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Protein

Beta-crystallin B3

Gene

CRYBB3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

GO - Biological processi

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

Keywords - Molecular functioni

Eye lens protein

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-crystallin B3
Alternative name(s):
Beta-B3 crystallin
Cleaved into the following chain:
Gene namesi
Name:CRYBB3
Synonyms:CRYB3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:2400. CRYBB3.

Pathology & Biotechi

Involvement in diseasei

Cataract 22, multiple types (CTRCT22)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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. CTRCT22 includes nuclear cataract among others. Nuclear cataracts affect the central nucleus of the eye, and 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.
See also OMIM:609741
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti165 – 1651G → R in CTRCT22. 1 Publication
Corresponds to variant rs74315490 [ dbSNP | Ensembl ].
VAR_025280
Natural varianti194 – 1941V → E in CTRCT22. 1 Publication
Corresponds to variant rs587777601 [ dbSNP | Ensembl ].
VAR_070031

Keywords - Diseasei

Cataract, Disease mutation

Organism-specific databases

MalaCardsiCRYBB3.
MIMi609741. phenotype.
Orphaneti98988. Anterior polar cataract.
98991. Nuclear cataract.
PharmGKBiPA26914.

Polymorphism and mutation databases

DMDMi311033476.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 211211Beta-crystallin B3PRO_0000057560Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 211210Beta-crystallin B3, N-terminally processedPRO_0000421774Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei2 – 21N-acetylalanine; in Beta-crystallin B3, N-terminally processedBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP26998.
PeptideAtlasiP26998.
PRIDEiP26998.

PTM databases

iPTMnetiP26998.
PhosphoSiteiP26998.

Expressioni

Gene expression databases

BgeeiP26998.
CleanExiHS_CRYBB3.
ExpressionAtlasiP26998. baseline and differential.
GenevisibleiP26998. HS.

Organism-specific databases

HPAiHPA045293.

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
CRYBA1P058133EBI-1965681,EBI-7043337

Protein-protein interaction databases

BioGridi107807. 4 interactions.
IntActiP26998. 3 interactions.
MINTiMINT-5161878.
STRINGi9606.ENSP00000215855.

Structurei

Secondary structure

1
211
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 317Combined sources
Helixi32 – 343Combined sources
Beta strandi38 – 436Combined sources
Beta strandi58 – 636Combined sources
Beta strandi66 – 716Combined sources
Helixi72 – 743Combined sources
Beta strandi76 – 816Combined sources
Beta strandi83 – 864Combined sources
Helixi89 – 924Combined sources
Beta strandi94 – 974Combined sources
Beta strandi103 – 1064Combined sources
Beta strandi115 – 1217Combined sources
Turni122 – 1243Combined sources
Beta strandi125 – 1339Combined sources
Helixi139 – 1424Combined sources
Beta strandi150 – 1567Combined sources
Beta strandi158 – 1636Combined sources
Turni164 – 1663Combined sources
Beta strandi167 – 1737Combined sources
Beta strandi175 – 1806Combined sources
Helixi181 – 1844Combined sources
Beta strandi193 – 1964Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QK3X-ray1.95A/B/C21-199[»]
ProteinModelPortaliP26998.
SMRiP26998. Positions 23-198.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 6340Beta/gamma crystallin 'Greek key' 1PROSITE-ProRule annotationAdd
BLAST
Domaini64 – 10845Beta/gamma crystallin 'Greek key' 2PROSITE-ProRule annotationAdd
BLAST
Domaini114 – 15542Beta/gamma crystallin 'Greek key' 3PROSITE-ProRule annotationAdd
BLAST
Domaini156 – 19843Beta/gamma crystallin 'Greek key' 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 2323N-terminal armAdd
BLAST
Regioni109 – 1135Connecting peptide
Regioni200 – 21112C-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

eggNOGiENOG410IJYD. Eukaryota.
ENOG410Y7P1. LUCA.
GeneTreeiENSGT00760000118812.
HOGENOMiHOG000234388.
HOVERGENiHBG003364.
InParanoidiP26998.
OMAiFGGRKME.
OrthoDBiEOG754HNK.
PhylomeDBiP26998.
TreeFamiTF331401.

Family and domain databases

InterProiIPR001064. Beta/gamma_crystallin.
IPR033115. CRYBB3.
IPR011024. G_crystallin-rel.
[Graphical view]
PANTHERiPTHR11818:SF13. PTHR11818:SF13. 1 hit.
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.

P26998-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEQHGAPEQ AAAGKSHGDL GGSYKVILYE LENFQGKRCE LSAECPSLTD
60 70 80 90 100
SLLEKVGSIQ VESGPWLAFE SRAFRGEQFV LEKGDYPRWD AWSNSRDSDS
110 120 130 140 150
LLSLRPLNID SPHHKLHLFE NPAFSGRKME IVDDDVPSLW AHGFQDRVAS
160 170 180 190 200
VRAINGTWVG YEFPGYRGRQ YVFERGEYRH WNEWDASQPQ LQSVRRIRDQ
210
KWHKRGRFPS S
Length:211
Mass (Da):24,252
Last modified:November 2, 2010 - v4
Checksum:iE5ABA1165C7B45BA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti130 – 1301E → D in CAA33242 (PubMed:2499686).Curated
Sequence conflicti173 – 1731F → L in CAA33242 (PubMed:2499686).Curated

Mass spectrometryi

Molecular mass is 24222±3 Da from positions 1 - 211. Determined by ESI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti105 – 1051R → Q.1 Publication
Corresponds to variant rs17670506 [ dbSNP | Ensembl ].
VAR_025277
Natural varianti113 – 1131H → D.3 Publications
Corresponds to variant rs9608378 [ dbSNP | Ensembl ].
VAR_025278
Natural varianti159 – 1591V → I.
Corresponds to variant rs4455261 [ dbSNP | Ensembl ].
VAR_025279
Natural varianti165 – 1651G → R in CTRCT22. 1 Publication
Corresponds to variant rs74315490 [ dbSNP | Ensembl ].
VAR_025280
Natural varianti194 – 1941V → E in CTRCT22. 1 Publication
Corresponds to variant rs587777601 [ dbSNP | Ensembl ].
VAR_070031

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR456427 mRNA. Translation: CAG30313.1.
Z99916 Genomic DNA. Translation: CAB17042.1.
BC069479 mRNA. Translation: AAH69479.2.
BC102021 mRNA. Translation: AAI02022.1.
BC102022 mRNA. Translation: AAI02023.1.
BC107482 mRNA. Translation: AAI07483.1.
U71216 mRNA. Translation: AAC50972.1.
X15144, X15145, X15146 Genomic DNA. Translation: CAA33242.2.
CCDSiCCDS13830.1.
PIRiS10089.
RefSeqiNP_004067.1. NM_004076.4.
UniGeneiHs.533022.

Genome annotation databases

EnsembliENST00000215855; ENSP00000215855; ENSG00000100053.
GeneIDi1417.
KEGGihsa:1417.
UCSCiuc003abo.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR456427 mRNA. Translation: CAG30313.1.
Z99916 Genomic DNA. Translation: CAB17042.1.
BC069479 mRNA. Translation: AAH69479.2.
BC102021 mRNA. Translation: AAI02022.1.
BC102022 mRNA. Translation: AAI02023.1.
BC107482 mRNA. Translation: AAI07483.1.
U71216 mRNA. Translation: AAC50972.1.
X15144, X15145, X15146 Genomic DNA. Translation: CAA33242.2.
CCDSiCCDS13830.1.
PIRiS10089.
RefSeqiNP_004067.1. NM_004076.4.
UniGeneiHs.533022.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QK3X-ray1.95A/B/C21-199[»]
ProteinModelPortaliP26998.
SMRiP26998. Positions 23-198.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107807. 4 interactions.
IntActiP26998. 3 interactions.
MINTiMINT-5161878.
STRINGi9606.ENSP00000215855.

PTM databases

iPTMnetiP26998.
PhosphoSiteiP26998.

Polymorphism and mutation databases

DMDMi311033476.

Proteomic databases

PaxDbiP26998.
PeptideAtlasiP26998.
PRIDEiP26998.

Protocols and materials databases

DNASUi1417.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000215855; ENSP00000215855; ENSG00000100053.
GeneIDi1417.
KEGGihsa:1417.
UCSCiuc003abo.3. human.

Organism-specific databases

CTDi1417.
GeneCardsiCRYBB3.
H-InvDBHIX0041179.
HGNCiHGNC:2400. CRYBB3.
HPAiHPA045293.
MalaCardsiCRYBB3.
MIMi123630. gene.
609741. phenotype.
neXtProtiNX_P26998.
Orphaneti98988. Anterior polar cataract.
98991. Nuclear cataract.
PharmGKBiPA26914.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJYD. Eukaryota.
ENOG410Y7P1. LUCA.
GeneTreeiENSGT00760000118812.
HOGENOMiHOG000234388.
HOVERGENiHBG003364.
InParanoidiP26998.
OMAiFGGRKME.
OrthoDBiEOG754HNK.
PhylomeDBiP26998.
TreeFamiTF331401.

Miscellaneous databases

GeneWikiiCRYBB3.
GenomeRNAii1417.
PROiP26998.
SOURCEiSearch...

Gene expression databases

BgeeiP26998.
CleanExiHS_CRYBB3.
ExpressionAtlasiP26998. baseline and differential.
GenevisibleiP26998. HS.

Family and domain databases

InterProiIPR001064. Beta/gamma_crystallin.
IPR033115. CRYBB3.
IPR011024. G_crystallin-rel.
[Graphical view]
PANTHERiPTHR11818:SF13. PTHR11818:SF13. 1 hit.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASP-113.
  2. "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].
  3. "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], VARIANTS GLN-105 AND ASP-113.
  4. "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: NUCLEOTIDE SEQUENCE [MRNA] OF 1-103, ACETYLATION AT MET-1, MASS SPECTROMETRY.
  5. "Different evolution rates within the lens-specific beta-crystallin gene family."
    Aarts H.J.M., Jacobs E.H.M., van Willigen G., Lubsen N.H., Schoenmakers J.G.G.
    J. Mol. Evol. 28:313-321(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 66-211, VARIANT ASP-113.
    Tissue: Lens.
  6. "Mutations in betaB3-crystallin associated with autosomal recessive cataract in two Pakistani families."
    Riazuddin S.A., Yasmeen A., Yao W., Sergeev Y.V., Zhang Q., Zulfiqar F., Riaz A., Riazuddin S., Hejtmancik J.F.
    Invest. Ophthalmol. Vis. Sci. 46:2100-2106(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CTRCT22 ARG-165.
  7. "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 CTRCT22 GLU-194.

Entry informationi

Entry nameiCRBB3_HUMAN
AccessioniPrimary (citable) accession number: P26998
Secondary accession number(s): Q3B7S9
, Q3T1B7, Q6ISK6, Q92965, Q9UH09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 2, 2010
Last modified: July 6, 2016
This is version 157 of the entry and version 4 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, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.