Reviewed,
UniProtKB/Swiss-Prot P02511 (CRYAB_HUMAN)
Last modified
November 3, 2009.
Version 121.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Alpha-crystallin B chain Alternative name(s): Alpha(B)-crystallin Rosenthal fiber component Heat shock protein beta-5 Short name=HspB5 Renal carcinoma antigen NY-REN-27 | ||||
| Gene names |
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| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 175 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | May contribute to the transparency and refractive index of the lens. |
| Subunit structure | Homodimer. Aggregates with homologous proteins, including CRYAA and the small heat shock protein HSPB1, to form large heteromeric complexes. Interacts with HSPBAP1 and TTN/titin. Ref.14 Ref.18 Ref.23 |
| Tissue specificity | Lens as well as other tissues. |
| Involvement in disease | Seen as Rosenthal fiber protein in the brain tissue of patients with Alexander disease. Defects in CRYAB are the cause of alpha-B crystallinopathy [MIM:608810]. Alpha-B crystallinopathy is a an autosomal dominant form of desmin-related myopathy (DRM) that results in weakness of the proximal and distal limb muscle (including neck, velopharynx, and trunk muscles), signs of cardiomyopathy and cataract. Patients with progressive myopathy characterized by myofibrillar degeneration that commences at the Z-disk, have been described. Mutations truncate the essential C-terminal domain of the protein required for the chaperone function. Crystallins do not turn over as the lens ages, providing ample opportunity for post-translational modifications or oxidations. These modifications may change crystallin solubility properties and favor senile cataract. |
| 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 component | Eye lens protein |
| Coding sequence diversity | Polymorphism |
| Disease | Cataract Desmin-related myopathy Disease mutation |
| PTM | Acetylation Glycoprotein Methylation Oxidation Phosphoprotein |
| Technical term | 3D-structure Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | anti-apoptosis Inferred from direct assay. Source: HGNC muscle contraction Ref.24Traceable author statement. Source: ProtInc negative regulation of intracellular transportInferred from direct assay. Source: HGNC protein folding Ref.24Non-traceable author statement. Source: ProtInc protein homooligomerizationInferred from direct assay. Source: UniProtKB response to heatInferred from electronic annotation. Source: InterPro |
| Molecular function | structural constituent of eye lens Inferred from electronic annotation. Source: UniProtKB-KW unfolded protein bindingInferred from physical interaction. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 175 | 175 | Alpha-crystallin B chain | PRO_0000125907 | |||||
Sites | |||||||||
| Site | 48 | 1 | Susceptible to oxidation | ||||||
| Site | 60 | 1 | Susceptible to oxidation | ||||||
| Site | 68 | 1 | Susceptible to oxidation | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine Probable Ref.14 | ||||||
| Modified residue | 19 | 1 | Phosphoserine Ref.15 Ref.21 | ||||||
| Modified residue | 21 | 1 | Phosphoserine Ref.21 | ||||||
| Modified residue | 22 | 1 | Omega-N-methylated arginine Ref.21 | ||||||
| Modified residue | 43 | 1 | Phosphoserine Ref.21 | ||||||
| Modified residue | 45 | 1 | Phosphoserine Ref.15 Ref.21 Ref.19 | ||||||
| Modified residue | 50 | 1 | Omega-N-methylated arginine Ref.21 | ||||||
| Modified residue | 53 | 1 | Phosphoserine Ref.21 | ||||||
| Modified residue | 59 | 1 | Phosphoserine Ref.15 Ref.21 Ref.19 | ||||||
| Modified residue | 76 | 1 | Phosphoserine Ref.21 | ||||||
| Modified residue | 92 | 1 | N6-acetyllysine; partial Ref.21 Ref.20 | ||||||
| Glycosylation | 170 | 1 | O-linked (GlcNAc) By similarity | ||||||
Natural variations | |||||||||
| Natural variant | 41 | 1 | S → Y: dbSNP rs2234703. | VAR_014607 | |||||
| Natural variant | 51 | 1 | P → L: dbSNP rs2234704. | VAR_014608 | |||||
| Natural variant | 120 | 1 | R → G in alpha-B crystallinopathy; decreased interactions with wild-type CRYAA and CRYAB but increased interactions with wild-type CRYBB2 and CRYGC. Ref.24 Ref.25 | VAR_007899 | |||||
Experimental info | |||||||||
| Sequence conflict | 165 | 1 | E → K in AAC19161. Ref.4 | ||||||
| Sequence conflict | 175 | 1 | K → KKMPFLELHFLKQESFPTSE in AAC19161. Ref.4 | ||||||
Sequences
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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: 838078] [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: 2387586] [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: 1407707] [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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [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. 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: 15489334] [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: 1560006] [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: 8999933] [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: 7498159] [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: 2539261] [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: 8142454] [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: 8175657] [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: 10508479] [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: 10930324] [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: 10751411] [Abstract] Cited for: INTERACTION WITH HSPBAP1. |
| [19] | "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: 11158243] [Abstract] Cited for: PHOSPHORYLATION AT SER-45 AND SER-59. |
| [20] | "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: 11369851] [Abstract] Cited for: ACETYLATION AT LYS-92. |
| [21] | "Shotgun identification of protein modifications from protein complexes and lens tissue." MacCoss M.J., McDonald W.H., Saraf A., Sadygov R., Clark J.M., Tasto J.J., Gould K.L., Wolters D., Washburn M., Weiss A., Clark J.I., Yates J.R. III Proc. Natl. Acad. Sci. U.S.A. 99:7900-7905(2002) [PubMed: 12060738] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-21; SER-43; SER-45; SER-53; SER-59 AND SER-76, METHYLATION AT ARG-22 AND ARG-50, ACETYLATION AT LYS-92, SUSCEPTIBILITY TO OXIDATION, MASS SPECTROMETRY. |
| [22] | "Myofibrillar myopathy caused by novel dominant negative alpha B-crystallin mutations." Selcen D., Engel A.G. Ann. Neurol. 54:804-810(2003) [PubMed: 14681890] [Abstract] Cited for: INVOLVEMENT IN ALPHA-B CRYSTALLINOPATHY. |
| [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: 14676215] [Abstract] Cited for: INTERACTION WITH TTN. |
| [24] | "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: 9731540] [Abstract] Cited for: VARIANT ALPHA-B CRYSTALLINOPATHY GLY-120. |
| [25] | "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: 12601044] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS ALPHA-B CRYSTALLINOPATHY GLY-120. |
| [26] | "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: 19646995] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 67-157, HOMODIMER. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 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. | |||||||||||||
| IPI | IPI00021369. | ||||||||||||
| PIR | CYHUAB. A35332. | ||||||||||||
| RefSeq | NP_001876.1. | ||||||||||||
| UniGene | Hs.408767 | ||||||||||||
3D structure databases | |||||||||||||
| |||||||||||||
| DisProt | DP00445. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | P02511. 2 interactions. | ||||||||||||
| STRING | P02511. | ||||||||||||
PTM databases | |||||||||||||
| GlycoSuiteDB | P02511. | ||||||||||||
| PhosphoSite | P02511. | ||||||||||||
2-D gel databases | |||||||||||||
| SWISS-2DPAGE | P02511. | ||||||||||||
| HSC-2DPAGE | P02511. | ||||||||||||
| REPRODUCTION-2DPAGE | IPI00021369. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | P02511. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENST00000227251; ENSP00000227251; ENSG00000109846; Homo sapiens. [Genome view] | ||||||||||||
| GeneID | 1410. | ||||||||||||
| KEGG | hsa:1410. | ||||||||||||
| UCSC | uc001pmf.1. human. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 1410. | ||||||||||||
| GeneCards | GC11M111284. | ||||||||||||
| H-InvDB | HIX0010115. | ||||||||||||
| HGNC | HGNC:2389. CRYAB. | ||||||||||||
| HPA | CAB002053. | ||||||||||||
| MIM | 123590. gene+phenotype. 608810. phenotype. | ||||||||||||
| Orphanet | 98910. Alpha-cristallinopathy. 98993. Cataract, posterior polar. 98995. Cataract, zonular. 91492. Non-syndromic congenital cataract. | ||||||||||||
| PharmGKB | PA26907. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | P02511. | ||||||||||||
| HOVERGEN | P02511. | ||||||||||||
| OMA | DRYVIYL. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | P02511. | ||||||||||||
| Bgee | P02511. | ||||||||||||
| CleanEx | HS_CRYAB. | ||||||||||||
| Genevestigator | P02511. | ||||||||||||
| GermOnline | ENSG00000109846. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR001436. Alpha-crystallin/HSP. IPR012273. Alpha-crystallin_B. IPR003090. Alpha-crystallin_N. IPR002068. Hsp20. [Graphical view] | ||||||||||||
| PANTHER | PTHR11527:SF37. A-crystallin_B. 1 hit. | ||||||||||||
| Pfam | PF00525. Crystallin. 1 hit. PF00011. HSP20. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00299. ACRYSTALLIN. | ||||||||||||
| ProDom | PD001193. Crystallin_N. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||
| PROSITE | PS01031. HSP20. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other Resources | |||||||||||||
| NextBio | 5765. | ||||||||||||
| PMAP-CutDB | P02511. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | CRYAB_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P02511 Secondary accession number(s): B0YIX0 Q9UC41 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any 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
| Human chromosome 11 Human chromosome 11: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


