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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)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

  • 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)DescriptionActionsGraphical viewLength
ChainiPRO_00001259131 – 175Alpha-crystallin B chainAdd BLAST175

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCurated1
Modified residuei19PhosphoserineBy similarity1
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
GlycosylationiCAR_000058170O-linked (GlcNAc)1 Publication1

Keywords - PTMi

Acetylation, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP23928.
PRIDEiP23928.

PTM databases

iPTMnetiP23928.
PhosphoSitePlusiP23928.

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

BgeeiENSRNOG00000010524.
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 interactors.
IntActiP23928. 3 interactors.
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.
OrthoDBiEOG091G0USC.
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 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 interactors.
IntActiP23928. 3 interactors.
MINTiMINT-6801317.
STRINGi10116.ENSRNOP00000055901.

PTM databases

iPTMnetiP23928.
PhosphoSitePlusiP23928.

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.
OrthoDBiEOG091G0USC.
PhylomeDBiP23928.
TreeFamiTF105049.

Enzyme and pathway databases

ReactomeiR-RNO-3371571. HSF1-dependent transactivation.

Miscellaneous databases

PROiP23928.

Gene expression databases

BgeeiENSRNOG00000010524.
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...

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: November 2, 2016
This is version 139 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.