Skip Header

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

UniProtKB - A0A140G945 (CRYA2_HUMAN)

Protein

Alpha-crystallin A2 chain

Gene

CRYAA2

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

View the complete GO annotation on QuickGO ...

<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

LigandMetal-binding, Zinc

<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 A2 chainCurated
Cleaved into the following 3 chains:
Alpha-crystallin A2(1-172)
Alpha-crystallin A2(1-168)
Alpha-crystallin A2(1-162)
<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:CRYAA2Imported
Synonyms:CRYAAImported
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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

More...EuPathDBi		HostDB:ENSG00000160202.7
HostDB:ENSG00000276076.4

Human Gene Nomenclature Database

More...HGNCi		HGNC:51901 CRYAA2

neXtProt; the human protein knowledge platform

More...neXtProti		NX_A0A140G945

<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; 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

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

Organism-specific databases

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		604219 phenotype

Open Targets

More...OpenTargetsi		ENSG00000160202

<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_00004445071 – 173Alpha-crystallin A2 chainAdd BLAST173
ChainiPRO_00004445081 – 172Alpha-crystallin A2(1-172)By similarityAdd BLAST172
ChainiPRO_00004445091 – 168Alpha-crystallin A2(1-168)By similarityAdd BLAST168
ChainiPRO_00004445101 – 162Alpha-crystallin A2(1-162)By similarityAdd 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, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		A0A140G945

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		A0A140G945 baseline and differential

<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 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

More...ProteinModelPortali		A0A140G945

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

More...SMRi		A0A140G945

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...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

More...eggNOGi		KOG3591 Eukaryota
ENOG410YERS LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000160159

KEGG Orthology (KO)

More...KOi		K09541

Identification of Orthologs from Complete Genome Data

More...OMAi		GERQDDH

Database of Orthologous Groups

More...OrthoDBi		1187096at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		A0A140G945

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.60.40.790, 1 hit

Integrated resource of protein families, domains and functional sites

More...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

More...PANTHERi		PTHR11527 PTHR11527, 1 hit
PTHR11527:SF36 PTHR11527:SF36, 1 hit

Pfam protein domain database

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

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF036514 Sm_HSP_B1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...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>Sequences (2+)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 describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: A0A140G945-1) [UniParc]FASTAAdd to basket

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

« Hide
        10         20         30         40         50
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:May 11, 2016 - v1
<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
Isoform 2 (identifier: A0A140G945-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-63: MDVTIQHPWF...RTVLDSGISE → MPVCPGDSHRPPKALPHLVCGRRGRQ

Note: Gene prediction based on EST data.Curated
Show »
Length:136
Mass (Da):15,316
Checksum:i23F971F4BB43EC62
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
A0A096LPJ9A0A096LPJ9_HUMAN
Alpha-crystallin A2 chain
CRYAA2
127Annotation 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>

<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

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0596041 – 63MDVTI…SGISE → MPVCPGDSHRPPKALPHLVC GRRGRQ in isoform 2. Add BLAST63

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
KM220588 mRNA Translation: AMM63583.1
KM220589 mRNA Translation: AMM63584.1
KM220590 mRNA Translation: AMM63585.1
KM220591 mRNA Translation: AMM63586.1
KM220592 mRNA Translation: AMM63587.1
AP001631 Genomic DNA No translation available.
FP236240 Genomic DNA No translation available.

The Consensus CDS (CCDS) project

More...CCDSi		CCDS82651.1 [A0A140G945-1]
CCDS82652.1 [A0A140G945-2]

NCBI Reference Sequences

More...RefSeqi		NP_000385.1, NM_000394.3 [A0A140G945-1]
NP_001300979.1, NM_001314050.2 [A0A140G945-1]
NP_001307648.1, NM_001320719.1 [A0A140G945-2]
XP_005261150.1, XM_005261093.3

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.184085

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000619537; ENSP00000482816; ENSG00000276076 [A0A140G945-1]
ENST00000624932; ENSP00000485302; ENSG00000276076 [A0A140G945-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		102724652
1409

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:102724652
hsa:1409

UCSC genome browser

More...UCSCi		uc061ywn.1 human

Keywords - Coding sequence diversityi

Alternative splicing

<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
KM220588 mRNA Translation: AMM63583.1
KM220589 mRNA Translation: AMM63584.1
KM220590 mRNA Translation: AMM63585.1
KM220591 mRNA Translation: AMM63586.1
KM220592 mRNA Translation: AMM63587.1
AP001631 Genomic DNA No translation available.
FP236240 Genomic DNA No translation available.
CCDSiCCDS82651.1 [A0A140G945-1]
CCDS82652.1 [A0A140G945-2]
RefSeqiNP_000385.1, NM_000394.3 [A0A140G945-1]
NP_001300979.1, NM_001314050.2 [A0A140G945-1]
NP_001307648.1, NM_001320719.1 [A0A140G945-2]
XP_005261150.1, XM_005261093.3
UniGeneiHs.184085

3D structure databases

ProteinModelPortaliA0A140G945
SMRiA0A140G945
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiA0A140G945

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000619537; ENSP00000482816; ENSG00000276076 [A0A140G945-1]
ENST00000624932; ENSP00000485302; ENSG00000276076 [A0A140G945-2]
GeneIDi102724652
1409
KEGGihsa:102724652
hsa:1409
UCSCiuc061ywn.1 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		102724652
1409
EuPathDBiHostDB:ENSG00000160202.7
HostDB:ENSG00000276076.4

GeneCards: human genes, protein and diseases

More...GeneCardsi		CRYAA2
HGNCiHGNC:51901 CRYAA2
MIMi604219 phenotype
neXtProtiNX_A0A140G945
OpenTargetsiENSG00000160202

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3591 Eukaryota
ENOG410YERS LUCA
GeneTreeiENSGT00940000160159
KOiK09541
OMAiGERQDDH
OrthoDBi1187096at2759
PhylomeDBiA0A140G945

Miscellaneous databases

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000160202 Expressed in 27 organ(s), highest expression level in adult mammalian kidney
ExpressionAtlasiA0A140G945 baseline and differential

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

More...ProtoNeti		Search...

<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 nameiCRYA2_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: A0A140G945
Secondary accession number(s): E9PHE4
<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: June 20, 2018
Last sequence update: May 11, 2016
Last modified: January 16, 2019
This is version 26 of the entry and version 1 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 chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again