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 Size
small nodes:
protein of unknown 3D structure
protein of unknown 3D structure
large nodes:
some 3D structure is known or predicted
some 3D structure is known or predicted
Node Color
colored nodes:
query proteins and first shell of interactors
query proteins and first shell of interactors
white nodes:
second shell of interactors
second shell of interactors
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 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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Your Input:
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Neighborhood |
Gene Fusion |
Cooccurence |
Coexpression |
Experiments |
Databases |
Textmining |
[Homology] |
Score |
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 | LIM2 | lens intrinsic membrane protein 2, 19kDa; 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 (215 aa) | ||||||||||||
Predicted Functional Partners:
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 | TMEM114 | transmembrane protein 114 (123 aa) |
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0.752 | ||||||||||
 | PDLIM7 | PDZ and LIM domain 7 (enigma); May function as a scaffold on which the coordinated assembly of proteins can occur. May play a role as an adapter that, via its PDZ domain, localizes LIM-binding proteins to actin filaments of both skeletal muscle and nonmuscle tissues. Involved in both of the two fundamental mechanisms of bone formation, direct bone formation (e.g. embryonic flat bones mandible and cranium), and endochondral bone formation (e.g. embryonic long bone development). Plays a role during fracture repair. Involved in BMP6 signaling pathway (By similarity) (457 aa) |
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0.742 | ||||||||||
 | CRYBB1 | crystallin, beta B1; Crystallins are the dominant structural components of the vertebrate eye lens (252 aa) |
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0.720 | ||||||||||
 | CRYAA | crystallin, alpha A; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions (173 aa) |
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0.688 | |||||||||
 | CRYGC | crystallin, gamma C; Crystallins are the dominant structural components of the vertebrate eye lens (174 aa) |
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0.649 | ||||||||||
 | LGALS3 | lectin, galactoside-binding, soluble, 3; Galactose-specific lectin which binds IgE. May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration. Together with DMBT1, required for terminal differentiation of columnar epithelial cells during early embryogenesis (By similarity). In the nucleus- acts as a pre-mRNA splicing factor. Involved in acute inflammatory responses including neutrophil activation and adhesion, chemoattraction of monocytes macrophages, opsonization of apoptotic neutrophils, and activation of mast cells (250 aa) |
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0.640 | |||||||||
 | ETFB | electron-transfer-flavoprotein, beta polypeptide; The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl- CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (346 aa) |
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0.610 | ||||||||||
 | CRYBA4 | crystallin, beta A4; Crystallins are the dominant structural components of the vertebrate eye lens (196 aa) |
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0.585 | ||||||||||
 | CRYBA1 | crystallin, beta A1; Crystallins are the dominant structural components of the vertebrate eye lens (215 aa) |
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0.583 | ||||||||||
 | GJA8 | gap junction protein, alpha 8, 50kDa (433 aa) |
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0.582 | ||||||||||
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
Other names: H. sapiens, Homo, Homo sapiens, human, man
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