HSPB6_MOUSE
ID HSPB6_MOUSE Reviewed; 162 AA.
AC Q5EBG6;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Heat shock protein beta-6;
DE Short=HspB6;
GN Name=Hspb6; Synonyms=Gm479;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP PHOSPHORYLATION AT SER-16.
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).
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:0000250|UniProtKB:O14558}.
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:0000250|UniProtKB:O14558,
CC ECO:0000250|UniProtKB:P97541}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14558}. Nucleus
CC {ECO:0000250|UniProtKB:O14558}. Secreted
CC {ECO:0000250|UniProtKB:O14558}. Note=Translocates to nuclear foci
CC during heat shock. {ECO:0000250|UniProtKB:O14558}.
CC -!- PTM: Phosphorylated at Ser-16 by PKA and probably PKD1K; required to
CC protect cardiomyocytes from apoptosis. {ECO:0000250|UniProtKB:O14558,
CC ECO:0000250|UniProtKB:P97541, ECO:0000269|PubMed:21334344}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; BC089621; AAH89621.1; -; mRNA.
DR CCDS; CCDS21097.1; -.
DR RefSeq; NP_001012401.1; NM_001012401.2.
DR AlphaFoldDB; Q5EBG6; -.
DR SMR; Q5EBG6; -.
DR BioGRID; 232583; 2.
DR IntAct; Q5EBG6; 1.
DR STRING; 10090.ENSMUSP00000039172; -.
DR iPTMnet; Q5EBG6; -.
DR PhosphoSitePlus; Q5EBG6; -.
DR jPOST; Q5EBG6; -.
DR MaxQB; Q5EBG6; -.
DR PaxDb; Q5EBG6; -.
DR PeptideAtlas; Q5EBG6; -.
DR PRIDE; Q5EBG6; -.
DR ProteomicsDB; 273281; -.
DR Antibodypedia; 4537; 378 antibodies from 37 providers.
DR DNASU; 243912; -.
DR Ensembl; ENSMUST00000044048; ENSMUSP00000039172; ENSMUSG00000036854.
DR GeneID; 243912; -.
DR KEGG; mmu:243912; -.
DR UCSC; uc009gew.1; mouse.
DR CTD; 126393; -.
DR MGI; MGI:2685325; Hspb6.
DR VEuPathDB; HostDB:ENSMUSG00000036854; -.
DR eggNOG; KOG3591; Eukaryota.
DR GeneTree; ENSGT00940000161100; -.
DR HOGENOM; CLU_095001_2_0_1; -.
DR InParanoid; Q5EBG6; -.
DR OMA; PVQPTWL; -.
DR OrthoDB; 1187096at2759; -.
DR PhylomeDB; Q5EBG6; -.
DR TreeFam; TF105049; -.
DR BioGRID-ORCS; 243912; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Hspb6; mouse.
DR PRO; PR:Q5EBG6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q5EBG6; protein.
DR Bgee; ENSMUSG00000036854; Expressed in interventricular septum and 186 other tissues.
DR Genevisible; Q5EBG6; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
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 Chaperone; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Secreted; Stress response.
FT CHAIN 1..162
FT /note="Heat shock protein beta-6"
FT /id="PRO_0000246077"
FT DOMAIN 56..162
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:0000250|UniProtKB:O14558"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21334344"
FT MOD_RES 66
FT /note="Deamidated glutamine"
FT /evidence="ECO:0000250|UniProtKB:P97541"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97541"
SQ SEQUENCE 162 AA; 17521 MW; D4CA1685AEBD3337 CRC64;
MEIPVPVQPS WLRRASAPLP GFSAPGRLFD QRFGEGLLEA ELASLCPAAI APYYLRAPSV
ALPTAQVSTD SGYFSVLLDV KHFLPEEISV KVVDDHVEVH ARHEERPDEH GFIAREFHRR
YRLPPGVDPA AVTSALSPEG VLSIQATPAS AQAQLPSPPA AK
