| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CA3 | GGT1 | ENSP00000285381 | ENSP00000383232 | Carbonic anhydrase 3; Reversible hydration of carbon dioxide; Carbonic anhydrases | Glutathione hydrolase 1 proenzyme; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione ( [...] | 0.687 |
| CA3 | GGT2 | ENSP00000285381 | ENSP00000385721 | Carbonic anhydrase 3; Reversible hydration of carbon dioxide; Carbonic anhydrases | Inactive glutathione hydrolase 2; Isoform 1, isoform 2 and isoform 3 lack catalytic activity due to its inability to undergo the autocatalytic cleavage needed to produce a mature, enzymatically active heterodimer; Gamma-glutamyltransferases | 0.687 |
| CA3 | GGTLC3 | ENSP00000285381 | ENSP00000477856 | Carbonic anhydrase 3; Reversible hydration of carbon dioxide; Carbonic anhydrases | Gamma-glutamyltransferase light chain family member 3; Gamma-glutamyltransferases | 0.687 |
| CA3 | TTC3 | ENSP00000285381 | ENSP00000381981 | Carbonic anhydrase 3; Reversible hydration of carbon dioxide; Carbonic anhydrases | E3 ubiquitin-protein ligase TTC3; E3 ubiquitin-protein ligase that mediates the ubiquitination and subsequent degradation of phosphorylated Akt (AKT1, AKT2 and AKT3) in the nucleus. Acts as a terminal regulator of Akt signaling after activation; its phosphorylation by Akt, which is a prerequisite for ubiquitin ligase activity, suggests the existence of a regulation mechanism required to control Akt levels after activation. Catalyzes the formation of ’Lys-48’- polyubiquitin chains. May play a role in neuronal differentiation inhibition via its interaction with CIT; Ring finger proteins | 0.794 |
| CCT3 | GGACT | ENSP00000295688 | ENSP00000365426 | T-complex protein 1 subunit gamma; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin; Chaperonins | Gamma-glutamylaminecyclotransferase; Contributes to degradation of proteins cross-linked by transglutaminases by degrading the cross-link between a lysine and a glutamic acid residue. Catalyzes the formation of 5-oxo-L- proline from L-gamma-glutamyl-L-epsilon-lysine. Inactive with L- gamma-glutamyl-alpha-amino acid substrates such as L-gamma- glutamyl-L-alpha-cysteine and L-gamma-glutamyl-L-alpha-alanine; Belongs to the gamma-glutamylcyclotransferase family | 0.407 |
| CCT3 | GGT1 | ENSP00000295688 | ENSP00000383232 | T-complex protein 1 subunit gamma; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin; Chaperonins | Glutathione hydrolase 1 proenzyme; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione ( [...] | 0.700 |
| CCT3 | GGT2 | ENSP00000295688 | ENSP00000385721 | T-complex protein 1 subunit gamma; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin; Chaperonins | Inactive glutathione hydrolase 2; Isoform 1, isoform 2 and isoform 3 lack catalytic activity due to its inability to undergo the autocatalytic cleavage needed to produce a mature, enzymatically active heterodimer; Gamma-glutamyltransferases | 0.700 |
| CCT3 | GGTLC3 | ENSP00000295688 | ENSP00000477856 | T-complex protein 1 subunit gamma; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin; Chaperonins | Gamma-glutamyltransferase light chain family member 3; Gamma-glutamyltransferases | 0.700 |
| CCT3 | TTC3 | ENSP00000295688 | ENSP00000381981 | T-complex protein 1 subunit gamma; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin; Chaperonins | E3 ubiquitin-protein ligase TTC3; E3 ubiquitin-protein ligase that mediates the ubiquitination and subsequent degradation of phosphorylated Akt (AKT1, AKT2 and AKT3) in the nucleus. Acts as a terminal regulator of Akt signaling after activation; its phosphorylation by Akt, which is a prerequisite for ubiquitin ligase activity, suggests the existence of a regulation mechanism required to control Akt levels after activation. Catalyzes the formation of ’Lys-48’- polyubiquitin chains. May play a role in neuronal differentiation inhibition via its interaction with CIT; Ring finger proteins | 0.733 |
| DSCR3 | TTC3 | ENSP00000311399 | ENSP00000381981 | Down syndrome critical region gene 3; Belongs to the VPS26 family | E3 ubiquitin-protein ligase TTC3; E3 ubiquitin-protein ligase that mediates the ubiquitination and subsequent degradation of phosphorylated Akt (AKT1, AKT2 and AKT3) in the nucleus. Acts as a terminal regulator of Akt signaling after activation; its phosphorylation by Akt, which is a prerequisite for ubiquitin ligase activity, suggests the existence of a regulation mechanism required to control Akt levels after activation. Catalyzes the formation of ’Lys-48’- polyubiquitin chains. May play a role in neuronal differentiation inhibition via its interaction with CIT; Ring finger proteins | 0.657 |
| GGACT | CCT3 | ENSP00000365426 | ENSP00000295688 | Gamma-glutamylaminecyclotransferase; Contributes to degradation of proteins cross-linked by transglutaminases by degrading the cross-link between a lysine and a glutamic acid residue. Catalyzes the formation of 5-oxo-L- proline from L-gamma-glutamyl-L-epsilon-lysine. Inactive with L- gamma-glutamyl-alpha-amino acid substrates such as L-gamma- glutamyl-L-alpha-cysteine and L-gamma-glutamyl-L-alpha-alanine; Belongs to the gamma-glutamylcyclotransferase family | T-complex protein 1 subunit gamma; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin; Chaperonins | 0.407 |
| GGACT | GGT1 | ENSP00000365426 | ENSP00000383232 | Gamma-glutamylaminecyclotransferase; Contributes to degradation of proteins cross-linked by transglutaminases by degrading the cross-link between a lysine and a glutamic acid residue. Catalyzes the formation of 5-oxo-L- proline from L-gamma-glutamyl-L-epsilon-lysine. Inactive with L- gamma-glutamyl-alpha-amino acid substrates such as L-gamma- glutamyl-L-alpha-cysteine and L-gamma-glutamyl-L-alpha-alanine; Belongs to the gamma-glutamylcyclotransferase family | Glutathione hydrolase 1 proenzyme; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione ( [...] | 0.627 |
| GGACT | GGT2 | ENSP00000365426 | ENSP00000385721 | Gamma-glutamylaminecyclotransferase; Contributes to degradation of proteins cross-linked by transglutaminases by degrading the cross-link between a lysine and a glutamic acid residue. Catalyzes the formation of 5-oxo-L- proline from L-gamma-glutamyl-L-epsilon-lysine. Inactive with L- gamma-glutamyl-alpha-amino acid substrates such as L-gamma- glutamyl-L-alpha-cysteine and L-gamma-glutamyl-L-alpha-alanine; Belongs to the gamma-glutamylcyclotransferase family | Inactive glutathione hydrolase 2; Isoform 1, isoform 2 and isoform 3 lack catalytic activity due to its inability to undergo the autocatalytic cleavage needed to produce a mature, enzymatically active heterodimer; Gamma-glutamyltransferases | 0.629 |
| GGACT | GGTLC3 | ENSP00000365426 | ENSP00000477856 | Gamma-glutamylaminecyclotransferase; Contributes to degradation of proteins cross-linked by transglutaminases by degrading the cross-link between a lysine and a glutamic acid residue. Catalyzes the formation of 5-oxo-L- proline from L-gamma-glutamyl-L-epsilon-lysine. Inactive with L- gamma-glutamyl-alpha-amino acid substrates such as L-gamma- glutamyl-L-alpha-cysteine and L-gamma-glutamyl-L-alpha-alanine; Belongs to the gamma-glutamylcyclotransferase family | Gamma-glutamyltransferase light chain family member 3; Gamma-glutamyltransferases | 0.629 |
| GGACT | TTC3 | ENSP00000365426 | ENSP00000381981 | Gamma-glutamylaminecyclotransferase; Contributes to degradation of proteins cross-linked by transglutaminases by degrading the cross-link between a lysine and a glutamic acid residue. Catalyzes the formation of 5-oxo-L- proline from L-gamma-glutamyl-L-epsilon-lysine. Inactive with L- gamma-glutamyl-alpha-amino acid substrates such as L-gamma- glutamyl-L-alpha-cysteine and L-gamma-glutamyl-L-alpha-alanine; Belongs to the gamma-glutamylcyclotransferase family | E3 ubiquitin-protein ligase TTC3; E3 ubiquitin-protein ligase that mediates the ubiquitination and subsequent degradation of phosphorylated Akt (AKT1, AKT2 and AKT3) in the nucleus. Acts as a terminal regulator of Akt signaling after activation; its phosphorylation by Akt, which is a prerequisite for ubiquitin ligase activity, suggests the existence of a regulation mechanism required to control Akt levels after activation. Catalyzes the formation of ’Lys-48’- polyubiquitin chains. May play a role in neuronal differentiation inhibition via its interaction with CIT; Ring finger proteins | 0.730 |
| GGT1 | CA3 | ENSP00000383232 | ENSP00000285381 | Glutathione hydrolase 1 proenzyme; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione ( [...] | Carbonic anhydrase 3; Reversible hydration of carbon dioxide; Carbonic anhydrases | 0.687 |
| GGT1 | CCT3 | ENSP00000383232 | ENSP00000295688 | Glutathione hydrolase 1 proenzyme; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione ( [...] | T-complex protein 1 subunit gamma; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin; Chaperonins | 0.700 |
| GGT1 | GGACT | ENSP00000383232 | ENSP00000365426 | Glutathione hydrolase 1 proenzyme; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione ( [...] | Gamma-glutamylaminecyclotransferase; Contributes to degradation of proteins cross-linked by transglutaminases by degrading the cross-link between a lysine and a glutamic acid residue. Catalyzes the formation of 5-oxo-L- proline from L-gamma-glutamyl-L-epsilon-lysine. Inactive with L- gamma-glutamyl-alpha-amino acid substrates such as L-gamma- glutamyl-L-alpha-cysteine and L-gamma-glutamyl-L-alpha-alanine; Belongs to the gamma-glutamylcyclotransferase family | 0.627 |
| GGT1 | GGT2 | ENSP00000383232 | ENSP00000385721 | Glutathione hydrolase 1 proenzyme; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione ( [...] | Inactive glutathione hydrolase 2; Isoform 1, isoform 2 and isoform 3 lack catalytic activity due to its inability to undergo the autocatalytic cleavage needed to produce a mature, enzymatically active heterodimer; Gamma-glutamyltransferases | 0.704 |
| GGT1 | SLC18A1 | ENSP00000383232 | ENSP00000387549 | Glutathione hydrolase 1 proenzyme; Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione ( [...] | Chromaffin granule amine transporter; Involved in the transport of biogenic monoamines, such as serotonin, from the cytoplasm into the secretory vesicles of neuroendocrine and endocrine cells; Belongs to the major facilitator superfamily. Vesicular transporter family | 0.497 |
