HUMAN:CRYAB

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	CRYAB (synonyms: CRYA2)
Protein Name(s)	Alpha-crystallin B chain Alpha(B)-crystallin Heat shock protein beta-5 HspB5 Renal carcinoma antigen NY-REN-27 Rosenthal fiber component
External Links
UniProt	P02511
EMBL	M28638 S45630 AF007162 AK314029 BT006770 EF444955 CH471065 BC007008 M24906
CCDS	CCDS8351.1
PIR	A35332
RefSeq	NP_001276736.1 NP_001276737.1 NP_001876.1
UniGene	Hs.53454 Hs.703770
PDB	2KLR 2WJ7 2Y1Y 2Y1Z 2Y22 2YGD 3L1G 3SGM 3SGN 3SGO 3SGP 3SGR 3SGS 4M5S 4M5T
PDBsum	2KLR 2WJ7 2Y1Y 2Y1Z 2Y22 2YGD 3L1G 3SGM 3SGN 3SGO 3SGP 3SGR 3SGS 4M5S 4M5T
DisProt	DP00445
ProteinModelPortal	P02511
SMR	P02511
BioGrid	107800
DIP	DIP-35017N
IntAct	P02511
MINT	MINT-221013
STRING	9606.ENSP00000227251
PhosphoSite	P02511
UniCarbKB	P02511
DMDM	117385
REPRODUCTION-2DPAGE	IPI00021369
SWISS-2DPAGE	P02511
UCD-2DPAGE	P02511
MaxQB	P02511
PaxDb	P02511
PRIDE	P02511
DNASU	1410
Ensembl	ENST00000227251 ENST00000526180 ENST00000527950 ENST00000531198 ENST00000533475 ENST00000616970
GeneID	1410
KEGG	hsa:1410
UCSC	uc001pmf.1
CTD	1410
GeneCards	GC11M111813
GeneReviews	CRYAB
HGNC	HGNC:2389
HPA	CAB002053 CAB040560 HPA028724
MIM	123590 608810 613763 613869 615184
neXtProt	NX_P02511
Orphanet	98910 154 280553 98993 98995
PharmGKB	PA26907
eggNOG	NOG246790
HOVERGEN	HBG054766
InParanoid	P02511
KO	K09542
OMA	LTITAPM
PhylomeDB	P02511
TreeFam	TF105049
ChiTaRS	CRYAB
EvolutionaryTrace	P02511
GeneWiki	CRYAB
GenomeRNAi	1410
NextBio	5765
PMAP-CutDB	P02511
PRO	PR:P02511
Proteomes	UP000005640
Bgee	P02511
CleanEx	HS_CRYAB
ExpressionAtlas	P02511
Genevestigator	P02511
GO	GO:0032432 GO:0009986 GO:0005737 GO:0005829 GO:0070062 GO:0005794 GO:0015630 GO:0005739 GO:0005634 GO:0005886 GO:0030018 GO:0042802 GO:0046872 GO:0042803 GO:0005212 GO:0051082 GO:0007568 GO:0060561 GO:0071480 GO:0002088 GO:0031109 GO:0006936 GO:0007517 GO:0043066 GO:0030308 GO:0043154 GO:0032387 GO:2000378 GO:0006457 GO:0051260 GO:0010941 GO:0032355 GO:0042542 GO:0001666 GO:0051403 GO:0007021
Gene3D	2.60.40.790
InterPro	IPR002068 IPR001436 IPR012273 IPR003090 IPR008978
PANTHER	PTHR11527:SF37
Pfam	PF00525 PF00011
PIRSF	PIRSF036514
PRINTS	PR00299
SUPFAM	SSF49764
PROSITE	PS01031

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:20587334^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:20587334^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:20587334^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:20587334^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	PMID:12235146^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0001540	amyloid-beta binding	PMID:23106396^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P05067:PRO_0000000093	F		Seeded From UniProt	complete
enables	GO:0044877	protein-containing complex binding	PMID:23106396^[3]	ECO:0000353	physical interaction evidence used in manual assertion	ComplexPortal:CPX-1180	F		Seeded From UniProt	complete
involved_in	GO:1905907	negative regulation of amyloid fibril formation	PMID:23106396^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P05067:PRO_0000000093)	Seeded From UniProt	complete
involved_in	GO:0032463	negative regulation of protein homooligomerization	PMID:23106396^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P05067:PRO_0000000093)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[5]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000054	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	PMID:9731540^[6]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	PMID:14752512^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032387	negative regulation of intracellular transport	PMID:14752512^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:14752512^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0051260	protein homooligomerization	PMID:16303126^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:16303126^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P07315	F		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:19646995^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02511	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:19464326^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:19464326^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0071480	cellular response to gamma radiation	PMID:23542032^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010941	regulation of cell death	PMID:23542032^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:26465331^[12]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02511	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:24183572^[13]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02511	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23188086^[14]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02511	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22153508^[15]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02511	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22143763^[16]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02511	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21464278^[17]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02511	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20802487^[18]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02511	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19651604^[19]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02511	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:18330356^[20]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02511	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:12601044^[21]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02511	F		Seeded From UniProt	complete
involved_in	GO:0060561	apoptotic process involved in morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23927 ensembl:ENSMUSP00000149803	P		Seeded From UniProt	complete
part_of	GO:0043292	contractile fiber	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23927 ensembl:ENSMUSP00000149803	C		Seeded From UniProt	complete
involved_in	GO:0043154	negative regulation of cysteine-type endopeptidase activity involved in apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23927 ensembl:ENSMUSP00000149803	P		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23927 ensembl:ENSMUSP00000149803	P		Seeded From UniProt	complete
involved_in	GO:0043010	camera-type eye development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23927 ensembl:ENSMUSP00000149803	P		Seeded From UniProt	complete
involved_in	GO:0042542	response to hydrogen peroxide	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23927 ensembl:ENSMUSP00000149803	P		Seeded From UniProt	complete
part_of	GO:0030018	Z disc	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23927 ensembl:ENSMUSP00000149803	C		Seeded From UniProt	complete
involved_in	GO:0010629	negative regulation of gene expression	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23927 ensembl:ENSMUSP00000149803	P		Seeded From UniProt	complete
involved_in	GO:0007517	muscle organ development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23927 ensembl:ENSMUSP00000149803	P		Seeded From UniProt	complete
involved_in	GO:0007021	tubulin complex assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23927 ensembl:ENSMUSP00000149803	P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23927 ensembl:ENSMUSP00000149803	C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23927 ensembl:ENSMUSP00000149803	C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23927 ensembl:ENSMUSP00000149803	C		Seeded From UniProt	complete
involved_in	GO:0002088	lens development in camera-type eye	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23927 ensembl:ENSMUSP00000149803	P		Seeded From UniProt	complete
involved_in	GO:0001666	response to hypoxia	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23927 ensembl:ENSMUSP00000149803	P		Seeded From UniProt	complete
involved_in	GO:2000378	negative regulation of reactive oxygen species metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	P		Seeded From UniProt	complete
part_of	GO:0097512	cardiac myofibril	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	C		Seeded From UniProt	complete
part_of	GO:0097060	synaptic membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	C		Seeded From UniProt	complete
involved_in	GO:0051403	stress-activated MAPK cascade	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	P		Seeded From UniProt	complete
part_of	GO:0045202	synapse	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	C		Seeded From UniProt	complete
part_of	GO:0043204	perikaryon	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	C		Seeded From UniProt	complete
part_of	GO:0043197	dendritic spine	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	C		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	P		Seeded From UniProt	complete
involved_in	GO:0042542	response to hydrogen peroxide	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	P		Seeded From UniProt	complete
part_of	GO:0032432	actin filament bundle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	C		Seeded From UniProt	complete
involved_in	GO:0032355	response to estradiol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	P		Seeded From UniProt	complete
part_of	GO:0031674	I band	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	C		Seeded From UniProt	complete
part_of	GO:0031430	M band	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	C		Seeded From UniProt	complete
involved_in	GO:0031109	microtubule polymerization or depolymerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	P		Seeded From UniProt	complete
part_of	GO:0030424	axon	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	C		Seeded From UniProt	complete
involved_in	GO:0030308	negative regulation of cell growth	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	P		Seeded From UniProt	complete
part_of	GO:0015630	microtubule cytoskeleton	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	C		Seeded From UniProt	complete
part_of	GO:0014069	postsynaptic density	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	C		Seeded From UniProt	complete
involved_in	GO:0010259	multicellular organism aging	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	P		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	C		Seeded From UniProt	complete
enables	GO:0008092	cytoskeletal protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	F		Seeded From UniProt	complete
enables	GO:0008017	microtubule binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	F		Seeded From UniProt	complete
involved_in	GO:0007568	aging	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	P		Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	P		Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23928 ensembl:ENSRNOP00000055901	C		Seeded From UniProt	complete
enables	GO:0005212	structural constituent of eye lens	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003090	F		Seeded From UniProt	complete
involved_in	GO:1905907	negative regulation of amyloid fibril formation	PMID:23106396^[3]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006936	muscle contraction	PMID:9731540^[6]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1900034	regulation of cellular response to heat	Reactome:R-HSA-3371571	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-5082356	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
enables	GO:0005212	structural constituent of eye lens	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0273	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 Deng, Y et al. (2010) Synergistic efficacy of LBH and alphaB-crystallin through inhibiting transcriptional activities of p53 and p21. BMB Rep 43 432-7 PubMed GONUTS page
↑ Pasta, SY et al. (2002) Role of the C-terminal extensions of alpha-crystallins. Swapping the C-terminal extension of alpha-crystallin to alphaB-crystallin results in enhanced chaperone activity. J. Biol. Chem. 277 45821-8 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 Narayan, P et al. (2012) Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones. Biochemistry 51 9270-6 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ ^6.0 ^6.1 Vicart, P et al. (1998) A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy. Nat. Genet. 20 92-5 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Mao, YW et al. (2004) Human alphaA- and alphaB-crystallins bind to Bax and Bcl-X(S) to sequester their translocation during staurosporine-induced apoptosis. Cell Death Differ. 11 512-26 PubMed GONUTS page
↑ ^8.0 ^8.1 Pigaga, V & Quinlan, RA (2006) Lenticular chaperones suppress the aggregation of the cataract-causing mutant T5P gamma C-crystallin. Exp. Cell Res. 312 51-62 PubMed GONUTS page
↑ Bagnéris, C et al. (2009) Crystal structures of alpha-crystallin domain dimers of alphaB-crystallin and Hsp20. J. Mol. Biol. 392 1242-52 PubMed GONUTS page
↑ ^10.0 ^10.1 Vos, MJ et al. (2009) HSPB7 is a SC35 speckle resident small heat shock protein. Biochim. Biophys. Acta 1793 1343-53 PubMed GONUTS page
↑ ^11.0 ^11.1 Yamashita, A et al. (2013) Protective role of the endoplasmic reticulum protein mitsugumin23 against ultraviolet C-induced cell death. FEBS Lett. 587 1299-303 PubMed GONUTS page
↑ Grose, JH et al. (2015) Characterization of the Cardiac Overexpression of HSPB2 Reveals Mitochondrial and Myogenic Roles Supported by a Cardiac HspB2 Interactome. PLoS ONE 10 e0133994 PubMed GONUTS page
↑ Kingsley, CN et al. (2013) Preferential and specific binding of human αB-crystallin to a cataract-related variant of γS-crystallin. Structure 21 2221-7 PubMed GONUTS page
↑ Delbecq, SP et al. (2012) Binding determinants of the small heat shock protein, αB-crystallin: recognition of the 'IxI' motif. EMBO J. 31 4587-94 PubMed GONUTS page
↑ Baldwin, AJ et al. (2011) The polydispersity of αB-crystallin is rationalized by an interconverting polyhedral architecture. Structure 19 1855-63 PubMed GONUTS page
↑ Braun, N et al. (2011) Multiple molecular architectures of the eye lens chaperone αB-crystallin elucidated by a triple hybrid approach. Proc. Natl. Acad. Sci. U.S.A. 108 20491-6 PubMed GONUTS page
↑ Jehle, S et al. (2011) N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity. Proc. Natl. Acad. Sci. U.S.A. 108 6409-14 PubMed GONUTS page
↑ Jehle, S et al. (2010) Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers. Nat. Struct. Mol. Biol. 17 1037-42 PubMed GONUTS page
↑ Peschek, J et al. (2009) The eye lens chaperone alpha-crystallin forms defined globular assemblies. Proc. Natl. Acad. Sci. U.S.A. 106 13272-7 PubMed GONUTS page
↑ DeGrado-Warren, J et al. (2008) Construction and characterization of a normalized yeast two-hybrid library derived from a human protein-coding clone collection. BioTechniques 44 265-73 PubMed GONUTS page
↑ Fu, L & Liang, JJ (2003) Alteration of protein-protein interactions of congenital cataract crystallin mutants. Invest. Ophthalmol. Vis. Sci. 44 1155-9 PubMed GONUTS page

[PMID:20587334-1] 1.0 ^1.1 ^1.2 ^1.3 Deng, Y et al. (2010) Synergistic efficacy of LBH and alphaB-crystallin through inhibiting transcriptional activities of p53 and p21. BMB Rep 43 432-7 PubMed GONUTS page

[PMID:12235146-2] Pasta, SY et al. (2002) Role of the C-terminal extensions of alpha-crystallins. Swapping the C-terminal extension of alpha-crystallin to alphaB-crystallin results in enhanced chaperone activity. J. Biol. Chem. 277 45821-8 PubMed GONUTS page

[PMID:23106396-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 Narayan, P et al. (2012) Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones. Biochemistry 51 9270-6 PubMed GONUTS page

[PMID:23533145-4] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:19056867-5] Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page

[PMID:9731540-6] 6.0 ^6.1 Vicart, P et al. (1998) A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy. Nat. Genet. 20 92-5 PubMed GONUTS page

[PMID:14752512-7] 7.0 ^7.1 ^7.2 Mao, YW et al. (2004) Human alphaA- and alphaB-crystallins bind to Bax and Bcl-X(S) to sequester their translocation during staurosporine-induced apoptosis. Cell Death Differ. 11 512-26 PubMed GONUTS page

[PMID:16303126-8] 8.0 ^8.1 Pigaga, V & Quinlan, RA (2006) Lenticular chaperones suppress the aggregation of the cataract-causing mutant T5P gamma C-crystallin. Exp. Cell Res. 312 51-62 PubMed GONUTS page

[PMID:19646995-9] Bagnéris, C et al. (2009) Crystal structures of alpha-crystallin domain dimers of alphaB-crystallin and Hsp20. J. Mol. Biol. 392 1242-52 PubMed GONUTS page

[PMID:19464326-10] 10.0 ^10.1 Vos, MJ et al. (2009) HSPB7 is a SC35 speckle resident small heat shock protein. Biochim. Biophys. Acta 1793 1343-53 PubMed GONUTS page

[PMID:23542032-11] 11.0 ^11.1 Yamashita, A et al. (2013) Protective role of the endoplasmic reticulum protein mitsugumin23 against ultraviolet C-induced cell death. FEBS Lett. 587 1299-303 PubMed GONUTS page

[PMID:26465331-12] Grose, JH et al. (2015) Characterization of the Cardiac Overexpression of HSPB2 Reveals Mitochondrial and Myogenic Roles Supported by a Cardiac HspB2 Interactome. PLoS ONE 10 e0133994 PubMed GONUTS page

[PMID:24183572-13] Kingsley, CN et al. (2013) Preferential and specific binding of human αB-crystallin to a cataract-related variant of γS-crystallin. Structure 21 2221-7 PubMed GONUTS page

[PMID:23188086-14] Delbecq, SP et al. (2012) Binding determinants of the small heat shock protein, αB-crystallin: recognition of the 'IxI' motif. EMBO J. 31 4587-94 PubMed GONUTS page

[PMID:22153508-15] Baldwin, AJ et al. (2011) The polydispersity of αB-crystallin is rationalized by an interconverting polyhedral architecture. Structure 19 1855-63 PubMed GONUTS page

[PMID:22143763-16] Braun, N et al. (2011) Multiple molecular architectures of the eye lens chaperone αB-crystallin elucidated by a triple hybrid approach. Proc. Natl. Acad. Sci. U.S.A. 108 20491-6 PubMed GONUTS page

[PMID:21464278-17] Jehle, S et al. (2011) N-terminal domain of alphaB-crystallin provides a conformational switch for multimerization and structural heterogeneity. Proc. Natl. Acad. Sci. U.S.A. 108 6409-14 PubMed GONUTS page

[PMID:20802487-18] Jehle, S et al. (2010) Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers. Nat. Struct. Mol. Biol. 17 1037-42 PubMed GONUTS page

[PMID:19651604-19] Peschek, J et al. (2009) The eye lens chaperone alpha-crystallin forms defined globular assemblies. Proc. Natl. Acad. Sci. U.S.A. 106 13272-7 PubMed GONUTS page

[PMID:18330356-20] DeGrado-Warren, J et al. (2008) Construction and characterization of a normalized yeast two-hybrid library derived from a human protein-coding clone collection. BioTechniques 44 265-73 PubMed GONUTS page

[PMID:12601044-21] Fu, L & Liang, JJ (2003) Alteration of protein-protein interactions of congenital cataract crystallin mutants. Invest. Ophthalmol. Vis. Sci. 44 1155-9 PubMed GONUTS page

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