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
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Gene Fusion
Cooccurrence
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[Homology]
Score
SLC25A38Mitochondrial glycine transporter; Mitochondrial glycine transporter that imports glycine into the mitochondrial matrix. Plays an important role in providing glycine for the first enzymatic step in heme biosynthesis, the condensation of glycine with succinyl-CoA to produce 5-aminolevulinate (ALA) in the mitochondrial matrix. Required during erythropoiesis. Belongs to the mitochondrial carrier (TC 2.A.29) family. SLC25A38 subfamily. (304 aa)    
Predicted Functional Partners:
GLRX5
Glutaredoxin-related protein 5, mitochondrial; Monothiol glutaredoxin involved in the biogenesis of iron- sulfur clusters. Involved in protein lipoylation, acting in the pathway that provides an iron-sulfur cluster to lipoate synthase. Required for normal iron homeostasis. Required for normal regulation of hemoglobin synthesis by the iron- sulfur protein ACO1. May protect cells against apoptosis due to reactive oxygen species and oxidative stress (By similarity).
   
  
 0.943
ALAS2
5-aminolevulinate synthase, erythroid-specific, mitochondrial; 5'-aminolevulinate synthase 2.
   
  
 0.878
ABCB7
ATP-binding cassette sub-family B member 7, mitochondrial; Could be involved in the transport of heme from the mitochondria to the cytosol. Plays a central role in the maturation of cytosolic iron-sulfur (Fe/S) cluster-containing proteins.
   
  
 0.785
PPOX
Protoporphyrinogen oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
   
  
 0.694
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).
   
  
 0.694
FECH
Ferrochelatase, mitochondrial; Catalyzes the ferrous insertion into protoporphyrin IX; Belongs to the ferrochelatase family.
   
  
 0.684
UROD
Uroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
   
  
 0.664
ABCB6
ATP-binding cassette sub-family B member 6, mitochondrial; Binds heme and porphyrins and functions in their ATP- dependent uptake into the mitochondria. Plays a crucial role in heme synthesis; Belongs to the ABC transporter superfamily. ABCB family. Heavy Metal importer (TC 3.A.1.210) subfamily.
   
  
 0.664
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.
   
  
 0.649
TFRC
Transferrin receptor protein 1, serum form; Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes. Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). A second ligand, the heditary hemochromatosis protein HFE, competes for binding with tra [...]
   
  
 0.637
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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