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P53674

- CRBB1_HUMAN

UniProt

P53674 - CRBB1_HUMAN

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Protein

Beta-crystallin B1

Gene

CRYBB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

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

GO - Biological processi

  1. visual perception Source: ProtInc
Complete GO annotation...

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

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 – 667Combined sources
Turni67 – 693Combined sources
Beta strandi70 – 789Combined sources
Turni83 – 875Combined sources
Beta strandi93 – 986Combined sources
Beta strandi101 – 1066Combined sources
Helixi107 – 1093Combined sources
Beta strandi110 – 1167Combined sources
Beta strandi118 – 1214Combined sources
Helixi124 – 1274Combined sources
Beta strandi138 – 1414Combined sources
Beta strandi150 – 1567Combined sources
Helixi157 – 1593Combined sources
Beta strandi160 – 16910Combined sources
Helixi174 – 1774Combined sources
Beta strandi185 – 19814Combined sources
Turni199 – 2013Combined sources
Beta strandi202 – 2087Combined sources
Beta strandi210 – 2156Combined sources
Helixi216 – 2194Combined sources
Beta strandi228 – 2325Combined sources

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.
GeneTreeiENSGT00760000118812.
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

        10         20         30         40         50
MSQAAKASAS ATVAVNPGPD TKGKGAPPAG TSPSPGTTLA PTTVPITSAK
60 70 80 90 100
AAELPPGNYR LVVFELENFQ GRRAEFSGEC SNLADRGFDR VRSIIVSAGP
110 120 130 140 150
WVAFEQSNFR GEMFILEKGE YPRWNTWSSS YRSDRLMSFR PIKMDAQEHK
160 170 180 190 200
ISLFEGANFK GNTIEIQGDD APSLWVYGFS DRVGSVKVSS GTWVGYQYPG
210 220 230 240 250
YRGYQYLLEP GDFRHWNEWG AFQPQMQSLR RLRDKQWHLE GSFPVLATEP

PK
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.
GeneTreei ENSGT00760000118812.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 144 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