P53674 (CRBB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-crystallin B1

Alternative name(s):
Beta-B1 crystallin

Gene names

Name:

CRYBB1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	252 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Crystallins are the dominant structural components of the vertebrate eye lens.
Subunit structure	Homo/heterodimer, or complexes of higher-order. The structure of beta-crystallin oligomers seems to be stabilized through interactions between the N-terminal arms.
Domain	Has a two-domain beta-structure, folded into four very similar Greek key motifs.
Post-translational modification	Specific cleavages in the N-terminal arm occur during lens maturation and give rise to truncated forms, leading to impaired oligomerization and protein insolubilization.
Involvement in disease	Cataract, congenital, nuclear, autosomal recessive 3 (CATCN3) [MIM:611544]: A congenital cataract affecting the central nucleus of the eye. Nucler cataracts are often not highly visually significant. The density of the opacities varies greatly from fine dots to a dense, white and chalk-like, central cataract. The condition is usually bilateral. Nuclear cataracts are often combined with opacified cortical fibers encircling the nuclear opacity, which are referred to as cortical riders. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Cataract-microcornea syndrome (CAMIS) [MIM:116150]: Characterized by the association of congenital cataract and microcornea without any other systemic anomaly or dysmorphism. Clinical findings include a corneal diameter inferior to 10 mm in both meridians in an otherwise normal eye, and an inherited cataract, which is most often bilateral posterior polar with opacification in the lens periphery. The cataract progresses to form a total cataract after visual maturity has been achieved, requiring cataract extraction in the first to third decade of life. Microcornea-cataract syndrome can be associated with other rare ocular manifestations, including myopia, iris coloboma, sclerocornea and Peters anomaly. Transmission is in most cases autosomal dominant, but cases of autosomal recessive transmission have recently been described. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.10
Sequence similarities	Belongs to the beta/gamma-crystallin family. Contains 4 beta/gamma crystallin 'Greek key' domains.
Mass spectrometry	Molecular mass is 27941±6 Da from positions 2 - 252. Determined by ESI. Ref.1

Ontologies

Keywords
Disease	Cataract Disease mutation
Domain	Repeat
Molecular function	Eye lens protein
PTM	Acetylation Oxidation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	visual perception Traceable author statement Ref.1. Source: ProtInc
Molecular_function	structural constituent of eye lens Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 252

251

Beta-crystallin B1

PRO_0000057550

Regions

Domain

59 – 98

40

Beta/gamma crystallin 'Greek key' 1

Domain

99 – 143

45

Beta/gamma crystallin 'Greek key' 2

Domain

149 – 190

42

Beta/gamma crystallin 'Greek key' 3

Domain

191 – 233

43

Beta/gamma crystallin 'Greek key' 4

Region

2 – 58

57

N-terminal arm

Region

144 – 148

5

Connecting peptide

Region

235 – 252

18

C-terminal arm

Sites

Site

216

1

Susceptible to oxidation

Site

226

1

Susceptible to oxidation

Amino acid modifications

Modified residue

2

1

N-acetylserine

Natural variations

Natural variant

129

1

S → R in CAMIS; significantly decreased thermal stability of CRYBB1/CRYBA1-crystallin heteromer but not CRYBB1-crystallin homomer. Ref.10

VAR_065296

Secondary structure

1

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252

Helix Strand Turn

Details...

Beta strand

60 – 66

7

Turn

67 – 69

3

Beta strand

70 – 78

9

Turn

83 – 87

5

Beta strand

93 – 98

6

Beta strand

101 – 106

6

Helix

107 – 109

3

Beta strand

110 – 116

7

Beta strand

118 – 121

4

Helix

124 – 127

4

Beta strand

138 – 141

4

Beta strand

150 – 156

7

Helix

157 – 159

3

Beta strand

160 – 169

10

Helix

174 – 177

4

Beta strand

185 – 198

14

Turn

199 – 201

3

Beta strand

202 – 208

7

Beta strand

210 – 215

6

Helix

216 – 219

4

Beta strand

228 – 232

5

Sequences

	Sequence		Length	Mass (Da)
	P53674 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 93D81A9C95A86F7F	FASTA	252	28,023
	10 20 30 40 50 60 MSQAAKASAS ATVAVNPGPD TKGKGAPPAG TSPSPGTTLA PTTVPITSAK AAELPPGNYR 70 80 90 100 110 120 LVVFELENFQ GRRAEFSGEC SNLADRGFDR VRSIIVSAGP WVAFEQSNFR GEMFILEKGE 130 140 150 160 170 180 YPRWNTWSSS YRSDRLMSFR PIKMDAQEHK ISLFEGANFK GNTIEIQGDD APSLWVYGFS 190 200 210 220 230 240 DRVGSVKVSS GTWVGYQYPG YRGYQYLLEP GDFRHWNEWG AFQPQMQSLR RLRDKQWHLE 250 GSFPVLATEP PK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The sequence of human betaB1-crystallin cDNA allows mass spectrometric detection of betaB1 protein missing portions of its N-terminal extension." David L.L., Lampi K.J., Lund A.L., Smith J.B. J. Biol. Chem. 271:4273-4279(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-22 AND 25-252, MASS SPECTROMETRY. Tissue: Lens.
[2]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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].
[5]	"Assignment of the beta B1 crystallin gene (CRYBB1) to human chromosome 22 and mouse chromosome 5." Hulsebos T.J.M., Gilbert D.J., Delattre O., Smink L.J., Dunham I., Westerveld A., Thomas G., Jenkins N.A., Copeland N.G. Genomics 29:712-718(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 200-246.
[6]	"Oligomerization and phase transitions in aqueous solutions of native and truncated human beta B1-crystallin." Annunziata O., Pande A., Pande J., Ogun O., Lubsen N.H., Benedek G.B. Biochemistry 44:1316-1328(2005) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[7]	"CRYBB1 mutation associated with congenital cataract and microcornea." Willoughby C.E., Shafiq A., Ferrini W., Chan L.L., Billingsley G., Priston M., Mok C., Chandna A., Kaye S., Heon E. Mol. Vis. 11:587-593(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN CAMIS.
[8]	"Crystal structure of truncated human betaB1-crystallin." Van Montfort R.L., Bateman O.A., Lubsen N.H., Slingsby C. Protein Sci. 12:2606-2612(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 43-252.
[9]	"Homozygous CRYBB1 deletion mutation underlies autosomal recessive congenital cataract." Cohen D., Bar-Yosef U., Levy J., Gradstein L., Belfair N., Ofir R., Joshua S., Lifshitz T., Carmi R., Birk O.S. Invest. Ophthalmol. Vis. Sci. 48:2208-2213(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN CATCN3.
[10]	"A novel mutation in CRYBB1 associated with congenital cataract-microcornea syndrome: the p.Ser129Arg mutation destabilizes the betaB1/betaA3-crystallin heteromer but not the betaB1-crystallin homomer." Wang K.J., Wang S., Cao N.-Q., Yan Y.-B., Zhu S.Q. Hum. Mutat. 32:E2050-E2060(2011) Cited for: VARIANT CAMIS ARG-129, CHARACTERIZATION OF VARIANT CAMIS ARG-129.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U35340 mRNA. Translation: AAC50383.1.
CR456425 mRNA. Translation: CAG30311.1.
Z95115 Genomic DNA. Translation: CAB08268.1.
BC036790 mRNA. Translation: AAH36790.1.
X86398 Genomic DNA. Translation: CAA60150.1.

IPI

IPI00216092.

PIR

S55441.

RefSeq

NP_001878.1. NM_001887.3.

UniGene

Hs.37135.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OKI	X-ray	1.40	A/B	43-252	[»]

ProteinModelPortal

P53674.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-5161833.

STRING

9606.ENSP00000215939.

PTM databases

PhosphoSite

P53674.

Polymorphism databases

DMDM

1706116.

Proteomic databases

PaxDb

P53674.

PeptideAtlas

P53674.

PRIDE

P53674.

Protocols and materials databases

DNASU

1414.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000215939; ENSP00000215939; ENSG00000100122.

GeneID

1414.

KEGG

hsa:1414.

UCSC

uc003acy.1. human.

Organism-specific databases

CTD

1414.

GeneCards

GC22M026995.

HGNC

HGNC:2397. CRYBB1.

MIM

116150. phenotype.
600929. gene+phenotype.
611544. phenotype.

neXtProt

NX_P53674.

Orphanet

1377. Cataract-microcornea syndrome.
98991. Nuclear cataract.
98984. Pulverulent cataract.

PharmGKB

PA26911.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG40509.

HOGENOM

HOG000234388.

HOVERGEN

HBG003364.

InParanoid

P53674.

OMA

MSFRPIK.

OrthoDB

EOG4Z0B6N.

Gene expression databases

Bgee

P53674.

CleanEx

HS_CRYBB1.

Genevestigator

P53674.

GermOnline

ENSG00000100122. Homo sapiens.

Family and domain databases

InterPro

IPR001064. Beta/gamma_crystallin.
IPR011024. G_crystallin-rel.
[Graphical view]

Pfam

PF00030. Crystall. 2 hits.
[Graphical view]

PRINTS

PR01367. BGCRYSTALLIN.

SMART

SM00247. XTALbg. 2 hits.
[Graphical view]

SUPFAM

SSF49695. G_crystallin_SF. 1 hit.

PROSITE

PS50915. CRYSTALLIN_BETA_GAMMA. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P53674.

GenomeRNAi

1414.

NextBio

5785.

PMAP-CutDB

P53674.

SOURCE

Search...

Entry information

Entry name

CRBB1_HUMAN

Accession

Primary (citable) accession number: P53674

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 131 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.