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P02511 (CRYAB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 174. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CRYAB
Synonyms:CRYA2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length175 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.14 Ref.18 Ref.23 Ref.25 Ref.28 Ref.31

Subcellular location

Cytoplasm. Nucleus. Note: Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles. Ref.24

Tissue specificity

Lens as well as other tissues.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22 Ref.29 Ref.30 Ref.34

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.26

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.32 Ref.33

Sequence similarities

Belongs to the small heat shock protein (HSP20) family.

Mass spectrometry

Molecular mass is 20201 Da from positions 1 - 175. Determined by ESI. Ref.15

Molecular mass is 20281 Da from positions 1 - 175. Determined by ESI. With 1 phosphate group. Ref.15

Molecular mass is 20360 Da from positions 1 - 175. Determined by ESI. With 2 phosphate groups. Ref.15

Molecular mass is 20199 Da from positions 1 - 175. Determined by ESI. Ref.17

Molecular mass is 20278 Da from positions 1 - 175. Determined by ESI. With 1 phosphate group. Ref.17

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   DiseaseCardiomyopathy
Cataract
Disease mutation
Myofibrillar myopathy
   LigandMetal-binding
Zinc
   Molecular functionChaperone
Eye lens protein
   PTMAcetylation
Glycoprotein
Oxidation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

apoptotic process involved in morphogenesis

Inferred from electronic annotation. Source: Ensembl

cellular response to gamma radiation

Inferred from mutant phenotype PubMed 23269685. Source: MGI

glucose metabolic process

Inferred from electronic annotation. Source: Ensembl

lens development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

microtubule polymerization or depolymerization

Inferred from electronic annotation. Source: Ensembl

muscle contraction

Traceable author statement Ref.29. Source: ProtInc

muscle organ development

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from direct assay PubMed 14752512. Source: HGNC

negative regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

negative regulation of intracellular transport

Inferred from direct assay PubMed 14752512. Source: HGNC

negative regulation of reactive oxygen species metabolic process

Inferred from electronic annotation. Source: Ensembl

protein folding

Non-traceable author statement Ref.29. Source: ProtInc

protein homooligomerization

Inferred from direct assay PubMed 16303126. Source: UniProtKB

regulation of cell death

Inferred from mutant phenotype PubMed 23269685. Source: MGI

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

stress-activated MAPK cascade

Inferred from electronic annotation. Source: Ensembl

tubulin complex assembly

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

Z disc

Inferred from electronic annotation. Source: Ensembl

actin filament bundle

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay Ref.24. Source: UniProtKB

cytosol

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

microtubule cytoskeleton

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay Ref.24. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionidentical protein binding

Inferred from physical interaction Ref.30PubMed 23188086. Source: IntAct

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 14752512. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.31. Source: UniProtKB

structural constituent of eye lens

Inferred from electronic annotation. Source: UniProtKB-KW

unfolded protein binding

Inferred from physical interaction PubMed 16303126. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 175175Alpha-crystallin B chain
PRO_0000125907

Sites

Metal binding831Zinc 1 By similarity
Metal binding1041Zinc 2 Probable
Metal binding1061Zinc 2 By similarity
Metal binding1111Zinc 1 Probable
Metal binding1191Zinc 1 Probable
Site481Susceptible to oxidation
Site601Susceptible to oxidation
Site681Susceptible to oxidation

Amino acid modifications

Modified residue11N-acetylmethionine Probable Ref.14
Modified residue191Phosphoserine Ref.15
Modified residue451Phosphoserine Ref.15 Ref.20
Modified residue591Phosphoserine Ref.15 Ref.20
Modified residue921N6-acetyllysine; partial Ref.21 Ref.27
Modified residue1661N6-acetyllysine Ref.27
Glycosylation1701O-linked (GlcNAc) By similarity

Natural variations

Natural variant411S → Y.
Corresponds to variant rs2234703 [ dbSNP | Ensembl ].
VAR_014607
Natural variant511P → L.
Corresponds to variant rs2234704 [ dbSNP | Ensembl ].
VAR_014608
Natural variant1091D → H in MFM2. Ref.34
VAR_069528
Natural variant1201R → G in MFM2; decreased interactions with wild-type CRYAA and CRYAB but increased interactions with wild-type CRYBB2 and CRYGC. Ref.29 Ref.30
Corresponds to variant rs28929489 [ dbSNP | Ensembl ].
VAR_007899
Natural variant1541G → S in CMD1II. Ref.33
VAR_070035
Natural variant1571R → H in CMD1II. Ref.32
VAR_070036

Experimental info

Sequence conflict1651E → K in AAC19161. Ref.4
Sequence conflict1751K → KKMPFLELHFLKQESFPTSE in AAC19161. Ref.4

Secondary structure

........................ 175
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02511 [UniParc].

Last modified January 1, 1990. Version 2.
Checksum: AE08BED46B7849CB

FASTA17520,159
        10         20         30         40         50         60 
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR PPSFLRAPSW 

        70         80         90        100        110        120 
FDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR 

       130        140        150        160        170 
KYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVT AAPKK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Antigens recognized by autologous antibody in patients with renal-cell carcinoma."
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.
Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract]
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]"Association of the chaperone alphaB-crystallin with titin in heart muscle."
Bullard B., Ferguson C., Minajeva A., Leake M.C., Gautel M., Labeit D., Ding L., Labeit S., Horwitz J., Leonard K.R., Linke W.A.
J. Biol. Chem. 279:7917-7924(2004) [PubMed] [Europe PMC] [Abstract]
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]"Alpha B-crystallin mutation in dilated cardiomyopathy."
Inagaki N., Hayashi T., Arimura T., Koga Y., Takahashi M., Shibata H., Teraoka K., Chikamori T., Yamashina A., Kimura A.
Biochem. Biophys. Res. Commun. 342:379-386(2006) [PubMed] [Europe PMC] [Abstract]
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]"A novel CRYAB mutation resulting in multisystemic disease."
Sacconi S., Feasson L., Antoine J.C., Pecheux C., Bernard R., Cobo A.M., Casarin A., Salviati L., Desnuelle C., Urtizberea A.
Neuromuscul. Disord. 22:66-72(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MFM2 HIS-109.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS8351.1.
PIRCYHUAB. A35332.
RefSeqNP_001276736.1. NM_001289807.1.
NP_001276737.1. NM_001289808.1.
NP_001876.1. NM_001885.2.
UniGeneHs.53454.
Hs.703770.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
DisProtDP00445.
ProteinModelPortalP02511.
SMRP02511. Positions 1-175.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107800. 55 interactions.
DIPDIP-35017N.
IntActP02511. 16 interactions.
MINTMINT-221013.
STRING9606.ENSP00000227251.

PTM databases

PhosphoSiteP02511.
UniCarbKBP02511.

Polymorphism databases

DMDM117385.

2D gel databases

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

Proteomic databases

MaxQBP02511.
PaxDbP02511.
PRIDEP02511.

Protocols and materials databases

DNASU1410.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000227251; ENSP00000227251; ENSG00000109846.
ENST00000526180; ENSP00000436051; ENSG00000109846.
ENST00000527950; ENSP00000437149; ENSG00000109846.
ENST00000531198; ENSP00000434247; ENSG00000109846.
ENST00000533475; ENSP00000433560; ENSG00000109846.
ENST00000571634; ENSP00000460615; ENSG00000263007.
ENST00000572605; ENSP00000459924; ENSG00000263007.
ENST00000573313; ENSP00000459140; ENSG00000263007.
ENST00000574550; ENSP00000461777; ENSG00000263007.
ENST00000576088; ENSP00000459809; ENSG00000263007.
GeneID1410.
KEGGhsa:1410.
UCSCuc001pmf.1. human.

Organism-specific databases

CTD1410.
GeneCardsGC11M111813.
GeneReviewsCRYAB.
HGNCHGNC:2389. CRYAB.
HPACAB002053.
CAB040560.
HPA028724.
MIM123590. gene.
608810. phenotype.
613763. phenotype.
613869. phenotype.
615184. phenotype.
neXtProtNX_P02511.
Orphanet98910. Alpha-crystallinopathy.
154. Familial isolated dilated cardiomyopathy.
280553. Fatal infantile hypertonic myofibrillar myopathy.
98993. Posterior polar cataract.
98995. Zonular cataract.
PharmGKBPA26907.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG246790.
HOVERGENHBG054766.
InParanoidP02511.
KOK09542.
OMARKQAPGP.
PhylomeDBP02511.
TreeFamTF105049.

Gene expression databases

ArrayExpressP02511.
BgeeP02511.
CleanExHS_CRYAB.
GenevestigatorP02511.

Family and domain databases

Gene3D2.60.40.790. 1 hit.
InterProIPR002068. a-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR012273. Alpha-crystallin_B.
IPR003090. Alpha-crystallin_N.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PANTHERPTHR11527:SF37. PTHR11527:SF37. 1 hit.
PfamPF00525. Crystallin. 1 hit.
PF00011. HSP20. 1 hit.
[Graphical view]
PIRSFPIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSPR00299. ACRYSTALLIN.
SUPFAMSSF49764. SSF49764. 1 hit.
PROSITEPS01031. HSP20. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCRYAB. human.
EvolutionaryTraceP02511.
GeneWikiCRYAB.
GenomeRNAi1410.
NextBio5765.
PMAP-CutDBP02511.
PROP02511.
SOURCESearch...

Entry information

Entry nameCRYAB_HUMAN
AccessionPrimary (citable) accession number: P02511
Secondary accession number(s): B0YIX0 expand/collapse secondary AC list , O43416, Q9UC37, Q9UC38, Q9UC39, Q9UC40, Q9UC41
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1990
Last modified: July 9, 2014
This is version 174 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM