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Protein

Alpha-crystallin A2 chain

Gene

CRYAA2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Sitei1Susceptible to oxidation1
Sitei18Susceptible to oxidation1
Sitei34Susceptible to oxidation1
Metal bindingi79Zinc 1Curated1
Metal bindingi100Zinc 2By similarity1
Metal bindingi102Zinc 2By similarity1
Metal bindingi107Zinc 1Curated1
Metal bindingi115Zinc 1Curated1
Sitei138Susceptible to oxidation1

GO - Molecular functioni

Keywordsi

LigandMetal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-crystallin A2 chainCurated
Cleaved into the following 3 chains:
Gene namesi
Name:CRYAA2Imported
Synonyms:CRYAAImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 21

Organism-specific databases

EuPathDBiHostDB:ENSG00000160202.7
HostDB:ENSG00000276076.4
HGNCiHGNC:51901 CRYAA2
neXtProtiNX_A0A140G945

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi123N → D: Impairs chaperone activity. 1 Publication1

Keywords - Diseasei

Cataract

Organism-specific databases

MIMi604219 phenotype
OpenTargetsiENSG00000160202

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
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
Disulfide bondi131 ↔ 1422 Publications
Modified residuei147Deamidated glutamine; partial1 Publication1
Glycosylationi162O-linked (GlcNAc) serineBy similarity1

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

PRIDEiA0A140G945

Expressioni

Gene expression databases

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

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

Structurei

3D structure databases

ProteinModelPortaliA0A140G945
SMRiA0A140G945
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini52 – 164sHSPPROSITE-ProRule annotationAdd BLAST113

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3591 Eukaryota
ENOG410YERS LUCA
GeneTreeiENSGT00760000119238
KOiK09541
OMAiGERQDDH
PhylomeDBiA0A140G945

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

Sequences (2+)i

Sequence statusi: Complete.

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

This entry describes 2 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
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

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:

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
Alternative sequenceiVSP_0596041 – 63MDVTI…SGISE → MPVCPGDSHRPPKALPHLVC GRRGRQ in isoform 2. Add BLAST63

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

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

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

CTDi102724652
1409
EuPathDBiHostDB:ENSG00000160202.7
HostDB:ENSG00000276076.4
GeneCardsiCRYAA2
HGNCiHGNC:51901 CRYAA2
MIMi604219 phenotype
neXtProtiNX_A0A140G945
OpenTargetsiENSG00000160202
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3591 Eukaryota
ENOG410YERS LUCA
GeneTreeiENSGT00760000119238
KOiK09541
OMAiGERQDDH
PhylomeDBiA0A140G945

Miscellaneous databases

SOURCEiSearch...

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
ProtoNetiSearch...

Entry informationi

Entry nameiCRYA2_HUMAN
AccessioniPrimary (citable) accession number: A0A140G945
Secondary accession number(s): E9PHE4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 20, 2018
Last sequence update: May 11, 2016
Last modified: November 7, 2018
This is version 24 of the entry and version 1 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Human chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
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Main funding by: National Institutes of Health

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