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
Homo sapiens (Human)
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
Sitei48Susceptible to oxidation1
Sitei60Susceptible to oxidation1
Sitei68Susceptible to oxidation1
Metal bindingi83Zinc 1By similarity1
Metal bindingi104Zinc 2Curated1
Metal bindingi106Zinc 2By similarity1
Metal bindingi111Zinc 1Curated1
Metal bindingi119Zinc 1Curated1

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW
  • microtubule binding Source: Ensembl
  • protein homodimerization activity Source: UniProtKB
  • structural constituent of eye lens Source: UniProtKB-KW
  • unfolded protein binding Source: UniProtKB

GO - Biological processi

  • aging Source: Ensembl
  • apoptotic process involved in morphogenesis Source: Ensembl
  • cellular response to gamma radiation Source: MGI
  • lens development in camera-type eye Source: Ensembl
  • microtubule polymerization or depolymerization Source: Ensembl
  • muscle contraction Source: ProtInc
  • muscle organ development Source: Ensembl
  • negative regulation of amyloid fibril formation Source: ARUK-UCL
  • negative regulation of apoptotic process Source: HGNC
  • negative regulation of cell growth Source: Ensembl
  • 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: HGNC
  • negative regulation of protein homooligomerization Source: ARUK-UCL
  • negative regulation of reactive oxygen species metabolic process Source: Ensembl
  • protein folding Source: ProtInc
  • protein homooligomerization Source: UniProtKB
  • protein stabilization Source: CAFA
  • regulation of cell death Source: MGI
  • regulation of cellular response to heat Source: Reactome
  • response to estradiol Source: Ensembl
  • response to hydrogen peroxide Source: Ensembl
  • response to hypoxia Source: Ensembl
  • stress-activated MAPK cascade Source: Ensembl
  • tubulin complex assembly Source: Ensembl

Keywordsi

Molecular functionChaperone, Eye lens protein
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-3371571. HSF1-dependent transactivation.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-crystallin B chain
Alternative name(s):
Alpha(B)-crystallin
Heat shock protein beta-5
Short name:
HspB5
Renal carcinoma antigen NY-REN-27
Rosenthal fiber component
Gene namesi
Name:CRYAB
Synonyms:CRYA2, HSPB5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:2389. CRYAB.

Subcellular locationi

GO - Cellular componenti

  • actin filament bundle Source: Ensembl
  • axon Source: Ensembl
  • cardiac myofibril Source: Ensembl
  • cell surface Source: Ensembl
  • cytoplasm Source: UniProtKB
  • cytosol Source: Ensembl
  • dendritic spine Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • Golgi apparatus Source: Ensembl
  • M band Source: Ensembl
  • microtubule cytoskeleton Source: Ensembl
  • mitochondrion Source: Ensembl
  • myelin sheath Source: Ensembl
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • perikaryon Source: Ensembl
  • postsynaptic density Source: Ensembl
  • synaptic membrane Source: Ensembl
  • Z disc Source: Ensembl

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Myopathy, myofibrillar, 2 (MFM2)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of myofibrillar myopathy, a group of chronic neuromuscular disorders characterized at ultrastructural level by disintegration of the sarcomeric Z disc and myofibrils, and replacement of the normal myofibrillar markings by small dense granules, or larger hyaline masses, or amorphous material. MFM2 is characterized by weakness of the proximal and distal limb muscles, weakness of the neck, velopharynx and trunk muscles, hypertrophic cardiomyopathy, and cataract in a subset of patients.
See also OMIM:608810
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_069528109D → H in MFM2. 1 PublicationCorresponds to variant dbSNP:rs387907339Ensembl.1
Natural variantiVAR_007899120R → G in MFM2; decreased interactions with wild-type CRYAA and CRYAB but increased interactions with wild-type CRYBB2 and CRYGC. 2 PublicationsCorresponds to variant dbSNP:rs28929489Ensembl.1
Cataract 16, multiple types (CTRCT16)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT16 includes posterior polar cataract, among others. Posterior polar cataract is a subcapsular opacity, usually disk-shaped, located at the back of the lens.
See also OMIM:613763
Myopathy, myofibrillar, fatal infantile hypertonic, alpha-B crystallin-related (MFMFIH-CRYAB)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of myofibrillar myopathy, a group of chronic neuromuscular disorders characterized at ultrastructural level by disintegration of the sarcomeric Z disc and myofibrils, and replacement of the normal myofibrillar markings by small dense granules, or larger hyaline masses, or amorphous material. MFMFIH-CRYAB has onset in the first weeks of life after a normal neonatal period. Affected infants show rapidly progressive muscular rigidity of the trunk and limbs associated with increasing respiratory difficulty resulting in death before age 3 years.
See also OMIM:613869
Cardiomyopathy, dilated 1II (CMD1II)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
See also OMIM:615184
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_070035154G → S in CMD1II. 1 PublicationCorresponds to variant dbSNP:rs150516929Ensembl.1
Natural variantiVAR_070036157R → H in CMD1II. 1 PublicationCorresponds to variant dbSNP:rs141638421Ensembl.1

Keywords - Diseasei

Cardiomyopathy, Cataract, Disease mutation, Myofibrillar myopathy

Organism-specific databases

DisGeNETi1410.
GeneReviewsiCRYAB.
MalaCardsiCRYAB.
MIMi608810. phenotype.
613763. phenotype.
613869. phenotype.
615184. phenotype.
OpenTargetsiENSG00000109846.
Orphaneti399058. Alpha-B crystallin-related late-onset distal myopathy.
154. Familial isolated dilated cardiomyopathy.
280553. Fatal infantile hypertonic myofibrillar myopathy.
98993. Posterior polar cataract.
98995. Zonular cataract.
PharmGKBiPA26907.

Chemistry databases

ChEMBLiCHEMBL3621022.

Polymorphism and mutation databases

BioMutaiCRYAB.
DMDMi117385.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001259071 – 175Alpha-crystallin B chainAdd BLAST175

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine2 Publications1
Modified residuei19Phosphoserine1 Publication1
Modified residuei45Phosphoserine2 Publications1
Modified residuei59PhosphoserineCombined sources2 Publications1
Modified residuei92N6-acetyllysine; partial2 Publications1
Modified residuei166N6-acetyllysine1 Publication1
Glycosylationi170O-linked (GlcNAc) threonineBy similarity1

Keywords - PTMi

Acetylation, Glycoprotein, Oxidation, Phosphoprotein

Proteomic databases

EPDiP02511.
PaxDbiP02511.
PeptideAtlasiP02511.
PRIDEiP02511.

2D gel databases

REPRODUCTION-2DPAGEiIPI00021369.
SWISS-2DPAGEiP02511.
UCD-2DPAGEiP02511.

PTM databases

iPTMnetiP02511.
PhosphoSitePlusiP02511.
UniCarbKBiP02511.

Miscellaneous databases

PMAP-CutDBiP02511.

Expressioni

Tissue specificityi

Lens as well as other tissues.

Gene expression databases

BgeeiENSG00000109846.
CleanExiHS_CRYAB.
ExpressionAtlasiP02511. baseline and differential.
GenevisibleiP02511. HS.

Organism-specific databases

HPAiCAB002053.
CAB040560.
HPA057100.

Interactioni

Subunit structurei

Heteropolymer composed of three CRYAA and one CRYAB subunits (PubMed:20836128). Aggregates with homologous proteins, including the small heat shock protein HSPB1, to form large heteromeric complexes (PubMed:10751411). Inter-subunit bridging via zinc ions enhances stability, which is crucial as there is no protein turn over in the lens (PubMed:22890888). Interacts with HSPBAP1 and TTN/titin (PubMed:14676215). Interacts with TMEM109 (PubMed:23542032).5 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • microtubule binding Source: Ensembl
  • protein homodimerization activity Source: UniProtKB
  • unfolded protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107800. 111 interactors.
DIPiDIP-35017N.
IntActiP02511. 20 interactors.
MINTiMINT-221013.
STRINGi9606.ENSP00000227251.

Structurei

Secondary structure

1175
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi68 – 70Combined sources3
Beta strandi72 – 80Combined sources9
Beta strandi82 – 84Combined sources3
Helixi86 – 88Combined sources3
Beta strandi89 – 94Combined sources6
Beta strandi97 – 109Combined sources13
Beta strandi112 – 123Combined sources12
Turni125 – 127Combined sources3
Helixi130 – 132Combined sources3
Beta strandi134 – 137Combined sources4
Beta strandi141 – 148Combined sources8
Beta strandi157 – 159Combined sources3
Beta strandi161 – 163Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KLRNMR-A/B1-175[»]
2N0KNMR-A/B64-152[»]
2WJ7X-ray2.63A/B/C/D/E67-157[»]
2Y1YX-ray2.00A71-157[»]
2Y1ZX-ray2.50A/B67-157[»]
2Y22X-ray3.70A/B/C/D/E/F67-157[»]
2YGDelectron microscopy9.40A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-175[»]
3J07Other-A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-175[»]
3L1GX-ray3.32A68-162[»]
3SGMX-ray1.70A/B/C/D90-100[»]
3SGNX-ray2.81A/B90-100[»]
3SGOX-ray2.56A90-100[»]
3SGPX-ray1.40A/B/C/D90-100[»]
3SGRX-ray2.17A/B/C/D/E/F90-100[»]
3SGSX-ray1.70A95-100[»]
4M5SX-ray1.37A68-153[»]
B156-164[»]
4M5TX-ray2.00A/C/E/G68-153[»]
B/D/F/H156-164[»]
DisProtiDP00445.
ProteinModelPortaliP02511.
SMRiP02511.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02511.

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.
HOVERGENiHBG054766.
InParanoidiP02511.
KOiK09542.
OMAiTAPMKKL.
OrthoDBiEOG091G0USC.
PhylomeDBiP02511.
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.

P02511-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR
60 70 80 90 100
PPSFLRAPSW FDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV
110 120 130 140 150
HGKHEERQDE HGFISREFHR KYRIPADVDP LTITSSLSSD GVLTVNGPRK
160 170
QVSGPERTIP ITREEKPAVT AAPKK
Length:175
Mass (Da):20,159
Last modified:January 1, 1990 - v2
Checksum:iAE08BED46B7849CB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti165E → K in AAC19161 (Ref. 4) Curated1
Sequence conflicti175K → KKMPFLELHFLKQESFPTSE in AAC19161 (Ref. 4) Curated1

Mass spectrometryi

Molecular mass is 20201 Da from positions 1 - 175. Determined by ESI. 2 Publications
Molecular mass is 20281 Da from positions 1 - 175. Determined by ESI. With 1 phosphate group.2 Publications
Molecular mass is 20360 Da from positions 1 - 175. Determined by ESI. With 2 phosphate groups.1 Publication
Molecular mass is 20199 Da from positions 1 - 175. Determined by ESI. 2 Publications
Molecular mass is 20278 Da from positions 1 - 175. Determined by ESI. With 1 phosphate group.2 Publications

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01460741S → Y. Corresponds to variant dbSNP:rs2234703Ensembl.1
Natural variantiVAR_01460851P → L. Corresponds to variant dbSNP:rs2234704Ensembl.1
Natural variantiVAR_069528109D → H in MFM2. 1 PublicationCorresponds to variant dbSNP:rs387907339Ensembl.1
Natural variantiVAR_007899120R → G in MFM2; decreased interactions with wild-type CRYAA and CRYAB but increased interactions with wild-type CRYBB2 and CRYGC. 2 PublicationsCorresponds to variant dbSNP:rs28929489Ensembl.1
Natural variantiVAR_070035154G → S in CMD1II. 1 PublicationCorresponds to variant dbSNP:rs150516929Ensembl.1
Natural variantiVAR_070036157R → H in CMD1II. 1 PublicationCorresponds to variant dbSNP:rs141638421Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28638 Genomic DNA. Translation: AAA52104.1.
S45630 mRNA. Translation: AAB23453.1.
AF007162 mRNA. Translation: AAC19161.1.
AK314029 mRNA. Translation: BAG36739.1.
BT006770 mRNA. Translation: AAP35416.1.
EF444955 Genomic DNA. Translation: ACA05949.1.
CH471065 Genomic DNA. Translation: EAW67162.1.
BC007008 mRNA. Translation: AAH07008.1.
M24906 mRNA. Translation: AAA60267.1.
CCDSiCCDS8351.1.
PIRiA35332. CYHUAB.
RefSeqiNP_001276736.1. NM_001289807.1.
NP_001276737.1. NM_001289808.1.
NP_001876.1. NM_001885.2.
XP_011540910.1. XM_011542608.1.
UniGeneiHs.53454.
Hs.703770.

Genome annotation databases

EnsembliENST00000227251; ENSP00000227251; ENSG00000109846.
ENST00000526180; ENSP00000436051; ENSG00000109846.
ENST00000527950; ENSP00000437149; ENSG00000109846.
ENST00000531198; ENSP00000434247; ENSG00000109846.
ENST00000533475; ENSP00000433560; ENSG00000109846.
ENST00000616970; ENSP00000483554; ENSG00000109846.
GeneIDi1410.
KEGGihsa:1410.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiCRYAB_HUMAN
AccessioniPrimary (citable) accession number: P02511
Secondary accession number(s): B0YIX0
, O43416, Q9UC37, Q9UC38, Q9UC39, Q9UC40, Q9UC41
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1990
Last modified: August 30, 2017
This is version 206 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families