node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CPR6 | CPR7 | YLR216C | YJR032W | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; plays a role in determining prion variants; binds to Hsp82p and contributes to chaperone activity; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase D subfamily. | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds to Hsp82p and contributes to chaperone activity; plays a role in determining prion variants. | 0.579 |
CPR6 | CPR8 | YLR216C | YNR028W | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; plays a role in determining prion variants; binds to Hsp82p and contributes to chaperone activity; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase D subfamily. | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; potential role in the secretory pathway; CPR8 has a paralog, CPR4, that arose from the whole genome duplication. | 0.601 |
CPR6 | ESS1 | YLR216C | YJR017C | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; plays a role in determining prion variants; binds to Hsp82p and contributes to chaperone activity; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase D subfamily. | Peptidyl-prolyl cis-trans isomerase ESS1; Peptidylprolyl-cis/trans-isomerase (PPIase); specific for phosphorylated S/T residues N-terminal to proline; regulates phosphorylation of RNAPII large subunit (Rpo21p) C-terminal domain (CTD) at Ser7; associates with phospho-Ser5 form of RNAPII in vivo; present along entire coding length of genes; represses initiation of CUTs; required for efficient termination of mRNA transcription, trimethylation of histone H3; human ortholog PIN1 can complement yeast null and ts mutants; Belongs to the PpiC/parvulin rotamase family. | 0.478 |
CPR6 | FPR1 | YLR216C | YNL135C | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; plays a role in determining prion variants; binds to Hsp82p and contributes to chaperone activity; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase D subfamily. | FK506-binding protein 1; Peptidyl-prolyl cis-trans isomerase (PPIase); binds to the drugs FK506 and rapamycin; also binds to the nonhistone chromatin binding protein Hmo1p and may regulate its assembly or function; N-terminally propionylated in vivo; mutation is functionally complemented by human FKBP1A. | 0.962 |
CPR6 | FPR3 | YLR216C | YML074C | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; plays a role in determining prion variants; binds to Hsp82p and contributes to chaperone activity; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase D subfamily. | FK506-binding nuclear protein; Nucleolar peptidyl-prolyl cis-trans isomerase (PPIase); FK506 binding protein; affects expression of multiple genes via its role in nucleosome assembly; phosphorylated by casein kinase II (Cka1p-Cka2p-Ckb1p-Ckb2p) and dephosphorylated by Ptp1p; PPIase domain acts as a transcriptional repressor when tethered to DNA by lexA, and repressor activity is dependent on PPIase activity; FPR3 has a paralog, FPR4, that arose from the whole genome duplication; Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily. | 0.616 |
CPR6 | FPR4 | YLR216C | YLR449W | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; plays a role in determining prion variants; binds to Hsp82p and contributes to chaperone activity; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase D subfamily. | FK506-binding protein 4; Peptidyl-prolyl cis-trans isomerase (PPIase); nuclear proline isomerase; affects expression of multiple genes via its role in nucleosome assembly; catalyzes isomerization of proline residues in histones H3 and H4, which affects lysine methylation of those histones; PPIase domain acts as a transcriptional repressor when tethered to DNA by lexA, and repressor activity is dependent on PPIase activity; contains a nucleoplasmin-like fold and can form pentamers; Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily. | 0.540 |
CPR6 | PRP19 | YLR216C | YLL036C | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; plays a role in determining prion variants; binds to Hsp82p and contributes to chaperone activity; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase D subfamily. | Pre-mRNA-processing factor 19; Splicing factor associated with the spliceosome; contains a U-box, a motif found in a class of ubiquitin ligases, and a WD40 domain; relocalizes to the cytosol in response to hypoxia; Belongs to the WD repeat PRP19 family. | 0.924 |
CPR6 | SYF1 | YLR216C | YDR416W | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; plays a role in determining prion variants; binds to Hsp82p and contributes to chaperone activity; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase D subfamily. | Pre-mRNA-splicing factor SYF1; Member of the NineTeen Complex (NTC); that contains Prp19p and stabilizes U6 snRNA in catalytic forms of the spliceosome containing U2, U5, and U6 snRNAs; null mutant has splicing defect and arrests in G2/M; relocalizes to the cytosol in response to hypoxia; homologs in human and C. elegans. | 0.920 |
CPR7 | CPR6 | YJR032W | YLR216C | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds to Hsp82p and contributes to chaperone activity; plays a role in determining prion variants. | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; plays a role in determining prion variants; binds to Hsp82p and contributes to chaperone activity; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase D subfamily. | 0.579 |
CPR7 | CPR8 | YJR032W | YNR028W | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds to Hsp82p and contributes to chaperone activity; plays a role in determining prion variants. | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; potential role in the secretory pathway; CPR8 has a paralog, CPR4, that arose from the whole genome duplication. | 0.661 |
CPR7 | FPR1 | YJR032W | YNL135C | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds to Hsp82p and contributes to chaperone activity; plays a role in determining prion variants. | FK506-binding protein 1; Peptidyl-prolyl cis-trans isomerase (PPIase); binds to the drugs FK506 and rapamycin; also binds to the nonhistone chromatin binding protein Hmo1p and may regulate its assembly or function; N-terminally propionylated in vivo; mutation is functionally complemented by human FKBP1A. | 0.573 |
CPR7 | FPR3 | YJR032W | YML074C | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds to Hsp82p and contributes to chaperone activity; plays a role in determining prion variants. | FK506-binding nuclear protein; Nucleolar peptidyl-prolyl cis-trans isomerase (PPIase); FK506 binding protein; affects expression of multiple genes via its role in nucleosome assembly; phosphorylated by casein kinase II (Cka1p-Cka2p-Ckb1p-Ckb2p) and dephosphorylated by Ptp1p; PPIase domain acts as a transcriptional repressor when tethered to DNA by lexA, and repressor activity is dependent on PPIase activity; FPR3 has a paralog, FPR4, that arose from the whole genome duplication; Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily. | 0.533 |
CPR7 | FPR4 | YJR032W | YLR449W | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds to Hsp82p and contributes to chaperone activity; plays a role in determining prion variants. | FK506-binding protein 4; Peptidyl-prolyl cis-trans isomerase (PPIase); nuclear proline isomerase; affects expression of multiple genes via its role in nucleosome assembly; catalyzes isomerization of proline residues in histones H3 and H4, which affects lysine methylation of those histones; PPIase domain acts as a transcriptional repressor when tethered to DNA by lexA, and repressor activity is dependent on PPIase activity; contains a nucleoplasmin-like fold and can form pentamers; Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily. | 0.450 |
CPR7 | PRP19 | YJR032W | YLL036C | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds to Hsp82p and contributes to chaperone activity; plays a role in determining prion variants. | Pre-mRNA-processing factor 19; Splicing factor associated with the spliceosome; contains a U-box, a motif found in a class of ubiquitin ligases, and a WD40 domain; relocalizes to the cytosol in response to hypoxia; Belongs to the WD repeat PRP19 family. | 0.635 |
CPR7 | SYF1 | YJR032W | YDR416W | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds to Hsp82p and contributes to chaperone activity; plays a role in determining prion variants. | Pre-mRNA-splicing factor SYF1; Member of the NineTeen Complex (NTC); that contains Prp19p and stabilizes U6 snRNA in catalytic forms of the spliceosome containing U2, U5, and U6 snRNAs; null mutant has splicing defect and arrests in G2/M; relocalizes to the cytosol in response to hypoxia; homologs in human and C. elegans. | 0.619 |
CPR8 | CPR6 | YNR028W | YLR216C | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; potential role in the secretory pathway; CPR8 has a paralog, CPR4, that arose from the whole genome duplication. | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; plays a role in determining prion variants; binds to Hsp82p and contributes to chaperone activity; protein abundance increases in response to DNA replication stress; Belongs to the cyclophilin-type PPIase family. PPIase D subfamily. | 0.601 |
CPR8 | CPR7 | YNR028W | YJR032W | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; potential role in the secretory pathway; CPR8 has a paralog, CPR4, that arose from the whole genome duplication. | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; binds to Hsp82p and contributes to chaperone activity; plays a role in determining prion variants. | 0.661 |
CPR8 | ESS1 | YNR028W | YJR017C | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; potential role in the secretory pathway; CPR8 has a paralog, CPR4, that arose from the whole genome duplication. | Peptidyl-prolyl cis-trans isomerase ESS1; Peptidylprolyl-cis/trans-isomerase (PPIase); specific for phosphorylated S/T residues N-terminal to proline; regulates phosphorylation of RNAPII large subunit (Rpo21p) C-terminal domain (CTD) at Ser7; associates with phospho-Ser5 form of RNAPII in vivo; present along entire coding length of genes; represses initiation of CUTs; required for efficient termination of mRNA transcription, trimethylation of histone H3; human ortholog PIN1 can complement yeast null and ts mutants; Belongs to the PpiC/parvulin rotamase family. | 0.840 |
CPR8 | FPR1 | YNR028W | YNL135C | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; potential role in the secretory pathway; CPR8 has a paralog, CPR4, that arose from the whole genome duplication. | FK506-binding protein 1; Peptidyl-prolyl cis-trans isomerase (PPIase); binds to the drugs FK506 and rapamycin; also binds to the nonhistone chromatin binding protein Hmo1p and may regulate its assembly or function; N-terminally propionylated in vivo; mutation is functionally complemented by human FKBP1A. | 0.736 |
CPR8 | FPR3 | YNR028W | YML074C | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; potential role in the secretory pathway; CPR8 has a paralog, CPR4, that arose from the whole genome duplication. | FK506-binding nuclear protein; Nucleolar peptidyl-prolyl cis-trans isomerase (PPIase); FK506 binding protein; affects expression of multiple genes via its role in nucleosome assembly; phosphorylated by casein kinase II (Cka1p-Cka2p-Ckb1p-Ckb2p) and dephosphorylated by Ptp1p; PPIase domain acts as a transcriptional repressor when tethered to DNA by lexA, and repressor activity is dependent on PPIase activity; FPR3 has a paralog, FPR4, that arose from the whole genome duplication; Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily. | 0.755 |