node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CRTAP | P3H1 | ENSGALP00000046912 | ENSGALP00000007707 | Cartilage-associated protein; Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues; Belongs to the leprecan family. | Prolyl 3-hydroxylase 1; Has prolyl 3-hydroxylase activity catalyzing the post- translational formation of 3-hydroxyproline in -Xaa-Pro-Gly-sequences in collagens, especially types IV and V. May be involved in the secretoty pathway of cells. Has growth suppressive activity in fibroblasts (By similarity); Belongs to the leprecan family. | 0.965 |
CRTAP | P4HA1 | ENSGALP00000046912 | ENSGALP00000047674 | Cartilage-associated protein; Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues; Belongs to the leprecan family. | Prolyl 4-hydroxylase subunit alpha-1; Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins; Belongs to the P4HA family. | 0.661 |
CRTAP | P4HA2 | ENSGALP00000046912 | ENSGALP00000010783 | Cartilage-associated protein; Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues; Belongs to the leprecan family. | Prolyl 4-hydroxylase subunit alpha-2; Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins; Belongs to the P4HA family. | 0.679 |
CRTAP | P4HA3 | ENSGALP00000046912 | ENSGALP00000044188 | Cartilage-associated protein; Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues; Belongs to the leprecan family. | Prolyl 4-hydroxylase subunit alpha 3. | 0.729 |
CRTAP | P4HB | ENSGALP00000046912 | ENSGALP00000064334 | Cartilage-associated protein; Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues; Belongs to the leprecan family. | Protein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). Also acts a structural subunit o [...] | 0.853 |
CRTAP | PPIB | ENSGALP00000046912 | ENSGALP00000061454 | Cartilage-associated protein; Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues; Belongs to the leprecan family. | Peptidyl-prolyl cis-trans isomerase B; PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding; Belongs to the cyclophilin-type PPIase family. PPIase B subfamily. | 0.995 |
ERO1A | ERO1B | ENSGALP00000020229 | ENSGALP00000047906 | Uncharacterized protein. | Endoplasmic reticulum oxidoreductase 1 beta. | 0.921 |
ERO1A | HSPA5 | ENSGALP00000020229 | ENSGALP00000001474 | Uncharacterized protein. | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...] | 0.579 |
ERO1A | P4HA1 | ENSGALP00000020229 | ENSGALP00000047674 | Uncharacterized protein. | Prolyl 4-hydroxylase subunit alpha-1; Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins; Belongs to the P4HA family. | 0.438 |
ERO1A | P4HB | ENSGALP00000020229 | ENSGALP00000064334 | Uncharacterized protein. | Protein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). Also acts a structural subunit o [...] | 0.968 |
ERO1B | ERO1A | ENSGALP00000047906 | ENSGALP00000020229 | Endoplasmic reticulum oxidoreductase 1 beta. | Uncharacterized protein. | 0.921 |
ERO1B | HSPA5 | ENSGALP00000047906 | ENSGALP00000001474 | Endoplasmic reticulum oxidoreductase 1 beta. | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...] | 0.600 |
ERO1B | P4HB | ENSGALP00000047906 | ENSGALP00000064334 | Endoplasmic reticulum oxidoreductase 1 beta. | Protein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). Also acts a structural subunit o [...] | 0.956 |
HSPA5 | ERO1A | ENSGALP00000001474 | ENSGALP00000020229 | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...] | Uncharacterized protein. | 0.579 |
HSPA5 | ERO1B | ENSGALP00000001474 | ENSGALP00000047906 | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...] | Endoplasmic reticulum oxidoreductase 1 beta. | 0.600 |
HSPA5 | P4HB | ENSGALP00000001474 | ENSGALP00000064334 | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...] | Protein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). Also acts a structural subunit o [...] | 0.860 |
HSPA5 | PPIB | ENSGALP00000001474 | ENSGALP00000061454 | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...] | Peptidyl-prolyl cis-trans isomerase B; PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding; Belongs to the cyclophilin-type PPIase family. PPIase B subfamily. | 0.562 |
MTTP | P4HB | ENSGALP00000056995 | ENSGALP00000064334 | Vitellogenin domain-containing protein. | Protein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). Also acts a structural subunit o [...] | 0.956 |
P3H1 | CRTAP | ENSGALP00000007707 | ENSGALP00000046912 | Prolyl 3-hydroxylase 1; Has prolyl 3-hydroxylase activity catalyzing the post- translational formation of 3-hydroxyproline in -Xaa-Pro-Gly-sequences in collagens, especially types IV and V. May be involved in the secretoty pathway of cells. Has growth suppressive activity in fibroblasts (By similarity); Belongs to the leprecan family. | Cartilage-associated protein; Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues; Belongs to the leprecan family. | 0.965 |
P3H1 | P4HA1 | ENSGALP00000007707 | ENSGALP00000047674 | Prolyl 3-hydroxylase 1; Has prolyl 3-hydroxylase activity catalyzing the post- translational formation of 3-hydroxyproline in -Xaa-Pro-Gly-sequences in collagens, especially types IV and V. May be involved in the secretoty pathway of cells. Has growth suppressive activity in fibroblasts (By similarity); Belongs to the leprecan family. | Prolyl 4-hydroxylase subunit alpha-1; Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins; Belongs to the P4HA family. | 0.618 |