Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as short tabular text output:
TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)
... as tabular text output:
TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... protein node degrees:
node degree of proteins in your network (given the current score cut-off)
... network coordinates:
a flat-file format describing the coordinates and colors of nodes in the network
... protein sequences:
MFA: multi-fasta format - containing the aminoacid sequences in the network
... protein annotations:
a tab-delimited file describing the names, domains and descriptions of proteins in your network
... functional annotations:
a tab-delimited file containing all known functional terms of protiens in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ALG14 | COLQ | ENSP00000359224 | ENSP00000373298 | UDP-N-acetylglucosamine transferase subunit ALG14 homolog; May be involved in protein N-glycosylation. May play a role in the second step of the dolichol-linked oligosaccharide pathway. May anchor the catalytic subunit ALG13 to the ER. Belongs to the ALG14 family. | Acetylcholinesterase collagenic tail peptide; Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina; Belongs to the COLQ family. | 0.656 |
| ALG14 | DPAGT1 | ENSP00000359224 | ENSP00000386597 | UDP-N-acetylglucosamine transferase subunit ALG14 homolog; May be involved in protein N-glycosylation. May play a role in the second step of the dolichol-linked oligosaccharide pathway. May anchor the catalytic subunit ALG13 to the ER. Belongs to the ALG14 family. | UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase; Catalyzes the initial step of dolichol-linked oligosaccharide biosynthesis in N-linked protein glycosylation pathway: transfers GlcNAc-1-P from UDP-GlcNAc onto the carrier lipid dolichyl phosphate (P-dolichol), yielding GlcNAc-P-P-dolichol. | 0.999 |
| ALG14 | PREPL | ENSP00000359224 | ENSP00000386543 | UDP-N-acetylglucosamine transferase subunit ALG14 homolog; May be involved in protein N-glycosylation. May play a role in the second step of the dolichol-linked oligosaccharide pathway. May anchor the catalytic subunit ALG13 to the ER. Belongs to the ALG14 family. | Prolyl endopeptidase-like; Serine peptidase whose precise substrate specificity remains unclear. Does not cleave peptides after a arginine or lysine residue. Regulates trans-Golgi network morphology and sorting by regulating the membrane binding of the AP-1 complex. May play a role in the regulation of synaptic vesicle exocytosis. | 0.665 |
| APEH | PREP | ENSP00000296456 | ENSP00000499089 | Acylamino-acid-releasing enzyme; This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus. It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser; Belongs to the peptidase S9C family. | Prolyl endopeptidase; Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long; Belongs to the peptidase S9A family. | 0.931 |
| APEH | PREPL | ENSP00000296456 | ENSP00000386543 | Acylamino-acid-releasing enzyme; This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus. It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser; Belongs to the peptidase S9C family. | Prolyl endopeptidase-like; Serine peptidase whose precise substrate specificity remains unclear. Does not cleave peptides after a arginine or lysine residue. Regulates trans-Golgi network morphology and sorting by regulating the membrane binding of the AP-1 complex. May play a role in the regulation of synaptic vesicle exocytosis. | 0.580 |
| CAMKMT | PPM1B | ENSP00000367755 | ENSP00000282412 | Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of 'Lys-116' in calmodulin. Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family. | Protein phosphatase 1B; Enzyme with a broad specificity. Dephosphorylates CDK2 and CDK6 in vitro. Dephosphorylates PRKAA1 and PRKAA2. Inhibits TBK1- mediated antiviral signaling by dephosphorylating it at 'Ser-172'. Plays an important role in the termination of TNF-alpha-mediated NF- kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB. | 0.953 |
| CAMKMT | PREP | ENSP00000367755 | ENSP00000499089 | Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of 'Lys-116' in calmodulin. Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family. | Prolyl endopeptidase; Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long; Belongs to the peptidase S9A family. | 0.524 |
| CAMKMT | PREPL | ENSP00000367755 | ENSP00000386543 | Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of 'Lys-116' in calmodulin. Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family. | Prolyl endopeptidase-like; Serine peptidase whose precise substrate specificity remains unclear. Does not cleave peptides after a arginine or lysine residue. Regulates trans-Golgi network morphology and sorting by regulating the membrane binding of the AP-1 complex. May play a role in the regulation of synaptic vesicle exocytosis. | 0.976 |
| CAMKMT | SLC3A1 | ENSP00000367755 | ENSP00000260649 | Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of 'Lys-116' in calmodulin. Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family. | Neutral and basic amino acid transport protein rBAT; Involved in the high-affinity, sodium-independent transport of cystine and neutral and dibasic amino acids (system B(0,+)-like activity). May function as an activator of SLC7A9 and be involved in the high-affinity reabsorption of cystine in the kidney tubule. | 0.935 |
| COLQ | ALG14 | ENSP00000373298 | ENSP00000359224 | Acetylcholinesterase collagenic tail peptide; Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina; Belongs to the COLQ family. | UDP-N-acetylglucosamine transferase subunit ALG14 homolog; May be involved in protein N-glycosylation. May play a role in the second step of the dolichol-linked oligosaccharide pathway. May anchor the catalytic subunit ALG13 to the ER. Belongs to the ALG14 family. | 0.656 |
| COLQ | DPAGT1 | ENSP00000373298 | ENSP00000386597 | Acetylcholinesterase collagenic tail peptide; Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina; Belongs to the COLQ family. | UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase; Catalyzes the initial step of dolichol-linked oligosaccharide biosynthesis in N-linked protein glycosylation pathway: transfers GlcNAc-1-P from UDP-GlcNAc onto the carrier lipid dolichyl phosphate (P-dolichol), yielding GlcNAc-P-P-dolichol. | 0.633 |
| COLQ | PREPL | ENSP00000373298 | ENSP00000386543 | Acetylcholinesterase collagenic tail peptide; Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina; Belongs to the COLQ family. | Prolyl endopeptidase-like; Serine peptidase whose precise substrate specificity remains unclear. Does not cleave peptides after a arginine or lysine residue. Regulates trans-Golgi network morphology and sorting by regulating the membrane binding of the AP-1 complex. May play a role in the regulation of synaptic vesicle exocytosis. | 0.521 |
| DPAGT1 | ALG14 | ENSP00000386597 | ENSP00000359224 | UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase; Catalyzes the initial step of dolichol-linked oligosaccharide biosynthesis in N-linked protein glycosylation pathway: transfers GlcNAc-1-P from UDP-GlcNAc onto the carrier lipid dolichyl phosphate (P-dolichol), yielding GlcNAc-P-P-dolichol. | UDP-N-acetylglucosamine transferase subunit ALG14 homolog; May be involved in protein N-glycosylation. May play a role in the second step of the dolichol-linked oligosaccharide pathway. May anchor the catalytic subunit ALG13 to the ER. Belongs to the ALG14 family. | 0.999 |
| DPAGT1 | COLQ | ENSP00000386597 | ENSP00000373298 | UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase; Catalyzes the initial step of dolichol-linked oligosaccharide biosynthesis in N-linked protein glycosylation pathway: transfers GlcNAc-1-P from UDP-GlcNAc onto the carrier lipid dolichyl phosphate (P-dolichol), yielding GlcNAc-P-P-dolichol. | Acetylcholinesterase collagenic tail peptide; Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina; Belongs to the COLQ family. | 0.633 |
| DPAGT1 | PREPL | ENSP00000386597 | ENSP00000386543 | UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase; Catalyzes the initial step of dolichol-linked oligosaccharide biosynthesis in N-linked protein glycosylation pathway: transfers GlcNAc-1-P from UDP-GlcNAc onto the carrier lipid dolichyl phosphate (P-dolichol), yielding GlcNAc-P-P-dolichol. | Prolyl endopeptidase-like; Serine peptidase whose precise substrate specificity remains unclear. Does not cleave peptides after a arginine or lysine residue. Regulates trans-Golgi network morphology and sorting by regulating the membrane binding of the AP-1 complex. May play a role in the regulation of synaptic vesicle exocytosis. | 0.583 |
| DPP8 | PREP | ENSP00000339208 | ENSP00000499089 | Dipeptidyl peptidase 8; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | Prolyl endopeptidase; Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long; Belongs to the peptidase S9A family. | 0.955 |
| DPP8 | PREPL | ENSP00000339208 | ENSP00000386543 | Dipeptidyl peptidase 8; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. | Prolyl endopeptidase-like; Serine peptidase whose precise substrate specificity remains unclear. Does not cleave peptides after a arginine or lysine residue. Regulates trans-Golgi network morphology and sorting by regulating the membrane binding of the AP-1 complex. May play a role in the regulation of synaptic vesicle exocytosis. | 0.507 |
| PPM1B | CAMKMT | ENSP00000282412 | ENSP00000367755 | Protein phosphatase 1B; Enzyme with a broad specificity. Dephosphorylates CDK2 and CDK6 in vitro. Dephosphorylates PRKAA1 and PRKAA2. Inhibits TBK1- mediated antiviral signaling by dephosphorylating it at 'Ser-172'. Plays an important role in the termination of TNF-alpha-mediated NF- kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB. | Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of 'Lys-116' in calmodulin. Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family. | 0.953 |
| PPM1B | PREP | ENSP00000282412 | ENSP00000499089 | Protein phosphatase 1B; Enzyme with a broad specificity. Dephosphorylates CDK2 and CDK6 in vitro. Dephosphorylates PRKAA1 and PRKAA2. Inhibits TBK1- mediated antiviral signaling by dephosphorylating it at 'Ser-172'. Plays an important role in the termination of TNF-alpha-mediated NF- kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB. | Prolyl endopeptidase; Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long; Belongs to the peptidase S9A family. | 0.495 |
| PPM1B | PREPL | ENSP00000282412 | ENSP00000386543 | Protein phosphatase 1B; Enzyme with a broad specificity. Dephosphorylates CDK2 and CDK6 in vitro. Dephosphorylates PRKAA1 and PRKAA2. Inhibits TBK1- mediated antiviral signaling by dephosphorylating it at 'Ser-172'. Plays an important role in the termination of TNF-alpha-mediated NF- kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB. | Prolyl endopeptidase-like; Serine peptidase whose precise substrate specificity remains unclear. Does not cleave peptides after a arginine or lysine residue. Regulates trans-Golgi network morphology and sorting by regulating the membrane binding of the AP-1 complex. May play a role in the regulation of synaptic vesicle exocytosis. | 0.967 |
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