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Protein

Alpha-crystallin A chain

Gene

CRYAA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei1 – 11Susceptible to oxidation
Sitei18 – 181Susceptible to oxidation
Sitei34 – 341Susceptible to oxidation
Metal bindingi79 – 791Zinc 1Curated
Metal bindingi100 – 1001Zinc 2By similarity
Metal bindingi102 – 1021Zinc 2By similarity
Metal bindingi107 – 1071Zinc 1Curated
Metal bindingi115 – 1151Zinc 1Curated
Sitei138 – 1381Susceptible to oxidation

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. metal ion binding Source: UniProtKB-KW
  3. structural constituent of eye lens Source: UniProtKB-KW
  4. unfolded protein binding Source: UniProtKB

GO - Biological processi

  1. negative regulation of apoptotic process Source: UniProtKB
  2. negative regulation of intracellular transport Source: HGNC
  3. protein homooligomerization Source: UniProtKB
  4. response to stimulus Source: UniProtKB-KW
  5. visual perception Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Eye lens protein

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-crystallin A chain
Alternative name(s):
Heat shock protein beta-4
Short name:
HspB4
Cleaved into the following 3 chains:
Gene namesi
Name:CRYAA
Synonyms:CRYA1, HSPB4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 21

Organism-specific databases

HGNCiHGNC:2388. CRYAA.

Subcellular locationi

  1. Cytoplasm 1 Publication
  2. Nucleus 1 Publication

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProtKB
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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

Cataract 9, multiple types (CTRCT9)6 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. 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.

See also OMIM:604219
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121R → C in CTRCT9. 1 Publication
VAR_070032
Natural varianti21 – 211R → L in CTRCT9; associated with macular hypoplasia and a generally hypopigmented fundus. 1 Publication
VAR_046892
Natural varianti49 – 491R → C in CTRCT9; nuclear cataract. 1 Publication
VAR_038375
Natural varianti116 – 1161R → C in CTRCT9; zonular central nuclear cataract; reduced chaperone-like activity and increased membrane-binding capacity. 2 Publications
VAR_003819
Natural varianti116 – 1161R → 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. 2 Publications
VAR_046893

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi123 – 1231N → D: Impairs chaperone activity. 1 Publication

Keywords - Diseasei

Cataract, Disease mutation

Organism-specific databases

MIMi604219. phenotype.
Orphaneti1377. Cataract-microcornea syndrome.
98991. Nuclear cataract.
98995. Zonular cataract.
PharmGKBiPA26906.

Polymorphism and mutation databases

BioMutaiCRYAA.
DMDMi1706112.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 173173Alpha-crystallin A chainPRO_0000125865Add
BLAST
Chaini1 – 172172Alpha-crystallin A(1-172)PRO_0000226639Add
BLAST
Chaini1 – 168168Alpha-crystallin A(1-168)PRO_0000423503Add
BLAST
Chaini1 – 162162Alpha-crystallin A(1-162)PRO_0000423504Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei6 – 61Deamidated glutamine; partial1 Publication
Modified residuei45 – 451Phosphoserine1 Publication
Modified residuei50 – 501Deamidated glutamine; partial1 Publication
Modified residuei70 – 701N6-acetyllysine2 Publications
Modified residuei90 – 901Deamidated glutamine; partial1 Publication
Modified residuei99 – 991N6-acetyllysine1 Publication
Modified residuei101 – 1011Deamidated asparagine; partial4 Publications
Modified residuei122 – 1221Phosphoserine3 Publications
Modified residuei123 – 1231Deamidated asparagine; partial1 Publication
Disulfide bondi131 ↔ 1422 Publications
Modified residuei147 – 1471Deamidated glutamine; partial1 Publication
Glycosylationi162 – 1621O-linked (GlcNAc)By similarity

Post-translational modificationi

O-glycosylated; contains N-acetylglucosamine side chains.
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.5 Publications
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.5 Publications
Acetylation at Lys-70 seems to increase chaperone activity.3 Publications
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.5 Publications

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Oxidation, Phosphoprotein

Proteomic databases

PaxDbiP02489.
PeptideAtlasiP02489.
PRIDEiP02489.

2D gel databases

SWISS-2DPAGEP02489.

PTM databases

PhosphoSiteiP02489.
UniCarbKBiP02489.

Expressioni

Tissue specificityi

Expressed in eye lens.1 Publication

Gene expression databases

BgeeiP02489.
CleanExiHS_CRYAA.
ExpressionAtlasiP02489. baseline.
GenevestigatoriP02489.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-6875961,EBI-6875961
CRYABP025117EBI-6875961,EBI-739060
CRYGCP073153EBI-6875961,EBI-6875941
GORASP2Q9H8Y84EBI-6875961,EBI-739467
HEL-S-101V9HW273EBI-6875961,EBI-10178933
SDCBPO005603EBI-6875961,EBI-727004
SPG21Q9NZD83EBI-6875961,EBI-742688
WDYHV1Q96HA83EBI-6875961,EBI-741158

Protein-protein interaction databases

BioGridi107799. 16 interactions.
DIPiDIP-41265N.
IntActiP02489. 9 interactions.
MINTiMINT-220977.
STRINGi9606.ENSP00000291554.

Structurei

3D structure databases

DisProtiDP00444.
ProteinModelPortaliP02489.
SMRiP02489. Positions 1-171.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the small heat shock protein (HSP20) family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG278874.
GeneTreeiENSGT00760000119238.
HOGENOMiHOG000233954.
HOVERGENiHBG054766.
InParanoidiP02489.
KOiK09541.
OMAiGPKVQSG.
OrthoDBiEOG7WHHBK.
PhylomeDBiP02489.
TreeFamiTF105049.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR002068. A-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR012274. Alpha-crystallin_A.
IPR003090. Alpha-crystallin_N.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PANTHERiPTHR11527:SF36. PTHR11527:SF36. 1 hit.
PfamiPF00525. Crystallin. 1 hit.
PF00011. HSP20. 1 hit.
[Graphical view]
PIRSFiPIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSiPR00299. ACRYSTALLIN.
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS01031. HSP20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P02489-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDVTIQHPWF KRTLGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ
60 70 80 90 100
SLFRTVLDSG ISEVRSDRDK FVIFLDVKHF SPEDLTVKVQ DDFVEIHGKH
110 120 130 140 150
NERQDDHGYI SREFHRRYRL PSNVDQSALS CSLSADGMLT FCGPKIQTGL
160 170
DATHAERAIP VSREEKPTSA PSS
Length:173
Mass (Da):19,909
Last modified:October 1, 1996 - v2
Checksum:i81804A8439837D50
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451S → T in AAA52105 (PubMed:3758227).Curated
Sequence conflicti153 – 1553THA → HT (PubMed:8587135).Curated

Mass spectrometryi

Molecular mass is 19950 Da from positions 1 - 173. Determined by ESI. 1 Publication
Molecular mass is 19863 Da from positions 1 - 172. Determined by ESI. 1 Publication
Molecular mass is 20029 Da from positions 1 - 173. Determined by ESI. With 1 phosphate group.1 Publication
Molecular mass is 19951 Da from positions 1 - 173. Determined by ESI. 1 Publication
Molecular mass is 19864 Da from positions 1 - 172. Determined by ESI. 1 Publication
Molecular mass is 19947 Da from positions 1 - 173. Determined by ESI. 1 Publication
Molecular mass is 19851 Da from positions 1 - 172. Determined by ESI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121R → C in CTRCT9. 1 Publication
VAR_070032
Natural varianti21 – 211R → L in CTRCT9; associated with macular hypoplasia and a generally hypopigmented fundus. 1 Publication
VAR_046892
Natural varianti49 – 491R → C in CTRCT9; nuclear cataract. 1 Publication
VAR_038375
Natural varianti105 – 1051D → H in a breast cancer sample; somatic mutation. 1 Publication
VAR_036564
Natural varianti116 – 1161R → C in CTRCT9; zonular central nuclear cataract; reduced chaperone-like activity and increased membrane-binding capacity. 2 Publications
VAR_003819
Natural varianti116 – 1161R → 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. 2 Publications
VAR_046893

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13695.1.
PIRiS03344. CYHUAA.
RefSeqiNP_000385.1. NM_000394.3.
XP_006723993.1. XM_006723930.2.
XP_006726864.1. XM_006726801.2.
UniGeneiHs.184085.

Genome annotation databases

EnsembliENST00000291554; ENSP00000291554; ENSG00000160202.
ENST00000619537; ENSP00000482816; ENSG00000276076.
GeneIDi102724652.
1409.
KEGGihsa:102724652.
hsa:1409.
UCSCiuc002zdd.1. human.

Polymorphism and mutation databases

BioMutaiCRYAA.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13695.1.
PIRiS03344. CYHUAA.
RefSeqiNP_000385.1. NM_000394.3.
XP_006723993.1. XM_006723930.2.
XP_006726864.1. XM_006726801.2.
UniGeneiHs.184085.

3D structure databases

DisProtiDP00444.
ProteinModelPortaliP02489.
SMRiP02489. Positions 1-171.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107799. 16 interactions.
DIPiDIP-41265N.
IntActiP02489. 9 interactions.
MINTiMINT-220977.
STRINGi9606.ENSP00000291554.

PTM databases

PhosphoSiteiP02489.
UniCarbKBiP02489.

Polymorphism and mutation databases

BioMutaiCRYAA.
DMDMi1706112.

2D gel databases

SWISS-2DPAGEP02489.

Proteomic databases

PaxDbiP02489.
PeptideAtlasiP02489.
PRIDEiP02489.

Protocols and materials databases

DNASUi1409.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000291554; ENSP00000291554; ENSG00000160202.
ENST00000619537; ENSP00000482816; ENSG00000276076.
GeneIDi102724652.
1409.
KEGGihsa:102724652.
hsa:1409.
UCSCiuc002zdd.1. human.

Organism-specific databases

CTDi1409.
GeneCardsiGC21P044589.
HGNCiHGNC:2388. CRYAA.
MIMi123580. gene.
604219. phenotype.
neXtProtiNX_P02489.
Orphaneti1377. Cataract-microcornea syndrome.
98991. Nuclear cataract.
98995. Zonular cataract.
PharmGKBiPA26906.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG278874.
GeneTreeiENSGT00760000119238.
HOGENOMiHOG000233954.
HOVERGENiHBG054766.
InParanoidiP02489.
KOiK09541.
OMAiGPKVQSG.
OrthoDBiEOG7WHHBK.
PhylomeDBiP02489.
TreeFamiTF105049.

Miscellaneous databases

GeneWikiiCRYAA.
NextBioi5761.
PROiP02489.
SOURCEiSearch...

Gene expression databases

BgeeiP02489.
CleanExiHS_CRYAA.
ExpressionAtlasiP02489. baseline.
GenevestigatoriP02489.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR002068. A-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR012274. Alpha-crystallin_A.
IPR003090. Alpha-crystallin_N.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PANTHERiPTHR11527:SF36. PTHR11527:SF36. 1 hit.
PfamiPF00525. Crystallin. 1 hit.
PF00011. HSP20. 1 hit.
[Graphical view]
PIRSFiPIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSiPR00299. ACRYSTALLIN.
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS01031. HSP20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiCRYAA_HUMAN
AccessioniPrimary (citable) accession number: P02489
Secondary accession number(s): Q53X53
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1996
Last modified: April 29, 2015
This is version 165 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 21
    Human chromosome 21: 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. 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.