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P02511

- CRYAB_HUMAN

UniProt

P02511 - CRYAB_HUMAN

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Protein

Alpha-crystallin B chain

Gene

CRYAB

Organism
Homo sapiens (Human)
Status
Reviewed - 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
Sitei48 – 481Susceptible to oxidation
Sitei60 – 601Susceptible to oxidation
Sitei68 – 681Susceptible to oxidation
Metal bindingi83 – 831Zinc 1By similarity
Metal bindingi104 – 1041Zinc 2Curated
Metal bindingi106 – 1061Zinc 2By similarity
Metal bindingi111 – 1111Zinc 1Curated
Metal bindingi119 – 1191Zinc 1Curated

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. metal ion binding Source: UniProtKB-KW
  3. protein homodimerization activity Source: UniProtKB
  4. structural constituent of eye lens Source: UniProtKB-KW
  5. unfolded protein binding Source: UniProtKB

GO - Biological processi

  1. aging Source: Ensembl
  2. apoptotic process involved in morphogenesis Source: Ensembl
  3. cellular response to gamma radiation Source: MGI
  4. glucose metabolic process Source: Ensembl
  5. lens development in camera-type eye Source: Ensembl
  6. microtubule polymerization or depolymerization Source: Ensembl
  7. muscle contraction Source: ProtInc
  8. muscle organ development Source: Ensembl
  9. negative regulation of apoptotic process Source: HGNC
  10. negative regulation of cell growth Source: Ensembl
  11. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  12. negative regulation of gene expression Source: Ensembl
  13. negative regulation of intracellular transport Source: HGNC
  14. negative regulation of reactive oxygen species metabolic process Source: Ensembl
  15. protein folding Source: ProtInc
  16. protein homooligomerization Source: UniProtKB
  17. regulation of cell death Source: MGI
  18. response to estradiol Source: Ensembl
  19. response to hydrogen peroxide Source: Ensembl
  20. response to hypoxia Source: Ensembl
  21. stress-activated MAPK cascade Source: Ensembl
  22. tubulin complex assembly Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Eye lens protein

Keywords - Ligandi

Metal-binding, Zinc

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:2389. CRYAB.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication
Note: Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles.

GO - Cellular componenti

  1. actin filament bundle Source: Ensembl
  2. cell surface Source: Ensembl
  3. cytoplasm Source: UniProtKB
  4. cytosol Source: Ensembl
  5. extracellular vesicular exosome Source: UniProtKB
  6. Golgi apparatus Source: Ensembl
  7. microtubule cytoskeleton Source: Ensembl
  8. mitochondrion Source: Ensembl
  9. nucleus Source: UniProtKB
  10. plasma membrane Source: Ensembl
  11. Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Myopathy, myofibrillar, 2 (MFM2) [MIM:608810]: A neuromuscular disorder that results in 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.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti109 – 1091D → H in MFM2. 1 Publication
VAR_069528
Natural varianti120 – 1201R → G in MFM2; decreased interactions with wild-type CRYAA and CRYAB but increased interactions with wild-type CRYBB2 and CRYGC. 1 Publication
Corresponds to variant rs28929489 [ dbSNP | Ensembl ].
VAR_007899
Cataract 16, multiple types (CTRCT16) [MIM:613763]: An 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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Myopathy, myofibrillar, fatal infantile hypertonic, alpha-B crystallin-related (MFMFIH-CRYAB) [MIM:613869]: A muscular dystrophy with 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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Cardiomyopathy, dilated 1II (CMD1II) [MIM:615184]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti154 – 1541G → S in CMD1II. 1 Publication
VAR_070035
Natural varianti157 – 1571R → H in CMD1II. 1 Publication
VAR_070036

Keywords - Diseasei

Cardiomyopathy, Cataract, Disease mutation, Myofibrillar myopathy

Organism-specific databases

MIMi608810. phenotype.
613763. phenotype.
613869. phenotype.
615184. phenotype.
Orphaneti98910. Alpha-crystallinopathy.
154. Familial isolated dilated cardiomyopathy.
280553. Fatal infantile hypertonic myofibrillar myopathy.
98993. Posterior polar cataract.
98995. Zonular cataract.
PharmGKBiPA26907.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 175175Alpha-crystallin B chainPRO_0000125907Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei19 – 191Phosphoserine1 Publication
Modified residuei45 – 451Phosphoserine2 Publications
Modified residuei59 – 591Phosphoserine2 Publications
Modified residuei92 – 921N6-acetyllysine; partial2 Publications
Modified residuei166 – 1661N6-acetyllysine1 Publication
Glycosylationi170 – 1701O-linked (GlcNAc)By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Oxidation, Phosphoprotein

Proteomic databases

MaxQBiP02511.
PaxDbiP02511.
PRIDEiP02511.

2D gel databases

REPRODUCTION-2DPAGEIPI00021369.
SWISS-2DPAGEP02511.
UCD-2DPAGEP02511.

PTM databases

PhosphoSiteiP02511.
UniCarbKBiP02511.

Miscellaneous databases

PMAP-CutDBP02511.

Expressioni

Tissue specificityi

Lens as well as other tissues.

Gene expression databases

BgeeiP02511.
CleanExiHS_CRYAB.
ExpressionAtlasiP02511. baseline and differential.
GenevestigatoriP02511.

Organism-specific databases

HPAiCAB002053.
CAB040560.
HPA028724.

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.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-739060,EBI-739060
CRYAAP024897EBI-739060,EBI-6875961
CRYBA1P058132EBI-739060,EBI-7043337
CRYGCP073153EBI-739060,EBI-6875941
HSPB1P047922EBI-739060,EBI-352682
HSPB8Q9UJY12EBI-739060,EBI-739074
Tmem109Q3UBX02EBI-739060,EBI-2366300From a different organism.

Protein-protein interaction databases

BioGridi107800. 91 interactions.
DIPiDIP-35017N.
IntActiP02511. 16 interactions.
MINTiMINT-221013.
STRINGi9606.ENSP00000227251.

Structurei

Secondary structure

1
175
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi68 – 703Combined sources
Beta strandi72 – 809Combined sources
Helixi86 – 883Combined sources
Beta strandi89 – 946Combined sources
Beta strandi97 – 10913Combined sources
Beta strandi112 – 12312Combined sources
Turni125 – 1273Combined sources
Helixi130 – 1323Combined sources
Beta strandi134 – 1374Combined sources
Beta strandi141 – 1488Combined sources
Beta strandi157 – 1593Combined sources
Beta strandi161 – 1633Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KLRNMR-A/B1-175[»]
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[»]
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. Positions 1-175.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02511.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG246790.
HOVERGENiHBG054766.
InParanoidiP02511.
KOiK09542.
OMAiRKQAPGP.
PhylomeDBiP02511.
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.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PANTHERiPTHR11527: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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti165 – 1651E → K in AAC19161. 1 PublicationCurated
Sequence conflicti175 – 1751K → KKMPFLELHFLKQESFPTSE in AAC19161. 1 PublicationCurated

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti41 – 411S → Y.
Corresponds to variant rs2234703 [ dbSNP | Ensembl ].
VAR_014607
Natural varianti51 – 511P → L.
Corresponds to variant rs2234704 [ dbSNP | Ensembl ].
VAR_014608
Natural varianti109 – 1091D → H in MFM2. 1 Publication
VAR_069528
Natural varianti120 – 1201R → G in MFM2; decreased interactions with wild-type CRYAA and CRYAB but increased interactions with wild-type CRYBB2 and CRYGC. 1 Publication
Corresponds to variant rs28929489 [ dbSNP | Ensembl ].
VAR_007899
Natural varianti154 – 1541G → S in CMD1II. 1 Publication
VAR_070035
Natural varianti157 – 1571R → H in CMD1II. 1 Publication
VAR_070036

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.
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.
UCSCiuc001pmf.1. human.

Polymorphism databases

DMDMi117385.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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 .
CCDSi CCDS8351.1.
PIRi A35332. CYHUAB.
RefSeqi NP_001276736.1. NM_001289807.1.
NP_001276737.1. NM_001289808.1.
NP_001876.1. NM_001885.2.
UniGenei Hs.53454.
Hs.703770.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KLR NMR - A/B 1-175 [» ]
2WJ7 X-ray 2.63 A/B/C/D/E 67-157 [» ]
2Y1Y X-ray 2.00 A 71-157 [» ]
2Y1Z X-ray 2.50 A/B 67-157 [» ]
2Y22 X-ray 3.70 A/B/C/D/E/F 67-157 [» ]
2YGD electron microscopy 9.40 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X 1-175 [» ]
3L1G X-ray 3.32 A 68-162 [» ]
3SGM X-ray 1.70 A/B/C/D 90-100 [» ]
3SGN X-ray 2.81 A/B 90-100 [» ]
3SGO X-ray 2.56 A 90-100 [» ]
3SGP X-ray 1.40 A/B/C/D 90-100 [» ]
3SGR X-ray 2.17 A/B/C/D/E/F 90-100 [» ]
3SGS X-ray 1.70 A 95-100 [» ]
4M5S X-ray 1.37 A 68-153 [» ]
B 156-164 [» ]
4M5T X-ray 2.00 A/C/E/G 68-153 [» ]
B/D/F/H 156-164 [» ]
DisProti DP00445.
ProteinModelPortali P02511.
SMRi P02511. Positions 1-175.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107800. 91 interactions.
DIPi DIP-35017N.
IntActi P02511. 16 interactions.
MINTi MINT-221013.
STRINGi 9606.ENSP00000227251.

PTM databases

PhosphoSitei P02511.
UniCarbKBi P02511.

Polymorphism databases

DMDMi 117385.

2D gel databases

REPRODUCTION-2DPAGE IPI00021369.
SWISS-2DPAGE P02511.
UCD-2DPAGE P02511.

Proteomic databases

MaxQBi P02511.
PaxDbi P02511.
PRIDEi P02511.

Protocols and materials databases

DNASUi 1410.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000227251 ; ENSP00000227251 ; ENSG00000109846 .
ENST00000526180 ; ENSP00000436051 ; ENSG00000109846 .
ENST00000527950 ; ENSP00000437149 ; ENSG00000109846 .
ENST00000531198 ; ENSP00000434247 ; ENSG00000109846 .
ENST00000533475 ; ENSP00000433560 ; ENSG00000109846 .
ENST00000616970 ; ENSP00000483554 ; ENSG00000109846 .
GeneIDi 1410.
KEGGi hsa:1410.
UCSCi uc001pmf.1. human.

Organism-specific databases

CTDi 1410.
GeneCardsi GC11M111813.
GeneReviewsi CRYAB.
HGNCi HGNC:2389. CRYAB.
HPAi CAB002053.
CAB040560.
HPA028724.
MIMi 123590. gene.
608810. phenotype.
613763. phenotype.
613869. phenotype.
615184. phenotype.
neXtProti NX_P02511.
Orphaneti 98910. Alpha-crystallinopathy.
154. Familial isolated dilated cardiomyopathy.
280553. Fatal infantile hypertonic myofibrillar myopathy.
98993. Posterior polar cataract.
98995. Zonular cataract.
PharmGKBi PA26907.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG246790.
HOVERGENi HBG054766.
InParanoidi P02511.
KOi K09542.
OMAi RKQAPGP.
PhylomeDBi P02511.
TreeFami TF105049.

Miscellaneous databases

ChiTaRSi CRYAB. human.
EvolutionaryTracei P02511.
GeneWikii CRYAB.
GenomeRNAii 1410.
NextBioi 5765.
PMAP-CutDB P02511.
PROi P02511.
SOURCEi Search...

Gene expression databases

Bgeei P02511.
CleanExi HS_CRYAB.
ExpressionAtlasi P02511. baseline and differential.
Genevestigatori P02511.

Family and domain databases

Gene3Di 2.60.40.790. 1 hit.
InterProi IPR002068. a-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR012273. Alpha-crystallin_B.
IPR003090. Alpha-crystallin_N.
IPR008978. HSP20-like_chaperone.
[Graphical view ]
PANTHERi PTHR11527:SF37. PTHR11527:SF37. 1 hit.
Pfami PF00525. Crystallin. 1 hit.
PF00011. HSP20. 1 hit.
[Graphical view ]
PIRSFi PIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSi PR00299. ACRYSTALLIN.
SUPFAMi SSF49764. SSF49764. 1 hit.
PROSITEi PS01031. HSP20. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The primary structure of the B2 chain of human alpha-crystallin."
    Kramps J.A., de Man B.M., de Jong W.W.
    FEBS Lett. 74:82-84(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE.
  2. "Human alpha B-crystallin gene and preferential promoter function in lens."
    Dubin R.A., Ally A.H., Chung S., Piatigorsky J.
    Genomics 7:594-601(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Accumulation of alpha B-crystallin in brains of patients with Alexander's disease is not due to an abnormality of the 5'-flanking and coding sequence of the genomic DNA."
    Iwaki A., Iwaki T., Goldman J.E., Ogomori K., Tateishi J., Sakaki Y.
    Neurosci. Lett. 140:89-92(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. Yu W., Sarginson J., Gibbs R.A.
    Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. NHLBI resequencing and genotyping service (RS&G)
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart.
  10. "Copurification of small heat shock protein with alpha B crystallin from human skeletal muscle."
    Kato K., Shinohara H., Goto S., Inaguma Y., Morishita R., Asano T.
    J. Biol. Chem. 267:7718-7725(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-24; 35-66 AND 118-175, ASSOCIATION WITH HSPB1.
    Tissue: Pectoralis muscle.
  11. "Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens."
    Lampi K.J., Ma Z., Shih M., Shearer T.R., Smith J.B., Smith D.L., David L.L.
    J. Biol. Chem. 272:2268-2275(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 57-66.
  12. "The major protein expression profile and two-dimensional protein database of human heart."
    Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A., Ershova E.S., Egorov T.A., Musalyamov A.K.
    Electrophoresis 16:1160-1169(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 83-89 AND 164-172.
    Tissue: Heart.
  13. "Alpha B-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain."
    Iwaki T., Kume-Iwaki A., Liem R.K.H., Goldman J.E.
    Cell 57:71-78(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 107-175.
  14. "Simultaneous racemization and isomerization at specific aspartic acid residues in alpha B-crystallin from the aged human lens."
    Fujii N., Ishibashi Y., Satoh K., Fujino M., Harada K.
    Biochim. Biophys. Acta 1204:157-163(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: RACEMIZATION/ISOMERIZATION OF SPECIFIC ASP.
  15. "Post-translational modifications of water-soluble human lens crystallins from young adults."
    Miesbauer L.R., Zhou X., Yang Z., Yang Z., Sun Y., Smith D.L., Smith J.B.
    J. Biol. Chem. 269:12494-12502(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-19; SER-45 AND SER-59, MASS SPECTROMETRY.
  16. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
    Tissue: Renal cell carcinoma.
  17. "The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage."
    Hanson S.R.A., Hasan A., Smith D.L., Smith J.B.
    Exp. Eye Res. 71:195-207(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY, SUSCEPTIBILITY TO OXIDATION, PHOSPHORYLATION.
  18. "Identification and characterization of a novel protein from Sertoli cells, PASS1, that associates with mammalian small stress protein hsp27."
    Liu C., Gilmont R.R., Benndorf R., Welsh M.J.
    J. Biol. Chem. 275:18724-18731(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSPBAP1.
  19. "Alpha-B crystallin gene (CRYAB) mutation causes dominant congenital posterior polar cataract in humans."
    Berry V., Francis P., Reddy M.A., Collyer D., Vithana E., MacKay I., Dawson G., Carey A.H., Moore A., Bhattacharya S.S., Quinlan R.A.
    Am. J. Hum. Genet. 69:1141-1145(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CTRCT16.
  20. "Ser-59 is the major phosphorylation site in alphaB-crystallin accumulated in the brains of patients with Alexander's disease."
    Kato K., Inaguma Y., Ito H., Iida K., Iwamoto I., Kamei K., Ochi N., Ohta H., Kishikawa M.
    J. Neurochem. 76:730-736(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-45 AND SER-59.
  21. "In vivo carbamylation and acetylation of water-soluble human lens alphaB-crystallin lysine 92."
    Lapko V.N., Smith D.L., Smith J.B.
    Protein Sci. 10:1130-1136(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-92.
  22. "Myofibrillar myopathy caused by novel dominant negative alpha B-crystallin mutations."
    Selcen D., Engel A.G.
    Ann. Neurol. 54:804-810(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MFM2.
  23. Cited for: INTERACTION WITH TTN.
  24. "HSPB7 is a SC35 speckle resident small heat shock protein."
    Vos M.J., Kanon B., Kampinga H.H.
    Biochim. Biophys. Acta 1793:1343-1353(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  25. "Importance of eye lens alpha-crystallin heteropolymer with 3:1 alphaA to alphaB ratio: stability, aggregation, and modifications."
    Srinivas P., Narahari A., Petrash J.M., Swamy M.J., Reddy G.B.
    IUBMB Life 62:693-702(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  26. "Infantile muscular dystrophy in Canadian aboriginals is an alphaB-crystallinopathy."
    Del Bigio M.R., Chudley A.E., Sarnat H.B., Campbell C., Goobie S., Chodirker B.N., Selcen D.
    Ann. Neurol. 69:866-871(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MFMFIH-CRYAB.
  27. "Acetylation of alphaA-crystallin in the human lens: effects on structure and chaperone function."
    Nagaraj R.H., Nahomi R.B., Shanthakumar S., Linetsky M., Padmanabha S., Pasupuleti N., Wang B., Santhoshkumar P., Panda A.K., Biswas A.
    Biochim. Biophys. Acta 1822:120-129(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-92 AND LYS-166.
  28. "Identification of histidine residues involved in Zn(2+) binding to alphaA- and alphaB-Crystallin by chemical modification and MALDI TOF mass spectrometry."
    Karmakar S., Das K.P.
    Protein J. 31:623-640(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, ZINC-BINDING SITES.
  29. "A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy."
    Vicart P., Caron A., Guicheney P., Li Z., Prevost M.-C., Faure A., Chateau D., Chapon F., Tome F., Dupret J.-M., Paulin D., Fardeau M.
    Nat. Genet. 20:92-95(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MFM2 GLY-120.
  30. "Alteration of protein-protein interactions of congenital cataract crystallin mutants."
    Fu L., Liang J.J.-N.
    Invest. Ophthalmol. Vis. Sci. 44:1155-1159(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS MFM2 GLY-120.
  31. "Crystal structures of alpha-crystallin domain dimers of alphaB-crystallin and Hsp20."
    Bagneris C., Bateman O.A., Naylor C.E., Cronin N., Boelens W.C., Keep N.H., Slingsby C.
    J. Mol. Biol. 392:1242-1252(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 67-157, HOMODIMERIZATION.
  32. Cited for: VARIANT CMD1II HIS-157.
  33. "alphaB-crystallin mutation in dilated cardiomyopathies: low prevalence in a consecutive series of 200 unrelated probands."
    Pilotto A., Marziliano N., Pasotti M., Grasso M., Costante A.M., Arbustini E.
    Biochem. Biophys. Res. Commun. 346:1115-1117(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CMD1II SER-154.
  34. Cited for: VARIANT MFM2 HIS-109.

Entry informationi

Entry nameiCRYAB_HUMAN
AccessioniPrimary (citable) accession number: P02511
Secondary accession number(s): B0YIX0
, O43416, Q9UC37, Q9UC38, Q9UC39, Q9UC40, Q9UC41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1990
Last modified: November 26, 2014
This is version 177 of the entry and version 2 of the sequence. [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

External Data

Dasty 3