],
"evidence": [
{
"id": "R-HSA-5693542",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5693542"
}
]
},
{
"id": "R-HSA-5693549",
"name": "ATM phosphorylates histone H2AFX on S139 at DNA DSBs",
"equation": "",
"summary": "ATM phosphorylates histone H2AFX (H2AX) on serine S139 within 1-3 minutes of double-strand break (DSB) formation, producing gamma-H2AX (gamma-H2AFX) (Rogakou et al.1998, Burma et al. 2001). Basal phosphorylation of H2AFX on tyrosine residue Y142 contributes to successful S139 phosphorylation and results in a transient diphosphorylated H2AFX (Cook et al. 2009). Gamma-H2AFX localizes to a region of about 2 Mbp surrounding the site of the DSB (Rogakou et al.1998), playing an essential role in the stable recruitment of other repair proteins and formation of ionizing radiation-induced foci (IRIF) at DSB sites (Paull et al. 2000, Celeste et al. 2002, Celeste et al. 2003, Stewart et al., 2003). Recruitment of MDC1 to gamma-H2AFX may be important for the sustained phosphorylation of H2AFX at DSBs (Stewart et al. 2003).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13315-1",
"Q92993-1",
"P49959-1",
"Q92878-1"
],
"evidence": [
{
"id": "R-HSA-5693549",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5693549"
}
]
},
{
"id": "R-HSA-5693551",
"name": "Phosphorylation of BRCA1-A complex at multiple sites by ATM",
"equation": "",
"summary": "ATM phosphorylates BRCA1 at serine residues S1387, S1423, S1457, and S1524 (Cortez et al. 1999, Gatei et al. 2000). At least a fraction of these sites and some additional BRCA1 SQ/TQ sites can also be phosphorylated by ATR (Tibbetts et al. 2000). ATM also phosphorylates BARD1, the heterodimerization partner of BRCA1, at threonine residues T714 and T734 (Kim et al. 2006).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P38398-1",
"Q13315-1",
"P46736-1",
"O96028-1",
"Q92993-1",
"O76064-1",
"P49959-1",
"Q8IYW5-1",
"Q99728-1",
"P61088-1",
"Q92878-1",
"O95714-1",
"Q8N2W9-1"
],
"evidence": [
{
"id": "R-HSA-5693551",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5693551"
}
]
},
{
"id": "R-HSA-5693561",
"name": "RAD51 binds BRCA2 at resected DNA DSBs",
"equation": "",
"summary": "BRCA2 and RAD51 interact directly through the highly conserved BRC repeats in BRCA2 (Venkitaraman 2002). CHEK1-mediated phosphorylation of BRCA2 (at threonine residue T3387) and RAD51 (at threonine residue T309) modulates their binding (Sorensen et al. 2005, Bahassi et al. 2008). One BRCA2 can bind up to six RAD51 molecules, thus playing an important role in RAD51 nucleation at the dsDNA-ssDNA junction created by resection of DNA double-strand breaks (DSBs) (Liu et al. 2010, Thorslund et al. 2010, Jensen et al. 2010). After the nucleation step, additional RAD51 molecules bind the ssDNA and multimerize, forming RAD51 nucleoprotein filaments (Yang et al. 2005). BRCA2-mediated RAD51 loading displaces the RPA complex from 3' overhanging ssDNA at DSBs (Liu et al. 2010, Jensen et al. 2010), possibly with other RPA-bound proteins, such as ATR:ATRIP and complexes involved in ATR catalytic activation.
BRCA2-binding partner SEM1 (DSS1) directly facilitates RPA release from ssDNA and its replacement with RAD51 (Zhao et al. 2015).
The interaction with DNA is critical for BRCA2 function, and the protein contains two different DNA binding regions. The amino-terminal DNA-binding domain (NTD) (residue 267-350) consists of a zinc finger-poly(adenosine diphosphate-ribose) polymerase (PARP)-like domain and binds to different DNA structures (ssDNA, dsDNA, tailed DNA, and gapped DNA) with similar affinity (von Nicolai et al. 2016). The carboxy-terminal DNA-binding domain CTD (residue 2,474-3,190) is significantly more complex with three OB-folds and an apical 3 bundle helix on top of a tower domain preceded by a helical domain (Yang et al. 2002). The proposed breast and ovarian cancer cluster regions (BCCR and OCCR) overlap with the CTD (Rebbeck et al. 2015, Gayther et al. 1997). Several common pathogenic mutations (ClinVar database) and loss-of-function mutations are found in this region including K2630A, K2630D, D2723H.",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-5684878",
"R-HSA-5684880"
],
"enzyme_list": [
"P38398-1",
"Q13315-1",
"Q92993-1",
"Q06609-1",
"Q13535-1",
"P54132-1",
"P49959-1",
"Q9UQ84-1",
"Q13472-1",
"Q99728-1",
"Q99708-1",
"Q9BX63-1",
"Q92878-1",
"Q99638-1"
],
"evidence": [
{
"id": "R-HSA-5693561",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5693561"
}
]
},
{
"id": "R-HSA-5693564",
"name": "Association of RAD51 with RAD52:DNA double-strand break ends",
"equation": "",
"summary": "RAD52 can simultaneously interact with RAD51 and RPA. The interaction with RAD51 may inhibit the formation of the invading RAD51 filament by sequestering RAD51 from RPA, thus promoting single strand annealing (SSA) instead of homologous recombination (Chen et al. 1999, Stark et al. 2004, Singleton et al. 2002, Mansour et al. 2008). The interaction of RAD51 and RAD52 is promoted by ABL1-mediated phosphorylation of both RAD51 and RAD52 (Chen et al. 1999, Van Dyck et al. 1999), which also increases RAD52 affinity for DNA (Honda et al. 2011).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P38398-1",
"Q13315-1",
"Q92993-1",
"Q06609-1",
"Q13535-1",
"P54132-1",
"P49959-1",
"Q9UQ84-1",
"Q13472-1",
"Q99728-1",
"Q99708-1",
"Q9BX63-1",
"Q92878-1",
"Q99638-1"
],
"evidence": [
{
"id": "R-HSA-5693564",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5693564"
}
]
},
{
"id": "R-HSA-5693566",
"name": "TP53BP1 associates with H4K20Me2 at DNA DSBs",
"equation": "",
"summary": "RNF8- and RNF168-mediated removal of KDM4A and KDM4B from H4K20Me2 (Me2-K21-HIST1H4A) enables TP53BP1 (53BP1) recruitment to WHSC1-methylated histone H4K20Me2 at DNA double-strand breaks (DSBs) (Pei et al. 2011, Mallette et al. 2012)",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13315-1",
"O96028-1",
"Q92993-1",
"O76064-1",
"P49959-1",
"Q8IYW5-1",
"P61088-1",
"Q92878-1",
"O95714-1",
"Q8N2W9-1"
],
"evidence": [
{
"id": "R-HSA-5693566",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5693566"
}
]
},
{
"id": "R-HSA-5693580",
"name": "Association of RAD52 with the RPA complex at resected DNA DSBs",
"equation": "",
"summary": "RAD52 heptamers bind 3' overhanging ssDNA at resected DNA double-strand breaks (DSBs) by simultaneously interacting with the DNA and the RPA complex. The conformation of the RAD52-ssDNA complex is thought to place the ssDNA on an exposed surface of the ring, in a configuration that may promote the DNA-DNA annealing of complementary DNA strands (Parsons et al. 2000). The interaction with RPA is necessary for RAD52-mediated homology driven repair (Park et al. 1996, Jackson et al. 2002). Phosphorylation of RAD52 at tyrosine residue Y104 by ABL1 in response to ATM signaling increases the affinity of RAD52 for DNA (Kitao et al. 2002, Cramer et al. 2008, Honda et al. 2011). Long range resection, which results in the activation of ATR/CHEK1 signaling, is needed for RAD52-mediated single strand annealing (SSA). RAD52 function may be promoted by a direct interaction with WRN helicase which participates in long-range resection of DNA DSBs (Baynton et al. 2003).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P38398-1",
"Q13315-1",
"Q92993-1",
"Q13535-1",
"P54132-1",
"P49959-1",
"Q9UQ84-1",
"Q13472-1",
"Q99728-1",
"Q99708-1",
"Q9BX63-1",
"Q92878-1",
"Q99638-1"
],
"evidence": [
{
"id": "R-HSA-5693580",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5693580"
}
]
},
{
"id": "R-HSA-5693583",
"name": "MDC1 associates with gamma-H2AFX at nuclear foci",
"equation": "",
"summary": "Recruitment of MDC1 to nuclear foci (IRIF - ionizing radiation induced foci) is mediated by phosphorylated H2AFX (gamma-H2AX, gamma-H2AFX). Once bound, MDC1 promotes sustained phosphorylation of H2AFX by enhancing the interaction between ATM and H2AFX. The BRCT domain of MDC1 binds gamma-H2AFX, while the FHA domain of MDC1 interacts with ATM. Thus, ATM, H2AFX and MDC1 form a positive feedback loop that amplifies downstream ATM signaling and phosphorylation of other ATM targets (Goldberg et al. 2003, Stewart et al. 2003, Stucki et al. 2005, Lou et al. 2006). MDC1 also binds NBN (NBS1) component of the MRN complex, serving as a molecular linker between the MRN complex and the ATM-phosphorylated H2AFX. Although the initial recruitment of the MRN complex to DNA double-strand breaks (DSBs) and ATM-mediated phosphorylation of NBN do not depend on MDC1, MDC1 is necessary for the retention of the MRN complex at DSB sites (Lukas et al. 2004).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13315-1",
"Q92993-1",
"P49959-1",
"Q92878-1"
],
"evidence": [
{
"id": "R-HSA-5693583",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5693583"
}
]
},
{
"id": "R-HSA-5693584",
"name": "Cleavage of Holliday junctions by GEN1 or SLX1A:SLX4:MUS81:EME1,(MUS81:EME2)",
"equation": "",
"summary": "Holliday junctions are efficiently cleaved either by GEN1 endonuclease or the SLX-MUS complex, composed of the SLX1A:SLX4 heterodimer and the heterodimer of MUS81 and EME1 (or, possibly, EME2). Both SLX1A:SLX4 and MUS1:EME1,EME2 possess endonucleolytic activity and act in a coordinated fashion. SLX1A:SLX4 cleaves the double Holliday junction first, which is followed by MUS81:EME1 (or MUS81:EME2) mediated cleavage of the incised Holliday junction. Cleavage by both GEN1 and SLX-MUS predominantly leads to exchange of genetic material between sister chromatids, creating crossover products (Wyatt et al. 2013, Sarbajna et al. 2014).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P38398-1",
"Q13315-1",
"Q92993-1",
"Q06609-1",
"P54132-1",
"P49959-1",
"Q9UQ84-1",
"Q13472-1",
"Q9BQ83-1",
"Q96NY9-1",
"Q99728-1",
"Q99708-1",
"Q9BX63-1",
"Q92878-1",
"Q17RS7-1"
],
"evidence": [
{
"id": "R-HSA-5693584",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5693584"
}
]
},
{
"id": "R-HSA-5693589",
"name": "D-loop dissociation and strand annealing",
"equation": "",
"summary": "Following repair synthesis, the extended D-loop strands may disassociate from their sister chromatid complements and reanneal with their original complementary strands. A DNA helicase RTEL1 disrupts preformed D-loops and promotes synthesis-dependent strand annealing, yielding non-crossover products and preventing excessive recombination between mitotic sister chromatids (Barber et al. 2008, Uringa et al. 2012).",
"cellular_location": "chromosome, nucleoplasm",
"input_participant_list": [],
"output_participant_list": [
"R-ALL-84009"
],
"enzyme_list": [
"Q9NZ71-1",
"P38398-1",
"Q13315-1",
"Q92993-1",
"Q06609-1",
"P54132-1",
"P49959-1",
"Q9UQ84-1",
"Q13472-1",
"Q99728-1",
"Q99708-1",
"Q9BX63-1",
"Q92878-1"
],
"evidence": [
{
"id": "R-HSA-5693589",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5693589"
}
]
},
{
"id": "R-HSA-5693593",
"name": "D-loop extension by DNA polymerases",
"equation": "",
"summary": "Following branch migration, the invading 3' resected ssDNA end of the double-strand break (DSB) acts as a primer for repair DNA synthesis using the complementary strand of the invaded duplex as a template. The replicative DNA polymerases delta (POLD) and likely epsilon (POLE), as well as translesion synthesis (TLS) DNA polymerases eta (POLH) and kappa (POLK) in complex with PCNA, RFC and RPA are implicated in DNA repair synthesis and D-loop extension. While TLS polymerases increase the efficiency of homologous recombination-related DNA synthesis and can directly interact with D-loop proteins RAD51, PALB2 and BRCA2, it is likely that replicative DNA polymerases POLD and POLE, with their high processivity and fidelity, perform the major role in D-loop extension (McIlwraith et al. 2005, Sebesta et al. 2013, Pomerantz et al. 2013, Buisson et al. 2014). In addition, the presence of RAD51-translocases, homologous to yeast Rad54, that remove RAD51 from the 3' invading strand, may be necessary for the catalytic activity of POLD or POLE (Li et al. 2009, Li and Heyer 2009).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P28340-1",
"Q07864-1",
"Q9UBT6-1",
"P38398-1",
"Q13315-1",
"Q92993-1",
"Q06609-1",
"P54132-1",
"P49959-1",
"Q9UQ84-1",
"Q13472-1",
"Q99728-1",
"Q99708-1",
"Q9BX63-1",
"Q92878-1",
"Q9Y253-1"
],
"evidence": [
{
"id": "R-HSA-5693593",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5693593"
}
]
},
{
"id": "R-HSA-5693598",
"name": "ATM phosphorylates NBN",
"equation": "",
"summary": "NSB1 (NBN) is a component of the MRN (MRE11:RAD50:NBN) complex which acts early in homologous recombination repair (HRR) during recognition and resection of double-strand breaks (DSBs). ATM-mediated phosphorylation of NBN at serine residue S343 is required for activation of the S-phase checkpoint in response to ionizing radiation (IR), ATM-dependent activation of CHK2 and cell survival after exposure to IR (Lim et al. 2000, Gatei et al. 2000, Lee and Paull 2004). The phosphorylation of NBN by ATM may be enhanced by the presence of BRCA1 (Foray et al. 2003).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13315-1",
"Q92993-1",
"P49959-1",
"Q92878-1"
],
"evidence": [
{
"id": "R-HSA-5693598",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5693598"
}
]
},
{
"id": "R-HSA-5693599",
"name": "Association of Ku heterodimer with ends of DNA double-strand break",
"equation": "",
"summary": "Ionizing radiation (IR) induces single-strand breaks, i.e., cleavage of the phosphodiester backbone. When two single-strand breaks occur within approximately 10 base pairs, a DNA double-strand break (DSB) results. IR-induced DSBs are complex DNA damage lesions, frequently containing base damage, 5'-OH groups, and 3'-hydroxy or phosphoglycolate groups that must be removed prior to ligation in the final step of NHEJ (Friedberg et al, 1995; Nikjoo et al, 2001; Valerie and Povirk, 2003). The Ku70/80 heterodimer (XRCC5:XRCC6) (Walker et al., 2001) binds to the ends of the double-strand break. Ku can translocate inwards from the site of the break in an ATP-independent manner (reviewed in Dynan and Yoo, 1998). Binding of XRCC5:XRCC6 to DNA DSBs competes away the MRN complex and associated proteins from the DNA DSB (Sun et al. 2012).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13315-1",
"P13010-1",
"O96028-1",
"Q92993-1",
"P12956-1",
"O76064-1",
"P49959-1",
"Q8IYW5-1",
"P61088-1",
"Q92878-1",
"O95714-1",
"Q8N2W9-1"
],
"evidence": [
{
"id": "R-HSA-5693599",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5693599"
}
]
},
{
"id": "R-HSA-5693602",
"name": "ATM recognizes H2AFX-Nucleosomes",
"equation": "",
"summary": "H2AFX (also known as H2AX) is a variant of histone H2A and is present in a portion of nucleosomes. While H2AFX-containing nucleosomes (H2AFX-nucleosomes) are not specifically recruited to the sites of DNA double-strand breaks (DSBs), ATM recognizes the carboxyl tails of H2AFX on H2AFX-nucleosomes in the vicinity of DSBs as a suitable phosphorylation substrate. The phosphorylated H2AFX (gamma-H2AX) plays a crucial role in the retention of DNA repair proteins at DSBs, manifested in the formation of ionizing radiation-induced foci (Paull et al. 2000, Celeste et al. 2002, Redon et al. 2002, Celeste et al. 2003, Fernandez-Capetillo et al. 2004).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13315-1",
"Q92993-1",
"P49959-1",
"Q92878-1"
],
"evidence": [
{
"id": "R-HSA-5693602",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5693602"
}
]
},
{
"id": "R-HSA-5693608",
"name": "Initial resection of double-strand break ends",
"equation": "",
"summary": "In order for repair of the DNA double-strand breaks to occur through homologous recombination or single strand annealing, the 5' ends of the break must first be resected to produce 3' overhanging single stranded DNA (ssDNA) that can subsequently invade homologous duplex DNA (e.g. in the sister chromatid) (Thompson et al. 2001, Kolpashchikov et al. 2001). The MRE11A component of the MRN complex possesses endonuclease activity (Trujillo et al. 1998, Hopfner et al. 2002) that is activated by binding of RBBP8 (CtIP) and BRCA1, in the presence of Mn2+ or Mg2+ ions (Sartori et al. 2007, Yun and Hiom 2009).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P38398-1",
"Q13315-1",
"Q92993-1",
"P49959-1",
"Q99728-1",
"Q99708-1",
"Q92878-1"
],
"evidence": [
{
"id": "R-HSA-5693608",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5693608"
}
]
},
{
"id": "R-HSA-5693609",
"name": "ATM phosphorylates TP53 at S15",
"equation": "",
"summary": "In response to DNA double strand breaks, serine at position 15 of the TP53 (p53) tumor suppressor protein is rapidly phosphorylated by the ATM kinase. This serves to stabilize the p53 protein. A rise in the levels of the p53 protein induces the expression of p21 cyclin-dependent kinase inhibitor. This prevents the normal progression from G1 to S phase, thus providing a check on replication of damaged DNA (Banin et al. 1998, Canman et al. 1998, Khanna et al. 1998).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13315-1"
],
"evidence": [
{
"id": "R-HSA-5693609",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5693609"
}
]
},
{
"id": "R-HSA-5693612",
"name": "MRN complex bound to DNA ends recruits ATM",
"equation": "",
"summary": "Activation of ATM kinase in response to DNA damage in the form of DNA double-strand breaks (DSBs) requires association of ATM dimers with the MRN complex bound to DNA ends. MRN subunit RAD50 is essential for ATM dimer binding (Lee and Paull 2005, Wu et al. 2007). ATM dimer exists in a preformed complex with KAT5 (Tip60) histone acetyltransferase (Sun et al. 2005).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13315-1",
"Q92993-1",
"P49959-1",
"Q92878-1"
],
"evidence": [
{
"id": "R-HSA-5693612",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5693612"
}
]
},
{
"id": "R-HSA-5693620",
"name": "D-loop formation mediated by PALB2, BRCA2 and RAD51",
"equation": "",
"summary": "A D-loop structure is formed when complementary duplex DNA (sister chromatid) is progressively invaded by the RAD51 nucleoprotein filament, with base pairing of the invading ssDNA and the complementary sister chromatid DNA strand (Sung et al. 2003). PALB2, RAD54, RAD51 paralogs (RAD51B, RAD51C, RAD51D, XRCC2, XRCC3), and RAD51AP1 synergistically stimulate RAD51 recombinase activity, thus enhancing RAD51-mediated strand exchange and promoting the formation of D-loop structures. PALB2 simultaneously interacts with RAD51, BRCA2 and RAD51AP1 (Modesti et al. 2007, Wiese et al. 2007, Buisson et al. 2010, Dray et al. 2010). The direct BRCA1 interaction with PALB2 helps to fine-tune the localization of BRCA2 and RAD51 at DNA double-strand breaks (DSBs) (Zhang et al. 2009, Sy et al. 2009). Phosphorylation of PALB2 by ATR on serine residue S59 promotes BRCA1-PALB2 interaction and the localization of PALB2 to DNA damage sites (Buisson et al. 2017).",
"cellular_location": "chromosome, nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P38398-1",
"Q13315-1",
"Q92993-1",
"Q06609-1",
"P54132-1",
"P49959-1",
"Q9UQ84-1",
"Q13472-1",
"Q99728-1",
"Q99708-1",
"Q9BX63-1",
"Q92878-1"
],
"evidence": [
{
"id": "R-HSA-5693620",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5693620"
}
]
},
{
"id": "R-HSA-6792712",
"name": "KAT5 acetylates ATM at shortened telomeres",
"equation": "",
"summary": "The histone acetyltransferase Tip60 (KAT5), in addition to forming a histone acetyltransferase complex with NuA4, forms another complex with ATM dimers. The ATM dimer:KAT5 complex is formed in the absence of DNA damage, but the acetyltransferase activity of KAT5 is activated by double strand DNA breaks (DNA DSBs) (Sun et al. 2005). The activation of KAT5 at shortened telomeres has not been experimentally studied, but KAT5 is assumed to be recruited to shortened telomeres, together with ATM, based on the analogy with ATM activation at DNA DSBs. It is likely that at shortened telomeres, similar to DNA DSBs, the MRN complex targets KAT5 to chromatin, where KAT5 associates with histone H3 trimethylated on lysine 10 (commonly known as H3K9me3 mark). Besides the MRN complex, the ability of KAT5 to access H3K9me3 depends on the DNA damage-induced displacement of HP1beta (CBX1) from H3K9me3 (Ayoub et al. 2008). Similar to DNA DSBs, HP1beta is also displaced from unprotected telomeres (Koering et al. 2002). Binding to H3K9me3 activates the acetyltransferase activity of KAT5 (Sun et al. 2009). KAT5 acetylates ATM on lysine residue K3016 in the highly conserved C-terminal FATC domain of ATM. ATM acetylation is likely needed for the activation of ATM kinase activity at shortened telomeres, as it needed for ATM activation at DNA DSBs (Sun et al. 2007).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13315-1",
"Q92993-1",
"P49959-1",
"Q92878-1"
],
"evidence": [
{
"id": "R-HSA-6792712",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6792712"
}
]
},
{
"id": "R-HSA-6797712",
"name": "CDK12 stimulates expression of DNA repair genes",
"equation": "",
"summary": "CDK12-mediated phosphorylation of the C-terminal domain (CTD) of the RNA polymerase II (RNA Pol II) subunit POLR2A (Rpb1) positively regulates transcription and, hence, expression of a set of DNA repair genes that encode long primary transcripts. CDK12, in complex with the TP53-regulated CCNK (cyclin K), phosphorylates POLR2A that was pre-phosphorylated by the CDK9-containing complex P-TEFb. CDK12-mediated phosphorylation of POLR2A is thought to increase the processivity of the RNA Pol II, enabling efficient transcription of long DNA repair genes (Blazek et al. 2011, Cheng et al. 2012, Bosken et al. 2014, Bartkowiak and Greenleaf 2015). CDK12 was shown to colocalize with the RNA Pol II complex at FANCD2, FANCI, ATM, CHEK1, MDC1, RAD51D and ATR gene loci (Ekumi et al. 2015) and to be necessary for achieving sufficient BRCA1 expression (Blazek et al. 2011). CDK12 positively regulates the expression of APEX1, involved in base excision repair (Liang et al. 2015). Recurrent CDK12 mutations are found in ovarian cancer. These mutations affect either the catalytic cleft of CDK12 or disable the interaction of CDK12 with CCNK, resulting in the loss of CDK12 function. Ovarian tumors that harbour inactivating CDK12 mutations exhibit decreased BRCA1 levels, defective homologous recombination repair, increased sensitivity to DNA crosslinking agents, and sensitivity to PARP inhibitors (Joshi et al. 2014, Ekumi et al. 2015).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P18074-1",
"P38398-1",
"Q13315-1",
"O14757-1",
"P24928-1",
"P50750-1",
"Q13535-1",
"P30876-1",
"P50613-1",
"Q9NYV4-1",
"P19447-1",
"Q9Y5B0-1"
],
"evidence": [
{
"id": "R-HSA-6797712",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6797712"
}
]
},
{
"id": "R-HSA-6798372",
"name": "ATM phosphorylates DYRK2",
"equation": "",
"summary": "Activated ATM kinase phosphorylates DYRK2 at threonine residue T106 (matching T33 in the shorter splicing isoform of DYRK2) and serine residue S442 (matching S369 in the shorter splicing isoform of DYRK2). ATM-mediated phosphorylation of DYRK2 prevents DYRK2 ubiquitination by MDM2 and the consequent DYRK2 degradation (Taira et al. 2010).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-6798368"
],
"enzyme_list": [
"Q13315-1",
"Q92630-1"
],
"evidence": [
{
"id": "R-HSA-6798372",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6798372"
}
]
},
{
"id": "R-HSA-6799097",
"name": "ATM phosphorylates ZNF420",
"equation": "",
"summary": "Activated ATM phosphorylates ZNF420 (Apak) at serine residue S68. Phosphorylation at S68 inhibits ZNF420 binding to the first intron of TP53AIP1 (p53AIP1) gene, thus facilitating TP53 (p53)-mediated expression of TP53AIP1 (Yuan et al. 2012). ATM-mediated phosphorylation of ZNF420 also inhibits ZNF420 interaction with TP53 and the consequent TP53 deacetylation (Tian et al. 2009).",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-1247509"
],
"output_participant_list": [
"R-ALL-113582",
"R-HSA-6799095"
],
"enzyme_list": [
"Q13315-1"
],
"evidence": [
{
"id": "R-HSA-6799097",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6799097"
}
]
},
{
"id": "R-HSA-6799332",
"name": "ATR phosphorylates TP53",
"equation": "",
"summary": "ATR, bound to DNA damage sites, phosphorylates TP53 (p53) at serine residue S15. S15 phosphorylation stabilizes TP53 by inhibiting the binding of TP53 to the ubiquitin ligase MDM2 (Tibbetts et al. 1999, Lakin et al. 1999).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P38398-1",
"Q13315-1",
"Q92993-1",
"Q13535-1",
"P54132-1",
"P49959-1",
"Q9UQ84-1",
"Q13472-1",
"Q99728-1",
"Q99708-1",
"Q9BX63-1",
"Q92878-1",
"Q99638-1"
],
"evidence": [
{
"id": "R-HSA-6799332",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6799332"
}
]
},
{
"id": "R-HSA-6800490",
"name": "ATM phosphorylates PIDD1",
"equation": "",
"summary": "In response to DNA damage, activated ATM phosphorylates PIDD1 at threonine residue T788, a prerequisite for the subsequent interaction with CRADD (RAIDD) (Ando et al. 2012).",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-6800483"
],
"output_participant_list": [],
"enzyme_list": [
"Q9HB75-1",
"Q13315-1"
],
"evidence": [
{
"id": "R-HSA-6800490",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6800490"
}
]
},
{
"id": "R-HSA-6804276",
"name": "ATM phosphorylates TTC5",
"equation": "",
"summary": "ATM phosphorylates TTC5 (Strap), a cofactor of TP53 (p53), on serine residue S203. Phosphorylation of S203 induces nuclear accumulation of TTC5, probably by interfering with the nuclear export signal at the N-terminus of TTC5 (Demonacos et al. 2004, Adams et al. 2008).",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-6804264"
],
"output_participant_list": [],
"enzyme_list": [
"Q13315-1"
],
"evidence": [
{
"id": "R-HSA-6804276",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6804276"
}
]
},
{
"id": "R-HSA-6804741",
"name": "MDM2 forms homo- or heterodimers",
"equation": "",
"summary": "To efficiently function as an E3 ubiquitin ligase, MDM2 has to form dimers or higher order oligomers. MDM2 can homodimerize (Cheng et al. 2011) or heterodimerize with MDM4 (MDMX) (Sharp et al. 1999, Huang et al. 2011, Pant et al. 2011). Dimerization involves the RING domain of MDM2 and/or MDM4. Heterodimers of MDM2 and MDM4 may be particularly important during embryonic development (Pant et al. 2011).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q00987-1",
"Q13315-1"
],
"evidence": [
{
"id": "R-HSA-6804741",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6804741"
}
]
},
{
"id": "R-HSA-6804955",
"name": "ATM phosphorylates MDM2",
"equation": "",
"summary": "ATM phosphorylates MDM2 on three serine residues (S386, S395, S407) and one threonine residue (T419) in vicinity to the RING domain. ATM-mediated phosphorylation of MDM2 in response to DNA damage (DNA double strand breaks) prevents MDM2 dimerization, binding of TP53 (p53) and MDM2-mediated ubiquitination of TP53 (Cheng et al. 2009, Cheng et al. 2011).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-6804954"
],
"enzyme_list": [
"Q00987-1",
"Q13315-1"
],
"evidence": [
{
"id": "R-HSA-6804955",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6804955"
}
]
},
{
"id": "R-HSA-69891",
"name": "Phosphorylation and activation of CHEK2 by ATM",
"equation": "",
"summary": "Activated ATM phosphorylates CHEK2 (CHK2, Cds1) on threonine residue T68 (Matsuoka et al. 2000, Melchionna et al. 2000). The presence of BRCA1 and TP53BP1 positively regulates ATM-mediated phosphorylation of CHEK2 (Wang et al. 2002, Foray et al. 2003). ATM-mediated phosphorylation causes formation of CHEK2 dimers and dissociation of CHEK2 from chromatin (Li and Stern 2005).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-113825"
],
"enzyme_list": [
"P38398-1",
"O96017-1",
"Q13315-1",
"P46736-1",
"O96028-1",
"Q92993-1",
"O76064-1",
"P49959-1",
"Q8IYW5-1",
"Q99728-1",
"P61088-1",
"Q92878-1",
"O95714-1",
"Q8N2W9-1"
],
"evidence": [
{
"id": "R-HSA-69891",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-69891"
}
]
},
{
"id": "R-HSA-912429",
"name": "Resolution of meiotic holliday junction",
"equation": "",
"summary": "Meiotic Holliday junctions are cleaved to yield either crossovers or non?crossovers (gene conversions). The resolvase or resolvases responsible for cleavage are unknown but a resolvase complex may include SLX4 and/or GEN1.
Two classes of crossovers have been defined: class I crossovers are dependent on the MutL homologs, MLH1 and MLH3, while class II crossovers are dependent on the MUS81-EME1 endonuclease. Class I crossovers constitute 90-95% of all crossovers, and correspond to meiotic nodules that contain MLH1and MLH3. These arise as a subset of the many hundreds of MSH4/MSH5-positive meiotic nodules that arise at the time of double Holliday junction formation. What happens to all the other meiotic nodules is not clear, but they most likely follow a second pathway that results in non-crossovers (or gene conversions). MLH1 and MLH3 form heterodimers that repair mismatches in duplex DNA. In mouse, MLH1 is required for crossovers but not for non?crossover resolution of Holliday junctions. About 10% of early meiotic nodules are somehow selected to become Class I crossover events, possibly by first losing BLM (and probably associated TOP3A), and acquiring MLH1 and MLH3.
The selection of sites for class II crossovers follows an, as yet, unknown pathway, but almost certainly stems from the same initiating D-loop intermediate.
In the process known as crossover interference, the presence of a crossover nodule inhibits formation of nearby crossover nodules so that crossovers are not clustered and each chromosome bivalent has at least one crossover. In mouse, crossover interference is seen among nodules at two stages: RPA?containing nodules during late zygonema and MLH1?containing nodules during pachynema. Class II crossovers are not subject to interference constraints.",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-68365",
"R-HSA-912478",
"R-HSA-912495"
],
"output_participant_list": [
"R-HSA-113843",
"R-HSA-50951"
],
"enzyme_list": [
"Q13315-1",
"P54132-1",
"Q13472-1",
"P11802-1",
"P24941-1"
],
"evidence": [
{
"id": "R-HSA-912429",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-912429"
}
]
},
{
"id": "R-HSA-912458",
"name": "Formation of meiotic heteroduplex",
"equation": "",
"summary": "Following double strand break (DSB) formation and strand resection, RAD51 and DMC1 coat single-stranded 3' ends of DNA and catalyze the search for homology and strand invasion into the DNA duplex of the chromosomal homolog (Baumann et al. 1996, Barlow et al. 1997, Benson et al. 1998, Baumann and West 1999, Masson et al. 1999, Sehorn et al. 2004, Murayama et al. 2008). The invading strand displaces the original strand of the chromosomal homolog creating a D-loop structure. Other proteins present in the complex are inferred from cytology (Barlow et al. 1997, Oliver-Bonet et al. 2005, Oliver-Bonet et al. 2007).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P38398-1",
"Q13315-1",
"Q06609-1",
"P11802-1",
"Q14565-1"
],
"evidence": [
{
"id": "R-HSA-912458",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-912458"
}
]
},
{
"id": "R-HSA-912496",
"name": "Formation of meiotic holliday junction",
"equation": "",
"summary": "The 3' end of the invading strand is extended by an unknown DNA polymerase and the extended strand is then ligated back to the original homolog, generating a double Holliday junction. MSH4 and MSH5 form heterodimers which bind Holliday junctions and, in the presence of ATP, slide along the parental duplexes (Bocker et al. 1999, Snowden et al. 2004, Snowden et al. 2008). MSH4 is present at hundreds of meiotic nodules during late zygotene but only about 10% of these nodules become crossovers (Oliver-Bonet et al. 2005). Bloom Syndrome protein (BLM) and Topoisomerase IIIa (TOP3A) are also present and may promote homologous recombination repair without crossing over (Johnson et al. 2000, Wu et al. 2000).",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-174881",
"R-HSA-912435",
"R-HSA-912452",
"R-HSA-912455"
],
"output_participant_list": [
"R-HSA-912490"
],
"enzyme_list": [
"Q13315-1",
"Q06609-1",
"P54132-1",
"Q13472-1",
"P11802-1",
"Q14565-1"
],
"evidence": [
{
"id": "R-HSA-912496",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-912496"
}
]
},
{
"id": "R-HSA-912503",
"name": "Formation of meiotic single-stranded DNA invasion complex",
"equation": "",
"summary": "Two RecA homologs, RAD51 and the meiosis-specific DMC1, coat single-stranded 3' ends of DNA produced by resection of double-strand breaks (Barlow et al. 1997, Masson et al. 1999, Sehorn et al. 2004, Sheridan et al. 2008, Okorokov et al. 2010). RAD51 and DMC1 interact and colocalize to the same early recombination nodules (Masson et al. 1999). Knockouts of DMC1 abolish recombination and synapsis therefore RAD51 is not sufficient for recombination.
Immunocytology shows the RPA heterotrimer arrives at recombination nodules with or after RAD51 and DMC1 (Golub et al. 1999, Oliver-Bonet et al. 2005, Oliver-Bonet et al. 2007)). (In mitotic recombination RPA precedes RAD51.)
BRCA1 and BRCA2 are found extensively distributed on synaptonemal complexes. Results from human cells and knockout mice indicate that BRCA2, RAD51C, and TEX15 participate in loading RAD51 and DMC1 onto single-stranded DNA (Thorslund et al. 2007). BRCA1 participates in loading RAD51 but not DMC1 (Scully et al. 1997).
The kinase ATM is also localized to double-strand breaks where it phosphorylates histone H2AX.
In human spermatocytes about 350 early recombination nodules form but only about 10% will continue on to make crossovers. The remaining 90% are believed to be resolved by synthesis-dependent strand annealing, which transfers short segments of DNA (about 0.2-2.0 kilobases) between homologs.",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P38398-1",
"Q13315-1",
"Q06609-1",
"P11802-1",
"Q14565-1"
],
"evidence": [
{
"id": "R-HSA-912503",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-912503"
}
]
},
{
"id": "R-HSA-9664850",
"name": "ATM binds PEX5",
"equation": "",
"summary": "The first step in pexophagy is the initiation by a signal that triggers downstream events to eventually degrade the peroxisome. Ataxia-telangiectasia mutated protein (ATM) is a serine/threonine protein kinase that is involve in DNA damage response. ATM is known to be involved in pexophagy (Katarzyna ZR et al. 2016). ATM binds with Peroxisomal targeting signal 1 receptor (PEX5) with the help of a SRL binding sequence in ATM (Zhang J et al. 2015).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13315-1"
],
"evidence": [
{
"id": "R-HSA-9664850",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664850"
}
]
},
{
"id": "R-HSA-9664855",
"name": "MAP1LC3B binds ATM dimer:Ub-p-PEX5:SQSTM1",
"equation": "",
"summary": "Sequestosome 1 (SQSTM1) is an autophagic receptor that recruits ubiquitinated cargo to the autophagosome. SQSTM1 contains a ubiquitin associated (UBA) domain that binds to monoubiquitinated Peroxisomal targeting signal 1 receptor (PEX5) in the peroxisome and an LC3 interacting region (LIR) that binds to Microtubule associated proteins 1A/1B light chain 3B (MAP1LC3B)/LC3 associated with the nascent autophagosome (Pankiv S et al. 2007). Subsequently, the peroxisome is degraded by the autophagy machinery.",
"cellular_location": "peroxisomal membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13315-1"
],
"evidence": [
{
"id": "R-HSA-9664855",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664855"
}
]
},
{
"id": "R-HSA-9664862",
"name": "ATM dimer:PEX5 phosphorylates PEX5",
"equation": "",
"summary": "When serine/threonine kinase Ataxia telangiectasia mutated protein (ATM) is activated it can phosphorylate Peroxisomal targeting signal 1 receptor protein (PEX5) at Ser141 (Zhang J et al. 2015).",
"cellular_location": "peroxisomal membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13315-1"
],
"evidence": [
{
"id": "R-HSA-9664862",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664862"
}
]
},
{
"id": "R-HSA-9664879",
"name": "ATM:PEX5 binds ATM",
"equation": "",
"summary": "After Peroxisomal targeting signal 1 receptor (PEX5) recruits Ataxia telangiectasia mutated protein (ATM) to the peroxisomal membrane, ATM is activated by the reactive oxygen species (ROS). ROS can oxidize and activate ATM by forming a disulphide cross-linked dimer at the Csy2991 residue (Guo Z et al. 2010).",
"cellular_location": "peroxisomal membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13315-1"
],
"evidence": [
{
"id": "R-HSA-9664879",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664879"
}
]
},
{
"id": "R-HSA-9664880",
"name": "MAP1LC3B binds ATM dimer:Ub-p-PEX5:SQSTM1:NBR1",
"equation": "",
"summary": "Autophagic receptors, Next to BRCA1 gene 1 protein (NBR1) and Sequestosome 1 (SQSTM1) cooperate to bind and recruit ubiquitinated peroxisomes to the autophagy machinery. NBR1 and SQSTM1 have similar protein domain architecture and bind to Microtubule associated proteins 1A/1B light chain 3B (MAP1LC3B)/LC3 via an LC3 interacting region (LIR) (Kirkin V et al. 2009). Subsequently, peroxisomes are engulfed within the autophagosome and degraded.",
"cellular_location": "peroxisomal membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13315-1"
],
"evidence": [
{
"id": "R-HSA-9664880",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664880"
}
]
},
{
"id": "R-HSA-9664881",
"name": "NBR1 binds ATM:Ub-p-PEX5:SQSTM1",
"equation": "",
"summary": "As autophagy receptors, Next to BRCA1 gene 1 protein (NBR1) and Sequestosome 1 (SQSTM1) can cooperate to achieve pexophagy. SQSTM1 supports NBR1 to bind ubiquitinated peroxisomes through its UBA domain and enhances the efficiency of the degradation process (Kirkin V et al. 2009).",
"cellular_location": "peroxisomal membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13315-1"
],
"evidence": [
{
"id": "R-HSA-9664881",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664881"
}
]
},
{
"id": "R-HSA-9664883",
"name": "ATM:PEX5 translocates from cytosol to peroxisomal membrane",
"equation": "",
"summary": "After the binding of Peroxisomal targeting signal 1 receptor (PEX5) and Ataxia telangiectasia mutated protein (ATM), PEX5 recruits the complex to the peroxisomal membrane for the next steps of the degradation process (Zhang J et al. 2015).",
"cellular_location": "cytosol, peroxisomal membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13315-1"
],
"evidence": [
{
"id": "R-HSA-9664883",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664883"
}
]
},
{
"id": "R-HSA-9664888",
"name": "ATM dimer:p-PEX5 ubiquitinates to form ATM dimer:Ub-p-PEX5",
"equation": "",
"summary": "Phosphorylation of Peroxisomal targeting signal 1 receptor protein (PEX5) at Ser141 promotes the ubiquitination of PEX5. The RING peroxins complex composed of: Peroxisome biogenesis factor 2 (PEX2), Peroxisome biogenesis factor 10 (PEX10), and Peroxisome assembly protein 12 (PEX12) form part of a peroxisome localized E3 ligase that ubiquitinates PEX5 at Lys209 (Zhang J et al. 2015). This mono ubiquitination of PEX5 helps to recruit the autophagy machinery to the peroxisome.",
"cellular_location": "peroxisomal membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13315-1"
],
"evidence": [
{
"id": "R-HSA-9664888",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664888"
}
]
},
{
"id": "R-HSA-9664892",
"name": "SQSTM1 binds ATM dimer:Ub-p-PEX5",
"equation": "",
"summary": "Sequestosome 1 (SQSTM1) is an autophagy adaptor that serves to bridge ubiquitinated cargo and the autophagosome. It binds ubiquitinated cargo via its UBA domain. SQSTM1 in the cytosol recognizes and binds with ubiquitinated Peroxisomal targeting signal 1 receptor (PEX5) in the peroxisomal membrane (Zhang et al. 2015).",
"cellular_location": "cytosol, peroxisomal membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13315-1"
],
"evidence": [
{
"id": "R-HSA-9664892",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664892"
}
]
},
{
"id": "R-HSA-9674127",
"name": "USP30 deubiquitinates ATM dimer:Ub-p-PEX5",
"equation": "",
"summary": "The deubiquitinase, Ubiquitin carboxyl-terminal hydrolase 30 (USP30) counters the action of E3 ligase on peroxisomal membrane proteins. USP30 can remove ubiquitin moieties from PEX5 thereby preventing pexophagy (Riccio V et al. 2019, Marcassa E et al. 2019)",
"cellular_location": "peroxisomal membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13315-1",
"Q70CQ3-1"
],
"evidence": [
{
"id": "R-HSA-9674127",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9674127"
}
]
},
{
"id": "R-HSA-9674131",
"name": "USP30 binds ATM dimer:Ub-p-PEX5",
"equation": "",
"summary": "As a deubiquitinase, Ubiquitin carboxyl-terminal hydrolase 30 (USP30) can reverse the action of E3 ligase on peroxisomal membrane proteins. Studies show that USP30 can localise in the peroxisomal membrane and interact with ubiquitinated PEX5 (Riccio V et al. 2019, Marcassa E et al. 2019).",
"cellular_location": "peroxisomal membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13315-1",
"Q70CQ3-1"
],
"evidence": [
{
"id": "R-HSA-9674131",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9674131"
}
]
},
{
"id": "R-HSA-9701199",
"name": "Defective D-loop formation mediated by PALB2, BRCA2 and RAD51 due to loss-of-function of BRCA1 in PALB2 binding",
"equation": "",
"summary": "The following missense mutants of BRCA1, reported in cancer, contain mutations in the second coiled coil domain, essential for binding to PALB2 (residues 1397-1424). They have been shown to be impaired in their ability both to bind to PALB2 and to rescue the gene conversion defect associated with BRCA1 depletion:
BRCA1 M1400V (Sy et al. 2009: partial loss of function)
BRCA1 L1407P (Sy et al. 2009); this mutation has also been modelled in mice, recapitulating the human Fanconi anemia phenotype (Park et al. 2020)
BRCA1 M1411T (Sy et al. 2009).
BRCA1 single nucleotide variants located in splicing regulatory regions have the potential to disrupt mRNA splicing and generate frameshift or in-frame proteins lacking functional domains. In this sense, several BRCA1 splicing mutations have been identified in hereditary breast/ovarian cancer cases and predicted to produce non-functional proteins that would lack the coiled-coil and BRCT domains. All variants are derived from ClinVar database (Landrum et al. 2018) and have been classified as pathogenic by expert panels. Variants are listed below and annotated according to the reference transcript NM_007294, but their annotation at the protein level is currently outside the scope of Reactome database:
c.135-1G>T
c.212+1G>A
c.212+1G>T
c.302-1G>C
c.302-2del
c.441+2T>G
c.4097-1G>A
c.4097-2A>G
c.4185+2_4185+22delinsA
c.4357+1G>A
c.4357+1G>T
c.4358_4484del127
c.4484+1del
c.4485-1G>T
c.4675+1G>A
c.4676-1G>A
c.4987-1G>A
c.4987-2A>G
c.547+1G>T
c.547+2T>A
c.5074+1G>A
c.5074+1G>T
c.5074+2T>C
c.5152+1G>T
c.5153-1G>A
c.5153-1G>C
c.5155delG
c.5155dup
c.5277+1_5277+6del
c.5277+1G>A
c.5278-2del
c.5331_5332+1delinsCAACAT
c.5332+1G>A
c.5468-1G>A
Many nonsense and frameshift mutants of BRCA1 reported in cancer result in prematurely truncated proteins. These mutant proteins resemble the synthetic BRCA1 fragment consisting of amino acids 1-1314, which is unable to interact with PALB2 (Sy et al. 2009). These BRCA1 truncation mutants are likely impaired in some of the other steps of DNA double-strand break repair (DSBR) that precede PALB2 binding but their effect on DSBR has not been comprehensively tested.
The following functionally uncharacterized nonsense mutants of BRCA1 , derived from COSMIC database (Forbes et al. 2017), which are truncated before the amino acid position 1314, have been annotated as candidates:
BRCA1 Q94*
BRCA1 E111*
BRCA1 E116*
BRCA1 Q126*
BRCA1 E149*
BRCA1 Q169*
BRCA1 Q202*
BRCA1 Q210*
BRCA1 E272*
BRCA1 Q317*
BRCA1 W372*
BRCA1 R388*
BRCA1 L431*
BRCA1 S451*
BRCA1 E457*
BRCA1 K467*
BRCA1 L474*
BRCA1 E515*
BRCA1 K519*
BRCA1 G535*
BRCA1 Q541*
BRCA1 Q544*
BRCA1 E572*
BRCA1 E577*
BRCA1 E597*
BRCA1 E648*
BRCA1 Y655*
BRCA1 Q667*
BRCA1 E673*
BRCA1 E720*
BRCA1 E733*
BRCA1 Y777*
BRCA1 E787*
BRCA1 K800*
BRCA1 E836*
BRCA1 E842*
BRCA1 E848*
BRCA1 S864*
BRCA1 E881*
BRCA1 E904*
BRCA1 G911*
BRCA1 Q934*
BRCA1 K935*
BRCA1 S988*
BRCA1 E1004*
BRCA1 S1007*
BRCA1 S1009*
BRCA1 E1033*
BRCA1 K1037*
BRCA1 E1107*
BRCA1 E1112*
BRCA1 Q1144*
BRCA1 K1160*
BRCA1 E1167*
BRCA1 R1203*
BRCA1 E1210*
BRCA1 E1214*
BRCA1 Q1240*
BRCA1 E1250*
BRCA1 E1258*
BRCA1 L1276*
BRCA1 Q1281*
The following functionally uncharacterized frameshift mutants of BRCA1 , derived from COSMIC database (Forbes et al. 2017), which are truncated before the amino acid position 1314, have been annotated as candidates:
BRCA1 R71Kfs*10
BRCA1 E75Kfs*13
BRCA1 V83Cfs*2
BRCA1 E111Gfs*3
BRCA1 P115*
BRCA1 Q172Nfs*62
BRCA1 Q210Sfs*6
BRCA1 A224Gfs*4
BRCA1 S242Rfs*5
BRCA1 N287Qfs*6
BRCA1 L290Yfs*8
BRCA1 D295Tfs*3
BRCA1 K339Rfs*2
BRCA1 V340Gfs*6
BRCA1 W372Yfs*5
BRCA1 S426*
BRCA1 H437*
BRCA1 R446Sfs*9
BRCA1 E453Rfs*22
BRCA1 T464Pfs*11
BRCA1 L502Afs*2
BRCA1 A521Qfs*11
BRCA1 N555Ifs*17
BRCA1 N555Kfs*17
BRCA1 N567Pfs*16
BRCA1 K608Ifs*3
BRCA1 K654Sfs*47
BRCA1 Y655Vfs*18
BRCA1 L668Pfs*33
BRCA1 E686*
BRCA1 N714Kfs*4
BRCA1 P724Lfs*12
BRCA1 E729Rfs*10
BRCA1 K739Ifs*15
BRCA1 V757Ffs*8
BRCA1 G813Dfs*2
BRCA1 H816Qfs*3
BRCA1 G817Vfs*29
BRCA1 F869Vfs*35
BRCA1 A878Gfs*24
BRCA1 S886Cfs*16
BRCA1 K893Rfs*107
BRCA1 K894Tfs*8
BRCA1 P897Kfs*5
BRCA1 N909Kfs*6
BRCA1 G911Efs*89
BRCA1 T922Lfs*77
BRCA1 I925Nfs*13
BRCA1 G928Afs*72
BRCA1 G948Efs*52
BRCA1 I986Sfs*14
BRCA1 F989Lfs*10
BRCA1 F989Lfs*11
BRCA1 E1013Nfs*4
BRCA1 N1029Kfs*3
BRCA1 N1045*
BRCA1 K1079Nfs*2
BRCA1 L1086Dfs*2
BRCA1 E1112Dfs*5
BRCA1 E1115*
BRCA1 N1121Kfs*12
BRCA1 Y1127Sfs*6
BRCA1 C1146Lfs*8
BRCA1 D1156Cfs*2
BRCA1 V1176Ffs*34
BRCA1 K1183Rfs*4
BRCA1 R1188Efs*3
BRCA1 S1217Rfs*21
BRCA1 E1219Ffs*12
BRCA1 C1225Sfs*10
BRCA1 K1254Nfs*11
BRCA1 N1265Kfs*4
BRCA1 E1282Afs*26
BRCA1 H1284Tfs*23
BRCA1 E1288Kfs*19",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P38398-1",
"Q13315-1",
"Q92993-1",
"Q06609-1",
"P54132-1",
"P49959-1",
"Q9UQ84-1",
"Q13472-1",
"Q99728-1",
"Q99708-1",
"Q9BX63-1",
"Q92878-1"
],
"evidence": [
{
"id": "R-HSA-9701199",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9701199"
}
]
},
{
"id": "R-HSA-9704330",
"name": "Defective D-loop formation mediated by PALB2, BRCA2 and RAD51 due to loss-of-function of PALB2 in BRCA1 binding",
"equation": "",
"summary": "The coiled-coil domain at the N-terminus of PALB2 represents a hotspot for mutations in PALB2. Several PALB2 missense mutants have been characterized either in targeted studies (Sy et al. 2009, Foo et al. 2017, Song et al. 2018) or as part of high throughput approaches to characterize clinical variants of uncertain significance (reviewed in Boonen et al. 2020).
The following PALB2 missense mutants have been shown to be at least partially defective in their ability to bind to BRCA1 (some of these mutants were also shown to be defective in their ability to homodimerize and to promote homologous recombination repair (HRR); in addition, some have been shown to confer sensitivity to DNA damaging agents or to PARP inhibitors):
PALB2 L21A (originally studied as a synthetic mutant with an amino acid substitution at one of the coiled-coil domain residues of PALB2 that are critical for BRCA1 binding and homodimerization (Sy et al. 2009, Song et al. 2018); this mutant has also been reported clinically, in Clingen Allele Registry (Pawliczek et al. 2018), as a consequence of an in-frame indel in PALB2)
PALB2 L24S (Boonen et al. 2019; Wiltshire et al. 2020; also shown to be defective in HRR (Boonen et al. 2019, Wiltshire et al. 2020), confer sensitivity to cisplatin (Wiltshire et al. 2020) and PARP inhibitor olaparib (Wiltshire et al. 2020))
PALB2 Y28C (partially impaired in BRCA1 binding, Foo et al. 2017; significantly impaired BRCA1 binding, Rodrigue et al. 2019; does not disrupt PALB2 self-interaction (Foo et al. 2017); not significantly defective in HRR and does not confer sensitivity to DNA damaging agents and PARP inhibitors (Foo et al. 2017); partially defective in HRR (Rodrigue et al. 2019, Wiltshire et al. 2020) and significantly sensitive to cisplatin and PARP inhibition (Boonen et al. 2019))
PALB2 L35P (Foo et al. 2017, Rodrigue et al. 2019, Boonen et al. 2019, Wiltshire et al. 2020; does not disrupt PALB2 self-interaction (Foo et al. 2017); also shown to be defective in HRR (Foo et al. 2017, Rodrigue et al. 2019, Boonen et al. 2019, Wiltshire et al. 2020), confer sensitivity to platinum salts (Foo et al. 2017, Boonen et al. 2019, Wiltshire et al. 2020), and confer sensitivity to PARP inhibitors (Foo et al. 2017, Boonen et al. 2019, Wiltshire et al. 2020))
PALB2 R37H (not significantly affected in BRCA1 binding, Foo et al. 2017; partially impaired in BRCA1 binding, Boonen et al. 2019; partially defective in HRR (Foo et al. 2017, Rodrigue et al. 2019, Boonen et al. 2019, Wiltshire et al. 2020))
Interestingly, some of the PALB2 variants that show a defective interaction with BRCA1, such as PALB2 L24S, PALB2 Y28C, and PALB2 L35P, seem to have slightly elevated protein levels (Foo et al. 2017, Boonen et al. 2019, Wiltshire et al. 2020).
Synthetic PALB2 mutants generated by directed mutagenesis, PALB2 L21P (Zhang et al. 2009), PALB2 L24P (Zhang et al. 2009), PALB2 Y28A (Sy et al. 2009) and PALB2 L35A (Sy et al. 2009) are also unable to bind BRCA1 and show impaired homologous recombination function.
The following PALB2 mutants, reported in cancer and predicted to be pathogenic, have not been functionally studied and are annotated as candidate loss-of-function mutants for BRCA1 binding based on their sequence similarity with functionally studied PALB2 mutants:
PALB2 L21F (similar to PALB2 L21A)
PALB2 L35F (similar to the synthetic mutant PALB2 L35A, described by Sy et al. 2009 and to the functionally characterized cancer-associated mutant PALB2 L35P)
PALB2 R37C (similar to PALB2 R37H)
PALB2 E12* (truncation mutants that lacks the coiled coil domain involved in BRCA1 binding, which maps to residues 9-42, as described by Sy et al. 2009; this truncation mutant may be a null mutant as the protein is predicted to have only the first 11 amino acids).
A comprehensive list of variants in the PALB2 gene is provided at the Leiden Open Variation Database (LOVD) (https://databases.lovd.nl/shared/genes/PALB2) (Fokkema et al. 2011).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P38398-1",
"Q13315-1",
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],
"evidence": [
{
"id": "R-HSA-9704330",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9704330"
}
]
},
{
"id": "R-HSA-9704408",
"name": "Defective D-loop formation mediated by PALB2, BRCA2 and RAD51 due to loss-of-function of PALB2 in binding to BRCA2/RAD51/RAD51C",
"equation": "",
"summary": "The WD40 domain located in the C-terminus of PALB2, between amino acid residues 853-1186, enables binding of PALB2 to BRCA2, RAD51, RAD51C, RNF168 and POLN (Luijsterburg et al. 2017, Buisson 2014). The synthetic truncation mutant of PALB2, PALB2deltaC, which ends at the proline residue P1097, lacks blades 5-7 of the WD40 domain and is completely unable to interact with RAD51C, RAD51 and BRCA2 (Park et al. 2014). Truncating nonsense and frameshift mutations in PALB2 that entirely or partially perturb the WD40 domain, as well as missense mutations in the WD40 domain are found in cancer (including familial breast cancer) and Fanconi anemia patients and are associated with impaired PALB2 binding to BRCA2, RAD51 and/or RAD51C, impaired assembly of RAD51 DNA double-strand break (DSB) repair foci, defective homologous recombination repair (HRR), and cellular sensitivity to DNA crosslinking agents such as mitomycin C (Erkko et al. 2007, Tischkowitz et al. 2007, Xia et al. 2007, Zhang et al. 2007, Park et al. 2014, Foo et al. 2017, Rodrigue et al. 2019, Boonen et al. 2019, Wiltshire et al. 2020). The WD40 domain is also important for PALB2 stability, as the PALB2 Y1183* mutant, which lacks the last four amino acids of PALB2, does not fold completely and is thus susceptible to degradation (Reid et al. 2007, Oliver et al. 2009). Many of the characterized missense mutations in the WD40 domain are associated with reduced PALB2 protein levels, thought to be due to reduced protein stability (Boonen et al. 2019, reviewed in Boonen et al. 2020). In addition, this domain also contains, buried within the propeller structure, a nuclear export signal (NES). Some of the WD40 missense mutants of PALB2 show moderate to significant cytosolic accumulation, possibly due to unmasking of the C terminal nuclear export signal (Rodrigue et al. 2019). The cancer mutant PALB2 W1038* is mislocalized to the cytoplasm, which impacts the functionality of PALB2 (Pauty et al. 2017). The following missense mutants described below also show mislocalization to the cytoplasm: PALB2 I944N, PALB2 L1070P, PALB2 L947F, PALB2 L947S, PALB2 T1030I, PALB2 G1043A, PALB2 L1119P and PALB2 W1140G (Wiltshire et al. 2019, Rodrigue et al. 2019).
The following PALB2 missense mutations that affect the WD40 domain have been shown to be defective in binding to BRCA2, RAD51 and/or RAD51C or to be defective in formation of RAD51 foci:
PALB2 W912G (Boonen et al. 2019: reduced number of RAD51 foci, defective HRR, sensitivity to PARP inhibitors, decreased protein stability)
PALB2 G937R (Boonen et al. 2019: modestly reduced number of RAD51 foci, defective HRR, sensitivity to PARP inhibitors, decreased protein stability)
PALB2 L939W (Park et al. 2014: significantly reduced binding to BRCA2 and RAD51, no significant effect on RAD51C binding, modest but significant decrease in DSB-initiated homologous recombination repair and assembly of RAD51 foci; Wiltshire et al. 2020: reduced binding to BRCA2 and RAD51)
PALB2 I944N (Boonen et al. 2019: defective HRR, sensitivity to PARP inhibitors, decreased protein stability; Wiltshire et al. 2020: reduced binding to BRCA2 and RAD51, partially defective HRR)
PALB2 L947F (Rodrigue et al. 2019: significantly reduced binding to BRCA2, moderate cytosolic accumulation, significant decrease in the number of RAD51 foci; Wiltshire et al. 2020: partially defective HRR)
PALB2 L947S (Rodrigue et al. 2019: significantly reduced binding to BRCA2, moderate cytosolic accumulation, significant decrease in the number of RAD51 foci; Boonen et al. 2019: reduced protein stability, partially defective HRR, partial sensitivity to PARP inhibitors; modestly decreased number of RAD51 foci; Wiltshire et al. 2020: partially defective HRR)
PALB2 L961P (Boonen et al. 2019: reduced number of RAD51 foci, defective HRR, sensitivity to PARP inhibitors, sensitivity to cisplatin, decreased protein stability)
PALB2 T1030I (Park et al. 2014: no effect on BRCA2 binding, significant reduction in RAD51 and RAD51C binding, reduced protein stability; Rodrigue: significantly reduced binding to BRCA2, significant cytosolic accumulation, defective HRR, significant decrease in the number of RAD51 foci; Boonen et al. 2019: defective HRR, sensitivity to PARP inhibitors, decreased protein stability; Wiltshire et al. 2020: partially defective HRR)
PALB2 G1043A (Rodrigue et al. 2019: significantly reduced binding to BRCA2, partially defective HRR; Wiltshire et al. 2020: partially defective HRR)
PALB2 G1043D (Boonen et al. 2019: reduced number of RAD51 foci, defective HRR, sensitivity to PARP inhibitors, decreased protein stability)
PALB2 L1070P (Boonen et al. 2019: decreased protein stability; Wiltshire et al. 2020: reduced binding to BRCA2)
PALB2 L1119P (Rodrigue et al. 2019: significantly reduced binding to BRCA2, moderate cytosolic accumulation, partially defective HRR, persistent RAD51 foci \u2013 suggestive of defective disassembly of RAD51 foci; Boonen et al. 2019: no significant reduction in HRR efficiency, no significant sensitivity to PARP inhibitors; Wiltshire et al. 2020: partially defective HRR)
PALB2 W1140G (Rodrigue et al. 2019: significantly reduced binding to BRCA2, moderate cytosolic accumulation, partially defective HRR, significantly reduced number of RAD51 foci; Wiltshire et al. 2020: partially defective HRR)
PALB2 L1143P (Park et al. 2014: modest but significant reduction in binding to BRCA2, RAD51 and RAD51C, modest but significant decrease in DSB-initiated homologous recombination repair and assembly of RAD51 foci).
Although the synthetic missense variant PALB2 A1025R has normal expression level, it is impaired in homologous recombination (Boonen et al. 2019), confirming previous studies that showed an impaired interaction with BRCA2 (Oliver et al. 2009, Rodrigue et al. 2019, Wiltshire et al. 2020).
The following truncation (nonsense and frameshift) mutants on PALB2 were shown to be defective in binding to BRCA2, RAD51 and/or RAD51C:
PALB2 Y551* nonsense mutant, first identified in a Fanconi anemia patient, is unable to interact with BRCA2, RAD51C and largely with RAD51 (Xia et al. 2007, Park et al. 2014); it was also shown to be defective in HRR (Boonen et al. 2019, Wiltshire et al. 2020) and to confer sensitivity to PARP inhibitors (Boonen et al. 2019).
PALB2 L531Cfs*3 frameshift mutant (c.1592delT), frequently present in Finnish familial breast cancer cases, has little BRCA2 binding capacity and is defective in homologous recombination repair and crosslink repair (Erkko et al. 2007).
Two additional frameshift mutants of PALB2 associated with a strong family history of breast cancer and impaired in their ability to bind to BRCA2 are:
PALB2 C77Vfs100* (Tischkowitz et al. 2007)
PALB2 T841Qfs10* (Tischkowitz et al. 2007; this mutant was also reported in Fanconi anemia by Reid et al. 2007)
The following candidate WD40 domain missense mutants of PALB2 have been shown to be functionally impaired in HRR but their ability to bind to BRCA2, RAD51 or RAD51C, or to form RAD51 foci, has not been tested (as indicated), or they are predicted to be pathogenic and share sequence similarity with functionally studied PALB2 mutants:
PALB2 L972Q (Boonen et al. 2019: decreased protein stability, defective HRR, sensitivity to PARP inhibitors)
PALB2 I1037T (Boonen et al. 2019: decreased protein stability, defective HRR)
PALB2 G1043C (similar to PALB2 G1043A and PALB2 G1043D)
PALB2 L1172P (Boonen et al. 2019: decreased protein stability, defective HRR, sensitivity to PARP inhibitors)
Based on their similarity with the synthetic PALB2deltaC mutant, truncation mutants of PALB2 derived from COSMIC database (Forbes et al. 2017) which have not been functionally studied and whose amino acid sequence terminates before the terminal P1097 residue of PALB2deltaC, are annotated as candidate loss-of-function mutants for BRCA2, RAD51 and RAD51C binding. Several truncation mutants in PALB2 that have been reported in Fanconi anemia and/or hereditary breast cancer are also annotated as candidates (Reid et al. 2007, Rahman et al. 2007). In addition, several PALB2 truncation mutants that were shown to be functionally impaired in HRR, but whose ability to bind to BRCA2, RAD51 or RAD51C has not been tested are also annotated as candidates (reviewed in Boonen et al. 2020).
The following nonsense mutants of PALB2, reported in cancer, are annotated as candidates:
PALB2 Q66*
PALB2 Q228*
PALB2 E230* (Boonen et al. 2019: defective HRR, sensitivity to PARP inhibitors)
PALB2 Q251* (Wiltshire et al. 2020: defective HRR)
PALB2 S254*
PALB2 E263*
PALB2 K346*
PALB2 Q370*
PALB2 E384*
PALB2 Y409* (Boonen et al. 2019: defective HRR, sensitivity to PARP inhibitors)
PALB2 R414*
PALB2 L451*
PALB2 S518*
PALB2 E545*
PALB2 Q559*
PALB2 W575*
PALB2 Q613*
PALB2 E658*
PALB2 E667*
PALB2 R753* (also reporter in Fanconi anemia, Reid et al. 2007)
PALB2 G796*
PALB2 G808*
PALB2 Q822*
PALB2 L857*
PALB2 E860*
PALB2 E884*
PALB2 E943*
PALB2 E956*
PALB2 Q988* (reported in Fanconi anemia by Reid et al. 2007)
PALB2 E1002*
PALB2 W1038* (Boonen et al. 2019: defective HRR, sensitivity to PARP inhibitors, reduced protein stability)
PALB2 Q1056*
PALB2 Q1091*
PALB2 Y1183* (this PALB2 mutant lacks only the four terminal amino acids, but was reported in hereditary breast cancer by Rahman et al. 2007 and in Fanconi anemia by Reid et al. 2007, the latter study suggesting that this is a null mutation, with no detectable protein; the mechanism is unclear, as significantly shorter C-terminally truncated PALB2 mutants are detectable)
The following frameshift mutants of PALB2, reported in cancer, are annotated as candidates:
PALB2 R37Cfs*5
PALB2 K43Rfs*10
PALB2 Q60Rfs*7 (Boonen et al. 2019: defective HRR, sensitivity to PARP inhibitors, possibly a null variant)
PALB2 I76Mfs*4
PALB2 I76Yfs*101
PALB2 H130Tfs*47
PALB2 V132Afs*45 (reported in Fanconi anemia by Reid et al. 2007)
PALB2 S172Gfs*4 (Boonen et al. 2019: defective HRR, sensitivity to PARP inhibitors, possibly a null variant)
PALB2 L176Nfs*3
PALB2 L253Yfs26* (reported in Fanconi anemia by Reid et al. 2007)
PALB2 I265Tfs*5
PALB2 N280Tfs*8
PALB2 I281Nfs*2
PALB2 M296*
PALB2 M296Nfs*7
PALB2 S299Yfs*3
PALB2 L304*
PALB2 F404Sfs*7
PALB2 I429Rfs*22
PALB2 H432Ffs*9
PALB2 F440Lfs*12
PALB2 N450Ifs*2
PALB2 P522Qfs*39
PALB2 F606Sfs*10
PALB2 P656Qfs*4
PALB2 E669Gfs*3 (Boonen et al. 2019: defective HRR, sensitivity to PARP inhibitors)
PALB2 D715Efs*2 (Wiltshire et al. 2020: defective HRR)
PALB2 M723Vfs*21
PALB2 R794Sfs*57
PALB2 T799Pfs53* (reported in Fanconi anemia by Reid et al. 2008)
PALB2 F816Sfs*35
PALB2 W877Gfs*12
PALB2 C882Wfs*3 (Boonen et al. 2019: defective HRR, sensitivity to PARP inhibitors)
PALB2 W898Efs*29
PALB2 A935*
PALB2 E956Kfs*6
PALB2 A995Cfs16* (reported in hereditary breast cancer by Rahman et al. 2007)
PALB2 L1006Ffs*5
PALB2 P1009Lfs*6 (Boonen et al. 2019: defective HRR, sensitivity to PARP inhibitors, reduced protein stability)
PALB2 E1010*
PALB2 I1035Mfs*6
PALB2 N1039Ifs2* (reported in Fanconi anemia by Reid et al. 2007 and in hereditary breast cancer by Rahman et al. 2007)
PALB2 K1098Nfs23* (reported in Fanconi anemia by Reid et al. 2007)
PALB2 Y1108Sfs*16 (Wiltshire et al. 2020: defective HRR)
PALB2 G1121Vfs*3 (Wiltshire et al. 2020: defective HRR)
PALB2 G1166Vfs*25 (Wiltshire et al. 2020: defective HRR)
A comprehensive list of variants in the PALB2 gene is provided at the Leiden Open Variation Database (LOVD) (https://databases.lovd.nl/shared/genes/PALB2) (Fokkema et al. 2011).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P38398-1",
"Q13315-1",
"Q92993-1",
"Q06609-1",
"P54132-1",
"P49959-1",
"Q9UQ84-1",
"Q13472-1",
"Q99728-1",
"Q99708-1",
"Q9BX63-1",
"Q92878-1"
],
"evidence": [
{
"id": "R-HSA-9704408",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9704408"
}
]
},
{
"id": "R-HSA-9709571",
"name": "BRCA2 mutants with BRC defects or a defect in the C-terminal RAD51 binding site do not bind RAD51",
"equation": "",
"summary": "BRCA2 contains 8 BRC repeats in its middle region, which are involved in binding to RAD51 at resected DNA double-strand breaks (DSBs) (Bork et al. 1996, Wong et al. 1997, Venkitaraman 2002). Some BRCA2 missense mutations reported in cancer have been shown to impair BRCA2 binding to RAD51.
BRCA2 G1529R mutant, involved in familial breast cancer, has a missense mutation that affects the fourth BRC repeat of BRCA2 (BRC4). The BRC4 construct which harbors the G1529R substitution shows 20-fold reduced binding to RAD51 relative to the wild type BRC4 (Chen et al. 1999). CHEK1 phosphorylation sites are preserved in BRCA2 G1529R mutant, but the phosphorylation is not shown as it has not been tested.
BRCA2 mutant BRCA2 G1529E is annotated as candidate mutant for the loss of RAD51 binding as it has been reported in cancer, is predicted to be pathogenic and involves the same amino acid residue as the functionally characterized BRCA2 G1529R mutant.
The C-terminal RAD51 interaction site, TR2, binds to RAD51 filaments and protects them from disassembly (Davies et al. 2007). TR2 is essential for the replication fork stabilization function of BRCA2 but dispensable for homology-directed repair (Schlacher et al. 2011). BRCA2 S3291A mutant, generated by directed mutagenesis, is unable to bind to RAD51. This mutant has not been reported in cancer but is documented as a BRCA2 allele in the ClinGen Allele Registry (Pawliczek et al. 2018).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P38398-1",
"Q13315-1",
"Q92993-1",
"Q06609-1",
"Q13535-1",
"P54132-1",
"P49959-1",
"Q9UQ84-1",
"Q13472-1",
"Q99728-1",
"Q99708-1",
"Q9BX63-1",
"Q92878-1",
"Q99638-1"
],
"evidence": [
{
"id": "R-HSA-9709571",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9709571"
}
]
},
{
"id": "R-HSA-9709601",
"name": "Defective recruitment of BRCA2 and RAD51 due to loss of BRCA2 function in PALB2 binding",
"equation": "",
"summary": "The extreme N-terminus of BRCA2, involving amino acid residues 10-40, is necessary and sufficient for PALB2 binding (Xia et al. 2006). Several germline BRCA2 missense mutations identified in breast cancer patients map to this region and impair the ability of BRCA2 recombinant constructs that include the first 60 amino acids of BRCA2 to bind to PALB2:
BRCA2 G25R (severely diminished binding to PALB2, Xia et al. 2006)
BRCA2 W31R (complete loss of PALB2 binding, Xia et al. 2006)
BRCA2 W31C (complete loss of PALB2 binding, Xia et al. 2006)
",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P38398-1",
"Q13315-1",
"Q92993-1",
"Q06609-1",
"P54132-1",
"P49959-1",
"Q9UQ84-1",
"Q13472-1",
"Q99728-1",
"Q99708-1",
"Q9BX63-1",
"Q92878-1"
],
"evidence": [
{
"id": "R-HSA-9709601",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9709601"
}
]
},
{
"id": "R-HSA-9853389",
"name": "FIGNL1 binds RAD51",
"equation": "",
"summary": "FIGNL1 strongly binds to RAD51 and localizes to ionizing radiation-induced DNA damage foci. The interaction involves the N-terminal half of FIGNL1, requiring conserved residues 295-344 called FIGNL1's RAD51 binding domain (FRBD). The efficiency of homologous recombination repair (HRR) is impaired in cells with FIGNL1 depletion (Yuan and Chen 2013). The interaction between FIGNL1 and RAD51 is conserved between human and Arabidopsis. The FIGNL1 binding partner FIRRM (also known as Apolo1 or FLIP or C1orf112) does not directly interact with RAD51 but depletion of either FIRRM or FIGNL1 negatively regulates the formation or the turnover of RAD51 foci in Arabidopsis (Fernandes et al. 2018).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q6PIW4-1",
"P38398-1",
"Q13315-1",
"Q92993-1",
"Q06609-1",
"P54132-1",
"P49959-1",
"Q9UQ84-1",
"Q13472-1",
"Q99728-1",
"Q99708-1",
"Q9BX63-1",
"Q92878-1"
],
"evidence": [
{
"id": "R-HSA-9853389",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9853389"
}
]
},
{
"id": "R-HSA-9980006",
"name": "ERCC1:XPF binds DNA DSBs with annealed 3' ssDNA overhangs and displaced flaps generated by SSA",
"equation": "",
"summary": "The endonuclease complex ERCC1:XPF (ERCC1:ERCC4) is recruited to single strand annealing (SSA) sites of DNA double-strand break (DSB) repair through direct interaction between XPF (ERCC4) and RAD52 (Motycka et al. 2004).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92889-1",
"P38398-1",
"Q13315-1",
"Q92993-1",
"Q06609-1",
"Q13535-1",
"P54132-1",
"P49959-1",
"Q9UQ84-1",
"Q13472-1",
"Q99728-1",
"Q99708-1",
"Q9BX63-1",
"Q92878-1",
"Q99638-1"
],
"evidence": [
{
"id": "R-HSA-9980006",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9980006"
}
]
},
{
"id": "R-HSA-9980021",
"name": "LIG1 binds SSA sites",
"equation": "",
"summary": "A DNA ligase, most likely LIG1 (DNA ligase I), ligates single strand breaks (SSBs) remaining after RAD52-mediated single strand annealing (SSA) of resected DNA double-strand breaks (DSBs) and cleavage of displaced flaps by ERCC1:XPF (ERCC1:ERCC4). LIG4 is not involved in SSA (Maruta et al. 2024), and the activity of LIG3 is inhibited in the presence of RAD51 (Batenburg et al. 2023). Therefore, the only remaining candidate DNA ligase is LIG1. While LIG1 does not require RPA to bind to single-strand breaks in DNA, the RPA complex, which coats long resected ends created during SSA and homologous recombination repair (HRR), greatly stimulates the catalytic activity of LIG1 (Ranalli et al. 2002).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q92889-1",
"P38398-1",
"Q13315-1",
"Q92993-1",
"Q06609-1",
"Q13535-1",
"P54132-1",
"P49959-1",
"Q9UQ84-1",
"Q13472-1",
"P18858-1",
"Q99728-1",
"Q99708-1",
"Q9BX63-1",
"Q92878-1",
"Q99638-1"
],
"evidence": [
{
"id": "R-HSA-9980021",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9980021"
}
]
}
],
"reaction_participants": [
{
"participant_id": "R-ALL-113582",
"participant_name": "ADP [nucleoplasm]",
"crossref": [
{
"id": "C00008",
"database": "COMPOUND",
"url": ""
},
{
"id": "456216",
"database": "ChEBI",
"url": ""
},
{
"id": "ZINC000012360703",
"database": "ZINC",
"url": ""
}
]
},
{
"participant_id": "R-ALL-1638790",
"participant_name": "Sister Chromatid [chromosome]",
"crossref": [
{
"id": "23367",
"database": "ChEBI",
"url": ""
}
]
},
{
"participant_id": "R-ALL-84009",
"participant_name": "ss-gap-reannealed DNA [nucleoplasm]",
"crossref": [
{
"id": "61120",
"database": "ChEBI",
"url": ""
}
]
},
{
"participant_id": "R-HSA-113825",
"participant_name": "p-T68-CHEK2 [nucleoplasm]",
"crossref": [
{
"id": "ENST00000649563",
"database": "ENSEMBL",
"url": ""
},
{
"id": "3I6U",
"database": "PDB",
"url": ""
},
{
"id": "ENSP00000404400",
"database": "ENSEMBL",
"url": ""
},
{
"id": "O96017",
"database": "Pharos - Targets",
"url": ""
},
{
"id": "2YIQ",
"database": "PDB",
"url": ""
},
{
"id": "CHK2_HUMAN",
"database": "ZINC - Investigational",
"url": ""
},
{
"id": "CHEK2",
"database": "Orphanet",
"url": ""
},
{
"id": "4BDG",
"database": "PDB",
"url": ""
},
{
"id": "ENST00000348295",
"database": "ENSEMBL",
"url": ""
},
{
"id": "2XM8",
"database": "PDB",
"url": ""
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}
]
},
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}
]
}
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},
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}
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},
{
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}
]
}
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}
]
},
{
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}
]
}
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},
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{
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}
]
},
{
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{
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}
]
}
]
},
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}
]
},
{
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{
"id": "O14757",
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}
]
}
]
},
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{
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"activity": "",
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}
]
},
{
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}
]
},
{
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{
"id": "O14874",
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}
]
},
{
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{
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}
]
}
]
},
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{
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{
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}
]
},
{
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{
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}
]
},
{
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}
]
},
{
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}
]
}
]
},
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"ec_number": "2.7.11.1",
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{
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}
]
},
{
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{
"id": "O14936",
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}
]
}
]
},
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{
"ec_number": "2.7.11.1",
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}
]
},
{
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{
"id": "O14965",
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}
]
}
]
},
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{
"ec_number": "2.7.11.1",
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}
]
},
{
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}
]
}
]
},
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{
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}
]
},
{
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}
]
}
]
},
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}
]
},
{
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{
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}
]
}
]
},
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{
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}
]
},
{
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{
"id": "O15264",
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}
]
}
]
},
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{
"id": "O15530",
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}
]
},
{
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{
"id": "O15530",
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}
]
}
]
},
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{
"ec_number": "2.7.11.25",
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}
]
},
{
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{
"id": "O43283",
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}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
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}
]
},
{
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{
"id": "O43293",
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}
]
}
]
},
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{
"ec_number": "2.7.11.25",
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{
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}
]
},
{
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{
"id": "O43318",
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}
]
}
]
},
{
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{
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}
]
},
{
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{
"id": "O43353",
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}
]
},
{
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{
"id": "O43353",
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}
]
}
]
},
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{
"ec_number": "2.7.11.1",
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{
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}
]
},
{
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{
"id": "O43683",
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}
]
}
]
},
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{
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{
"id": "O43781",
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]
},
{
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{
"id": "O43781",
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}
]
}
]
},
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "O60229",
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]
},
{
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{
"id": "O60229",
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}
]
}
]
},
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{
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{
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]
},
{
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{
"id": "O60285",
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}
]
}
]
},
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{
"ec_number": "2.7.11.1",
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{
"id": "O60307",
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]
},
{
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{
"id": "O60307",
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}
]
}
]
},
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{
"ec_number": "2.7.11.1",
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{
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]
},
{
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{
"id": "O60566",
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]
}
]
},
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{
"ec_number": "2.7.11.39",
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{
"id": "O75116",
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]
},
{
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{
"id": "O75116",
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]
}
]
},
{
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{
"ec_number": "1.14.11.69",
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{
"id": "O75164",
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}
]
},
{
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{
"id": "O75164",
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"url": "https://www.uniprot.org/uniprotkb/O75164"
}
]
},
{
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{
"id": "O75164",
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}
]
},
{
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{
"id": "O75164",
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}
]
}
]
},
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{
"ec_number": "2.7.11.1",
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{
"id": "O75385",
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}
]
},
{
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{
"id": "O75385",
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]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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"id": "O75460",
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}
]
},
{
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{
"id": "O75460",
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}
]
},
{
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"evidence": [
{
"id": "O75460",
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}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "O75582",
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}
]
},
{
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{
"id": "O75582",
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]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "O75676",
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]
},
{
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{
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"database": "UniProtKB",
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}
]
}
]
},
{
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{
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{
"id": "O75716",
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"url": "https://www.uniprot.org/uniprotkb/O75716"
}
]
},
{
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{
"id": "O75716",
"database": "UniProtKB",
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}
]
},
{
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"activity": "",
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{
"id": "O75716",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O75716"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "O75716",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O75716"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "O75914",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O75914"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
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{
"id": "O75914",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "O75962",
"database": "UniProtKB",
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}
]
},
{
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"activity": "",
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{
"id": "O75962",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O75962"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.22",
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{
"id": "O76039",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O76039"
}
]
},
{
"ec_number": "2.7.11.22",
"activity": "",
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{
"id": "O76039",
"database": "UniProtKB",
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}
]
}
]
},
{
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"gene_name": "RNF8",
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{
"ec_number": "2.3.2.27",
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{
"id": "O76064",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O76064"
}
]
},
{
"ec_number": "2.3.2.27",
"activity": "",
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{
"id": "O76064",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O76064"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "O94768",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O94768"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "O94768",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O94768"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "O94804",
"database": "UniProtKB",
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}
]
},
{
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"activity": "",
"evidence": [
{
"id": "O94804",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
"ec_number": "2.7.11.13",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "O94806",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O94806"
}
]
},
{
"ec_number": "2.7.11.13",
"activity": "",
"evidence": [
{
"id": "O94806",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O94806"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.22",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "O94921",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O94921"
}
]
},
{
"ec_number": "2.7.11.22",
"activity": "",
"evidence": [
{
"id": "O94921",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O94921"
}
]
}
]
},
{
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{
"ec_number": "1.14.11.66",
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"evidence": [
{
"id": "O94953",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O94953"
}
]
},
{
"ec_number": "1.14.11.66",
"activity": "",
"evidence": [
{
"id": "O94953",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O94953"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.25",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "O95382",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O95382"
}
]
},
{
"ec_number": "2.7.11.25",
"activity": "",
"evidence": [
{
"id": "O95382",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O95382"
}
]
}
]
},
{
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{
"ec_number": "3.1.3.48",
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"evidence": [
{
"id": "O95677",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O95677"
}
]
},
{
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"activity": "",
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{
"id": "O95677",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O95677"
}
]
}
]
},
{
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{
"ec_number": "2.3.2.26",
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{
"id": "O95714",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O95714"
}
]
},
{
"ec_number": "2.3.2.26",
"activity": "",
"evidence": [
{
"id": "O95714",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O95714"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "O95747",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O95747"
}
]
},
{
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"activity": "",
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{
"id": "O95747",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O95747"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "O95819",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O95819"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "O95819",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O95819"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "O95835",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O95835"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "O95835",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O95835"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "O96013",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O96013"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "O96013",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O96013"
}
]
}
]
},
{
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"gene_name": "CHEK2",
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "O96017",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O96017"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "O96017",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O96017"
}
]
}
]
},
{
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{
"ec_number": "2.1.1.357",
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"evidence": [
{
"id": "O96028",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O96028"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "O96028",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/O96028"
}
]
}
]
},
{
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{
"ec_number": "2.7.10.2",
"activity": "L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+).",
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{
"id": "P00519",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P00519"
}
]
},
{
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"activity": "",
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{
"id": "P00519",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P00519"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P00540",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P00540"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "P00540",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P00540"
}
]
}
]
},
{
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"gene_name": "PGK1",
"activity": [
{
"ec_number": "2.7.2.3",
"activity": "(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP.",
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{
"id": "P00558",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P00558"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "P00558",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P00558"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "P00558",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P00558"
}
]
},
{
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"activity": "",
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{
"id": "P00558",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P00558"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "P04049",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P04049"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "P04049",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P04049"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.13",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P05129",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P05129"
}
]
},
{
"ec_number": "2.7.11.13",
"activity": "",
"evidence": [
{
"id": "P05129",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P05129"
}
]
}
]
},
{
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"activity": [
{
"ec_number": "2.7.11.13",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P05771",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P05771"
}
]
},
{
"ec_number": "2.7.11.13",
"activity": "",
"evidence": [
{
"id": "P05771",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P05771"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.22",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P06493",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P06493"
}
]
},
{
"ec_number": "2.7.11.23",
"activity": "[DNA-directed RNA polymerase] + ATP = phospho-[DNA-directed RNA polymerase] + ADP + H(+).",
"evidence": [
{
"id": "P06493",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P06493"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "P06493",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P06493"
}
]
},
{
"ec_number": "2.7.11.22",
"activity": "",
"evidence": [
{
"id": "P06493",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P06493"
}
]
}
]
},
{
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"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "P0C263",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P0C263"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "P0C263",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P0C263"
}
]
}
]
},
{
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"gene_name": "SBK3",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "P0C264",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P0C264"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "P0C264",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P0C264"
}
]
}
]
},
{
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"gene_name": "ARAF",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P10398",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P10398"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "P10398",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P10398"
}
]
}
]
},
{
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"gene_name": "BCR",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P11274",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P11274"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "P11274",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P11274"
}
]
}
]
},
{
"uniprot_ac": "P11309",
"gene_name": "PIM1",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P11309",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P11309"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "P11309",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P11309"
}
]
}
]
},
{
"uniprot_ac": "P11801",
"gene_name": "PSKH1",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P11801",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P11801"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "P11801",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P11801"
}
]
}
]
},
{
"uniprot_ac": "P11802",
"gene_name": "CDK4",
"activity": [
{
"ec_number": "2.7.11.22",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P11802",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P11802"
}
]
},
{
"ec_number": "2.7.11.22",
"activity": "",
"evidence": [
{
"id": "P11802",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P11802"
}
]
}
]
},
{
"uniprot_ac": "P12956",
"gene_name": "XRCC6",
"activity": [
{
"ec_number": "4.2.99.18",
"activity": "2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+).",
"evidence": [
{
"id": "P12956",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P12956"
}
]
},
{
"ec_number": "5.6.2.4",
"activity": "ATP + H2O = ADP + phosphate + H(+).",
"evidence": [
{
"id": "P12956",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P12956"
}
]
},
{
"ec_number": "4.2.99.18",
"activity": "",
"evidence": [
{
"id": "P12956",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P12956"
}
]
},
{
"ec_number": "5.6.2.4",
"activity": "",
"evidence": [
{
"id": "P12956",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P12956"
}
]
}
]
},
{
"uniprot_ac": "P13010",
"gene_name": "XRCC5",
"activity": [
{
"ec_number": "4.2.99.18",
"activity": "2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+).",
"evidence": [
{
"id": "P13010",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P13010"
}
]
},
{
"ec_number": "5.6.2.4",
"activity": "ATP + H2O = ADP + phosphate + H(+).",
"evidence": [
{
"id": "P13010",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P13010"
}
]
},
{
"ec_number": "4.2.99.18",
"activity": "",
"evidence": [
{
"id": "P13010",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P13010"
}
]
},
{
"ec_number": "5.6.2.4",
"activity": "",
"evidence": [
{
"id": "P13010",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P13010"
}
]
}
]
},
{
"uniprot_ac": "P14618",
"gene_name": "PKM",
"activity": [
{
"ec_number": "2.7.10.2",
"activity": "L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P14618",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P14618"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P14618",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P14618"
}
]
},
{
"ec_number": "2.7.1.40",
"activity": "ITP + pyruvate = IDP + phosphoenolpyruvate + H(+).",
"evidence": [
{
"id": "P14618",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P14618"
}
]
},
{
"ec_number": "2.7.1.40",
"activity": "",
"evidence": [
{
"id": "P14618",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P14618"
}
]
}
]
},
{
"uniprot_ac": "P15056",
"gene_name": "BRAF",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P15056",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P15056"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "P15056",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P15056"
}
]
}
]
},
{
"uniprot_ac": "P15531",
"gene_name": "NME1",
"activity": [
{
"ec_number": "3.1.11.-",
"activity": "",
"evidence": [
{
"id": "P15531",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P15531"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P15531",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P15531"
}
]
},
{
"ec_number": "2.7.4.6",
"activity": "UDP + ATP = UTP + ADP.",
"evidence": [
{
"id": "P15531",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P15531"
}
]
},
{
"ec_number": "2.7.13.3",
"activity": "ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.",
"evidence": [
{
"id": "P15531",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P15531"
}
]
},
{
"ec_number": "2.7.4.18",
"activity": "(2E,6E)-farnesyl diphosphate + ATP = (2E,6E)-farnesyl triphosphate + ADP.",
"evidence": [
{
"id": "P15531",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P15531"
}
]
},
{
"ec_number": "3.1.24.-",
"activity": "",
"evidence": [
{
"id": "P15531",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P15531"
}
]
},
{
"ec_number": "2.7.4.6",
"activity": "",
"evidence": [
{
"id": "P15531",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P15531"
}
]
},
{
"ec_number": "2.7.4.18",
"activity": "",
"evidence": [
{
"id": "P15531",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P15531"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "P15531",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P15531"
}
]
}
]
},
{
"uniprot_ac": "P17252",
"gene_name": "PRKCA",
"activity": [
{
"ec_number": "2.7.11.13",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P17252",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P17252"
}
]
},
{
"ec_number": "2.7.11.13",
"activity": "",
"evidence": [
{
"id": "P17252",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P17252"
}
]
}
]
},
{
"uniprot_ac": "P17612",
"gene_name": "PRKACA",
"activity": [
{
"ec_number": "2.7.11.11",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P17612",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P17612"
}
]
},
{
"ec_number": "2.7.11.11",
"activity": "",
"evidence": [
{
"id": "P17612",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P17612"
}
]
}
]
},
{
"uniprot_ac": "P18074",
"gene_name": "ERCC2",
"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.",
"evidence": [
{
"id": "P18074",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P18074"
}
]
},
{
"ec_number": "5.6.2.3",
"activity": "",
"evidence": [
{
"id": "P18074",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P18074"
}
]
}
]
},
{
"uniprot_ac": "P18858",
"gene_name": "LIG1",
"activity": [
{
"ec_number": "6.5.1.1",
"activity": "ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.",
"evidence": [
{
"id": "P18858",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P18858"
}
]
},
{
"ec_number": "6.5.1.1",
"activity": "",
"evidence": [
{
"id": "P18858",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P18858"
}
]
}
]
},
{
"uniprot_ac": "P19447",
"gene_name": "ERCC3",
"activity": [
{
"ec_number": "5.6.2.4",
"activity": "ATP + H2O = ADP + phosphate + H(+).",
"evidence": [
{
"id": "P19447",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P19447"
}
]
},
{
"ec_number": "5.6.2.4",
"activity": "",
"evidence": [
{
"id": "P19447",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P19447"
}
]
}
]
},
{
"uniprot_ac": "P19525",
"gene_name": "EIF2AK2",
"activity": [
{
"ec_number": "2.7.10.2",
"activity": "L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P19525",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P19525"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P19525",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P19525"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "P19525",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P19525"
}
]
},
{
"ec_number": "2.7.10.2",
"activity": "",
"evidence": [
{
"id": "P19525",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P19525"
}
]
}
]
},
{
"uniprot_ac": "P19784",
"gene_name": "CSNK2A2",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P19784",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P19784"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "P19784",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P19784"
}
]
}
]
},
{
"uniprot_ac": "P20794",
"gene_name": "MAK",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P20794",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P20794"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "P20794",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P20794"
}
]
}
]
},
{
"uniprot_ac": "P21127",
"gene_name": "CDK11B",
"activity": [
{
"ec_number": "2.7.11.22",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P21127",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P21127"
}
]
},
{
"ec_number": "2.7.11.23",
"activity": "[DNA-directed RNA polymerase] + ATP = phospho-[DNA-directed RNA polymerase] + ADP + H(+).",
"evidence": [
{
"id": "P21127",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P21127"
}
]
},
{
"ec_number": "2.7.11.23",
"activity": "",
"evidence": [
{
"id": "P21127",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P21127"
}
]
},
{
"ec_number": "2.7.11.22",
"activity": "",
"evidence": [
{
"id": "P21127",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P21127"
}
]
}
]
},
{
"uniprot_ac": "P21675",
"gene_name": "TAF1",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P21675",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P21675"
}
]
},
{
"ec_number": "2.3.1.48",
"activity": "L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+).",
"evidence": [
{
"id": "P21675",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P21675"
}
]
},
{
"ec_number": "2.3.1.48",
"activity": "",
"evidence": [
{
"id": "P21675",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P21675"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "P21675",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P21675"
}
]
}
]
},
{
"uniprot_ac": "P22612",
"gene_name": "PRKACG",
"activity": [
{
"ec_number": "2.7.11.11",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P22612",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P22612"
}
]
},
{
"ec_number": "2.7.11.11",
"activity": "",
"evidence": [
{
"id": "P22612",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P22612"
}
]
}
]
},
{
"uniprot_ac": "P22694",
"gene_name": "PRKACB",
"activity": [
{
"ec_number": "2.7.11.11",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P22694",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P22694"
}
]
},
{
"ec_number": "2.7.11.11",
"activity": "",
"evidence": [
{
"id": "P22694",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P22694"
}
]
}
]
},
{
"uniprot_ac": "P23443",
"gene_name": "RPS6KB1",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P23443",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P23443"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "P23443",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P23443"
}
]
}
]
},
{
"uniprot_ac": "P24723",
"gene_name": "PRKCH",
"activity": [
{
"ec_number": "2.7.11.13",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P24723",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P24723"
}
]
},
{
"ec_number": "2.7.11.13",
"activity": "",
"evidence": [
{
"id": "P24723",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P24723"
}
]
}
]
},
{
"uniprot_ac": "P24928",
"gene_name": "POLR2A",
"activity": [
{
"ec_number": "3.1.13.-",
"activity": "",
"evidence": [
{
"id": "P24928",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P24928"
}
]
},
{
"ec_number": "2.7.7.48",
"activity": "RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate.",
"evidence": [
{
"id": "P24928",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P24928"
}
]
},
{
"ec_number": "2.7.7.6",
"activity": "RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate.",
"evidence": [
{
"id": "P24928",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P24928"
}
]
},
{
"ec_number": "2.7.7.6",
"activity": "",
"evidence": [
{
"id": "P24928",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P24928"
}
]
}
]
},
{
"uniprot_ac": "P24941",
"gene_name": "CDK2",
"activity": [
{
"ec_number": "2.7.11.22",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P24941",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P24941"
}
]
},
{
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{
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}
]
}
]
},
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{
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{
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}
]
},
{
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}
]
}
]
},
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{
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{
"id": "P27448",
"database": "UniProtKB",
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}
]
},
{
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{
"id": "P27448",
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}
]
}
]
},
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{
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}
]
},
{
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}
]
},
{
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{
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}
]
}
]
},
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{
"ec_number": "2.7.11.24",
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}
]
},
{
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{
"id": "P28482",
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}
]
}
]
},
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{
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}
]
},
{
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}
]
},
{
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{
"id": "P30876",
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}
]
},
{
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{
"id": "P30876",
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}
]
}
]
},
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{
"ec_number": "2.7.11.24",
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}
]
},
{
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{
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}
]
}
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{
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}
]
},
{
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{
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}
]
}
]
},
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}
]
},
{
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{
"id": "P31751",
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}
]
}
]
},
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}
]
},
{
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{
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}
]
},
{
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{
"id": "P33076",
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}
]
}
]
},
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{
"id": "P33981",
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}
]
},
{
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{
"id": "P33981",
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}
]
}
]
},
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{
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}
]
},
{
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{
"id": "P36507",
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}
]
}
]
},
{
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{
"ec_number": "2.3.2.27",
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{
"id": "P38398",
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}
]
},
{
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{
"id": "P38398",
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}
]
}
]
},
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{
"ec_number": "2.7.11.25",
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{
"id": "P41279",
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}
]
},
{
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{
"id": "P41279",
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}
]
}
]
},
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{
"ec_number": "2.7.11.13",
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{
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}
]
},
{
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{
"id": "P41743",
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}
]
}
]
},
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{
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}
]
},
{
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{
"id": "P42336",
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}
]
},
{
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{
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"url": "https://www.uniprot.org/uniprotkb/P42336"
}
]
},
{
"ec_number": "2.7.1.137",
"activity": "",
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{
"id": "P42336",
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}
]
},
{
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{
"id": "P42336",
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}
]
}
]
},
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{
"ec_number": "2.7.11.1",
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}
]
},
{
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{
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}
]
},
{
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{
"id": "P42338",
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}
]
},
{
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{
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}
]
},
{
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{
"id": "P42338",
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}
]
}
]
},
{
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{
"ec_number": "2.7.10.2",
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{
"id": "P42345",
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}
]
},
{
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{
"id": "P42345",
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}
]
},
{
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"evidence": [
{
"id": "P42345",
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}
]
}
]
},
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{
"ec_number": "2.7.11.24",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "P45983",
"database": "UniProtKB",
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}
]
},
{
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"activity": "",
"evidence": [
{
"id": "P45983",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
"ec_number": "2.7.11.24",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "P45984",
"database": "UniProtKB",
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}
]
},
{
"ec_number": "2.7.11.24",
"activity": "",
"evidence": [
{
"id": "P45984",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P45984"
}
]
}
]
},
{
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{
"ec_number": "2.7.12.2",
"activity": "L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P45985",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P45985"
}
]
},
{
"ec_number": "2.7.12.2",
"activity": "",
"evidence": [
{
"id": "P45985",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P45985"
}
]
}
]
},
{
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{
"ec_number": "2.7.12.2",
"activity": "L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P46734",
"database": "UniProtKB",
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}
]
},
{
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"activity": "",
"evidence": [
{
"id": "P46734",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P46734"
}
]
}
]
},
{
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{
"ec_number": "3.4.19.-",
"activity": "",
"evidence": [
{
"id": "P46736",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P46736"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P48729",
"database": "UniProtKB",
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}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "P48729",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "P48730",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P48730"
}
]
},
{
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"activity": "L-seryl-[tau protein] + ATP = O-phospho-L-seryl-[tau protein] + ADP + H(+).",
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{
"id": "P48730",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P48730"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "P48730",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P48730"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P48736",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P48736"
}
]
},
{
"ec_number": "2.7.1.153",
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{
"id": "P48736",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P48736"
}
]
},
{
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{
"id": "P48736",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P48736"
}
]
},
{
"ec_number": "2.7.1.154",
"activity": "a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) + ADP + H(+).",
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{
"id": "P48736",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P48736"
}
]
},
{
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{
"id": "P48736",
"database": "UniProtKB",
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}
]
},
{
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"activity": "",
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}
]
},
{
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{
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}
]
}
]
},
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{
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{
"id": "P49137",
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}
]
},
{
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{
"id": "P49137",
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}
]
}
]
},
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{
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{
"id": "P49336",
"database": "UniProtKB",
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}
]
},
{
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{
"id": "P49336",
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}
]
},
{
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{
"id": "P49336",
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}
]
},
{
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"activity": "",
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{
"id": "P49336",
"database": "UniProtKB",
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}
]
}
]
},
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{
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{
"id": "P49674",
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}
]
},
{
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{
"id": "P49674",
"database": "UniProtKB",
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}
]
}
]
},
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{
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{
"id": "P49759",
"database": "UniProtKB",
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}
]
},
{
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"activity": "",
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{
"id": "P49759",
"database": "UniProtKB",
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}
]
}
]
},
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{
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{
"id": "P49760",
"database": "UniProtKB",
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}
]
},
{
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"activity": "",
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{
"id": "P49760",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P49760"
}
]
}
]
},
{
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{
"ec_number": "2.7.12.1",
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{
"id": "P49761",
"database": "UniProtKB",
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}
]
},
{
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"activity": "",
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{
"id": "P49761",
"database": "UniProtKB",
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}
]
}
]
},
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{
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{
"id": "P49840",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P49840"
}
]
},
{
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"evidence": [
{
"id": "P49840",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P49840"
}
]
},
{
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"activity": "",
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{
"id": "P49840",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P49840"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
"id": "P49841",
"database": "UniProtKB",
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}
]
},
{
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{
"id": "P49841",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P49841"
}
]
},
{
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"activity": "",
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{
"id": "P49841",
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}
]
},
{
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{
"id": "P49841",
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}
]
},
{
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"activity": "",
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{
"id": "P49841",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P49841"
}
]
}
]
},
{
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{
"ec_number": "3.1.-.-",
"activity": "",
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{
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"database": "UniProtKB",
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}
]
}
]
},
{
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{
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{
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}
]
},
{
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{
"id": "P50613",
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}
]
},
{
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{
"id": "P50613",
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"url": "https://www.uniprot.org/uniprotkb/P50613"
}
]
},
{
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{
"id": "P50613",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P50613"
}
]
},
{
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{
"id": "P50613",
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"url": "https://www.uniprot.org/uniprotkb/P50613"
}
]
},
{
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{
"id": "P50613",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P50613"
}
]
}
]
},
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{
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{
"id": "P50750",
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}
]
},
{
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{
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}
]
},
{
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{
"id": "P50750",
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"url": "https://www.uniprot.org/uniprotkb/P50750"
}
]
},
{
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{
"id": "P50750",
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}
]
}
]
},
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{
"ec_number": "2.7.11.1",
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{
"id": "P51617",
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}
]
},
{
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{
"id": "P51617",
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"url": "https://www.uniprot.org/uniprotkb/P51617"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
"id": "P51812",
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"url": "https://www.uniprot.org/uniprotkb/P51812"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "P51812",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P51812"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
"id": "P51817",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P51817"
}
]
},
{
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{
"id": "P51817",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "P51955",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P51955"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "P51955",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P51955"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "P51956",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P51956"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "P51956",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P51956"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "P51957",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P51957"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "P51957",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P51957"
}
]
}
]
},
{
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{
"ec_number": "2.7.12.2",
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{
"id": "P52564",
"database": "UniProtKB",
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}
]
},
{
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"activity": "",
"evidence": [
{
"id": "P52564",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P52564"
}
]
}
]
},
{
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{
"ec_number": "3.1.3.16",
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"evidence": [
{
"id": "P53041",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P53041"
}
]
},
{
"ec_number": "3.1.3.16",
"activity": "",
"evidence": [
{
"id": "P53041",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P53041"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.21",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "P53350",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P53350"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "P53350",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P53350"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
"id": "P53355",
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"url": "https://www.uniprot.org/uniprotkb/P53355"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "P53355",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "P53667",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P53667"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "P53667",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P53667"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "P53671",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P53671"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "P53671",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P53671"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.24",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "P53778",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P53778"
}
]
},
{
"ec_number": "2.7.11.24",
"activity": "",
"evidence": [
{
"id": "P53778",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P53778"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.24",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "P53779",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P53779"
}
]
},
{
"ec_number": "2.7.11.24",
"activity": "",
"evidence": [
{
"id": "P53779",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P53779"
}
]
}
]
},
{
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{
"ec_number": "5.6.2.4",
"activity": "ATP + H2O = ADP + phosphate + H(+).",
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{
"id": "P54132",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P54132"
}
]
},
{
"ec_number": "5.6.2.4",
"activity": "",
"evidence": [
{
"id": "P54132",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P54132"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "P54646",
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"url": "https://www.uniprot.org/uniprotkb/P54646"
}
]
},
{
"ec_number": "2.7.11.31",
"activity": "L-seryl-[acetyl-CoA carboxylase] + ATP = O-phospho-L-seryl-[acetyl-CoA carboxylase] + ADP + H(+).",
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{
"id": "P54646",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P54646"
}
]
},
{
"ec_number": "2.7.11.1",
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{
"id": "P54646",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P54646"
}
]
}
]
},
{
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"activity": [
{
"ec_number": "2.7.11.1",
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{
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"url": "https://www.uniprot.org/uniprotkb/P57058"
}
]
},
{
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{
"id": "P57058",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
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"database": "UniProtKB",
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}
]
},
{
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{
"id": "P57059",
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}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "P57078",
"database": "UniProtKB",
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}
]
},
{
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{
"id": "P57078",
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}
]
}
]
},
{
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{
"ec_number": "2.3.2.23",
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"evidence": [
{
"id": "P61088",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P61088"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "P61088",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P61088"
}
]
}
]
},
{
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{
"ec_number": "2.3.2.-",
"activity": "",
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{
"id": "P63279",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P63279"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
"id": "P68400",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P68400"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "P68400",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P68400"
}
]
}
]
},
{
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{
"ec_number": "2.3.2.27",
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"evidence": [
{
"id": "P78317",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P78317"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "P78317",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P78317"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
"id": "P78362",
"database": "UniProtKB",
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}
]
},
{
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"activity": "",
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{
"id": "P78362",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
"id": "P78368",
"database": "UniProtKB",
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}
]
},
{
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"activity": "",
"evidence": [
{
"id": "P78368",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P78368"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
"id": "P78527",
"database": "UniProtKB",
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}
]
},
{
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"activity": "",
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{
"id": "P78527",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P78527"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.25",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
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"database": "UniProtKB",
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}
]
},
{
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"activity": "",
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{
"id": "P80192",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/P80192"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.22",
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"database": "UniProtKB",
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}
]
},
{
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"activity": "",
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{
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"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q00526"
}
]
}
]
},
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{
"ec_number": "2.7.11.22",
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"database": "UniProtKB",
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}
]
},
{
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"activity": "",
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{
"id": "Q00532",
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}
]
}
]
},
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{
"ec_number": "2.7.11.22",
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"id": "Q00534",
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}
]
},
{
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{
"id": "Q00534",
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}
]
}
]
},
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{
"ec_number": "2.7.11.1",
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}
]
},
{
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"activity": "",
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{
"id": "Q00535",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q00535"
}
]
}
]
},
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{
"ec_number": "2.7.11.22",
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{
"id": "Q00536",
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}
]
},
{
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"activity": "",
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{
"id": "Q00536",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
"ec_number": "2.7.11.22",
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{
"id": "Q00537",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q00537"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "Q00537",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q00537"
}
]
}
]
},
{
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{
"ec_number": "2.3.2.27",
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{
"id": "Q00987",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q00987"
}
]
},
{
"ec_number": "2.3.2.27",
"activity": "",
"evidence": [
{
"id": "Q00987",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q00987"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q02156",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q02156"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "Q02156",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q02156"
}
]
},
{
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"evidence": [
{
"id": "Q02156",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q02156"
}
]
},
{
"ec_number": "2.7.11.13",
"activity": "",
"evidence": [
{
"id": "Q02156",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q02156"
}
]
}
]
},
{
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{
"ec_number": "2.7.12.2",
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"evidence": [
{
"id": "Q02750",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q02750"
}
]
},
{
"ec_number": "2.7.12.2",
"activity": "",
"evidence": [
{
"id": "Q02750",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q02750"
}
]
}
]
},
{
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"activity": [
{
"ec_number": "2.7.11.25",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q02779",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q02779"
}
]
},
{
"ec_number": "2.7.11.25",
"activity": "",
"evidence": [
{
"id": "Q02779",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q02779"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.13",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q04759",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q04759"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "Q04759",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q04759"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q05513",
"database": "UniProtKB",
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}
]
},
{
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"activity": "",
"evidence": [
{
"id": "Q05513",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q05513"
}
]
},
{
"ec_number": "2.7.11.13",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q05513",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q05513"
}
]
},
{
"ec_number": "2.7.11.13",
"activity": "",
"evidence": [
{
"id": "Q05513",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q05513"
}
]
}
]
},
{
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{
"ec_number": "2.7.10.2",
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{
"id": "Q05655",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q05655"
}
]
},
{
"ec_number": "2.7.11.13",
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"evidence": [
{
"id": "Q05655",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q05655"
}
]
},
{
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"evidence": [
{
"id": "Q05655",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q05655"
}
]
}
]
},
{
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"gene_name": "RAD51",
"activity": [
{
"ec_number": "3.6.4.-",
"activity": "",
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{
"id": "Q06609",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q06609"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.22",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q07002",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q07002"
}
]
},
{
"ec_number": "2.7.11.22",
"activity": "",
"evidence": [
{
"id": "Q07002",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q07002"
}
]
}
]
},
{
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"activity": [
{
"ec_number": "2.7.7.7",
"activity": "DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate.",
"evidence": [
{
"id": "Q07864",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q07864"
}
]
},
{
"ec_number": "2.7.7.7",
"activity": "",
"evidence": [
{
"id": "Q07864",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q07864"
}
]
},
{
"ec_number": "3.1.11.-",
"activity": "",
"evidence": [
{
"id": "Q07864",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q07864"
}
]
}
]
},
{
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{
"ec_number": "2.7.10.2",
"activity": "L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q07912",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q07912"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q07912",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q07912"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
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{
"id": "Q07912",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q07912"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "Q07912",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q07912"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q09013",
"database": "UniProtKB",
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}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
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{
"id": "Q09013",
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"url": "https://www.uniprot.org/uniprotkb/Q09013"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q12851",
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}
]
},
{
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{
"id": "Q12851",
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}
]
}
]
},
{
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{
"ec_number": "2.7.11.25",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q12852",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q12852"
}
]
},
{
"ec_number": "2.7.11.25",
"activity": "",
"evidence": [
{
"id": "Q12852",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q12852"
}
]
}
]
},
{
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"gene_name": "STK4",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q13043",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13043"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "Q13043",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13043"
}
]
}
]
},
{
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"gene_name": "PRKAA1",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q13131",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13131"
}
]
},
{
"ec_number": "2.7.11.26",
"activity": "L-seryl-[tau protein] + ATP = O-phospho-L-seryl-[tau protein] + ADP + H(+).",
"evidence": [
{
"id": "Q13131",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13131"
}
]
},
{
"ec_number": "2.7.11.31",
"activity": "L-seryl-[acetyl-CoA carboxylase] + ATP = O-phospho-L-seryl-[acetyl-CoA carboxylase] + ADP + H(+).",
"evidence": [
{
"id": "Q13131",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13131"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "Q13131",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13131"
}
]
}
]
},
{
"uniprot_ac": "Q13153",
"gene_name": "PAK1",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q13153",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13153"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "Q13153",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13153"
}
]
}
]
},
{
"uniprot_ac": "Q13163",
"gene_name": "MAP2K5",
"activity": [
{
"ec_number": "2.7.12.2",
"activity": "L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q13163",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13163"
}
]
},
{
"ec_number": "2.7.12.2",
"activity": "",
"evidence": [
{
"id": "Q13163",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13163"
}
]
}
]
},
{
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"gene_name": "MAPK7",
"activity": [
{
"ec_number": "2.7.11.24",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q13164",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13164"
}
]
},
{
"ec_number": "2.7.11.24",
"activity": "",
"evidence": [
{
"id": "Q13164",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13164"
}
]
}
]
},
{
"uniprot_ac": "Q13177",
"gene_name": "PAK2",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q13177",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13177"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "Q13177",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13177"
}
]
}
]
},
{
"uniprot_ac": "Q13188",
"gene_name": "STK3",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q13188",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13188"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "Q13188",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13188"
}
]
}
]
},
{
"uniprot_ac": "Q13232",
"gene_name": "NME3",
"activity": [
{
"ec_number": "2.7.4.6",
"activity": "UDP + ATP = UTP + ADP.",
"evidence": [
{
"id": "Q13232",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13232"
}
]
},
{
"ec_number": "2.7.4.6",
"activity": "",
"evidence": [
{
"id": "Q13232",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13232"
}
]
}
]
},
{
"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/uniprotkb/Q13233"
}
]
},
{
"ec_number": "2.7.11.25",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q13233",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13233"
}
]
},
{
"ec_number": "2.7.11.25",
"activity": "",
"evidence": [
{
"id": "Q13233",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13233"
}
]
}
]
},
{
"uniprot_ac": "Q13237",
"gene_name": "PRKG2",
"activity": [
{
"ec_number": "2.7.11.12",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q13237",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13237"
}
]
},
{
"ec_number": "2.7.11.12",
"activity": "",
"evidence": [
{
"id": "Q13237",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13237"
}
]
}
]
},
{
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"gene_name": "ATM",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q13315",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13315"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "Q13315",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13315"
}
]
}
]
},
{
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"gene_name": "ROCK1",
"activity": [
{
"ec_number": "2.7.11.39",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q13464",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13464"
}
]
},
{
"ec_number": "2.7.11.39",
"activity": "",
"evidence": [
{
"id": "Q13464",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13464"
}
]
}
]
},
{
"uniprot_ac": "Q13472",
"gene_name": "TOP3A",
"activity": [
{
"ec_number": "5.6.2.1",
"activity": "ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.",
"evidence": [
{
"id": "Q13472",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13472"
}
]
},
{
"ec_number": "5.6.2.1",
"activity": "",
"evidence": [
{
"id": "Q13472",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13472"
}
]
}
]
},
{
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"gene_name": "PRP4K",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q13523",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13523"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "Q13523",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13523"
}
]
}
]
},
{
"uniprot_ac": "Q13535",
"gene_name": "ATR",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q13535",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13535"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "Q13535",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13535"
}
]
}
]
},
{
"uniprot_ac": "Q13546",
"gene_name": "RIPK1",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q13546",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13546"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "Q13546",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13546"
}
]
}
]
},
{
"uniprot_ac": "Q13554",
"gene_name": "CAMK2B",
"activity": [
{
"ec_number": "2.7.11.17",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q13554",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13554"
}
]
},
{
"ec_number": "2.7.11.17",
"activity": "",
"evidence": [
{
"id": "Q13554",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13554"
}
]
}
]
},
{
"uniprot_ac": "Q13555",
"gene_name": "CAMK2G",
"activity": [
{
"ec_number": "2.7.11.17",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q13555",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13555"
}
]
},
{
"ec_number": "2.7.11.17",
"activity": "",
"evidence": [
{
"id": "Q13555",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13555"
}
]
}
]
},
{
"uniprot_ac": "Q13557",
"gene_name": "CAMK2D",
"activity": [
{
"ec_number": "2.7.11.17",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q13557",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13557"
}
]
},
{
"ec_number": "2.7.11.17",
"activity": "",
"evidence": [
{
"id": "Q13557",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13557"
}
]
}
]
},
{
"uniprot_ac": "Q13627",
"gene_name": "DYRK1A",
"activity": [
{
"ec_number": "2.7.11.23",
"activity": "[DNA-directed RNA polymerase] + ATP = phospho-[DNA-directed RNA polymerase] + ADP + H(+).",
"evidence": [
{
"id": "Q13627",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13627"
}
]
},
{
"ec_number": "2.7.12.1",
"activity": "L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q13627",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13627"
}
]
},
{
"ec_number": "2.7.11.23",
"activity": "",
"evidence": [
{
"id": "Q13627",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13627"
}
]
},
{
"ec_number": "2.7.12.1",
"activity": "",
"evidence": [
{
"id": "Q13627",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13627"
}
]
}
]
},
{
"uniprot_ac": "Q13976",
"gene_name": "PRKG1",
"activity": [
{
"ec_number": "2.7.11.12",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q13976",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13976"
}
]
},
{
"ec_number": "2.7.11.12",
"activity": "",
"evidence": [
{
"id": "Q13976",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q13976"
}
]
}
]
},
{
"uniprot_ac": "Q14004",
"gene_name": "CDK13",
"activity": [
{
"ec_number": "2.7.11.22",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q14004",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q14004"
}
]
},
{
"ec_number": "2.7.11.23",
"activity": "[DNA-directed RNA polymerase] + ATP = phospho-[DNA-directed RNA polymerase] + ADP + H(+).",
"evidence": [
{
"id": "Q14004",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q14004"
}
]
},
{
"ec_number": "2.7.11.22",
"activity": "",
"evidence": [
{
"id": "Q14004",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q14004"
}
]
},
{
"ec_number": "2.7.11.23",
"activity": "",
"evidence": [
{
"id": "Q14004",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q14004"
}
]
},
{
"ec_number": "2.7.11.24",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q14004",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q14004"
}
]
},
{
"ec_number": "2.7.11.24",
"activity": "",
"evidence": [
{
"id": "Q14004",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q14004"
}
]
}
]
},
{
"uniprot_ac": "Q14012",
"gene_name": "CAMK1",
"activity": [
{
"ec_number": "2.7.11.17",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q14012",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q14012"
}
]
},
{
"ec_number": "2.7.11.17",
"activity": "",
"evidence": [
{
"id": "Q14012",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q14012"
}
]
}
]
},
{
"uniprot_ac": "Q14296",
"gene_name": "FASTK",
"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q14296",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q14296"
}
]
},
{
"ec_number": "2.7.11.8",
"activity": "L-seryl-[Fas-activated protein] + ATP = O-phospho-L-seryl-[Fas-activated protein] + ADP + H(+).",
"evidence": [
{
"id": "Q14296",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q14296"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "Q14296",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q14296"
}
]
},
{
"ec_number": "2.7.11.8",
"activity": "",
"evidence": [
{
"id": "Q14296",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q14296"
}
]
}
]
},
{
"uniprot_ac": "Q14565",
"gene_name": "DMC1",
"activity": [
{
"ec_number": "3.6.4.-",
"activity": "",
"evidence": [
{
"id": "Q14565",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q14565"
}
]
}
]
},
{
"uniprot_ac": "Q14680",
"gene_name": "MELK",
"activity": [
{
"ec_number": "2.7.10.2",
"activity": "L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q14680",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q14680"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q14680",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q14680"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "Q14680",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q14680"
}
]
}
]
},
{
"uniprot_ac": "Q15131",
"gene_name": "CDK10",
"activity": [
{
"ec_number": "2.7.11.22",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q15131",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q15131"
}
]
},
{
"ec_number": "2.7.11.22",
"activity": "",
"evidence": [
{
"id": "Q15131",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q15131"
}
]
}
]
},
{
"uniprot_ac": "Q15139",
"gene_name": "PRKD1",
"activity": [
{
"ec_number": "2.7.11.13",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q15139",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q15139"
}
]
},
{
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}
]
}
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},
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},
{
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}
]
}
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}
]
},
{
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}
]
}
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},
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]
},
{
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}
]
}
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},
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{
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]
},
{
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}
]
}
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{
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}
]
},
{
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}
]
}
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]
},
{
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}
]
}
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]
},
{
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}
]
}
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]
},
{
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}
]
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]
},
{
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}
]
}
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},
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]
},
{
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]
}
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}
]
},
{
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}
]
}
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},
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}
]
},
{
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{
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}
]
}
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},
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]
},
{
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{
"id": "Q16584",
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}
]
}
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},
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]
},
{
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]
}
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{
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]
},
{
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]
}
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},
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{
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]
},
{
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]
},
{
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{
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]
},
{
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]
}
]
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{
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]
},
{
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{
"id": "Q16822",
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}
]
},
{
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{
"id": "Q16822",
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]
}
]
},
{
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{
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]
}
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},
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]
},
{
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}
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},
{
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}
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},
{
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{
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{
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},
{
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]
},
{
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},
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]
},
{
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]
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},
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]
},
{
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]
},
{
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]
}
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},
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]
},
{
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]
}
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},
{
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},
{
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]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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]
},
{
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]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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"id": "Q5VT25",
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]
},
{
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"id": "Q5VT25",
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]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
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]
},
{
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]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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"id": "Q6DT37",
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]
},
{
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{
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]
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]
},
{
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}
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}
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{
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}
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}
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{
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}
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{
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}
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{
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}
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},
{
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}
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{
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}
]
}
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{
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}
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{
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}
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]
},
{
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]
}
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{
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}
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{
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}
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},
{
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}
]
}
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{
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}
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]
},
{
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{
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{
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{
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}
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{
"ec_number": "2.7.11.1",
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]
},
{
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{
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}
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"ec_number": "2.3.2.27",
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{
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},
{
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]
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{
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{
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]
},
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}
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]
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{
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{
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{
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]
}
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]
},
{
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]
}
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},
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]
},
{
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{
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]
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]
},
{
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{
"id": "Q8WXR4",
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]
},
{
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{
"id": "Q8WXR4",
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]
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},
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"ec_number": "2.7.11.1",
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{
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{
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{
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}
]
},
{
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{
"id": "Q99502",
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}
]
},
{
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{
"id": "Q99502",
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}
]
},
{
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{
"id": "Q99502",
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}
]
}
]
},
{
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{
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{
"id": "Q99504",
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}
]
},
{
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{
"id": "Q99504",
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}
]
}
]
},
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{
"ec_number": "2.7.11.25",
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{
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}
]
},
{
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{
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}
]
}
]
},
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{
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}
]
},
{
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{
"id": "Q99570",
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}
]
}
]
},
{
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{
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{
"id": "Q99638",
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}
]
},
{
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{
"id": "Q99638",
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}
]
}
]
},
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{
"id": "Q99640",
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}
]
},
{
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{
"id": "Q99640",
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}
]
}
]
},
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{
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}
]
},
{
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}
]
}
]
},
{
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{
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}
]
}
]
},
{
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{
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{
"id": "Q99728",
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}
]
},
{
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{
"id": "Q99728",
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}
]
}
]
},
{
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{
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}
]
},
{
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{
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}
]
}
]
},
{
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]
},
{
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{
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}
]
}
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},
{
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{
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}
]
}
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},
{
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]
},
{
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]
}
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},
{
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{
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]
},
{
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},
{
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{
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]
}
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},
{
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{
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]
},
{
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{
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}
]
}
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},
{
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{
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]
},
{
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{
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}
]
}
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},
{
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{
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]
},
{
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{
"id": "Q9BWU1",
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}
]
}
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},
{
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{
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{
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]
},
{
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{
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}
]
}
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},
{
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{
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]
},
{
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{
"id": "Q9BX84",
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]
}
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},
{
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{
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]
},
{
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{
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]
}
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},
{
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{
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]
},
{
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{
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]
}
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},
{
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{
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]
},
{
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{
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]
}
]
},
{
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{
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]
},
{
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{
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]
}
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},
{
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{
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]
},
{
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{
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]
}
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},
{
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{
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]
},
{
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]
}
]
},
{
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{
"ec_number": "2.7.11.13",
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]
},
{
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{
"id": "Q9BZL6",
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]
}
]
},
{
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{
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]
},
{
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]
}
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},
{
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]
},
{
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]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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]
},
{
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]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
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]
},
{
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{
"id": "Q9H2G2",
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]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
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]
},
{
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{
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]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
"id": "Q9H2X6",
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]
},
{
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{
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}
]
}
]
},
{
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{
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{
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}
]
},
{
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"activity": "",
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{
"id": "Q9H422",
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"url": "https://www.uniprot.org/uniprotkb/Q9H422"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
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"url": "https://www.uniprot.org/uniprotkb/Q9H4A3"
}
]
},
{
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{
"id": "Q9H4A3",
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}
]
}
]
},
{
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{
"ec_number": "2.7.11.21",
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{
"id": "Q9H4B4",
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"url": "https://www.uniprot.org/uniprotkb/Q9H4B4"
}
]
},
{
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"activity": "",
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{
"id": "Q9H4B4",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9H4B4"
}
]
}
]
},
{
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{
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{
"id": "Q9HAZ1",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9HAZ1"
}
]
},
{
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{
"id": "Q9HAZ1",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
"ec_number": "3.4.21.-",
"activity": "",
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{
"id": "Q9HB75",
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}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
"id": "Q9HBH9",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9HBH9"
}
]
},
{
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"activity": "",
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{
"id": "Q9HBH9",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
"id": "Q9HBY8",
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}
]
},
{
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"evidence": [
{
"id": "Q9HBY8",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9HBY8"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.34",
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{
"id": "Q9HC98",
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}
]
},
{
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{
"id": "Q9HC98",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
"id": "Q9HCP0",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9HCP0"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "Q9HCP0",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9HCP0"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q9NQU5",
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"url": "https://www.uniprot.org/uniprotkb/Q9NQU5"
}
]
},
{
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{
"id": "Q9NQU5",
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}
]
}
]
},
{
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{
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{
"id": "Q9NR20",
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}
]
},
{
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{
"id": "Q9NR20",
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}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
"id": "Q9NRH2",
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}
]
},
{
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{
"id": "Q9NRH2",
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"url": "https://www.uniprot.org/uniprotkb/Q9NRH2"
}
]
}
]
},
{
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{
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{
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}
]
},
{
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{
"id": "Q9NRM7",
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}
]
}
]
},
{
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{
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{
"id": "Q9NRP7",
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}
]
},
{
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{
"id": "Q9NRP7",
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}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
"id": "Q9NSY1",
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}
]
},
{
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"activity": "",
"evidence": [
{
"id": "Q9NSY1",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9NSY1"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
"id": "Q9NWZ3",
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}
]
},
{
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{
"id": "Q9NWZ3",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
"id": "Q9NY57",
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}
]
},
{
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{
"id": "Q9NY57",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
"ec_number": "2.7.11.25",
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{
"id": "Q9NYL2",
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"url": "https://www.uniprot.org/uniprotkb/Q9NYL2"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "Q9NYL2",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9NYL2"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.22",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q9NYV4",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9NYV4"
}
]
},
{
"ec_number": "2.7.11.23",
"activity": "[DNA-directed RNA polymerase] + ATP = phospho-[DNA-directed RNA polymerase] + ADP + H(+).",
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{
"id": "Q9NYV4",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9NYV4"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "Q9NYV4",
"database": "UniProtKB",
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}
]
},
{
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"activity": "",
"evidence": [
{
"id": "Q9NYV4",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9NYV4"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.21",
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{
"id": "Q9NYY3",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9NYY3"
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]
},
{
"ec_number": "2.7.11.21",
"activity": "",
"evidence": [
{
"id": "Q9NYY3",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9NYY3"
}
]
}
]
},
{
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"gene_name": "RTEL1",
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{
"ec_number": "5.6.2.-",
"activity": "",
"evidence": [
{
"id": "Q9NZ71",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9NZ71"
}
]
}
]
},
{
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{
"ec_number": "2.7.10.2",
"activity": "L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+).",
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{
"id": "Q9NZJ5",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9NZJ5"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q9NZJ5",
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}
]
},
{
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{
"id": "Q9NZJ5",
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"url": "https://www.uniprot.org/uniprotkb/Q9NZJ5"
}
]
},
{
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"activity": "",
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{
"id": "Q9NZJ5",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9NZJ5"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q9P0L2",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9P0L2"
}
]
},
{
"ec_number": "2.7.11.26",
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{
"id": "Q9P0L2",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9P0L2"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "Q9P0L2",
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]
},
{
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{
"id": "Q9P0L2",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9P0L2"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q9P1W9",
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]
},
{
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{
"id": "Q9P1W9",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9P1W9"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q9P286",
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]
},
{
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{
"id": "Q9P286",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9P286"
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]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q9P289",
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]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "Q9P289",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9P289"
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]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q9P2K8",
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]
},
{
"ec_number": "2.7.11.1",
"activity": "",
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{
"id": "Q9P2K8",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9P2K8"
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]
}
]
},
{
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{
"ec_number": "2.7.11.24",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q9UBE8",
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"url": "https://www.uniprot.org/uniprotkb/Q9UBE8"
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]
},
{
"ec_number": "2.7.11.24",
"activity": "",
"evidence": [
{
"id": "Q9UBE8",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9UBE8"
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]
}
]
},
{
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"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q9UBS0",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9UBS0"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "Q9UBS0",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9UBS0"
}
]
}
]
},
{
"uniprot_ac": "Q9UBT6",
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{
"ec_number": "2.7.7.7",
"activity": "DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate.",
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{
"id": "Q9UBT6",
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"url": "https://www.uniprot.org/uniprotkb/Q9UBT6"
}
]
},
{
"ec_number": "2.7.7.7",
"activity": "",
"evidence": [
{
"id": "Q9UBT6",
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"url": "https://www.uniprot.org/uniprotkb/Q9UBT6"
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]
}
]
},
{
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{
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}
]
},
{
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{
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}
]
}
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},
{
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{
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{
"id": "Q9UEW8",
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}
]
},
{
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"evidence": [
{
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}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
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}
]
},
{
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"activity": "",
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{
"id": "Q9UHD2",
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}
]
}
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},
{
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{
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{
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}
]
},
{
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{
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}
]
}
]
},
{
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{
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{
"id": "Q9UK32",
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}
]
},
{
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{
"id": "Q9UK32",
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}
]
}
]
},
{
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{
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{
"id": "Q9UKE5",
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}
]
},
{
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{
"id": "Q9UKE5",
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}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
"id": "Q9UKI8",
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}
]
},
{
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"evidence": [
{
"id": "Q9UKI8",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9UKI8"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
"id": "Q9UL54",
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}
]
},
{
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{
"id": "Q9UL54",
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}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
"id": "Q9UPE1",
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}
]
},
{
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{
"id": "Q9UPE1",
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"url": "https://www.uniprot.org/uniprotkb/Q9UPE1"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q9UPZ9",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9UPZ9"
}
]
},
{
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"activity": "",
"evidence": [
{
"id": "Q9UPZ9",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9UPZ9"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.22",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q9UQ07",
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"url": "https://www.uniprot.org/uniprotkb/Q9UQ07"
}
]
},
{
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{
"id": "Q9UQ07",
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"url": "https://www.uniprot.org/uniprotkb/Q9UQ07"
}
]
},
{
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{
"id": "Q9UQ07",
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}
]
},
{
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"evidence": [
{
"id": "Q9UQ07",
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}
]
}
]
},
{
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{
"ec_number": "3.1.-.-",
"activity": "",
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{
"id": "Q9UQ84",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9UQ84"
}
]
}
]
},
{
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{
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{
"id": "Q9UQ88",
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"url": "https://www.uniprot.org/uniprotkb/Q9UQ88"
}
]
},
{
"ec_number": "2.7.11.23",
"activity": "[DNA-directed RNA polymerase] + ATP = phospho-[DNA-directed RNA polymerase] + ADP + H(+).",
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{
"id": "Q9UQ88",
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}
]
},
{
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"evidence": [
{
"id": "Q9UQ88",
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}
]
},
{
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"activity": "",
"evidence": [
{
"id": "Q9UQ88",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9UQ88"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
"id": "Q9UQB9",
"database": "UniProtKB",
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}
]
},
{
"ec_number": "2.7.11.1",
"activity": "",
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{
"id": "Q9UQB9",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9UQB9"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.17",
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{
"id": "Q9UQM7",
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}
]
},
{
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{
"id": "Q9UQM7",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9UQM7"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
"id": "Q9Y243",
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]
},
{
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{
"id": "Q9Y243",
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}
]
}
]
},
{
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{
"ec_number": "2.7.7.7",
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{
"id": "Q9Y253",
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]
},
{
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{
"id": "Q9Y253",
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]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
"id": "Q9Y2H1",
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]
},
{
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{
"id": "Q9Y2H1",
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]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q9Y2H9",
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]
},
{
"ec_number": "2.7.11.1",
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{
"id": "Q9Y2H9",
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]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q9Y2I7",
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]
},
{
"ec_number": "2.7.1.150",
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{
"id": "Q9Y2I7",
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"url": "https://www.uniprot.org/uniprotkb/Q9Y2I7"
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]
},
{
"ec_number": "2.7.1.150",
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"evidence": [
{
"id": "Q9Y2I7",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9Y2I7"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
"id": "Q9Y2K2",
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}
]
},
{
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{
"id": "Q9Y2K2",
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]
}
]
},
{
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{
"ec_number": "2.7.11.25",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q9Y2U5",
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]
},
{
"ec_number": "2.7.11.25",
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{
"id": "Q9Y2U5",
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]
}
]
},
{
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{
"ec_number": "2.7.11.1",
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{
"id": "Q9Y3S1",
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]
},
{
"ec_number": "2.7.11.1",
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{
"id": "Q9Y3S1",
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]
}
]
},
{
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{
"ec_number": "2.7.12.1",
"activity": "L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+).",
"evidence": [
{
"id": "Q9Y463",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9Y463"
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]
},
{
"ec_number": "2.7.12.1",
"activity": "",
"evidence": [
{
"id": "Q9Y463",
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]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q9Y4B6",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9Y4B6"
}
]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q9Y4K4",
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]
},
{
"ec_number": "2.7.11.1",
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{
"id": "Q9Y4K4",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9Y4K4"
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]
}
]
},
{
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{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q9Y572",
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]
},
{
"ec_number": "2.7.11.1",
"activity": "",
"evidence": [
{
"id": "Q9Y572",
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"url": "https://www.uniprot.org/uniprotkb/Q9Y572"
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]
}
]
},
{
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{
"ec_number": "3.1.3.16",
"activity": "O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] + phosphate.",
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{
"id": "Q9Y5B0",
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}
]
},
{
"ec_number": "3.1.3.16",
"activity": "",
"evidence": [
{
"id": "Q9Y5B0",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9Y5B0"
}
]
}
]
},
{
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{
"ec_number": "3.1.11.-",
"activity": "",
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{
"id": "Q9Y5B8",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9Y5B8"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q9Y5B8",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9Y5B8"
}
]
}
]
},
{
"uniprot_ac": "Q9Y5S2",
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"activity": [
{
"ec_number": "2.7.11.1",
"activity": "L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+).",
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{
"id": "Q9Y5S2",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9Y5S2"
}
]
},
{
"ec_number": "2.7.11.1",
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"evidence": [
{
"id": "Q9Y5S2",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprotkb/Q9Y5S2"
}
]
}
]
},
{
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