Version 5.4
Homo sapiens Protein: CRYBA2
Summary
InnateDB Protein IDBP-246356.4
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol CRYBA2
Protein Name crystallin, beta A2
Synonyms CTRCT42;
Species Homo sapiens
Ensembl Protein ENSP00000375946
InnateDB Gene IDBG-81228 (CRYBA2)
Protein Structure
UniProt Annotation
Function Crystallins are the dominant structural components of the vertebrate eye lens.
Subcellular Localization
Disease Associations Note=Defects in CRYBA2 may be a cause of congenital cataract. Cataract is an opacification of the crystalline lens of the eye that frequently resulting in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive.
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 5 experimentally validated interaction(s) in this database.
Experimentally validated
Total 5 [view]
Protein-Protein 5 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0005212 structural constituent of eye lens
Biological Process
GO:0008150 biological_process
Cellular Component
GO:0005575 cellular_component
Protein Structure and Domains
PDB ID
InterPro IPR001064 Beta/gamma crystallin
IPR011024 Gamma-crystallin-related
PFAM PF00030
PRINTS PR01367
PIRSF
SMART SM00247
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt P53672
PhosphoSite PhosphoSite-P53672
TrEMBL C9JDH2
UniProt Splice Variant
Entrez Gene 1412
UniGene
RefSeq NP_476435
HUGO HGNC:2395
OMIM 600836
CCDS CCDS2429
HPRD 02905
IMGT
EMBL AC097468 AF166331 BC006285 BT007447 CH471063 X86395 X86396
GenPept AAD45388 AAH06285 AAP36115 AAX88918 CAA60147 CAA60148 EAW70665 EAW70666 EAW70667

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca