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C21orf62 C21orf62 CALCOCO1 CALCOCO1 IGDCC3 IGDCC3 CRYBA2 CRYBA2 ESYT3 ESYT3 CRYBB1 CRYBB1 CRYBB2 CRYBB2 CRYAA CRYAA CRYAB CRYAB CRYBB3 CRYBB3 CRYM CRYM
"CRYBA2" - crystallin, beta A2 in Homo sapiens
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 protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
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colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
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
database edge
from curated databases
experiment edge
experimentally determined
Predicted Interactions
neighborhood edge
gene neighborhood
fusion edge
gene fusions
cooccurrence edge
gene co-occurrence
Others
textmining edge
textmining
coexpression edge
co-expression
homology edge
protein homology
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[Homology]
Score
CRYBA2crystallin, beta A2; Crystallins are the dominant structural components of the vertebrate eye lens (197 aa)    
Predicted Functional Partners:
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)
      score_image     score_image   0.685
CRYBB3
crystallin, beta B3; Crystallins are the dominant structural components of the vertebrate eye lens (211 aa)
        score_image   score_image score_image 0.603
CRYBB2
crystallin, beta B2; Crystallins are the dominant structural components of the vertebrate eye lens (205 aa)
        score_image   score_image score_image 0.603
CRYBB1
crystallin, beta B1; Crystallins are the dominant structural components of the vertebrate eye lens (252 aa)
      score_image score_image   score_image score_image 0.602
IGDCC3
immunoglobulin superfamily, DCC subclass, member 3 (814 aa)
            score_image   0.552
CRYAB
crystallin, alpha B; 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 (175 aa)
            score_image   0.509
CALCOCO1
calcium binding and coiled-coil domain 1; Functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). Recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. Involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. Functions as a secondary coactivator in LEF1- mediated transcriptional activation via its inte [...] (691 aa)
        score_image       0.506
C21orf62
chromosome 21 open reading frame 62 (219 aa)
            score_image   0.506
CRYM
crystallin, mu; Specifically catalyzes the reduction of imine bonds in brain substrates that may include cystathionine ketimine (CysK) and lanthionine ketimine (LK). Binds thyroid hormone which is a strong reversible inhibitor. Presumably involved in the regulation of the free intracellular concentration of triiodothyronine and access to its nuclear receptors (314 aa)
            score_image   0.481
ESYT3
extended synaptotagmin-like protein 3; May play a role as calcium-regulated intrinsic membrane protein (By similarity) (886 aa)
            score_image   0.471
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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