ID CRYAB_HUMAN Reviewed; 175 AA. AC P02511; B0YIX0; O43416; Q9UC37; Q9UC38; Q9UC39; Q9UC40; Q9UC41; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 2. DT 22-FEB-2023, entry version 245. DE RecName: Full=Alpha-crystallin B chain; DE AltName: Full=Alpha(B)-crystallin; DE AltName: Full=Heat shock protein beta-5; DE Short=HspB5; DE AltName: Full=Renal carcinoma antigen NY-REN-27; DE AltName: Full=Rosenthal fiber component; GN Name=CRYAB {ECO:0000312|HGNC:HGNC:2389}; Synonyms=CRYA2, HSPB5; 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 PRELIMINARY PROTEIN SEQUENCE, TISSUE SPECIFICITY, AND ACETYLATION AT MET-1. RX PubMed=838078; DOI=10.1016/0014-5793(77)80757-6; RA Kramps J.A., de Man B.M., de Jong W.W.; RT "The primary structure of the B2 chain of human alpha-crystallin."; RL FEBS Lett. 74:82-84(1977). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. RX PubMed=2387586; DOI=10.1016/0888-7543(90)90204-8; RA Dubin R.A., Ally A.H., Chung S., Piatigorsky J.; RT "Human alpha B-crystallin gene and preferential promoter function in RT lens."; RL Genomics 7:594-601(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1407707; DOI=10.1016/0304-3940(92)90689-5; RA Iwaki A., Iwaki T., Goldman J.E., Ogomori K., Tateishi J., Sakaki Y.; RT "Accumulation of alpha B-crystallin in brains of patients with Alexander's RT disease is not due to an abnormality of the 5'-flanking and coding sequence RT of the genomic DNA."; RL Neurosci. Lett. 140:89-92(1992). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Yu W., Sarginson J., Gibbs R.A.; RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NHLBI resequencing and genotyping service (RS&G); RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Heart; 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 [10] RP PROTEIN SEQUENCE OF 2-24; 35-66 AND 118-175, AND ASSOCIATION WITH HSPB1. RC TISSUE=Pectoralis muscle; RX PubMed=1560006; DOI=10.1016/s0021-9258(18)42574-4; RA Kato K., Shinohara H., Goto S., Inaguma Y., Morishita R., Asano T.; RT "Copurification of small heat shock protein with alpha B crystallin from RT human skeletal muscle."; RL J. Biol. Chem. 267:7718-7725(1992). RN [11] RP PROTEIN SEQUENCE OF 57-66. RX PubMed=8999933; DOI=10.1074/jbc.272.4.2268; RA Lampi K.J., Ma Z., Shih M., Shearer T.R., Smith J.B., Smith D.L., RA David L.L.; RT "Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the RT identification of the major proteins in young human lens."; RL J. Biol. Chem. 272:2268-2275(1997). RN [12] RP PROTEIN SEQUENCE OF 83-89 AND 164-172. RC TISSUE=Heart; RX PubMed=7498159; DOI=10.1002/elps.11501601192; RA Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A., RA Ershova E.S., Egorov T.A., Musalyamov A.K.; RT "The major protein expression profile and two-dimensional protein database RT of human heart."; RL Electrophoresis 16:1160-1169(1995). RN [13] RP NUCLEOTIDE SEQUENCE [MRNA] OF 107-175. RX PubMed=2539261; DOI=10.1016/0092-8674(89)90173-6; RA Iwaki T., Kume-Iwaki A., Liem R.K.H., Goldman J.E.; RT "Alpha B-crystallin is expressed in non-lenticular tissues and accumulates RT in Alexander's disease brain."; RL Cell 57:71-78(1989). RN [14] RP RACEMIZATION/ISOMERIZATION OF SPECIFIC ASP, AND ACETYLATION AT MET-1. RX PubMed=8142454; DOI=10.1016/0167-4838(94)90003-5; RA Fujii N., Ishibashi Y., Satoh K., Fujino M., Harada K.; RT "Simultaneous racemization and isomerization at specific aspartic acid RT residues in alpha B-crystallin from the aged human lens."; RL Biochim. Biophys. Acta 1204:157-163(1994). RN [15] RP PHOSPHORYLATION AT SER-19; SER-45 AND SER-59, AND MASS SPECTROMETRY. RX PubMed=8175657; DOI=10.1016/s0021-9258(18)99902-3; RA Miesbauer L.R., Zhou X., Yang Z., Yang Z., Sun Y., Smith D.L., Smith J.B.; RT "Post-translational modifications of water-soluble human lens crystallins RT from young adults."; RL J. Biol. Chem. 269:12494-12502(1994). RN [16] RP IDENTIFICATION AS A RENAL CANCER ANTIGEN. RC TISSUE=Renal cell carcinoma; RX PubMed=10508479; RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5; RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., RA Old L.J.; RT "Antigens recognized by autologous antibody in patients with renal-cell RT carcinoma."; RL Int. J. Cancer 83:456-464(1999). RN [17] RP MASS SPECTROMETRY, SUSCEPTIBILITY TO OXIDATION, AND PHOSPHORYLATION. RX PubMed=10930324; DOI=10.1006/exer.2000.0868; RA Hanson S.R.A., Hasan A., Smith D.L., Smith J.B.; RT "The major in vivo modifications of the human water-insoluble lens RT crystallins are disulfide bonds, deamidation, methionine oxidation and RT backbone cleavage."; RL Exp. Eye Res. 71:195-207(2000). RN [18] RP INTERACTION WITH HSPBAP1. RX PubMed=10751411; DOI=10.1074/jbc.m001981200; RA Liu C., Gilmont R.R., Benndorf R., Welsh M.J.; RT "Identification and characterization of a novel protein from Sertoli cells, RT PASS1, that associates with mammalian small stress protein hsp27."; RL J. Biol. Chem. 275:18724-18731(2000). RN [19] RP INVOLVEMENT IN CTRCT16. RX PubMed=11577372; DOI=10.1086/324158; RA Berry V., Francis P., Reddy M.A., Collyer D., Vithana E., MacKay I., RA Dawson G., Carey A.H., Moore A., Bhattacharya S.S., Quinlan R.A.; RT "Alpha-B crystallin gene (CRYAB) mutation causes dominant congenital RT posterior polar cataract in humans."; RL Am. J. Hum. Genet. 69:1141-1145(2001). RN [20] RP PHOSPHORYLATION AT SER-45 AND SER-59. RX PubMed=11158243; DOI=10.1046/j.1471-4159.2001.00038.x; RA Kato K., Inaguma Y., Ito H., Iida K., Iwamoto I., Kamei K., Ochi N., RA Ohta H., Kishikawa M.; RT "Ser-59 is the major phosphorylation site in alphaB-crystallin accumulated RT in the brains of patients with Alexander's disease."; RL J. Neurochem. 76:730-736(2001). RN [21] RP ACETYLATION AT LYS-92. RX PubMed=11369851; DOI=10.1110/ps.40901; RA Lapko V.N., Smith D.L., Smith J.B.; RT "In vivo carbamylation and acetylation of water-soluble human lens alphaB- RT crystallin lysine 92."; RL Protein Sci. 10:1130-1136(2001). RN [22] RP INVOLVEMENT IN MFM2. RX PubMed=14681890; DOI=10.1002/ana.10767; RA Selcen D., Engel A.G.; RT "Myofibrillar myopathy caused by novel dominant negative alpha B-crystallin RT mutations."; RL Ann. Neurol. 54:804-810(2003). RN [23] RP INTERACTION WITH TTN. RX PubMed=14676215; DOI=10.1074/jbc.m307473200; RA Bullard B., Ferguson C., Minajeva A., Leake M.C., Gautel M., Labeit D., RA Ding L., Labeit S., Horwitz J., Leonard K.R., Linke W.A.; RT "Association of the chaperone alphaB-crystallin with titin in heart RT muscle."; RL J. Biol. Chem. 279:7917-7924(2004). RN [24] RP SUBCELLULAR LOCATION. RX PubMed=19464326; DOI=10.1016/j.bbamcr.2009.05.005; RA Vos M.J., Kanon B., Kampinga H.H.; RT "HSPB7 is a SC35 speckle resident small heat shock protein."; RL Biochim. Biophys. Acta 1793:1343-1353(2009). RN [25] RP SUBUNIT. RX PubMed=20836128; DOI=10.1002/iub.373; RA Srinivas P., Narahari A., Petrash J.M., Swamy M.J., Reddy G.B.; RT "Importance of eye lens alpha-crystallin heteropolymer with 3:1 alphaA to RT alphaB ratio: stability, aggregation, and modifications."; RL IUBMB Life 62:693-702(2010). RN [26] RP INVOLVEMENT IN MFMFIH-CRYAB. RX PubMed=21337604; DOI=10.1002/ana.22331; RA Del Bigio M.R., Chudley A.E., Sarnat H.B., Campbell C., Goobie S., RA Chodirker B.N., Selcen D.; RT "Infantile muscular dystrophy in Canadian aboriginals is an alphaB- RT crystallinopathy."; RL Ann. Neurol. 69:866-871(2011). RN [27] RP ACETYLATION AT LYS-92 AND LYS-166. RX PubMed=22120592; DOI=10.1016/j.bbadis.2011.11.011; RA Nagaraj R.H., Nahomi R.B., Shanthakumar S., Linetsky M., Padmanabha S., RA Pasupuleti N., Wang B., Santhoshkumar P., Panda A.K., Biswas A.; RT "Acetylation of alphaA-crystallin in the human lens: effects on structure RT and chaperone function."; RL Biochim. Biophys. Acta 1822:120-129(2012). RN [28] RP SUBUNIT, AND ZINC-BINDING SITES. RX PubMed=22890888; DOI=10.1007/s10930-012-9439-0; RA Karmakar S., Das K.P.; RT "Identification of histidine residues involved in Zn(2+) binding to RT alphaA- and alphaB-Crystallin by chemical modification and MALDI TOF mass RT spectrometry."; RL Protein J. 31:623-640(2012). RN [29] RP INTERACTION WITH TMEM109. RX PubMed=23542032; DOI=10.1016/j.febslet.2013.03.024; RA Yamashita A., Taniwaki T., Kaikoi Y., Yamazaki T.; RT "Protective role of the endoplasmic reticulum protein mitsugumin23 against RT ultraviolet C-induced cell death."; RL FEBS Lett. 587:1299-1303(2013). RN [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [31] RP INTERACTION WITH DES. RX PubMed=28470624; DOI=10.1007/s12192-017-0788-7; RA Sharma S., Conover G.M., Elliott J.L., Der Perng M., Herrmann H., RA Quinlan R.A.; RT "alphaB-crystallin is a sensor for assembly intermediates and for the RT subunit topology of desmin intermediate filaments."; RL Cell Stress Chaperones 22:613-626(2017). RN [32] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INVOLVEMENT IN RESTRICTIVE RP CARDIOMYOPATHY, VARIANT GLY-109, AND CHARACTERIZATION OF VARIANT GLY-109 RP AND GLY-120. RX PubMed=28493373; DOI=10.1002/humu.23248; RA Brodehl A., Gaertner-Rommel A., Klauke B., Grewe S.A., Schirmer I., RA Peterschroeder A., Faber L., Vorgerd M., Gummert J., Anselmetti D., RA Schulz U., Paluszkiewicz L., Milting H.; RT "The novel alphaB-crystallin (CRYAB) mutation p.D109G causes restrictive RT cardiomyopathy."; RL Hum. Mutat. 38:947-952(2017). RN [33] RP FUNCTION, AND INTERACTION WITH ATP6V1A AND MTOR. RX PubMed=31786107; DOI=10.1016/j.bbagen.2019.129496; RA Cui X., Feng R., Wang J., Du C., Pi X., Chen D., Li J., Li H., Zhang J., RA Zhang J., Mu H., Zhang F., Liu M., Hu Y.; RT "Heat shock factor 4 regulates lysosome activity by modulating the alphaB- RT crystallin-ATP6V1A-mTOR complex in ocular lens."; RL Biochim. Biophys. Acta 1864:129496-129496(2020). RN [34] RP SUBCELLULAR LOCATION, AND INTERACTION WITH TMED10. RX PubMed=32272059; DOI=10.1016/j.cell.2020.03.031; RA Zhang M., Liu L., Lin X., Wang Y., Li Y., Guo Q., Li S., Sun Y., Tao X., RA Zhang D., Lv X., Zheng L., Ge L.; RT "A Translocation Pathway for Vesicle-Mediated Unconventional Protein RT Secretion."; RL Cell 181:637-652(2020). RN [35] RP X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 67-157, AND HOMODIMERIZATION. RX PubMed=19646995; DOI=10.1016/j.jmb.2009.07.069; RA Bagneris C., Bateman O.A., Naylor C.E., Cronin N., Boelens W.C., Keep N.H., RA Slingsby C.; RT "Crystal structures of alpha-crystallin domain dimers of alphaB-crystallin RT and Hsp20."; RL J. Mol. Biol. 392:1242-1252(2009). RN [36] RP VARIANT MFM2 GLY-120. RX PubMed=9731540; DOI=10.1038/1765; RA Vicart P., Caron A., Guicheney P., Li Z., Prevost M.-C., Faure A., RA Chateau D., Chapon F., Tome F., Dupret J.-M., Paulin D., Fardeau M.; RT "A missense mutation in the alphaB-crystallin chaperone gene causes a RT desmin-related myopathy."; RL Nat. Genet. 20:92-95(1998). RN [37] RP CHARACTERIZATION OF VARIANTS MFM2 GLY-120. RX PubMed=12601044; DOI=10.1167/iovs.02-0950; RA Fu L., Liang J.J.-N.; RT "Alteration of protein-protein interactions of congenital cataract RT crystallin mutants."; RL Invest. Ophthalmol. Vis. Sci. 44:1155-1159(2003). RN [38] RP VARIANT CMD1II HIS-157. RX PubMed=16483541; DOI=10.1016/j.bbrc.2006.01.154; RA Inagaki N., Hayashi T., Arimura T., Koga Y., Takahashi M., Shibata H., RA Teraoka K., Chikamori T., Yamashina A., Kimura A.; RT "Alpha B-crystallin mutation in dilated cardiomyopathy."; RL Biochem. Biophys. Res. Commun. 342:379-386(2006). RN [39] RP VARIANT CMD1II SER-154. RX PubMed=16793013; DOI=10.1016/j.bbrc.2006.05.203; RA Pilotto A., Marziliano N., Pasotti M., Grasso M., Costante A.M., RA Arbustini E.; RT "alphaB-crystallin mutation in dilated cardiomyopathies: low prevalence in RT a consecutive series of 200 unrelated probands."; RL Biochem. Biophys. Res. Commun. 346:1115-1117(2006). RN [40] RP VARIANT CTRCT16 THR-171. RX PubMed=18587492; RA Devi R.R., Yao W., Vijayalakshmi P., Sergeev Y.V., Sundaresan P., RA Hejtmancik J.F.; RT "Crystallin gene mutations in Indian families with inherited pediatric RT cataract."; RL Mol. Vis. 14:1157-1170(2008). RN [41] RP VARIANT CTRCT16 CYS-69. RX PubMed=21866213; RA Sun W., Xiao X., Li S., Guo X., Zhang Q.; RT "Mutation analysis of 12 genes in Chinese families with congenital RT cataracts."; RL Mol. Vis. 17:2197-2206(2011). RN [42] RP VARIANT MFM2 HIS-109. RX PubMed=21920752; DOI=10.1016/j.nmd.2011.07.004; RA Sacconi S., Feasson L., Antoine J.C., Pecheux C., Bernard R., Cobo A.M., RA Casarin A., Salviati L., Desnuelle C., Urtizberea A.; RT "A novel CRYAB mutation resulting in multisystemic disease."; RL Neuromuscul. Disord. 22:66-72(2012). CC -!- FUNCTION: May contribute to the transparency and refractive index of CC the lens. Has chaperone-like activity, preventing aggregation of CC various proteins under a wide range of stress conditions. In lens CC epithelial cells, stabilizes the ATP6V1A protein, preventing its CC degradation by the proteasome (By similarity). CC {ECO:0000250|UniProtKB:P23927}. CC -!- SUBUNIT: Heteromer composed of three CRYAA and one CRYAB subunits CC (PubMed:20836128). Aggregates with homologous proteins, including the CC small heat shock protein HSPB1, to form large heteromeric complexes CC (PubMed:10751411). Inter-subunit bridging via zinc ions enhances CC stability, which is crucial as there is no protein turn over in the CC lens (PubMed:22890888). Interacts with HSPBAP1 and TTN/titin CC (PubMed:14676215). Interacts with TMEM109 (PubMed:23542032). Interacts CC with DES; binds rapidly during early stages of DES filament assembly CC and a reduced binding seen in the later stages (PubMed:28470624). CC Interacts with TMED10; the interaction mediates the translocation from CC the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate CC compartment) and thereby secretion (PubMed:32272059). Interacts with CC ATP6V1A and with MTOR, forming a ternary complex (PubMed:31786107). CC {ECO:0000269|PubMed:10751411, ECO:0000269|PubMed:14676215, CC ECO:0000269|PubMed:20836128, ECO:0000269|PubMed:22890888, CC ECO:0000269|PubMed:23542032, ECO:0000269|PubMed:28470624, CC ECO:0000269|PubMed:31786107, ECO:0000269|PubMed:32272059}. CC -!- INTERACTION: CC P02511; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-739060, EBI-10173507; CC P02511; P09525: ANXA4; NbExp=3; IntAct=EBI-739060, EBI-2556852; CC P02511; P05067: APP; NbExp=7; IntAct=EBI-739060, EBI-77613; CC P02511; Q6QEF8-4: CORO6; NbExp=3; IntAct=EBI-739060, EBI-10699285; CC P02511; Q14194: CRMP1; NbExp=3; IntAct=EBI-739060, EBI-473101; CC P02511; P02489: CRYAA; NbExp=18; IntAct=EBI-739060, EBI-6875961; CC P02511; P02511: CRYAB; NbExp=30; IntAct=EBI-739060, EBI-739060; CC P02511; P05813: CRYBA1; NbExp=2; IntAct=EBI-739060, EBI-7043337; CC P02511; P07315: CRYGC; NbExp=3; IntAct=EBI-739060, EBI-6875941; CC P02511; P22914: CRYGS; NbExp=2; IntAct=EBI-739060, EBI-11308647; CC P02511; P35222: CTNNB1; NbExp=6; IntAct=EBI-739060, EBI-491549; CC P02511; O00471: EXOC5; NbExp=3; IntAct=EBI-739060, EBI-949824; CC P02511; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-739060, EBI-739467; CC P02511; Q96LI6-3: HSFY2; NbExp=3; IntAct=EBI-739060, EBI-25830912; CC P02511; P04792: HSPB1; NbExp=6; IntAct=EBI-739060, EBI-352682; CC P02511; Q16082: HSPB2; NbExp=3; IntAct=EBI-739060, EBI-739395; CC P02511; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-739060, EBI-12111050; CC P02511; P60891: PRPS1; NbExp=3; IntAct=EBI-739060, EBI-749195; CC P02511; Q8WUY3: PRUNE2; NbExp=3; IntAct=EBI-739060, EBI-743880; CC P02511; Q3UBX0: Tmem109; Xeno; NbExp=2; IntAct=EBI-739060, EBI-2366300; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19464326, CC ECO:0000269|PubMed:28493373}. Nucleus {ECO:0000269|PubMed:19464326}. CC Secreted {ECO:0000269|PubMed:32272059}. Lysosome CC {ECO:0000250|UniProtKB:P23927}. Note=Translocates to the nucleus during CC heat shock and resides in sub-nuclear structures known as SC35 speckles CC or nuclear splicing speckles (PubMed:19464326). Localizes at the Z- CC bands and the intercalated disk in cardiomyocytes (PubMed:28493373). CC Can be secreted; the secretion is dependent on protein unfolding and CC facilitated by the cargo receptor TMED10; it results in protein CC translocation from the cytoplasm into the ERGIC (endoplasmic reticulum- CC Golgi intermediate compartment) followed by vesicle entry and secretion CC (PubMed:32272059). {ECO:0000269|PubMed:19464326, CC ECO:0000269|PubMed:28493373, ECO:0000269|PubMed:32272059}. CC -!- TISSUE SPECIFICITY: Lens as well as other tissues (PubMed:838078, CC PubMed:2387586). Expressed in myocardial tissue (PubMed:28493373). CC {ECO:0000269|PubMed:2387586, ECO:0000269|PubMed:28493373, CC ECO:0000269|PubMed:838078}. CC -!- MASS SPECTROMETRY: Mass=20201; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:10930324, ECO:0000269|PubMed:8175657}; CC -!- MASS SPECTROMETRY: Mass=20281; Method=Electrospray; Note=With 1 CC phosphate group.; Evidence={ECO:0000269|PubMed:10930324, CC ECO:0000269|PubMed:8175657}; CC -!- MASS SPECTROMETRY: Mass=20360; Method=Electrospray; Note=With 2 CC phosphate groups.; Evidence={ECO:0000269|PubMed:8175657}; CC -!- MASS SPECTROMETRY: Mass=20199; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:10930324, ECO:0000269|PubMed:8175657}; CC -!- MASS SPECTROMETRY: Mass=20278; Method=Electrospray; Note=With 1 CC phosphate group.; Evidence={ECO:0000269|PubMed:10930324, CC ECO:0000269|PubMed:8175657}; CC -!- DISEASE: Myopathy, myofibrillar, 2 (MFM2) [MIM:608810]: A form of CC myofibrillar myopathy, a group of chronic neuromuscular disorders CC characterized at ultrastructural level by disintegration of the CC sarcomeric Z disk and myofibrils, and replacement of the normal CC myofibrillar markings by small dense granules, or larger hyaline CC masses, or amorphous material. MFM2 is characterized by weakness of the CC proximal and distal limb muscles, weakness of the neck, velopharynx and CC trunk muscles, hypertrophic cardiomyopathy, and cataract in a subset of CC patients. {ECO:0000269|PubMed:12601044, ECO:0000269|PubMed:14681890, CC ECO:0000269|PubMed:21920752, ECO:0000269|PubMed:9731540}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Cataract 16, multiple types (CTRCT16) [MIM:613763]: 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. CTRCT16 CC includes posterior polar cataract, among others. Posterior polar CC cataract is a subcapsular opacity, usually disk-shaped, located at the CC back of the lens. {ECO:0000269|PubMed:11577372, CC ECO:0000269|PubMed:18587492, ECO:0000269|PubMed:21866213}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Note=CRYAB mutations may be involved in restrictive CC cardiomyopathy (RCM), a rare non-ischemic myocardial disease. RCM is CC characterized by restrictive ventricular-filling physiology in the CC presence of normal or reduced diastolic and/or systolic volumes (of 1 CC or both ventricles), biatrial enlargement, and normal ventricular wall CC thickness. {ECO:0000269|PubMed:28493373}. CC -!- DISEASE: Myopathy, myofibrillar, fatal infantile hypertonic, alpha-B CC crystallin-related (MFMFIH-CRYAB) [MIM:613869]: A form of myofibrillar CC myopathy, a group of chronic neuromuscular disorders characterized at CC ultrastructural level by disintegration of the sarcomeric Z disk and CC myofibrils, and replacement of the normal myofibrillar markings by CC small dense granules, or larger hyaline masses, or amorphous material. CC MFMFIH-CRYAB has onset in the first weeks of life after a normal CC neonatal period. Affected infants show rapidly progressive muscular CC rigidity of the trunk and limbs associated with increasing respiratory CC difficulty resulting in death before age 3 years. CC {ECO:0000269|PubMed:21337604}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Cardiomyopathy, dilated 1II (CMD1II) [MIM:615184]: A disorder CC characterized by ventricular dilation and impaired systolic function, CC resulting in congestive heart failure and arrhythmia. Patients are at CC risk of premature death. {ECO:0000269|PubMed:16483541, CC ECO:0000269|PubMed:16793013}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family. CC {ECO:0000255|PROSITE-ProRule:PRU00285}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/40156/CRYAB"; 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; M28638; AAA52104.1; -; Genomic_DNA. DR EMBL; S45630; AAB23453.1; -; mRNA. DR EMBL; AF007162; AAC19161.1; -; mRNA. DR EMBL; AK314029; BAG36739.1; -; mRNA. DR EMBL; BT006770; AAP35416.1; -; mRNA. DR EMBL; EF444955; ACA05949.1; -; Genomic_DNA. DR EMBL; CH471065; EAW67162.1; -; Genomic_DNA. DR EMBL; BC007008; AAH07008.1; -; mRNA. DR EMBL; M24906; AAA60267.1; -; mRNA. DR CCDS; CCDS8351.1; -. DR PIR; A35332; CYHUAB. DR RefSeq; NP_001276736.1; NM_001289807.1. DR RefSeq; NP_001276737.1; NM_001289808.1. DR RefSeq; NP_001876.1; NM_001885.2. DR RefSeq; XP_011540910.1; XM_011542608.1. DR PDB; 2KLR; NMR; -; A/B=1-175. DR PDB; 2N0K; NMR; -; A/B=64-152. DR PDB; 2WJ7; X-ray; 2.63 A; A/B/C/D/E=67-157. DR PDB; 2Y1Y; X-ray; 2.00 A; A=71-157. DR PDB; 2Y1Z; X-ray; 2.50 A; A/B=67-157. DR PDB; 2Y22; X-ray; 3.70 A; A/B/C/D/E/F=67-157. DR PDB; 2YGD; EM; 9.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-175. DR PDB; 3J07; Other; -; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-175. DR PDB; 3L1G; X-ray; 3.32 A; A=68-162. DR PDB; 3SGM; X-ray; 1.70 A; A/B/C/D=90-100. DR PDB; 3SGN; X-ray; 2.81 A; A/B=90-100. DR PDB; 3SGO; X-ray; 2.56 A; A=90-100. DR PDB; 3SGP; X-ray; 1.40 A; A/B/C/D=90-100. DR PDB; 3SGR; X-ray; 2.17 A; A/B/C/D/E/F=90-100. DR PDB; 3SGS; X-ray; 1.70 A; A=95-100. DR PDB; 4M5S; X-ray; 1.37 A; A=68-153, B=156-164. DR PDB; 4M5T; X-ray; 2.00 A; A/C/E/G=68-153, B/D/F/H=156-164. DR PDB; 5VVV; X-ray; 2.80 A; B/D=38-50. DR PDB; 6BP9; NMR; -; A/B=64-152. DR PDB; 7ROJ; X-ray; 1.60 A; A/B/C/D/E/F/G/H/I/J/K/L=90-100. DR PDBsum; 2KLR; -. DR PDBsum; 2N0K; -. DR PDBsum; 2WJ7; -. DR PDBsum; 2Y1Y; -. DR PDBsum; 2Y1Z; -. DR PDBsum; 2Y22; -. DR PDBsum; 2YGD; -. DR PDBsum; 3J07; -. DR PDBsum; 3L1G; -. DR PDBsum; 3SGM; -. DR PDBsum; 3SGN; -. DR PDBsum; 3SGO; -. DR PDBsum; 3SGP; -. DR PDBsum; 3SGR; -. DR PDBsum; 3SGS; -. DR PDBsum; 4M5S; -. DR PDBsum; 4M5T; -. DR PDBsum; 5VVV; -. DR PDBsum; 6BP9; -. DR PDBsum; 7ROJ; -. DR AlphaFoldDB; P02511; -. DR BMRB; P02511; -. DR SMR; P02511; -. DR BioGRID; 107800; 214. DR CORUM; P02511; -. DR DIP; DIP-35017N; -. DR IntAct; P02511; 62. DR MINT; P02511; -. DR STRING; 9606.ENSP00000433560; -. DR BindingDB; P02511; -. DR ChEMBL; CHEMBL3621022; -. DR MoonDB; P02511; Curated. DR TCDB; 8.A.172.1.1; the Alpha-crystallin chaperone (crya) family. DR GlyConnect; 33; 1 O-GlcNAc glycan. DR GlyCosmos; P02511; 2 sites, 1 glycan. DR GlyGen; P02511; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P02511; -. DR MetOSite; P02511; -. DR PhosphoSitePlus; P02511; -. DR BioMuta; CRYAB; -. DR DMDM; 117385; -. DR REPRODUCTION-2DPAGE; IPI00021369; -. DR SWISS-2DPAGE; P02511; -. DR UCD-2DPAGE; P02511; -. DR EPD; P02511; -. DR jPOST; P02511; -. DR MassIVE; P02511; -. DR PaxDb; P02511; -. DR PeptideAtlas; P02511; -. DR PRIDE; P02511; -. DR ProteomicsDB; 51527; -. DR Antibodypedia; 3674; 1729 antibodies from 48 providers. DR CPTC; P02511; 3 antibodies. DR DNASU; 1410; -. DR Ensembl; ENST00000227251.7; ENSP00000227251.3; ENSG00000109846.9. DR Ensembl; ENST00000526180.6; ENSP00000436051.1; ENSG00000109846.9. DR Ensembl; ENST00000527899.6; ENSP00000436089.2; ENSG00000109846.9. DR Ensembl; ENST00000527950.5; ENSP00000437149.1; ENSG00000109846.9. DR Ensembl; ENST00000531198.5; ENSP00000434247.1; ENSG00000109846.9. DR Ensembl; ENST00000533475.6; ENSP00000433560.1; ENSG00000109846.9. DR Ensembl; ENST00000533879.2; ENSP00000435931.2; ENSG00000109846.9. DR Ensembl; ENST00000616970.5; ENSP00000483554.1; ENSG00000109846.9. DR Ensembl; ENST00000650687.2; ENSP00000499082.1; ENSG00000109846.9. DR Ensembl; ENST00000651164.1; ENSP00000498735.1; ENSG00000109846.9. DR GeneID; 1410; -. DR KEGG; hsa:1410; -. DR MANE-Select; ENST00000650687.2; ENSP00000499082.1; NM_001289808.2; NP_001276737.1. DR AGR; HGNC:2389; -. DR CTD; 1410; -. DR DisGeNET; 1410; -. DR GeneCards; CRYAB; -. DR HGNC; HGNC:2389; CRYAB. DR HPA; ENSG00000109846; Tissue enhanced (brain, heart muscle, skeletal muscle, tongue). DR MalaCards; CRYAB; -. DR MIM; 123590; gene. DR MIM; 608810; phenotype. DR MIM; 613763; phenotype. DR MIM; 613869; phenotype. DR MIM; 615184; phenotype. DR neXtProt; NX_P02511; -. DR OpenTargets; ENSG00000109846; -. DR Orphanet; 399058; Alpha-B crystallin-related late-onset myopathy. DR Orphanet; 441452; Early-onset lamellar cataract. DR Orphanet; 98991; Early-onset nuclear cataract. DR Orphanet; 98993; Early-onset posterior polar cataract. DR Orphanet; 154; Familial isolated dilated cardiomyopathy. DR Orphanet; 280553; Fatal infantile hypertonic myofibrillar myopathy. DR PharmGKB; PA26907; -. DR VEuPathDB; HostDB:ENSG00000109846; -. DR eggNOG; KOG3591; Eukaryota. DR GeneTree; ENSGT00940000157434; -. DR InParanoid; P02511; -. DR OMA; RDEHGWI; -. DR OrthoDB; 3014506at2759; -. DR PhylomeDB; P02511; -. DR TreeFam; TF105049; -. DR PathwayCommons; P02511; -. DR Reactome; R-HSA-3371571; HSF1-dependent transactivation. DR SignaLink; P02511; -. DR SIGNOR; P02511; -. DR BioGRID-ORCS; 1410; 23 hits in 1155 CRISPR screens. DR ChiTaRS; CRYAB; human. DR EvolutionaryTrace; P02511; -. DR GeneWiki; CRYAB; -. DR GenomeRNAi; 1410; -. DR Pharos; P02511; Tchem. DR PRO; PR:P02511; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P02511; protein. DR Bgee; ENSG00000109846; Expressed in left ventricle myocardium and 204 other tissues. DR ExpressionAtlas; P02511; baseline and differential. DR Genevisible; P02511; HS. DR GO; GO:0032432; C:actin filament bundle; IEA:Ensembl. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0097512; C:cardiac myofibril; IEA:Ensembl. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0031430; C:M band; IEA:Ensembl. DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0043204; C:perikaryon; IEA:Ensembl. DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0097060; C:synaptic membrane; IEA:Ensembl. DR GO; GO:0030018; C:Z disc; IEA:Ensembl. DR GO; GO:0001540; F:amyloid-beta binding; IPI:ARUK-UCL. DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008017; F:microtubule binding; IEA:Ensembl. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; IPI:ARUK-UCL. DR GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IDA:UniProtKB. DR GO; GO:0051082; F:unfolded protein binding; IPI:UniProtKB. DR GO; GO:0060561; P:apoptotic process involved in morphogenesis; IEA:Ensembl. DR GO; GO:0071480; P:cellular response to gamma radiation; IMP:MGI. DR GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl. DR GO; GO:0031109; P:microtubule polymerization or depolymerization; IEA:Ensembl. DR GO; GO:0010259; P:multicellular organism aging; IEA:Ensembl. DR GO; GO:0006936; P:muscle contraction; TAS:ProtInc. DR GO; GO:0007517; P:muscle organ development; IEA:Ensembl. DR GO; GO:1905907; P:negative regulation of amyloid fibril formation; IDA:ARUK-UCL. DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:HGNC-UCL. DR GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl. DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl. DR GO; GO:0032387; P:negative regulation of intracellular transport; IDA:HGNC-UCL. DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IDA:ARUK-UCL. DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IEA:Ensembl. DR GO; GO:0006457; P:protein folding; NAS:ProtInc. DR GO; GO:0042026; P:protein refolding; IBA:GO_Central. DR GO; GO:0050821; P:protein stabilization; IMP:CAFA. DR GO; GO:0010941; P:regulation of cell death; IMP:MGI. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0009408; P:response to heat; IBA:GO_Central. DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0051403; P:stress-activated MAPK cascade; IEA:Ensembl. DR GO; GO:0007021; P:tubulin complex assembly; IEA:Ensembl. DR CDD; cd06498; ACD_alphaB-crystallin_HspB5; 1. DR DisProt; DP00445; -. DR Gene3D; 2.60.40.790; -; 1. DR InterPro; IPR002068; A-crystallin/Hsp20_dom. DR InterPro; IPR037882; ACD_alphaB-crystallin. DR InterPro; IPR001436; Alpha-crystallin/sHSP_animal. DR InterPro; IPR003090; Alpha-crystallin_N. DR InterPro; IPR008978; HSP20-like_chaperone. DR PANTHER; PTHR45640:SF5; ALPHA-CRYSTALLIN B CHAIN; 1. DR PANTHER; PTHR45640; HEAT SHOCK PROTEIN HSP-12.2-RELATED; 1. DR Pfam; PF00525; Crystallin; 1. DR Pfam; PF00011; HSP20; 1. DR PIRSF; PIRSF036514; Sm_HSP_B1; 1. DR PRINTS; PR00299; ACRYSTALLIN. DR SUPFAM; SSF49764; HSP20-like chaperones; 1. DR PROSITE; PS01031; SHSP; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cardiomyopathy; Cataract; Chaperone; Cytoplasm; KW Direct protein sequencing; Disease variant; Eye lens protein; Glycoprotein; KW Lysosome; Metal-binding; Myofibrillar myopathy; Nucleus; Oxidation; KW Phosphoprotein; Reference proteome; Secreted; Zinc. FT CHAIN 1..175 FT /note="Alpha-crystallin B chain" FT /id="PRO_0000125907" FT DOMAIN 56..164 FT /note="sHSP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285" FT REGION 146..175 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 159..175 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 83 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 104 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000305" FT BINDING 106 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 111 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 119 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000305" FT SITE 48 FT /note="Susceptible to oxidation" FT SITE 60 FT /note="Susceptible to oxidation" FT SITE 68 FT /note="Susceptible to oxidation" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|PubMed:8142454, FT ECO:0000269|PubMed:838078" FT MOD_RES 19 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:8175657" FT MOD_RES 45 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:11158243, FT ECO:0000269|PubMed:8175657" FT MOD_RES 59 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:11158243, FT ECO:0000269|PubMed:8175657, ECO:0007744|PubMed:24275569" FT MOD_RES 92 FT /note="N6-acetyllysine; partial" FT /evidence="ECO:0000269|PubMed:11369851, FT ECO:0000269|PubMed:22120592" FT MOD_RES 166 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:22120592" FT CARBOHYD 170 FT /note="O-linked (GlcNAc) threonine" FT /evidence="ECO:0000250" FT VARIANT 41 FT /note="S -> Y (in dbSNP:rs2234703)" FT /id="VAR_014607" FT VARIANT 51 FT /note="P -> L (in dbSNP:rs2234704)" FT /id="VAR_014608" FT VARIANT 69 FT /note="R -> C (in CTRCT16; unknown pathological FT significance; dbSNP:rs139750142)" FT /evidence="ECO:0000269|PubMed:21866213" FT /id="VAR_084806" FT VARIANT 109 FT /note="D -> G (probable disease-associated variant found in FT patients with restrictive cardiomyopathy; reduces CRYAB and FT DES localization at the Z-bands and the intercalated disk FT in the myocardium; cytoplasmic aggregations of CRYAB and FT DES; dbSNP:rs1114167341)" FT /evidence="ECO:0000269|PubMed:28493373" FT /id="VAR_079841" FT VARIANT 109 FT /note="D -> H (in MFM2; dbSNP:rs387907339)" FT /evidence="ECO:0000269|PubMed:21920752" FT /id="VAR_069528" FT VARIANT 120 FT /note="R -> G (in MFM2; decreased interactions with wild- FT type CRYAA and CRYAB but increased interactions with wild- FT type CRYBB2 and CRYGC; cytoplasmic aggregation; FT dbSNP:rs104894201)" FT /evidence="ECO:0000269|PubMed:12601044, FT ECO:0000269|PubMed:28493373, ECO:0000269|PubMed:9731540" FT /id="VAR_007899" FT VARIANT 154 FT /note="G -> S (in CMD1II; dbSNP:rs150516929)" FT /evidence="ECO:0000269|PubMed:16793013" FT /id="VAR_070035" FT VARIANT 157 FT /note="R -> H (in CMD1II; dbSNP:rs141638421)" FT /evidence="ECO:0000269|PubMed:16483541" FT /id="VAR_070036" FT VARIANT 171 FT /note="A -> T (in CTRCT16; unknown pathological FT significance; dbSNP:rs370803064)" FT /evidence="ECO:0000269|PubMed:18587492" FT /id="VAR_084807" FT CONFLICT 165 FT /note="E -> K (in Ref. 4; AAC19161)" FT /evidence="ECO:0000305" FT CONFLICT 175 FT /note="K -> KKMPFLELHFLKQESFPTSE (in Ref. 4; AAC19161)" FT /evidence="ECO:0000305" FT STRAND 68..70 FT /evidence="ECO:0007829|PDB:4M5S" FT STRAND 72..80 FT /evidence="ECO:0007829|PDB:4M5S" FT STRAND 82..84 FT /evidence="ECO:0007829|PDB:2N0K" FT HELIX 86..88 FT /evidence="ECO:0007829|PDB:4M5S" FT STRAND 89..94 FT /evidence="ECO:0007829|PDB:4M5S" FT STRAND 97..109 FT /evidence="ECO:0007829|PDB:4M5S" FT STRAND 112..123 FT /evidence="ECO:0007829|PDB:4M5S" FT TURN 125..127 FT /evidence="ECO:0007829|PDB:2KLR" FT HELIX 130..132 FT /evidence="ECO:0007829|PDB:4M5S" FT STRAND 134..137 FT /evidence="ECO:0007829|PDB:4M5S" FT STRAND 141..148 FT /evidence="ECO:0007829|PDB:4M5S" FT STRAND 157..159 FT /evidence="ECO:0007829|PDB:4M5T" FT STRAND 161..163 FT /evidence="ECO:0007829|PDB:4M5T" SQ SEQUENCE 175 AA; 20159 MW; AE08BED46B7849CB CRC64; MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR PPSFLRAPSW FDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR KYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVT AAPKK //