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
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Score
HSF4Heat shock factor protein 4; DNA-binding protein that specifically binds heat shock promoter elements (HSE). Isoform HSF4A represses transcription while the isoform HSF4B activates transcription. Belongs to the HSF family. (492 aa)    
Predicted Functional Partners:
HSF2
Heat shock factor protein 2; DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked.
    
 
0.989
HSF1
Heat shock factor protein 1; Functions as a stress-inducible and DNA-binding transcription factor that plays a central role in the transcriptional activation of the heat shock response (HSR), leading to the expression of a large class of molecular chaperones heat shock proteins (HSPs) that protect cells from cellular insults' damage. In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA-binding inactivated monomeric form. Upon exposure to heat and other stress stimuli, undergoes homotrimerization and activates HSP gene transcription [...]
  
 
0.880
BFSP2
Phakinin; Required for the correct formation and organization of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA.
      
 0.753
LIM2
Lens fiber membrane intrinsic protein; Present in the thicker 16-17 nm junctions of mammalian lens fiber cells, where it may contribute to cell junctional organization. Acts as a receptor for calmodulin. May play an important role in both lens development and cataractogenesis; Belongs to the PMP-22/EMP/MP20 family.
   
  
 0.724
GJA8
Gap junction alpha-8 protein; Structural component of eye lens gap junctions. Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane (By similarity). Small molecules and ions diffuse from one cell to a neighboring cell via the central pore.
   
  
 0.723
CRYBB1
Beta-crystallin B1; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family.
    
 
 0.705
CRYGD
Gamma-crystallin D; Crystallins are the dominant structural components of the vertebrate eye lens.
      
 0.702
CRYGS
Gamma-crystallin S; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family.
   
  
 0.696
MIP
Lens fiber major intrinsic protein; Water channel. Channel activity is down- regulated by CALM when cytoplasmic Ca(2+) levels are increased. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core (By similarity). Plays a role in cell- to-cell adhesion and facilitates gap junction coupling ; Belongs to the MIP/aquaporin (TC 1.A.8) family.
    
 
 0.686
BFSP1
Filensin C-terminal fragment; Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA. Involved in altering the calcium regulation of MIP water permeability.
      
 0.681
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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