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CRYAB crystallin alpha B [ Bos taurus (domestic cattle) ]

Gene ID: 281719, updated on 30-Jan-2025
Official Symbol
CRYABprovided by VGNC
Official Full Name
crystallin alpha Bprovided by VGNC
Primary source
VGNC:VGNC:27732
See related
BGD:BT10069; EnsemblRapid:ENSBTAG00070033367
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Bos taurus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos
Annotation information
Annotation category: partial on reference assembly
Orthologs
human mouse all
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See CRYAB in Genome Data Viewer
Location:
chromosome: 15
Exon count:
3
Annotation release Status Assembly Chr Location
RS_2024_12 current ARS-UCD2.0 (GCF_002263795.3) 15 NC_037342.1 (22242397..22245623, complement)

Chromosome 15 - NC_037342.1Genomic Context describing neighboring genes Neighboring gene ferredoxin-fold anticodon binding domain containing 1 Neighboring gene cilia and flagella associated protein 68 Neighboring gene heat shock protein family B (small) member 2 Neighboring gene chromosome 15 C11orf52 homolog

Genomic Sequence:
NC_037342.1 Chromosome 15 Reference ARS-UCD2.0 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

  • Project title: Dominette sequence data
  • BioProject: PRJNA294306
  • Analysis date: Tue Dec 17 08:57:05 2024

Related articles in PubMed

  1. Non-enzymatic glycation of α-crystallin as an in vitro model for aging, diabetes and degenerative diseases. Karumanchi DK, et al. Amino Acids, 2015 Dec. PMID 26215735
  2. Identification of the posttranslational modifications of bovine lens alpha B-crystallins by mass spectrometry. Smith JB, et al. Protein Sci, 1992 May. PMID 1304359, Free PMC Article
  3. The in vivo phosphorylation sites of bovine alpha B-crystallin. Voorter CE, et al. FEBS Lett, 1989 Dec 18. PMID 2599111
  4. The phosphorylation sites of the B2 chain of bovine alpha-crystallin. Chiesa R, et al. Biochem Biophys Res Commun, 1987 May 14. PMID 3579961
  5. The amino-acids sequence of the alphaB2 chain of bovine alpha-crystallin. Van Der Ouderaa FJ, et al. Eur J Biochem, 1974 Nov 1. PMID 4477528

See all (21) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. analysis of the structural, molecular and spectroscopic changes in alpha-crystallin protein as it slowly denatures due to aggregation induced by non-enzymatic glycation
    Title: Non-enzymatic glycation of α-crystallin as an in vitro model for aging, diabetes and degenerative diseases.
  2. The alphaB-crystallin content of bovine type I muscle fibers is quantitatively similar to that in the predominantly type I fibers of rat soleus muscle.
    Title: Absolute amounts and diffusibility of HSP72, HSP25, and αB-crystallin in fast- and slow-twitch skeletal muscle fibers of rat.
  3. These results show that between pH 7 and 10 the protein undergoes a reversible thermal transition.
    Title: Thermal and acid denaturation of bovine lens α-crystallin.
  4. alpha-crystallin is characterized by homogeneous distribution of scattering density in the domains inaccessible for water penetration
    Title: Study of α-crystallin structure by small angle neutron scattering with contrast variation.
  5. In the presence of alpha-crystallin or GroEL the kinetic of GAPDH aggregation is changed from the diffusion-limited cluster-cluster aggregation to the reaction-limited cluster-cluster aggregation.
    Title: Comparative analysis of the effects of alpha-crystallin and GroEL on the kinetics of thermal aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase.
  6. The study provides evidence for the regulation of the chaperone activity of alphaB-crystallin by phosphorylation and indicates that this may play an important role in alleviating the pathogenic effects associated with protein conformational diseases.
    Title: Mimicking phosphorylation of alphaB-crystallin affects its chaperone activity.
  7. The results are consistent with the hypothesis that short-range, weak, attractive interactions between alpha- and gamma-crystallins are necessary for maximum transparency of the lens.
    Title: Age-dependent association of gamma-crystallins with aged alpha-crystallins from old bovine lens.
  8. analysis of alpha-crystallin assisted refolding of enzyme substrates
    Title: Alpha-crystallin assisted refolding of enzyme substrates: optimization of external parameters.
  9. one of the functions of alphaB-crystallin is to bind microtubules via microtubule binding proteins and to give the MTs resistance to disassembly
    Title: alphaB-Crystallin-coated MAP microtubule resists nocodazole and calcium-induced disassembly.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

Markers

Homology

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables structural constituent of eye lens IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables unfolded protein binding IEA
Inferred from Electronic Annotation
more info
 PubMed 
Process Evidence Code Pubs
involved_in negative regulation of apoptotic process IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in protein refolding IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in response to heat IEA
Inferred from Electronic Annotation
more info
 PubMed 
Component Evidence Code Pubs
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
 PubMed 
located_in nucleus IEA
Inferred from Electronic Annotation
more info
 PubMed 
Preferred Names
alpha-crystallin B chain
Names
alpha crystallin B
alpha(B)-crystallin
crystallin, alpha polypeptide 2

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_174290.2 → NP_776715.1  alpha-crystallin B chain

    See identical proteins and their annotated locations for NP_776715.1

    Status: PROVISIONAL

    Source sequence(s)
    AF029793
    UniProtKB/Swiss-Prot
    O46508, P02510, Q3SZQ9
    UniProtKB/TrEMBL
    A0A452DHT5
    Related
    ENSBTAP00070046067.1, ENSBTAT00070075471.1
    Conserved Domains (2) summary
    cd06498
    Location:67 → 150
    ACD_alphaB-crystallin_HspB5; Alpha-crystallin domain found in the small heat shock protein (sHsp) alphaB-crystallin (HspB5, 20kDa). sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers ...
    pfam00525
    Location:1 → 52
    Crystallin; Alpha crystallin A chain, N terminal

RefSeqs of Annotated Genomes: GCF_002263795.3-RS_2024_12

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference ARS-UCD2.0 Primary Assembly

Genomic

  1. NC_037342.1 Reference ARS-UCD2.0 Primary Assembly

    Range
    22242397..22245623 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)
Nucleotide Protein Strain
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P02510.2 GenPept UniProtKB/Swiss-Prot:P02510

Gene LinkOut

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