Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P43320 (CRBB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-crystallin B2
Alternative name(s):
Beta-B2 crystallin
Beta-crystallin Bp
Gene names
Name:CRYBB2
Synonyms:CRYB2, CRYB2A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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. Ref.12

Domain

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

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.11

Sequence similarities

Belongs to the beta/gamma-crystallin family.

Contains 4 beta/gamma crystallin 'Greek key' domains.

Mass spectrometry

Molecular mass is 23291±3 Da from positions 2 - 205. Determined by ESI. Ref.7

Molecular mass is 23289 Da from positions 2 - 205. Determined by ESI. Ref.9

Molecular mass is 23290 Da from positions 2 - 205. Determined by ESI. Ref.10

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself5EBI-974082,EBI-974082

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 205204Beta-crystallin B2
PRO_0000057553

Regions

Domain17 – 5640Beta/gamma crystallin 'Greek key' 1
Domain57 – 10145Beta/gamma crystallin 'Greek key' 2
Domain107 – 14842Beta/gamma crystallin 'Greek key' 3
Domain149 – 19143Beta/gamma crystallin 'Greek key' 4
Region2 – 1615N-terminal arm
Region102 – 1065Connecting peptide
Region193 – 20513C-terminal arm

Sites

Site591Susceptible to oxidation
Site1221Susceptible to oxidation
Site1511Susceptible to oxidation

Amino acid modifications

Modified residue21N-acetylalanine Ref.6

Natural variations

Natural variant651A → S.
Corresponds to variant rs16986560 [ dbSNP | Ensembl ].
VAR_038431

Secondary structure

....................................... 205
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P43320 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: FD95C354724A67D0

FASTA20523,380
        10         20         30         40         50         60 
MASDHQTQAG KPQSLNPKII IFEQENFQGH SHELNGPCPN LKETGVEKAG SVLVQAGPWV 

        70         80         90        100        110        120 
GYEQANCKGE QFVFEKGEYP RWDSWTSSRR TDSLSSLRPI KVDSQEHKII LYENPNFTGK 

       130        140        150        160        170        180 
KMEIIDDDVP SFHAHGYQEK VSSVRVQSGT WVGYQYPGYR GLQYLLEKGD YKDSSDFGAP 

       190        200 
HPQVQSVRRI RDMQWHQRGA FHPSN 

« Hide

References

« Hide 'large scale' references
[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]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Web resources

Eye disease Crystallin, beta-B2 (CRYBB2)

Leiden Open Variation Database (LOVD)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L10035 mRNA. Translation: AAA16864.1.
U72404 expand/collapse EMBL AC list , 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.
CCDSCCDS13831.1.
PIRJC2009.
RefSeqNP_000487.1. NM_000496.2.
XP_006724204.1. XM_006724141.1.
UniGeneHs.373074.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YTQX-ray1.70A2-205[»]
ProteinModelPortalP43320.
SMRP43320. Positions 15-195.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107805. 6 interactions.
IntActP43320. 6 interactions.
MINTMINT-221083.
STRING9606.ENSP00000215861.

PTM databases

PhosphoSiteP43320.

Polymorphism databases

DMDM1169091.

Proteomic databases

PaxDbP43320.
PeptideAtlasP43320.
PRIDEP43320.

Protocols and materials databases

DNASU1415.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000398215; ENSP00000381273; ENSG00000244752.
GeneID1415.
KEGGhsa:1415.
UCSCuc003abp.1. human.

Organism-specific databases

CTD1415.
GeneCardsGC22P025615.
HGNCHGNC:2398. CRYBB2.
HPAHPA043749.
MIM123620. gene.
601547. phenotype.
neXtProtNX_P43320.
Orphanet98985. Cataract with Y-shaped suture opacities.
1377. Cataract-microcornea syndrome.
98989. Cerulean cataract.
98986. Coppock-like cataract.
98991. Nuclear cataract.
98994. Total congenital cataract.
PharmGKBPA26912.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41590.
HOGENOMHOG000234388.
HOVERGENHBG003364.
InParanoidP43320.
OMAGFQYLFE.
OrthoDBEOG754HNK.
PhylomeDBP43320.
TreeFamTF331401.

Gene expression databases

BgeeP43320.
CleanExHS_CRYBB2.
GenevestigatorP43320.

Family and domain databases

InterProIPR001064. Beta/gamma_crystallin.
IPR011024. G_crystallin-rel.
[Graphical view]
PfamPF00030. Crystall. 2 hits.
[Graphical view]
PRINTSPR01367. BGCRYSTALLIN.
SMARTSM00247. XTALbg. 2 hits.
[Graphical view]
SUPFAMSSF49695. SSF49695. 1 hit.
PROSITEPS50915. CRYSTALLIN_BETA_GAMMA. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCRYBB2. human.
EvolutionaryTraceP43320.
GeneWikiCRYBB2.
GenomeRNAi1415.
NextBio5789.
PROP43320.
SOURCESearch...

Entry information

Entry nameCRBB2_HUMAN
AccessionPrimary (citable) accession number: P43320
Secondary accession number(s): Q9UCM8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM