STRINGSTRING
STRING protein interaction network
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.
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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
PGA12_2Phosphomutase-like protein 3. (307 aa)    
Predicted Functional Partners:
Cantr_07008
Aminotran_1_2 domain-containing protein.
      
 0.597
Cantr_06542
Uncharacterized protein.
      
 0.558
Cantr_01484
Uncharacterized protein.
      
 0.558
PDC2_0
Protein PDC2.
      
 0.544
PDC2_1
Protein PDC2.
      
 0.544
THI20_1
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI20.
      
 0.476
THI20_0
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI20.
      
 0.476
THI4_2
Thiamine thiazole synthase; Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5- (2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron- dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance; Belongs to the T [...]
      
 0.452
THI4_1
Thiamine thiazole synthase; Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5- (2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron- dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance; Belongs to the T [...]
      
 0.452
THI4_0
Thiamine thiazole synthase; Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5- (2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron- dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance; Belongs to the T [...]
      
 0.452
Your Current Organism:
Candida viswanathii
NCBI taxonomy Id: 5486
Other names: ATCC 22981, C. viswanathii, CBS 4024, CCRC 21330, CCRC:21330, Candida lodderae, Candida viswanathii Viswanathan & H.S. Randhawa ex R.S. Sandhu & H.S. Randhawa, 2015, DBVPG 6189, IFO 10321, JCM 9567, NRRL Y-6660
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