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P53674

- CRBB1_HUMAN

UniProt

P53674 - CRBB1_HUMAN

Protein

Beta-crystallin B1

Gene

CRYBB1

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
    Sitei216 – 2161Susceptible to oxidation
    Sitei226 – 2261Susceptible to oxidation

    GO - Molecular functioni

    1. structural constituent of eye lens Source: UniProtKB-KW

    GO - Biological processi

    1. visual perception Source: ProtInc

    Keywords - Molecular functioni

    Eye lens protein

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-crystallin B1
    Alternative name(s):
    Beta-B1 crystallin
    Gene namesi
    Name:CRYBB1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:2397. CRYBB1.

    Pathology & Biotechi

    Involvement in diseasei

    Cataract 17, multiple types (CTRCT17) [MIM:611544]: 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. CTRCT17 includes nuclear and pulverulent cataracts, among others. Nuclear cataracts affect the central nucleus of the eye, are often not highly visually significant. The density of the opacities varies greatly from fine dots to a dense, white and chalk-like, central cataract. The condition is usually bilateral. Nuclear cataracts are often combined with opacified cortical fibers encircling the nuclear opacity, which are referred to as cortical riders. Pulverulent cataracts are characterized by a dust-like, 'pulverised' appearance of the opacities which can be found in any part of the lens.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti96 – 961V → F in CTRCT17. 1 Publication
    VAR_070030
    CRYBB1 mutations may be a cause of congenital cataract and microcornea syndrome (CCMC), a disease characterized by the association of congenital cataract and microcornea without any other systemic anomaly or dysmorphism. Clinical findings include a corneal diameter inferior to 10 mm in both meridians in an otherwise normal eye, and an inherited cataract, which is most often bilateral posterior polar with opacification in the lens periphery. The cataract progresses to form a total cataract after visual maturity has been achieved, requiring cataract extraction in the first to third decade of life (PubMed:16110300 and PubMed:21972112).

    Keywords - Diseasei

    Cataract, Disease mutation

    Organism-specific databases

    MIMi611544. phenotype.
    Orphaneti1377. Cataract-microcornea syndrome.
    98991. Nuclear cataract.
    98984. Pulverulent cataract.
    PharmGKBiPA26911.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 252251Beta-crystallin B1PRO_0000057550Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication

    Post-translational modificationi

    Specific cleavages in the N-terminal arm occur during lens maturation and give rise to truncated forms, leading to impaired oligomerization and protein insolubilization.

    Keywords - PTMi

    Acetylation, Oxidation

    Proteomic databases

    PaxDbiP53674.
    PeptideAtlasiP53674.
    PRIDEiP53674.

    PTM databases

    PhosphoSiteiP53674.

    Miscellaneous databases

    PMAP-CutDBP53674.

    Expressioni

    Gene expression databases

    BgeeiP53674.
    CleanExiHS_CRYBB1.
    GenevestigatoriP53674.

    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.

    Protein-protein interaction databases

    BioGridi107804. 2 interactions.
    IntActiP53674. 3 interactions.
    MINTiMINT-5161833.
    STRINGi9606.ENSP00000215939.

    Structurei

    Secondary structure

    1
    252
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi60 – 667
    Turni67 – 693
    Beta strandi70 – 789
    Turni83 – 875
    Beta strandi93 – 986
    Beta strandi101 – 1066
    Helixi107 – 1093
    Beta strandi110 – 1167
    Beta strandi118 – 1214
    Helixi124 – 1274
    Beta strandi138 – 1414
    Beta strandi150 – 1567
    Helixi157 – 1593
    Beta strandi160 – 16910
    Helixi174 – 1774
    Beta strandi185 – 19814
    Turni199 – 2013
    Beta strandi202 – 2087
    Beta strandi210 – 2156
    Helixi216 – 2194
    Beta strandi228 – 2325

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1OKIX-ray1.40A/B43-252[»]
    ProteinModelPortaliP53674.
    SMRiP53674. Positions 55-237.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP53674.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini59 – 9840Beta/gamma crystallin 'Greek key' 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini99 – 14345Beta/gamma crystallin 'Greek key' 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini149 – 19042Beta/gamma crystallin 'Greek key' 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini191 – 23343Beta/gamma crystallin 'Greek key' 4PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 5857N-terminal armAdd
    BLAST
    Regioni144 – 1485Connecting peptide
    Regioni235 – 25218C-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

    eggNOGiNOG40509.
    HOGENOMiHOG000234388.
    HOVERGENiHBG003364.
    InParanoidiP53674.
    OMAiSCCHNIS.
    OrthoDBiEOG754HNK.
    PhylomeDBiP53674.
    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.

    P53674-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQAAKASAS ATVAVNPGPD TKGKGAPPAG TSPSPGTTLA PTTVPITSAK    50
    AAELPPGNYR LVVFELENFQ GRRAEFSGEC SNLADRGFDR VRSIIVSAGP 100
    WVAFEQSNFR GEMFILEKGE YPRWNTWSSS YRSDRLMSFR PIKMDAQEHK 150
    ISLFEGANFK GNTIEIQGDD APSLWVYGFS DRVGSVKVSS GTWVGYQYPG 200
    YRGYQYLLEP GDFRHWNEWG AFQPQMQSLR RLRDKQWHLE GSFPVLATEP 250
    PK 252
    Length:252
    Mass (Da):28,023
    Last modified:January 23, 2007 - v2
    Checksum:i93D81A9C95A86F7F
    GO

    Mass spectrometryi

    Molecular mass is 27941±6 Da from positions 2 - 252. Determined by ESI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti96 – 961V → F in CTRCT17. 1 Publication
    VAR_070030
    Natural varianti129 – 1291S → R in CCMC; probable disease-associated mutation found in a family with autosomal dominant congenital cataract and microcornea; significantly decreased thermal stability of CRYBB1/CRYBA1-crystallin heteromer but not CRYBB1-crystallin homomer. 1 Publication
    VAR_065296

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U35340 mRNA. Translation: AAC50383.1.
    CR456425 mRNA. Translation: CAG30311.1.
    Z95115 Genomic DNA. Translation: CAB08268.1.
    BC036790 mRNA. Translation: AAH36790.1.
    X86398 Genomic DNA. Translation: CAA60150.1.
    CCDSiCCDS13840.1.
    PIRiS55441.
    RefSeqiNP_001878.1. NM_001887.3.
    UniGeneiHs.37135.

    Genome annotation databases

    EnsembliENST00000215939; ENSP00000215939; ENSG00000100122.
    GeneIDi1414.
    KEGGihsa:1414.
    UCSCiuc003acy.1. human.

    Polymorphism databases

    DMDMi1706116.

    Cross-referencesi

    Web resourcesi

    Eye disease Crystallin, beta-B1 (CRYBB1)

    Leiden Open Variation Database (LOVD)

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U35340 mRNA. Translation: AAC50383.1 .
    CR456425 mRNA. Translation: CAG30311.1 .
    Z95115 Genomic DNA. Translation: CAB08268.1 .
    BC036790 mRNA. Translation: AAH36790.1 .
    X86398 Genomic DNA. Translation: CAA60150.1 .
    CCDSi CCDS13840.1.
    PIRi S55441.
    RefSeqi NP_001878.1. NM_001887.3.
    UniGenei Hs.37135.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1OKI X-ray 1.40 A/B 43-252 [» ]
    ProteinModelPortali P53674.
    SMRi P53674. Positions 55-237.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107804. 2 interactions.
    IntActi P53674. 3 interactions.
    MINTi MINT-5161833.
    STRINGi 9606.ENSP00000215939.

    PTM databases

    PhosphoSitei P53674.

    Polymorphism databases

    DMDMi 1706116.

    Proteomic databases

    PaxDbi P53674.
    PeptideAtlasi P53674.
    PRIDEi P53674.

    Protocols and materials databases

    DNASUi 1414.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000215939 ; ENSP00000215939 ; ENSG00000100122 .
    GeneIDi 1414.
    KEGGi hsa:1414.
    UCSCi uc003acy.1. human.

    Organism-specific databases

    CTDi 1414.
    GeneCardsi GC22M026995.
    HGNCi HGNC:2397. CRYBB1.
    MIMi 600929. gene.
    611544. phenotype.
    neXtProti NX_P53674.
    Orphaneti 1377. Cataract-microcornea syndrome.
    98991. Nuclear cataract.
    98984. Pulverulent cataract.
    PharmGKBi PA26911.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG40509.
    HOGENOMi HOG000234388.
    HOVERGENi HBG003364.
    InParanoidi P53674.
    OMAi SCCHNIS.
    OrthoDBi EOG754HNK.
    PhylomeDBi P53674.
    TreeFami TF331401.

    Miscellaneous databases

    EvolutionaryTracei P53674.
    GeneWikii CRYBB1.
    GenomeRNAii 1414.
    NextBioi 5785.
    PMAP-CutDB P53674.
    PROi P53674.
    SOURCEi Search...

    Gene expression databases

    Bgeei P53674.
    CleanExi HS_CRYBB1.
    Genevestigatori P53674.

    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. "The sequence of human betaB1-crystallin cDNA allows mass spectrometric detection of betaB1 protein missing portions of its N-terminal extension."
      David L.L., Lampi K.J., Lund A.L., Smith J.B.
      J. Biol. Chem. 271:4273-4279(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-22 AND 25-252, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY.
      Tissue: Lens.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "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].
    4. "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].
    5. "Assignment of the beta B1 crystallin gene (CRYBB1) to human chromosome 22 and mouse chromosome 5."
      Hulsebos T.J.M., Gilbert D.J., Delattre O., Smink L.J., Dunham I., Westerveld A., Thomas G., Jenkins N.A., Copeland N.G.
      Genomics 29:712-718(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 200-246.
    6. "A nonsense mutation in CRYBB1 associated with autosomal dominant cataract linked to human chromosome 22q."
      Mackay D.S., Boskovska O.B., Knopf H.L., Lampi K.J., Shiels A.
      Am. J. Hum. Genet. 71:1216-1221(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CTRCT17.
    7. "Oligomerization and phase transitions in aqueous solutions of native and truncated human beta B1-crystallin."
      Annunziata O., Pande A., Pande J., Ogun O., Lubsen N.H., Benedek G.B.
      Biochemistry 44:1316-1328(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    8. "CRYBB1 mutation associated with congenital cataract and microcornea."
      Willoughby C.E., Shafiq A., Ferrini W., Chan L.L., Billingsley G., Priston M., Mok C., Chandna A., Kaye S., Heon E.
      Mol. Vis. 11:587-593(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CCMC.
    9. "Crystal structure of truncated human betaB1-crystallin."
      Van Montfort R.L., Bateman O.A., Lubsen N.H., Slingsby C.
      Protein Sci. 12:2606-2612(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 43-252.
    10. "Homozygous CRYBB1 deletion mutation underlies autosomal recessive congenital cataract."
      Cohen D., Bar-Yosef U., Levy J., Gradstein L., Belfair N., Ofir R., Joshua S., Lifshitz T., Carmi R., Birk O.S.
      Invest. Ophthalmol. Vis. Sci. 48:2208-2213(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CTRCT17.
    11. "A novel mutation in CRYBB1 associated with congenital cataract-microcornea syndrome: the p.Ser129Arg mutation destabilizes the betaB1/betaA3-crystallin heteromer but not the betaB1-crystallin homomer."
      Wang K.J., Wang S., Cao N.-Q., Yan Y.-B., Zhu S.Q.
      Hum. Mutat. 32:E2050-E2060(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CCMC ARG-129, CHARACTERIZATION OF VARIANT CCMC ARG-129.
    12. "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 CTRCT17 PHE-96.

    Entry informationi

    Entry nameiCRBB1_HUMAN
    AccessioniPrimary (citable) accession number: P53674
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    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