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P05813

- CRBA1_HUMAN

UniProt

P05813 - CRBA1_HUMAN

Protein

Beta-crystallin A3

Gene

CRYBA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 4 (01 Nov 1997)
      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
    Sitei126 – 1261Susceptible to oxidation

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. structural constituent of eye lens Source: UniProtKB-KW

    GO - Biological processi

    1. lens development in camera-type eye Source: Ensembl
    2. visual perception Source: UniProtKB

    Keywords - Molecular functioni

    Eye lens protein

    Names & Taxonomyi

    Protein namesi
    Gene namesi
    Name:CRYBA1
    Synonyms:CRYB1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:2394. CRYBA1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB

    Pathology & Biotechi

    Involvement in diseasei

    Cataract 10, multiple types (CTRCT10) [MIM:600881]: 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. CTRCT10 includes congenital zonular with sutural opacities, among others. This is a form of zonular cataract with an erect Y-shaped anterior and an inverted Y-shaped posterior sutural opacities. Zonular or lamellar cataracts are opacities, broad or narrow, usually consisting of powdery white dots affecting only certain layers or zones between the cortex and nucleus of an otherwise clear lens. The opacity may be so dense as to render the entire central region of the lens completely opaque, or so translucent that vision is hardly if at all impeded. Zonular cataracts generally do not involve the embryonic nucleus, though sometimes they involve the fetal nucleus. Usually sharply separated from a clear cortex outside them, they may have projections from their outer edges known as riders or spokes.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Cataract

    Organism-specific databases

    MIMi600881. phenotype.
    Orphaneti98985. Cataract with Y-shaped suture opacities.
    98995. Zonular cataract.
    PharmGKBiPA26908.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 215215Beta-crystallin A3PRO_0000006331Add
    BLAST
    Chaini23 – 215193Beta-crystallin A3, isoform A1, Delta4 formPRO_0000226692Add
    BLAST
    Chaini26 – 215190Beta-crystallin A3, isoform A1, Delta7 formPRO_0000226693Add
    BLAST
    Chaini27 – 215189Beta-crystallin A3, isoform A1, Delta8 formPRO_0000226694Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei82 – 821S-glutathionyl cysteine; alternate1 Publication
    Modified residuei82 – 821S-methylcysteine; alternate1 Publication
    Modified residuei117 – 1171S-glutathionyl cysteine; alternate1 Publication
    Modified residuei117 – 1171S-methylcysteine; alternate1 Publication
    Modified residuei185 – 1851S-methylcysteine1 Publication

    Post-translational modificationi

    Specific cleavages in the N-terminal arm occur during lens maturation and give rise to several truncated forms. Cleavages do not seem to have adverse effects on solubility.1 Publication
    S-methylation and glutathionylation occur in normal young lenses and do not seem to be detrimental.1 Publication
    Isoform A1 initiator methionine is removed. The new N-terminal amino acid is then N-acetylated.2 Publications

    Keywords - PTMi

    Acetylation, Glutathionylation, Methylation, Oxidation

    Proteomic databases

    PaxDbiP05813.
    PRIDEiP05813.

    PTM databases

    PhosphoSiteiP05813.

    Expressioni

    Gene expression databases

    BgeeiP05813.
    CleanExiHS_CRYBA1.
    GenevestigatoriP05813.

    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
    CRYABP025112EBI-7043337,EBI-739060

    Protein-protein interaction databases

    BioGridi107801. 3 interactions.
    IntActiP05813. 4 interactions.
    MINTiMINT-3388142.
    STRINGi9606.ENSP00000225387.

    Structurei

    3D structure databases

    ProteinModelPortaliP05813.
    SMRiP05813. Positions 27-215.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 7040Beta/gamma crystallin 'Greek key' 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini71 – 11747Beta/gamma crystallin 'Greek key' 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini124 – 16542Beta/gamma crystallin 'Greek key' 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini166 – 21449Beta/gamma crystallin 'Greek key' 4PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 3030N-terminal armAdd
    BLAST
    Regioni118 – 1236Connecting peptide

    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

    eggNOGiNOG47808.
    HOGENOMiHOG000234388.
    HOVERGENiHBG003364.
    InParanoidiP05813.
    OrthoDBiEOG7K9K40.
    PhylomeDBiP05813.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform A3 (identifier: P05813-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    METQAEQQEL ETLPTTKMAQ TNPTPGSLGP WKITIYDQEN FQGKRMEFTS    50
    SCPNVSERSF DNVRSLKVES GAWIGYEHTS FCGQQFILER GEYPRWDAWS 100
    GSNAYHIERL MSFRPICSAN HKESKMTIFE KENFIGRQWE ISDDYPSLQA 150
    MGWFNNEVGS MKIQSGAWVC YQYPGYRGYQ YILECDHHGG DYKHWREWGS 200
    HAQTSQIQSI RRIQQ 215
    Length:215
    Mass (Da):25,150
    Last modified:November 1, 1997 - v4
    Checksum:iC544564835688A19
    GO
    Isoform A1 (identifier: P05813-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-17: Missing.

    Note: Initiator Met-1 is removed. Contains a N-acetylalanine at position 2.

    Show »
    Length:198
    Mass (Da):23,191
    Checksum:i95954586F78B1B4C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti107 – 1071I → M in AAA52107. (PubMed:3745196)Curated
    Sequence conflicti116 – 1161I → F in AAA52107. (PubMed:3745196)Curated
    Sequence conflicti172 – 1743QYP → HYL in AAA52107. (PubMed:3745196)Curated
    Sequence conflicti184 – 1841E → K in AAA52107. (PubMed:3745196)Curated
    Sequence conflicti189 – 1891G → E in AAA52107. (PubMed:3745196)Curated

    Mass spectrometryi

    Molecular mass is 25192±3 Da from positions 1 - 215. Determined by ESI. 1 Publication
    Molecular mass is 25192 Da from positions 1 - 215. Determined by ESI. 1 Publication
    Molecular mass is 23101±3 Da from positions 19 - 215. Determined by ESI. 1 Publication
    Molecular mass is 23102 Da from positions 19 - 215. Determined by ESI. 1 Publication
    Molecular mass is 22646 Da from positions 23 - 215. Determined by ESI. 1 Publication
    Molecular mass is 22351 Da from positions 26 - 215. Determined by ESI. 1 Publication
    Molecular mass is 22294 Da from positions 27 - 215. Determined by ESI. 1 Publication

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1717Missing in isoform A1. CuratedVSP_018710Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14306
    , M14301, M14302, M14303, M14304, M14305 Genomic DNA. Translation: AAA52107.1.
    BC069537 mRNA. Translation: AAH69537.1.
    BC113693 mRNA. Translation: AAI13694.1.
    U59058 mRNA. Translation: AAC50971.1.
    CCDSiCCDS11249.1. [P05813-1]
    PIRiA25202. CYHUB3.
    RefSeqiNP_005199.2. NM_005208.4. [P05813-1]
    UniGeneiHs.46275.

    Genome annotation databases

    EnsembliENST00000225387; ENSP00000225387; ENSG00000108255. [P05813-1]
    GeneIDi1411.
    KEGGihsa:1411.
    UCSCiuc002hdw.3. human. [P05813-1]

    Polymorphism databases

    DMDMi2506317.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Web resourcesi

    Eye disease Crystallin, beta-A1 (CRYBA1)

    Leiden Open Variation Database (LOVD)

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14306
    , M14301 , M14302 , M14303 , M14304 , M14305 Genomic DNA. Translation: AAA52107.1 .
    BC069537 mRNA. Translation: AAH69537.1 .
    BC113693 mRNA. Translation: AAI13694.1 .
    U59058 mRNA. Translation: AAC50971.1 .
    CCDSi CCDS11249.1. [P05813-1 ]
    PIRi A25202. CYHUB3.
    RefSeqi NP_005199.2. NM_005208.4. [P05813-1 ]
    UniGenei Hs.46275.

    3D structure databases

    ProteinModelPortali P05813.
    SMRi P05813. Positions 27-215.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107801. 3 interactions.
    IntActi P05813. 4 interactions.
    MINTi MINT-3388142.
    STRINGi 9606.ENSP00000225387.

    PTM databases

    PhosphoSitei P05813.

    Polymorphism databases

    DMDMi 2506317.

    Proteomic databases

    PaxDbi P05813.
    PRIDEi P05813.

    Protocols and materials databases

    DNASUi 1411.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000225387 ; ENSP00000225387 ; ENSG00000108255 . [P05813-1 ]
    GeneIDi 1411.
    KEGGi hsa:1411.
    UCSCi uc002hdw.3. human. [P05813-1 ]

    Organism-specific databases

    CTDi 1411.
    GeneCardsi GC17P027573.
    HGNCi HGNC:2394. CRYBA1.
    MIMi 123610. gene.
    600881. phenotype.
    neXtProti NX_P05813.
    Orphaneti 98985. Cataract with Y-shaped suture opacities.
    98995. Zonular cataract.
    PharmGKBi PA26908.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG47808.
    HOGENOMi HOG000234388.
    HOVERGENi HBG003364.
    InParanoidi P05813.
    OrthoDBi EOG7K9K40.
    PhylomeDBi P05813.
    TreeFami TF331401.

    Miscellaneous databases

    GeneWikii Crystallin,_beta_A1.
    GenomeRNAii 1411.
    NextBioi 5769.
    PROi P05813.
    SOURCEi Search...

    Gene expression databases

    Bgeei P05813.
    CleanExi HS_CRYBA1.
    Genevestigatori P05813.

    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. "Characterization of the human beta-crystallin gene Hu beta A3/A1 reveals ancestral relationships among the beta gamma-crystallin superfamily."
      Hogg D., Tsui L.-C., Gorin M., Breitman M.L.
      J. Biol. Chem. 261:12420-12427(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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].
    3. "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: NUCLEOTIDE SEQUENCE [MRNA] OF 44-215, PROTEIN SEQUENCE OF 23-30 AND 197-211, ACETYLATION AT MET-1, CLEAVAGE OF INITIATOR METHIONINE (ISOFORM A1), ACETYLATION AT ALA-2 (ISOFORM A1), MASS SPECTROMETRY.
    4. "Autosomal dominant zonular cataract with sutural opacities is associated with a splice mutation in the betaA3/A1-crystallin gene."
      Kannabiran C., Rogan P.K., Olmos L., Basti S., Rao G.N., Kaiser-Kupfer M., Hejtmancik J.F.
      Mol. Vis. 4:21-21(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CTRCT10.
    5. "Characterization of the G91del CRYBA1/3-crystallin protein: a cause of human inherited cataract."
      Reddy M.A., Bateman O.A., Chakarova C., Ferris J., Berry V., Lomas E., Sarra R., Smith M.A., Moore A.T., Bhattacharya S.S., Slingsby C.
      Hum. Mol. Genet. 13:945-953(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CTRCT10.
    6. "Modifications of human betaA1/betaA3-crystallins include S-methylation, glutathiolation, and truncation."
      Lapko V.N., Cerny R.L., Smith D.L., Smith J.B.
      Protein Sci. 14:45-54(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF N-TERMINUS, ACETYLATION AT MET-1, CLEAVAGE OF INITIATOR METHIONINE (ISOFORM A1), ACETYLATION AT ALA-2 (ISOFORM A1), METHYLATION AT CYS-82; CYS-117 AND CYS-185, GLUTATHIONYLATION AT CYS-82 AND CYS-117, MASS SPECTROMETRY.

    Entry informationi

    Entry nameiCRBA1_HUMAN
    AccessioniPrimary (citable) accession number: P05813
    Secondary accession number(s): Q13633, Q14CM9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 148 of the entry and version 4 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 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3