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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi83 – 831Zinc 1By similarity
Metal bindingi104 – 1041Zinc 2By similarity
Metal bindingi106 – 1061Zinc 2By similarity
Metal bindingi111 – 1111Zinc 1By similarity
Metal bindingi119 – 1191Zinc 1By similarity

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 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 reactive oxygen species metabolic process Source: Ensembl
  • protein folding Source: Ensembl
  • protein homooligomerization 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
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Eye lens protein

Keywords - Ligandi

Metal-binding, Zinc

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 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
  • cell surface Source: Ensembl
  • contractile fiber Source: MGI
  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • extracellular exosome Source: MGI
  • Golgi apparatus Source: Ensembl
  • microtubule cytoskeleton Source: Ensembl
  • mitochondrion Source: MGI
  • myelin sheath Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: MGI
  • Z disc Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 175175Alpha-crystallin B chainPRO_0000125910Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCurated
Modified residuei19 – 191PhosphoserineBy similarity
Modified residuei22 – 221Omega-N-methylated arginineBy similarity
Modified residuei45 – 451PhosphoserineBy similarity
Modified residuei50 – 501Omega-N-methylated arginineBy similarity
Modified residuei59 – 591PhosphoserineBy similarity
Modified residuei92 – 921N6-acetyllysineBy similarity
Modified residuei166 – 1661N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP23927.
PaxDbiP23927.
PRIDEiP23927.

2D gel databases

SWISS-2DPAGEP23927.

PTM databases

PhosphoSiteiP23927.

Expressioni

Tissue specificityi

Lens as well as other tissues.

Gene expression databases

BgeeiP23927.
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 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CRYGDP073202EBI-299046,EBI-7673124From a different organism.

Protein-protein interaction databases

BioGridi198909. 8 interactions.
DIPiDIP-31060N.
IntActiP23927. 11 interactions.
MINTiMINT-1591396.
STRINGi10090.ENSMUSP00000034562.

Structurei

3D structure databases

ProteinModelPortaliP23927.
SMRiP23927. Positions 1-175.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG246790.
HOGENOMiHOG000233954.
HOVERGENiHBG054766.
InParanoidiP23927.
KOiK09542.
OMAiLTITAPM.
OrthoDBiEOG7WHHBK.
PhylomeDBiP23927.
TreeFamiTF105049.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR002068. A-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR012273. Alpha-crystallin_B.
IPR003090. Alpha-crystallin_N.
IPR031107. HSP20.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PANTHERiPTHR11527. PTHR11527. 1 hit.
PTHR11527:SF37. PTHR11527:SF37. 1 hit.
PfamiPF00525. Crystallin. 1 hit.
PF00011. HSP20. 1 hit.
[Graphical view]
PIRSFiPIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSiPR00299. ACRYSTALLIN.
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS01031. HSP20. 1 hit.
[Graphical view]

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_006509970.2.
UniGeneiMm.178.

Genome annotation databases

EnsembliENSMUST00000034562; ENSMUSP00000034562; ENSMUSG00000032060.
GeneIDi12955.
KEGGimmu:12955.
UCSCiuc009pkl.1. mouse.

Cross-referencesi

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_006509970.2.
UniGeneiMm.178.

3D structure databases

ProteinModelPortaliP23927.
SMRiP23927. Positions 1-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198909. 8 interactions.
DIPiDIP-31060N.
IntActiP23927. 11 interactions.
MINTiMINT-1591396.
STRINGi10090.ENSMUSP00000034562.

PTM databases

PhosphoSiteiP23927.

2D gel databases

SWISS-2DPAGEP23927.

Proteomic databases

MaxQBiP23927.
PaxDbiP23927.
PRIDEiP23927.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034562; ENSMUSP00000034562; ENSMUSG00000032060.
GeneIDi12955.
KEGGimmu:12955.
UCSCiuc009pkl.1. mouse.

Organism-specific databases

CTDi1410.
MGIiMGI:88516. Cryab.

Phylogenomic databases

eggNOGiNOG246790.
HOGENOMiHOG000233954.
HOVERGENiHBG054766.
InParanoidiP23927.
KOiK09542.
OMAiLTITAPM.
OrthoDBiEOG7WHHBK.
PhylomeDBiP23927.
TreeFamiTF105049.

Miscellaneous databases

ChiTaRSiCryab. mouse.
NextBioi282674.
PROiP23927.
SOURCEiSearch...

Gene expression databases

BgeeiP23927.
CleanExiMM_CRYAB.
ExpressionAtlasiP23927. baseline and differential.
GenevisibleiP23927. MM.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR002068. A-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR012273. Alpha-crystallin_B.
IPR003090. Alpha-crystallin_N.
IPR031107. HSP20.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PANTHERiPTHR11527. PTHR11527. 1 hit.
PTHR11527:SF37. PTHR11527:SF37. 1 hit.
PfamiPF00525. Crystallin. 1 hit.
PF00011. HSP20. 1 hit.
[Graphical view]
PIRSFiPIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSiPR00299. ACRYSTALLIN.
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS01031. HSP20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiCRYAB_MOUSE
AccessioniPrimary (citable) accession number: P23927
Secondary accession number(s): Q64325
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: July 15, 1999
Last modified: June 24, 2015
This is version 141 of the entry and version 2 of the sequence. [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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.