CRGB_HUMAN
ID CRGB_HUMAN Reviewed; 175 AA.
AC P07316; Q17RB5; Q53ST2;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Gamma-crystallin B;
DE AltName: Full=Gamma-B-crystallin;
DE AltName: Full=Gamma-crystallin 1-2;
GN Name=CRYGB; Synonyms=CRYG2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-111.
RX PubMed=4065573; DOI=10.1016/0378-1119(85)90218-5;
RA den Dunnen J.T., Moormann R.J.M., Cremers F.P.M., Schoenmakers J.G.G.;
RT "Two human gamma-crystallin genes are linked and riddled with Alu-
RT repeats.";
RL Gene 38:197-204(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-111.
RX PubMed=2777080; DOI=10.1016/0378-1119(89)90223-0;
RA den Dunnen J.T., van Neck J.W., Cremers F.P.M., Lubsen N.H.,
RA Schoenmakers J.G.G.;
RT "Nucleotide sequence of the rat gamma-crystallin gene region and comparison
RT with an orthologous human region.";
RL Gene 78:201-213(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-111.
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INVOLVEMENT IN CTRCT39.
RX PubMed=23288985;
RA Al Fadhli S., Abdelmoaty S., Al-Hajeri A., Behbehani A., Alkuraya F.;
RT "Novel crystallin gamma B mutations in a Kuwaiti family with autosomal
RT dominant congenital cataracts reveal genetic and clinical heterogeneity.";
RL Mol. Vis. 18:2931-2936(2012).
RN [6]
RP 3D-STRUCTURE MODELING.
RX PubMed=12507494; DOI=10.1016/s0006-291x(02)02895-4;
RA Salim A., Zaidi Z.H.;
RT "Homology models of human gamma-crystallins: structural study of the
RT extensive charge network in gamma-crystallins.";
RL Biochem. Biophys. Res. Commun. 300:624-630(2003).
RN [7]
RP 3D-STRUCTURE MODELING.
RX PubMed=14517968; DOI=10.1002/prot.10493;
RA Salim A., Bano A., Zaidi Z.H.;
RT "Prediction of possible sites for posttranslational modifications in human
RT gamma crystallins: effect of glycation on the structure of human gamma-B-
RT crystallin as analyzed by molecular modeling.";
RL Proteins 53:162-173(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-174.
RX PubMed=17628592; DOI=10.1016/j.jmb.2007.06.045;
RA Ebersbach H., Fiedler E., Scheuermann T., Fiedler M., Stubbs M.T.,
RA Reimann C., Proetzel G., Rudolph R., Fiedler U.;
RT "Affilin-novel binding molecules based on human gamma-B-crystallin, an all
RT beta-sheet protein.";
RL J. Mol. Biol. 372:172-185(2007).
RN [9]
RP VARIANTS ILE-73 AND LEU-111.
RX PubMed=12011157; DOI=10.1136/jmg.39.5.352;
RA Santhiya S.T., Shyam Manohar M., Rawlley D., Vijayalakshmi P.,
RA Namperumalsamy P., Gopinath P.M., Loester J., Graw J.;
RT "Novel mutations in the gamma-crystallin genes cause autosomal dominant
RT congenital cataracts.";
RL J. Med. Genet. 39:352-358(2002).
RN [10]
RP VARIANT LEU-111.
RX PubMed=12676897; DOI=10.1136/jmg.40.4.262;
RA Nandrot E., Slingsby C., Basak A., Cherif-Chefchaouni M., Benazzouz B.,
RA Hajaji Y., Boutayeb S., Gribouval O., Arbogast L., Berraho A., Abitbol M.,
RA Hilal L.;
RT "Gamma-D crystallin gene (CRYGD) mutation causes autosomal dominant
RT congenital cerulean cataracts.";
RL J. Med. Genet. 40:262-267(2003).
CC -!- FUNCTION: Crystallins are the dominant structural components of the
CC vertebrate eye lens.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- DOMAIN: Has a two-domain beta-structure, folded into four very similar
CC Greek key motifs.
CC -!- DISEASE: Cataract 39, multiple types (CTRCT39) [MIM:615188]: An
CC opacification of the crystalline lens of the eye that frequently
CC results in visual impairment or blindness. Opacities vary in
CC morphology, are often confined to a portion of the lens, and may be
CC static or progressive. In general, the more posteriorly located and
CC dense an opacity, the greater the impact on visual function. CTRCT39
CC includes lamellar, anterior polar, and complete cataracts.
CC {ECO:0000269|PubMed:23288985}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the beta/gamma-crystallin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M11971; AAA52113.1; -; Genomic_DNA.
DR EMBL; M11970; AAA52113.1; JOINED; Genomic_DNA.
DR EMBL; M19364; AAA52109.1; -; Genomic_DNA.
DR EMBL; AC016697; AAX93219.1; -; Genomic_DNA.
DR EMBL; BC074944; AAH74944.1; -; mRNA.
DR EMBL; BC074945; AAH74945.1; -; mRNA.
DR EMBL; BC117384; AAI17385.1; -; mRNA.
DR EMBL; BC117388; AAI17389.1; -; mRNA.
DR CCDS; CCDS2380.1; -.
DR PIR; A24520; CYHUG1.
DR RefSeq; NP_005201.2; NM_005210.3.
DR PDB; 2JDF; X-ray; 1.70 A; A=2-175.
DR PDB; 2JDG; X-ray; 2.00 A; A=2-175.
DR PDBsum; 2JDF; -.
DR PDBsum; 2JDG; -.
DR AlphaFoldDB; P07316; -.
DR SMR; P07316; -.
DR BioGRID; 107809; 5.
DR IntAct; P07316; 1.
DR STRING; 9606.ENSP00000260988; -.
DR iPTMnet; P07316; -.
DR PhosphoSitePlus; P07316; -.
DR BioMuta; CRYGB; -.
DR DMDM; 311033463; -.
DR MassIVE; P07316; -.
DR PaxDb; P07316; -.
DR PeptideAtlas; P07316; -.
DR PRIDE; P07316; -.
DR ProteomicsDB; 51986; -.
DR Antibodypedia; 34195; 67 antibodies from 16 providers.
DR DNASU; 1419; -.
DR Ensembl; ENST00000260988.5; ENSP00000260988.4; ENSG00000182187.4.
DR GeneID; 1419; -.
DR KEGG; hsa:1419; -.
DR MANE-Select; ENST00000260988.5; ENSP00000260988.4; NM_005210.4; NP_005201.2.
DR UCSC; uc002vcp.5; human.
DR CTD; 1419; -.
DR DisGeNET; 1419; -.
DR GeneCards; CRYGB; -.
DR HGNC; HGNC:2409; CRYGB.
DR HPA; ENSG00000182187; Not detected.
DR MalaCards; CRYGB; -.
DR MIM; 123670; gene.
DR MIM; 615188; phenotype.
DR neXtProt; NX_P07316; -.
DR OpenTargets; ENSG00000182187; -.
DR Orphanet; 98988; Early-onset anterior polar cataract.
DR Orphanet; 441452; Early-onset lamellar cataract.
DR Orphanet; 98994; Total early-onset cataract.
DR PharmGKB; PA26916; -.
DR VEuPathDB; HostDB:ENSG00000182187; -.
DR eggNOG; ENOG502RXJY; Eukaryota.
DR GeneTree; ENSGT00940000159232; -.
DR HOGENOM; CLU_081883_1_1_1; -.
DR InParanoid; P07316; -.
DR OMA; AYRMKIY; -.
DR OrthoDB; 1220704at2759; -.
DR PhylomeDB; P07316; -.
DR PathwayCommons; P07316; -.
DR SignaLink; P07316; -.
DR BioGRID-ORCS; 1419; 17 hits in 1063 CRISPR screens.
DR EvolutionaryTrace; P07316; -.
DR GeneWiki; CRYGB; -.
DR GenomeRNAi; 1419; -.
DR Pharos; P07316; Tbio.
DR PRO; PR:P07316; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P07316; protein.
DR Bgee; ENSG00000182187; Expressed in substantia nigra and 21 other tissues.
DR Genevisible; P07316; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005212; F:structural constituent of eye lens; IBA:GO_Central.
DR GO; GO:0002088; P:lens development in camera-type eye; IBA:GO_Central.
DR GO; GO:0070309; P:lens fiber cell morphogenesis; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; IBA:GO_Central.
DR InterPro; IPR001064; Beta/gamma_crystallin.
DR InterPro; IPR011024; G_crystallin-like.
DR Pfam; PF00030; Crystall; 2.
DR PRINTS; PR01367; BGCRYSTALLIN.
DR SMART; SM00247; XTALbg; 2.
DR SUPFAM; SSF49695; SSF49695; 1.
DR PROSITE; PS50915; CRYSTALLIN_BETA_GAMMA; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Cataract; Eye lens protein; Reference proteome; Repeat.
FT CHAIN 1..175
FT /note="Gamma-crystallin B"
FT /id="PRO_0000057586"
FT DOMAIN 2..40
FT /note="Beta/gamma crystallin 'Greek key' 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 41..83
FT /note="Beta/gamma crystallin 'Greek key' 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 89..129
FT /note="Beta/gamma crystallin 'Greek key' 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT DOMAIN 130..172
FT /note="Beta/gamma crystallin 'Greek key' 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00028"
FT REGION 84..88
FT /note="Connecting peptide"
FT VARIANT 73
FT /note="S -> I"
FT /evidence="ECO:0000269|PubMed:12011157"
FT /id="VAR_021140"
FT VARIANT 90
FT /note="R -> T (in dbSNP:rs2241980)"
FT /id="VAR_029517"
FT VARIANT 111
FT /note="I -> L (in dbSNP:rs796287)"
FT /evidence="ECO:0000269|PubMed:12011157,
FT ECO:0000269|PubMed:12676897, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2777080, ECO:0000269|PubMed:4065573"
FT /id="VAR_021141"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:2JDF"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:2JDF"
FT STRAND 13..21
FT /evidence="ECO:0007829|PDB:2JDF"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:2JDF"
FT STRAND 34..48
FT /evidence="ECO:0007829|PDB:2JDF"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:2JDF"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:2JDF"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:2JDF"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:2JDF"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:2JDF"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:2JDF"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:2JDF"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:2JDF"
FT STRAND 100..108
FT /evidence="ECO:0007829|PDB:2JDF"
FT HELIX 113..117
FT /evidence="ECO:0007829|PDB:2JDF"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:2JDF"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:2JDF"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:2JDF"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:2JDF"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:2JDF"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:2JDF"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:2JDF"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:2JDF"
SQ SEQUENCE 175 AA; 20908 MW; E0B605353FC62AFC CRC64;
MGKITFYEDR AFQGRSYECT TDCPNLQPYF SRCNSIRVES GCWMIYERPN YQGHQYFLRR
GEYPDYQQWM GLSDSIRSCC LIPPHSGAYR MKIYDRDELR GQMSELTDDC ISVQDRFHLT
EIHSLNVLEG SWILYEMPNY RGRQYLLRPG EYRRFLDWGA PNAKVGSLRR VMDLY
