LOCUS       NM_000496                769 bp    mRNA    linear   PRI 01-AUG-2024
DEFINITION  Homo sapiens crystallin beta B2 (CRYBB2), mRNA.
ACCESSION   NM_000496
VERSION     NM_000496.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (bases 1 to 769)
  AUTHORS   Sun,J., Morishima,K., Inoue,R., Sugiyama,M. and Takata,T.
  TITLE     Characterization of betaB2-crystallin tryptophan mutants reveals
            two different folding states in solution
  JOURNAL   Protein Sci 33 (7), e5092 (2024)
   PUBMED   38924206
  REMARK    GeneRIF: Characterization of betaB2-crystallin tryptophan mutants
            reveals two different folding states in solution.
REFERENCE   2  (bases 1 to 769)
  AUTHORS   Tovar-Ramirez,M.E., Schuth,N., Rodriguez-Meza,O., Kroll,T.,
            Saab-Rincon,G., Costas,M., Lampi,K. and Quintanar,L.
  TITLE     ATCUN-like Copper Site in betaB2-Crystallin Plays a Protective Role
            in Cataract-Associated Aggregation
  JOURNAL   Inorg Chem 62 (27), 10592-10604 (2023)
   PUBMED   37379524
  REMARK    GeneRIF: ATCUN-like Copper Site in betaB2-Crystallin Plays a
            Protective Role in Cataract-Associated Aggregation.
REFERENCE   3  (bases 1 to 769)
  AUTHORS   Wu,J., Chen,S., Xu,J., Xu,W., Zheng,S., Tian,Q., Luo,C., Chen,X.
            and Shentu,X.
  TITLE     Insight into Pathogenic Mechanism Underlying the Hereditary
            Cataract Caused by betaB2-G149V Mutation
  JOURNAL   Biomolecules 13 (5), 864 (2023)
   PUBMED   37238733
  REMARK    GeneRIF: Insight into Pathogenic Mechanism Underlying the
            Hereditary Cataract Caused by betaB2-G149V Mutation.
            Publication Status: Online-Only
REFERENCE   4  (bases 1 to 769)
  AUTHORS   Velasco-Bolom,J.L. and Dominguez,L.
  TITLE     Conformational stability of the deamidated and mutated human
            betaB2-crystallin
  JOURNAL   Biophys Chem 296, 106986 (2023)
   PUBMED   36905841
  REMARK    GeneRIF: Conformational stability of the deamidated and mutated
            human betaB2-crystallin.
REFERENCE   5  (bases 1 to 769)
  AUTHORS   Yan,Y., Narayan,A., Cho,S., Cheng,Z., Liu,J.O., Zhu,H., Wang,G.,
            Wharram,B., Lisok,A., Brummet,M., Saeki,H., Huang,T.,
            Gabrielson,K., Gabrielson,E., Cope,L., Kanaan,Y.M., Afsari,A.,
            Naab,T., Yfantis,H.G., Ambs,S., Pomper,M.G., Sukumar,S. and
            Merino,V.F.
  TITLE     CRYbetaB2 enhances tumorigenesis through upregulation of nucleolin
            in triple negative breast cancer
  JOURNAL   Oncogene 40 (38), 5752-5763 (2021)
   PUBMED   34341513
  REMARK    GeneRIF: CRYbetaB2 enhances tumorigenesis through upregulation of
            nucleolin in triple negative breast cancer.
REFERENCE   6  (bases 1 to 769)
  AUTHORS   Miesbauer,L.R., Zhou,X., Yang,Z., Yang,Z., Sun,Y., Smith,D.L. and
            Smith,J.B.
  TITLE     Post-translational modifications of water-soluble human lens
            crystallins from young adults
  JOURNAL   J Biol Chem 269 (17), 12494-12502 (1994)
   PUBMED   8175657
REFERENCE   7  (bases 1 to 769)
  AUTHORS   Chambers,C. and Russell,P.
  TITLE     Sequence of the human lens beta B2-crystallin-encoding cDNA
  JOURNAL   Gene 133 (2), 295-299 (1993)
   PUBMED   8224918
REFERENCE   8  (bases 1 to 769)
  AUTHORS   Datiles,M.B., Schumer,D.J., Zigler,J.S. Jr., Russell,P.,
            Anderson,L. and Garland,D.
  TITLE     Two-dimensional gel electrophoretic analysis of human lens proteins
  JOURNAL   Curr Eye Res 11 (7), 669-677 (1992)
   PUBMED   1521468
REFERENCE   9  (bases 1 to 769)
  AUTHORS   Hulsebos,T.J., Bijlsma,E.K., Geurts van Kessel,A.H.,
            Brakenhoff,R.H. and Westerveld,A.
  TITLE     Direct assignment of the human beta B2 and beta B3 crystallin genes
            to 22q11.2----q12: markers for neurofibromatosis 2
  JOURNAL   Cytogenet Cell Genet 56 (3-4), 171-175 (1991)
   PUBMED   2055112
REFERENCE   10 (bases 1 to 769)
  AUTHORS   Aarts,H.J., Den Dunnen,J.T., Lubsen,N.H. and Schoenmakers,J.G.
  TITLE     Linkage between the beta B2 and beta B3 crystallin genes in man and
            rat: a remnant of an ancient beta-crystallin gene cluster
  JOURNAL   Gene 59 (1), 127-135 (1987)
   PUBMED   3436525
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z99916.1, BF847403.1,
            BC069535.1 and BM667912.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 23, 2018 this sequence version replaced NM_000496.2.
            
            Summary: Crystallins are separated into two classes:
            taxon-specific, or enzyme, and ubiquitous. The latter class
            constitutes the major proteins of vertebrate eye lens and maintains
            the transparency and refractive index of the lens. Since lens
            central fiber cells lose their nuclei during development, these
            crystallins are made and then retained throughout life, making them
            extremely stable proteins. Mammalian lens crystallins are divided
            into alpha, beta, and gamma families; beta and gamma crystallins
            are also considered as a superfamily. Alpha and beta families are
            further divided into acidic and basic groups. Seven protein regions
            exist in crystallins: four homologous motifs, a connecting peptide,
            and N- and C-terminal extensions. Beta-crystallins, the most
            heterogeneous, differ by the presence of the C-terminal extension
            (present in the basic group, none in the acidic group).
            Beta-crystallins form aggregates of different sizes and are able to
            self-associate to form dimers or to form heterodimers with other
            beta-crystallins. This gene, a beta basic group member, is part of
            a gene cluster with beta-A4, beta-B1, and beta-B3. A
            chain-terminating mutation was found to cause type 2 cerulean
            cataracts. [provided by RefSeq, Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BY794982.2, KR052784.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968968, SAMEA2148874
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000398215.3/ ENSP00000381273.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
            COMPLETENESS: full length.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-6                 Z99916.1           65790-65795
            7-42                BF847403.1         178-213             c
            43-722              BC069535.1         1-680
            723-769             BM667912.1         19-65               c
FEATURES             Location/Qualifiers
     source          1..769
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q11.23"
     gene            1..769
                     /gene="CRYBB2"
                     /gene_synonym="CCA2; CRYB2; CRYB2A; CTRCT3; D22S665"
                     /note="crystallin beta B2"
                     /db_xref="GeneID:1415"
                     /db_xref="HGNC:HGNC:2398"
                     /db_xref="MIM:123620"
     exon            1..28
                     /gene="CRYBB2"
                     /gene_synonym="CCA2; CRYB2; CRYB2A; CTRCT3; D22S665"
                     /inference="alignment:Splign:2.1.0"
     exon            29..108
                     /gene="CRYBB2"
                     /gene_synonym="CCA2; CRYB2; CRYB2A; CTRCT3; D22S665"
                     /inference="alignment:Splign:2.1.0"
     CDS             55..672
                     /gene="CRYBB2"
                     /gene_synonym="CCA2; CRYB2; CRYB2A; CTRCT3; D22S665"
                     /note="eye lens structural protein; beta-B2 crystallin;
                     beta-crystallin Bp; CTA-221G9.7"
                     /codon_start=1
                     /product="beta-crystallin B2"
                     /protein_id="NP_000487.1"
                     /db_xref="CCDS:CCDS13831.1"
                     /db_xref="GeneID:1415"
                     /db_xref="HGNC:HGNC:2398"
                     /db_xref="MIM:123620"
                     /translation="MASDHQTQAGKPQSLNPKIIIFEQENFQGHSHELNGPCPNLKET
                     GVEKAGSVLVQAGPWVGYEQANCKGEQFVFEKGEYPRWDSWTSSRRTDSLSSLRPIKV
                     DSQEHKIILYENPNFTGKKMEIIDDDVPSFHAHGYQEKVSSVRVQSGTWVGYQYPGYR
                     GLQYLLEKGDYKDSSDFGAPHPQVQSVRRIRDMQWHQRGAFHPSN"
     exon            109..227
                     /gene="CRYBB2"
                     /gene_synonym="CCA2; CRYB2; CRYB2A; CTRCT3; D22S665"
                     /inference="alignment:Splign:2.1.0"
     exon            228..360
                     /gene="CRYBB2"
                     /gene_synonym="CCA2; CRYB2; CRYB2A; CTRCT3; D22S665"
                     /inference="alignment:Splign:2.1.0"
     exon            361..503
                     /gene="CRYBB2"
                     /gene_synonym="CCA2; CRYB2; CRYB2A; CTRCT3; D22S665"
                     /inference="alignment:Splign:2.1.0"
     exon            504..769
                     /gene="CRYBB2"
                     /gene_synonym="CCA2; CRYB2; CRYB2A; CTRCT3; D22S665"
                     /inference="alignment:Splign:2.1.0"
     regulatory      747..752
                     /regulatory_class="polyA_signal_sequence"
                     /gene="CRYBB2"
                     /gene_synonym="CCA2; CRYB2; CRYB2A; CTRCT3; D22S665"
                     /note="hexamer: AATAAA"
     polyA_site      769
                     /gene="CRYBB2"
                     /gene_synonym="CCA2; CRYB2; CRYB2A; CTRCT3; D22S665"
                     /note="major polyA site"
ORIGIN      
        1 acggcactcg caggggctgg tgtcactggt cattcctgca caggacagtc caccatggcc
       61 tcagatcacc agacccaggc gggcaagcca cagtccctca accccaagat catcatcttt
      121 gagcaggaaa actttcaagg ccactcgcat gagctcaatg ggccctgccc caacctgaag
      181 gaaactggcg tggagaaggc aggttctgtc ctagtgcagg ctggaccctg ggtgggctat
      241 gaacaggcca actgcaaggg cgagcagttt gtgtttgaga agggtgagta cccccgctgg
      301 gactcatgga ccagcagccg aaggacggac tccctcagct ccctgaggcc catcaaagtg
      361 gacagccaag agcacaagat catcctctat gaaaacccca acttcaccgg gaagaagatg
      421 gaaatcatag atgacgatgt acccagcttc cacgcccatg gctaccagga gaaggtgtca
      481 tctgtgcggg tgcagagtgg cacgtgggtt ggctaccagt accccggcta ccgtgggctg
      541 cagtacctgc tggagaaggg agactacaag gacagcagcg actttggggc ccctcacccc
      601 caggtgcagt ccgtgcgccg tatccgcgac atgcagtggc accaacgtgg tgccttccac
      661 ccctccaact agtgccctcc ccaccatgcc tccttcccag gacccaggtc tgctgcccag
      721 gaaccctcca gacctcccag agagtgaata aagtgtgact tgcaacttg
//
