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Protein

Alpha-crystallin B chain

Gene

Cryab

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi83Zinc 1By similarity1
Metal bindingi104Zinc 2By similarity1
Metal bindingi106Zinc 2By similarity1
Metal bindingi111Zinc 1By similarity1
Metal bindingi119Zinc 1By similarity1

GO - Molecular functioni

GO - Biological processi

  • aging Source: Ensembl
  • apoptotic process involved in morphogenesis Source: MGI
  • camera-type eye development Source: MGI
  • cellular response to gamma radiation Source: MGI
  • lens development in camera-type eye Source: MGI
  • microtubule polymerization or depolymerization Source: Ensembl
  • muscle organ development Source: MGI
  • negative regulation of amyloid fibril formation Source: MGI
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of cell growth Source: Ensembl
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
  • negative regulation of gene expression Source: MGI
  • negative regulation of intracellular transport Source: MGI
  • negative regulation of protein homooligomerization Source: MGI
  • negative regulation of reactive oxygen species metabolic process Source: Ensembl
  • protein folding Source: Ensembl
  • protein homooligomerization Source: MGI
  • protein stabilization Source: MGI
  • regulation of cell death Source: MGI
  • response to estradiol Source: Ensembl
  • response to hydrogen peroxide Source: MGI
  • response to hypoxia Source: MGI
  • stress-activated MAPK cascade Source: Ensembl
  • tubulin complex assembly Source: MGI

Keywordsi

Molecular functionChaperone, Eye lens protein
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-3371571. HSF1-dependent transactivation.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-crystallin B chain
Alternative name(s):
Alpha(B)-crystallin
P23
Gene namesi
Name:Cryab
Synonyms:Crya2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:88516. Cryab.

Subcellular locationi

  • 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

GO - Cellular componenti

  • actin filament bundle Source: Ensembl
  • axon Source: Ensembl
  • cardiac myofibril Source: Ensembl
  • cell surface Source: Ensembl
  • contractile fiber Source: MGI
  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • dendritic spine Source: Ensembl
  • extracellular exosome Source: MGI
  • Golgi apparatus Source: Ensembl
  • M band Source: Ensembl
  • microtubule cytoskeleton Source: Ensembl
  • mitochondrion Source: MGI
  • myelin sheath Source: UniProtKB
  • nucleus Source: UniProtKB
  • perikaryon Source: Ensembl
  • plasma membrane Source: MGI
  • postsynaptic density Source: Ensembl
  • synaptic membrane Source: Ensembl
  • Z disc Source: MGI

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001259101 – 175Alpha-crystallin B chainAdd BLAST175

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarityCurated1
Modified residuei19PhosphoserineCombined sources1
Modified residuei22Omega-N-methylated arginineBy similarity1
Modified residuei45PhosphoserineBy similarity1
Modified residuei50Omega-N-methylated arginineBy similarity1
Modified residuei59PhosphoserineCombined sources1
Modified residuei92N6-acetyllysineBy similarity1
Modified residuei166N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP23927.
PeptideAtlasiP23927.
PRIDEiP23927.
TopDownProteomicsiP23927.

2D gel databases

SWISS-2DPAGEiP23927.

PTM databases

iPTMnetiP23927.
PhosphoSitePlusiP23927.

Expressioni

Tissue specificityi

Lens as well as other tissues.

Gene expression databases

BgeeiENSMUSG00000032060.
CleanExiMM_CRYAB.
ExpressionAtlasiP23927. baseline and differential.
GenevisibleiP23927. MM.

Interactioni

Subunit structurei

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. Interacts with TMEM109.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CRYGDP073202EBI-299046,EBI-7673124From Homo sapiens.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198909. 8 interactors.
DIPiDIP-31060N.
IntActiP23927. 13 interactors.
MINTiMINT-1591396.
STRINGi10090.ENSMUSP00000034562.

Structurei

3D structure databases

ProteinModelPortaliP23927.
SMRiP23927.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini56 – 164sHSPPROSITE-ProRule annotationAdd BLAST109

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3591. Eukaryota.
ENOG410YERS. LUCA.
GeneTreeiENSGT00760000119238.
HOGENOMiHOG000233954.
HOVERGENiHBG054766.
InParanoidiP23927.
KOiK09542.
OMAiTAPMKKL.
OrthoDBiEOG091G0USC.
PhylomeDBiP23927.
TreeFamiTF105049.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiView protein in InterPro
IPR002068. A-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR012273. Alpha-crystallin_B.
IPR003090. Alpha-crystallin_N.
IPR031107. HSP20.
IPR008978. HSP20-like_chaperone.
PANTHERiPTHR11527. PTHR11527. 1 hit.
PTHR11527:SF229. PTHR11527:SF229. 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.

Sequencei

Sequence statusi: Complete.

P23927-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFST ATSLSPFYLR
60 70 80 90 100
PPSFLRAPSW IDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV
110 120 130 140 150
HGKHEERQDE HGFISREFHR KYRIPADVDP LTITSSLSSD GVLTVNGPRK
160 170
QVSGPERTIP ITREEKPAVA AAPKK
Length:175
Mass (Da):20,069
Last modified:July 15, 1999 - v2
Checksum:i46702976C008EFD3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63170 mRNA. Translation: AAA37472.1.
M73741 Genomic DNA. Translation: AAA67045.1.
BC010768 mRNA. Translation: AAH10768.1.
M25770 Genomic DNA. Translation: AAA37133.1.
CCDSiCCDS23172.1.
PIRiA39608.
RefSeqiNP_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_006509970.3.
UniGeneiMm.178.

Genome annotation databases

EnsembliENSMUST00000034562; ENSMUSP00000034562; ENSMUSG00000032060.
ENSMUST00000214962; ENSMUSP00000149759; ENSMUSG00000032060.
ENSMUST00000216755; ENSMUSP00000150669; ENSMUSG00000032060.
ENSMUST00000217475; ENSMUSP00000149803; ENSMUSG00000032060.
GeneIDi12955.
KEGGimmu:12955.
UCSCiuc009pkl.2. mouse.

Similar proteinsi

Entry informationi

Entry nameiCRYAB_MOUSE
AccessioniPrimary (citable) accession number: P23927
Secondary accession number(s): Q64325
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: July 15, 1999
Last modified: August 30, 2017
This is version 162 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families