P53672 · CRBA2_HUMAN
- ProteinBeta-crystallin A2
- GeneCRYBA2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids197 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Crystallins are the dominant structural components of the vertebrate eye lens.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Molecular Function | identical protein binding | |
Molecular Function | structural constituent of eye lens | |
Biological Process | lens development in camera-type eye | |
Biological Process | visual perception |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBeta-crystallin A2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP53672
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Involvement in disease
Cataract 42 (CTRCT42)
- Note
- DescriptionAn opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function.
- See alsoMIM:115900
Natural variants in CTRCT42
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_070029 | 50 | V>M | in CTRCT42 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_070208 | 7 | in dbSNP:rs141631259 | |||
Sequence: P → S | ||||||
Natural variant | VAR_070029 | 50 | in CTRCT42 | |||
Sequence: V → M |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 297 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000057539 | 1-197 | Beta-crystallin A2 | |||
Sequence: MSSAPAPGPAPASLTLWDEEDFQGRRCRLLSDCANVCERGGLPRVRSVKVENGVWVAFEYPDFQGQQFILEKGDYPRWSAWSGSSSHNSNQLLSFRPVLCANHNDSRVTLFEGDNFQGCKFDLVDDYPSLPSMGWASKDVGSLKVSSGAWVAYQYPGYRGYQYVLERDRHSGEFCTYGELGTQAHTGQLQSIRRVQH |
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Homo/heterodimer, or complexes of higher-order. The structure of beta-crystallin oligomers seems to be stabilized through interactions between the N-terminal arms (By similarity).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-11 | N-terminal arm | ||||
Sequence: MSSAPAPGPAP | ||||||
Domain | 12-52 | Beta/gamma crystallin 'Greek key' 1 | ||||
Sequence: ASLTLWDEEDFQGRRCRLLSDCANVCERGGLPRVRSVKVEN | ||||||
Domain | 53-99 | Beta/gamma crystallin 'Greek key' 2 | ||||
Sequence: GVWVAFEYPDFQGQQFILEKGDYPRWSAWSGSSSHNSNQLLSFRPVL | ||||||
Region | 100-105 | Connecting peptide | ||||
Sequence: CANHND | ||||||
Domain | 106-147 | Beta/gamma crystallin 'Greek key' 3 | ||||
Sequence: SRVTLFEGDNFQGCKFDLVDDYPSLPSMGWASKDVGSLKVSS | ||||||
Domain | 148-196 | Beta/gamma crystallin 'Greek key' 4 | ||||
Sequence: GAWVAYQYPGYRGYQYVLERDRHSGEFCTYGELGTQAHTGQLQSIRRVQ |
Domain
Has a two-domain beta-structure, folded into four very similar Greek key motifs.
Sequence similarities
Belongs to the beta/gamma-crystallin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length197
- Mass (Da)22,096
- Last updated2007-01-23 v3
- ChecksumF9C8E7CD48EB16C7
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C9JDH2 | C9JDH2_HUMAN | CRYBA2 | 128 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 117 | in Ref. 6; CAA60147 | ||||
Sequence: Q → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF166331 EMBL· GenBank· DDBJ | AAD45388.1 EMBL· GenBank· DDBJ | mRNA | ||
BT007447 EMBL· GenBank· DDBJ | AAP36115.1 EMBL· GenBank· DDBJ | mRNA | ||
AC097468 EMBL· GenBank· DDBJ | AAX88918.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471063 EMBL· GenBank· DDBJ | EAW70665.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC006285 EMBL· GenBank· DDBJ | AAH06285.1 EMBL· GenBank· DDBJ | mRNA | ||
X86395 EMBL· GenBank· DDBJ | CAA60147.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X86396 EMBL· GenBank· DDBJ | CAA60148.1 EMBL· GenBank· DDBJ | Genomic DNA |