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    CRYAB crystallin alpha B [ Homo sapiens (human) ]

    Gene ID: 1410, updated on 17-Feb-2017
    Official Symbol
    CRYABprovided by HGNC
    Official Full Name
    crystallin alpha Bprovided by HGNC
    Primary source
    HGNC:HGNC:2389
    See related
    Ensembl:ENSG00000109846 MIM:123590; Vega:OTTHUMG00000166885
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Homo sapiens
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
    Also known as
    MFM2; CRYA2; CTPP2; HSPB5; CMD1II; CTRCT16; HEL-S-101
    Summary
    Mammalian lens crystallins are divided into alpha, beta, and gamma families. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2014]
    Orthologs
    Location:
    11q23.1
    Exon count:
    6
    Annotation release Status Assembly Chr Location
    108 current GRCh38.p7 (GCF_000001405.33) 11 NC_000011.10 (111908620..111913213, complement)
    105 previous assembly GRCh37.p13 (GCF_000001405.25) 11 NC_000011.9 (111779350..111782473, complement)

    Chromosome 11 - NC_000011.10Genomic Context describing neighboring genes Neighboring gene ferredoxin-fold anticodon binding domain containing 1 Neighboring gene chromosome 11 open reading frame 1 Neighboring gene ribosomal protein L37a pseudogene 8 Neighboring gene HSPB2-C11orf52 readthrough (NMD candidate) Neighboring gene uncharacterized LOC105369494 Neighboring gene heat shock protein family B (small) member 2 Neighboring gene chromosome 11 open reading frame 52 Neighboring gene DIX domain containing 1

    GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

    Replication interactions

    Interaction Pubs
    Knockdown of crystallin, alpha B (CRYAB) by siRNA inhibits the early stages of HIV-1 replication in 293T cells infected with VSV-G pseudotyped HIV-1 PubMed

    Protein interactions

    Protein Gene Interaction Pubs
    Tat tat HIV-1 Tat peptide enhances entry of alpha B crystallin into lens cells PubMed

    Go to the HIV-1, Human Interaction Database

    • Longevity regulating pathway - multiple species, organism-specific biosystem (from KEGG)
      Longevity regulating pathway - multiple species, organism-specific biosystemAging is a complex process of accumulation of molecular, cellular, and organ damage, leading to loss of function and increased vulnerability to disease and death. Despite the complexity of aging, rec...
    • Longevity regulating pathway - multiple species, conserved biosystem (from KEGG)
      Longevity regulating pathway - multiple species, conserved biosystemAging is a complex process of accumulation of molecular, cellular, and organ damage, leading to loss of function and increased vulnerability to disease and death. Despite the complexity of aging, rec...
    • Protein processing in endoplasmic reticulum, organism-specific biosystem (from KEGG)
      Protein processing in endoplasmic reticulum, organism-specific biosystemThe endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylate...
    • Protein processing in endoplasmic reticulum, conserved biosystem (from KEGG)
      Protein processing in endoplasmic reticulum, conserved biosystemThe endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylate...
    Products Interactant Other Gene Complex Source Pubs Description

    Markers

    Homology

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    identical protein binding IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    metal ion binding IEA
    Inferred from Electronic Annotation
    more info
     
    microtubule binding IEA
    Inferred from Electronic Annotation
    more info
     
    protein binding IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    protein homodimerization activity IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    structural constituent of eye lens IEA
    Inferred from Electronic Annotation
    more info
     
    unfolded protein binding IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    Process Evidence Code Pubs
    aging IEA
    Inferred from Electronic Annotation
    more info
     
    cellular response to gamma radiation IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    microtubule polymerization or depolymerization IEA
    Inferred from Electronic Annotation
    more info
     
    muscle contraction TAS
    Traceable Author Statement
    more info
    PubMed 
    negative regulation of amyloid fibril formation IDA
    Inferred from Direct Assay
    more info
    PubMed 
    negative regulation of amyloid fibril formation TAS
    Traceable Author Statement
    more info
    PubMed 
    negative regulation of apoptotic process IDA
    Inferred from Direct Assay
    more info
    PubMed 
    negative regulation of cell growth IEA
    Inferred from Electronic Annotation
    more info
     
    negative regulation of intracellular transport IDA
    Inferred from Direct Assay
    more info
    PubMed 
    negative regulation of protein homooligomerization IDA
    Inferred from Direct Assay
    more info
    PubMed 
    negative regulation of reactive oxygen species metabolic process IEA
    Inferred from Electronic Annotation
    more info
     
    protein folding IEA
    Inferred from Electronic Annotation
    more info
     
    protein homooligomerization IDA
    Inferred from Direct Assay
    more info
    PubMed 
    regulation of cell death IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    regulation of cellular response to heat TAS
    Traceable Author Statement
    more info
     
    response to estradiol IEA
    Inferred from Electronic Annotation
    more info
     
    response to hydrogen peroxide IEA
    Inferred from Electronic Annotation
    more info
     
    stress-activated MAPK cascade IEA
    Inferred from Electronic Annotation
    more info
     
    Component Evidence Code Pubs
    Golgi apparatus IEA
    Inferred from Electronic Annotation
    more info
     
    I band IEA
    Inferred from Electronic Annotation
    more info
     
    M band IEA
    Inferred from Electronic Annotation
    more info
     
    actin filament bundle IEA
    Inferred from Electronic Annotation
    more info
     
    axon IEA
    Inferred from Electronic Annotation
    more info
     
    cardiac myofibril IEA
    Inferred from Electronic Annotation
    more info
     
    cell surface IEA
    Inferred from Electronic Annotation
    more info
     
    cytoplasm IDA
    Inferred from Direct Assay
    more info
    PubMed 
    dendritic spine IEA
    Inferred from Electronic Annotation
    more info
     
    extracellular exosome IDA
    Inferred from Direct Assay
    more info
    PubMed 
    microtubule cytoskeleton IEA
    Inferred from Electronic Annotation
    more info
     
    nucleoplasm TAS
    Traceable Author Statement
    more info
     
    nucleus IDA
    Inferred from Direct Assay
    more info
    PubMed 
    perikaryon IEA
    Inferred from Electronic Annotation
    more info
     
    postsynaptic density IEA
    Inferred from Electronic Annotation
    more info
     
    synaptic membrane IEA
    Inferred from Electronic Annotation
    more info
     
    Preferred Names
    alpha-crystallin B chain
    Names
    epididymis secretory protein Li 101
    heat shock protein beta-5
    heat-shock 20 kD like-protein
    renal carcinoma antigen NY-REN-27
    rosenthal fiber component

    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.

    Genomic

    1. NG_009824.2 RefSeqGene

      Range
      15510..20103
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001289807.1NP_001276736.1  alpha-crystallin B chain isoform 1

      See identical proteins and their annotated locations for NP_001276736.1

      Status: REVIEWED

      Source sequence(s)
      BC007008, BF339748, BI759672, BM721803, DB506606
      Consensus CDS
      CCDS8351.1
      UniProtKB/Swiss-Prot
      P02511
      UniProtKB/TrEMBL
      V9HW27
      Conserved Domains (3) summary
      cd06498
      Location:67150
      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 ...
      COG0071
      Location:11161
      IbpA; Molecular chaperone IbpA, HSP20 family [Posttranslational modification, protein turnover, chaperones]
      pfam00525
      Location:151
      Crystallin; Alpha crystallin A chain, N terminal
    2. NM_001289808.1NP_001276737.1  alpha-crystallin B chain isoform 1

      See identical proteins and their annotated locations for NP_001276737.1

      Status: REVIEWED

      Source sequence(s)
      BC007008, BE076509, BF339748, BI548180, BM721803
      Consensus CDS
      CCDS8351.1
      UniProtKB/Swiss-Prot
      P02511
      UniProtKB/TrEMBL
      V9HW27
      Related
      ENSP00000436051, OTTHUMP00000234278, ENST00000526180, OTTHUMT00000391654
      Conserved Domains (3) summary
      cd06498
      Location:67150
      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 ...
      COG0071
      Location:11161
      IbpA; Molecular chaperone IbpA, HSP20 family [Posttranslational modification, protein turnover, chaperones]
      pfam00525
      Location:151
      Crystallin; Alpha crystallin A chain, N terminal
    3. NM_001330379.1NP_001317308.1  alpha-crystallin B chain isoform 2

      Status: REVIEWED

      Source sequence(s)
      AP000907, BF339748, BQ437433
      Consensus CDS
      CCDS81626.1
      UniProtKB/TrEMBL
      A0A024R3B9
    4. NM_001885.2NP_001876.1  alpha-crystallin B chain isoform 1

      See identical proteins and their annotated locations for NP_001876.1

      Status: REVIEWED

      Source sequence(s)
      BC007008, BF339748, BM721803, DB506606
      Consensus CDS
      CCDS8351.1
      UniProtKB/Swiss-Prot
      P02511
      UniProtKB/TrEMBL
      V9HW27
      Related
      ENSP00000483554, ENST00000616970
      Conserved Domains (3) summary
      cd06498
      Location:67150
      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 ...
      COG0071
      Location:11161
      IbpA; Molecular chaperone IbpA, HSP20 family [Posttranslational modification, protein turnover, chaperones]
      pfam00525
      Location:151
      Crystallin; Alpha crystallin A chain, N terminal

    RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 108 details...Open this link in a new tab

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

    Reference GRCh38.p7 Primary Assembly

    Genomic

    1. NC_000011.10 Reference GRCh38.p7 Primary Assembly

      Range
      111908620..111913213 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_011542608.1XP_011540910.1  alpha-crystallin B chain isoform X1

      See identical proteins and their annotated locations for XP_011540910.1

      UniProtKB/Swiss-Prot
      P02511
      UniProtKB/TrEMBL
      V9HW27
      Conserved Domains (3) summary
      cd06498
      Location:67150
      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 ...
      COG0071
      Location:11161
      IbpA; Molecular chaperone IbpA, HSP20 family [Posttranslational modification, protein turnover, chaperones]
      pfam00525
      Location:151
      Crystallin; Alpha crystallin A chain, N terminal
    2. XM_011542609.2XP_011540911.1  alpha-crystallin B chain isoform X2

      Related
      ENSP00000435046, OTTHUMP00000234280, ENST00000533280, OTTHUMT00000391656
      Conserved Domains (2) summary
      COG0071
      Location:694
      IbpA; Molecular chaperone IbpA, HSP20 family [Posttranslational modification, protein turnover, chaperones]
      cl00175
      Location:183
      alpha-crystallin-Hsps_p23-like; alpha-crystallin domain (ACD) found in alpha-crystallin-type small heat shock proteins, and a similar domain found in p23 (a cochaperone for Hsp90) and in other p23-like proteins.

    Alternate CHM1_1.1

    Genomic

    1. NC_018922.2 Alternate CHM1_1.1

      Range
      111662424..111667017 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)
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