node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CDKN1A | PCNA | ENSP00000244741 | ENSP00000368438 | cyclin-dependent kinase inhibitor 1A (p21, Cip1); May be the important intermediate by which p53/TP53 mediates its role as an inhibitor of cellular proliferation in response to DNA damage. Binds to and inhibits cyclin-dependent kinase activity, preventing phosphorylation of critical cyclin- dependent kinase substrates and blocking cell cycle progression. Functions in the nuclear localization and assembly of cyclin D- CDK4 complex and promotes its kinase activity towards RB1. At higher stoichiometric ratios, inhibits the kinase activity of the cyclin D-CDK4 complex | proliferating cell nuclear antigen; Auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase’s processibility during elongation of the leading strand. Induces a robust stimulatory effect on the 3’- 5’ exonuclease and 3’-phosphodiesterase, but not apurinic- apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA re [...] | 0.999 |
FEN1 | LIG1 | ENSP00000305480 | ENSP00000263274 | flap structure-specific endonuclease 1; Structure-specific nuclease with 5’-flap endonuclease and 5’-3’ exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5’-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5’-end of a downstream Okazaki fragment. It enters the flap from the 5’-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminat [...] | ligase I, DNA, ATP-dependent; DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair | 0.958 |
FEN1 | MSH6 | ENSP00000305480 | ENSP00000234420 | flap structure-specific endonuclease 1; Structure-specific nuclease with 5’-flap endonuclease and 5’-3’ exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5’-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5’-end of a downstream Okazaki fragment. It enters the flap from the 5’-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminat [...] | mutS homolog 6 (E. coli); Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resyn [...] | 0.690 |
FEN1 | PCNA | ENSP00000305480 | ENSP00000368438 | flap structure-specific endonuclease 1; Structure-specific nuclease with 5’-flap endonuclease and 5’-3’ exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5’-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5’-end of a downstream Okazaki fragment. It enters the flap from the 5’-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminat [...] | proliferating cell nuclear antigen; Auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase’s processibility during elongation of the leading strand. Induces a robust stimulatory effect on the 3’- 5’ exonuclease and 3’-phosphodiesterase, but not apurinic- apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA re [...] | 0.999 |
FEN1 | POLD1 | ENSP00000305480 | ENSP00000406046 | flap structure-specific endonuclease 1; Structure-specific nuclease with 5’-flap endonuclease and 5’-3’ exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5’-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5’-end of a downstream Okazaki fragment. It enters the flap from the 5’-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminat [...] | polymerase (DNA directed), delta 1, catalytic subunit; Possesses two enzymatic activities- DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3’- to 5’-direction. Required with its accessory proteins (proliferating cell nuclear antigen (PCNA) and replication factor C (RFC) or activator 1) for leading strand synthesis. Also involved in completing Okazaki fragments initiated by the DNA polymerase alpha/primase complex | 0.971 |
FEN1 | POLH | ENSP00000305480 | ENSP00000361310 | flap structure-specific endonuclease 1; Structure-specific nuclease with 5’-flap endonuclease and 5’-3’ exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5’-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5’-end of a downstream Okazaki fragment. It enters the flap from the 5’-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminat [...] | polymerase (DNA directed), eta; DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Plays an important role in the repair of UV-induced pyrimidine dimers. Depending on the context, it inserts the correct base, but causes frequent base transitions and transversions. May play a role in hypermutation at immunoglobulin genes. Forms a Schiff base with 5’-deoxyribose phosphate at abasic sites, but does not have lyase activity. Targets POLI to replication foci | 0.644 |
FEN1 | RFC1 | ENSP00000305480 | ENSP00000371321 | flap structure-specific endonuclease 1; Structure-specific nuclease with 5’-flap endonuclease and 5’-3’ exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5’-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5’-end of a downstream Okazaki fragment. It enters the flap from the 5’-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminat [...] | replication factor C (activator 1) 1, 145kDa; The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. This subunit binds to the primer-template junction. Binds the PO-B transcription element as well as other GA rich DNA sequences. Could play a role in DNA transcription regulation as well as DNA replication and/or repair. Can bind single- or double-stranded DNA | 0.736 |
FEN1 | RFC3 | ENSP00000305480 | ENSP00000369411 | flap structure-specific endonuclease 1; Structure-specific nuclease with 5’-flap endonuclease and 5’-3’ exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5’-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5’-end of a downstream Okazaki fragment. It enters the flap from the 5’-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminat [...] | replication factor C (activator 1) 3, 38kDa; The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1 | 0.684 |
FEN1 | RFC4 | ENSP00000305480 | ENSP00000296273 | flap structure-specific endonuclease 1; Structure-specific nuclease with 5’-flap endonuclease and 5’-3’ exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5’-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5’-end of a downstream Okazaki fragment. It enters the flap from the 5’-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminat [...] | replication factor C (activator 1) 4, 37kDa; The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1. This subunit may be involved in the elongation of the multiprimed DNA template | 0.780 |
FEN1 | RFC5 | ENSP00000305480 | ENSP00000408295 | flap structure-specific endonuclease 1; Structure-specific nuclease with 5’-flap endonuclease and 5’-3’ exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5’-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5’-end of a downstream Okazaki fragment. It enters the flap from the 5’-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminat [...] | replication factor C (activator 1) 5, 36.5kDa; The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1 | 0.744 |
LIG1 | FEN1 | ENSP00000263274 | ENSP00000305480 | ligase I, DNA, ATP-dependent; DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair | flap structure-specific endonuclease 1; Structure-specific nuclease with 5’-flap endonuclease and 5’-3’ exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5’-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5’-end of a downstream Okazaki fragment. It enters the flap from the 5’-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminat [...] | 0.958 |
LIG1 | PCNA | ENSP00000263274 | ENSP00000368438 | ligase I, DNA, ATP-dependent; DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair | proliferating cell nuclear antigen; Auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase’s processibility during elongation of the leading strand. Induces a robust stimulatory effect on the 3’- 5’ exonuclease and 3’-phosphodiesterase, but not apurinic- apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA re [...] | 0.999 |
LIG1 | POLD1 | ENSP00000263274 | ENSP00000406046 | ligase I, DNA, ATP-dependent; DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair | polymerase (DNA directed), delta 1, catalytic subunit; Possesses two enzymatic activities- DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3’- to 5’-direction. Required with its accessory proteins (proliferating cell nuclear antigen (PCNA) and replication factor C (RFC) or activator 1) for leading strand synthesis. Also involved in completing Okazaki fragments initiated by the DNA polymerase alpha/primase complex | 0.947 |
LIG1 | RFC1 | ENSP00000263274 | ENSP00000371321 | ligase I, DNA, ATP-dependent; DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair | replication factor C (activator 1) 1, 145kDa; The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. This subunit binds to the primer-template junction. Binds the PO-B transcription element as well as other GA rich DNA sequences. Could play a role in DNA transcription regulation as well as DNA replication and/or repair. Can bind single- or double-stranded DNA | 0.586 |
LIG1 | RFC3 | ENSP00000263274 | ENSP00000369411 | ligase I, DNA, ATP-dependent; DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair | replication factor C (activator 1) 3, 38kDa; The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1 | 0.692 |
LIG1 | RFC4 | ENSP00000263274 | ENSP00000296273 | ligase I, DNA, ATP-dependent; DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair | replication factor C (activator 1) 4, 37kDa; The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1. This subunit may be involved in the elongation of the multiprimed DNA template | 0.762 |
LIG1 | RFC5 | ENSP00000263274 | ENSP00000408295 | ligase I, DNA, ATP-dependent; DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair | replication factor C (activator 1) 5, 36.5kDa; The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1 | 0.780 |
MSH6 | FEN1 | ENSP00000234420 | ENSP00000305480 | mutS homolog 6 (E. coli); Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resyn [...] | flap structure-specific endonuclease 1; Structure-specific nuclease with 5’-flap endonuclease and 5’-3’ exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5’-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5’-end of a downstream Okazaki fragment. It enters the flap from the 5’-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminat [...] | 0.690 |
MSH6 | PCNA | ENSP00000234420 | ENSP00000368438 | mutS homolog 6 (E. coli); Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resyn [...] | proliferating cell nuclear antigen; Auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase’s processibility during elongation of the leading strand. Induces a robust stimulatory effect on the 3’- 5’ exonuclease and 3’-phosphodiesterase, but not apurinic- apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA re [...] | 0.999 |
MSH6 | POLD1 | ENSP00000234420 | ENSP00000406046 | mutS homolog 6 (E. coli); Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resyn [...] | polymerase (DNA directed), delta 1, catalytic subunit; Possesses two enzymatic activities- DNA synthesis (polymerase) and an exonucleolytic activity that degrades single stranded DNA in the 3’- to 5’-direction. Required with its accessory proteins (proliferating cell nuclear antigen (PCNA) and replication factor C (RFC) or activator 1) for leading strand synthesis. Also involved in completing Okazaki fragments initiated by the DNA polymerase alpha/primase complex | 0.961 |