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P23927 (CRYAB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-crystallin B chain
Alternative name(s):
Alpha(B)-crystallin
P23
Gene names
Name:Cryab
Synonyms:Crya2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length175 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May contribute 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.

Subunit structure

Heteropolymer composed of three CRYAA and one CRYAB subunits. Aggregates with homologous proteins, including the small heat shock protein HSPB1, to form large heteromeric complexes. Inter-subunit bridging via zinc ions enhances stability, which is crucial as there is no protein turn over in the lens. Interacts with HSPBAP1 and TTN/titin By similarity. Ref.6

Subcellular location

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

Tissue specificity

Lens as well as other tissues.

Sequence similarities

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

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   LigandMetal-binding
Zinc
   Molecular functionChaperone
Eye lens protein
   PTMAcetylation
Methylation
Oxidation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

apoptotic process involved in morphogenesis

Inferred from genetic interaction PubMed 16439475. Source: MGI

camera-type eye development

Inferred from genetic interaction PubMed 12546709. Source: MGI

cellular response to gamma radiation

Inferred from sequence orthology PubMed 23542032. Source: MGI

glucose metabolic process

Inferred from electronic annotation. Source: Ensembl

lens development in camera-type eye

Inferred from genetic interaction PubMed 16439475. Source: MGI

microtubule polymerization or depolymerization

Inferred from electronic annotation. Source: Ensembl

muscle organ development

Inferred from genetic interaction PubMed 11687538. Source: MGI

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 18191123. Source: MGI

negative regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

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

Inferred from genetic interaction PubMed 16439475. Source: MGI

negative regulation of gene expression

Inferred from mutant phenotype PubMed 17893660. Source: MGI

negative regulation of intracellular transport

Inferred from electronic annotation. Source: Ensembl

negative regulation of reactive oxygen species metabolic process

Inferred from electronic annotation. Source: Ensembl

protein folding

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

regulation of cell death

Inferred from sequence orthology PubMed 23542032. Source: MGI

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to hydrogen peroxide

Inferred from mutant phenotype PubMed 17438522. Source: MGI

response to hypoxia

Inferred from mutant phenotype PubMed 18191123. Source: MGI

stress-activated MAPK cascade

Inferred from electronic annotation. Source: Ensembl

tubulin complex assembly

Inferred from mutant phenotype PubMed 16675842. Source: MGI

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

Z disc

Inferred from direct assay PubMed 14627610. Source: MGI

actin filament bundle

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from electronic annotation. Source: Ensembl

contractile fiber

Inferred from direct assay PubMed 14627610. Source: MGI

cytosol

Inferred from direct assay PubMed 18191123. Source: MGI

microtubule cytoskeleton

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from direct assay PubMed 18191123. Source: MGI

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 14627610. Source: MGI

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 22289178. Source: IntAct

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

structural constituent of eye lens

Traceable author statement PubMed 12546709. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CRYGDP073202EBI-299046,EBI-7673124From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 175175Alpha-crystallin B chain
PRO_0000125910

Sites

Metal binding831Zinc 1 By similarity
Metal binding1041Zinc 2 By similarity
Metal binding1061Zinc 2 By similarity
Metal binding1111Zinc 1 By similarity
Metal binding1191Zinc 1 By similarity
Site481Susceptible to oxidation By similarity
Site601Susceptible to oxidation By similarity
Site681Susceptible to oxidation By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Probable
Modified residue191Phosphoserine By similarity
Modified residue221Omega-N-methylated arginine By similarity
Modified residue451Phosphoserine By similarity
Modified residue501Omega-N-methylated arginine By similarity
Modified residue591Phosphoserine By similarity
Modified residue921N6-acetyllysine By similarity
Modified residue1661N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P23927 [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: 46702976C008EFD3

FASTA17520,069
        10         20         30         40         50         60 
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFST ATSLSPFYLR PPSFLRAPSW 

        70         80         90        100        110        120 
IDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR 

       130        140        150        160        170 
KYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVA AAPKK 

« Hide

References

« Hide 'large scale' references
[1]"Alpha B crystallin accumulation is a specific response to Ha-ras and v-mos oncogene expression in mouse NIH 3T3 fibroblasts."
Klemenz R., Froehli E., Aoyama A., Hoffmann S., Simpson R.J., Moritz R.L., Schaeffer R.
Mol. Cell. Biol. 11:803-812(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-10 AND 68-81.
[2]"Structure and alternate tissue-preferred transcription initiation of the mouse alpha B-crystallin/small heat shock protein gene."
Frederikse P.H., Dubin R.A., Haynes J.I., Piatigorsky J.
Nucleic Acids Res. 22:5686-5694(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BALB/c.
Tissue: Lung.
[3]"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].
Strain: FVB/N.
Tissue: Kidney.
[4]"Expression of the murine alpha B-crystallin gene is not restricted to the lens."
Dubin R.A., Wawrousek E.F., Piatigorsky J.
Mol. Cell. Biol. 9:1083-1091(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
[5]Lubec G., Klug S.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 12-22 AND 124-149, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hippocampus.
[6]"Identification and characterization of a novel protein from Sertoli cells, PASS1, that associates with mammalian small stress protein hsp27."
Liu C., Gilmont R.R., Benndorf R., Welsh M.J.
J. Biol. Chem. 275:18724-18731(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HSPBAP1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M63170 mRNA. Translation: AAA37472.1.
M73741 Genomic DNA. Translation: AAA67045.1.
BC010768 mRNA. Translation: AAH10768.1.
M25770 Genomic DNA. Translation: AAA37133.1.
CCDSCCDS23172.1.
PIRA39608.
RefSeqNP_001276711.1. NM_001289782.1.
NP_001276713.1. NM_001289784.1.
NP_001276714.1. NM_001289785.1.
NP_034094.1. NM_009964.3.
XP_006510033.1. XM_006509970.1.
UniGeneMm.178.

3D structure databases

ProteinModelPortalP23927.
SMRP23927. Positions 1-175.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198909. 7 interactions.
DIPDIP-31060N.
IntActP23927. 11 interactions.
MINTMINT-1591396.

PTM databases

PhosphoSiteP23927.

2D gel databases

SWISS-2DPAGEP23927.

Proteomic databases

MaxQBP23927.
PaxDbP23927.
PRIDEP23927.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034562; ENSMUSP00000034562; ENSMUSG00000032060.
GeneID12955.
KEGGmmu:12955.
UCSCuc009pkl.1. mouse.

Organism-specific databases

CTD1410.
MGIMGI:88516. Cryab.

Phylogenomic databases

eggNOGNOG246790.
HOGENOMHOG000233954.
HOVERGENHBG054766.
InParanoidP23927.
KOK09542.
OMARKQAPGP.
OrthoDBEOG7WHHBK.
PhylomeDBP23927.
TreeFamTF105049.

Gene expression databases

ArrayExpressP23927.
BgeeP23927.
CleanExMM_CRYAB.
GenevestigatorP23927.

Family and domain databases

Gene3D2.60.40.790. 1 hit.
InterProIPR002068. a-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR012273. Alpha-crystallin_B.
IPR003090. Alpha-crystallin_N.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PANTHERPTHR11527:SF37. PTHR11527:SF37. 1 hit.
PfamPF00525. Crystallin. 1 hit.
PF00011. HSP20. 1 hit.
[Graphical view]
PIRSFPIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSPR00299. ACRYSTALLIN.
SUPFAMSSF49764. SSF49764. 1 hit.
PROSITEPS01031. HSP20. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCRYAB. mouse.
NextBio282674.
PROP23927.
SOURCESearch...

Entry information

Entry nameCRYAB_MOUSE
AccessionPrimary (citable) accession number: P23927
Secondary accession number(s): Q64325
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: July 15, 1999
Last modified: July 9, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot