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P43320

- CRBB2_HUMAN

UniProt

P43320 - CRBB2_HUMAN

Protein

Beta-crystallin B2

Gene

CRYBB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Crystallins are the dominant structural components of the vertebrate eye lens.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei59 – 591Susceptible to oxidation
    Sitei122 – 1221Susceptible to oxidation
    Sitei151 – 1511Susceptible to oxidation

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. structural constituent of eye lens Source: UniProtKB-KW
    3. structural molecule activity Source: ProtInc

    GO - Biological processi

    1. camera-type eye development Source: Ensembl
    2. response to stimulus Source: UniProtKB-KW
    3. visual perception Source: ProtInc

    Keywords - Molecular functioni

    Eye lens protein

    Keywords - Biological processi

    Sensory transduction, Vision

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-crystallin B2
    Alternative name(s):
    Beta-B2 crystallin
    Beta-crystallin Bp
    Gene namesi
    Name:CRYBB2
    Synonyms:CRYB2, CRYB2A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:2398. CRYBB2.

    Pathology & Biotechi

    Involvement in diseasei

    Cataract 3, multiple types (CTRCT3) [MIM:601547]: 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. CTRCT3 includes congenital cerulean and sutural cataract with punctate and cerulean opacities, among others. Cerulean cataract is characterized by peripheral bluish and white opacifications organized in concentric layers with occasional central lesions arranged radially. The opacities are observed in the superficial layers of the fetal nucleus as well as the adult nucleus of the lens. Involvement is usually bilateral. Visual acuity is only mildly reduced in childhood. In adulthood, the opacifications may progress, making lens extraction necessary. Histologically the lesions are described as fusiform cavities between lens fibers which contain a deeply staining granular material. Although the lesions may take on various colors, a dull blue is the most common appearance and is responsible for the designation cerulean cataract. Sutural cataract with punctate and cerulean opacities is characterized by white opacification around the anterior and posterior Y sutures, and grayish and bluish, spindle shaped, oval punctate and cerulean opacities of various sizes arranged in lamellar form. The spots are more concentrated towards the peripheral layers and do not delineate the embryonal or fetal nucleus. Phenotypic variation with respect to the size and density of the sutural opacities as well as the number and position of punctate and cerulean spots is observed among affected subjects.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Cataract

    Organism-specific databases

    MIMi601547. phenotype.
    Orphaneti98985. Cataract with Y-shaped suture opacities.
    1377. Cataract-microcornea syndrome.
    98989. Cerulean cataract.
    98986. Coppock-like cataract.
    98991. Nuclear cataract.
    98994. Total congenital cataract.
    PharmGKBiPA26912.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 205204Beta-crystallin B2PRO_0000057553Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation, Oxidation

    Proteomic databases

    PaxDbiP43320.
    PeptideAtlasiP43320.
    PRIDEiP43320.

    PTM databases

    PhosphoSiteiP43320.

    Expressioni

    Gene expression databases

    BgeeiP43320.
    CleanExiHS_CRYBB2.
    GenevestigatoriP43320.

    Organism-specific databases

    HPAiHPA043749.

    Interactioni

    Subunit structurei

    Homo/heterodimer, or complexes of higher-order. The structure of beta-crystallin oligomers seems to be stabilized through interactions between the N-terminal arms By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-974082,EBI-974082

    Protein-protein interaction databases

    BioGridi107805. 6 interactions.
    IntActiP43320. 6 interactions.
    MINTiMINT-221083.
    STRINGi9606.ENSP00000215861.

    Structurei

    Secondary structure

    1
    205
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi18 – 247
    Beta strandi31 – 366
    Helixi41 – 444
    Beta strandi50 – 567
    Beta strandi59 – 646
    Turni65 – 673
    Beta strandi68 – 747
    Beta strandi76 – 794
    Helixi82 – 843
    Beta strandi96 – 994
    Beta strandi108 – 1147
    Turni115 – 1173
    Beta strandi118 – 12710
    Helixi133 – 1353
    Beta strandi143 – 1464
    Beta strandi151 – 1566
    Turni157 – 1593
    Beta strandi160 – 1667
    Beta strandi168 – 1714
    Helixi174 – 1774
    Beta strandi180 – 1823
    Beta strandi186 – 1894

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YTQX-ray1.70A2-205[»]
    ProteinModelPortaliP43320.
    SMRiP43320. Positions 15-195.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP43320.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 5640Beta/gamma crystallin 'Greek key' 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini57 – 10145Beta/gamma crystallin 'Greek key' 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini107 – 14842Beta/gamma crystallin 'Greek key' 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini149 – 19143Beta/gamma crystallin 'Greek key' 4PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 1615N-terminal armAdd
    BLAST
    Regioni102 – 1065Connecting peptide
    Regioni193 – 20513C-terminal armAdd
    BLAST

    Domaini

    Has a two-domain beta-structure, folded into four very similar Greek key motifs.

    Sequence similaritiesi

    Belongs to the beta/gamma-crystallin family.Curated
    Contains 4 beta/gamma crystallin 'Greek key' domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG41590.
    HOGENOMiHOG000234388.
    HOVERGENiHBG003364.
    InParanoidiP43320.
    OMAiGFQYLFE.
    OrthoDBiEOG754HNK.
    PhylomeDBiP43320.
    TreeFamiTF331401.

    Family and domain databases

    InterProiIPR001064. Beta/gamma_crystallin.
    IPR011024. G_crystallin-rel.
    [Graphical view]
    PfamiPF00030. Crystall. 2 hits.
    [Graphical view]
    PRINTSiPR01367. BGCRYSTALLIN.
    SMARTiSM00247. XTALbg. 2 hits.
    [Graphical view]
    SUPFAMiSSF49695. SSF49695. 1 hit.
    PROSITEiPS50915. CRYSTALLIN_BETA_GAMMA. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P43320-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASDHQTQAG KPQSLNPKII IFEQENFQGH SHELNGPCPN LKETGVEKAG    50
    SVLVQAGPWV GYEQANCKGE QFVFEKGEYP RWDSWTSSRR TDSLSSLRPI 100
    KVDSQEHKII LYENPNFTGK KMEIIDDDVP SFHAHGYQEK VSSVRVQSGT 150
    WVGYQYPGYR GLQYLLEKGD YKDSSDFGAP HPQVQSVRRI RDMQWHQRGA 200
    FHPSN 205
    Length:205
    Mass (Da):23,380
    Last modified:January 23, 2007 - v2
    Checksum:iFD95C354724A67D0
    GO

    Mass spectrometryi

    Molecular mass is 23291±3 Da from positions 2 - 205. Determined by ESI. 1 Publication
    Molecular mass is 23289 Da from positions 2 - 205. Determined by ESI. 1 Publication
    Molecular mass is 23290 Da from positions 2 - 205. Determined by ESI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti65 – 651A → S.
    Corresponds to variant rs16986560 [ dbSNP | Ensembl ].
    VAR_038431

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L10035 mRNA. Translation: AAA16864.1.
    U72404
    , U72400, U72401, U72402, U72403 Genomic DNA. Translation: AAB39700.1.
    CR456426 mRNA. Translation: CAG30312.1.
    Z99916 Genomic DNA. Translation: CAB17043.1.
    BC069535 mRNA. Translation: AAH69535.1.
    CCDSiCCDS13831.1.
    PIRiJC2009.
    RefSeqiNP_000487.1. NM_000496.2.
    XP_006724204.1. XM_006724141.1.
    UniGeneiHs.373074.

    Genome annotation databases

    EnsembliENST00000398215; ENSP00000381273; ENSG00000244752.
    GeneIDi1415.
    KEGGihsa:1415.
    UCSCiuc003abp.1. human.

    Polymorphism databases

    DMDMi1169091.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Eye disease Crystallin, beta-B2 (CRYBB2)

    Leiden Open Variation Database (LOVD)

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L10035 mRNA. Translation: AAA16864.1 .
    U72404
    , U72400 , U72401 , U72402 , U72403 Genomic DNA. Translation: AAB39700.1 .
    CR456426 mRNA. Translation: CAG30312.1 .
    Z99916 Genomic DNA. Translation: CAB17043.1 .
    BC069535 mRNA. Translation: AAH69535.1 .
    CCDSi CCDS13831.1.
    PIRi JC2009.
    RefSeqi NP_000487.1. NM_000496.2.
    XP_006724204.1. XM_006724141.1.
    UniGenei Hs.373074.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YTQ X-ray 1.70 A 2-205 [» ]
    ProteinModelPortali P43320.
    SMRi P43320. Positions 15-195.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107805. 6 interactions.
    IntActi P43320. 6 interactions.
    MINTi MINT-221083.
    STRINGi 9606.ENSP00000215861.

    PTM databases

    PhosphoSitei P43320.

    Polymorphism databases

    DMDMi 1169091.

    Proteomic databases

    PaxDbi P43320.
    PeptideAtlasi P43320.
    PRIDEi P43320.

    Protocols and materials databases

    DNASUi 1415.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000398215 ; ENSP00000381273 ; ENSG00000244752 .
    GeneIDi 1415.
    KEGGi hsa:1415.
    UCSCi uc003abp.1. human.

    Organism-specific databases

    CTDi 1415.
    GeneCardsi GC22P025615.
    HGNCi HGNC:2398. CRYBB2.
    HPAi HPA043749.
    MIMi 123620. gene.
    601547. phenotype.
    neXtProti NX_P43320.
    Orphaneti 98985. Cataract with Y-shaped suture opacities.
    1377. Cataract-microcornea syndrome.
    98989. Cerulean cataract.
    98986. Coppock-like cataract.
    98991. Nuclear cataract.
    98994. Total congenital cataract.
    PharmGKBi PA26912.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG41590.
    HOGENOMi HOG000234388.
    HOVERGENi HBG003364.
    InParanoidi P43320.
    OMAi GFQYLFE.
    OrthoDBi EOG754HNK.
    PhylomeDBi P43320.
    TreeFami TF331401.

    Miscellaneous databases

    ChiTaRSi CRYBB2. human.
    EvolutionaryTracei P43320.
    GeneWikii CRYBB2.
    GenomeRNAii 1415.
    NextBioi 5789.
    PROi P43320.
    SOURCEi Search...

    Gene expression databases

    Bgeei P43320.
    CleanExi HS_CRYBB2.
    Genevestigatori P43320.

    Family and domain databases

    InterProi IPR001064. Beta/gamma_crystallin.
    IPR011024. G_crystallin-rel.
    [Graphical view ]
    Pfami PF00030. Crystall. 2 hits.
    [Graphical view ]
    PRINTSi PR01367. BGCRYSTALLIN.
    SMARTi SM00247. XTALbg. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49695. SSF49695. 1 hit.
    PROSITEi PS50915. CRYSTALLIN_BETA_GAMMA. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of the human lens beta B2-crystallin-encoding cDNA."
      Chambers C., Russell P.
      Gene 133:295-299(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lens.
    2. "Autosomal dominant cerulean cataract is associated with a chain termination mutation in the human beta-crystallin gene CRYBB2."
      Litt M., Carrero-Valenzuela R., Lamorticella D.M., Schultz D.W., Mitchell T.N., Kramer P., Maumenee I.H.
      Hum. Mol. Genet. 6:665-668(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN CTRCT3.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
    6. "Amino acid sequence of human lens beta B2-crystallin."
      Miesbauer L.R., Smith J.B., Smith D.L.
      Protein Sci. 2:290-291(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-205, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2.
      Tissue: Lens.
    7. "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 192-205, MASS SPECTROMETRY.
    8. "Two-dimensional gel electrophoretic analysis of human lens proteins."
      Datiles M.B., Schumer D.J., Zigler J.S. Jr., Russell P., Anderson L., Garland D.
      Curr. Eye Res. 11:669-677(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 123-142.
      Tissue: Lens.
    9. "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: MASS SPECTROMETRY.
    10. "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: MASS SPECTROMETRY.
    11. "Genetic heterogeneity of the Coppock-like cataract: a mutation in CRYBB2 on chromosome 22q11.2."
      Gill D., Klose R., Munier F.L., McFadden M., Priston M., Billingsley G., Ducrey N., Schorderet D.F., Heon E.
      Invest. Ophthalmol. Vis. Sci. 41:159-165(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CTRCT3.
    12. "Mutation of interfaces in domain-swapped human betaB2-crystallin."
      Smith M.A., Bateman O.A., Jaenicke R., Slingsby C.
      Protein Sci. 16:615-625(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-205, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiCRBB2_HUMAN
    AccessioniPrimary (citable) accession number: P43320
    Secondary accession number(s): Q9UCM8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 143 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3