Heat shock protein beta-1 - Mus musculus (Mouse)

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P14602 (HSPB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 138. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

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Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Heat shock protein beta-1
Short name=HspB1

Alternative name(s):
Growth-related 25 kDa protein
Heat shock 25 kDa protein
Short name=HSP 25
Heat shock 27 kDa protein
Short name=HSP 27
p25

Gene names

Name:	Hspb1
Synonyms:	Hsp25, Hsp27

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	209 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in stress resistance and actin organization.
Subunit structure	Associates with alpha- and beta-tubulin, microtubules and CRYAB. Interacts with HSPB8 By similarity. Interacts with HSPBAP1 and TGFB1I1. Ref.9 Ref.10
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Cytoplasm › cytoskeleton › spindle By similarity. 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 By similarity.
Post-translational modification	Phosphorylation by MAPKAPK2 and MAPKAPK3 in response to stress leads to dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair its chaperone activity and ability to protect against oxidative stress effectively. Phosphorylation by MAPKAPK5 in response to PKA stimulation induces F-actin rearrangement.
Disruption phenotype	No visible phoenotype. Mice are viable and fertile with no apparent morphological abnormalities in tissues under physiological conditions. Ref.11
Sequence similarities	Belongs to the small heat shock protein (HSP20) family.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing
Molecular function	Chaperone
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from electronic annotation. Source: Compara blood vessel endothelial cell migration Inferred from electronic annotation. Source: Compara cellular response to vascular endothelial growth factor stimulus Inferred from electronic annotation. Source: Compara endothelial cell chemotaxis Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from direct assay PubMed 15731106. Source: BHF-UCL positive regulation of interleukin-1 beta production Inferred from direct assay PubMed 12385642. Source: BHF-UCL positive regulation of tumor necrosis factor biosynthetic process Inferred from direct assay PubMed 12385642. Source: BHF-UCL regulation of I-kappaB kinase/NF-kappaB cascade Inferred from direct assay PubMed 12385642. Source: BHF-UCL response to unfolded protein Non-traceable author statement PubMed 10859165. Source: BHF-UCL response to virus Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular_component	Z disc Inferred from direct assay PubMed 14627610. Source: MGI cell surface Inferred from sequence or structural similarity. Source: BHF-UCL nucleus Inferred from direct assay PubMed 11774370. Source: MGI plasma membrane Inferred from direct assay PubMed 14627610. Source: MGI proteasome complex Inferred from sequence or structural similarity. Source: BHF-UCL spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	protein kinase C binding Inferred from direct assay PubMed 15731106. Source: BHF-UCL protein kinase C inhibitor activity Inferred from direct assay PubMed 15731106. Source: BHF-UCL ubiquitin binding Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] Note: Additional isoforms seem to exist.

Isoform A (identifier: P14602-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform B (identifier: P14602-2) The sequence of this isoform differs from the canonical sequence as follows: 61-72: Missing.

Isoform C (identifier: P14602-3) The sequence of this isoform differs from the canonical sequence as follows: 37-70: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 209

209

Heat shock protein beta-1

PRO_0000125928

Regions

Region

74 – 209

136

Interaction with TGFB1I1 By similarity

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine; by MAPKAPK2, MAPKAPK3, PKA and PKC Ref.6 Ref.7 Ref.12

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine; by MAPKAPK2, MAPKAPK3, MAPKAPK5, PKA and PKC Ref.6 Ref.7

Modified residue

Phosphoserine By similarity

Modified residue

127

N6-acetyllysine By similarity

Modified residue

203

Phosphoserine By similarity

Natural variations

Alternative sequence

37 – 70

Missing in isoform C.

VSP_002423

Alternative sequence

61 – 72

Missing in isoform B.

VSP_002422

Experimental info

Sequence conflict

S → T in AAA18335. Ref.4

Sequence conflict

S → T in AAA18336. Ref.4

Sequence conflict

S → T in AAA18337. Ref.4

Sequence conflict

E → G in AAA18335. Ref.4

Sequence conflict

67 – 68

PA → L in AAA18335. Ref.4

Sequence conflict

Missing in CAA32818. Ref.3

Sequence conflict

Missing in CAB37341. Ref.3

Sequence conflict

108 – 109

FA → VI in CAA32818. Ref.3

Sequence conflict

108 – 109

FA → VI in CAB37341. Ref.3

Sequence conflict

141

C → Q AA sequence Ref.3

Sequence conflict

181

A → T in CAA32818. Ref.3

Sequence conflict

181

A → T in CAB37341. Ref.3

Sequences

Sequence		Length	Mass (Da)
Isoform A [UniParc]. Last modified June 1, 1994. Version 3. Checksum: 31BD9FAF4E107C50 Show »	FASTA	209	23,014
10 20 30 40 50 60 MTERRVPFSL LRSPSWEPFR DWYPAHSRLF DQAFGVPRLP DEWSQWFSAA GWPGYVRPLP 70 80 90 100 110 120 AATAEGPAAV TLAAPAFSRA LNRQLSSGVS EIRQTADRWR VSLDVNHFAP EELTVKTKEG 130 140 150 160 170 180 VVEITGKHEE RQDEHGYISR CFTRKYTLPP GVDPTLVSSS LSPEGTLTVE APLPKAVTQS 190 200 AEITIPVTFE ARAQIGGPEA GKSEQSGAK « Hide
Isoform B [UniParc]. Checksum: 071D3C112509C01A Show »	FASTA	197	21,961
10 20 30 40 50 60 MTERRVPFSL LRSPSWEPFR DWYPAHSRLF DQAFGVPRLP DEWSQWFSAA GWPGYVRPLP 70 80 90 100 110 120 AAPAFSRALN RQLSSGVSEI RQTADRWRVS LDVNHFAPEE LTVKTKEGVV EITGKHEERQ 130 140 150 160 170 180 DEHGYISRCF TRKYTLPPGV DPTLVSSSLS PEGTLTVEAP LPKAVTQSAE ITIPVTFEAR 190 AQIGGPEAGK SEQSGAK « Hide
Isoform C [UniParc]. Checksum: AA7E60872B1C485B Show »	FASTA	175	19,380
10 20 30 40 50 60 MTERRVPFSL LRSPSWEPFR DWYPAHSRLF DQAFGVTLAA PAFSRALNRQ LSSGVSEIRQ 70 80 90 100 110 120 TADRWRVSLD VNHFAPEELT VKTKEGVVEI TGKHEERQDE HGYISRCFTR KYTLPPGVDP 130 140 150 160 170 TLVSSSLSPE GTLTVEAPLP KAVTQSAEIT IPVTFEARAQ IGGPEAGKSE QSGAK « Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and organisation of a murine gene encoding small heat-shock protein Hsp25." Gaestel M., Gotthardt R., Mueller T. Gene 128:279-283(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
[2]	"Cloning of the mouse hsp25 gene and an extremely conserved hsp25 pseudogene." Froehli E., Aoyama X., Klemenz R. Gene 128:273-277(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
[3]	"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." Gaestel M., Gross B., Benndorf R., Strauss M., Schunk W.-H., Kraft R., Otto A., Boehm H., Stahl J., Drabsch H., Bielka H. Eur. J. Biochem. 179:209-213(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A), PARTIAL PROTEIN SEQUENCE.
[4]	"Differential estrogenic regulation of small M(r) heat shock protein expression in osteoblasts." Cooper L.F., Uoshima K. J. Biol. Chem. 269:7869-7873(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C). Tissue: Bone.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). Strain: FVB/N. Tissue: Mammary gland.
[6]	"Identification of the phosphorylation sites of the murine small heat shock protein hsp25." Gaestel M., Schroeder W., Benndorf R., Lippmann C., Buchner K., Hucho F., Erdmann V.A., Bielka H. J. Biol. Chem. 266:14721-14724(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-15 AND SER-86.
[7]	"Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins." Stokoe D., Engel K., Campbell D.G., Cohen P., Gaestel M. FEBS Lett. 313:307-313(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-15 AND SER-86 BY MAPKAPK2.
[8]	"Small heat shock proteins are molecular chaperones." Jakob U., Gaestel M., Engel K., Buchner J. J. Biol. Chem. 268:1517-1520(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY MAPKAPK2.
[9]	"Identification and characterization of a novel protein from Sertoli cells, PASS1, that associates with mammalian small stress protein hsp27." Liu C., Gilmont R.R., Benndorf R., Welsh M.J. J. Biol. Chem. 275:18724-18731(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HSPBAP1.
[10]	"Identification and characterization of hic-5/ARA55 as an hsp27 binding protein." Jia Y., Ransom R.F., Shibanuma M., Liu C., Welsh M.J., Smoyer W.E. J. Biol. Chem. 276:39911-39918(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TGFB1I1.
[11]	"Insights into function and regulation of small heat shock protein 25 (HSPB1) in a mouse model with targeted gene disruption." Huang L., Min J.N., Masters S., Mivechi N.F., Moskophidis D. Genesis 45:487-501(2007) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[12]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, MASS SPECTROMETRY. Tissue: Liver.
[13]	"Distinct roles of MK2 and MK5 in cAMP/PKA- and stress/p38MAPK-induced heat shock protein 27 phosphorylation." Shiryaev A., Dumitriu G., Moens U. J. Mol. Signal. 6:4-4(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY MAPKAPK5.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X14687 mRNA. Translation: CAA32818.1. X14686 mRNA. Translation: CAB37341.1. L11609, L11608 Genomic DNA. Translation: AAA37862.1. L07577 Genomic DNA. Translation: AAA37861.1. U03560 mRNA. Translation: AAA18335.1. U03561 mRNA. Translation: AAA18336.1. U03562 mRNA. Translation: AAA18337.1. BC018257 mRNA. Translation: AAH18257.1.
IPI	IPI00128522. IPI00468068. IPI00623819.
PIR	A53423. JN0679. I49763. S02143.
RefSeq	NP_038588.2. NM_013560.2.
UniGene	Mm.13849.
3D structure databases
DisProt	DP00142.
ProteinModelPortal	P14602.
SMR	P14602. Positions 20-195.
ModBase	Search...
Protein-protein interaction databases
IntAct	P14602. 6 interactions.
MINT	MINT-4098074.
STRING	10090.ENSMUSP00000005077.
PTM databases
PhosphoSite	P14602.
2D gel databases
REPRODUCTION-2DPAGE	IPI00128522. IPI00468068. P14602.
SWISS-2DPAGE	P14602.
UCD-2DPAGE	P14602.
Proteomic databases
PaxDb	P14602.
PRIDE	P14602.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000005077; ENSMUSP00000005077; ENSMUSG00000004951.
GeneID	15507.
KEGG	mmu:15507.
UCSC	uc008zze.2. mouse.
Organism-specific databases
CTD	3315.
MGI	MGI:96240. Hspb1.
Phylogenomic databases
eggNOG	NOG307785.
HOGENOM	HOG000233955.
HOVERGEN	HBG054766.
InParanoid	P14602.
KO	K04455.
OMA	RTPSWDP.
OrthoDB	EOG4DR9DF.
Gene expression databases
ArrayExpress	P14602.
Bgee	P14602.
CleanEx	MM_HSPB1.
Genevestigator	P14602.
GermOnline	ENSMUSG00000004951. Mus musculus.
Family and domain databases
InterPro	IPR002068. a-crystallin/Hsp20_dom. IPR001436. Alpha-crystallin/HSP. IPR008978. HSP20-like_chaperone. [Graphical view]
Pfam	PF00011. HSP20. 1 hit. [Graphical view]
PIRSF	PIRSF036514. Sm_HSP_B1. 1 hit.
PRINTS	PR00299. ACRYSTALLIN.
SUPFAM	SSF49764. HSP20_chap. 1 hit.
PROSITE	PS01031. HSP20. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	288412.
SOURCE	Search...

Entry information

Entry name

HSPB1_MOUSE

Accession

Primary (citable) accession number: P14602

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	June 1, 1994
Last modified:	May 29, 2013
This is version 138 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents