HSPB1_BOVIN
ID HSPB1_BOVIN Reviewed; 201 AA.
AC Q3T149;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; BC102129; AAI02130.1; -; mRNA.
DR RefSeq; XP_005225172.1; XM_005225115.1.
DR AlphaFoldDB; Q3T149; -.
DR SMR; Q3T149; -.
DR iPTMnet; Q3T149; -.
DR PaxDb; Q3T149; -.
DR PeptideAtlas; Q3T149; -.
DR PRIDE; Q3T149; -.
DR Ensembl; ENSBTAT00000044397; ENSBTAP00000041898; ENSBTAG00000011969.
DR GeneID; 516099; -.
DR CTD; 3315; -.
DR VEuPathDB; HostDB:ENSBTAG00000011969; -.
DR eggNOG; KOG3591; Eukaryota.
DR GeneTree; ENSGT00940000155882; -.
DR InParanoid; Q3T149; -.
DR OMA; EEWAQWF; -.
DR OrthoDB; 1187096at2759; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000011969; Expressed in bone marrow and 104 other tissues.
DR ExpressionAtlas; Q3T149; baseline and differential.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0001533; C:cornified envelope; IEA:Ensembl.
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:0030018; C:Z disc; IEA:Ensembl.
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:0005080; F:protein kinase C binding; IEA:Ensembl.
DR GO; GO:0008426; F:protein kinase C inhibitor activity; IEA:Ensembl.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
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:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IEA:Ensembl.
DR GO; GO:0038033; P:positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IEA:Ensembl.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0009408; P:response to heat; IBA:GO_Central.
DR GO; GO:0009615; P:response to virus; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Acetylation; Chaperone; Cytoplasm; Cytoskeleton; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Stress response.
FT CHAIN 1..201
FT /note="Heat shock protein beta-1"
FT /id="PRO_0000125924"
FT DOMAIN 72..180
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 68..201
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 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 74
FT /note="Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 78
FT /note="Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5"
FT /evidence="ECO:0000250|UniProtKB:P14602"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 82
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 119
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 170
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04792"
SQ SEQUENCE 201 AA; 22393 MW; 9CEAFF050B7FAD24 CRC64;
MAERRVPFSL LRGPSWDPFR DWYPAHSRLF DQAFGLPRLP EEWSQWLSHS GWPGYVRALP
AAAIEGPAYN RALSRQLSSG VSEIQQTADR WRVSLDVNHF APEELTVKTK DGVVEITGKH
EERQDEHGYI SRCFTRKYTL PPGVDPTLVS SSLSPEGTLT VEAPLPKSAT QSAEITIPVT
FQARAQLGGP EAGKSEQPEN K
