ID HSPB6_HUMAN Reviewed; 160 AA. AC O14558; O14551; Q6NVI3; Q96MG9; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2002, sequence version 2. DT 24-JAN-2024, entry version 182. DE RecName: Full=Heat shock protein beta-6; DE Short=HspB6; DE AltName: Full=Heat shock 20 kDa-like protein p20; GN Name=HSPB6; 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 [LARGE SCALE MRNA]. RC TISSUE=Skeletal muscle; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-20. RC TISSUE=Skin; 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 [4] RP PROTEIN SEQUENCE OF 2-160, AND CHARACTERIZATION. RC TISSUE=Muscle; RX PubMed=8195168; DOI=10.1016/s0021-9258(17)36606-1; RA Kato K., Goto S., Inaguma Y., Hasegawa K., Morishita R., Asano T.; RT "Purification and characterization of a 20-kDa protein that is highly RT homologous to alpha B crystallin."; RL J. Biol. Chem. 269:15302-15309(1994). RN [5] RP FUNCTION, AND INTERACTION WITH BAG3. RX PubMed=19845507; DOI=10.1042/bj20090907; RA Fuchs M., Poirier D.J., Seguin S.J., Lambert H., Carra S., Charette S.J., RA Landry J.; RT "Identification of the key structural motifs involved in HspB8/HspB6-Bag3 RT interaction."; RL Biochem. J. 425:245-255(2009). RN [6] RP FUNCTION. RX PubMed=14717697; DOI=10.1046/j.1432-1033.2003.03928.x; RA Bukach O.V., Seit-Nebi A.S., Marston S.B., Gusev N.B.; RT "Some properties of human small heat shock protein Hsp20 (HspB6)."; RL Eur. J. Biochem. 271:291-302(2004). RN [7] 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 [8] RP REVIEW ON FUNCTION IN MUSCLE. RX PubMed=19568960; DOI=10.1007/s12192-009-0127-8; RA Dreiza C.M., Komalavilas P., Furnish E.J., Flynn C.R., Sheller M.R., RA Smoke C.C., Lopes L.B., Brophy C.M.; RT "The small heat shock protein, HSPB6, in muscle function and disease."; RL Cell Stress Chaperones 15:1-11(2010). RN [9] RP REVIEW ON FUNCTION IN MUSCLE. RX PubMed=19777375; DOI=10.1007/s12192-009-0141-x; RA Seit-Nebi A.S., Gusev N.B.; RT "Versatility of the small heat shock protein HSPB6 (Hsp20)."; RL Cell Stress Chaperones 15:233-236(2010). RN [10] RP FUNCTION. RX PubMed=20843828; DOI=10.1093/hmg/ddq398; RA Vos M.J., Zijlstra M.P., Kanon B., van Waarde-Verhagen M.A., Brunt E.R., RA Oosterveld-Hut H.M., Carra S., Sibon O.C., Kampinga H.H.; RT "HSPB7 is the most potent polyQ aggregation suppressor within the HSPB RT family of molecular chaperones."; RL Hum. Mol. Genet. 19:4677-4693(2010). RN [11] RP INTERACTION WITH HSPB1. RX PubMed=21641913; DOI=10.1016/j.jmb.2011.05.024; RA Baranova E.V., Weeks S.D., Beelen S., Bukach O.V., Gusev N.B., RA Strelkov S.V.; RT "Three-dimensional structure of alpha-crystallin domain dimers of human RT small heat shock proteins HSPB1 and HSPB6."; RL J. Mol. Biol. 411:110-122(2011). RN [12] RP PHOSPHORYLATION AT SER-16, AND INTERACTION WITH PDE4A AND PDE4D. RX PubMed=21334344; DOI=10.1016/j.yjmcc.2011.02.006; RA Sin Y.Y., Edwards H.V., Li X., Day J.P., Christian F., Dunlop A.J., RA Adams D.R., Zaccolo M., Houslay M.D., Baillie G.S.; RT "Disruption of the cyclic AMP phosphodiesterase-4 (PDE4)-HSP20 complex RT attenuates the beta-agonist induced hypertrophic response in cardiac RT myocytes."; RL J. Mol. Cell. Cardiol. 50:872-883(2011). RN [13] RP INTERACTION WITH YWHAZ, AND FUNCTION. RX PubMed=22794279; DOI=10.1021/bi300674e; RA Sluchanko N.N., Artemova N.V., Sudnitsyna M.V., Safenkova I.V., RA Antson A.A., Levitsky D.I., Gusev N.B.; RT "Monomeric 14-3-3zeta has a chaperone-like activity and is stabilized by RT phosphorylated HspB6."; RL Biochemistry 51:6127-6138(2012). RN [14] RP SUBUNIT. RX PubMed=22002549; DOI=10.1007/s12192-011-0296-0; RA Mymrikov E.V., Seit-Nebi A.S., Gusev N.B.; RT "Heterooligomeric complexes of human small heat shock proteins."; RL Cell Stress Chaperones 17:157-169(2012). RN [15] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KDR. RX PubMed=22427880; DOI=10.1371/journal.pone.0032765; RA Zhang X., Wang X., Zhu H., Kranias E.G., Tang Y., Peng T., Chang J., RA Fan G.C.; RT "Hsp20 functions as a novel cardiokine in promoting angiogenesis via RT activation of VEGFR2."; RL PLoS ONE 7:E32765-E32765(2012). RN [16] RP INTERACTION WITH HSPB1. RX PubMed=23948568; DOI=10.1016/j.abb.2013.07.028; RA Nefedova V.V., Sudnitsyna M.V., Strelkov S.V., Gusev N.B.; RT "Structure and properties of G84R and L99M mutants of human small heat RT shock protein HspB1 correlating with motor neuropathy."; RL Arch. Biochem. Biophys. 538:16-24(2013). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, 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 [18] RP INTERACTION WITH CRYAB, AND MUTAGENESIS OF SER-134. RX PubMed=26098708; DOI=10.1021/acs.biochem.5b00490; RA Delbecq S.P., Rosenbaum J.C., Klevit R.E.; RT "A mechanism of subunit recruitment in human small heat shock protein RT oligomers."; RL Biochemistry 54:4276-4284(2015). RN [19] RP INTERACTION WITH PRKD1. RX PubMed=26443497; DOI=10.1002/cbf.3147; RA Sin Y.Y., Baillie G.S.; RT "Heat shock protein 20 (HSP20) is a novel substrate for protein kinase D1 RT (PKD1)."; RL Cell Biochem. Funct. 33:421-426(2015). RN [20] RP SUBUNIT. RX PubMed=27717639; DOI=10.1016/j.abb.2016.10.002; RA Heirbaut M., Lermyte F., Martin E.M., Beelen S., Verschueren T., Sobott F., RA Strelkov S.V., Weeks S.D.; RT "The preferential heterodimerization of human small heat shock proteins RT HSPB1 and HSPB6 is dictated by the N-terminal domain."; RL Arch. Biochem. Biophys. 610:41-50(2016). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 57-160, SUBUNIT, AND MUTAGENESIS RP OF ILE-3 AND VAL-5. RX PubMed=24382496; DOI=10.1016/j.jsb.2013.12.009; RA Weeks S.D., Baranova E.V., Heirbaut M., Beelen S., Shkumatov A.V., RA Gusev N.B., Strelkov S.V.; RT "Molecular structure and dynamics of the dimeric human small heat shock RT protein HSPB6."; RL J. Struct. Biol. 185:342-354(2014). RN [22] RP VARIANT LEU-20, AND CHARACTERIZATION OF VARIANT LEU-20. RX PubMed=18790732; DOI=10.1074/jbc.m802307200; RA Nicolaou P., Knoell R., Haghighi K., Fan G.C., Dorn G.W. II, Hasenfub G., RA Kranias E.G.; RT "Human mutation in the anti-apoptotic heat shock protein 20 abrogates its RT cardioprotective effects."; RL J. Biol. Chem. 283:33465-33471(2008). CC -!- FUNCTION: Small heat shock protein which functions as a molecular CC chaperone probably maintaining denatured proteins in a folding- CC competent state. Seems to have versatile functions in various CC biological processes. Plays a role in regulating muscle function such CC as smooth muscle vasorelaxation and cardiac myocyte contractility. May CC regulate myocardial angiogenesis implicating KDR. Overexpression CC mediates cardioprotection and angiogenesis after induced damage. CC Stabilizes monomeric YWHAZ thereby supporting YWHAZ chaperone-like CC activity. {ECO:0000269|PubMed:14717697, ECO:0000269|PubMed:19845507, CC ECO:0000269|PubMed:20843828, ECO:0000269|PubMed:22427880, ECO:0000305, CC ECO:0000305|PubMed:22794279}. CC -!- SUBUNIT: Homodimer. Small heat shock proteins form high molecular mass CC oligomers containing variable number of monomers; these oligomers CC display a very flexible quaternary structure easily exchanging their CC subunits. Heterooligomer with HSPB1; formed through oligomerization of CC HSPB1:HSBP6 dimers; subunit exchange leads to formation of at least two CC different heterooligomeric complexes, differing in variable quantities CC of HSPB1 and HSPB6 homodimers in addition to HSPB1:HSPB6 heterodimers. CC Heterooligomer with CRYAB; large heterooligomers consist of CRYAB CC homodimers and HSPB5:HSPB6 heterodimers but lacking HSPB6 homodimers. CC Interacts with BAG3. Interacts (phosphorylated) with YWHAZ. Interacts CC with PDE4A and PDE4D; required for maintenance of the non- CC phosphorylated state of HSPB6 under basal conditions. Interacts with CC KDR. Interacts with PRKD1. {ECO:0000269|PubMed:19845507, CC ECO:0000269|PubMed:21334344, ECO:0000269|PubMed:21641913, CC ECO:0000269|PubMed:22002549, ECO:0000269|PubMed:22427880, CC ECO:0000269|PubMed:22794279, ECO:0000269|PubMed:23948568, CC ECO:0000269|PubMed:24382496, ECO:0000269|PubMed:26443497, CC ECO:0000269|PubMed:27717639}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19464326}. Nucleus CC {ECO:0000269|PubMed:19464326}. Secreted {ECO:0000269|PubMed:22427880}. CC Note=Translocates to nuclear foci during heat shock. CC {ECO:0000269|PubMed:19464326}. CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:8195168}. CC -!- PTM: Phosphorylated at Ser-16 by PKA and probably PKD1K; required to CC protect cardiomyocytes from apoptosis. {ECO:0000250|UniProtKB:P97541, CC ECO:0000250|UniProtKB:Q5EBG6, ECO:0000305|PubMed:26443497}. CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family. CC {ECO:0000255|PROSITE-ProRule:PRU00285}. 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; AK056951; BAB71323.1; -; mRNA. DR EMBL; AC002398; AAB81196.1; -; Genomic_DNA. DR EMBL; BC068046; AAH68046.1; -; mRNA. DR CCDS; CCDS12475.1; -. DR PIR; B53814; B53814. DR PIR; T00703; T00703. DR RefSeq; NP_653218.1; NM_144617.2. DR PDB; 4JUS; X-ray; 2.50 A; A/B/C/D/E/F/G/H=57-160. DR PDB; 4JUT; X-ray; 2.20 A; A/B/C/D/E/F/G/H=57-160. DR PDB; 5LTW; X-ray; 4.50 A; C/D/G/H/K/L=1-149. DR PDB; 5LU1; X-ray; 2.40 A; C/D/G/H=13-20. DR PDB; 5LU2; X-ray; 2.50 A; C/D=11-23. DR PDB; 5LUM; X-ray; 2.60 A; A/B/C/D/E=72-149, F/G/H/I/J=2-10. DR PDB; 5OK9; X-ray; 2.35 A; A/B/E/F=12-19. DR PDB; 5OKF; X-ray; 3.20 A; A/B/C/D=12-19. DR PDBsum; 4JUS; -. DR PDBsum; 4JUT; -. DR PDBsum; 5LTW; -. DR PDBsum; 5LU1; -. DR PDBsum; 5LU2; -. DR PDBsum; 5LUM; -. DR PDBsum; 5OK9; -. DR PDBsum; 5OKF; -. DR AlphaFoldDB; O14558; -. DR SMR; O14558; -. DR BioGRID; 125988; 16. DR IntAct; O14558; 11. DR MINT; O14558; -. DR STRING; 9606.ENSP00000004982; -. DR iPTMnet; O14558; -. DR PhosphoSitePlus; O14558; -. DR BioMuta; HSPB6; -. DR REPRODUCTION-2DPAGE; O14558; -. DR jPOST; O14558; -. DR MassIVE; O14558; -. DR PaxDb; 9606-ENSP00000468057; -. DR PeptideAtlas; O14558; -. DR ProteomicsDB; 48083; -. DR Antibodypedia; 4537; 418 antibodies from 37 providers. DR DNASU; 126393; -. DR Ensembl; ENST00000004982.6; ENSP00000004982.3; ENSG00000004776.13. DR GeneID; 126393; -. DR KEGG; hsa:126393; -. DR MANE-Select; ENST00000004982.6; ENSP00000004982.3; NM_144617.3; NP_653218.1. DR AGR; HGNC:26511; -. DR CTD; 126393; -. DR DisGeNET; 126393; -. DR GeneCards; HSPB6; -. DR HGNC; HGNC:26511; HSPB6. DR HPA; ENSG00000004776; Tissue enhanced (skeletal muscle, tongue). DR MIM; 610695; gene. DR neXtProt; NX_O14558; -. DR OpenTargets; ENSG00000004776; -. DR PharmGKB; PA134983584; -. DR VEuPathDB; HostDB:ENSG00000004776; -. DR eggNOG; KOG3591; Eukaryota. DR GeneTree; ENSGT00940000161100; -. DR HOGENOM; CLU_095001_2_0_1; -. DR InParanoid; O14558; -. DR OMA; PVQPTWL; -. DR OrthoDB; 3014506at2759; -. DR PhylomeDB; O14558; -. DR PathwayCommons; O14558; -. DR SignaLink; O14558; -. DR SIGNOR; O14558; -. DR BioGRID-ORCS; 126393; 12 hits in 1148 CRISPR screens. DR ChiTaRS; HSPB6; human. DR GeneWiki; HSPB6; -. DR GenomeRNAi; 126393; -. DR Pharos; O14558; Tbio. DR PRO; PR:O14558; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; O14558; Protein. DR Bgee; ENSG00000004776; Expressed in hindlimb stylopod muscle and 151 other cell types or tissues. DR ExpressionAtlas; O14558; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0044183; F:protein folding chaperone; IDA:DisProt. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0051087; F:protein-folding chaperone binding; IPI:UniProtKB. DR GO; GO:0005212; F:structural constituent of eye lens; IEA:InterPro. DR GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB. DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central. DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB. DR GO; GO:0042026; P:protein refolding; IBA:GO_Central. DR GO; GO:0009408; P:response to heat; IBA:GO_Central. DR CDD; cd06478; ACD_HspB4-5-6; 1. DR DisProt; DP01131; -. DR Gene3D; 2.60.40.790; -; 1. DR InterPro; IPR002068; A-crystallin/Hsp20_dom. DR InterPro; IPR001436; Alpha-crystallin/sHSP_animal. DR InterPro; IPR003090; Alpha-crystallin_N. DR InterPro; IPR008978; HSP20-like_chaperone. DR PANTHER; PTHR45640:SF2; HEAT SHOCK PROTEIN BETA-6; 1. DR PANTHER; PTHR45640; HEAT SHOCK PROTEIN HSP-12.2-RELATED; 1. DR Pfam; PF00525; Crystallin; 1. DR Pfam; PF00011; HSP20; 1. DR PRINTS; PR00299; ACRYSTALLIN. DR SUPFAM; SSF49764; HSP20-like chaperones; 1. DR PROSITE; PS01031; SHSP; 1. DR UCD-2DPAGE; O14558; -. DR Genevisible; O14558; HS. PE 1: Evidence at protein level; KW 3D-structure; Chaperone; Cytoplasm; Direct protein sequencing; Nucleus; KW Phosphoprotein; Reference proteome; Secreted; Stress response. FT CHAIN 1..160 FT /note="Heat shock protein beta-6" FT /id="PRO_0000125939" FT DOMAIN 55..160 FT /note="sHSP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285" FT REGION 1..72 FT /note="Involved in stabilization of the HSPB1:HSBP6 FT heterodimer" FT /evidence="ECO:0000269|PubMed:27717639" FT MOD_RES 16 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000269|PubMed:21334344, FT ECO:0007744|PubMed:24275569" FT MOD_RES 66 FT /note="Deamidated glutamine" FT /evidence="ECO:0000250|UniProtKB:P97541" FT VARIANT 20 FT /note="P -> L (decreases phosphorylation at Ser-16; FT abolishes cardioprotective effects; dbSNP:rs11549029)" FT /evidence="ECO:0000269|PubMed:18790732" FT /id="VAR_077818" FT MUTAGEN 3 FT /note="I->G: Increases homodimer-based self-association FT properties; increases chaperone activity; when associated FT with G-5." FT /evidence="ECO:0000269|PubMed:24382496" FT MUTAGEN 5 FT /note="V->G: Increases homodimer-based self-association FT properties; increases chaperone activity; when associated FT with G-3." FT /evidence="ECO:0000269|PubMed:24382496" FT MUTAGEN 67 FT /note="V->G: No effect on homodimer-based self-association FT properties; no effect on chaperone activity." FT /evidence="ECO:0000269|PubMed:24382496" FT MUTAGEN 134 FT /note="S->Q: Decreases heteromer formation with CRYAB." FT CONFLICT 64..66 FT /note="Missing (in Ref. 2; AAB81196)" FT /evidence="ECO:0000305" FT STRAND 3..5 FT /evidence="ECO:0007829|PDB:5LUM" FT STRAND 7..9 FT /evidence="ECO:0007829|PDB:5LUM" FT STRAND 69..71 FT /evidence="ECO:0007829|PDB:4JUS" FT STRAND 74..79 FT /evidence="ECO:0007829|PDB:4JUT" FT HELIX 85..87 FT /evidence="ECO:0007829|PDB:4JUT" FT STRAND 88..93 FT /evidence="ECO:0007829|PDB:4JUT" FT STRAND 96..107 FT /evidence="ECO:0007829|PDB:4JUT" FT STRAND 109..122 FT /evidence="ECO:0007829|PDB:4JUT" FT HELIX 129..131 FT /evidence="ECO:0007829|PDB:4JUT" FT STRAND 133..136 FT /evidence="ECO:0007829|PDB:4JUT" FT STRAND 140..146 FT /evidence="ECO:0007829|PDB:4JUT" SQ SEQUENCE 160 AA; 17136 MW; 3BFB1FFB5877F2E7 CRC64; MEIPVPVQPS WLRRASAPLP GLSAPGRLFD QRFGEGLLEA ELAALCPTTL APYYLRAPSV ALPVAQVPTD PGHFSVLLDV KHFSPEEIAV KVVGEHVEVH ARHEERPDEH GFVAREFHRR YRLPPGVDPA AVTSALSPEG VLSIQAAPAS AQAPPPAAAK //