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CRYBB2 crystallin beta B2 [ Bos taurus (domestic cattle) ]

Gene ID: 287011, updated on 30-Jan-2025

Summary

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Official Symbol
CRYBB2provided by VGNC
Official Full Name
crystallin beta B2provided by VGNC
Primary source
VGNC:VGNC:27737
See related
BGD:BT10539; EnsemblRapid:ENSBTAG00070019229
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
Orthologs
human mouse all
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Genomic context

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See CRYBB2 in Genome Data Viewer
Location:
chromosome: 17
Exon count:
7
Annotation release Status Assembly Chr Location
RS_2024_12 current ARS-UCD2.0 (GCF_002263795.3) 17 NC_037344.1 (65304388..65318606)

Chromosome 17 - NC_037344.1Genomic Context describing neighboring genes Neighboring gene KIAA1671 Neighboring gene uncharacterized LOC132342637 Neighboring gene crystallin beta B3 Neighboring gene uncharacterized LOC112442007 Neighboring gene uncharacterized LOC132342638

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_037344.1 Chromosome 17 Reference ARS-UCD2.0 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

Expression

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

Bibliography

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Related articles in PubMed

  1. 1H-NMR spectroscopy of beta B2-crystallin from bovine eye lens. Conformation of the N- and C-terminal extensions. Carver JA, et al. Eur J Biochem, 1993 Apr 1. PMID 8477703
  2. Primary structure of the bovine beta-crystallin Bp chain. Internal duplication and homology with gamma-crystallin. Driessen HP, et al. Eur J Biochem, 1981 Dec. PMID 7035168
  3. Nucleotide sequence for the cDNA of the bovine beta B2 crystallin and assignment of the orthologous human locus to chromosome 22. Hogg D, et al. Curr Eye Res, 1987 Nov. PMID 3427982
  4. X-ray analysis of beta B2-crystallin and evolution of oligomeric lens proteins. Bax B, et al. Nature, 1990 Oct 25. PMID 2234050
  5. Detection and structural features of the betaB2-B3-crystallin heterodimer by radical probe mass spectrometry (RP-MS). Diemer H, et al. J Mass Spectrom, 2009 May. PMID 19206113

See all (10) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. detection & sructure of the betaB2-B3-crystallin heterodimer; results suggest the betaB2 subunit adopts a more compacted form than in its monomeric form in order for much of its structure to be enveloped by the betaB3 subunit within the heterodimer
    Title: Detection and structural features of the betaB2-B3-crystallin heterodimer by radical probe mass spectrometry (RP-MS).
  2. combined with previously reported observations of alpha-crystallin quaternary structure have led us to propose a structural model of how activated alpha-crystallin chaperones unfolded betaB2-crystallin
    Title: Association of partially folded lens betaB2-crystallins with the alpha-crystallin molecular chaperone.
  3. Mass spectrometry analysis and a database search identified carbamylated proteins originating from alphaA-crystallin, betaB2- and gammaS-(betaS)-crystallins.
    Title: Identification of the primary targets of carbamylation in bovine lens proteins by mass spectrometry.
  4. Results show that both betaB2- and betaA3-crystallin bind calcium with moderate affinity.
    Title: Calcium-binding to lens betaB2- and betaA3-crystallins suggests that all beta-crystallins are calcium-binding proteins.
Submit: New GeneRIF Correction

General gene information

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Homology

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables structural constituent of eye lens IEA
Inferred from Electronic Annotation
more info
 PubMed 
Process Evidence Code Pubs
involved_in lens development in camera-type eye IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in visual perception IEA
Inferred from Electronic Annotation
more info
 PubMed 

General protein information

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Preferred Names
beta-crystallin B2
Names
beta-B2 crystallin
beta-crystallin Bp

NCBI Reference Sequences (RefSeq)

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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_174807.1 → NP_777232.1  beta-crystallin B2

    See identical proteins and their annotated locations for NP_777232.1

    Status: PROVISIONAL

    Source sequence(s)
    M22466
    UniProtKB/Swiss-Prot
    P02522
    UniProtKB/TrEMBL
    A0AAF7AFV8
    Related
    ENSBTAP00070026114.1, ENSBTAT00070043403.1
    Conserved Domains (2) summary
    smart00247
    Location:18 → 100
    XTALbg; Beta/gamma crystallins
    pfam00030
    Location:108 → 190
    Crystall; Beta/Gamma crystallin

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_037344.1 Reference ARS-UCD2.0 Primary Assembly

    Range
    65304388..65318606
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_024977034.1 → XP_024832802.1  beta-crystallin B2 isoform X1

    UniProtKB/Swiss-Prot
    P02522
    UniProtKB/TrEMBL
    A0AAF7AFV8
    Related
    ENSBTAP00070026131.1, ENSBTAT00070043423.1
    Conserved Domains (2) summary
    smart00247
    Location:18 → 100
    XTALbg; Beta/gamma crystallins
    pfam00030
    Location:108 → 190
    Crystall; Beta/Gamma crystallin
Nucleotide Protein Strain
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P02522.3 GenPept UniProtKB/Swiss-Prot:P02522

Gene LinkOut

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