HSPB1_CRILO
ID HSPB1_CRILO Reviewed; 213 AA.
AC P15991;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Heat shock protein beta-1;
DE Short=HspB1;
DE AltName: Full=Heat shock 27 kDa protein;
DE Short=HSP 27;
GN Name=HSPB1; Synonyms=HSP27;
OS Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10030;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung fibroblast;
RX PubMed=2326203; DOI=10.1093/nar/18.6.1637;
RA Lavoie J., Chretien P., Landry J.;
RT "Sequence of the Chinese hamster small heat shock protein HSP27.";
RL Nucleic Acids Res. 18:1637-1637(1990).
CC -!- FUNCTION: Small heat shock protein which functions as a molecular
CC chaperone probably maintaining denatured proteins in a folding-
CC competent state. Plays a role in stress resistance and actin
CC organization. Through its molecular chaperone activity may regulate
CC numerous biological processes including the phosphorylation and the
CC axonal transport of neurofilament proteins.
CC {ECO:0000250|UniProtKB:P04792}.
CC -!- SUBUNIT: Homooligomer. Homodimer; becomes monomeric upon activation.
CC Heterooligomer; with HSPB6. Associates with alpha- and beta-tubulin.
CC Interacts with TGFB1I1. Interacts with CRYAB. Interacts with HSPB8.
CC Interacts with HSPBAP1. {ECO:0000250|UniProtKB:P04792}.
CC -!- INTERACTION:
CC P15991; Q9UER7: DAXX; Xeno; NbExp=3; IntAct=EBI-1559114, EBI-77321;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04792}. Nucleus
CC {ECO:0000250|UniProtKB:P04792}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:P04792}. Note=Cytoplasmic in interphase cells.
CC Colocalizes with mitotic spindles in mitotic cells. Translocates to the
CC nucleus during heat shock and resides in sub-nuclear structures known
CC as SC35 speckles or nuclear splicing speckles.
CC {ECO:0000250|UniProtKB:P04792}.
CC -!- PTM: Phosphorylated upon exposure to protein kinase C activators and
CC heat shock. Phosphorylation by MAPKAPK2 and MAPKAPK3 in response to
CC stress dissociates HSPB1 from large small heat-shock protein (sHsps)
CC oligomers and impairs its chaperone activity and ability to protect
CC against oxidative stress effectively. Phosphorylation by MAPKAPK5 in
CC response to PKA stimulation induces F-actin rearrangement.
CC {ECO:0000250|UniProtKB:P04792}.
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; X51747; CAA36036.1; -; mRNA.
DR PIR; S15907; S15907.
DR AlphaFoldDB; P15991; -.
DR SMR; P15991; -.
DR IntAct; P15991; 3.
DR MINT; P15991; -.
DR iPTMnet; P15991; -.
DR PRIDE; P15991; -.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0044183; F:protein folding chaperone; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0099641; P:anterograde axonal protein transport; ISS:UniProtKB.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISS:UniProtKB.
DR CDD; cd06475; ACD_HspB1_like; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR InterPro; IPR037876; ACD_HspB1.
DR InterPro; IPR001436; Alpha-crystallin/sHSP_animal.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR PANTHER; PTHR45640; PTHR45640; 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 Acetylation; Chaperone; Cytoplasm; Cytoskeleton; Methylation; Nucleus;
KW Phosphoprotein; Stress response.
FT CHAIN 1..213
FT /note="Heat shock protein beta-1"
FT /id="PRO_0000125926"
FT DOMAIN 84..192
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 78..213
FT /note="Interaction with TGFB1I1"
FT /evidence="ECO:0000250"
FT MOD_RES 12
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42930"
FT MOD_RES 15
FT /note="Phosphoserine; by MAPKAPK2 and MAPKAPK3"
FT /evidence="ECO:0000250|UniProtKB:P14602"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42930"
FT MOD_RES 90
FT /note="Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5"
FT /evidence="ECO:0000250|UniProtKB:P14602"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 131
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
SQ SEQUENCE 213 AA; 23419 MW; 29E633DBBFA3F89F CRC64;
MTERRVPFSL LRSPSWEPFR DWYPAHSRLF DQAFGVPRLP DEWSQWFSAA GWPGYVRPLP
AATAEGPAAV ALAAPLAAPA FHRALNRQLS SGVSEIRQTA DRWRVSLDVN HFAPEELTVK
TKEGVVEITG KHEERQDEHG YISRCFTRKY TLPPGVDPTL VSSSLSPEGT LTVEAPLPKT
ATQSAEITIP VTFEARAQIG GQEAGKSEQS GAK
