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:
a 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 to each other.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
AQR94727.1Hypothetical protein. (137 aa)    
Predicted Functional Partners:
slyA_5
Transcriptional regulator SlyA.
       0.804
glgA_2
Glycogen synthase; Synthesizes alpha-1,4-glucan chains using ADP-glucose.
   
    0.485
AQR94728.1
Acyltransferase PapA5.
       0.475
malP_1
Maltodextrin phosphorylase; 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.
   
    0.446
glgP_1
Glycogen phosphorylase; 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.
   
    0.446
ysdC
Putative aminopeptidase YsdC.
   
    0.446
glgP_2
Glycogen phosphorylase; 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.
   
    0.446
Your Current Organism:
Clostridium saccharoperbutylacetonicum
NCBI taxonomy Id: 36745
Other names: ATCC 27021, C. saccharoperbutylacetonicum, Clostridium saccharoperbutylacetonicum Keis et al. 2001, DSM 14923, NCIMB 12606, strain N1-4 (HMT)
Server load: low (36%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.