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PMP22 protein (human) - STRING interaction network
"PMP22" - Peripheral myelin protein 22 in Homo sapiens
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Predicted Interactions
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textmining
co-expression
protein homology
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PMP22Peripheral myelin protein 22; Might be involved in growth regulation, and in myelinization in the peripheral nervous system; Belongs to the PMP-22/EMP/MP20 family (160 aa)    
Predicted Functional Partners:
MPZ
Myelin protein P0; Is an adhesion molecule necessary for normal myelination in the peripheral nervous system. It mediates adhesion between adjacent myelin wraps and ultimately drives myelin compaction; Ig-like cell adhesion molecule family (248 aa)
     
 
  0.919
LAMB1
Laminin subunit beta-1; Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Involved in the organization of the laminar architecture of cerebral cortex. It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons. Radial glial cells play a central role in cerebral cortical dev [...] (1786 aa)
     
 
    0.905
ITGB4
Integrin beta-4; Integrin alpha-6/beta-4 is a receptor for laminin. Plays a critical structural role in the hemidesmosome of epithelial cells. Is required for the regulation of keratinocyte polarity and motility. ITGA6-ITGB4 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling. ITGA6-ITGB4 binds to IGF1 and this binding is essential for IGF1 signaling (1822 aa)
     
 
  0.905
ITGA6
Integrin alpha-6; Integrin alpha-6/beta-1 is a receptor for laminin on platelets. Integrin alpha-6/beta-4 is a receptor for laminin in epithelial cells and it plays a critical structural role in the hemidesmosome (By similarity). ITGA6-ITGB4 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling. ITGA6-ITGB4 binds to IGF1 and this binding is essential for IGF1 signaling (1091 aa)
         
    0.900
LAMA1
Laminin subunit alpha-1; Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components (3075 aa)
         
    0.900
LAMC2
Laminin subunit gamma-2; Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Ladsin exerts cell- scattering activity toward a wide variety of cells, including epithelial, endothelial, and fibroblastic cells (1193 aa)
         
    0.900
GJB1
Gap junction beta-1 protein; One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell (283 aa)
     
   
  0.792
CLDN11
Claudin-11; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium- independent cell-adhesion activity; Claudins (207 aa)
           
  0.747
TSPAN4
Tetraspanin-4; Tetraspanin 4; Belongs to the tetraspanin (TM4SF) family (238 aa)
     
   
  0.698
MAG
Myelin-associated glycoprotein; Adhesion molecule that mediates interactions between myelinating cells and neurons by binding to neuronal sialic acid- containing gangliosides and to the glycoproteins RTN4R and RTN4RL2 (By similarity). Not required for initial myelination, but seems to play a role in the maintenance of normal axon myelination. Protects motoneurons against apoptosis, also after injury; protection against apoptosis is probably mediated via interaction with neuronal RTN4R and RTN4RL2. Required to prevent degeneration of myelinated axons in adults; this probably depends on [...] (626 aa)
     
   
  0.684
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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