E9PJL7 · E9PJL7_HUMAN

  • Protein
    Alpha-crystallin B chain
  • Gene
    CRYAB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    2/5

Function

function

May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. In lens epithelial cells, stabilizes the ATP6V1A protein, preventing its degradation by the proteasome.

Features

Showing features for binding site.

1129102030405060708090100110120
TypeIDPosition(s)Description
Binding site104Zn2+ 1 (UniProtKB | ChEBI)
Binding site106Zn2+ 1 (UniProtKB | ChEBI)
Binding site111Zn2+ 1 (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentlysosome
Cellular Componentnucleus
Molecular Functionmetal ion binding
Molecular Functionstructural constituent of eye lens

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Alpha-crystallin B chain
  • Alternative names
    • Alpha(B)-crystallin

Gene names

    • Name
      CRYAB

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    E9PJL7

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Genetic variation databases

PTM/Processing

Features

Showing features for modified residue (large scale data).

TypeIDPosition(s)SourceDescription
Modified residue (large scale data)19PRIDEPhosphoserine
Modified residue (large scale data)21PRIDEPhosphoserine
Modified residue (large scale data)59PRIDEPhosphoserine
Modified residue (large scale data)76PRIDEPhosphoserine

Keywords

Proteomic databases

Expression

Gene expression databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain56-129SHSP

Sequence similarities

Belongs to the small heat shock protein (HSP20) family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    129
  • Mass (Da)
    15,348
  • Last updated
    2016-10-05 v8
  • Checksum
    D17735009A3B75B1
MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVD

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
P02511CRYAB_HUMANCRYAB175
E9PRA8E9PRA8_HUMANCRYAB155
E9PS12E9PS12_HUMANCRYAB77
E9PNH7E9PNH7_HUMANCRYAB106
A0A024R3B9A0A024R3B9_HUMANCRYAB108

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue129

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP000907
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
KF455510
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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