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P53674 (CRBB1_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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-crystallin B1
Alternative name(s):
Beta-B1 crystallin
Gene names
Name:CRYBB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length252 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.

Domain

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

Post-translational modification

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

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6 Ref.10 Ref.12

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 (Ref.8 and Ref.11). Ref.8 Ref.11

Sequence similarities

Belongs to the beta/gamma-crystallin family.

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

Mass spectrometry

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

Ontologies

Keywords
   DiseaseCataract
Disease mutation
   DomainRepeat
   Molecular functionEye lens protein
   PTMAcetylation
Oxidation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processvisual perception

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionstructural constituent of eye lens

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 252251Beta-crystallin B1
PRO_0000057550

Regions

Domain59 – 9840Beta/gamma crystallin 'Greek key' 1
Domain99 – 14345Beta/gamma crystallin 'Greek key' 2
Domain149 – 19042Beta/gamma crystallin 'Greek key' 3
Domain191 – 23343Beta/gamma crystallin 'Greek key' 4
Region2 – 5857N-terminal arm
Region144 – 1485Connecting peptide
Region235 – 25218C-terminal arm

Sites

Site2161Susceptible to oxidation
Site2261Susceptible to oxidation

Amino acid modifications

Modified residue21N-acetylserine Ref.1

Natural variations

Natural variant961V → F in CTRCT17. Ref.12
VAR_070030
Natural variant1291S → 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. Ref.11
VAR_065296

Secondary structure

.................................. 252
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P53674 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 93D81A9C95A86F7F

FASTA25228,023
        10         20         30         40         50         60 
MSQAAKASAS ATVAVNPGPD TKGKGAPPAG TSPSPGTTLA PTTVPITSAK AAELPPGNYR 

        70         80         90        100        110        120 
LVVFELENFQ GRRAEFSGEC SNLADRGFDR VRSIIVSAGP WVAFEQSNFR GEMFILEKGE 

       130        140        150        160        170        180 
YPRWNTWSSS YRSDRLMSFR PIKMDAQEHK ISLFEGANFK GNTIEIQGDD APSLWVYGFS 

       190        200        210        220        230        240 
DRVGSVKVSS GTWVGYQYPG YRGYQYLLEP GDFRHWNEWG AFQPQMQSLR RLRDKQWHLE 

       250 
GSFPVLATEP PK 

« Hide

References

« Hide 'large scale' references
[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]"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].
[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. 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].
[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.
+Additional computationally mapped references.

Web resources

Eye disease Crystallin, beta-B1 (CRYBB1)

Leiden Open Variation Database (LOVD)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS13840.1.
PIRS55441.
RefSeqNP_001878.1. NM_001887.3.
UniGeneHs.37135.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OKIX-ray1.40A/B43-252[»]
ProteinModelPortalP53674.
SMRP53674. Positions 55-237.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107804. 2 interactions.
IntActP53674. 3 interactions.
MINTMINT-5161833.
STRING9606.ENSP00000215939.

PTM databases

PhosphoSiteP53674.

Polymorphism databases

DMDM1706116.

Proteomic databases

PaxDbP53674.
PeptideAtlasP53674.
PRIDEP53674.

Protocols and materials databases

DNASU1414.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000215939; ENSP00000215939; ENSG00000100122.
GeneID1414.
KEGGhsa:1414.
UCSCuc003acy.1. human.

Organism-specific databases

CTD1414.
GeneCardsGC22M026995.
HGNCHGNC:2397. CRYBB1.
MIM600929. gene.
611544. phenotype.
neXtProtNX_P53674.
Orphanet1377. Cataract-microcornea syndrome.
98991. Nuclear cataract.
98984. Pulverulent cataract.
PharmGKBPA26911.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40509.
HOGENOMHOG000234388.
HOVERGENHBG003364.
InParanoidP53674.
OMASCCHNIS.
OrthoDBEOG754HNK.
PhylomeDBP53674.
TreeFamTF331401.

Gene expression databases

BgeeP53674.
CleanExHS_CRYBB1.
GenevestigatorP53674.

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

EvolutionaryTraceP53674.
GeneWikiCRYBB1.
GenomeRNAi1414.
NextBio5785.
PMAP-CutDBP53674.
PROP53674.
SOURCESearch...

Entry information

Entry nameCRBB1_HUMAN
AccessionPrimary (citable) accession number: P53674
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
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