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P43320

- CRBB2_HUMAN

UniProt

P43320 - CRBB2_HUMAN

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Protein

Beta-crystallin B2

Gene

CRYBB2

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. identical protein binding Source: IntAct
  2. structural constituent of eye lens Source: UniProtKB-KW
  3. structural molecule activity Source: ProtInc

GO - Biological processi

  1. camera-type eye development Source: Ensembl
  2. response to stimulus Source: UniProtKB-KW
  3. visual perception Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Eye lens protein

Keywords - Biological processi

Sensory transduction, Vision

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-crystallin B2
Alternative name(s):
Beta-B2 crystallin
Beta-crystallin Bp
Gene namesi
Name:CRYBB2
Synonyms:CRYB2, CRYB2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:2398. CRYBB2.

Pathology & Biotechi

Involvement in diseasei

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

Keywords - Diseasei

Cataract

Organism-specific databases

MIMi601547. phenotype.
Orphaneti98985. Cataract with Y-shaped suture opacities.
1377. Cataract-microcornea syndrome.
98989. Cerulean cataract.
98986. Coppock-like cataract.
98991. Nuclear cataract.
98994. Total congenital cataract.
PharmGKBiPA26912.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 205204Beta-crystallin B2PRO_0000057553Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP43320.
PeptideAtlasiP43320.
PRIDEiP43320.

PTM databases

PhosphoSiteiP43320.

Expressioni

Gene expression databases

BgeeiP43320.
CleanExiHS_CRYBB2.
ExpressionAtlasiP43320. baseline.
GenevestigatoriP43320.

Organism-specific databases

HPAiHPA043749.

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
itself5EBI-974082,EBI-974082

Protein-protein interaction databases

BioGridi107805. 6 interactions.
IntActiP43320. 6 interactions.
MINTiMINT-221083.
STRINGi9606.ENSP00000215861.

Structurei

Secondary structure

1
205
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 247Combined sources
Beta strandi31 – 366Combined sources
Helixi41 – 444Combined sources
Beta strandi50 – 567Combined sources
Beta strandi59 – 646Combined sources
Turni65 – 673Combined sources
Beta strandi68 – 747Combined sources
Beta strandi76 – 794Combined sources
Helixi82 – 843Combined sources
Beta strandi96 – 994Combined sources
Beta strandi108 – 1147Combined sources
Turni115 – 1173Combined sources
Beta strandi118 – 12710Combined sources
Helixi133 – 1353Combined sources
Beta strandi143 – 1464Combined sources
Beta strandi151 – 1566Combined sources
Turni157 – 1593Combined sources
Beta strandi160 – 1667Combined sources
Beta strandi168 – 1714Combined sources
Helixi174 – 1774Combined sources
Beta strandi180 – 1823Combined sources
Beta strandi186 – 1894Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YTQX-ray1.70A2-205[»]
ProteinModelPortaliP43320.
SMRiP43320. Positions 15-195.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43320.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 5640Beta/gamma crystallin 'Greek key' 1PROSITE-ProRule annotationAdd
BLAST
Domaini57 – 10145Beta/gamma crystallin 'Greek key' 2PROSITE-ProRule annotationAdd
BLAST
Domaini107 – 14842Beta/gamma crystallin 'Greek key' 3PROSITE-ProRule annotationAdd
BLAST
Domaini149 – 19143Beta/gamma crystallin 'Greek key' 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 1615N-terminal armAdd
BLAST
Regioni102 – 1065Connecting peptide
Regioni193 – 20513C-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

eggNOGiNOG41590.
HOGENOMiHOG000234388.
HOVERGENiHBG003364.
InParanoidiP43320.
OMAiGFQYLFE.
OrthoDBiEOG754HNK.
PhylomeDBiP43320.
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.

P43320-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASDHQTQAG KPQSLNPKII IFEQENFQGH SHELNGPCPN LKETGVEKAG
60 70 80 90 100
SVLVQAGPWV GYEQANCKGE QFVFEKGEYP RWDSWTSSRR TDSLSSLRPI
110 120 130 140 150
KVDSQEHKII LYENPNFTGK KMEIIDDDVP SFHAHGYQEK VSSVRVQSGT
160 170 180 190 200
WVGYQYPGYR GLQYLLEKGD YKDSSDFGAP HPQVQSVRRI RDMQWHQRGA

FHPSN
Length:205
Mass (Da):23,380
Last modified:January 23, 2007 - v2
Checksum:iFD95C354724A67D0
GO

Mass spectrometryi

Molecular mass is 23291±3 Da from positions 2 - 205. Determined by ESI. 1 Publication
Molecular mass is 23289 Da from positions 2 - 205. Determined by ESI. 1 Publication
Molecular mass is 23290 Da from positions 2 - 205. Determined by ESI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti65 – 651A → S.
Corresponds to variant rs16986560 [ dbSNP | Ensembl ].
VAR_038431

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10035 mRNA. Translation: AAA16864.1.
U72404
, 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.
CCDSiCCDS13831.1.
PIRiJC2009.
RefSeqiNP_000487.1. NM_000496.2.
XP_006724204.1. XM_006724141.1.
UniGeneiHs.373074.

Genome annotation databases

EnsembliENST00000398215; ENSP00000381273; ENSG00000244752.
GeneIDi1415.
KEGGihsa:1415.
UCSCiuc003abp.1. human.

Polymorphism databases

DMDMi1169091.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Eye disease Crystallin, beta-B2 (CRYBB2)

Leiden Open Variation Database (LOVD)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10035 mRNA. Translation: AAA16864.1 .
U72404
, 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 .
CCDSi CCDS13831.1.
PIRi JC2009.
RefSeqi NP_000487.1. NM_000496.2.
XP_006724204.1. XM_006724141.1.
UniGenei Hs.373074.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YTQ X-ray 1.70 A 2-205 [» ]
ProteinModelPortali P43320.
SMRi P43320. Positions 15-195.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107805. 6 interactions.
IntActi P43320. 6 interactions.
MINTi MINT-221083.
STRINGi 9606.ENSP00000215861.

PTM databases

PhosphoSitei P43320.

Polymorphism databases

DMDMi 1169091.

Proteomic databases

PaxDbi P43320.
PeptideAtlasi P43320.
PRIDEi P43320.

Protocols and materials databases

DNASUi 1415.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000398215 ; ENSP00000381273 ; ENSG00000244752 .
GeneIDi 1415.
KEGGi hsa:1415.
UCSCi uc003abp.1. human.

Organism-specific databases

CTDi 1415.
GeneCardsi GC22P025615.
HGNCi HGNC:2398. CRYBB2.
HPAi HPA043749.
MIMi 123620. gene.
601547. phenotype.
neXtProti NX_P43320.
Orphaneti 98985. Cataract with Y-shaped suture opacities.
1377. Cataract-microcornea syndrome.
98989. Cerulean cataract.
98986. Coppock-like cataract.
98991. Nuclear cataract.
98994. Total congenital cataract.
PharmGKBi PA26912.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG41590.
HOGENOMi HOG000234388.
HOVERGENi HBG003364.
InParanoidi P43320.
OMAi GFQYLFE.
OrthoDBi EOG754HNK.
PhylomeDBi P43320.
TreeFami TF331401.

Miscellaneous databases

ChiTaRSi CRYBB2. human.
EvolutionaryTracei P43320.
GeneWikii CRYBB2.
GenomeRNAii 1415.
NextBioi 5789.
PROi P43320.
SOURCEi Search...

Gene expression databases

Bgeei P43320.
CleanExi HS_CRYBB2.
ExpressionAtlasi P43320. baseline.
Genevestigatori P43320.

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. "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. 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.
    , 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.

Entry informationi

Entry nameiCRBB2_HUMAN
AccessioniPrimary (citable) accession number: P43320
Secondary accession number(s): Q9UCM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 145 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