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Protein

Beta-crystallin B1

Gene

CRYBB1

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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000100122-MONOMER.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:2397. CRYBB1.

Pathology & Biotechi

Involvement in diseasei

Cataract 17, multiple types (CTRCT17)3 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. 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.
See also OMIM:611544
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07003096V → F in CTRCT17. 1 Publication1

CRYBB1 mutations may be a cause of congenital cataract and microcornea syndrome, 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

DisGeNETi1414.
MalaCardsiCRYBB1.
MIMi611544. phenotype.
OpenTargetsiENSG00000100122.
Orphaneti1377. Cataract-microcornea syndrome.
98991. Nuclear cataract.
98984. Pulverulent cataract.
PharmGKBiPA26911.

Polymorphism and mutation databases

BioMutaiCRYBB1.
DMDMi1706116.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000575502 – 252Beta-crystallin B1Add BLAST251

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1

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

EPDiP53674.
PaxDbiP53674.
PeptideAtlasiP53674.
PRIDEiP53674.

PTM databases

iPTMnetiP53674.
PhosphoSitePlusiP53674.

Miscellaneous databases

PMAP-CutDBP53674.

Expressioni

Gene expression databases

BgeeiENSG00000100122.
CleanExiHS_CRYBB1.
GenevisibleiP53674. HS.

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
CRYBA1P058136EBI-7519424,EBI-7043337
TERF1P542742EBI-7519424,EBI-710997

Protein-protein interaction databases

BioGridi107804. 4 interactors.
IntActiP53674. 8 interactors.
MINTiMINT-5161833.
STRINGi9606.ENSP00000215939.

Structurei

Secondary structure

1252
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi60 – 66Combined sources7
Turni67 – 69Combined sources3
Beta strandi70 – 78Combined sources9
Turni83 – 87Combined sources5
Beta strandi93 – 98Combined sources6
Beta strandi101 – 106Combined sources6
Helixi107 – 109Combined sources3
Beta strandi110 – 116Combined sources7
Beta strandi118 – 121Combined sources4
Helixi124 – 127Combined sources4
Beta strandi138 – 141Combined sources4
Beta strandi150 – 156Combined sources7
Helixi157 – 159Combined sources3
Beta strandi160 – 169Combined sources10
Helixi174 – 177Combined sources4
Beta strandi185 – 198Combined sources14
Turni199 – 201Combined sources3
Beta strandi202 – 208Combined sources7
Beta strandi210 – 215Combined sources6
Helixi216 – 219Combined sources4
Beta strandi228 – 232Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OKIX-ray1.40A/B43-252[»]
ProteinModelPortaliP53674.
SMRiP53674.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53674.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini59 – 98Beta/gamma crystallin 'Greek key' 1PROSITE-ProRule annotationAdd BLAST40
Domaini99 – 143Beta/gamma crystallin 'Greek key' 2PROSITE-ProRule annotationAdd BLAST45
Domaini149 – 190Beta/gamma crystallin 'Greek key' 3PROSITE-ProRule annotationAdd BLAST42
Domaini191 – 233Beta/gamma crystallin 'Greek key' 4PROSITE-ProRule annotationAdd BLAST43

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 58N-terminal armAdd BLAST57
Regioni144 – 148Connecting peptide5
Regioni235 – 252C-terminal armAdd BLAST18

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

eggNOGiENOG410IJ9M. Eukaryota.
ENOG410ZYKU. LUCA.
GeneTreeiENSGT00760000118812.
HOGENOMiHOG000234388.
HOVERGENiHBG003364.
InParanoidiP53674.
OMAiMSFRPIK.
OrthoDBiEOG091G0JIZ.
PhylomeDBiP53674.
TreeFamiTF331401.

Family and domain databases

InterProiIPR001064. Beta/gamma_crystallin.
IPR033059. CRYBB1.
IPR011024. G_crystallin-rel.
[Graphical view]
PANTHERiPTHR11818:SF12. PTHR11818:SF12. 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.

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_07003096V → F in CTRCT17. 1 Publication1
Natural variantiVAR_065296129S → R 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 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
XP_011528201.1. XM_011529899.2.
UniGeneiHs.37135.

Genome annotation databases

EnsembliENST00000215939; ENSP00000215939; ENSG00000100122.
GeneIDi1414.
KEGGihsa:1414.
UCSCiuc003acy.2. human.

Cross-referencesi

Web resourcesi

Eye disease Crystallin, beta-B1 (CRYBB1)

Leiden Open Variation Database (LOVD)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
XP_011528201.1. XM_011529899.2.
UniGeneiHs.37135.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OKIX-ray1.40A/B43-252[»]
ProteinModelPortaliP53674.
SMRiP53674.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107804. 4 interactors.
IntActiP53674. 8 interactors.
MINTiMINT-5161833.
STRINGi9606.ENSP00000215939.

PTM databases

iPTMnetiP53674.
PhosphoSitePlusiP53674.

Polymorphism and mutation databases

BioMutaiCRYBB1.
DMDMi1706116.

Proteomic databases

EPDiP53674.
PaxDbiP53674.
PeptideAtlasiP53674.
PRIDEiP53674.

Protocols and materials databases

DNASUi1414.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000215939; ENSP00000215939; ENSG00000100122.
GeneIDi1414.
KEGGihsa:1414.
UCSCiuc003acy.2. human.

Organism-specific databases

CTDi1414.
DisGeNETi1414.
GeneCardsiCRYBB1.
HGNCiHGNC:2397. CRYBB1.
MalaCardsiCRYBB1.
MIMi600929. gene.
611544. phenotype.
neXtProtiNX_P53674.
OpenTargetsiENSG00000100122.
Orphaneti1377. Cataract-microcornea syndrome.
98991. Nuclear cataract.
98984. Pulverulent cataract.
PharmGKBiPA26911.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJ9M. Eukaryota.
ENOG410ZYKU. LUCA.
GeneTreeiENSGT00760000118812.
HOGENOMiHOG000234388.
HOVERGENiHBG003364.
InParanoidiP53674.
OMAiMSFRPIK.
OrthoDBiEOG091G0JIZ.
PhylomeDBiP53674.
TreeFamiTF331401.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000100122-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP53674.
GeneWikiiCRYBB1.
GenomeRNAii1414.
PMAP-CutDBP53674.
PROiP53674.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100122.
CleanExiHS_CRYBB1.
GenevisibleiP53674. HS.

Family and domain databases

InterProiIPR001064. Beta/gamma_crystallin.
IPR033059. CRYBB1.
IPR011024. G_crystallin-rel.
[Graphical view]
PANTHERiPTHR11818:SF12. PTHR11818:SF12. 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 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: November 30, 2016
This is version 162 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.