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Beta-crystallin B1 (Beta-B1 crystallin)

 CRBB1_HUMAN             Reviewed;         252 AA.
P53674;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
18-JUL-2018, entry version 172.
RecName: Full=Beta-crystallin B1;
AltName: Full=Beta-B1 crystallin;
Name=CRYBB1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-22 AND 25-252,
CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS
SPECTROMETRY.
TISSUE=Lens;
PubMed=8626774;
David L.L., Lampi K.J., Lund A.L., Smith J.B.;
"The sequence of human betaB1-crystallin cDNA allows mass
spectrometric detection of betaB1 protein missing portions of its N-
terminal extension.";
J. Biol. Chem. 271:4273-4279(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
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.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
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.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 200-246.
PubMed=8575764; DOI=10.1006/geno.1995.9947;
Hulsebos T.J.M., Gilbert D.J., Delattre O., Smink L.J., Dunham I.,
Westerveld A., Thomas G., Jenkins N.A., Copeland N.G.;
"Assignment of the beta B1 crystallin gene (CRYBB1) to human
chromosome 22 and mouse chromosome 5.";
Genomics 29:712-718(1995).
[6]
INVOLVEMENT IN CTRCT17.
PubMed=12360425; DOI=10.1086/344212;
Mackay D.S., Boskovska O.B., Knopf H.L., Lampi K.J., Shiels A.;
"A nonsense mutation in CRYBB1 associated with autosomal dominant
cataract linked to human chromosome 22q.";
Am. J. Hum. Genet. 71:1216-1221(2002).
[7]
CHARACTERIZATION.
PubMed=15667225; DOI=10.1021/bi048419f;
Annunziata O., Pande A., Pande J., Ogun O., Lubsen N.H., Benedek G.B.;
"Oligomerization and phase transitions in aqueous solutions of native
and truncated human beta B1-crystallin.";
Biochemistry 44:1316-1328(2005).
[8]
INVOLVEMENT IN CONGENITAL CATARACT-MICROCORNEA SYNDROME.
PubMed=16110300;
Willoughby C.E., Shafiq A., Ferrini W., Chan L.L., Billingsley G.,
Priston M., Mok C., Chandna A., Kaye S., Heon E.;
"CRYBB1 mutation associated with congenital cataract and
microcornea.";
Mol. Vis. 11:587-593(2005).
[9]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 43-252.
PubMed=14573871; DOI=10.1110/ps.03265903;
Van Montfort R.L., Bateman O.A., Lubsen N.H., Slingsby C.;
"Crystal structure of truncated human betaB1-crystallin.";
Protein Sci. 12:2606-2612(2003).
[10]
INVOLVEMENT IN CTRCT17.
PubMed=17460281; DOI=10.1167/iovs.06-1019;
Cohen D., Bar-Yosef U., Levy J., Gradstein L., Belfair N., Ofir R.,
Joshua S., Lifshitz T., Carmi R., Birk O.S.;
"Homozygous CRYBB1 deletion mutation underlies autosomal recessive
congenital cataract.";
Invest. Ophthalmol. Vis. Sci. 48:2208-2213(2007).
[11]
INVOLVEMENT IN CONGENITAL CATARACT-MICROCORNEA SYNDROME, VARIANT
ARG-129, AND CHARACTERIZATION OF VARIANT ARG-129.
PubMed=21972112; DOI=10.1002/humu.21436;
Wang K.J., Wang S., Cao N.-Q., Yan Y.-B., Zhu S.Q.;
"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.";
Hum. Mutat. 32:E2050-E2060(2011).
[12]
VARIANT CTRCT17 PHE-96.
PubMed=23508780; DOI=10.1007/s00439-013-1289-0;
Reis L.M., Tyler R.C., Muheisen S., Raggio V., Salviati L., Han D.P.,
Costakos D., Yonath H., Hall S., Power P., Semina E.V.;
"Whole exome sequencing in dominant cataract identifies a new
causative factor, CRYBA2, and a variety of novel alleles in known
genes.";
Hum. Genet. 132:761-770(2013).
-!- FUNCTION: Crystallins are the dominant structural components of
the vertebrate eye lens.
-!- SUBUNIT: Homo/heterodimer, or complexes of higher-order. The
structure of beta-crystallin oligomers seems to be stabilized
through interactions between the N-terminal arms.
-!- INTERACTION:
P05813:CRYBA1; NbExp=9; IntAct=EBI-7519424, EBI-7043337;
P54274:TERF1; NbExp=2; IntAct=EBI-7519424, EBI-710997;
-!- DOMAIN: Has a two-domain beta-structure, folded into four very
similar Greek key motifs.
-!- PTM: Specific cleavages in the N-terminal arm occur during lens
maturation and give rise to truncated forms, leading to impaired
oligomerization and protein insolubilization.
-!- MASS SPECTROMETRY: Mass=27941; Mass_error=6; Method=Electrospray;
Range=2-252; Evidence={ECO:0000269|PubMed:8626774};
-!- DISEASE: Cataract 17, multiple types (CTRCT17) [MIM:611544]: 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.
CTRCT17 includes nuclear and pulverulent cataracts, among others.
Nuclear cataracts affect the central nucleus of the eye, 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. Pulverulent cataracts are characterized by a dust-like,
'pulverised' appearance of the opacities which can be found in any
part of the lens. {ECO:0000269|PubMed:12360425,
ECO:0000269|PubMed:17460281, ECO:0000269|PubMed:23508780}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Note=CRYBB1 mutations may be a cause of congenital
cataract and microcornea syndrome, a disease 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 (PubMed:16110300 and
PubMed:21972112). {ECO:0000305|PubMed:16110300,
ECO:0000305|PubMed:21972112}.
-!- SIMILARITY: Belongs to the beta/gamma-crystallin family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Eye disease Crystallin, beta-B1 (CRYBB1);
Note=Leiden Open Variation Database (LOVD);
URL="http://www.lovd.nl/CRYBB1";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U35340; AAC50383.1; -; mRNA.
EMBL; CR456425; CAG30311.1; -; mRNA.
EMBL; Z95115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC036790; AAH36790.1; -; mRNA.
EMBL; X86398; CAA60150.1; -; Genomic_DNA.
CCDS; CCDS13840.1; -.
PIR; S55441; S55441.
RefSeq; NP_001878.1; NM_001887.3.
RefSeq; XP_011528201.1; XM_011529899.2.
UniGene; Hs.37135; -.
PDB; 1OKI; X-ray; 1.40 A; A/B=43-252.
PDBsum; 1OKI; -.
ProteinModelPortal; P53674; -.
SMR; P53674; -.
BioGrid; 107804; 5.
IntAct; P53674; 9.
MINT; P53674; -.
STRING; 9606.ENSP00000215939; -.
iPTMnet; P53674; -.
PhosphoSitePlus; P53674; -.
BioMuta; CRYBB1; -.
DMDM; 1706116; -.
EPD; P53674; -.
PaxDb; P53674; -.
PeptideAtlas; P53674; -.
PRIDE; P53674; -.
ProteomicsDB; 56607; -.
DNASU; 1414; -.
Ensembl; ENST00000215939; ENSP00000215939; ENSG00000100122.
GeneID; 1414; -.
KEGG; hsa:1414; -.
UCSC; uc003acy.2; human.
CTD; 1414; -.
DisGeNET; 1414; -.
EuPathDB; HostDB:ENSG00000100122.5; -.
GeneCards; CRYBB1; -.
HGNC; HGNC:2397; CRYBB1.
HPA; CAB010058; -.
HPA; HPA003448; -.
MalaCards; CRYBB1; -.
MIM; 600929; gene.
MIM; 611544; phenotype.
neXtProt; NX_P53674; -.
OpenTargets; ENSG00000100122; -.
Orphanet; 1377; Cataract-microcornea syndrome.
Orphanet; 98991; Nuclear cataract.
Orphanet; 98984; Pulverulent cataract.
PharmGKB; PA26911; -.
eggNOG; ENOG410IJ9M; Eukaryota.
eggNOG; ENOG410ZYKU; LUCA.
GeneTree; ENSGT00760000118812; -.
HOGENOM; HOG000234388; -.
HOVERGEN; HBG003364; -.
InParanoid; P53674; -.
OMA; HKISLFE; -.
OrthoDB; EOG091G0JIZ; -.
PhylomeDB; P53674; -.
TreeFam; TF331401; -.
SIGNOR; P53674; -.
EvolutionaryTrace; P53674; -.
GeneWiki; CRYBB1; -.
GenomeRNAi; 1414; -.
PMAP-CutDB; P53674; -.
PRO; PR:P53674; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000100122; -.
CleanEx; HS_CRYBB1; -.
Genevisible; P53674; HS.
GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
GO; GO:0007601; P:visual perception; TAS:ProtInc.
InterPro; IPR001064; Beta/gamma_crystallin.
InterPro; IPR033059; CRYBB1.
InterPro; IPR011024; G_crystallin-like.
PANTHER; PTHR11818:SF12; PTHR11818:SF12; 1.
Pfam; PF00030; Crystall; 2.
PRINTS; PR01367; BGCRYSTALLIN.
SMART; SM00247; XTALbg; 2.
SUPFAM; SSF49695; SSF49695; 1.
PROSITE; PS50915; CRYSTALLIN_BETA_GAMMA; 4.
1: Evidence at protein level;
3D-structure; Acetylation; Cataract; Complete proteome;
Direct protein sequencing; Disease mutation; Eye lens protein;
Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:8626774}.
CHAIN 2 252 Beta-crystallin B1.
/FTId=PRO_0000057550.
DOMAIN 59 98 Beta/gamma crystallin 'Greek key' 1.
{ECO:0000255|PROSITE-ProRule:PRU00028}.
DOMAIN 99 143 Beta/gamma crystallin 'Greek key' 2.
{ECO:0000255|PROSITE-ProRule:PRU00028}.
DOMAIN 149 190 Beta/gamma crystallin 'Greek key' 3.
{ECO:0000255|PROSITE-ProRule:PRU00028}.
DOMAIN 191 233 Beta/gamma crystallin 'Greek key' 4.
{ECO:0000255|PROSITE-ProRule:PRU00028}.
REGION 2 58 N-terminal arm.
REGION 144 148 Connecting peptide.
REGION 235 252 C-terminal arm.
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:8626774}.
VARIANT 96 96 V -> F (in CTRCT17).
{ECO:0000269|PubMed:23508780}.
/FTId=VAR_070030.
VARIANT 129 129 S -> R (probable disease-associated
mutation found in a family with autosomal
dominant congenital cataract and
microcornea; significantly decreased
thermal stability of CRYBB1/CRYBA1-
crystallin heteromer but not CRYBB1-
crystallin homomer; dbSNP:rs1114167433).
{ECO:0000269|PubMed:21972112}.
/FTId=VAR_065296.
STRAND 60 66 {ECO:0000244|PDB:1OKI}.
TURN 67 69 {ECO:0000244|PDB:1OKI}.
STRAND 70 78 {ECO:0000244|PDB:1OKI}.
TURN 83 87 {ECO:0000244|PDB:1OKI}.
STRAND 93 98 {ECO:0000244|PDB:1OKI}.
STRAND 101 106 {ECO:0000244|PDB:1OKI}.
HELIX 107 109 {ECO:0000244|PDB:1OKI}.
STRAND 110 116 {ECO:0000244|PDB:1OKI}.
STRAND 118 121 {ECO:0000244|PDB:1OKI}.
HELIX 124 127 {ECO:0000244|PDB:1OKI}.
STRAND 138 141 {ECO:0000244|PDB:1OKI}.
STRAND 150 156 {ECO:0000244|PDB:1OKI}.
HELIX 157 159 {ECO:0000244|PDB:1OKI}.
STRAND 160 169 {ECO:0000244|PDB:1OKI}.
HELIX 174 177 {ECO:0000244|PDB:1OKI}.
STRAND 185 198 {ECO:0000244|PDB:1OKI}.
TURN 199 201 {ECO:0000244|PDB:1OKI}.
STRAND 202 208 {ECO:0000244|PDB:1OKI}.
STRAND 210 215 {ECO:0000244|PDB:1OKI}.
HELIX 216 219 {ECO:0000244|PDB:1OKI}.
STRAND 228 232 {ECO:0000244|PDB:1OKI}.
SEQUENCE 252 AA; 28023 MW; 93D81A9C95A86F7F CRC64;
MSQAAKASAS ATVAVNPGPD TKGKGAPPAG TSPSPGTTLA PTTVPITSAK AAELPPGNYR
LVVFELENFQ GRRAEFSGEC SNLADRGFDR VRSIIVSAGP WVAFEQSNFR GEMFILEKGE
YPRWNTWSSS YRSDRLMSFR PIKMDAQEHK ISLFEGANFK GNTIEIQGDD APSLWVYGFS
DRVGSVKVSS GTWVGYQYPG YRGYQYLLEP GDFRHWNEWG AFQPQMQSLR RLRDKQWHLE
GSFPVLATEP PK


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