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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)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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Eye lens protein

Keywords - Ligandi

Metal-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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 175175Alpha-crystallin B chainPRO_0000125906Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei19 – 191Phosphoserine2 Publications
Modified residuei22 – 221Omega-N-methylated arginineBy similarity
Modified residuei45 – 451Phosphoserine3 Publications
Modified residuei50 – 501Omega-N-methylated arginineBy similarity
Modified residuei59 – 591Phosphoserine2 Publications
Glycosylationi90 – 901N-linked (Glc) (glycation)Curated
Modified residuei92 – 921N6-acetyllysine; alternateBy similarity
Glycosylationi92 – 921N-linked (Glc) (glycation); alternateCurated
Modified residuei166 – 1661N6-acetyllysineBy similarity

Post-translational modificationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei72 – 721Not glycated
Sitei82 – 821Not glycated
Sitei103 – 1031Not glycated
Sitei121 – 1211Not glycated
Sitei150 – 1501Not glycated
Sitei166 – 1661Not glycated
Sitei174 – 1741Not glycated
Sitei175 – 1751Not glycated

Keywords - PTMi

Acetylation, Glycation, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP02510.
PRIDEiP02510.

2D gel databases

UCD-2DPAGEP02510.

PTM databases

iPTMnetiP02510.
UniCarbKBiP02510.

Expressioni

Tissue specificityi

Lens as well as other tissues.

Gene expression databases

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 interaction.
DIPiDIP-43761N.
MINTiMINT-1486058.
STRINGi9913.ENSBTAP00000000556.

Structurei

3D structure databases

ProteinModelPortaliP02510.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3591. Eukaryota.
ENOG410YERS. LUCA.
HOGENOMiHOG000233954.
HOVERGENiHBG054766.
InParanoidiP02510.
KOiK09542.
OMAiTITAPMK.
OrthoDBiEOG7WHHBK.
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.

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP02510.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP02510.
UniCarbKBiP02510.

2D gel databases

UCD-2DPAGEP02510.

Proteomic databases

PaxDbiP02510.
PRIDEiP02510.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1410.

Phylogenomic databases

eggNOGiKOG3591. Eukaryota.
ENOG410YERS. LUCA.
HOGENOMiHOG000233954.
HOVERGENiHBG054766.
InParanoidiP02510.
KOiK09542.
OMAiTITAPMK.
OrthoDBiEOG7WHHBK.
TreeFamiTF105049.

Enzyme and pathway databases

ReactomeiR-BTA-3371571. HSF1-dependent transactivation.

Gene expression databases

ExpressionAtlasiP02510. baseline and differential.

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. "The amino-acids sequence of the alphaB2 chain of bovine alpha-crystallin."
    van der Ouderaa F.J., de Jong W.W., Hilderink A., Bloemendal H.
    Eur. J. Biochem. 49:157-168(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. de Jong W.W.
    Submitted (NOV-1991) to UniProtKB
    Cited for: SEQUENCE REVISION TO 80.
  3. Kelley P.B., Abraham E.C., Zhao H.R., Shroff N.P., Cherian M., Thomas J.J.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Testis.
  5. "Comparison of the homologous carboxy-terminal domain and tail of alpha-crystallin and small heat shock protein."
    Merck K.B., Horwitz J., Kersten M., Overkamp P., Gaestel M., Bloemendal H., de Jong W.W.
    Mol. Biol. Rep. 18:209-215(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 69-175.
  6. "The phosphorylation sites of the B2 chain of bovine alpha-crystallin."
    Chiesa R., Gawinowicz-Kolks M.A., Kleiman N.J., Spector A.
    Biochem. Biophys. Res. Commun. 144:1340-1347(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-45 AND SER-59.
  7. Cited for: PHOSPHORYLATION AT SER-19 AND SER-45.
  8. "Identification of the posttranslational modifications of bovine lens alpha B-crystallins by mass spectrometry."
    Smith J.B., Sun Y., Smith D.L., Green B.
    Protein Sci. 1:601-608(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 80, PHOSPHORYLATION AT SER-19; SER-45 AND SER-59.
  9. "Site selectivity in the glycation of alpha A- and alpha B-crystallins by glucose."
    Abraham E.C., Cherian M., Smith J.B.
    Biochem. Biophys. Res. Commun. 201:1451-1456(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCATION AT LYS-90 AND LYS-92, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiCRYAB_BOVIN
AccessioniPrimary (citable) accession number: P02510
Secondary accession number(s): O46508, Q3SZQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1991
Last modified: June 8, 2016
This is version 137 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. 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.