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Protein

Beta-crystallin A4

Gene

CRYBA4

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

  • camera-type eye development Source: UniProtKB
  • visual perception Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Eye lens protein

Enzyme and pathway databases

BioCyciZFISH:G66-32983-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-crystallin A4
Alternative name(s):
Beta-A4 crystallin
Gene namesi
Name:CRYBA4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:2396. CRYBA4.

Pathology & Biotechi

Involvement in diseasei

Cataract 23 (CTRCT23)1 Publication
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. CTRCT23 is a zonular cataract. Zonular or lamellar cataracts are opacities, broad or narrow, usually consisting of powdery white dots affecting only certain layers or zones between the cortex and nucleus of an otherwise clear lens. The opacity may be so dense as to render the entire central region of the lens completely opaque, or so translucent that vision is hardly if at all impeded. Zonular cataracts generally do not involve the embryonic nucleus, though sometimes they involve the fetal nucleus. Usually sharply separated from a clear cortex outside them, they may have projections from their outer edges known as riders or spokes.
See also OMIM:610425
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02952869L → P in CTRCT23; the patient has cataract and bilateral microphthalmia; the mutation is predicted to disrupt the beta-sheet structure of the protein. 1 PublicationCorresponds to variant rs74315487dbSNPEnsembl.1
Natural variantiVAR_02952994F → S in CTRCT23; modeling suggests that this substitution would significantly reduce the intrinsic stability of the crystalline monomer. 1 PublicationCorresponds to variant rs74315486dbSNPEnsembl.1

Keywords - Diseasei

Cataract, Disease mutation

Organism-specific databases

DisGeNETi1413.
MalaCardsiCRYBA4.
MIMi610425. phenotype.
OpenTargetsiENSG00000196431.
Orphaneti1377. Cataract-microcornea syndrome.
98995. Zonular cataract.
PharmGKBiPA26910.

Polymorphism and mutation databases

BioMutaiCRYBA4.
DMDMi2506318.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000575452 – 196Beta-crystallin A4Add BLAST195

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP53673.
PeptideAtlasiP53673.
PRIDEiP53673.

PTM databases

iPTMnetiP53673.
PhosphoSitePlusiP53673.

Expressioni

Gene expression databases

BgeeiENSG00000196431.
CleanExiHS_CRYBA4.
ExpressionAtlasiP53673. baseline and differential.
GenevisibleiP53673. 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 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CEP76Q8TAP65EBI-7519711,EBI-742887

Protein-protein interaction databases

BioGridi107803. 14 interactors.
IntActiP53673. 3 interactors.
MINTiMINT-5161963.
STRINGi9606.ENSP00000346805.

Structurei

Secondary structure

1196
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi13 – 19Combined sources7
Helixi20 – 22Combined sources3
Beta strandi23 – 31Combined sources9
Helixi36 – 39Combined sources4
Beta strandi46 – 52Combined sources7
Beta strandi54 – 59Combined sources6
Helixi60 – 62Combined sources3
Beta strandi63 – 69Combined sources7
Beta strandi71 – 74Combined sources4
Helixi78 – 81Combined sources4
Beta strandi93 – 96Combined sources4
Helixi102 – 104Combined sources3
Beta strandi106 – 113Combined sources8
Beta strandi119 – 124Combined sources6
Helixi130 – 132Combined sources3
Beta strandi136 – 138Combined sources3
Beta strandi141 – 154Combined sources14
Turni155 – 157Combined sources3
Beta strandi158 – 165Combined sources8
Helixi169 – 171Combined sources3
Turni176 – 178Combined sources3
Beta strandi190 – 193Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LWKX-ray1.70A8-196[»]
ProteinModelPortaliP53673.
SMRiP53673.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53673.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini12 – 51Beta/gamma crystallin 'Greek key' 1PROSITE-ProRule annotationAdd BLAST40
Domaini52 – 98Beta/gamma crystallin 'Greek key' 2PROSITE-ProRule annotationAdd BLAST47
Domaini105 – 146Beta/gamma crystallin 'Greek key' 3PROSITE-ProRule annotationAdd BLAST42
Domaini147 – 195Beta/gamma crystallin 'Greek key' 4PROSITE-ProRule annotationAdd BLAST49

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 11N-terminal arm10
Regioni99 – 104Connecting peptide6

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

eggNOGiENOG410IE7N. Eukaryota.
ENOG410YIM8. LUCA.
GeneTreeiENSGT00760000118812.
HOGENOMiHOG000234388.
HOVERGENiHBG003364.
InParanoidiP53673.
OMAiFQVQSVR.
OrthoDBiEOG091G0JYH.
PhylomeDBiP53673.
TreeFamiTF331401.

Family and domain databases

InterProiIPR001064. Beta/gamma_crystallin.
IPR033342. CRYBA4.
IPR011024. G_crystallin-rel.
[Graphical view]
PANTHERiPTHR11818:SF19. PTHR11818:SF19. 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.

P53673-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLQCTKSAG PWKMVVWDED GFQGRRHEFT AECPSVLELG FETVRSLKVL
60 70 80 90 100
SGAWVGFEHA GFQGQQYILE RGEYPSWDAW GGNTAYPAER LTSFRPAACA
110 120 130 140 150
NHRDSRLTIF EQENFLGKKG ELSDDYPSLQ AMGWEGNEVG SFHVHSGAWV
160 170 180 190
CSQFPGYRGF QYVLECDHHS GDYKHFREWG SHAPTFQVQS IRRIQQ
Length:196
Mass (Da):22,374
Last modified:January 23, 2007 - v3
Checksum:i104EC68E3CDE5740
GO

Sequence cautioni

The sequence CAG30310 differs from that shown. Reason: Erroneous initiation.Curated

Mass spectrometryi

Molecular mass is 22285±3 Da from positions 2 - 196. Determined by ESI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03382436V → M.Corresponds to variant rs35520672dbSNPEnsembl.1
Natural variantiVAR_02952869L → P in CTRCT23; the patient has cataract and bilateral microphthalmia; the mutation is predicted to disrupt the beta-sheet structure of the protein. 1 PublicationCorresponds to variant rs74315487dbSNPEnsembl.1
Natural variantiVAR_01490384T → M.Corresponds to variant rs4277dbSNPEnsembl.1
Natural variantiVAR_02952994F → S in CTRCT23; modeling suggests that this substitution would significantly reduce the intrinsic stability of the crystalline monomer. 1 PublicationCorresponds to variant rs74315486dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59057 mRNA. Translation: AAC50970.1.
CR456424 mRNA. Translation: CAG30310.1. Different initiation.
Z95115 Genomic DNA. Translation: CAI17980.2.
BC069404 mRNA. Translation: AAH69404.1.
BC096171 mRNA. Translation: AAH96171.1.
BC096172 mRNA. Translation: AAH96172.1.
BC096173 mRNA. Translation: AAH96173.1.
BC096174 mRNA. Translation: AAH96174.1.
S67583 Genomic DNA. Translation: AAD13994.1.
CCDSiCCDS13841.1.
PIRiI54083.
RefSeqiNP_001877.1. NM_001886.2.
XP_016884087.1. XM_017028598.1.
UniGeneiHs.57690.

Genome annotation databases

EnsembliENST00000354760; ENSP00000346805; ENSG00000196431.
GeneIDi1413.
KEGGihsa:1413.
UCSCiuc003acz.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59057 mRNA. Translation: AAC50970.1.
CR456424 mRNA. Translation: CAG30310.1. Different initiation.
Z95115 Genomic DNA. Translation: CAI17980.2.
BC069404 mRNA. Translation: AAH69404.1.
BC096171 mRNA. Translation: AAH96171.1.
BC096172 mRNA. Translation: AAH96172.1.
BC096173 mRNA. Translation: AAH96173.1.
BC096174 mRNA. Translation: AAH96174.1.
S67583 Genomic DNA. Translation: AAD13994.1.
CCDSiCCDS13841.1.
PIRiI54083.
RefSeqiNP_001877.1. NM_001886.2.
XP_016884087.1. XM_017028598.1.
UniGeneiHs.57690.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LWKX-ray1.70A8-196[»]
ProteinModelPortaliP53673.
SMRiP53673.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107803. 14 interactors.
IntActiP53673. 3 interactors.
MINTiMINT-5161963.
STRINGi9606.ENSP00000346805.

PTM databases

iPTMnetiP53673.
PhosphoSitePlusiP53673.

Polymorphism and mutation databases

BioMutaiCRYBA4.
DMDMi2506318.

Proteomic databases

PaxDbiP53673.
PeptideAtlasiP53673.
PRIDEiP53673.

Protocols and materials databases

DNASUi1413.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000354760; ENSP00000346805; ENSG00000196431.
GeneIDi1413.
KEGGihsa:1413.
UCSCiuc003acz.4. human.

Organism-specific databases

CTDi1413.
DisGeNETi1413.
GeneCardsiCRYBA4.
HGNCiHGNC:2396. CRYBA4.
MalaCardsiCRYBA4.
MIMi123631. gene.
610425. phenotype.
neXtProtiNX_P53673.
OpenTargetsiENSG00000196431.
Orphaneti1377. Cataract-microcornea syndrome.
98995. Zonular cataract.
PharmGKBiPA26910.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IE7N. Eukaryota.
ENOG410YIM8. LUCA.
GeneTreeiENSGT00760000118812.
HOGENOMiHOG000234388.
HOVERGENiHBG003364.
InParanoidiP53673.
OMAiFQVQSVR.
OrthoDBiEOG091G0JYH.
PhylomeDBiP53673.
TreeFamiTF331401.

Enzyme and pathway databases

BioCyciZFISH:G66-32983-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP53673.
GeneWikiiCRYBA4.
GenomeRNAii1413.
PROiP53673.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000196431.
CleanExiHS_CRYBA4.
ExpressionAtlasiP53673. baseline and differential.
GenevisibleiP53673. HS.

Family and domain databases

InterProiIPR001064. Beta/gamma_crystallin.
IPR033342. CRYBA4.
IPR011024. G_crystallin-rel.
[Graphical view]
PANTHERiPTHR11818:SF19. PTHR11818:SF19. 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 nameiCRBA4_HUMAN
AccessioniPrimary (citable) accession number: P53673
Secondary accession number(s): Q4VB22, Q6ICE4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 157 of the entry and version 3 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.