HSPB6_HUMAN
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 03-AUG-2022, entry version 174.
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}.
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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; 15.
DR IntAct; O14558; 11.
DR MINT; O14558; -.
DR STRING; 9606.ENSP00000468057; -.
DR iPTMnet; O14558; -.
DR PhosphoSitePlus; O14558; -.
DR BioMuta; HSPB6; -.
DR REPRODUCTION-2DPAGE; O14558; -.
DR UCD-2DPAGE; O14558; -.
DR jPOST; O14558; -.
DR MassIVE; O14558; -.
DR PaxDb; O14558; -.
DR PeptideAtlas; O14558; -.
DR PRIDE; O14558; -.
DR ProteomicsDB; 48083; -.
DR Antibodypedia; 4537; 378 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 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; 1187096at2759; -.
DR PhylomeDB; O14558; -.
DR PathwayCommons; O14558; -.
DR SignaLink; O14558; -.
DR SIGNOR; O14558; -.
DR BioGRID-ORCS; 126393; 10 hits in 1071 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 149 other tissues.
DR ExpressionAtlas; O14558; baseline and differential.
DR Genevisible; O14558; HS.
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:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS: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 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; PTHR45640; 1.
DR Pfam; PF00525; Crystallin; 1.
DR Pfam; PF00011; HSP20; 1.
DR PRINTS; PR00299; ACRYSTALLIN.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
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
