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:
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 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
Cooccurence
Coexpression
Experiments
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[Homology]
Score
ALADDelta-aminolevulinic acid dehydratase; Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen; Belongs to the ALAD family (330 aa)    
Predicted Functional Partners:
HMBS
Porphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps; Belongs to the HMBS family
 
 0.997
ALAS2
5-aminolevulinate synthase, erythroid-specific, mitochondrial; 5'-aminolevulinate synthase 2
  
 
 0.985
ALAS1
5-aminolevulinate synthase, nonspecific, mitochondrial; 5'-aminolevulinate synthase 1; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family
  
 
 0.985
UROD
Uroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III
 
 
 0.980
UROS
Uroporphyrinogen-III synthase; Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III, the branch point for the various sub-pathways leading to the wide diversity of porphyrins. Porphyrins act as cofactors for a multitude of enzymes that perform a variety of processes within the cell such as methionine synthesis (vitamin B12) or oxygen transport (heme)
  
 
 0.978
CPOX
Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial; Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX
  
  
 0.957
FECH
Ferrochelatase, mitochondrial; Catalyzes the ferrous insertion into protoporphyrin IX; Belongs to the ferrochelatase family
  
  
 0.947
PPOX
Protoporphyrinogen/coproporphyrinogen iii oxidase; Protoporphyrinogen oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX
  
  
 0.942
SLC25A38
Solute carrier family 25 member 38; Mitochondrial carrier required during erythropoiesis. Probably involved in the biosynthesis of heme, possibly by facilitating 5-aminolevulinate (ALA) production. May act by importing glycine into mitochondria or by exchanging glycine for ALA across the mitochondrial inner membrane; Belongs to the mitochondrial carrier (TC 2.A.29) family. SLC25A38 subfamily
   
  
 0.793
ATP5B
ATP synthase subunit beta, mitochondrial; Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the c [...]
 
 
 
 0.780
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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