node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CICDH | ICDH | Q9SRZ6 | Q9SLK0 | Cytosolic isocitrate dehydrogenase [NADP]; May supply 2-oxoglutarate for amino acid biosynthesis and ammonia assimilation via the glutamine synthetase/glutamate synthase (GS/GOGAT) pathway. May be involved in the production of NADPH to promote redox signaling or homeostasis in response to oxidative stress. Belongs to the isocitrate and isopropylmalate dehydrogenases family. | Peroxisomal isocitrate dehydrogenase [NADP]; May be involved in response to oxidative stresses. Belongs to the isocitrate and isopropylmalate dehydrogenases family. | 0.901 |
CICDH | T15N1.80 | Q9SRZ6 | Q8LPJ5 | Cytosolic isocitrate dehydrogenase [NADP]; May supply 2-oxoglutarate for amino acid biosynthesis and ammonia assimilation via the glutamine synthetase/glutamate synthase (GS/GOGAT) pathway. May be involved in the production of NADPH to promote redox signaling or homeostasis in response to oxidative stress. Belongs to the isocitrate and isopropylmalate dehydrogenases family. | Isocitrate dehydrogenase [NADP], chloroplastic/mitochondrial; May be involved in response to oxidative stresses. Belongs to the isocitrate and isopropylmalate dehydrogenases family. | 0.901 |
CNX1 | CRT1 | P29402 | O04151 | Calnexin homolog 1; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity); Belongs to the calreticulin family. | Calreticulin-1; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). | 0.955 |
CNX1 | CRT2 | P29402 | Q38858 | Calnexin homolog 1; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity); Belongs to the calreticulin family. | Calreticulin-2; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). | 0.956 |
CNX1 | CRT3 | P29402 | O04153 | Calnexin homolog 1; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity); Belongs to the calreticulin family. | Calreticulin-3; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Required for elongation factor Tu receptor (EFR) accumulation and for EFR, but not flagellin-sensing 2 (FLS2) signaling. | 0.933 |
CNX1 | T2I1_50 | P29402 | Q38798 | Calnexin homolog 1; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity); Belongs to the calreticulin family. | Calnexin homolog 2; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity). | 0.939 |
CNX1 | XYLT | P29402 | Q9LDH0 | Calnexin homolog 1; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity); Belongs to the calreticulin family. | Beta-1,2-xylosyltransferase; Glycosyltransferase involved in the xylosylation of N-glycans. Possesses beta-1,2-xylosyltransferase activity, transferring xylose from UDP-xylose to the core beta-linked mannose of N-glycans. Involved in the biosynthesis of glycoprotein bound N-glycans. Does not require metal ions for its activity. | 0.601 |
CRT1 | CNX1 | O04151 | P29402 | Calreticulin-1; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). | Calnexin homolog 1; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity); Belongs to the calreticulin family. | 0.955 |
CRT1 | CRT2 | O04151 | Q38858 | Calreticulin-1; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). | Calreticulin-2; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). | 0.948 |
CRT1 | CRT3 | O04151 | O04153 | Calreticulin-1; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). | Calreticulin-3; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Required for elongation factor Tu receptor (EFR) accumulation and for EFR, but not flagellin-sensing 2 (FLS2) signaling. | 0.916 |
CRT1 | T2I1_50 | O04151 | Q38798 | Calreticulin-1; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). | Calnexin homolog 2; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity). | 0.950 |
CRT1 | XYLT | O04151 | Q9LDH0 | Calreticulin-1; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). | Beta-1,2-xylosyltransferase; Glycosyltransferase involved in the xylosylation of N-glycans. Possesses beta-1,2-xylosyltransferase activity, transferring xylose from UDP-xylose to the core beta-linked mannose of N-glycans. Involved in the biosynthesis of glycoprotein bound N-glycans. Does not require metal ions for its activity. | 0.575 |
CRT2 | CNX1 | Q38858 | P29402 | Calreticulin-2; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). | Calnexin homolog 1; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity); Belongs to the calreticulin family. | 0.956 |
CRT2 | CRT1 | Q38858 | O04151 | Calreticulin-2; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). | Calreticulin-1; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). | 0.948 |
CRT2 | CRT3 | Q38858 | O04153 | Calreticulin-2; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). | Calreticulin-3; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Required for elongation factor Tu receptor (EFR) accumulation and for EFR, but not flagellin-sensing 2 (FLS2) signaling. | 0.919 |
CRT2 | T2I1_50 | Q38858 | Q38798 | Calreticulin-2; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). | Calnexin homolog 2; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity). | 0.951 |
CRT2 | XYLT | Q38858 | Q9LDH0 | Calreticulin-2; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). | Beta-1,2-xylosyltransferase; Glycosyltransferase involved in the xylosylation of N-glycans. Possesses beta-1,2-xylosyltransferase activity, transferring xylose from UDP-xylose to the core beta-linked mannose of N-glycans. Involved in the biosynthesis of glycoprotein bound N-glycans. Does not require metal ions for its activity. | 0.574 |
CRT3 | CNX1 | O04153 | P29402 | Calreticulin-3; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Required for elongation factor Tu receptor (EFR) accumulation and for EFR, but not flagellin-sensing 2 (FLS2) signaling. | Calnexin homolog 1; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (By similarity); Belongs to the calreticulin family. | 0.933 |
CRT3 | CRT1 | O04153 | O04151 | Calreticulin-3; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Required for elongation factor Tu receptor (EFR) accumulation and for EFR, but not flagellin-sensing 2 (FLS2) signaling. | Calreticulin-1; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). | 0.916 |
CRT3 | CRT2 | O04153 | Q38858 | Calreticulin-3; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Required for elongation factor Tu receptor (EFR) accumulation and for EFR, but not flagellin-sensing 2 (FLS2) signaling. | Calreticulin-2; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). | 0.919 |