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 27-JUL-2011, entry version 142. 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; Synonyms=CRYA2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP PRELIMINARY PROTEIN SEQUENCE. RX MEDLINE=77116204; 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]. RX MEDLINE=90353958; 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 MEDLINE=93025869; 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 RT Alexander's disease is not due to an abnormality of the 5'-flanking RT and coding sequence 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 RT 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 RP HSPB1. RC TISSUE=Pectoralis muscle; RX MEDLINE=92218434; PubMed=1560006; RA Kato K., Shinohara H., Goto S., Inaguma Y., Morishita R., Asano T.; RT "Copurification of small heat shock protein with alpha B crystallin RT from human skeletal muscle."; RL J. Biol. Chem. 267:7718-7725(1992). RN [11] RP PROTEIN SEQUENCE OF 57-66. RX MEDLINE=97152999; 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 RT the 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 MEDLINE=96007936; 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 RT database of human heart."; RL Electrophoresis 16:1160-1169(1995). RN [13] RP NUCLEOTIDE SEQUENCE [MRNA] OF 107-175. RX MEDLINE=89195224; 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 RT accumulates in Alexander's disease brain."; RL Cell 57:71-78(1989). RN [14] RP RACEMIZATION/ISOMERIZATION OF SPECIFIC ASP. RX MEDLINE=94190996; 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; RA Miesbauer L.R., Zhou X., Yang Z., Yang Z., Sun Y., Smith D.L., RA Smith J.B.; RT "Post-translational modifications of water-soluble human lens RT crystallins 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 MEDLINE=99438124; 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- RT cell 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 MEDLINE=20317062; 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 RT cells, PASS1, that associates with mammalian small stress protein RT hsp27."; RL J. Biol. Chem. 275:18724-18731(2000). RN [19] RP INVOLVEMENT IN CTPP2. 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 MEDLINE=21103870; PubMed=11158243; RX 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 RT accumulated 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 RT alphaB-crystallin lysine 92."; RL Protein Sci. 10:1130-1136(2001). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-21; SER-43; RP SER-45; SER-53; SER-59 AND SER-76, METHYLATION AT ARG-22 AND ARG-50, RP ACETYLATION AT LYS-92, SUSCEPTIBILITY TO OXIDATION, AND MASS RP SPECTROMETRY. RC TISSUE=Lens; RX MEDLINE=22056091; PubMed=12060738; DOI=10.1073/pnas.122231399; RA MacCoss M.J., McDonald W.H., Saraf A., Sadygov R., Clark J.M., RA Tasto J.J., Gould K.L., Wolters D., Washburn M., Weiss A., Clark J.I., RA Yates J.R. III; RT "Shotgun identification of protein modifications from protein RT complexes and lens tissue."; RL Proc. Natl. Acad. Sci. U.S.A. 99:7900-7905(2002). RN [23] RP INVOLVEMENT IN MFM-CRYAB. RX PubMed=14681890; DOI=10.1002/ana.10767; RA Selcen D., Engel A.G.; RT "Myofibrillar myopathy caused by novel dominant negative alpha B- RT crystallin mutations."; RL Ann. Neurol. 54:804-810(2003). RN [24] RP INTERACTION WITH TTN. RX PubMed=14676215; DOI=10.1074/jbc.M307473200; RA Bullard B., Ferguson C., Minajeva A., Leake M.C., Gautel M., RA Labeit D., 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 [25] 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 [26] RP VARIANT MFM-CRYAB GLY-120. RX MEDLINE=98400266; 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 [27] RP CHARACTERIZATION OF VARIANTS MFM-CRYAB GLY-120. RX MEDLINE=22489080; 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 [28] RP X-RAY CRYSTALLOGRAPHY (2.63 ANGSTROMS) OF 67-157, AND RP 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., RA Keep N.H., Slingsby C.; RT "Crystal structures of alpha-crystallin domain dimers of alphaB- RT crystallin and Hsp20."; RL J. Mol. Biol. 392:1242-1252(2009). CC -!- FUNCTION: May contribute to the transparency and refractive index CC of the lens. CC -!- SUBUNIT: Homodimer. Aggregates with homologous proteins, including CC CRYAA and the small heat shock protein HSPB1, to form large CC heteromeric complexes. Interacts with HSPBAP1 and TTN/titin. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocates to the CC nucleus during heat shock and resides in sub-nuclear structures CC known as SC35 speckles or nuclear splicing speckles. CC -!- TISSUE SPECIFICITY: Lens as well as other tissues. CC -!- MASS SPECTROMETRY: Mass=20201; Method=Electrospray; Range=1-175; CC Source=PubMed:8175657; CC -!- MASS SPECTROMETRY: Mass=20281; Method=Electrospray; Range=1-175; CC Note=With 1 phosphate group; Source=PubMed:8175657; CC -!- MASS SPECTROMETRY: Mass=20360; Method=Electrospray; Range=1-175; CC Note=With 2 phosphate groups; Source=PubMed:8175657; CC -!- MASS SPECTROMETRY: Mass=20199; Method=Electrospray; Range=1-175; CC Source=PubMed:10930324; CC -!- MASS SPECTROMETRY: Mass=20278; Method=Electrospray; Range=1-175; CC Note=With 1 phosphate group; Source=PubMed:10930324; CC -!- DISEASE: Defects in CRYAB are the cause of myofibrillar alpha-B CC crystallin-related (MFM-CRYAB) [MIM:608810]. A neuromuscular CC disorder that results in weakness of the proximal and distal limb CC muscles, weakness of the neck, velopharynx and trunk muscles, CC hypetrophic cardiomyopathy, and cataract in a subset of patients. CC -!- DISEASE: Defects in CRYAB are the cause of cataract posterior CC polar type 2 (CTPP2) [MIM:613763]. A subcapsular opacity, usually CC disk-shaped, located at the back of the lens. It can have a marked CC effect on visual acuity. CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) CC family. CC -!- WEB RESOURCE: Name=GeneReviews; CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/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 IPI; IPI00021369; -. DR PIR; A35332; CYHUAB. DR RefSeq; NP_001876.1; NM_001885.1. DR UniGene; Hs.53454; -. DR PDB; 2KLR; NMR; -; A/B=1-175. 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; 3L1G; X-ray; 3.32 A; A=68-162. DR PDBsum; 2KLR; -. DR PDBsum; 2WJ7; -. DR PDBsum; 2Y1Y; -. DR PDBsum; 2Y1Z; -. DR PDBsum; 2Y22; -. DR PDBsum; 3L1G; -. DR ProteinModelPortal; P02511; -. DR SMR; P02511; 68-162. DR DisProt; DP00445; -. DR DIP; DIP-35017N; -. DR IntAct; P02511; 9. DR MINT; MINT-221013; -. DR STRING; P02511; -. DR GlycoSuiteDB; P02511; -. DR PhosphoSite; P02511; -. DR SWISS-2DPAGE; P02511; -. DR REPRODUCTION-2DPAGE; IPI00021369; -. DR UCD-2DPAGE; P02511; -. DR PRIDE; P02511; -. DR Ensembl; ENST00000227251; ENSP00000227251; ENSG00000109846. DR GeneID; 1410; -. DR KEGG; hsa:1410; -. DR UCSC; uc001pmf.1; human. DR CTD; 1410; -. DR GeneCards; GC11M107703; -. DR HGNC; HGNC:2389; CRYAB. DR HPA; CAB002053; -. DR HPA; CAB040560; -. DR HPA; HPA028724; -. DR MIM; 123590; gene. DR MIM; 608810; phenotype. DR MIM; 613763; phenotype. DR neXtProt; NX_P02511; -. DR Orphanet; 98910; Alpha-crystallinopathy. DR Orphanet; 98993; Posterior polar cataract. DR Orphanet; 98995; Zonular cataract. DR PharmGKB; PA26907; -. DR eggNOG; prNOG15526; -. DR GeneTree; ENSGT00550000074302; -. DR HOVERGEN; HBG054766; -. DR InParanoid; P02511; -. DR OMA; PGPERTI; -. DR OrthoDB; EOG4G1MHK; -. DR PhylomeDB; P02511; -. DR NextBio; 5765; -. DR PMAP-CutDB; P02511; -. DR ArrayExpress; P02511; -. DR Bgee; P02511; -. DR CleanEx; HS_CRYAB; -. DR Genevestigator; P02511; -. DR GermOnline; ENSG00000109846; Homo sapiens. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW. DR GO; GO:0051082; F:unfolded protein binding; IPI:UniProtKB. DR GO; GO:0006916; P:anti-apoptosis; IDA:HGNC. DR GO; GO:0006936; P:muscle contraction; TAS:ProtInc. DR GO; GO:0032387; P:negative regulation of intracellular transport; IDA:HGNC. DR GO; GO:0006457; P:protein folding; NAS:ProtInc. DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB. DR GO; GO:0009408; P:response to heat; IEA:InterPro. DR InterPro; IPR001436; Alpha-crystallin/HSP. DR InterPro; IPR012273; Alpha-crystallin_B. DR InterPro; IPR003090; Alpha-crystallin_N. DR InterPro; IPR002068; Hsp20. DR InterPro; IPR008978; HSP20-like_chaperone. DR PANTHER; PTHR11527:SF37; A-crystallin_B; 1. DR Pfam; PF00525; Crystallin; 1. DR Pfam; PF00011; HSP20; 1. DR PRINTS; PR00299; ACRYSTALLIN. DR SUPFAM; SSF49764; HSP20_chap; 1. DR PROSITE; PS01031; HSP20; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cataract; Complete proteome; Cytoplasm; KW Direct protein sequencing; Disease mutation; Eye lens protein; KW Glycoprotein; Methylation; Myofibrillar myopathy; Nucleus; Oxidation; KW Phosphoprotein; Polymorphism. FT CHAIN 1 175 Alpha-crystallin B chain. FT /FTId=PRO_0000125907. FT SITE 48 48 Susceptible to oxidation. FT SITE 60 60 Susceptible to oxidation. FT SITE 68 68 Susceptible to oxidation. FT MOD_RES 1 1 N-acetylmethionine (Probable). FT MOD_RES 19 19 Phosphoserine. FT MOD_RES 21 21 Phosphoserine. FT MOD_RES 22 22 Omega-N-methylated arginine. FT MOD_RES 43 43 Phosphoserine. FT MOD_RES 45 45 Phosphoserine. FT MOD_RES 50 50 Omega-N-methylated arginine. FT MOD_RES 53 53 Phosphoserine. FT MOD_RES 59 59 Phosphoserine. FT MOD_RES 76 76 Phosphoserine. FT MOD_RES 92 92 N6-acetyllysine; partial. FT CARBOHYD 170 170 O-linked (GlcNAc) (By similarity). FT VARIANT 41 41 S -> Y (in dbSNP:rs2234703). FT /FTId=VAR_014607. FT VARIANT 51 51 P -> L (in dbSNP:rs2234704). FT /FTId=VAR_014608. FT VARIANT 120 120 R -> G (in MFM-CRYAB; decreased FT interactions with wild-type CRYAA and FT CRYAB but increased interactions with FT wild-type CRYBB2 and CRYGC; FT dbSNP:rs28929489). FT /FTId=VAR_007899. FT CONFLICT 165 165 E -> K (in Ref. 4; AAC19161). FT CONFLICT 175 175 K -> KKMPFLELHFLKQESFPTSE (in Ref. 4; FT AAC19161). FT STRAND 68 70 FT STRAND 75 79 FT HELIX 86 88 FT STRAND 90 93 FT STRAND 97 101 FT STRAND 114 123 FT HELIX 130 132 FT STRAND 134 137 FT STRAND 143 146 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 //