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Protein

Beta-crystallin B2

Gene

CRYBB2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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
  • protein homodimerization activity Source: Ensembl
  • 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

Keywordsi

Molecular functionEye lens protein
Biological processSensory transduction, Vision

Enzyme and pathway databases

SIGNORiP43320

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

EuPathDBiHostDB:ENSG00000244752.2
HGNCiHGNC:2398 CRYBB2
MIMi123620 gene
neXtProtiNX_P43320

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

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: Ensembl

Protein-protein interaction databases

BioGridi107805, 6 interactors
IntActiP43320, 8 interactors
MINTiP43320
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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IJYD Eukaryota
ENOG410Y7P1 LUCA
GeneTreeiENSGT00760000118812
HOGENOMiHOG000234388
HOVERGENiHBG003364
InParanoidiP43320
OMAiYEQASCK
OrthoDBiEOG091G0KRX
PhylomeDBiP43320
TreeFamiTF331401

Family and domain databases

InterProiView protein in InterPro
IPR001064 Beta/gamma_crystallin
IPR033058 CRYBB2
IPR011024 G_crystallin-like
PANTHERiPTHR11818:SF11 PTHR11818:SF11, 1 hit
PfamiView protein in Pfam
PF00030 Crystall, 2 hits
PRINTSiPR01367 BGCRYSTALLIN
SMARTiView protein in SMART
SM00247 XTALbg, 2 hits
SUPFAMiSSF49695 SSF49695, 1 hit
PROSITEiView protein in PROSITE
PS50915 CRYSTALLIN_BETA_GAMMA, 4 hits

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 dbSNP:rs16986560Ensembl.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 No translation available.
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

Similar proteinsi

Entry informationi

Entry nameiCRBB2_HUMAN
AccessioniPrimary (citable) accession number: P43320
Secondary accession number(s): Q9UCM8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 170 of the entry and version 2 of the sequence. See 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health