| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CPR4 | CPR7 | YCR069W | YJR032W | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; has a potential role in the secretory pathway; CPR4 has a paralog, CPR8, 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. | 0.738 |
| CPR4 | ESS1 | YCR069W | YJR017C | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; has a potential role in the secretory pathway; CPR4 has a paralog, CPR8, 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. | 0.749 |
| CPR4 | FPR1 | YCR069W | YNL135C | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; has a potential role in the secretory pathway; CPR4 has a paralog, CPR8, 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. | 0.622 |
| CPR4 | FPR3 | YCR069W | YML074C | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; has a potential role in the secretory pathway; CPR4 has a paralog, CPR8, 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. | 0.630 |
| CPR4 | FPR4 | YCR069W | YLR449W | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; has a potential role in the secretory pathway; CPR4 has a paralog, CPR8, that arose from the whole genome duplication. | 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. | 0.631 |
| CPR4 | NOP1 | YCR069W | YDL014W | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; has a potential role in the secretory pathway; CPR4 has a paralog, CPR8, that arose from the whole genome duplication. | rRNA 2'-O-methyltransferase fibrillarin; Histone glutamine methyltransferase, modifies H2A at Q105 in nucleolus; component of the small subunit processome complex, which is required for processing of pre-18S rRNA; ortholog of mammalian fibrillarin; inviability of the null mutant is functionally complemented by human FBL. | 0.696 |
| CPR4 | PRP19 | YCR069W | YLL036C | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; has a potential role in the secretory pathway; CPR4 has a paralog, CPR8, that arose from the whole genome duplication. | 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. | 0.623 |
| CPR4 | SYF1 | YCR069W | YDR416W | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; has a potential role in the secretory pathway; CPR4 has a paralog, CPR8, that arose from the whole genome duplication. | 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 |
| CPR4 | YFR018C | YCR069W | YFR018C | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; has a potential role in the secretory pathway; CPR4 has a paralog, CPR8, that arose from the whole genome duplication. | Uncharacterized protein YFR018C; Putative protein of unknown function; SWAT-GFP and seamless GFP fusion proteins localize to the endoplasmic reticulum and mCherry fusion protein localizes to the vacuole. | 0.758 |
| CPR4 | YPL162C | YCR069W | YPL162C | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; has a potential role in the secretory pathway; CPR4 has a paralog, CPR8, that arose from the whole genome duplication. | Vacuolar membrane protein YPL162C; Putative protein of unknown function; green fluorescent protein (GFP)-fusion protein localizes to the membrane of vacuole with cell cycle-correlated morphology. | 0.643 |
| CPR7 | CPR4 | YJR032W | YCR069W | 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; has a potential role in the secretory pathway; CPR4 has a paralog, CPR8, that arose from the whole genome duplication. | 0.738 |
| 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 |
| ESS1 | CPR4 | YJR017C | YCR069W | 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. | Peptidyl-prolyl cis-trans isomerase (cyclophilin); catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues; has a potential role in the secretory pathway; CPR4 has a paralog, CPR8, that arose from the whole genome duplication. | 0.749 |
| ESS1 | FPR1 | YJR017C | YNL135C | 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. | 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. | 0.764 |
| ESS1 | FPR3 | YJR017C | YML074C | 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. | 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. | 0.463 |
| ESS1 | FPR4 | YJR017C | YLR449W | 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. | 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. | 0.598 |