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Protein

Beta-crystallin A3

Gene

CRYBA1

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

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

Keywords - Molecular functioni

Eye lens protein

Names & Taxonomyi

Protein namesi
Gene namesi
Name:CRYBA1
Synonyms:CRYB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:2394. CRYBA1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Cataract 10, multiple types (CTRCT10)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. CTRCT10 includes congenital zonular with sutural opacities, among others. This is a form of zonular cataract with an erect Y-shaped anterior and an inverted Y-shaped posterior sutural opacities. 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:600881

Keywords - Diseasei

Cataract

Organism-specific databases

MIMi600881. phenotype.
Orphaneti98985. Cataract with Y-shaped suture opacities.
98995. Zonular cataract.
PharmGKBiPA26908.

Polymorphism and mutation databases

BioMutaiCRYBA1.
DMDMi2506317.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 215215Beta-crystallin A3PRO_0000006331Add
BLAST
Chaini23 – 215193Beta-crystallin A3, isoform A1, Delta4 formPRO_0000226692Add
BLAST
Chaini26 – 215190Beta-crystallin A3, isoform A1, Delta7 formPRO_0000226693Add
BLAST
Chaini27 – 215189Beta-crystallin A3, isoform A1, Delta8 formPRO_0000226694Add
BLAST
Isoform A1 (identifier: P05813-2)
Initiator methioninei1 – 11Removed

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei82 – 821S-glutathionyl cysteine; alternate1 Publication
Modified residuei82 – 821S-methylcysteine; alternate1 Publication
Modified residuei117 – 1171S-glutathionyl cysteine; alternate1 Publication
Modified residuei117 – 1171S-methylcysteine; alternate1 Publication
Modified residuei185 – 1851S-methylcysteine1 Publication
Isoform A1 (identifier: P05813-2)
Modified residuei2 – 21N-acetylalanine

Post-translational modificationi

Specific cleavages in the N-terminal arm occur during lens maturation and give rise to several truncated forms. Cleavages do not seem to have adverse effects on solubility.1 Publication
S-methylation and glutathionylation occur in normal young lenses and do not seem to be detrimental.1 Publication
Isoform A1 initiator methionine is removed. The new N-terminal amino acid is then N-acetylated.2 Publications

Keywords - PTMi

Acetylation, Glutathionylation, Methylation, Oxidation

Proteomic databases

PaxDbiP05813.
PRIDEiP05813.

PTM databases

PhosphoSiteiP05813.

Expressioni

Gene expression databases

BgeeiP05813.
CleanExiHS_CRYBA1.
ExpressionAtlasiP05813. baseline and differential.
GenevisibleiP05813. 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
CRYABP025112EBI-7043337,EBI-739060
CRYBB1P536746EBI-7043337,EBI-7519424
CRYBB3P269983EBI-7043337,EBI-1965681
RBPMSQ930623EBI-7043337,EBI-740322
RHOXF2Q9BQY43EBI-7043337,EBI-372094

Protein-protein interaction databases

BioGridi107801. 7 interactions.
IntActiP05813. 6 interactions.
MINTiMINT-3388142.
STRINGi9606.ENSP00000225387.

Structurei

3D structure databases

ProteinModelPortaliP05813.
SMRiP05813. Positions 27-215.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 7040Beta/gamma crystallin 'Greek key' 1PROSITE-ProRule annotationAdd
BLAST
Domaini71 – 11747Beta/gamma crystallin 'Greek key' 2PROSITE-ProRule annotationAdd
BLAST
Domaini124 – 16542Beta/gamma crystallin 'Greek key' 3PROSITE-ProRule annotationAdd
BLAST
Domaini166 – 21449Beta/gamma crystallin 'Greek key' 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 3030N-terminal armAdd
BLAST
Regioni118 – 1236Connecting peptide

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

eggNOGiNOG47808.
GeneTreeiENSGT00760000118812.
HOGENOMiHOG000234388.
HOVERGENiHBG003364.
InParanoidiP05813.
OMAiSLGPWKI.
OrthoDBiEOG7K9K40.
PhylomeDBiP05813.
TreeFamiTF331401.

Family and domain databases

InterProiIPR001064. Beta/gamma_crystallin.
IPR011024. G_crystallin-rel.
[Graphical view]
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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform A3 (identifier: P05813-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
METQAEQQEL ETLPTTKMAQ TNPTPGSLGP WKITIYDQEN FQGKRMEFTS
60 70 80 90 100
SCPNVSERSF DNVRSLKVES GAWIGYEHTS FCGQQFILER GEYPRWDAWS
110 120 130 140 150
GSNAYHIERL MSFRPICSAN HKESKMTIFE KENFIGRQWE ISDDYPSLQA
160 170 180 190 200
MGWFNNEVGS MKIQSGAWVC YQYPGYRGYQ YILECDHHGG DYKHWREWGS
210
HAQTSQIQSI RRIQQ
Length:215
Mass (Da):25,150
Last modified:November 1, 1997 - v4
Checksum:iC544564835688A19
GO
Isoform A1 (identifier: P05813-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: Missing.

Show »
Length:198
Mass (Da):23,191
Checksum:i95954586F78B1B4C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti107 – 1071I → M in AAA52107 (PubMed:3745196).Curated
Sequence conflicti116 – 1161I → F in AAA52107 (PubMed:3745196).Curated
Sequence conflicti172 – 1743QYP → HYL in AAA52107 (PubMed:3745196).Curated
Sequence conflicti184 – 1841E → K in AAA52107 (PubMed:3745196).Curated
Sequence conflicti189 – 1891G → E in AAA52107 (PubMed:3745196).Curated

Mass spectrometryi

Molecular mass is 25192±3 Da from positions 1 - 215. Determined by ESI. 1 Publication
Molecular mass is 25192 Da from positions 1 - 215. Determined by ESI. 1 Publication
Molecular mass is 23101±3 Da from positions 19 - 215. Determined by ESI. 1 Publication
Molecular mass is 23102 Da from positions 19 - 215. Determined by ESI. 1 Publication
Molecular mass is 22646 Da from positions 23 - 215. Determined by ESI. 1 Publication
Molecular mass is 22351 Da from positions 26 - 215. Determined by ESI. 1 Publication
Molecular mass is 22294 Da from positions 27 - 215. Determined by ESI. 1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1717Missing in isoform A1. CuratedVSP_018710Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14306
, M14301, M14302, M14303, M14304, M14305 Genomic DNA. Translation: AAA52107.1.
BC069537 mRNA. Translation: AAH69537.1.
BC113693 mRNA. Translation: AAI13694.1.
U59058 mRNA. Translation: AAC50971.1.
CCDSiCCDS11249.1. [P05813-1]
PIRiA25202. CYHUB3.
RefSeqiNP_005199.2. NM_005208.4. [P05813-1]
UniGeneiHs.46275.

Genome annotation databases

EnsembliENST00000225387; ENSP00000225387; ENSG00000108255.
GeneIDi1411.
KEGGihsa:1411.
UCSCiuc002hdw.3. human. [P05813-1]

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Web resourcesi

Eye disease Crystallin, beta-A1 (CRYBA1)

Leiden Open Variation Database (LOVD)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14306
, M14301, M14302, M14303, M14304, M14305 Genomic DNA. Translation: AAA52107.1.
BC069537 mRNA. Translation: AAH69537.1.
BC113693 mRNA. Translation: AAI13694.1.
U59058 mRNA. Translation: AAC50971.1.
CCDSiCCDS11249.1. [P05813-1]
PIRiA25202. CYHUB3.
RefSeqiNP_005199.2. NM_005208.4. [P05813-1]
UniGeneiHs.46275.

3D structure databases

ProteinModelPortaliP05813.
SMRiP05813. Positions 27-215.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107801. 7 interactions.
IntActiP05813. 6 interactions.
MINTiMINT-3388142.
STRINGi9606.ENSP00000225387.

PTM databases

PhosphoSiteiP05813.

Polymorphism and mutation databases

BioMutaiCRYBA1.
DMDMi2506317.

Proteomic databases

PaxDbiP05813.
PRIDEiP05813.

Protocols and materials databases

DNASUi1411.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000225387; ENSP00000225387; ENSG00000108255.
GeneIDi1411.
KEGGihsa:1411.
UCSCiuc002hdw.3. human. [P05813-1]

Organism-specific databases

CTDi1411.
GeneCardsiGC17P027573.
HGNCiHGNC:2394. CRYBA1.
MIMi123610. gene.
600881. phenotype.
neXtProtiNX_P05813.
Orphaneti98985. Cataract with Y-shaped suture opacities.
98995. Zonular cataract.
PharmGKBiPA26908.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG47808.
GeneTreeiENSGT00760000118812.
HOGENOMiHOG000234388.
HOVERGENiHBG003364.
InParanoidiP05813.
OMAiSLGPWKI.
OrthoDBiEOG7K9K40.
PhylomeDBiP05813.
TreeFamiTF331401.

Miscellaneous databases

ChiTaRSiCRYBA1. human.
GeneWikiiCrystallin,_beta_A1.
GenomeRNAii1411.
NextBioi5769.
PROiP05813.
SOURCEiSearch...

Gene expression databases

BgeeiP05813.
CleanExiHS_CRYBA1.
ExpressionAtlasiP05813. baseline and differential.
GenevisibleiP05813. HS.

Family and domain databases

InterProiIPR001064. Beta/gamma_crystallin.
IPR011024. G_crystallin-rel.
[Graphical view]
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. "Characterization of the human beta-crystallin gene Hu beta A3/A1 reveals ancestral relationships among the beta gamma-crystallin superfamily."
    Hogg D., Tsui L.-C., Gorin M., Breitman M.L.
    J. Biol. Chem. 261:12420-12427(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "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].
  3. "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 44-215, PROTEIN SEQUENCE OF 23-30 AND 197-211, ACETYLATION AT MET-1, CLEAVAGE OF INITIATOR METHIONINE (ISOFORM A1), ACETYLATION AT ALA-2 (ISOFORM A1), MASS SPECTROMETRY.
  4. "Autosomal dominant zonular cataract with sutural opacities is associated with a splice mutation in the betaA3/A1-crystallin gene."
    Kannabiran C., Rogan P.K., Olmos L., Basti S., Rao G.N., Kaiser-Kupfer M., Hejtmancik J.F.
    Mol. Vis. 4:21-21(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CTRCT10.
  5. "Characterization of the G91del CRYBA1/3-crystallin protein: a cause of human inherited cataract."
    Reddy M.A., Bateman O.A., Chakarova C., Ferris J., Berry V., Lomas E., Sarra R., Smith M.A., Moore A.T., Bhattacharya S.S., Slingsby C.
    Hum. Mol. Genet. 13:945-953(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CTRCT10.
  6. "Modifications of human betaA1/betaA3-crystallins include S-methylation, glutathiolation, and truncation."
    Lapko V.N., Cerny R.L., Smith D.L., Smith J.B.
    Protein Sci. 14:45-54(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF N-TERMINUS, ACETYLATION AT MET-1, CLEAVAGE OF INITIATOR METHIONINE (ISOFORM A1), ACETYLATION AT ALA-2 (ISOFORM A1), METHYLATION AT CYS-82; CYS-117 AND CYS-185, GLUTATHIONYLATION AT CYS-82 AND CYS-117, MASS SPECTROMETRY.

Entry informationi

Entry nameiCRBA1_HUMAN
AccessioniPrimary (citable) accession number: P05813
Secondary accession number(s): Q13633, Q14CM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1997
Last modified: July 22, 2015
This is version 156 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.