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P02489 (CRYAA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-crystallin A chain
Alternative name(s):
Heat shock protein beta-4
Short name=HspB4
Gene names
Name:CRYAA
Synonyms:CRYA1, HSPB4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length173 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Contributes to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. Ref.24

Subunit structure

Heteropolymer composed of three CRYAA and one CRYAB subunits. Inter-subunit bridging via zinc ions enhances stability, which is crucial as there is no protein turn over in the lens. Can also form homodimers and higher homooligomers. Age-dependent C-terminal truncation affects oligomerization. Ref.21 Ref.23 Ref.25

Subcellular location

Cytoplasm. Nucleus. Note: Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles. Ref.22

Tissue specificity

Expressed in eye lens. Ref.19

Post-translational modification

O-glycosylated; contains N-acetylglucosamine side chains. Ref.11

Deamidation of Asn-101 in lens occurs mostly during the first 30 years of age, followed by a small additional amount of deamidation (approximately 5%) during the next approximately 38 years, resulting in a maximum of approximately 50% deamidation during the lifetime of the individual.

Phosphorylation on Ser-122 seems to be developmentally regulated. Absent in the first months of life, it appears during the first 12 years of human lifetime. The relative amount of phosphorylated form versus unphosphorylated form does not change over the lifetime of the individual. Ref.12 Ref.13 Ref.14 Ref.16 Ref.17

Acetylation at Lys-70 seems to increase chaperone activity. Ref.1 Ref.16 Ref.24

Undergoes age-dependent proteolytical cleavage at the C-terminus. Alpha-crystallin A(1-172) is the most predominant form produced most rapidly during the first 12 years of age and after this age is present in approximatley 50% of the lens molecules.

Involvement in disease

Alpha-crystallin A 1-172 is found at nearly twofold higher levels in diabetic lenses than in age-matched control lenses (Ref.19).

Cataract 9, multiple types (CTRCT9) [MIM:604219]: An 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. CTRCT9 includes nuclear, zonular central nuclear, anterior polar, cortical, embryonal, anterior subcapsular, fan-shaped, and total cataracts, among others. In some cases cataract is associated with microcornea without any other systemic anomaly or dysmorphism. Microcornea is defined by a corneal diameter inferior to 10 mm in both meridians in an otherwise normal eye.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.26 Ref.27 Ref.28 Ref.29 Ref.31 Ref.32 Ref.33

Sequence similarities

Belongs to the small heat shock protein (HSP20) family.

Mass spectrometry

Molecular mass is 19950 Da from positions 1 - 173. Determined by ESI. Ref.12

Molecular mass is 19863 Da from positions 1 - 172. Determined by ESI. Ref.12

Molecular mass is 20029 Da from positions 1 - 173. Determined by ESI. With 1 phosphate group. Ref.12

Molecular mass is 19951 Da from positions 1 - 173. Determined by ESI. Ref.16

Molecular mass is 19864 Da from positions 1 - 172. Determined by ESI. Ref.16

Molecular mass is 19947 Da from positions 1 - 173. Determined by ESI. Ref.17

Molecular mass is 19851 Da from positions 1 - 172. Determined by ESI. Ref.17

Ontologies

Keywords
   Biological processSensory transduction
Vision
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DiseaseCataract
Disease mutation
   LigandMetal-binding
Zinc
   Molecular functionChaperone
Eye lens protein
   PTMAcetylation
Disulfide bond
Glycoprotein
Oxidation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament organization

Inferred from electronic annotation. Source: Ensembl

apoptotic process involved in morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic camera-type eye morphogenesis

Inferred from electronic annotation. Source: Ensembl

lens fiber cell morphogenesis

Inferred from electronic annotation. Source: Ensembl

mitochondrion organization

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from mutant phenotype Ref.28. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

negative regulation of intracellular transport

Inferred from direct assay PubMed 14752512. Source: HGNC

positive regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

protein folding

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from direct assay PubMed 16303126. Source: UniProtKB

response to UV-A

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to lead ion

Inferred from electronic annotation. Source: Ensembl

tubulin complex assembly

Inferred from electronic annotation. Source: Ensembl

visual perception

Inferred from mutant phenotype Ref.28PubMed 18587492Ref.26. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.22. Source: UniProtKB

nucleus

Inferred from direct assay Ref.22. Source: UniProtKB

   Molecular_functionidentical protein binding

Inferred from physical interaction PubMed 12601044PubMed 22085609. Source: IntAct

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 14752512. Source: UniProtKB

structural constituent of eye lens

Inferred from electronic annotation. Source: UniProtKB-KW

unfolded protein binding

Inferred from mutant phenotype Ref.32. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 173173Alpha-crystallin A chain
PRO_0000125865
Chain1 – 172172Alpha-crystallin A(1-172)
PRO_0000226639
Chain1 – 168168Alpha-crystallin A(1-168)
PRO_0000423503
Chain1 – 162162Alpha-crystallin A(1-162)
PRO_0000423504

Sites

Metal binding791Zinc 1 Probable
Metal binding1001Zinc 2 By similarity
Metal binding1021Zinc 2 By similarity
Metal binding1071Zinc 1 Probable
Metal binding1151Zinc 1 Probable
Site11Susceptible to oxidation
Site181Susceptible to oxidation
Site341Susceptible to oxidation
Site1381Susceptible to oxidation

Amino acid modifications

Modified residue11N-acetylmethionine Ref.1
Modified residue61Deamidated glutamine; partial Ref.14
Modified residue451Phosphoserine Ref.14
Modified residue501Deamidated glutamine; partial Ref.14
Modified residue701N6-acetyllysine Ref.16 Ref.24
Modified residue901Deamidated glutamine; partial Ref.14
Modified residue991N6-acetyllysine Ref.24
Modified residue1011Deamidated asparagine; partial Ref.12 Ref.14 Ref.15 Ref.16
Modified residue1221Phosphoserine Ref.12 Ref.13 Ref.14
Modified residue1231Deamidated asparagine; partial Ref.20
Modified residue1471Deamidated glutamine; partial Ref.14
Glycosylation1621O-linked (GlcNAc) By similarity
Disulfide bond131 ↔ 142 Ref.12 Ref.14

Natural variations

Natural variant121R → C in CTRCT9. Ref.33
VAR_070032
Natural variant211R → L in CTRCT9; associated with macular hypoplasia and a generally hypopigmented fundus. Ref.29
VAR_046892
Natural variant491R → C in CTRCT9; nuclear cataract. Ref.28
VAR_038375
Natural variant1051D → H in a breast cancer sample; somatic mutation. Ref.30
VAR_036564
Natural variant1161R → C in CTRCT9; zonular central nuclear cataract; reduced chaperone-like activity and increased membrane-binding capacity. Ref.26 Ref.27
VAR_003819
Natural variant1161R → H in CTRCT9; reverse phase-high-performance liquid chromatography suggests an increase hydrophobicity of the mutant protein; loss of chaperone activity of the mutant is seen in DL-dithiothreitol-induced insulin aggregation assay; fast protein liquid chromatography purification shows that the mutant protein has increased binding affinity to lysozyme. Ref.31 Ref.32
VAR_046893

Experimental info

Mutagenesis1231N → D: Impairs chaperone activity. Ref.20
Sequence conflict451S → T in AAA52105. Ref.9
Sequence conflict153 – 1553THA → HT Ref.2

Sequences

Sequence LengthMass (Da)Tools
P02489 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 81804A8439837D50

FASTA17319,909
        10         20         30         40         50         60 
MDVTIQHPWF KRTLGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ SLFRTVLDSG 

        70         80         90        100        110        120 
ISEVRSDRDK FVIFLDVKHF SPEDLTVKVQ DDFVEIHGKH NERQDDHGYI SREFHRRYRL 

       130        140        150        160        170 
PSNVDQSALS CSLSADGMLT FCGPKIQTGL DATHAERAIP VSREEKPTSA PSS 

« Hide

References

« Hide 'large scale' references
[1]"The amino acid sequence of the A chain of human alpha-crystallin."
de Jong W.W., Terwindt E.C., Bloemendal H.
FEBS Lett. 58:310-313(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE, ACETYLATION AT MET-1.
[2]"A reassessment of mammalian alpha A-crystallin sequences using DNA sequencing: implications for anthropoid affinities of tarsier."
Jaworski C.J.
J. Mol. Evol. 41:901-908(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lens.
[3]"Cloning, expression, and chaperone-like activity of human alphaA-crystallin."
Andley U.P., Mathur S., Griest T.A., Petrash J.M.
J. Biol. Chem. 271:31973-31980(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lens.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The DNA sequence of human chromosome 21."
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. expand/collapse author list , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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].
Tissue: Colon.
[8]"A pseudo-exon in the functional human alpha A-crystallin gene."
Jaworski C.J., Piatigorsky J.
Nature 337:752-754(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-104.
[9]"Isolation and partial characterization of the human alpha A-crystallin gene."
McDevitt D.S., Hawkins J.W., Jaworski C.J., Piatigorsky J.
Exp. Eye Res. 43:285-291(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-63 AND 166-173.
Tissue: Spleen.
[10]"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: PROTEIN SEQUENCE OF 13-21 AND 79-88.
[11]"Vertebrate lens alpha-crystallins are modified by O-linked N-acetylglucosamine."
Roquemore E.P., Dell A., Morris H.R., Panico M., Reason A.J., Savoy L.-A., Wistow G.J., Zigler J.S. Jr., Earles B.J., Hart G.W.
J. Biol. Chem. 267:555-563(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE OF CARBOHYDRATE.
[12]"Post-translational modifications of water-soluble human lens crystallins from young adults."
Miesbauer L.R., Zhou X., Yang Z., Yang Z., Sun Y., Smith D.L., Smith J.B.
J. Biol. Chem. 269:12494-12502(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-122, DISULFIDE BOND, PROTEOLYTIC PROCESSING OF C-TERMINAL, DEAMIDATION AT ASN-101, MASS SPECTROMETRY.
[13]"Differential phosphorylation of alpha-A crystallin in human lens of different age."
Takemoto L.J.
Exp. Eye Res. 62:499-504(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-122.
[14]"Modifications of the water-insoluble human lens alpha-crystallins."
Lund A.L., Smith J.B., Smith D.L.
Exp. Eye Res. 63:661-672(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING, SUSCEPTIBILITY TO OXIDATION, PHOSPHORYLATION AT SER-45 AND SER-122, DISULFIDE BOND, DEAMIDATION AT GLN-6; GLN-50; GLN-90; ASN-101 AND GLN-147, IDENTIFICATION BY MASS SPECTROMETRY.
[15]"Quantitation of asparagine-101 deamidation from alpha-A crystallin during aging of the human lens."
Takemoto L.J.
Curr. Eye Res. 17:247-250(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: DEAMIDATION AT ASN-101.
[16]"In vivo acetylation identified at lysine 70 of human lens alphaA-crystallin."
Lin P.P., Barry R.C., Smith D.L., Smith J.B.
Protein Sci. 7:1451-1457(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING OF C-TERMINAL, ACETYLATION AT LYS-70, PHOSPHORYLATION, DEAMIDATION AT ASN-101, MASS SPECTROMETRY.
[17]"The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage."
Hanson S.R.A., Hasan A., Smith D.L., Smith J.B.
Exp. Eye Res. 71:195-207(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, SUSCEPTIBILITY TO OXIDATION, PROTEOLYTIC PROCESSING OF C-TERMINAL, MASS SPECTROMETRY.
[18]"Chaperone-like activity of alpha-crystallin and other small heat shock proteins."
Ganea E.
Curr. Protein Pept. Sci. 2:205-225(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[19]"Enhanced C-terminal truncation of alphaA- and alphaB-crystallins in diabetic lenses."
Thampi P., Hassan A., Smith J.B., Abraham E.C.
Invest. Ophthalmol. Vis. Sci. 43:3265-3272(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING, TISSUE SPECIFICITY.
[20]"Structural and functional roles of deamidation and/or truncation of N- or C-termini in human alpha A-crystallin."
Chaves J.M., Srivastava K., Gupta R., Srivastava O.P.
Biochemistry 47:10069-10083(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: DEAMIDATION AT ASN-123, MUTAGENESIS OF ASN-123.
[21]"C-Terminal truncation affects subunit exchange of human alphaA-crystallin with alphaB-crystallin."
Kallur L.S., Aziz A., Abraham E.C.
Mol. Cell. Biochem. 308:85-91(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[22]"HSPB7 is a SC35 speckle resident small heat shock protein."
Vos M.J., Kanon B., Kampinga H.H.
Biochim. Biophys. Acta 1793:1343-1353(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[23]"Importance of eye lens alpha-crystallin heteropolymer with 3:1 alphaA to alphaB ratio: stability, aggregation, and modifications."
Srinivas P., Narahari A., Petrash J.M., Swamy M.J., Reddy G.B.
IUBMB Life 62:693-702(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[24]"Acetylation of alphaA-crystallin in the human lens: effects on structure and chaperone function."
Nagaraj R.H., Nahomi R.B., Shanthakumar S., Linetsky M., Padmanabha S., Pasupuleti N., Wang B., Santhoshkumar P., Panda A.K., Biswas A.
Biochim. Biophys. Acta 1822:120-129(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ACETYLATION AT LYS-70 AND LYS-99.
[25]"Identification of histidine residues involved in Zn(2+) binding to alphaA- and alphaB-Crystallin by chemical modification and MALDI TOF mass spectrometry."
Karmakar S., Das K.P.
Protein J. 31:623-640(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, ZINC-BINDING SITES.
[26]"Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA."
Litt M., Kramer P., la Morticella D.M., Murphey W., Lovrien E.W., Weleber R.G.
Hum. Mol. Genet. 7:471-474(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CTRCT9 CYS-116.
[27]"Structural and functional changes in the alpha A-crystallin R116C mutant in hereditary cataracts."
Cobb B.A., Petrash J.M.
Biochemistry 39:15791-15798(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT CTRCT9 CYS-116.
[28]"Cell death triggered by a novel mutation in the alphaA-crystallin gene underlies autosomal dominant cataract linked to chromosome 21q."
Mackay D.S., Andley U.P., Shiels A.
Eur. J. Hum. Genet. 11:784-793(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CTRCT9 CYS-49.
[29]"Congenital cataract and macular hypoplasia in humans associated with a de novo mutation in CRYAA and compound heterozygous mutations in P."
Graw J., Klopp N., Illig T., Preising M.N., Lorenz B.
Graefes Arch. Clin. Exp. Ophthalmol. 244:912-919(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CTRCT9 LEU-21.
[30]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-105.
[31]"Clinical variability of autosomal dominant cataract, microcornea and corneal opacity and novel mutation in the alpha A crystallin gene (CRYAA)."
Richter L., Flodman P., Barria von-Bischhoffshausen F., Burch D., Brown S., Nguyen L., Turner J., Spence M.A., Bateman J.B.
Am. J. Med. Genet. A 146:833-842(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CTRCT9 HIS-116.
[32]"A novel mutation in AlphaA-crystallin (CRYAA) caused autosomal dominant congenital cataract in a large Chinese family."
Gu F., Luo W., Li X., Wang Z., Lu S., Zhang M., Zhao B., Zhu S., Feng S., Yan Y.-B., Huang S., Ma X.
Hum. Mutat. 29:769-769(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CTRCT9 HIS-116, CHARACTERIZATION OF VARIANT CTRCT9 HIS-116.
[33]"Whole exome sequencing in dominant cataract identifies a new causative factor, CRYBA2, and a variety of novel alleles in known genes."
Reis L.M., Tyler R.C., Muheisen S., Raggio V., Salviati L., Han D.P., Costakos D., Yonath H., Hall S., Power P., Semina E.V.
Hum. Genet. 132:761-770(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CTRCT9 CYS-12.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U05569 mRNA. Translation: AAA97523.1.
U66584 mRNA. Translation: AAC50900.1.
X14789 mRNA. Translation: CAA32891.1.
CR407691 mRNA. Translation: CAG28619.1.
AP001631 Genomic DNA. No translation available.
AP001748 Genomic DNA. Translation: BAA95535.1.
CH471079 Genomic DNA. Translation: EAX09497.1.
CH471079 Genomic DNA. Translation: EAX09498.1.
BC069528 mRNA. Translation: AAH69528.1.
BC113598 mRNA. Translation: AAI13599.1.
M35628 Genomic DNA. Translation: AAA52106.1.
M35629 Genomic DNA. Translation: AAA52105.1.
CCDSCCDS13695.1.
PIRCYHUAA. S03344.
RefSeqNP_000385.1. NM_000394.3.
XP_006723993.1. XM_006723930.1.
XP_006726864.1. XM_006726801.1.
UniGeneHs.184085.

3D structure databases

DisProtDP00444.
ProteinModelPortalP02489.
SMRP02489. Positions 1-171.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107799. 12 interactions.
DIPDIP-41265N.
IntActP02489. 4 interactions.
MINTMINT-220977.
STRING9606.ENSP00000291554.

PTM databases

PhosphoSiteP02489.
UniCarbKBP02489.

Polymorphism databases

DMDM1706112.

2D gel databases

SWISS-2DPAGEP02489.

Proteomic databases

PaxDbP02489.
PeptideAtlasP02489.
PRIDEP02489.

Protocols and materials databases

DNASU1409.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000291554; ENSP00000291554; ENSG00000160202.
GeneID102724652.
1409.
KEGGhsa:1409.
UCSCuc002zdd.1. human.

Organism-specific databases

CTD1409.
GeneCardsGC21P044589.
HGNCHGNC:2388. CRYAA.
MIM123580. gene.
604219. phenotype.
neXtProtNX_P02489.
Orphanet1377. Cataract-microcornea syndrome.
98991. Nuclear cataract.
98995. Zonular cataract.
PharmGKBPA26906.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG278874.
HOGENOMHOG000233954.
HOVERGENHBG054766.
InParanoidP02489.
KOK09541.
OMAGPKVQSG.
OrthoDBEOG7WHHBK.
PhylomeDBP02489.
TreeFamTF105049.

Gene expression databases

ArrayExpressP02489.
BgeeP02489.
CleanExHS_CRYAA.
GenevestigatorP02489.

Family and domain databases

Gene3D2.60.40.790. 1 hit.
InterProIPR002068. a-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR012274. Alpha-crystallin_A.
IPR003090. Alpha-crystallin_N.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PANTHERPTHR11527:SF36. PTHR11527:SF36. 1 hit.
PfamPF00525. Crystallin. 1 hit.
PF00011. HSP20. 1 hit.
[Graphical view]
PIRSFPIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSPR00299. ACRYSTALLIN.
SUPFAMSSF49764. SSF49764. 1 hit.
PROSITEPS01031. HSP20. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCRYAA.
GenomeRNAi1409.
NextBio5761.
PROP02489.
SOURCESearch...

Entry information

Entry nameCRYAA_HUMAN
AccessionPrimary (citable) accession number: P02489
Secondary accession number(s): Q53X53
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM