13 items (human) - STRING interaction network

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

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experimentally determined

Predicted Interactions

gene neighborhood

gene fusions

gene co-occurrence

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co-expression

protein homology

Your Input:
	CRYBB3	Beta-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)
	CRYBA1	Beta-crystallin A3, isoform A1, Delta4 form; Crystallins are the dominant structural components of the vertebrate eye lens. (215 aa)
	CRYGB	Gamma-crystallin B; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. (175 aa)
	ATP5F1B	ATP synthase subunit beta, mitochondrial; Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the c [...] (529 aa)
	CRYGD	Gamma-crystallin D; Crystallins are the dominant structural components of the vertebrate eye lens. (174 aa)
	CRYAA	Alpha-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)
	CRYBA2	Beta-crystallin A2; Crystallins are the dominant structural components of the vertebrate eye lens. (197 aa)
	CRYBA4	Beta-crystallin A4; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. (196 aa)
	CRYBB1	Beta-crystallin B1; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. (252 aa)
	UBQLN1	Ubiquilin-1; Plays an important role in the regulation of different protein degradation mechanisms and pathways including ubiquitin- proteasome system (UPS), autophagy and endoplasmic reticulum-associated protein degradation (ERAD) pathway. Mediates the proteasomal targeting of misfolded or accumulated proteins for degradation by binding (via UBA domain) to their polyubiquitin chains and by interacting (via ubiquitin-like domain) with the subunits of the proteasome. Plays a role in the ERAD pathway via its interaction with ER-localized proteins UBXN4, VCP and HERPUD1 and may form a lin [...] (589 aa)
	CRYGS	Gamma-crystallin S; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family. (178 aa)
	ESR1	Estrogen receptor; Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE- independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial a [...] (595 aa)
	CRYAB	Alpha-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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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
CRYAA	CRYAB	ENSP00000291554	ENSP00000433560	Alpha-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.	Alpha-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.	0.996
CRYAA	CRYBA1	ENSP00000291554	ENSP00000225387	Alpha-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.	Beta-crystallin A3, isoform A1, Delta4 form; Crystallins are the dominant structural components of the vertebrate eye lens.	0.987
CRYAA	CRYBA2	ENSP00000291554	ENSP00000295728	Alpha-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.	Beta-crystallin A2; Crystallins are the dominant structural components of the vertebrate eye lens.	0.817
CRYAA	CRYBA4	ENSP00000291554	ENSP00000346805	Alpha-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.	Beta-crystallin A4; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family.	0.909
CRYAA	CRYBB1	ENSP00000291554	ENSP00000497249	Alpha-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.	Beta-crystallin B1; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family.	0.860
CRYAA	CRYBB3	ENSP00000291554	ENSP00000215855	Alpha-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.	Beta-crystallin B3, N-terminally processed; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family.	0.886
CRYAA	CRYGB	ENSP00000291554	ENSP00000260988	Alpha-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.	Gamma-crystallin B; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family.	0.811
CRYAA	CRYGD	ENSP00000291554	ENSP00000264376	Alpha-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.	Gamma-crystallin D; Crystallins are the dominant structural components of the vertebrate eye lens.	0.916
CRYAA	CRYGS	ENSP00000291554	ENSP00000376287	Alpha-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.	Gamma-crystallin S; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family.	0.960
CRYAB	CRYAA	ENSP00000433560	ENSP00000291554	Alpha-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.	Alpha-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.	0.996
CRYAB	CRYBA1	ENSP00000433560	ENSP00000225387	Alpha-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.	Beta-crystallin A3, isoform A1, Delta4 form; Crystallins are the dominant structural components of the vertebrate eye lens.	0.911
CRYAB	CRYBA2	ENSP00000433560	ENSP00000295728	Alpha-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.	Beta-crystallin A2; Crystallins are the dominant structural components of the vertebrate eye lens.	0.738
CRYAB	CRYBA4	ENSP00000433560	ENSP00000346805	Alpha-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.	Beta-crystallin A4; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family.	0.811
CRYAB	CRYBB1	ENSP00000433560	ENSP00000497249	Alpha-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.	Beta-crystallin B1; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family.	0.823
CRYAB	CRYBB3	ENSP00000433560	ENSP00000215855	Alpha-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.	Beta-crystallin B3, N-terminally processed; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family.	0.820
CRYAB	CRYGB	ENSP00000433560	ENSP00000260988	Alpha-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.	Gamma-crystallin B; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family.	0.667
CRYAB	CRYGD	ENSP00000433560	ENSP00000264376	Alpha-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.	Gamma-crystallin D; Crystallins are the dominant structural components of the vertebrate eye lens.	0.924
CRYAB	CRYGS	ENSP00000433560	ENSP00000376287	Alpha-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.	Gamma-crystallin S; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family.	0.924
CRYBA1	CRYAA	ENSP00000225387	ENSP00000291554	Beta-crystallin A3, isoform A1, Delta4 form; Crystallins are the dominant structural components of the vertebrate eye lens.	Alpha-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.	0.987
CRYBA1	CRYAB	ENSP00000225387	ENSP00000433560	Beta-crystallin A3, isoform A1, Delta4 form; Crystallins are the dominant structural components of the vertebrate eye lens.	Alpha-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.	0.911