Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Alpha-crystallin B chain

Gene

CRYAB

Organism
Bos taurus (Bovine)
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

Keywordsi

Molecular functionChaperone, Eye lens protein
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-BTA-3371571. HSF1-dependent transactivation.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-crystallin B chain
Alternative name(s):
Alpha(B)-crystallin
Gene namesi
Name:CRYAB
Synonyms:CRYA2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 15

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001259061 – 175Alpha-crystallin B chainAdd BLAST175

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine1 Publication1
Modified residuei19Phosphoserine2 Publications1
Modified residuei22Omega-N-methylated arginineBy similarity1
Modified residuei45Phosphoserine3 Publications1
Modified residuei50Omega-N-methylated arginineBy similarity1
Modified residuei59Phosphoserine2 Publications1
Glycosylationi90N-linked (Glc) (glycation) lysineCurated1
Modified residuei92N6-acetyllysine; alternateBy similarity1
Glycosylationi92N-linked (Glc) (glycation) lysine; alternateCurated1
Modified residuei166N6-acetyllysineBy similarity1

Post-translational modificationi

It is not known whether either Lys-90, or Lys-92, or both are glycated.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei72Not glycated1
Sitei82Not glycated1
Sitei103Not glycated1
Sitei121Not glycated1
Sitei150Not glycated1
Sitei166Not glycated1
Sitei174Not glycated1
Sitei175Not glycated1

Keywords - PTMi

Acetylation, Glycation, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP02510.
PeptideAtlasiP02510.
PRIDEiP02510.

2D gel databases

UCD-2DPAGEiP02510.

PTM databases

iPTMnetiP02510.
UniCarbKBiP02510.

Expressioni

Tissue specificityi

Lens as well as other tissues.

Gene expression databases

BgeeiENSBTAG00000000434.
ExpressionAtlasiP02510. baseline and differential.

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi159035. 1 interactor.
DIPiDIP-43761N.
MINTiMINT-1486058.
STRINGi9913.ENSBTAP00000000556.

Structurei

3D structure databases

ProteinModelPortaliP02510.
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.
InParanoidiP02510.
KOiK09542.
OMAiTAPMKKL.
OrthoDBiEOG091G0USC.
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.

P02510-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPA STSLSPFYLR
60 70 80 90 100
PPSFLRAPSW IDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV
110 120 130 140 150
HGKHEERQDE HGFISREFHR KYRIPADVDP LAITSSLSSD GVLTVNGPRK
160 170
QASGPERTIP ITREEKPAVT AAPKK
Length:175
Mass (Da):20,037
Last modified:November 1, 1991 - v2
Checksum:iE0CFBBA8D6DE82B2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF029793 mRNA. Translation: AAB95323.2.
BC102745 mRNA. Translation: AAI02746.1.
PIRiA42446. CYBOAB.
RefSeqiNP_776715.1. NM_174290.2.
UniGeneiBt.88059.

Genome annotation databases

EnsembliENSBTAT00000000556; ENSBTAP00000000556; ENSBTAG00000000434.
GeneIDi281719.
KEGGibta:281719.

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.

Entry informationi

Entry nameiCRYAB_BOVIN
AccessioniPrimary (citable) accession number: P02510
Secondary accession number(s): O46508, Q3SZQ9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1991
Last modified: July 5, 2017
This is version 146 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. SIMILARITY comments
    Index of protein domains and families