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P23927

- CRYAB_MOUSE

UniProt

P23927 - CRYAB_MOUSE

Protein

Alpha-crystallin B chain

Gene

Cryab

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei48 – 481Susceptible to oxidationBy similarity
    Sitei60 – 601Susceptible to oxidationBy similarity
    Sitei68 – 681Susceptible to oxidationBy similarity
    Metal bindingi83 – 831Zinc 1By similarity
    Metal bindingi104 – 1041Zinc 2By similarity
    Metal bindingi106 – 1061Zinc 2By similarity
    Metal bindingi111 – 1111Zinc 1By similarity
    Metal bindingi119 – 1191Zinc 1By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. protein homodimerization activity Source: UniProtKB
    4. structural constituent of eye lens Source: MGI

    GO - Biological processi

    1. aging Source: Ensembl
    2. apoptotic process involved in morphogenesis Source: MGI
    3. camera-type eye development Source: MGI
    4. cellular response to gamma radiation Source: MGI
    5. glucose metabolic process Source: Ensembl
    6. lens development in camera-type eye Source: MGI
    7. microtubule polymerization or depolymerization Source: Ensembl
    8. muscle organ development Source: MGI
    9. negative regulation of apoptotic process Source: MGI
    10. negative regulation of cell growth Source: Ensembl
    11. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
    12. negative regulation of gene expression Source: MGI
    13. negative regulation of intracellular transport Source: Ensembl
    14. negative regulation of reactive oxygen species metabolic process Source: Ensembl
    15. protein folding Source: Ensembl
    16. protein homooligomerization Source: Ensembl
    17. regulation of cell death Source: MGI
    18. response to estradiol Source: Ensembl
    19. response to hydrogen peroxide Source: MGI
    20. response to hypoxia Source: MGI
    21. stress-activated MAPK cascade Source: Ensembl
    22. tubulin complex assembly Source: MGI

    Keywords - Molecular functioni

    Chaperone, Eye lens protein

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-crystallin B chain
    Alternative name(s):
    Alpha(B)-crystallin
    P23
    Gene namesi
    Name:Cryab
    Synonyms:Crya2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:88516. Cryab.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity
    Note: Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles.By similarity

    GO - Cellular componenti

    1. actin filament bundle Source: Ensembl
    2. cell surface Source: Ensembl
    3. contractile fiber Source: MGI
    4. cytosol Source: MGI
    5. Golgi apparatus Source: Ensembl
    6. microtubule cytoskeleton Source: Ensembl
    7. mitochondrion Source: MGI
    8. nucleus Source: UniProtKB
    9. plasma membrane Source: MGI
    10. Z disc Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 175175Alpha-crystallin B chainPRO_0000125910Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineCurated
    Modified residuei19 – 191PhosphoserineBy similarity
    Modified residuei22 – 221Omega-N-methylated arginineBy similarity
    Modified residuei45 – 451PhosphoserineBy similarity
    Modified residuei50 – 501Omega-N-methylated arginineBy similarity
    Modified residuei59 – 591PhosphoserineBy similarity
    Modified residuei92 – 921N6-acetyllysineBy similarity
    Modified residuei166 – 1661N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Methylation, Oxidation, Phosphoprotein

    Proteomic databases

    MaxQBiP23927.
    PaxDbiP23927.
    PRIDEiP23927.

    2D gel databases

    SWISS-2DPAGEP23927.

    PTM databases

    PhosphoSiteiP23927.

    Expressioni

    Tissue specificityi

    Lens as well as other tissues.

    Gene expression databases

    ArrayExpressiP23927.
    BgeeiP23927.
    CleanExiMM_CRYAB.
    GenevestigatoriP23927.

    Interactioni

    Subunit structurei

    Heteropolymer composed of three CRYAA and one CRYAB subunits. Aggregates with homologous proteins, including the small heat shock protein HSPB1, to form large heteromeric complexes. Inter-subunit bridging via zinc ions enhances stability, which is crucial as there is no protein turn over in the lens. Interacts with HSPBAP1 and TTN/titin By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CRYGDP073202EBI-299046,EBI-7673124From a different organism.

    Protein-protein interaction databases

    BioGridi198909. 7 interactions.
    DIPiDIP-31060N.
    IntActiP23927. 11 interactions.
    MINTiMINT-1591396.

    Structurei

    3D structure databases

    ProteinModelPortaliP23927.
    SMRiP23927. Positions 1-175.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the small heat shock protein (HSP20) family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG246790.
    HOGENOMiHOG000233954.
    HOVERGENiHBG054766.
    InParanoidiP23927.
    KOiK09542.
    OMAiRKQAPGP.
    OrthoDBiEOG7WHHBK.
    PhylomeDBiP23927.
    TreeFamiTF105049.

    Family and domain databases

    Gene3Di2.60.40.790. 1 hit.
    InterProiIPR002068. a-crystallin/Hsp20_dom.
    IPR001436. Alpha-crystallin/HSP.
    IPR012273. Alpha-crystallin_B.
    IPR003090. Alpha-crystallin_N.
    IPR008978. HSP20-like_chaperone.
    [Graphical view]
    PANTHERiPTHR11527:SF37. PTHR11527:SF37. 1 hit.
    PfamiPF00525. Crystallin. 1 hit.
    PF00011. HSP20. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036514. Sm_HSP_B1. 1 hit.
    PRINTSiPR00299. ACRYSTALLIN.
    SUPFAMiSSF49764. SSF49764. 1 hit.
    PROSITEiPS01031. HSP20. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P23927-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFST ATSLSPFYLR    50
    PPSFLRAPSW IDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV 100
    HGKHEERQDE HGFISREFHR KYRIPADVDP LTITSSLSSD GVLTVNGPRK 150
    QVSGPERTIP ITREEKPAVA AAPKK 175
    Length:175
    Mass (Da):20,069
    Last modified:July 15, 1999 - v2
    Checksum:i46702976C008EFD3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63170 mRNA. Translation: AAA37472.1.
    M73741 Genomic DNA. Translation: AAA67045.1.
    BC010768 mRNA. Translation: AAH10768.1.
    M25770 Genomic DNA. Translation: AAA37133.1.
    CCDSiCCDS23172.1.
    PIRiA39608.
    RefSeqiNP_001276711.1. NM_001289782.1.
    NP_001276713.1. NM_001289784.1.
    NP_001276714.1. NM_001289785.1.
    NP_034094.1. NM_009964.3.
    XP_006510033.1. XM_006509970.1.
    UniGeneiMm.178.

    Genome annotation databases

    EnsembliENSMUST00000034562; ENSMUSP00000034562; ENSMUSG00000032060.
    GeneIDi12955.
    KEGGimmu:12955.
    UCSCiuc009pkl.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63170 mRNA. Translation: AAA37472.1 .
    M73741 Genomic DNA. Translation: AAA67045.1 .
    BC010768 mRNA. Translation: AAH10768.1 .
    M25770 Genomic DNA. Translation: AAA37133.1 .
    CCDSi CCDS23172.1.
    PIRi A39608.
    RefSeqi NP_001276711.1. NM_001289782.1.
    NP_001276713.1. NM_001289784.1.
    NP_001276714.1. NM_001289785.1.
    NP_034094.1. NM_009964.3.
    XP_006510033.1. XM_006509970.1.
    UniGenei Mm.178.

    3D structure databases

    ProteinModelPortali P23927.
    SMRi P23927. Positions 1-175.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198909. 7 interactions.
    DIPi DIP-31060N.
    IntActi P23927. 11 interactions.
    MINTi MINT-1591396.

    PTM databases

    PhosphoSitei P23927.

    2D gel databases

    SWISS-2DPAGE P23927.

    Proteomic databases

    MaxQBi P23927.
    PaxDbi P23927.
    PRIDEi P23927.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034562 ; ENSMUSP00000034562 ; ENSMUSG00000032060 .
    GeneIDi 12955.
    KEGGi mmu:12955.
    UCSCi uc009pkl.1. mouse.

    Organism-specific databases

    CTDi 1410.
    MGIi MGI:88516. Cryab.

    Phylogenomic databases

    eggNOGi NOG246790.
    HOGENOMi HOG000233954.
    HOVERGENi HBG054766.
    InParanoidi P23927.
    KOi K09542.
    OMAi RKQAPGP.
    OrthoDBi EOG7WHHBK.
    PhylomeDBi P23927.
    TreeFami TF105049.

    Miscellaneous databases

    ChiTaRSi CRYAB. mouse.
    NextBioi 282674.
    PROi P23927.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P23927.
    Bgeei P23927.
    CleanExi MM_CRYAB.
    Genevestigatori P23927.

    Family and domain databases

    Gene3Di 2.60.40.790. 1 hit.
    InterProi IPR002068. a-crystallin/Hsp20_dom.
    IPR001436. Alpha-crystallin/HSP.
    IPR012273. Alpha-crystallin_B.
    IPR003090. Alpha-crystallin_N.
    IPR008978. HSP20-like_chaperone.
    [Graphical view ]
    PANTHERi PTHR11527:SF37. PTHR11527:SF37. 1 hit.
    Pfami PF00525. Crystallin. 1 hit.
    PF00011. HSP20. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036514. Sm_HSP_B1. 1 hit.
    PRINTSi PR00299. ACRYSTALLIN.
    SUPFAMi SSF49764. SSF49764. 1 hit.
    PROSITEi PS01031. HSP20. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Alpha B crystallin accumulation is a specific response to Ha-ras and v-mos oncogene expression in mouse NIH 3T3 fibroblasts."
      Klemenz R., Froehli E., Aoyama A., Hoffmann S., Simpson R.J., Moritz R.L., Schaeffer R.
      Mol. Cell. Biol. 11:803-812(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-10 AND 68-81.
    2. "Structure and alternate tissue-preferred transcription initiation of the mouse alpha B-crystallin/small heat shock protein gene."
      Frederikse P.H., Dubin R.A., Haynes J.I., Piatigorsky J.
      Nucleic Acids Res. 22:5686-5694(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: BALB/c.
      Tissue: Lung.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Kidney.
    4. "Expression of the murine alpha B-crystallin gene is not restricted to the lens."
      Dubin R.A., Wawrousek E.F., Piatigorsky J.
      Mol. Cell. Biol. 9:1083-1091(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
    5. Lubec G., Klug S.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 12-22 AND 124-149, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hippocampus.
    6. "Identification and characterization of a novel protein from Sertoli cells, PASS1, that associates with mammalian small stress protein hsp27."
      Liu C., Gilmont R.R., Benndorf R., Welsh M.J.
      J. Biol. Chem. 275:18724-18731(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HSPBAP1.

    Entry informationi

    Entry nameiCRYAB_MOUSE
    AccessioniPrimary (citable) accession number: P23927
    Secondary accession number(s): Q64325
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: July 15, 1999
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3