HSPB1_RAT
ID HSPB1_RAT Reviewed; 206 AA.
AC P42930; Q63922; Q9QWA8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 152.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8793069; DOI=10.1095/biolreprod55.1.141;
RA Welsh M.J., Wu W., Parvinen M., Gilmont R.R.;
RT "Variation in expression of hsp27 messenger ribonucleic acid during the
RT cycle of the seminiferous epithelium and co-localization of hsp27 and
RT microfilaments in Sertoli cells of the rat.";
RL Biol. Reprod. 55:141-151(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=7916612; DOI=10.1006/bbrc.1993.2631;
RA Uoshima K., Handelman B., Cooper L.F.;
RT "Isolation and characterization of a rat HSP 27 gene.";
RL Biochem. Biophys. Res. Commun. 197:1388-1395(1993).
RN [3]
RP PROTEIN SEQUENCE OF 13-19; 21-31; 42-83; 104-123; 133-140 AND 190-206,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Skeletal muscle;
RX PubMed=8282729; DOI=10.1093/oxfordjournals.jbchem.a124184;
RA Inaguma Y., Goto S., Shinohara H., Hasegawa K., Ohshima K., Kato K.;
RT "Physiological and pathological changes in levels of the two small stress
RT proteins, HSP27 and alpha B crystallin, in rat hindlimb muscles.";
RL J. Biochem. 114:378-384(1993).
RN [4]
RP PROTEIN SEQUENCE OF 29-38, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [5]
RP INTERACTION WITH HSPBAP1.
RX 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 cells,
RT PASS1, that associates with mammalian small stress protein hsp27.";
RL J. Biol. Chem. 275:18724-18731(2000).
RN [6]
RP INTERACTION WITH TGFB1I1.
RX PubMed=11546764; DOI=10.1074/jbc.m103510200;
RA Jia Y., Ransom R.F., Shibanuma M., Liu C., Welsh M.J., Smoyer W.E.;
RT "Identification and characterization of hic-5/ARA55 as an hsp27 binding
RT protein.";
RL J. Biol. Chem. 276:39911-39918(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-86 AND SER-90, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-15 AND SER-86, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By
CC similarity). Interacts with TGFB1I1 (PubMed:11546764). Interacts with
CC CRYAB (By similarity). Interacts with HSPB8 (By similarity). Interacts
CC with HSPBAP1 (PubMed:10751411). {ECO:0000250|UniProtKB:P04792,
CC ECO:0000269|PubMed:10751411, ECO:0000269|PubMed:11546764}.
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 -!- TISSUE SPECIFICITY: Expressed in a variety of tissues. High levels in
CC lung, adrenal, xiphoid, adipose tissue, heart and striated and smooth
CC muscle, lower levels in the CNS. Adult levels are much higher in the
CC slow-twitch soleus muscle than in the fast-twitch rectus femoris and
CC extensor digitorum muscles. {ECO:0000269|PubMed:8282729}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the soleus and rectus femoris muscles
CC at prenatal day 2, increasing to a maximum at postnatal day 3.
CC Expression in the rectus femoris muscle then decreases reaching adult
CC levels within a few weeks. {ECO:0000269|PubMed:8282729}.
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; M86389; AAA41353.1; -; mRNA.
DR EMBL; S67755; AAB29536.2; -; Genomic_DNA.
DR PIR; JN0924; JN0924.
DR AlphaFoldDB; P42930; -.
DR SMR; P42930; -.
DR BioGRID; 246632; 5.
DR IntAct; P42930; 4.
DR MINT; P42930; -.
DR STRING; 10116.ENSRNOP00000032902; -.
DR iPTMnet; P42930; -.
DR PhosphoSitePlus; P42930; -.
DR jPOST; P42930; -.
DR PaxDb; P42930; -.
DR PRIDE; P42930; -.
DR RGD; 61306; Hspb1.
DR eggNOG; KOG3591; Eukaryota.
DR InParanoid; P42930; -.
DR PhylomeDB; P42930; -.
DR Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-RNO-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-RNO-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-RNO-9009391; Extra-nuclear estrogen signaling.
DR PRO; PR:P42930; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0097512; C:cardiac myofibril; IDA:RGD.
DR GO; GO:0043292; C:contractile fiber; ISO:RGD.
DR GO; GO:0001533; C:cornified envelope; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0031674; C:I band; IDA:RGD.
DR GO; GO:0031430; C:M band; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098839; C:postsynaptic density membrane; IDA:RGD.
DR GO; GO:0000502; C:proteasome complex; IDA:RGD.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
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:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0005080; F:protein kinase C binding; ISO:RGD.
DR GO; GO:0008426; F:protein kinase C inhibitor activity; ISO:RGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0043130; F:ubiquitin binding; IDA:RGD.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0099641; P:anterograde axonal protein transport; ISS:UniProtKB.
DR GO; GO:1903545; P:cellular response to butyrate; IEP:RGD.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0071348; P:cellular response to interleukin-11; IEP:RGD.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISO:RGD.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:RGD.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:1903202; P:negative regulation of oxidative stress-induced cell death; IMP:RGD.
DR GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:RGD.
DR GO; GO:0045590; P:negative regulation of regulatory T cell differentiation; IMP:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; ISO:RGD.
DR GO; GO:0038033; P:positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IGI:ParkinsonsUK-UCL.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:1990776; P:response to angiotensin; IEP:RGD.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
DR GO; GO:0002931; P:response to ischemia; IEP:RGD.
DR GO; GO:0035994; P:response to muscle stretch; IEP:RGD.
DR GO; GO:0009615; P:response to virus; ISO:RGD.
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; Direct protein sequencing;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Stress response.
FT CHAIN 1..206
FT /note="Heat shock protein beta-1"
FT /id="PRO_0000125930"
FT DOMAIN 80..188
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 74..206
FT /note="Interaction with TGFB1I1"
FT /evidence="ECO:0000269|PubMed:11546764"
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:0007744|PubMed:22673903"
FT MOD_RES 15
FT /note="Phosphoserine; by MAPKAPK2 and MAPKAPK3"
FT /evidence="ECO:0000305, ECO:0007744|PubMed:22673903"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 86
FT /note="Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 127
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT CONFLICT 49
FT /note="S -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="R -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="Missing (in Ref. 2; AAB29536)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 206 AA; 22893 MW; 1CEC75582E5E34B2 CRC64;
MTERRVPFSL LRSPSWEPFR DWYPAHSRLF DQAFGVPRFP DEWSQWFSSA GWPGYVRPLP
AATAEGPAAV TLARPAFSRA LNRQLSSGVS EIRQTADRWR VSLDVNHFAP EELTVKTKEG
VVEITGKHEE RQDEHGYISR CFTRKYTLPP GVDPTLVSSS LSPEGTLTVE APLPKAVTQS
AEITIPVTFE ARAQIGGPES EQSGAK
