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Protein

Beta-crystallin B2

Gene

CRYBB2

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

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

GO - Biological processi

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

Keywords - Molecular functioni

Eye lens protein

Keywords - Biological processi

Sensory transduction, Vision

Enzyme and pathway databases

BioCyciZFISH:ENSG00000100058-MONOMER.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:2398. CRYBB2.

Pathology & Biotechi

Involvement in diseasei

Cataract 3, multiple types (CTRCT3)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. 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.
See also OMIM:601547

Keywords - Diseasei

Cataract

Organism-specific databases

DisGeNETi1415.
MalaCardsiCRYBB2.
MIMi601547. phenotype.
OpenTargetsiENSG00000244752.
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.

Polymorphism and mutation databases

BioMutaiCRYBB2.
DMDMi1169091.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000575532 – 205Beta-crystallin B2Add BLAST204

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP43320.
PeptideAtlasiP43320.
PRIDEiP43320.

PTM databases

iPTMnetiP43320.
PhosphoSitePlusiP43320.

Expressioni

Gene expression databases

BgeeiENSG00000244752.
CleanExiHS_CRYBB2.
ExpressionAtlasiP43320. baseline and differential.
GenevisibleiP43320. HS.

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

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi107805. 6 interactors.
IntActiP43320. 6 interactors.
MINTiMINT-221083.
STRINGi9606.ENSP00000381273.

Structurei

Secondary structure

1205
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi18 – 24Combined sources7
Beta strandi31 – 36Combined sources6
Helixi41 – 44Combined sources4
Beta strandi50 – 56Combined sources7
Beta strandi59 – 64Combined sources6
Turni65 – 67Combined sources3
Beta strandi68 – 74Combined sources7
Beta strandi76 – 79Combined sources4
Helixi82 – 84Combined sources3
Beta strandi96 – 99Combined sources4
Beta strandi108 – 114Combined sources7
Turni115 – 117Combined sources3
Beta strandi118 – 127Combined sources10
Helixi133 – 135Combined sources3
Beta strandi143 – 146Combined sources4
Beta strandi151 – 156Combined sources6
Turni157 – 159Combined sources3
Beta strandi160 – 166Combined sources7
Beta strandi168 – 171Combined sources4
Helixi174 – 177Combined sources4
Beta strandi180 – 182Combined sources3
Beta strandi186 – 189Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP43320.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini17 – 56Beta/gamma crystallin 'Greek key' 1PROSITE-ProRule annotationAdd BLAST40
Domaini57 – 101Beta/gamma crystallin 'Greek key' 2PROSITE-ProRule annotationAdd BLAST45
Domaini107 – 148Beta/gamma crystallin 'Greek key' 3PROSITE-ProRule annotationAdd BLAST42
Domaini149 – 191Beta/gamma crystallin 'Greek key' 4PROSITE-ProRule annotationAdd BLAST43

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 16N-terminal armAdd BLAST15
Regioni102 – 106Connecting peptide5
Regioni193 – 205C-terminal armAdd BLAST13

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.
InParanoidiP43320.
OMAiHELTGPC.
OrthoDBiEOG091G0KRX.
PhylomeDBiP43320.
TreeFamiTF331401.

Family and domain databases

InterProiIPR001064. Beta/gamma_crystallin.
IPR033058. CRYBB2.
IPR011024. G_crystallin-rel.
[Graphical view]
PANTHERiPTHR11818:SF11. PTHR11818:SF11. 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.

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_03843165A → S.Corresponds to variant rs16986560dbSNPEnsembl.1

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_006724141.3.
XP_011528202.1. XM_011529900.2.
UniGeneiHs.373074.

Genome annotation databases

EnsembliENST00000398215; ENSP00000381273; ENSG00000244752.
GeneIDi1415.
KEGGihsa:1415.

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.
CCDSiCCDS13831.1.
PIRiJC2009.
RefSeqiNP_000487.1. NM_000496.2.
XP_006724204.1. XM_006724141.3.
XP_011528202.1. XM_011529900.2.
UniGeneiHs.373074.

3D structure databases

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

Protein-protein interaction databases

BioGridi107805. 6 interactors.
IntActiP43320. 6 interactors.
MINTiMINT-221083.
STRINGi9606.ENSP00000381273.

PTM databases

iPTMnetiP43320.
PhosphoSitePlusiP43320.

Polymorphism and mutation databases

BioMutaiCRYBB2.
DMDMi1169091.

Proteomic databases

PaxDbiP43320.
PeptideAtlasiP43320.
PRIDEiP43320.

Protocols and materials databases

DNASUi1415.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000398215; ENSP00000381273; ENSG00000244752.
GeneIDi1415.
KEGGihsa:1415.

Organism-specific databases

CTDi1415.
DisGeNETi1415.
GeneCardsiCRYBB2.
HGNCiHGNC:2398. CRYBB2.
HPAiHPA043749.
MalaCardsiCRYBB2.
MIMi123620. gene.
601547. phenotype.
neXtProtiNX_P43320.
OpenTargetsiENSG00000244752.
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.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJYD. Eukaryota.
ENOG410Y7P1. LUCA.
GeneTreeiENSGT00760000118812.
HOGENOMiHOG000234388.
HOVERGENiHBG003364.
InParanoidiP43320.
OMAiHELTGPC.
OrthoDBiEOG091G0KRX.
PhylomeDBiP43320.
TreeFamiTF331401.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000100058-MONOMER.

Miscellaneous databases

ChiTaRSiCRYBB2. human.
EvolutionaryTraceiP43320.
GeneWikiiCRYBB2.
GenomeRNAii1415.
PROiP43320.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000244752.
CleanExiHS_CRYBB2.
ExpressionAtlasiP43320. baseline and differential.
GenevisibleiP43320. HS.

Family and domain databases

InterProiIPR001064. Beta/gamma_crystallin.
IPR033058. CRYBB2.
IPR011024. G_crystallin-rel.
[Graphical view]
PANTHERiPTHR11818:SF11. PTHR11818:SF11. 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...

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 2, 2016
This is version 161 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

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.