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
ATP7BCopper-transporting ATPase 2; Copper ion transmembrane transporter involved in the export of copper out of the cells. It is involved in copper homeostasis in the liver, where it ensures the efflux of copper from hepatocytes into the bile in response to copper overload. Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily. (1465 aa)    
Predicted Functional Partners:
ATOX1
Copper transport protein ATOX1; Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense; Belongs to the ATX1 family.
    
 
 0.998
CCS
Copper chaperone for superoxide dismutase; Delivers copper to copper zinc superoxide dismutase (SOD1); In the C-terminal section; belongs to the Cu-Zn superoxide dismutase family.
  
 0.992
CP
Ceruloplasmin; Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane. Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1. May also play a role in fetal lung development or pulmonary antioxidant defense (By similarity).
  
 
 0.979
COMMD1
COMM domain-containing protein 1; Proposed scaffold protein that is implicated in diverse physiological processes and whose function may be in part linked to its ability to regulate ubiquitination of specific cellular proteins. Can modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes by displacing CAND1; in vitro promotes CRL E3 activity and dissociates CAND1 from CUL1 and CUL2. Promotes ubiquitination of NF-kappa-B subunit RELA and its subsequent proteasomal degradation. Down-regulates NF-kappa-B activity. Involved in the regulation of membrane expression and ubiquitin [...]
    
 
 0.978
SLC31A1
High affinity copper uptake protein 1; High-affinity, saturable copper transporter involved in dietary copper uptake.
   
 
 0.943
SLC31A2
Probable low affinity copper uptake protein 2; Involved in low-affinity copper uptake.
    
 
 0.930
ATP7A
Copper-transporting ATPase 1; May supply copper to copper-requiring proteins within the secretory pathway, when localized in the trans-Golgi network. Under conditions of elevated extracellular copper, it relocalized to the plasma membrane where it functions in the efflux of copper from cells; Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.
  
 
0.908
GLRX
Glutaredoxin-1; Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins; Belongs to the glutaredoxin family.
   
 
 0.856
ATP13A3
ATPase 13A3; Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type V subfamily.
  
 0.827
MT1E
Metallothionein; Metallothioneins have a high content of cysteine residues that bind various heavy metals.
      
 0.823
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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