CRYAB protein (human) - STRING database

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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.

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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.

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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; Small heat shock proteins (175 aa)

Predicted Functional Partners:

MGEA5

0.960

HSF1

0.946

CRYA1

0.913

CRYBB2

0.903

HSPB4

0.898

CRYBA1

0.873

CRYBB1

0.852

CRYGS

0.842

CRYGC

0.833

PRNP

0.832

Your Current Organism:

Homo sapiens

NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man

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a tab-delimited file describing the names, domains and annotated functions of the network proteins

Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
CRYA1	CRYAB	ENSP00000482816	ENSP00000433560	Alpha-crystallin A chain; 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; Small heat shock proteins	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; Small heat shock proteins	0.913
CRYA1	CRYBA1	ENSP00000482816	ENSP00000225387	Alpha-crystallin A chain; 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; Small heat shock proteins	Beta-crystallin A3; Crystallins are the dominant structural components of the vertebrate eye lens	0.905
CRYA1	CRYBB1	ENSP00000482816	ENSP00000215939	Alpha-crystallin A chain; 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; Small heat shock proteins	Beta-crystallin B1; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family	0.940
CRYA1	CRYBB2	ENSP00000482816	ENSP00000381273	Alpha-crystallin A chain; 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; Small heat shock proteins	Beta-crystallin B2; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family	0.934
CRYA1	CRYGC	ENSP00000482816	ENSP00000282141	Alpha-crystallin A chain; 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; Small heat shock proteins	Gamma-crystallin C; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family	0.855
CRYA1	CRYGS	ENSP00000482816	ENSP00000376287	Alpha-crystallin A chain; 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; Small heat shock proteins	Beta-crystallin S; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family	0.838
CRYA1	MGEA5	ENSP00000482816	ENSP00000354850	Alpha-crystallin A chain; 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; Small heat shock proteins	Protein O-GlcNAcase; Isoform 1- Cleaves GlcNAc but not GalNAc from O- glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4- methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl- beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro). Does not bind acetyl-CoA and does not have histone acetyltransferase activity; Belongs to the glycosyl hydrolase 84 family	0.586
CRYAB	CRYA1	ENSP00000433560	ENSP00000482816	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; Small heat shock proteins	Alpha-crystallin A chain; 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; Small heat shock proteins	0.913
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; Small heat shock proteins	Beta-crystallin A3; Crystallins are the dominant structural components of the vertebrate eye lens	0.873
CRYAB	CRYBB1	ENSP00000433560	ENSP00000215939	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; Small heat shock proteins	Beta-crystallin B1; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family	0.852
CRYAB	CRYBB2	ENSP00000433560	ENSP00000381273	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; Small heat shock proteins	Beta-crystallin B2; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family	0.903
CRYAB	CRYGC	ENSP00000433560	ENSP00000282141	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; Small heat shock proteins	Gamma-crystallin C; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family	0.833
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; Small heat shock proteins	Beta-crystallin S; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family	0.842
CRYAB	HSF1	ENSP00000433560	ENSP00000431512	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; Small heat shock proteins	Heat shock factor protein 1; Function 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 [...]	0.946
CRYAB	HSPB4	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; Small heat shock proteins	Crystallin, alpha A; 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; Small heat shock proteins	0.898
CRYAB	MGEA5	ENSP00000433560	ENSP00000354850	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; Small heat shock proteins	Protein O-GlcNAcase; Isoform 1- Cleaves GlcNAc but not GalNAc from O- glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4- methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl- beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro). Does not bind acetyl-CoA and does not have histone acetyltransferase activity; Belongs to the glycosyl hydrolase 84 family	0.960
CRYAB	PRNP	ENSP00000433560	ENSP00000368752	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; Small heat shock proteins	Major prion protein; Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as a agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) (By similarity). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1 deaminase degr [...]	0.832
CRYBA1	CRYA1	ENSP00000225387	ENSP00000482816	Beta-crystallin A3; Crystallins are the dominant structural components of the vertebrate eye lens	Alpha-crystallin A chain; 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; Small heat shock proteins	0.905
CRYBA1	CRYAB	ENSP00000225387	ENSP00000433560	Beta-crystallin A3; 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; Small heat shock proteins	0.873
CRYBA1	CRYBB1	ENSP00000225387	ENSP00000215939	Beta-crystallin A3; Crystallins are the dominant structural components of the vertebrate eye lens	Beta-crystallin B1; Crystallins are the dominant structural components of the vertebrate eye lens; Belongs to the beta/gamma-crystallin family	0.721

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