P02511 (CRYAB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CRYAB
Synonyms:	CRYA2

Organism

Homo sapiens (Human)

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.
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.24 Ref.29
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.25
Tissue specificity	Lens as well as other tissues.
Involvement in disease	Defects in CRYAB are the cause of myopathy myofibrillar type 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, hypetrophic cardiomyopathy, and cataract in a subset of patients. Ref.23 Ref.27 Ref.28 Defects in CRYAB are the cause of cataract posterior polar type 2 (CTPP2) [MIM:613763]. A subcapsular opacity, usually disk-shaped, located at the back of the lens. It can have a marked effect on visual acuity. Ref.19 Defects in CRYAB are the cause of myopathy myofibrillar fatal infantile hypertonic alpha-B crystallin-related (MFMFIH-CRYAB) [MIM:613869]. MFMFIH-CRYAB is 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.
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	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Disease	Cataract Disease mutation Myofibrillar myopathy
Molecular function	Eye lens protein
PTM	Acetylation Glycoprotein Methylation Oxidation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	anti-apoptosis Inferred from direct assay. Source: HGNC muscle contraction Traceable author statement. Source: ProtInc negative regulation of intracellular transport Inferred from direct assay. Source: HGNC protein folding Non-traceable author statement. Source: ProtInc protein homooligomerization Inferred from direct assay. Source: UniProtKB
Cellular component	cytoplasm Inferred from direct assay Ref.25. Source: UniProtKB nucleus Inferred from direct assay Ref.25. Source: UniProtKB
Molecular function	protein homodimerization activity Inferred from physical interaction Ref.29. Source: UniProtKB structural constituent of eye lens Inferred from electronic annotation. Source: UniProtKB-KW unfolded protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSPB8	Q9UJY1	2	EBI-739060,EBI-739074

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.22

Modified residue

21

1

Phosphoserine Ref.22

Modified residue

22

1

Omega-N-methylated arginine Ref.22

Modified residue

43

1

Phosphoserine Ref.22

Modified residue

45

1

Phosphoserine Ref.15 Ref.20 Ref.22

Modified residue

50

1

Omega-N-methylated arginine Ref.22

Modified residue

53

1

Phosphoserine Ref.22

Modified residue

59

1

Phosphoserine Ref.15 Ref.20 Ref.22

Modified residue

76

1

Phosphoserine Ref.22

Modified residue

92

1

N6-acetyllysine; partial Ref.21 Ref.22

Glycosylation

170

1

O-linked (GlcNAc) By similarity

Natural variations

Natural variant

41

1

S → Y.
Corresponds to variant rs2234703 [ dbSNP | Ensembl ].

VAR_014607

Natural variant

51

1

P → L.
Corresponds to variant rs2234704 [ dbSNP | Ensembl ].

VAR_014608

Natural variant

120

1

R → G in MFM2; decreased interactions with wild-type CRYAA and CRYAB but increased interactions with wild-type CRYBB2 and CRYGC. Ref.27 Ref.28
Corresponds to variant rs28929489 [ dbSNP | Ensembl ].

VAR_007899

Experimental info

Sequence conflict

165

1

E → K in AAC19161. Ref.4

Sequence conflict

175

1

K → KKMPFLELHFLKQESFPTSE in AAC19161. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

175

Helix Strand Turn

Details...

Beta strand

68 – 70

3

Beta strand

75 – 79

5

Helix

86 – 88

3

Beta strand

90 – 93

4

Beta strand

97 – 101

5

Beta strand

114 – 123

10

Helix

130 – 132

3

Beta strand

134 – 137

4

Beta strand

143 – 146

4

Sequences

	Sequence		Length	Mass (Da)
	P02511 [UniParc]. Last modified January 1, 1990. Version 2. Checksum: AE08BED46B7849CB	FASTA	175	20,159
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 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. , 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: 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]	"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: 11577372] [Abstract] Cited for: INVOLVEMENT IN CTPP2.
[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: 11158243] [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: 11369851] [Abstract] Cited for: ACETYLATION AT LYS-92.
[22]	"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. Tissue: Lens.
[23]	"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 MFM2.
[24]	"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.
[25]	"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: 19464326] [Abstract] Cited for: SUBCELLULAR LOCATION.
[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: 21337604] [Abstract] Cited for: INVOLVEMENT IN MFMFIH-CRYAB.
[27]	"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 MFM2 GLY-120.
[28]	"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 MFM2 GLY-120.
[29]	"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, HOMODIMERIZATION.
+	Additional computationally mapped references.

Web resources

GeneReviews

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.

IPI

IPI00021369.

PIR

CYHUAB. A35332.

RefSeq

NP_001876.1. NM_001885.1.

UniGene

Hs.53454.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
3L1G	X-ray	3.32	A	68-162	[»]

ProteinModelPortal

P02511.

SMR

P02511. Positions 68-162.

DisProt

DP00445.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35017N.

IntAct

P02511. 6 interactions.

MINT

MINT-221013.

STRING

P02511.

PTM databases

GlycoSuiteDB

P02511.

PhosphoSite

P02511.

Polymorphism databases

DMDM

117385.

2D gel databases

SWISS-2DPAGE

P02511.

REPRODUCTION-2DPAGE

IPI00021369.

UCD-2DPAGE

P02511.

Proteomic databases

PRIDE

P02511.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000227251; ENSP00000227251; ENSG00000109846.

GeneID

1410.

KEGG

hsa:1410.

UCSC

uc001pmf.1. human.

Organism-specific databases

CTD

1410.

GeneCards

GC11M111813.

HGNC

HGNC:2389. CRYAB.

HPA

CAB002053.
CAB040560.
HPA028724.

MIM

123590. gene.
608810. phenotype.
613763. phenotype.
613869. phenotype.

neXtProt

NX_P02511.

Orphanet

98910. Alpha-crystallinopathy.
98993. Posterior polar cataract.
98995. Zonular cataract.

PharmGKB

PA26907.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG15526.

GeneTree

ENSGT00550000074302.

HOVERGEN

HBG054766.

InParanoid

P02511.

OMA

PGPERTI.

OrthoDB

EOG4G1MHK.

PhylomeDB

P02511.

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.
IPR008978. HSP20-like_chaperone.
[Graphical view]

KO

K09542.

PANTHER

PTHR11527:SF37. A-crystallin_B. 1 hit.

Pfam

PF00525. Crystallin. 1 hit.
PF00011. HSP20. 1 hit.
[Graphical view]

PIRSF

PIRSF036514. Sm_HSP_B1. 1 hit.

PRINTS

PR00299. ACRYSTALLIN.

SUPFAM

SSF49764. HSP20_chap. 1 hit.

PROSITE

PS01031. HSP20. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

5765.

PMAP-CutDB

P02511.

SOURCE

Search...

Entry information

Entry name

CRYAB_HUMAN

Accession

Primary (citable) accession number: P02511
Secondary accession number(s): B0YIX0 , O43416, Q9UC37, Q9UC38, Q9UC39, Q9UC40, Q9UC41

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 1, 1990
Last modified:	January 25, 2012
This is version 147 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.