STRINGSTRING
CRYGS CRYGS CRYBB2 CRYBB2 MIP MIP CPOX CPOX CRYAA2 CRYAA2 CRYBA4 CRYBA4 BFSP1 BFSP1 CRYBG3 CRYBG3 CRYBB1 CRYBB1 CRYGN CRYGN BFSP2 BFSP2 HSPB2 HSPB2 CRYGA CRYGA CRYBA2 CRYBA2 CRYAA CRYAA CRYGC CRYGC CRYGD CRYGD CRYGB CRYGB CRYBA1 CRYBA1 LIM2 LIM2 CRYBB3 CRYBB3 HSPB6 HSPB6 VIM VIM CRYAB CRYAB
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:
CRYGSGamma-crystallin S; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. (178 aa)
CRYBB2Beta-crystallin B2; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. (205 aa)
MIPLens 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. (263 aa)
CPOXOxygen-dependent coproporphyrinogen-III oxidase, mitochondrial; Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen- IX. (454 aa)
CRYAA2Crystallin alpha A2. (173 aa)
CRYBA4Beta-crystallin A4; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. (196 aa)
BFSP1Filensin 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. (665 aa)
CRYBG3Very large A-kinase anchor protein; [Isoform vlAKAP]: Anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA). (2970 aa)
CRYBB1Beta-crystallin B1; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. (252 aa)
CRYGNCrystallin gamma N. (182 aa)
BFSP2Phakinin; Required for the correct formation and organization of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA. (415 aa)
HSPB2Heat shock protein beta-2; May regulate the kinase DMPK. (182 aa)
CRYGAGamma-crystallin A; Crystallins are the dominant structural components of the vertebrate eye lens. (174 aa)
CRYBA2Beta-crystallin A2; Crystallins are the dominant structural components of the vertebrate eye lens. (197 aa)
CRYAAAlpha-crystallin A2(1-162); Contributes 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. Belongs to the small heat shock protein (HSP20) family. (173 aa)
CRYGCGamma-crystallin C; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. (174 aa)
CRYGDGamma-crystallin D; Crystallins are the dominant structural components of the vertebrate eye lens. (174 aa)
CRYGBGamma-crystallin B; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. (175 aa)
CRYBA1Beta-crystallin A3, isoform A1, Delta4 form; Crystallins are the dominant structural components of the vertebrate eye lens. (215 aa)
LIM2Lens 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. (215 aa)
CRYBB3Beta-crystallin B3, N-terminally processed; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. (211 aa)
HSPB6Heat shock protein beta-6; Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding- competent state. Seems to have versatile functions in various biological processes. Plays a role in regulating muscle function such as smooth muscle vasorelaxation and cardiac myocyte contractility. May regulate myocardial angiogenesis implicating KDR. Overexpression mediates cardioprotection and angiogenesis after induced damage. Stabilizes monomeric YWHAZ thereby supporting YWHAZ chaperone-like activity. (160 aa)
VIMVimentin; Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. (466 aa)
CRYABAlpha-crystallin B chain; 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)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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