STRINGSTRING
PGM1 protein (Latimeria chalumnae) - STRING interaction network
"PGM1" - Phosphoglucomutase 1 in Latimeria chalumnae
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 Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
PGM1Phosphoglucomutase 1 (593 aa)    
Predicted Functional Partners:
GPI
Glucose-6-phosphate isomerase (555 aa)
   
  0.995
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 (1365 aa)
   
 
  0.991
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 (838 aa)
   
 
  0.989
PYGB
Phosphorylase, glycogen; 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 (267 aa)
   
 
  0.989
UGP2
UDP-glucose pyrophosphorylase 2 (507 aa)
 
 
 
  0.978
PGM2L1
Phosphoglucomutase 2-like 1 (528 aa)
   
  0.969
HK2
Hexokinase-2 (918 aa)
     
 
  0.963
GCK
Glucokinase (hexokinase 4) (400 aa)
     
 
  0.963
HK1
Hexokinase 1 (919 aa)
     
 
  0.963
HKDC1
Hexokinase domain containing 1 (923 aa)
     
 
  0.963
Your Current Organism:
Latimeria chalumnae
NCBI taxonomy Id: 7897
Other names: Actinistia, Choanichthyes, Coelacanthidae, Coelacanthiformes, Coelacanthimorpha, Crossopterygii, L. chalumnae, Latimeria, Latimeria chalumnae, Latimeriidae, coelacanth, coelacanths, lobe-finned fishes
Server load: low (6%) [HD]