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P02489

- CRYAA_HUMAN

UniProt

P02489 - CRYAA_HUMAN

Protein

Alpha-crystallin A chain

Gene

CRYAA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Contributes 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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei1 – 11Susceptible to oxidation
    Sitei18 – 181Susceptible to oxidation
    Sitei34 – 341Susceptible to oxidation
    Metal bindingi79 – 791Zinc 1Curated
    Metal bindingi100 – 1001Zinc 2By similarity
    Metal bindingi102 – 1021Zinc 2By similarity
    Metal bindingi107 – 1071Zinc 1Curated
    Metal bindingi115 – 1151Zinc 1Curated
    Sitei138 – 1381Susceptible to oxidation

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. structural constituent of eye lens Source: UniProtKB-KW
    5. unfolded protein binding Source: UniProtKB

    GO - Biological processi

    1. actin filament organization Source: Ensembl
    2. apoptotic process involved in morphogenesis Source: Ensembl
    3. embryonic camera-type eye morphogenesis Source: Ensembl
    4. lens fiber cell morphogenesis Source: Ensembl
    5. mitochondrion organization Source: Ensembl
    6. negative regulation of apoptotic process Source: UniProtKB
    7. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    8. negative regulation of gene expression Source: Ensembl
    9. negative regulation of intracellular transport Source: HGNC
    10. positive regulation of cell growth Source: Ensembl
    11. positive regulation of protein phosphorylation Source: Ensembl
    12. protein folding Source: Ensembl
    13. protein homooligomerization Source: UniProtKB
    14. response to drug Source: Ensembl
    15. response to glucocorticoid Source: Ensembl
    16. response to hydrogen peroxide Source: Ensembl
    17. response to hypoxia Source: Ensembl
    18. response to lead ion Source: Ensembl
    19. response to UV-A Source: Ensembl
    20. tubulin complex assembly Source: Ensembl
    21. visual perception Source: UniProtKB

    Keywords - Molecular functioni

    Chaperone, Eye lens protein

    Keywords - Biological processi

    Sensory transduction, Vision

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-crystallin A chain
    Alternative name(s):
    Heat shock protein beta-4
    Short name:
    HspB4
    Cleaved into the following 3 chains:
    Gene namesi
    Name:CRYAA
    Synonyms:CRYA1, HSPB4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:2388. CRYAA.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Alpha-crystallin A 1-172 is found at nearly twofold higher levels in diabetic lenses than in age-matched control lenses.1 Publication
    Cataract 9, multiple types (CTRCT9) [MIM:604219]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT9 includes nuclear, zonular central nuclear, anterior polar, cortical, embryonal, anterior subcapsular, fan-shaped, and total cataracts, among others. In some cases cataract is associated with microcornea without any other systemic anomaly or dysmorphism. Microcornea is defined by a corneal diameter inferior to 10 mm in both meridians in an otherwise normal eye.6 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti12 – 121R → C in CTRCT9. 1 Publication
    VAR_070032
    Natural varianti21 – 211R → L in CTRCT9; associated with macular hypoplasia and a generally hypopigmented fundus. 1 Publication
    VAR_046892
    Natural varianti49 – 491R → C in CTRCT9; nuclear cataract. 1 Publication
    VAR_038375
    Natural varianti116 – 1161R → C in CTRCT9; zonular central nuclear cataract; reduced chaperone-like activity and increased membrane-binding capacity. 1 Publication
    VAR_003819
    Natural varianti116 – 1161R → H in CTRCT9; reverse phase-high-performance liquid chromatography suggests an increase hydrophobicity of the mutant protein; loss of chaperone activity of the mutant is seen in DL-dithiothreitol-induced insulin aggregation assay; fast protein liquid chromatography purification shows that the mutant protein has increased binding affinity to lysozyme. 2 Publications
    VAR_046893

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi123 – 1231N → D: Impairs chaperone activity. 1 Publication

    Keywords - Diseasei

    Cataract, Disease mutation

    Organism-specific databases

    MIMi604219. phenotype.
    Orphaneti1377. Cataract-microcornea syndrome.
    98991. Nuclear cataract.
    98995. Zonular cataract.
    PharmGKBiPA26906.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 173173Alpha-crystallin A chainPRO_0000125865Add
    BLAST
    Chaini1 – 172172Alpha-crystallin A(1-172)PRO_0000226639Add
    BLAST
    Chaini1 – 168168Alpha-crystallin A(1-168)PRO_0000423503Add
    BLAST
    Chaini1 – 162162Alpha-crystallin A(1-162)PRO_0000423504Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei6 – 61Deamidated glutamine; partial1 Publication
    Modified residuei45 – 451Phosphoserine1 Publication
    Modified residuei50 – 501Deamidated glutamine; partial1 Publication
    Modified residuei70 – 701N6-acetyllysine2 Publications
    Modified residuei90 – 901Deamidated glutamine; partial1 Publication
    Modified residuei99 – 991N6-acetyllysine1 Publication
    Modified residuei101 – 1011Deamidated asparagine; partial4 Publications
    Modified residuei122 – 1221Phosphoserine3 Publications
    Modified residuei123 – 1231Deamidated asparagine; partial1 Publication
    Disulfide bondi131 ↔ 1422 Publications
    Modified residuei147 – 1471Deamidated glutamine; partial1 Publication
    Glycosylationi162 – 1621O-linked (GlcNAc)By similarity

    Post-translational modificationi

    O-glycosylated; contains N-acetylglucosamine side chains.
    Deamidation of Asn-101 in lens occurs mostly during the first 30 years of age, followed by a small additional amount of deamidation (approximately 5%) during the next approximately 38 years, resulting in a maximum of approximately 50% deamidation during the lifetime of the individual.5 Publications
    Phosphorylation on Ser-122 seems to be developmentally regulated. Absent in the first months of life, it appears during the first 12 years of human lifetime. The relative amount of phosphorylated form versus unphosphorylated form does not change over the lifetime of the individual.5 Publications
    Acetylation at Lys-70 seems to increase chaperone activity.3 Publications
    Undergoes age-dependent proteolytical cleavage at the C-terminus. Alpha-crystallin A(1-172) is the most predominant form produced most rapidly during the first 12 years of age and after this age is present in approximatley 50% of the lens molecules.5 Publications

    Keywords - PTMi

    Acetylation, Disulfide bond, Glycoprotein, Oxidation, Phosphoprotein

    Proteomic databases

    PaxDbiP02489.
    PeptideAtlasiP02489.
    PRIDEiP02489.

    2D gel databases

    SWISS-2DPAGEP02489.

    PTM databases

    PhosphoSiteiP02489.
    UniCarbKBiP02489.

    Expressioni

    Tissue specificityi

    Expressed in eye lens.1 Publication

    Gene expression databases

    ArrayExpressiP02489.
    BgeeiP02489.
    CleanExiHS_CRYAA.
    GenevestigatoriP02489.

    Interactioni

    Subunit structurei

    Heteropolymer composed of three CRYAA and one CRYAB subunits. Inter-subunit bridging via zinc ions enhances stability, which is crucial as there is no protein turn over in the lens. Can also form homodimers and higher homooligomers. Age-dependent C-terminal truncation affects oligomerization.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-6875961,EBI-6875961
    CRYABP025117EBI-6875961,EBI-739060
    CRYGCP073153EBI-6875961,EBI-6875941

    Protein-protein interaction databases

    BioGridi107799. 12 interactions.
    DIPiDIP-41265N.
    IntActiP02489. 4 interactions.
    MINTiMINT-220977.
    STRINGi9606.ENSP00000291554.

    Structurei

    3D structure databases

    DisProtiDP00444.
    ProteinModelPortaliP02489.
    SMRiP02489. Positions 1-171.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG278874.
    HOGENOMiHOG000233954.
    HOVERGENiHBG054766.
    InParanoidiP02489.
    KOiK09541.
    OMAiGPKVQSG.
    OrthoDBiEOG7WHHBK.
    PhylomeDBiP02489.
    TreeFamiTF105049.

    Family and domain databases

    Gene3Di2.60.40.790. 1 hit.
    InterProiIPR002068. a-crystallin/Hsp20_dom.
    IPR001436. Alpha-crystallin/HSP.
    IPR012274. Alpha-crystallin_A.
    IPR003090. Alpha-crystallin_N.
    IPR008978. HSP20-like_chaperone.
    [Graphical view]
    PANTHERiPTHR11527:SF36. PTHR11527:SF36. 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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P02489-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDVTIQHPWF KRTLGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ    50
    SLFRTVLDSG ISEVRSDRDK FVIFLDVKHF SPEDLTVKVQ DDFVEIHGKH 100
    NERQDDHGYI SREFHRRYRL PSNVDQSALS CSLSADGMLT FCGPKIQTGL 150
    DATHAERAIP VSREEKPTSA PSS 173
    Length:173
    Mass (Da):19,909
    Last modified:October 1, 1996 - v2
    Checksum:i81804A8439837D50
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti45 – 451S → T in AAA52105. (PubMed:3758227)Curated
    Sequence conflicti153 – 1553THA → HT(PubMed:8587135)Curated

    Mass spectrometryi

    Molecular mass is 19950 Da from positions 1 - 173. Determined by ESI. 1 Publication
    Molecular mass is 19863 Da from positions 1 - 172. Determined by ESI. 1 Publication
    Molecular mass is 20029 Da from positions 1 - 173. Determined by ESI. With 1 phosphate group.1 Publication
    Molecular mass is 19951 Da from positions 1 - 173. Determined by ESI. 1 Publication
    Molecular mass is 19864 Da from positions 1 - 172. Determined by ESI. 1 Publication
    Molecular mass is 19947 Da from positions 1 - 173. Determined by ESI. 1 Publication
    Molecular mass is 19851 Da from positions 1 - 172. Determined by ESI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti12 – 121R → C in CTRCT9. 1 Publication
    VAR_070032
    Natural varianti21 – 211R → L in CTRCT9; associated with macular hypoplasia and a generally hypopigmented fundus. 1 Publication
    VAR_046892
    Natural varianti49 – 491R → C in CTRCT9; nuclear cataract. 1 Publication
    VAR_038375
    Natural varianti105 – 1051D → H in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036564
    Natural varianti116 – 1161R → C in CTRCT9; zonular central nuclear cataract; reduced chaperone-like activity and increased membrane-binding capacity. 1 Publication
    VAR_003819
    Natural varianti116 – 1161R → H in CTRCT9; reverse phase-high-performance liquid chromatography suggests an increase hydrophobicity of the mutant protein; loss of chaperone activity of the mutant is seen in DL-dithiothreitol-induced insulin aggregation assay; fast protein liquid chromatography purification shows that the mutant protein has increased binding affinity to lysozyme. 2 Publications
    VAR_046893

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U05569 mRNA. Translation: AAA97523.1.
    U66584 mRNA. Translation: AAC50900.1.
    X14789 mRNA. Translation: CAA32891.1.
    CR407691 mRNA. Translation: CAG28619.1.
    AP001631 Genomic DNA. No translation available.
    AP001748 Genomic DNA. Translation: BAA95535.1.
    CH471079 Genomic DNA. Translation: EAX09497.1.
    CH471079 Genomic DNA. Translation: EAX09498.1.
    BC069528 mRNA. Translation: AAH69528.1.
    BC113598 mRNA. Translation: AAI13599.1.
    M35628 Genomic DNA. Translation: AAA52106.1.
    M35629 Genomic DNA. Translation: AAA52105.1.
    CCDSiCCDS13695.1.
    PIRiS03344. CYHUAA.
    RefSeqiNP_000385.1. NM_000394.3.
    XP_006723993.1. XM_006723930.1.
    XP_006726864.1. XM_006726801.1.
    UniGeneiHs.184085.

    Genome annotation databases

    EnsembliENST00000291554; ENSP00000291554; ENSG00000160202.
    GeneIDi102724652.
    1409.
    KEGGihsa:102724652.
    hsa:1409.
    UCSCiuc002zdd.1. human.

    Polymorphism databases

    DMDMi1706112.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U05569 mRNA. Translation: AAA97523.1 .
    U66584 mRNA. Translation: AAC50900.1 .
    X14789 mRNA. Translation: CAA32891.1 .
    CR407691 mRNA. Translation: CAG28619.1 .
    AP001631 Genomic DNA. No translation available.
    AP001748 Genomic DNA. Translation: BAA95535.1 .
    CH471079 Genomic DNA. Translation: EAX09497.1 .
    CH471079 Genomic DNA. Translation: EAX09498.1 .
    BC069528 mRNA. Translation: AAH69528.1 .
    BC113598 mRNA. Translation: AAI13599.1 .
    M35628 Genomic DNA. Translation: AAA52106.1 .
    M35629 Genomic DNA. Translation: AAA52105.1 .
    CCDSi CCDS13695.1.
    PIRi S03344. CYHUAA.
    RefSeqi NP_000385.1. NM_000394.3.
    XP_006723993.1. XM_006723930.1.
    XP_006726864.1. XM_006726801.1.
    UniGenei Hs.184085.

    3D structure databases

    DisProti DP00444.
    ProteinModelPortali P02489.
    SMRi P02489. Positions 1-171.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107799. 12 interactions.
    DIPi DIP-41265N.
    IntActi P02489. 4 interactions.
    MINTi MINT-220977.
    STRINGi 9606.ENSP00000291554.

    PTM databases

    PhosphoSitei P02489.
    UniCarbKBi P02489.

    Polymorphism databases

    DMDMi 1706112.

    2D gel databases

    SWISS-2DPAGE P02489.

    Proteomic databases

    PaxDbi P02489.
    PeptideAtlasi P02489.
    PRIDEi P02489.

    Protocols and materials databases

    DNASUi 1409.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000291554 ; ENSP00000291554 ; ENSG00000160202 .
    GeneIDi 102724652.
    1409.
    KEGGi hsa:102724652.
    hsa:1409.
    UCSCi uc002zdd.1. human.

    Organism-specific databases

    CTDi 1409.
    GeneCardsi GC21P044589.
    HGNCi HGNC:2388. CRYAA.
    MIMi 123580. gene.
    604219. phenotype.
    neXtProti NX_P02489.
    Orphaneti 1377. Cataract-microcornea syndrome.
    98991. Nuclear cataract.
    98995. Zonular cataract.
    PharmGKBi PA26906.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG278874.
    HOGENOMi HOG000233954.
    HOVERGENi HBG054766.
    InParanoidi P02489.
    KOi K09541.
    OMAi GPKVQSG.
    OrthoDBi EOG7WHHBK.
    PhylomeDBi P02489.
    TreeFami TF105049.

    Miscellaneous databases

    GeneWikii CRYAA.
    GenomeRNAii 1409.
    NextBioi 5761.
    PROi P02489.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02489.
    Bgeei P02489.
    CleanExi HS_CRYAA.
    Genevestigatori P02489.

    Family and domain databases

    Gene3Di 2.60.40.790. 1 hit.
    InterProi IPR002068. a-crystallin/Hsp20_dom.
    IPR001436. Alpha-crystallin/HSP.
    IPR012274. Alpha-crystallin_A.
    IPR003090. Alpha-crystallin_N.
    IPR008978. HSP20-like_chaperone.
    [Graphical view ]
    PANTHERi PTHR11527:SF36. PTHR11527:SF36. 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. "The amino acid sequence of the A chain of human alpha-crystallin."
      de Jong W.W., Terwindt E.C., Bloemendal H.
      FEBS Lett. 58:310-313(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY PROTEIN SEQUENCE, ACETYLATION AT MET-1.
    2. "A reassessment of mammalian alpha A-crystallin sequences using DNA sequencing: implications for anthropoid affinities of tarsier."
      Jaworski C.J.
      J. Mol. Evol. 41:901-908(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lens.
    3. "Cloning, expression, and chaperone-like activity of human alphaA-crystallin."
      Andley U.P., Mathur S., Griest T.A., Petrash J.M.
      J. Biol. Chem. 271:31973-31980(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lens.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "The DNA sequence of human chromosome 21."
      Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
      , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
      Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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].
      Tissue: Colon.
    8. "A pseudo-exon in the functional human alpha A-crystallin gene."
      Jaworski C.J., Piatigorsky J.
      Nature 337:752-754(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-104.
    9. "Isolation and partial characterization of the human alpha A-crystallin gene."
      McDevitt D.S., Hawkins J.W., Jaworski C.J., Piatigorsky J.
      Exp. Eye Res. 43:285-291(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-63 AND 166-173.
      Tissue: Spleen.
    10. "Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens."
      Lampi K.J., Ma Z., Shih M., Shearer T.R., Smith J.B., Smith D.L., David L.L.
      J. Biol. Chem. 272:2268-2275(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 13-21 AND 79-88.
    11. "Vertebrate lens alpha-crystallins are modified by O-linked N-acetylglucosamine."
      Roquemore E.P., Dell A., Morris H.R., Panico M., Reason A.J., Savoy L.-A., Wistow G.J., Zigler J.S. Jr., Earles B.J., Hart G.W.
      J. Biol. Chem. 267:555-563(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE OF CARBOHYDRATE.
    12. "Post-translational modifications of water-soluble human lens crystallins from young adults."
      Miesbauer L.R., Zhou X., Yang Z., Yang Z., Sun Y., Smith D.L., Smith J.B.
      J. Biol. Chem. 269:12494-12502(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-122, DISULFIDE BOND, PROTEOLYTIC PROCESSING OF C-TERMINAL, DEAMIDATION AT ASN-101, MASS SPECTROMETRY.
    13. "Differential phosphorylation of alpha-A crystallin in human lens of different age."
      Takemoto L.J.
      Exp. Eye Res. 62:499-504(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-122.
    14. "Modifications of the water-insoluble human lens alpha-crystallins."
      Lund A.L., Smith J.B., Smith D.L.
      Exp. Eye Res. 63:661-672(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING, SUSCEPTIBILITY TO OXIDATION, PHOSPHORYLATION AT SER-45 AND SER-122, DISULFIDE BOND, DEAMIDATION AT GLN-6; GLN-50; GLN-90; ASN-101 AND GLN-147, IDENTIFICATION BY MASS SPECTROMETRY.
    15. "Quantitation of asparagine-101 deamidation from alpha-A crystallin during aging of the human lens."
      Takemoto L.J.
      Curr. Eye Res. 17:247-250(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEAMIDATION AT ASN-101.
    16. "In vivo acetylation identified at lysine 70 of human lens alphaA-crystallin."
      Lin P.P., Barry R.C., Smith D.L., Smith J.B.
      Protein Sci. 7:1451-1457(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF C-TERMINAL, ACETYLATION AT LYS-70, PHOSPHORYLATION, DEAMIDATION AT ASN-101, MASS SPECTROMETRY.
    17. "The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage."
      Hanson S.R.A., Hasan A., Smith D.L., Smith J.B.
      Exp. Eye Res. 71:195-207(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, SUSCEPTIBILITY TO OXIDATION, PROTEOLYTIC PROCESSING OF C-TERMINAL, MASS SPECTROMETRY.
    18. "Chaperone-like activity of alpha-crystallin and other small heat shock proteins."
      Ganea E.
      Curr. Protein Pept. Sci. 2:205-225(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    19. "Enhanced C-terminal truncation of alphaA- and alphaB-crystallins in diabetic lenses."
      Thampi P., Hassan A., Smith J.B., Abraham E.C.
      Invest. Ophthalmol. Vis. Sci. 43:3265-3272(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING, TISSUE SPECIFICITY.
    20. "Structural and functional roles of deamidation and/or truncation of N- or C-termini in human alpha A-crystallin."
      Chaves J.M., Srivastava K., Gupta R., Srivastava O.P.
      Biochemistry 47:10069-10083(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEAMIDATION AT ASN-123, MUTAGENESIS OF ASN-123.
    21. "C-Terminal truncation affects subunit exchange of human alphaA-crystallin with alphaB-crystallin."
      Kallur L.S., Aziz A., Abraham E.C.
      Mol. Cell. Biochem. 308:85-91(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    22. "HSPB7 is a SC35 speckle resident small heat shock protein."
      Vos M.J., Kanon B., Kampinga H.H.
      Biochim. Biophys. Acta 1793:1343-1353(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    23. "Importance of eye lens alpha-crystallin heteropolymer with 3:1 alphaA to alphaB ratio: stability, aggregation, and modifications."
      Srinivas P., Narahari A., Petrash J.M., Swamy M.J., Reddy G.B.
      IUBMB Life 62:693-702(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    24. "Acetylation of alphaA-crystallin in the human lens: effects on structure and chaperone function."
      Nagaraj R.H., Nahomi R.B., Shanthakumar S., Linetsky M., Padmanabha S., Pasupuleti N., Wang B., Santhoshkumar P., Panda A.K., Biswas A.
      Biochim. Biophys. Acta 1822:120-129(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ACETYLATION AT LYS-70 AND LYS-99.
    25. "Identification of histidine residues involved in Zn(2+) binding to alphaA- and alphaB-Crystallin by chemical modification and MALDI TOF mass spectrometry."
      Karmakar S., Das K.P.
      Protein J. 31:623-640(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, ZINC-BINDING SITES.
    26. "Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA."
      Litt M., Kramer P., la Morticella D.M., Murphey W., Lovrien E.W., Weleber R.G.
      Hum. Mol. Genet. 7:471-474(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CTRCT9 CYS-116.
    27. "Structural and functional changes in the alpha A-crystallin R116C mutant in hereditary cataracts."
      Cobb B.A., Petrash J.M.
      Biochemistry 39:15791-15798(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT CTRCT9 CYS-116.
    28. "Cell death triggered by a novel mutation in the alphaA-crystallin gene underlies autosomal dominant cataract linked to chromosome 21q."
      Mackay D.S., Andley U.P., Shiels A.
      Eur. J. Hum. Genet. 11:784-793(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CTRCT9 CYS-49.
    29. "Congenital cataract and macular hypoplasia in humans associated with a de novo mutation in CRYAA and compound heterozygous mutations in P."
      Graw J., Klopp N., Illig T., Preising M.N., Lorenz B.
      Graefes Arch. Clin. Exp. Ophthalmol. 244:912-919(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CTRCT9 LEU-21.
    30. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-105.
    31. "Clinical variability of autosomal dominant cataract, microcornea and corneal opacity and novel mutation in the alpha A crystallin gene (CRYAA)."
      Richter L., Flodman P., Barria von-Bischhoffshausen F., Burch D., Brown S., Nguyen L., Turner J., Spence M.A., Bateman J.B.
      Am. J. Med. Genet. A 146:833-842(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CTRCT9 HIS-116.
    32. "A novel mutation in AlphaA-crystallin (CRYAA) caused autosomal dominant congenital cataract in a large Chinese family."
      Gu F., Luo W., Li X., Wang Z., Lu S., Zhang M., Zhao B., Zhu S., Feng S., Yan Y.-B., Huang S., Ma X.
      Hum. Mutat. 29:769-769(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CTRCT9 HIS-116, CHARACTERIZATION OF VARIANT CTRCT9 HIS-116.
    33. "Whole exome sequencing in dominant cataract identifies a new causative factor, CRYBA2, and a variety of novel alleles in known genes."
      Reis L.M., Tyler R.C., Muheisen S., Raggio V., Salviati L., Han D.P., Costakos D., Yonath H., Hall S., Power P., Semina E.V.
      Hum. Genet. 132:761-770(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CTRCT9 CYS-12.

    Entry informationi

    Entry nameiCRYAA_HUMAN
    AccessioniPrimary (citable) accession number: P02489
    Secondary accession number(s): Q53X53
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 160 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 21
      Human chromosome 21: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3