Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Size
small nodes:
protein of unknown 3D structure
protein of unknown 3D structure
large nodes:
some 3D structure is known or predicted
some 3D structure is known or predicted
Node Color
colored nodes:
query proteins and first shell of interactors
query proteins and first shell of interactors
white nodes:
second shell of interactors
second shell of interactors
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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 | PYGM | phosphorylase, glycogen, muscle; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties (By similarity) (842 aa) | ||
 | GNPTG | N-acetylglucosamine-1-phosphate transferase, gamma subunit; May recognize the substrate of GlcNAc-1- phosphotransferase but also the lysosomal proteins with mannose-6- phosphate residues (305 aa) | ||
 | PYGL | phosphorylase, glycogen, liver; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties (By similarity) (847 aa) | ||
 | PYGB | phosphorylase, glycogen; brain; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties (By similarity) (843 aa) | ||
 | TUSC3 | tumor suppressor candidate 3; Magnesium transporter. May be involved in N- glycosylation through its association with N-oligosaccharyl transferase (348 aa) | ||
 | MLEC | malectin; Carbohydrate-binding protein with a strong ligand preference for Glc2-N-glycan. May play a role in the early steps of protein N-glycosylation (By similarity) (292 aa) | ||
 | MOGS | mannosyl-oligosaccharide glucosidase; Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor in a highly specific manner (837 aa) | ||
 | CANX | calnexin; 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. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor- mediated endocytosis at [...] (592 aa) | ||
 | PRKCSH | protein kinase C substrate 80K-H; Regulatory subunit of glucosidase II (528 aa) | ||
 | AGL | amylo-alpha-1, 6-glucosidase, 4-alpha-glucanotransferase (1532 aa) | ||
 | HSP90B1 | heat shock protein 90kDa beta (Grp94), member 1; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (803 aa) | ||
 | CALR | calreticulin; Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity) (417 aa) | ||
 | CLGN | calmegin; Probably plays an important role in spermatogenesis. Binds calcium ions (610 aa) | ||
 | P4HB | prolyl 4-hydroxylase, beta polypeptide; 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). May be involved with [...] (508 aa) | ||
 | GANAB | glucosidase, alpha; neutral AB; Cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins (966 aa) | ||
 | MAN1A2 | mannosidase, alpha, class 1A, member 2; Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2) (641 aa) | ||
 | ERGIC2 | ERGIC and golgi 2; Possible role in transport between endoplasmic reticulum and Golgi (By similarity) (377 aa) | ||
 | AMY2B | amylase, alpha 2B (pancreatic) (511 aa) | ||
 | MAGT1 | magnesium transporter 1; May be involved in N-glycosylation through its association with N-oligosaccharyl transferase. May be involved in Mg(2+) transport in epithelial cells (367 aa) | ||
 | MAN1A1 | mannosidase, alpha, class 1A, member 1; Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2) (653 aa) | ||
 | AMY1C | amylase, alpha 1C (salivary) (511 aa) | ||
 | MAN1B1 | mannosidase, alpha, class 1B, member 1; Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trims the carbohydrates to Man(5-6)GlcNAc(2) (699 aa) | ||
 | MAN1C1 | mannosidase, alpha, class 1C, member 1; Involved in the maturation of Asn-linked oligosaccharides. Trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce first Man(8)GlcNAc(2) then Man(6)GlcNAc and a small amount of Man(5)GlcNAc (630 aa) | ||
 | PRRC2A | proline-rich coiled-coil 2A (2157 aa) | ||
 | AMY2A | amylase, alpha 2A (pancreatic) (511 aa) | ||
 | ZNF469 | zinc finger protein 469; May be involved in transcriptional regulation (3925 aa) | ||
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
Other names: H. sapiens, Homo, Homo sapiens, human, man
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