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Protein

Alpha-crystallin B chain

Gene

CRYAB

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -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

Organism-specific databases

VGNCiVGNC:27732 CRYAB

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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

CarbonylDBiP02510
GlyConnecti32
37
38
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. Interacts with DES; binds rapidly during early stages of DES filament assembly and a reduced binding seen in the later stages.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CRYAAP024704EBI-7824601,EBI-15796552

GO - Molecular functioni

Protein-protein interaction databases

BioGridi159035, 1 interactor
DIPiDIP-43761N
IntActiP02510, 2 interactors
MINTiP02510
STRINGi9913.ENSBTAP00000000556

Structurei

3D structure databases

ProteinModelPortaliP02510
SMRiP02510
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

CDDicd06498 ACD_alphaB-crystallin_HspB5, 1 hit
Gene3Di2.60.40.790, 1 hit
InterProiView protein in InterPro
IPR002068 A-crystallin/Hsp20_dom
IPR037882 ACD_alphaB-crystallin
IPR001436 Alpha-crystallin/HSP
IPR003090 Alpha-crystallin_N
IPR031107 HSP20
IPR008978 HSP20-like_chaperone
PANTHERiPTHR11527 PTHR11527, 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

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: April 25, 2018
This is version 153 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
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Main funding by: National Institutes of Health