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Entry version 204 (10 Apr 2019)
Sequence version 2 (01 Oct 1996)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei1Susceptible to oxidation1
Sitei18Susceptible to oxidation1
Sitei34Susceptible to oxidation1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi79Zinc 1Curated1
Metal bindingi100Zinc 2By similarity1
Metal bindingi102Zinc 2By similarity1
Metal bindingi107Zinc 1Curated1
Metal bindingi115Zinc 1Curated1
Sitei138Susceptible to oxidation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChaperone, Eye lens protein
Biological processSensory transduction, Vision
LigandMetal-binding, Zinc

Enzyme and pathway databases

SIGNOR Signaling Network Open Resource

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SIGNORi
P02489

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
P02489 Curated

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CRYAA
Synonyms:CRYA1, HSPB4
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 21

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000160202.7

Human Gene Nomenclature Database

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HGNCi
HGNC:2388 CRYAA

Online Mendelian Inheritance in Man (OMIM)

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MIMi
123580 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P02489

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Alpha-crystallin A 1-172 is found at nearly twofold higher levels in diabetic lenses than in age-matched control lenses.1 Publication
Cataract 9, multiple types (CTRCT9)7 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)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_07003212R → C in CTRCT9. 1 PublicationCorresponds to variant dbSNP:rs397515624EnsemblClinVar.1
Natural variantiVAR_04689221R → L in CTRCT9; associated with macular hypoplasia and a generally hypopigmented fundus. 1 Publication1
Natural variantiVAR_03837549R → C in CTRCT9; nuclear cataract. 1 PublicationCorresponds to variant dbSNP:rs74315441EnsemblClinVar.1
Natural variantiVAR_003819116R → C in CTRCT9; zonular central nuclear cataract; reduced chaperone-like activity and increased membrane-binding capacity. 2 PublicationsCorresponds to variant dbSNP:rs74315439EnsemblClinVar.1
Natural variantiVAR_046893116R → 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 PublicationsCorresponds to variant dbSNP:rs121912973EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi123N → D: Impairs chaperone activity. 1 Publication1

Keywords - Diseasei

Cataract, Disease mutation

Organism-specific databases

DisGeNET

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DisGeNETi
102724652
1409

MalaCards human disease database

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MalaCardsi
CRYAA
MIMi604219 phenotype

Open Targets

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OpenTargetsi
ENSG00000160202

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
1377 Cataract-microcornea syndrome
98988 Early-onset anterior polar cataract
441452 Early-onset lamellar cataract
98991 Early-onset nuclear cataract
98994 Total early-onset cataract

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA26906

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
CRYAA

Domain mapping of disease mutations (DMDM)

More...
DMDMi
1706112

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001258651 – 173Alpha-crystallin A chainAdd BLAST173
ChainiPRO_00002266391 – 172Alpha-crystallin A(1-172)Add BLAST172
ChainiPRO_00004235031 – 168Alpha-crystallin A(1-168)Add BLAST168
ChainiPRO_00004235041 – 162Alpha-crystallin A(1-162)Add BLAST162

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionine1 Publication1
Modified residuei6Deamidated glutamine; partial1 Publication1
Modified residuei45Phosphoserine1 Publication1
Modified residuei50Deamidated glutamine; partial1 Publication1
Modified residuei70N6-acetyllysine2 Publications1
Modified residuei90Deamidated glutamine; partial1 Publication1
Modified residuei99N6-acetyllysine1 Publication1
Modified residuei101Deamidated asparagine; partial4 Publications1
Modified residuei122Phosphoserine3 Publications1
Modified residuei123Deamidated asparagine; partial1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi131 ↔ 1422 Publications
Modified residuei147Deamidated glutamine; partial1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi162O-linked (GlcNAc) serineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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 approximately 50% of the lens molecules.5 Publications

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Oxidation, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P02489

PeptideAtlas

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PeptideAtlasi
P02489

PRoteomics IDEntifications database

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PRIDEi
P02489

ProteomicsDB human proteome resource

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ProteomicsDBi
51526

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P02489

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
33

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P02489

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P02489

UniCarbKB; an annotated and curated database of glycan structures

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UniCarbKBi
P02489

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in eye lens.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000160202 Expressed in 27 organ(s), highest expression level in adult mammalian kidney

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P02489 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P02489 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA037737
HPA038430

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
107799, 68 interactors

Database of interacting proteins

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DIPi
DIP-41265N

Protein interaction database and analysis system

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IntActi
P02489, 9 interactors

Molecular INTeraction database

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MINTi
P02489

STRING: functional protein association networks

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STRINGi
9606.ENSP00000482816

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P02489

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P02489

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini52 – 164sHSPPROSITE-ProRule annotationAdd BLAST113

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3591 Eukaryota
ENOG410YERS LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000160159

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000233954

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG054766

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P02489

KEGG Orthology (KO)

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KOi
K09541

Identification of Orthologs from Complete Genome Data

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OMAi
GERQDDH

Database of Orthologous Groups

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OrthoDBi
1187096at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P02489

TreeFam database of animal gene trees

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TreeFami
TF105049

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.790, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR002068 A-crystallin/Hsp20_dom
IPR001436 Alpha-crystallin/HSP
IPR012274 Alpha-crystallin_A
IPR003090 Alpha-crystallin_N
IPR031107 HSP20
IPR008978 HSP20-like_chaperone

The PANTHER Classification System

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PANTHERi
PTHR11527 PTHR11527, 1 hit
PTHR11527:SF36 PTHR11527:SF36, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00525 Crystallin, 1 hit
PF00011 HSP20, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF036514 Sm_HSP_B1, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00299 ACRYSTALLIN

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49764 SSF49764, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01031 SHSP, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i81804A8439837D50
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E7EWH7E7EWH7_HUMAN
Alpha-crystallin A chain
CRYAA
153Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti45S → T in AAA52105 (PubMed:3758227).Curated1
Sequence conflicti153 – 155THA → HT (PubMed:8587135).Curated3

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>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)DescriptionActionsGraphical viewLength
Natural variantiVAR_07003212R → C in CTRCT9. 1 PublicationCorresponds to variant dbSNP:rs397515624EnsemblClinVar.1
Natural variantiVAR_04689221R → L in CTRCT9; associated with macular hypoplasia and a generally hypopigmented fundus. 1 Publication1
Natural variantiVAR_03837549R → C in CTRCT9; nuclear cataract. 1 PublicationCorresponds to variant dbSNP:rs74315441EnsemblClinVar.1
Natural variantiVAR_036564105D → H in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_003819116R → C in CTRCT9; zonular central nuclear cataract; reduced chaperone-like activity and increased membrane-binding capacity. 2 PublicationsCorresponds to variant dbSNP:rs74315439EnsemblClinVar.1
Natural variantiVAR_046893116R → 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 PublicationsCorresponds to variant dbSNP:rs121912973EnsemblClinVar.1

Sequence databases

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EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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

The Consensus CDS (CCDS) project

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CCDSi
CCDS13695.1

Protein sequence database of the Protein Information Resource

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PIRi
S03344 CYHUAA

NCBI Reference Sequences

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RefSeqi
NP_000385.1, NM_000394.3
NP_001300979.1, NM_001314050.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.184085

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000291554; ENSP00000291554; ENSG00000160202

Database of genes from NCBI RefSeq genomes

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GeneIDi
102724652
1409

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:102724652
hsa:1409

UCSC genome browser

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UCSCi
uc002zdd.3 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
NP_001300979.1, NM_001314050.2
UniGeneiHs.184085

3D structure databases

ProteinModelPortaliP02489
SMRiP02489
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107799, 68 interactors
DIPiDIP-41265N
IntActiP02489, 9 interactors
MINTiP02489
STRINGi9606.ENSP00000482816

Protein family/group databases

MoonDBiP02489 Curated

PTM databases

GlyConnecti33
iPTMnetiP02489
PhosphoSitePlusiP02489
UniCarbKBiP02489

Polymorphism and mutation databases

BioMutaiCRYAA
DMDMi1706112

2D gel databases

SWISS-2DPAGEiP02489

Proteomic databases

PaxDbiP02489
PeptideAtlasiP02489
PRIDEiP02489
ProteomicsDBi51526

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
1409
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000291554; ENSP00000291554; ENSG00000160202
GeneIDi102724652
1409
KEGGihsa:102724652
hsa:1409
UCSCiuc002zdd.3 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
102724652
1409
DisGeNETi102724652
1409
EuPathDBiHostDB:ENSG00000160202.7

GeneCards: human genes, protein and diseases

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GeneCardsi
CRYAA
HGNCiHGNC:2388 CRYAA
HPAiHPA037737
HPA038430
MalaCardsiCRYAA
MIMi123580 gene
604219 phenotype
neXtProtiNX_P02489
OpenTargetsiENSG00000160202
Orphaneti1377 Cataract-microcornea syndrome
98988 Early-onset anterior polar cataract
441452 Early-onset lamellar cataract
98991 Early-onset nuclear cataract
98994 Total early-onset cataract
PharmGKBiPA26906

GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

eggNOGiKOG3591 Eukaryota
ENOG410YERS LUCA
GeneTreeiENSGT00940000160159
HOGENOMiHOG000233954
HOVERGENiHBG054766
InParanoidiP02489
KOiK09541
OMAiGERQDDH
OrthoDBi1187096at2759
PhylomeDBiP02489
TreeFamiTF105049

Enzyme and pathway databases

SIGNORiP02489

Miscellaneous databases

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
CRYAA

Protein Ontology

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PROi
PR:P02489

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSG00000160202 Expressed in 27 organ(s), highest expression level in adult mammalian kidney
ExpressionAtlasiP02489 baseline and differential
GenevisibleiP02489 HS

Family and domain databases

Gene3Di2.60.40.790, 1 hit
InterProiView protein in InterPro
IPR002068 A-crystallin/Hsp20_dom
IPR001436 Alpha-crystallin/HSP
IPR012274 Alpha-crystallin_A
IPR003090 Alpha-crystallin_N
IPR031107 HSP20
IPR008978 HSP20-like_chaperone
PANTHERiPTHR11527 PTHR11527, 1 hit
PTHR11527:SF36 PTHR11527:SF36, 1 hit
PfamiView protein in Pfam
PF00525 Crystallin, 1 hit
PF00011 HSP20, 1 hit
PIRSFiPIRSF036514 Sm_HSP_B1, 1 hit
PRINTSiPR00299 ACRYSTALLIN
SUPFAMiSSF49764 SSF49764, 1 hit
PROSITEiView protein in PROSITE
PS01031 SHSP, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCRYAA_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P02489
Secondary accession number(s): Q53X53
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1996
Last modified: April 10, 2019
This is version 204 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. Human chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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