HSPB1

Functionⁱ

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. Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins.By similarity

GO - Molecular functionⁱ

identical protein binding Source: UniProtKB
protein binding involved in protein folding Source: UniProtKB
protein homodimerization activity Source: UniProtKB

Complete GO annotation...

GO - Biological processⁱ

anterograde axonal protein transport Source: UniProtKB
chaperone-mediated protein folding Source: UniProtKB
regulation of protein phosphorylation Source: UniProtKB

Complete GO annotation...

Keywordsⁱ

Molecular function	Chaperone
Biological process	Stress response

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Heat shock protein beta-1 Short name: HspB1 Alternative name(s): Heat shock 27 kDa protein Short name: HSP 27
Gene namesⁱ	Name:HSPB1 Synonyms:HSP27
Organismⁱ	Bos taurus (Bovine)
Taxonomic identifierⁱ	9913 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos
Proteomesⁱ	UP000009136 Componentⁱ: Unplaced

Subcellular locationⁱ

Cytoplasm
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:P04792 (HSPB1_HUMAN)
Nucleus
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:P04792 (HSPB1_HUMAN)
Cytoplasm › cytoskeleton › spindle
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:P04792 (HSPB1_HUMAN)

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

GO - Cellular componentⁱ

axon cytoplasm Source: GOC
cytoplasm Source: UniProtKB
nucleus Source: UniProtKB
spindle Source: UniProtKB-SubCell

Complete GO annotation...

Keywords - Cellular componentⁱ

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000125924	1 – 201	Heat shock protein beta-1Add BLAST		201

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	12	Omega-N-methylarginineBy similarity	1
Modified residueⁱ	15	Phosphoserine; by MAPKAPK2 and MAPKAPK3By similarity	1
Modified residueⁱ	27	PhosphoserineBy similarity	1
Modified residueⁱ	74	Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5By similarity	1
Modified residueⁱ	78	Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5By similarity	1
Modified residueⁱ	79	PhosphoserineBy similarity	1
Modified residueⁱ	82	PhosphoserineBy similarity	1
Modified residueⁱ	94	PhosphoserineBy similarity	1
Modified residueⁱ	119	N6-acetyllysineBy similarity	1
Modified residueⁱ	170	PhosphothreonineBy similarity	1
Modified residueⁱ	172	PhosphoserineBy similarity	1
Modified residueⁱ	195	PhosphoserineBy similarity	1

Post-translational modificationⁱ

Phosphorylated upon exposure to protein kinase C activators and heat shock. 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.By similarity

Keywords - PTMⁱ

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbⁱ	Q3T149.
PeptideAtlas More...PeptideAtlasⁱ	Q3T149.
PRIDEⁱ	Q3T149.

PTM databases

iPTMnetⁱ	Q3T149.

iPTMnetⁱ

Q3T149.

Interactionⁱ

Subunit structureⁱ

Homooligomer. Homodimer; becomes monomeric upon activation. Heterooligomer; with HSPB6. Associates with alpha- and beta-tubulin. Interacts with TGFB1I1. Interacts with CRYAB. Interacts with HSPB8. Interacts with HSPBAP1.By similarity

GO - Molecular functionⁱ

identical protein binding Source: UniProtKB
protein binding involved in protein folding Source: UniProtKB
protein homodimerization activity Source: UniProtKB

Complete GO annotation...

Protein-protein interaction databases

STRINGⁱ	9913.ENSBTAP00000015883.

STRINGⁱ

9913.ENSBTAP00000015883.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q3T149.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	72 – 180	sHSPPROSITE-ProRule annotationAdd BLAST		109

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	68 – 201	Interaction with TGFB1I1By similarityAdd BLAST		134

Sequence similaritiesⁱ

Belongs to the small heat shock protein (HSP20) family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGⁱ	KOG3591. Eukaryota. ENOG410YERS. LUCA.
HOGENOMⁱ	HOG000233955.
HOVERGENⁱ	HBG054766.
InParanoidⁱ	Q3T149.

Family and domain databases

Gene3Dⁱ	2.60.40.790. 1 hit.
InterProⁱ	View protein in InterPro IPR002068. A-crystallin/Hsp20_dom. IPR001436. Alpha-crystallin/HSP. IPR031107. HSP20. IPR008978. HSP20-like_chaperone.
PANTHERⁱ	PTHR11527. PTHR11527. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00011. HSP20. 1 hit.
PRINTSⁱ	PR00299. ACRYSTALLIN.
SUPFAMⁱ	SSF49764. SSF49764. 1 hit.
PROSITEⁱ	View protein in PROSITE PS01031. SHSP. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

Q3T149-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MAERRVPFSL LRGPSWDPFR DWYPAHSRLF DQAFGLPRLP EEWSQWLSHS 
        60         70         80         90        100
GWPGYVRALP AAAIEGPAYN RALSRQLSSG VSEIQQTADR WRVSLDVNHF 
       110        120        130        140        150
APEELTVKTK DGVVEITGKH EERQDEHGYI SRCFTRKYTL PPGVDPTLVS 
       160        170        180        190        200
SSLSPEGTLT VEAPLPKSAT QSAEITIPVT FQARAQLGGP EAGKSEQPEN 

K

Length:201

Mass (Da):22,393

Last modified:October 11, 2005 - v1

Checksum:ⁱ9CEAFF050B7FAD24

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	BC102129 mRNA. Translation: AAI02130.1.
NCBI Reference Sequences More...RefSeqⁱ	XP_005225172.1. XM_005225115.1.
UniGeneⁱ	Bt.4415.

Genome annotation databases

GeneIDⁱ	516099.

GeneIDⁱ

516099.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	BC102129 mRNA. Translation: AAI02130.1.
NCBI Reference Sequences More...RefSeqⁱ	XP_005225172.1. XM_005225115.1.
UniGeneⁱ	Bt.4415.

3D structure databases

ProteinModelPortalⁱ	Q3T149.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	9913.ENSBTAP00000015883.

STRINGⁱ

9913.ENSBTAP00000015883.

PTM databases

iPTMnetⁱ	Q3T149.

iPTMnetⁱ

Q3T149.

Proteomic databases

PaxDbⁱ	Q3T149.
PeptideAtlas More...PeptideAtlasⁱ	Q3T149.
PRIDEⁱ	Q3T149.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

GeneIDⁱ	516099.

GeneIDⁱ

516099.

Organism-specific databases

CTDⁱ	3315.

CTDⁱ

3315.

Phylogenomic databases

eggNOGⁱ	KOG3591. Eukaryota. ENOG410YERS. LUCA.
HOGENOMⁱ	HOG000233955.
HOVERGENⁱ	HBG054766.
InParanoidⁱ	Q3T149.

Family and domain databases

Gene3Dⁱ	2.60.40.790. 1 hit.
InterProⁱ	View protein in InterPro IPR002068. A-crystallin/Hsp20_dom. IPR001436. Alpha-crystallin/HSP. IPR031107. HSP20. IPR008978. HSP20-like_chaperone.
PANTHERⁱ	PTHR11527. PTHR11527. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00011. HSP20. 1 hit.
PRINTSⁱ	PR00299. ACRYSTALLIN.
SUPFAMⁱ	SSF49764. SSF49764. 1 hit.
PROSITEⁱ	View protein in PROSITE PS01031. SHSP. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	HSPB1_BOVIN
Accessionⁱ	Q3T149Primary (citable) accession number: Q3T149
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
	Last sequence update:	October 11, 2005
	Last modified:	May 10, 2017
	This is version 76 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q3T149 (HSPB1_BOVIN)

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Heat shock protein beta-1

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ