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Protein

Alpha-crystallin B chain

Gene

Cryab

Organism
Rattus norvegicus (Rat)
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

  • cytoskeletal protein binding Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • microtubule binding Source: RGD
  • protein homodimerization activity Source: UniProtKB
  • structural constituent of eye lens Source: RGD

GO - Biological processi

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

Keywords - Molecular functioni

Chaperone, Eye lens protein

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-RNO-3371571. HSF1-dependent transactivation.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-crystallin B chain
Alternative name(s):
Alpha(B)-crystallin
Gene namesi
Name:Cryab
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi2414. 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: RGD
  • axon Source: RGD
  • cardiac myofibril Source: RGD
  • cell surface Source: RGD
  • cytosol Source: Ensembl
  • dendritic spine Source: RGD
  • extracellular exosome Source: Ensembl
  • Golgi apparatus Source: RGD
  • I band Source: RGD
  • M band Source: RGD
  • microtubule cytoskeleton Source: RGD
  • mitochondrion Source: Ensembl
  • myelin sheath Source: Ensembl
  • nucleus Source: UniProtKB
  • perikaryon Source: RGD
  • postsynaptic density Source: RGD
  • synapse Source: RGD
  • synaptic membrane Source: RGD
  • Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 175175Alpha-crystallin B chainPRO_0000125913Add
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 – 591PhosphoserineCombined sources
Modified residuei92 – 921N6-acetyllysineBy similarity
Modified residuei166 – 1661N6-acetyllysineBy similarity
Glycosylationi170 – 1701O-linked (GlcNAc)1 PublicationCAR_000058

Keywords - PTMi

Acetylation, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP23928.
PRIDEiP23928.

PTM databases

iPTMnetiP23928.
PhosphoSiteiP23928.

Expressioni

Tissue specificityi

Lens as well as other tissues.

Developmental stagei

Levels are low in both the slow-twitch soleus and fast-twitch rectus femoris muscles at prenatal day 2, then increase slowly until postnatal day 3. At 2 weeks, levels in the rectus femoris muscle then decrease while those in the soleus muscle increase sharply, reaching adult levels by 4 weeks.1 Publication

Gene expression databases

GenevisibleiP23928. RN.

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
Crybb1Q9WVJ52EBI-916888,EBI-8520354From a different organism.

GO - Molecular functioni

  • cytoskeletal protein binding Source: RGD
  • microtubule binding Source: RGD
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi247455. 3 interactions.
IntActiP23928. 3 interactions.
MINTiMINT-6801317.
STRINGi10116.ENSRNOP00000055901.

Structurei

3D structure databases

ProteinModelPortaliP23928.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3591. Eukaryota.
ENOG410YERS. LUCA.
GeneTreeiENSGT00760000119238.
HOGENOMiHOG000233954.
HOVERGENiHBG054766.
InParanoidiP23928.
KOiK09542.
OMAiTITAPMK.
OrthoDBiEOG7WHHBK.
PhylomeDBiP23928.
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.

P23928-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFST ATSLSPFYLR
60 70 80 90 100
PPSFLRAPSW IDTGLSEMRM EKDRFSVNLD VKHFSPEELK VKVLGDVIEV
110 120 130 140 150
HGKHEERQDE HGFISREFHR KYRIPADVDP LTITSSLSSD GVLTVNGPRK
160 170
QASGPERTIP ITREEKPAVT AAPKK
Length:175
Mass (Da):20,089
Last modified:March 1, 1992 - v1
Checksum:iAB66796291518B9B
GO

Sequence cautioni

The sequence CAA42911.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S74229 mRNA. Translation: AAB20759.1.
S77138 mRNA. Translation: AAP31995.1.
M55534 mRNA. Translation: AAA40977.1.
X60352 mRNA. Translation: CAA42911.1. Different initiation.
X60351 mRNA. Translation: CAA42910.1.
S77142 mRNA. No translation available.
U04320 Unassigned DNA. Translation: AAA03655.1.
M24092 mRNA. Translation: AAA40978.1.
PIRiA23681.
RefSeqiNP_037067.1. NM_012935.4.
UniGeneiRn.98208.

Genome annotation databases

EnsembliENSRNOT00000059127; ENSRNOP00000055901; ENSRNOG00000010524.
GeneIDi25420.
KEGGirno:25420.
UCSCiRGD:2414. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S74229 mRNA. Translation: AAB20759.1.
S77138 mRNA. Translation: AAP31995.1.
M55534 mRNA. Translation: AAA40977.1.
X60352 mRNA. Translation: CAA42911.1. Different initiation.
X60351 mRNA. Translation: CAA42910.1.
S77142 mRNA. No translation available.
U04320 Unassigned DNA. Translation: AAA03655.1.
M24092 mRNA. Translation: AAA40978.1.
PIRiA23681.
RefSeqiNP_037067.1. NM_012935.4.
UniGeneiRn.98208.

3D structure databases

ProteinModelPortaliP23928.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247455. 3 interactions.
IntActiP23928. 3 interactions.
MINTiMINT-6801317.
STRINGi10116.ENSRNOP00000055901.

PTM databases

iPTMnetiP23928.
PhosphoSiteiP23928.

Proteomic databases

PaxDbiP23928.
PRIDEiP23928.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000059127; ENSRNOP00000055901; ENSRNOG00000010524.
GeneIDi25420.
KEGGirno:25420.
UCSCiRGD:2414. rat.

Organism-specific databases

CTDi1410.
RGDi2414. Cryab.

Phylogenomic databases

eggNOGiKOG3591. Eukaryota.
ENOG410YERS. LUCA.
GeneTreeiENSGT00760000119238.
HOGENOMiHOG000233954.
HOVERGENiHBG054766.
InParanoidiP23928.
KOiK09542.
OMAiTITAPMK.
OrthoDBiEOG7WHHBK.
PhylomeDBiP23928.
TreeFamiTF105049.

Enzyme and pathway databases

ReactomeiR-RNO-3371571. HSF1-dependent transactivation.

Miscellaneous databases

NextBioi606579.
PROiP23928.

Gene expression databases

GenevisibleiP23928. RN.

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. "Multiple mRNAs of rat brain alpha-crystallin B chain result from alternative transcriptional initiation."
    Iwaki A., Iwaki T., Goldman J.E., Liem R.K.
    J. Biol. Chem. 265:22197-22203(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Alpha B-crystallin exists as an independent protein in the heart and in the lens."
    Bhat S.P., Horwitz J., Srinivasan A.N., Ding L.
    Eur. J. Biochem. 202:775-781(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Heart and Lens.
  3. "Early changes of alpha B-crystallin mRNA in rat skeletal muscle to mechanical tension and denervation."
    Atomi Y., Yamada S., Nishida T.
    Biochem. Biophys. Res. Commun. 181:1323-1330(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  4. Srinivasan A.N., Bhat S.P.
    Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Spleen.
  5. "Alpha B-crystallin in skeletal muscle: purification and localization."
    Atomi Y., Yamada S., Strohman R., Nonomura Y.
    J. Biochem. 110:812-822(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Strain: Wistar.
    Tissue: Skeletal muscle.
  6. "Alpha-B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues."
    Bhat S.P., Nagineni C.N.
    Biochem. Biophys. Res. Commun. 158:319-325(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 140-175.
    Tissue: Heart.
  7. "Physiological and pathological changes in levels of the two small stress proteins, HSP27 and alpha B crystallin, in rat hindlimb muscles."
    Inaguma Y., Goto S., Shinohara H., Hasegawa K., Ohshima K., Kato K.
    J. Biochem. 114:378-384(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  8. "Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin."
    Roquemore E.P., Chevrier M.R., Cotter R.J., Hart G.W.
    Biochemistry 35:3578-3586(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-170.
  9. "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.
  10. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCRYAB_RAT
AccessioniPrimary (citable) accession number: P23928
Secondary accession number(s): Q6LDR2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: February 17, 2016
This is version 136 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.