P15991 (HSPB1_CRILO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Heat shock 27 kDa protein
Short name=HSP 27

Gene names

Name:	HSPB1
Synonyms:	HSP27

Organism

Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster)

Taxonomic identifier

10030 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus

Protein attributes

Sequence length	213 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 and HSPBAP1 By similarity.
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 By similarity.
Sequence similarities	Belongs to the small heat shock protein (HSP20) family.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm Cytoskeleton Nucleus
Molecular function	Chaperone
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DAXX	Q9UER7	3	EBI-1559114,EBI-77321	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 213	213	Heat shock protein beta-1		PRO_0000125926
Regions
	Region	78 – 213	136	Interaction with TGFB1I1 By similarity
Amino acid modifications
	Modified residue	13	1	Phosphoserine By similarity
	Modified residue	15	1	Phosphoserine; by MAPKAPK2 and MAPKAPK3 By similarity
	Modified residue	27	1	Phosphoserine By similarity
	Modified residue	90	1	Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5 By similarity
	Modified residue	91	1	Phosphoserine By similarity
	Modified residue	131	1	N6-acetyllysine By similarity
	Modified residue	207	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P15991 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 29E633DBBFA3F89F	FASTA	213	23,419
	10 20 30 40 50 60 MTERRVPFSL LRSPSWEPFR DWYPAHSRLF DQAFGVPRLP DEWSQWFSAA GWPGYVRPLP 70 80 90 100 110 120 AATAEGPAAV ALAAPLAAPA FHRALNRQLS SGVSEIRQTA DRWRVSLDVN HFAPEELTVK 130 140 150 160 170 180 TKEGVVEITG KHEERQDEHG YISRCFTRKY TLPPGVDPTL VSSSLSPEGT LTVEAPLPKT 190 200 210 ATQSAEITIP VTFEARAQIG GQEAGKSEQS GAK

References

[1]	"Sequence of the Chinese hamster small heat shock protein HSP27." Lavoie J., Chretien P., Landry J. Nucleic Acids Res. 18:1637-1637(1990) [PubMed: 2326203] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung fibroblast.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X51747 mRNA. Translation: CAA36036.1.
PIR	S15907.
3D structure databases
ProteinModelPortal	P15991.
ModBase	Search...
Protein-protein interaction databases
IntAct	P15991. 3 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG054766.
Family and domain databases
InterPro	IPR001436. Alpha-crystallin/HSP. IPR002068. Hsp20. 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...

Entry information

Entry name

HSPB1_CRILO

Accession

Primary (citable) accession number: P15991

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	January 25, 2012
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program