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
HCCSCytochrome c heme lyase; Links covalently the heme group to the apoprotein of cytochrome c. (271 aa)    
Predicted Functional Partners:
COX10
Protoheme IX farnesyltransferase, mitochondrial; Converts protoheme IX and farnesyl diphosphate to heme O. Belongs to the ubiA prenyltransferase family.
   
 
 0.918
LOC100355645
Uncharacterized protein.
 
  
 
 0.901
FECH
Ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX.
     
 0.873
HMOX2
Heme oxygenase 2; Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter.
     
 0.862
HMOX1
Heme oxygenase 1.
     
 0.857
TIMMDC1
Translocase of inner mitochondrial membrane domain containing 1.
    
   0.760
CYCS
Cytochrome c; Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
   
 0.759
LOC100354468
Cytochrome c domain-containing protein; Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
   
 0.742
LOC100341515
Cytochrome c domain-containing protein; Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
   
 0.742
LOC108178730
Cytochrome c domain-containing protein; Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
   
 0.742
Your Current Organism:
Oryctolagus cuniculus
NCBI taxonomy Id: 9986
Other names: European rabbit, Japanese white rabbit, Lepus cuniculus, New Zealand rabbit, O. cuniculus, domestic rabbit, rabbit, rabbits
Server load: medium (52%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.