| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CDC5L | DNAJC7 | ENSP00000360532 | ENSP00000406463 | CDC5 cell division cycle 5-like (S. pombe); DNA-binding protein involved in cell cycle control. May act as a transcription activator. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing | DnaJ (Hsp40) homolog, subfamily C, member 7; Acts as co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone- substrate complexes. Recruits NR1I3 to the cytoplasm (By similarity) | 0.527 |
| CDC5L | PPIL2 | ENSP00000360532 | ENSP00000390427 | CDC5 cell division cycle 5-like (S. pombe); DNA-binding protein involved in cell cycle control. May act as a transcription activator. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing | peptidylprolyl isomerase (cyclophilin)-like 2; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | 0.721 |
| CDC5L | UBE4A | ENSP00000360532 | ENSP00000387362 | CDC5 cell division cycle 5-like (S. pombe); DNA-binding protein involved in cell cycle control. May act as a transcription activator. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing | ubiquitination factor E4A; Binds to the ubiquitin moieties of preformed conjugates and catalyzes ubiquitin chain assembly in conjunction with E1, E2, and E3 (By similarity) | 0.482 |
| CDC5L | UBOX5 | ENSP00000360532 | ENSP00000217173 | CDC5 cell division cycle 5-like (S. pombe); DNA-binding protein involved in cell cycle control. May act as a transcription activator. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing | U-box domain containing 5 | 0.629 |
| CDC5L | WDSUB1 | ENSP00000360532 | ENSP00000352820 | CDC5 cell division cycle 5-like (S. pombe); DNA-binding protein involved in cell cycle control. May act as a transcription activator. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing | WD repeat, sterile alpha motif and U-box domain containing 1 | 0.586 |
| DNAJC7 | CDC5L | ENSP00000406463 | ENSP00000360532 | DnaJ (Hsp40) homolog, subfamily C, member 7; Acts as co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone- substrate complexes. Recruits NR1I3 to the cytoplasm (By similarity) | CDC5 cell division cycle 5-like (S. pombe); DNA-binding protein involved in cell cycle control. May act as a transcription activator. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing | 0.527 |
| DNAJC7 | PPIL2 | ENSP00000406463 | ENSP00000390427 | DnaJ (Hsp40) homolog, subfamily C, member 7; Acts as co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone- substrate complexes. Recruits NR1I3 to the cytoplasm (By similarity) | peptidylprolyl isomerase (cyclophilin)-like 2; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides | 0.667 |
| DNAJC7 | UBE4A | ENSP00000406463 | ENSP00000387362 | DnaJ (Hsp40) homolog, subfamily C, member 7; Acts as co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone- substrate complexes. Recruits NR1I3 to the cytoplasm (By similarity) | ubiquitination factor E4A; Binds to the ubiquitin moieties of preformed conjugates and catalyzes ubiquitin chain assembly in conjunction with E1, E2, and E3 (By similarity) | 0.656 |
| DNAJC7 | UBOX5 | ENSP00000406463 | ENSP00000217173 | DnaJ (Hsp40) homolog, subfamily C, member 7; Acts as co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone- substrate complexes. Recruits NR1I3 to the cytoplasm (By similarity) | U-box domain containing 5 | 0.670 |
| DNAJC7 | WDSUB1 | ENSP00000406463 | ENSP00000352820 | DnaJ (Hsp40) homolog, subfamily C, member 7; Acts as co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone- substrate complexes. Recruits NR1I3 to the cytoplasm (By similarity) | WD repeat, sterile alpha motif and U-box domain containing 1 | 0.641 |
| FBXW2 | PAK1IP1 | ENSP00000363036 | ENSP00000368887 | F-box and WD repeat domain containing 2; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex | PAK1 interacting protein 1; Negatively regulates the PAK1 kinase. PAK1 is a member of the PAK kinase family, which have been shown to play a positive role in the regulation of signaling pathways involving MAPK8 and RELA. PAK1 exists as an inactive homodimer, which is activated by binding of small GTPases such as CDC42 to an N-terminal regulatory domain. PAK1IP1 also binds to the N-terminus of PAK1, and inhibits the specific activation of PAK1 by CDC42 | 0.687 |
| FBXW2 | WDR31 | ENSP00000363036 | ENSP00000363308 | F-box and WD repeat domain containing 2; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex | WD repeat domain 31 | 0.516 |
| FBXW2 | WDSUB1 | ENSP00000363036 | ENSP00000352820 | F-box and WD repeat domain containing 2; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex | WD repeat, sterile alpha motif and U-box domain containing 1 | 0.533 |
| PAK1IP1 | FBXW2 | ENSP00000368887 | ENSP00000363036 | PAK1 interacting protein 1; Negatively regulates the PAK1 kinase. PAK1 is a member of the PAK kinase family, which have been shown to play a positive role in the regulation of signaling pathways involving MAPK8 and RELA. PAK1 exists as an inactive homodimer, which is activated by binding of small GTPases such as CDC42 to an N-terminal regulatory domain. PAK1IP1 also binds to the N-terminus of PAK1, and inhibits the specific activation of PAK1 by CDC42 | F-box and WD repeat domain containing 2; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex | 0.687 |
| PAK1IP1 | PEX7 | ENSP00000368887 | ENSP00000315680 | PAK1 interacting protein 1; Negatively regulates the PAK1 kinase. PAK1 is a member of the PAK kinase family, which have been shown to play a positive role in the regulation of signaling pathways involving MAPK8 and RELA. PAK1 exists as an inactive homodimer, which is activated by binding of small GTPases such as CDC42 to an N-terminal regulatory domain. PAK1IP1 also binds to the N-terminus of PAK1, and inhibits the specific activation of PAK1 by CDC42 | peroxisomal biogenesis factor 7; Binds to the N-terminal PTS2-type peroxisomal targeting signal and plays an essential role in peroxisomal protein import | 0.449 |
| PAK1IP1 | TRAF7 | ENSP00000368887 | ENSP00000318944 | PAK1 interacting protein 1; Negatively regulates the PAK1 kinase. PAK1 is a member of the PAK kinase family, which have been shown to play a positive role in the regulation of signaling pathways involving MAPK8 and RELA. PAK1 exists as an inactive homodimer, which is activated by binding of small GTPases such as CDC42 to an N-terminal regulatory domain. PAK1IP1 also binds to the N-terminus of PAK1, and inhibits the specific activation of PAK1 by CDC42 | TNF receptor-associated factor 7, E3 ubiquitin protein ligase; E3 ubiquitin ligase capable of auto-ubiquitination, following phosphorylation by MAP3K3. Potentiates MEKK3-mediated activation of the NF-kappa-B, JUN/AP1 and DDIT3 transcriptional regulators. Induces apoptosis when overexpressed | 0.468 |
| PAK1IP1 | WDR31 | ENSP00000368887 | ENSP00000363308 | PAK1 interacting protein 1; Negatively regulates the PAK1 kinase. PAK1 is a member of the PAK kinase family, which have been shown to play a positive role in the regulation of signaling pathways involving MAPK8 and RELA. PAK1 exists as an inactive homodimer, which is activated by binding of small GTPases such as CDC42 to an N-terminal regulatory domain. PAK1IP1 also binds to the N-terminus of PAK1, and inhibits the specific activation of PAK1 by CDC42 | WD repeat domain 31 | 0.622 |
| PAK1IP1 | WDSUB1 | ENSP00000368887 | ENSP00000352820 | PAK1 interacting protein 1; Negatively regulates the PAK1 kinase. PAK1 is a member of the PAK kinase family, which have been shown to play a positive role in the regulation of signaling pathways involving MAPK8 and RELA. PAK1 exists as an inactive homodimer, which is activated by binding of small GTPases such as CDC42 to an N-terminal regulatory domain. PAK1IP1 also binds to the N-terminus of PAK1, and inhibits the specific activation of PAK1 by CDC42 | WD repeat, sterile alpha motif and U-box domain containing 1 | 0.476 |
| PEX7 | PAK1IP1 | ENSP00000315680 | ENSP00000368887 | peroxisomal biogenesis factor 7; Binds to the N-terminal PTS2-type peroxisomal targeting signal and plays an essential role in peroxisomal protein import | PAK1 interacting protein 1; Negatively regulates the PAK1 kinase. PAK1 is a member of the PAK kinase family, which have been shown to play a positive role in the regulation of signaling pathways involving MAPK8 and RELA. PAK1 exists as an inactive homodimer, which is activated by binding of small GTPases such as CDC42 to an N-terminal regulatory domain. PAK1IP1 also binds to the N-terminus of PAK1, and inhibits the specific activation of PAK1 by CDC42 | 0.449 |
| PEX7 | WDSUB1 | ENSP00000315680 | ENSP00000352820 | peroxisomal biogenesis factor 7; Binds to the N-terminal PTS2-type peroxisomal targeting signal and plays an essential role in peroxisomal protein import | WD repeat, sterile alpha motif and U-box domain containing 1 | 0.475 |
Share
