Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

  1. structural constituent of eye lens Source: UniProtKB-KW

GO - Biological processi

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

Keywords - Molecular functioni

Eye lens protein

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
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:2396. CRYBA4.

Pathology & Biotechi

Involvement in diseasei

Cataract 231 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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti69 – 691L → P in CTRCT23; the patient has cataract and bilateral microphthalmia; the mutation is predicted to disrupt the beta-sheet structure of the protein. 1 Publication
VAR_029528
Natural varianti94 – 941F → S in CTRCT23; modeling suggests that this substitution would significantly reduce the intrinsic stability of the crystalline monomer. 1 Publication
VAR_029529

Keywords - Diseasei

Cataract, Disease mutation

Organism-specific databases

MIMi610425. phenotype.
Orphaneti1377. Cataract-microcornea syndrome.
2543. Microphthalmia - cataract.
98995. Zonular cataract.
PharmGKBiPA26910.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 196195Beta-crystallin A4PRO_0000057545Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP53673.
PRIDEiP53673.

PTM databases

PhosphoSiteiP53673.

Expressioni

Gene expression databases

BgeeiP53673.
CleanExiHS_CRYBA4.
GenevestigatoriP53673.

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

Protein-protein interaction databases

BioGridi107803. 1 interaction.
IntActiP53673. 2 interactions.
MINTiMINT-5161963.
STRINGi9606.ENSP00000346805.

Structurei

Secondary structure

1
196
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 197Combined sources
Helixi20 – 223Combined sources
Beta strandi23 – 319Combined sources
Helixi36 – 394Combined sources
Beta strandi46 – 527Combined sources
Beta strandi54 – 596Combined sources
Helixi60 – 623Combined sources
Beta strandi63 – 697Combined sources
Beta strandi71 – 744Combined sources
Helixi78 – 814Combined sources
Beta strandi93 – 964Combined sources
Helixi102 – 1043Combined sources
Beta strandi106 – 1138Combined sources
Beta strandi119 – 1246Combined sources
Helixi130 – 1323Combined sources
Beta strandi136 – 1383Combined sources
Beta strandi141 – 15414Combined sources
Turni155 – 1573Combined sources
Beta strandi158 – 1658Combined sources
Helixi169 – 1713Combined sources
Turni176 – 1783Combined sources
Beta strandi190 – 1934Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LWKX-ray1.70A8-196[»]
ProteinModelPortaliP53673.
SMRiP53673. Positions 8-196.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53673.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 5140Beta/gamma crystallin 'Greek key' 1PROSITE-ProRule annotationAdd
BLAST
Domaini52 – 9847Beta/gamma crystallin 'Greek key' 2PROSITE-ProRule annotationAdd
BLAST
Domaini105 – 14642Beta/gamma crystallin 'Greek key' 3PROSITE-ProRule annotationAdd
BLAST
Domaini147 – 19549Beta/gamma crystallin 'Greek key' 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 1110N-terminal arm
Regioni99 – 1046Connecting 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

eggNOGiNOG39249.
GeneTreeiENSGT00760000118812.
HOGENOMiHOG000234388.
HOVERGENiHBG003364.
InParanoidiP53673.
OMAiCTKSAGH.
OrthoDBiEOG7K9K40.
PhylomeDBiP53673.
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]

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 CAG30310.1 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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 361V → M.
Corresponds to variant rs35520672 [ dbSNP | Ensembl ].
VAR_033824
Natural varianti69 – 691L → P in CTRCT23; the patient has cataract and bilateral microphthalmia; the mutation is predicted to disrupt the beta-sheet structure of the protein. 1 Publication
VAR_029528
Natural varianti84 – 841T → M.
Corresponds to variant rs4277 [ dbSNP | Ensembl ].
VAR_014903
Natural varianti94 – 941F → S in CTRCT23; modeling suggests that this substitution would significantly reduce the intrinsic stability of the crystalline monomer. 1 Publication
VAR_029529

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.
UniGeneiHs.57690.

Genome annotation databases

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

Polymorphism databases

DMDMi2506318.

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.
UniGeneiHs.57690.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LWKX-ray1.70A8-196[»]
ProteinModelPortaliP53673.
SMRiP53673. Positions 8-196.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107803. 1 interaction.
IntActiP53673. 2 interactions.
MINTiMINT-5161963.
STRINGi9606.ENSP00000346805.

PTM databases

PhosphoSiteiP53673.

Polymorphism databases

DMDMi2506318.

Proteomic databases

PaxDbiP53673.
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.
GeneCardsiGC22P027017.
HGNCiHGNC:2396. CRYBA4.
MIMi123631. gene.
610425. phenotype.
neXtProtiNX_P53673.
Orphaneti1377. Cataract-microcornea syndrome.
2543. Microphthalmia - cataract.
98995. Zonular cataract.
PharmGKBiPA26910.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG39249.
GeneTreeiENSGT00760000118812.
HOGENOMiHOG000234388.
HOVERGENiHBG003364.
InParanoidiP53673.
OMAiCTKSAGH.
OrthoDBiEOG7K9K40.
PhylomeDBiP53673.
TreeFamiTF331401.

Miscellaneous databases

EvolutionaryTraceiP53673.
GeneWikiiCRYBA4.
GenomeRNAii1413.
NextBioi5781.
PROiP53673.
SOURCEiSearch...

Gene expression databases

BgeeiP53673.
CleanExiHS_CRYBA4.
GenevestigatoriP53673.

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. "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], PROTEIN SEQUENCE OF 14-25; 159-174 AND 178-192, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, MASS SPECTROMETRY.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
  5. "Regional fine mapping of the beta crystallin genes on chromosome 22 excludes these genes as physically linked markers for neurofibromatosis type 2."
    Bijlsma E.K., Delattre O., Juyn J.A., Melot T., Westerveld A., Dumanski J.P., Thomas G., Hulsebos T.J.M.
    Genes Chromosomes Cancer 8:112-118(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 150-194.
  6. Cited for: VARIANTS CTRCT23 PRO-69 AND SER-94.

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: February 4, 2015
This is version 141 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

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.