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P23927

- CRYAB_MOUSE

UniProt

P23927 - CRYAB_MOUSE

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Protein

Alpha-crystallin B chain

Gene

Cryab

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. metal ion binding Source: UniProtKB-KW
  2. protein homodimerization activity Source: UniProtKB
  3. structural constituent of eye lens Source: MGI

GO - Biological processi

  1. aging Source: Ensembl
  2. apoptotic process involved in morphogenesis Source: MGI
  3. camera-type eye development Source: MGI
  4. cellular response to gamma radiation Source: MGI
  5. glucose metabolic process Source: Ensembl
  6. lens development in camera-type eye Source: MGI
  7. microtubule polymerization or depolymerization Source: Ensembl
  8. muscle organ development Source: MGI
  9. negative regulation of apoptotic process Source: MGI
  10. negative regulation of cell growth Source: Ensembl
  11. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
  12. negative regulation of gene expression Source: MGI
  13. negative regulation of intracellular transport Source: Ensembl
  14. negative regulation of reactive oxygen species metabolic process Source: Ensembl
  15. protein folding Source: Ensembl
  16. protein homooligomerization Source: Ensembl
  17. regulation of cell death Source: MGI
  18. response to estradiol Source: Ensembl
  19. response to hydrogen peroxide Source: MGI
  20. response to hypoxia Source: MGI
  21. stress-activated MAPK cascade Source: Ensembl
  22. 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: 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

  1. actin filament bundle Source: Ensembl
  2. cell surface Source: Ensembl
  3. contractile fiber Source: MGI
  4. cytosol Source: MGI
  5. extracellular vesicular exosome Source: Ensembl
  6. Golgi apparatus Source: Ensembl
  7. microtubule cytoskeleton Source: Ensembl
  8. mitochondrion Source: MGI
  9. nucleus Source: UniProtKB
  10. plasma membrane Source: MGI
  11. 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.
GenevestigatoriP23927.

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. 7 interactions.
DIPiDIP-31060N.
IntActiP23927. 11 interactions.
MINTiMINT-1591396.

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.
OMAiRKQAPGP.
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.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PANTHERiPTHR11527: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:
EMBL
GenBank
DDBJ
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_006509970.1.
UniGeneiMm.178.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M63170 mRNA. Translation: AAA37472.1 .
M73741 Genomic DNA. Translation: AAA67045.1 .
BC010768 mRNA. Translation: AAH10768.1 .
M25770 Genomic DNA. Translation: AAA37133.1 .
CCDSi CCDS23172.1.
PIRi A39608.
RefSeqi NP_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.
UniGenei Mm.178.

3D structure databases

ProteinModelPortali P23927.
SMRi P23927. Positions 1-175.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198909. 7 interactions.
DIPi DIP-31060N.
IntActi P23927. 11 interactions.
MINTi MINT-1591396.

PTM databases

PhosphoSitei P23927.

2D gel databases

SWISS-2DPAGE P23927.

Proteomic databases

MaxQBi P23927.
PaxDbi P23927.
PRIDEi P23927.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034562 ; ENSMUSP00000034562 ; ENSMUSG00000032060 .
GeneIDi 12955.
KEGGi mmu:12955.
UCSCi uc009pkl.1. mouse.

Organism-specific databases

CTDi 1410.
MGIi MGI:88516. Cryab.

Phylogenomic databases

eggNOGi NOG246790.
HOGENOMi HOG000233954.
HOVERGENi HBG054766.
InParanoidi P23927.
KOi K09542.
OMAi RKQAPGP.
OrthoDBi EOG7WHHBK.
PhylomeDBi P23927.
TreeFami TF105049.

Miscellaneous databases

ChiTaRSi CRYAB. mouse.
NextBioi 282674.
PROi P23927.
SOURCEi Search...

Gene expression databases

Bgeei P23927.
CleanExi MM_CRYAB.
ExpressionAtlasi P23927. baseline and differential.
Genevestigatori P23927.

Family and domain databases

Gene3Di 2.60.40.790. 1 hit.
InterProi IPR002068. a-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR012273. Alpha-crystallin_B.
IPR003090. Alpha-crystallin_N.
IPR008978. HSP20-like_chaperone.
[Graphical view ]
PANTHERi PTHR11527:SF37. PTHR11527:SF37. 1 hit.
Pfami PF00525. Crystallin. 1 hit.
PF00011. HSP20. 1 hit.
[Graphical view ]
PIRSFi PIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSi PR00299. ACRYSTALLIN.
SUPFAMi SSF49764. SSF49764. 1 hit.
PROSITEi PS01031. HSP20. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 133 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