node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
DDB1 | EME1 | ENSP00000301764 | ENSP00000376952 | damage-specific DNA binding protein 1, 127kDa; Required for DNA repair. Binds to DDB2 to form the UV- damaged DNA-binding protein complex (the UV-DDB complex). The UV- DDB complex may recognize UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also appears to function as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which [...] | essential meiotic endonuclease 1 homolog 1 (S. pombe); Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5’-end at the branch nick. Typical substrates include 3’- flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks | 0.578 |
DDB1 | ERCC4 | ENSP00000301764 | ENSP00000310520 | damage-specific DNA binding protein 1, 127kDa; Required for DNA repair. Binds to DDB2 to form the UV- damaged DNA-binding protein complex (the UV-DDB complex). The UV- DDB complex may recognize UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also appears to function as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which [...] | excision repair cross-complementing rodent repair deficiency, complementation group 4; Structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair. Involved in homologous recombination that assists in removing interstrand cross-link | 0.986 |
DDB1 | FEN1 | ENSP00000301764 | ENSP00000305480 | damage-specific DNA binding protein 1, 127kDa; Required for DNA repair. Binds to DDB2 to form the UV- damaged DNA-binding protein complex (the UV-DDB complex). The UV- DDB complex may recognize UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also appears to function as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which [...] | 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 [...] | 0.428 |
DDB1 | MUS81 | ENSP00000301764 | ENSP00000307853 | damage-specific DNA binding protein 1, 127kDa; Required for DNA repair. Binds to DDB2 to form the UV- damaged DNA-binding protein complex (the UV-DDB complex). The UV- DDB complex may recognize UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also appears to function as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which [...] | MUS81 endonuclease homolog (S. cerevisiae); Interacts with EME1 and EME2 to form a DNA structure- specific endonuclease with substrate preference for branched DNA structures with a 5’-end at the branch nick. Typical substrates include 3’-flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks | 0.613 |
DDB1 | SLX4 | ENSP00000301764 | ENSP00000294008 | damage-specific DNA binding protein 1, 127kDa; Required for DNA repair. Binds to DDB2 to form the UV- damaged DNA-binding protein complex (the UV-DDB complex). The UV- DDB complex may recognize UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also appears to function as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which [...] | SLX4 structure-specific endonuclease subunit homolog (S. cerevisiae); Regulatory subunit that interacts with and increases the activity of different structure-specific endonucleases. Has several distinct roles in protecting genome stability by resolving diverse forms of deleterious DNA structures originating from replication and recombination intermediates and from DNA damage. Component of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introduc [...] | 0.799 |
EME1 | DDB1 | ENSP00000376952 | ENSP00000301764 | essential meiotic endonuclease 1 homolog 1 (S. pombe); Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5’-end at the branch nick. Typical substrates include 3’- flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks | damage-specific DNA binding protein 1, 127kDa; Required for DNA repair. Binds to DDB2 to form the UV- damaged DNA-binding protein complex (the UV-DDB complex). The UV- DDB complex may recognize UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also appears to function as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which [...] | 0.578 |
EME1 | ERCC4 | ENSP00000376952 | ENSP00000310520 | essential meiotic endonuclease 1 homolog 1 (S. pombe); Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5’-end at the branch nick. Typical substrates include 3’- flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks | excision repair cross-complementing rodent repair deficiency, complementation group 4; Structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair. Involved in homologous recombination that assists in removing interstrand cross-link | 0.786 |
EME1 | FEN1 | ENSP00000376952 | ENSP00000305480 | essential meiotic endonuclease 1 homolog 1 (S. pombe); Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5’-end at the branch nick. Typical substrates include 3’- flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks | 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 [...] | 0.636 |
EME1 | MUS81 | ENSP00000376952 | ENSP00000307853 | essential meiotic endonuclease 1 homolog 1 (S. pombe); Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5’-end at the branch nick. Typical substrates include 3’- flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks | MUS81 endonuclease homolog (S. cerevisiae); Interacts with EME1 and EME2 to form a DNA structure- specific endonuclease with substrate preference for branched DNA structures with a 5’-end at the branch nick. Typical substrates include 3’-flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks | 0.999 |
EME1 | RAD54L | ENSP00000376952 | ENSP00000361043 | essential meiotic endonuclease 1 homolog 1 (S. pombe); Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5’-end at the branch nick. Typical substrates include 3’- flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks | RAD54-like (S. cerevisiae); Involved in DNA repair and mitotic recombination. Functions in the recombinational DNA repair (RAD52) pathway. Dissociates RAD51 from nucleoprotein filaments formed on dsDNA. Could be involved in the turnover of RAD51 protein-dsDNA filaments (By similarity). May play also an essential role in telomere length maintenance and telomere capping in mammalian cells | 0.622 |
EME1 | SLX1A | ENSP00000376952 | ENSP00000251303 | essential meiotic endonuclease 1 homolog 1 (S. pombe); Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5’-end at the branch nick. Typical substrates include 3’- flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks | SLX1 structure-specific endonuclease subunit homolog A (S. cerevisiae); Catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for 5’-flap structures, and promotes symmetrical cleavage of static and migrating Holliday junctions (HJs). Resolves HJs by generating two pairs of ligatable, nicked duplex products | 0.918 |
EME1 | SLX1B | ENSP00000376952 | ENSP00000328940 | essential meiotic endonuclease 1 homolog 1 (S. pombe); Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5’-end at the branch nick. Typical substrates include 3’- flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks | SLX1 structure-specific endonuclease subunit homolog B (S. cerevisiae); Catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for 5’-flap structures, and promotes symmetrical cleavage of static and migrating Holliday junctions (HJs). Resolves HJs by generating two pairs of ligatable, nicked duplex products (By similarity) | 0.818 |
EME1 | SLX4 | ENSP00000376952 | ENSP00000294008 | essential meiotic endonuclease 1 homolog 1 (S. pombe); Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5’-end at the branch nick. Typical substrates include 3’- flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks | SLX4 structure-specific endonuclease subunit homolog (S. cerevisiae); Regulatory subunit that interacts with and increases the activity of different structure-specific endonucleases. Has several distinct roles in protecting genome stability by resolving diverse forms of deleterious DNA structures originating from replication and recombination intermediates and from DNA damage. Component of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introduc [...] | 0.963 |
ERCC4 | DDB1 | ENSP00000310520 | ENSP00000301764 | excision repair cross-complementing rodent repair deficiency, complementation group 4; Structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair. Involved in homologous recombination that assists in removing interstrand cross-link | damage-specific DNA binding protein 1, 127kDa; Required for DNA repair. Binds to DDB2 to form the UV- damaged DNA-binding protein complex (the UV-DDB complex). The UV- DDB complex may recognize UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also appears to function as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which [...] | 0.986 |
ERCC4 | EME1 | ENSP00000310520 | ENSP00000376952 | excision repair cross-complementing rodent repair deficiency, complementation group 4; Structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair. Involved in homologous recombination that assists in removing interstrand cross-link | essential meiotic endonuclease 1 homolog 1 (S. pombe); Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5’-end at the branch nick. Typical substrates include 3’- flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks | 0.786 |
ERCC4 | FANCM | ENSP00000310520 | ENSP00000267430 | excision repair cross-complementing rodent repair deficiency, complementation group 4; Structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair. Involved in homologous recombination that assists in removing interstrand cross-link | Fanconi anemia, complementation group M; ATPase required for FANCD2 ubiquitination, a key reaction in DNA repair. Binds to ssDNA but not to dsDNA. Recruited to forks stalled by DNA interstrand cross-links, and required for cellular resistance to such lesions | 0.850 |
ERCC4 | FEN1 | ENSP00000310520 | ENSP00000305480 | excision repair cross-complementing rodent repair deficiency, complementation group 4; Structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair. Involved in homologous recombination that assists in removing interstrand cross-link | 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 [...] | 0.914 |
ERCC4 | MUS81 | ENSP00000310520 | ENSP00000307853 | excision repair cross-complementing rodent repair deficiency, complementation group 4; Structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair. Involved in homologous recombination that assists in removing interstrand cross-link | MUS81 endonuclease homolog (S. cerevisiae); Interacts with EME1 and EME2 to form a DNA structure- specific endonuclease with substrate preference for branched DNA structures with a 5’-end at the branch nick. Typical substrates include 3’-flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks | 0.991 |
ERCC4 | RAD54L | ENSP00000310520 | ENSP00000361043 | excision repair cross-complementing rodent repair deficiency, complementation group 4; Structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair. Involved in homologous recombination that assists in removing interstrand cross-link | RAD54-like (S. cerevisiae); Involved in DNA repair and mitotic recombination. Functions in the recombinational DNA repair (RAD52) pathway. Dissociates RAD51 from nucleoprotein filaments formed on dsDNA. Could be involved in the turnover of RAD51 protein-dsDNA filaments (By similarity). May play also an essential role in telomere length maintenance and telomere capping in mammalian cells | 0.662 |
ERCC4 | SLX1A | ENSP00000310520 | ENSP00000251303 | excision repair cross-complementing rodent repair deficiency, complementation group 4; Structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair. Involved in homologous recombination that assists in removing interstrand cross-link | SLX1 structure-specific endonuclease subunit homolog A (S. cerevisiae); Catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for 5’-flap structures, and promotes symmetrical cleavage of static and migrating Holliday junctions (HJs). Resolves HJs by generating two pairs of ligatable, nicked duplex products | 0.953 |