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Heat shock protein beta-1 (HspB1) (Growth-related 25 kDa protein) (Heat shock 25 kDa protein) (HSP 25) (Heat shock 27 kDa protein) (HSP 27) (p25)

 HSPB1_MOUSE             Reviewed;         209 AA.
P14602;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 3.
27-SEP-2017, entry version 178.
RecName: Full=Heat shock protein beta-1;
Short=HspB1;
AltName: Full=Growth-related 25 kDa protein;
AltName: Full=Heat shock 25 kDa protein;
Short=HSP 25;
AltName: Full=Heat shock 27 kDa protein;
Short=HSP 27;
AltName: Full=p25;
Name=Hspb1; Synonyms=Hsp25, Hsp27;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
PubMed=8514194; DOI=10.1016/0378-1119(93)90575-N;
Gaestel M., Gotthardt R., Mueller T.;
"Structure and organisation of a murine gene encoding small heat-shock
protein Hsp25.";
Gene 128:279-283(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
PubMed=8514193; DOI=10.1016/0378-1119(93)90574-M;
Froehli E., Aoyama X., Klemenz R.;
"Cloning of the mouse hsp25 gene and an extremely conserved hsp25
pseudogene.";
Gene 128:273-277(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A), AND PARTIAL PROTEIN
SEQUENCE.
PubMed=2645135; DOI=10.1111/j.1432-1033.1989.tb14542.x;
Gaestel M., Gross B., Benndorf R., Strauss M., Schunk W.-H., Kraft R.,
Otto A., Boehm H., Stahl J., Drabsch H., Bielka H.;
"Molecular cloning, sequencing and expression in Escherichia coli of
the 25-kDa growth-related protein of Ehrlich ascites tumor and its
homology to mammalian stress proteins.";
Eur. J. Biochem. 179:209-213(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
TISSUE=Bone;
PubMed=8132504;
Cooper L.F., Uoshima K.;
"Differential estrogenic regulation of small M(r) heat shock protein
expression in osteoblasts.";
J. Biol. Chem. 269:7869-7873(1994).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PHOSPHORYLATION AT SER-15 AND SER-86.
PubMed=1860870;
Gaestel M., Schroeder W., Benndorf R., Lippmann C., Buchner K.,
Hucho F., Erdmann V.A., Bielka H.;
"Identification of the phosphorylation sites of the murine small heat
shock protein hsp25.";
J. Biol. Chem. 266:14721-14724(1991).
[7]
PHOSPHORYLATION AT SER-15 AND SER-86 BY MAPKAPK2.
PubMed=1332886; DOI=10.1016/0014-5793(92)81216-9;
Stokoe D., Engel K., Campbell D.G., Cohen P., Gaestel M.;
"Identification of MAPKAP kinase 2 as a major enzyme responsible for
the phosphorylation of the small mammalian heat shock proteins.";
FEBS Lett. 313:307-313(1992).
[8]
PHOSPHORYLATION BY MAPKAPK2.
PubMed=8093612;
Jakob U., Gaestel M., Engel K., Buchner J.;
"Small heat shock proteins are molecular chaperones.";
J. Biol. Chem. 268:1517-1520(1993).
[9]
INTERACTION WITH HSPBAP1.
PubMed=10751411; DOI=10.1074/jbc.M001981200;
Liu C., Gilmont R.R., Benndorf R., Welsh M.J.;
"Identification and characterization of a novel protein from Sertoli
cells, PASS1, that associates with mammalian small stress protein
hsp27.";
J. Biol. Chem. 275:18724-18731(2000).
[10]
INTERACTION WITH HSPB8.
PubMed=11342557; DOI=10.1074/jbc.M103001200;
Benndorf R., Sun X., Gilmont R.R., Biederman K.J., Molloy M.P.,
Goodmurphy C.W., Cheng H., Andrews P.C., Welsh M.J.;
"HSP22, a new member of the small heat shock protein superfamily,
interacts with mimic of phosphorylated HSP27 (3DHSP27).";
J. Biol. Chem. 276:26753-26761(2001).
[11]
INTERACTION WITH TGFB1I1.
PubMed=11546764; DOI=10.1074/jbc.M103510200;
Jia Y., Ransom R.F., Shibanuma M., Liu C., Welsh M.J., Smoyer W.E.;
"Identification and characterization of hic-5/ARA55 as an hsp27
binding protein.";
J. Biol. Chem. 276:39911-39918(2001).
[12]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17661394; DOI=10.1002/dvg.20319;
Huang L., Min J.N., Masters S., Mivechi N.F., Moskophidis D.;
"Insights into function and regulation of small heat shock protein 25
(HSPB1) in a mouse model with targeted gene disruption.";
Genesis 45:487-501(2007).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[15]
PHOSPHORYLATION BY MAPKAPK5.
PubMed=21575178; DOI=10.1186/1750-2187-6-4;
Shiryaev A., Dumitriu G., Moens U.;
"Distinct roles of MK2 and MK5 in cAMP/PKA- and stress/p38MAPK-induced
heat shock protein 27 phosphorylation.";
J. Mol. Signal. 6:4-4(2011).
[16]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-12, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Small heat shock protein which functions as a molecular
chaperone probably maintaining denatured proteins in a folding-
competent state. Plays a role in stress resistance and actin
organization (PubMed:17661394). Through its molecular chaperone
activity may regulate numerous biological processes including the
phosphorylation and the axonal transport of neurofilament proteins
(By similarity). {ECO:0000250|UniProtKB:P04792,
ECO:0000269|PubMed:17661394}.
-!- SUBUNIT: Homooligomer. Homodimer; becomes monomeric upon
activation. Heterooligomer; with HSPB6. Associates with alpha- and
beta-tubulin (By similarity). Interacts with TGFB1I1
(PubMed:11546764). Interacts with CRYAB (By similarity). Interacts
with HSPB8 (PubMed:11342557). Interacts with HSPBAP1
(PubMed:10751411). {ECO:0000250|UniProtKB:P04792,
ECO:0000269|PubMed:10751411, ECO:0000269|PubMed:11342557,
ECO:0000269|PubMed:11546764}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04792}.
Nucleus {ECO:0000250|UniProtKB:P04792}. Cytoplasm, cytoskeleton,
spindle {ECO:0000250|UniProtKB:P04792}. Note=Cytoplasmic in
interphase cells. Colocalizes with mitotic spindles in mitotic
cells. Translocates to the nucleus during heat shock and resides
in sub-nuclear structures known as SC35 speckles or nuclear
splicing speckles. {ECO:0000250|UniProtKB:P04792}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Additional isoforms seem to exist.;
Name=A;
IsoId=P14602-1; Sequence=Displayed;
Name=B;
IsoId=P14602-2; Sequence=VSP_002422;
Name=C;
IsoId=P14602-3; Sequence=VSP_002423;
-!- PTM: Phosphorylated upon exposure to protein kinase C activators
and heat shock (By similarity). Phosphorylation by MAPKAPK2 and
MAPKAPK3 in response to stress dissociates HSPB1 from large small
heat-shock protein (sHsps) oligomers and impairs its chaperone
activity and ability to protect against oxidative stress
effectively. Phosphorylation by MAPKAPK5 in response to PKA
stimulation induces F-actin rearrangement (PubMed:1332886,
PubMed:1860870, PubMed:21575178, PubMed:8093612).
{ECO:0000250|UniProtKB:P04792, ECO:0000269|PubMed:1332886,
ECO:0000269|PubMed:1860870, ECO:0000269|PubMed:21575178,
ECO:0000269|PubMed:8093612}.
-!- DISRUPTION PHENOTYPE: Mice are viable and fertile with no apparent
morphological abnormalities in tissues under physiological
conditions. {ECO:0000269|PubMed:17661394}.
-!- SIMILARITY: Belongs to the small heat shock protein (HSP20)
family. {ECO:0000255|PROSITE-ProRule:PRU00285}.
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EMBL; X14687; CAA32818.1; -; mRNA.
EMBL; X14686; CAB37341.1; -; mRNA.
EMBL; L11609; AAA37862.1; -; Genomic_DNA.
EMBL; L11608; AAA37862.1; JOINED; Genomic_DNA.
EMBL; L07577; AAA37861.1; -; Genomic_DNA.
EMBL; U03560; AAA18335.1; -; mRNA.
EMBL; U03561; AAA18336.1; -; mRNA.
EMBL; U03562; AAA18337.1; -; mRNA.
EMBL; BC018257; AAH18257.1; -; mRNA.
CCDS; CCDS39320.1; -. [P14602-1]
PIR; A53423; A53423.
PIR; I49763; JN0679.
PIR; S02143; S02143.
RefSeq; NP_038588.2; NM_013560.2. [P14602-1]
UniGene; Mm.13849; -.
DisProt; DP00142; -.
ProteinModelPortal; P14602; -.
SMR; P14602; -.
BioGrid; 200449; 16.
CORUM; P14602; -.
IntAct; P14602; 8.
MINT; MINT-4098074; -.
STRING; 10090.ENSMUSP00000005077; -.
iPTMnet; P14602; -.
PhosphoSitePlus; P14602; -.
REPRODUCTION-2DPAGE; IPI00128522; -.
REPRODUCTION-2DPAGE; IPI00468068; -.
REPRODUCTION-2DPAGE; P14602; -.
SWISS-2DPAGE; P14602; -.
UCD-2DPAGE; P14602; -.
PaxDb; P14602; -.
PeptideAtlas; P14602; -.
PRIDE; P14602; -.
Ensembl; ENSMUST00000005077; ENSMUSP00000005077; ENSMUSG00000004951. [P14602-1]
GeneID; 15507; -.
KEGG; mmu:15507; -.
UCSC; uc008zze.2; mouse. [P14602-1]
CTD; 3315; -.
MGI; MGI:96240; Hspb1.
eggNOG; KOG3591; Eukaryota.
eggNOG; ENOG410YERS; LUCA.
GeneTree; ENSGT00760000119238; -.
HOGENOM; HOG000233955; -.
HOVERGEN; HBG054766; -.
InParanoid; P14602; -.
KO; K04455; -.
OMA; FDQSFGM; -.
OrthoDB; EOG091G0USC; -.
PhylomeDB; P14602; -.
TreeFam; TF105049; -.
Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
PRO; PR:P14602; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000004951; -.
CleanEx; MM_HSPB1; -.
ExpressionAtlas; P14602; baseline and differential.
Genevisible; P14602; MM.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0043292; C:contractile fiber; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0031012; C:extracellular matrix; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0005622; C:intracellular; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0000502; C:proteasome complex; ISS:BHF-UCL.
GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO; GO:0030018; C:Z disc; IDA:MGI.
GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
GO; GO:0044183; F:protein binding involved in protein folding; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0005080; F:protein kinase C binding; IDA:BHF-UCL.
GO; GO:0008426; F:protein kinase C inhibitor activity; IDA:BHF-UCL.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0043130; F:ubiquitin binding; ISS:BHF-UCL.
GO; GO:0099641; P:anterograde axonal protein transport; ISS:UniProtKB.
GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISO:MGI.
GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IDA:MGI.
GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IDA:BHF-UCL.
GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:BHF-UCL.
GO; GO:0070527; P:platelet aggregation; ISO:MGI.
GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:MGI.
GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; ISO:MGI.
GO; GO:0038033; P:positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway; ISO:MGI.
GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:BHF-UCL.
GO; GO:0042535; P:positive regulation of tumor necrosis factor biosynthetic process; IDA:BHF-UCL.
GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IDA:BHF-UCL.
GO; GO:0001932; P:regulation of protein phosphorylation; ISO:MGI.
GO; GO:0006986; P:response to unfolded protein; NAS:BHF-UCL.
GO; GO:0009615; P:response to virus; ISS:BHF-UCL.
GO; GO:0001895; P:retina homeostasis; IEA:Ensembl.
Gene3D; 2.60.40.790; -; 1.
InterPro; IPR002068; A-crystallin/Hsp20_dom.
InterPro; IPR001436; Alpha-crystallin/HSP.
InterPro; IPR031107; HSP20.
InterPro; IPR008978; HSP20-like_chaperone.
PANTHER; PTHR11527; PTHR11527; 1.
Pfam; PF00011; HSP20; 1.
PRINTS; PR00299; ACRYSTALLIN.
SUPFAM; SSF49764; SSF49764; 1.
PROSITE; PS01031; SHSP; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Chaperone; Complete proteome;
Cytoplasm; Cytoskeleton; Direct protein sequencing; Methylation;
Nucleus; Phosphoprotein; Reference proteome; Stress response.
CHAIN 1 209 Heat shock protein beta-1.
/FTId=PRO_0000125928.
DOMAIN 80 188 sHSP. {ECO:0000255|PROSITE-
ProRule:PRU00285}.
REGION 74 209 Interaction with TGFB1I1. {ECO:0000250}.
MOD_RES 12 12 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000250|UniProtKB:P42930}.
MOD_RES 15 15 Phosphoserine; by MAPKAPK2, MAPKAPK3, PKA
and PKC. {ECO:0000269|PubMed:1332886,
ECO:0000269|PubMed:1860870}.
MOD_RES 27 27 Phosphoserine.
{ECO:0000250|UniProtKB:P42930}.
MOD_RES 86 86 Phosphoserine; by MAPKAPK2, MAPKAPK3,
MAPKAPK5, PKA and PKC.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:1332886,
ECO:0000269|PubMed:1860870}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000250|UniProtKB:P04792}.
MOD_RES 90 90 Phosphoserine.
{ECO:0000250|UniProtKB:P04792}.
MOD_RES 102 102 Phosphoserine.
{ECO:0000250|UniProtKB:P04792}.
MOD_RES 127 127 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04792}.
MOD_RES 178 178 Phosphothreonine.
{ECO:0000250|UniProtKB:P04792}.
MOD_RES 180 180 Phosphoserine.
{ECO:0000250|UniProtKB:P04792}.
MOD_RES 203 203 Phosphoserine.
{ECO:0000250|UniProtKB:P04792}.
VAR_SEQ 37 70 Missing (in isoform C).
{ECO:0000303|PubMed:8132504}.
/FTId=VSP_002423.
VAR_SEQ 61 72 Missing (in isoform B).
{ECO:0000303|PubMed:8132504}.
/FTId=VSP_002422.
CONFLICT 13 13 S -> T (in Ref. 4; AAA18335/AAA18336/
AAA18337). {ECO:0000305}.
CONFLICT 17 17 E -> G (in Ref. 4; AAA18335).
{ECO:0000305}.
CONFLICT 67 68 PA -> L (in Ref. 4; AAA18335).
{ECO:0000305}.
CONFLICT 99 99 Missing (in Ref. 3; CAA32818/CAB37341).
{ECO:0000305}.
CONFLICT 108 109 FA -> VI (in Ref. 3; CAA32818/CAB37341).
{ECO:0000305}.
CONFLICT 141 141 C -> Q (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 181 181 A -> T (in Ref. 3; CAA32818/CAB37341).
{ECO:0000305}.
SEQUENCE 209 AA; 23014 MW; 31BD9FAF4E107C50 CRC64;
MTERRVPFSL LRSPSWEPFR DWYPAHSRLF DQAFGVPRLP DEWSQWFSAA GWPGYVRPLP
AATAEGPAAV TLAAPAFSRA LNRQLSSGVS EIRQTADRWR VSLDVNHFAP EELTVKTKEG
VVEITGKHEE RQDEHGYISR CFTRKYTLPP GVDPTLVSSS LSPEGTLTVE APLPKAVTQS
AEITIPVTFE ARAQIGGPEA GKSEQSGAK


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