HSPB1 Gene

HGNC Family	Heat shock proteins
Name	heat shock 27kDa protein 1
Description	This gene encodes a member of the small heat shock protein (HSP20) family of proteins. In response to environmental stress, the encoded protein translocates from the cytoplasm to the nucleus and functions as a molecular chaperone that promotes the correct folding of other proteins. This protein plays an important role in the differentiation of a wide variety of cell types. Expression of this gene is correlated with poor clinical outcome in multiple human cancers, and the encoded protein may promote cancer cell proliferation and metastasis, while protecting cancer cells from apoptosis. Mutations in this gene have been identified in human patients with Charcot-Marie-Tooth disease and distal hereditary motor neuropathy. [provided by RefSeq, Aug 2017]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n HSPB1 (also known as Hsp27) is a multifunctional small heat shock protein that plays a central role in cellular stress responses, survival, and disease. Mutations in HSPB1 have been linked to neurodegenerative conditions such as Charcot–Marie–Tooth disease, where they disrupt neurofilament assembly and compromise cell viability."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " HSPB1 functions as a molecular chaperone that limits the aggregation of damaged proteins and modulates apoptotic signaling by interfering with caspase activation, thereby promoting resistance to a wide range of cytotoxic insults."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": " Its anti‐apoptotic activity is further evidenced by its ability to enhance the proteasomal degradation of ubiquitinated proteins, which facilitates activation of survival pathways such as NF‑κB."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n In cancer cells, stress‐inducing agents (e.g., erastin) elevate HSPB1 expression in an HSF1‐dependent manner, and its phosphorylation—mediated by kinases such as protein kinase C, p38 MAPK/MAPKAPK2, and Akt—is critical for its cytoprotective functions. Phosphorylated HSPB1 reduces the accumulation of lipid reactive oxygen species, thereby acting as a negative regulator of ferroptosis and diminishing the anticancer efficacy of ferroptosis inducers."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": " In addition, HSPB1 phosphorylation downstream of ATM enhances its binding to key metabolic enzymes such as G6PD, contributing to an efficient antioxidant response"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": ", while in neutrophils, Akt‐mediated phosphorylation of HSPB1 modulates its association with Akt to affect cell survival."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n In oncogenic settings, elevated HSPB1 levels have been associated with aggressive phenotypes. For instance, increased expression in HER‑2/neu–positive breast tumors suggests a role in promoting tumor progression."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": " In prostate cancer, androgen‐induced HSPB1 phosphorylation displaces Hsp90 from the androgen receptor (AR), thereby enhancing AR nuclear translocation, stability, and transcriptional activity; this feed‑forward loop supports cell survival and may drive endocrine resistance."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "9"}]}, {"type": "t", "text": " Moreover, HSPB1 contributes to epithelial–mesenchymal transition by facilitating IL‑6–dependent STAT3/Twist signaling, which underlies increased cell motility and metastatic capacity."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "10"}]}, {"type": "t", "text": "\n "}]}, {"type": "t", "text": "\n \n "}, {"type": "p", "children": [{"type": "t", "text": "\n Beyond its roles in apoptosis and cancer progression, HSPB1 regulates cytoskeletal dynamics and mitochondrial quality control. Its phosphorylation in cardiomyocytes is implicated in the reorganization of actin filaments and regulation of cell contractility"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "11"}]}, {"type": "t", "text": ", and in endothelial cells, HSPB1 is phosphorylated downstream of HMGB1–RAGE signaling to modulate the actin network and vascular permeability."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "12"}]}, {"type": "t", "text": " Collectively, these activities underscore the capacity of HSPB1 to fine‑tune critical signaling networks that govern cell survival, stress adaptation, and disease progression.\n "}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Shoshana Shendelman, Alan Jonason, Cecile Martinat, et al. "}, {"type": "b", "children": [{"type": "t", "text": "DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS Biol (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pbio.0020362"}], "href": "https://doi.org/10.1371/journal.pbio.0020362"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15502874"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15502874"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "C G Concannon, A M Gorman, A Samali "}, {"type": "b", "children": [{"type": "t", "text": "On the role of Hsp27 in regulating apoptosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Apoptosis (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1023/a:1021601103096"}], "href": "https://doi.org/10.1023/a:1021601103096"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12510153"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12510153"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Arnaud Parcellier, Elise Schmitt, Sandeep Gurbuxani, et al. "}, {"type": "b", "children": [{"type": "t", "text": "HSP27 is a ubiquitin-binding protein involved in I-kappaBalpha proteasomal degradation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.23.16.5790-5802.2003"}], "href": "https://doi.org/10.1128/MCB.23.16.5790-5802.2003"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12897149"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12897149"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Ju-Tao Feng, Yin-Kun Liu, Hai-Yan Song, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Heat-shock protein 27: a potential biomarker for hepatocellular carcinoma identified by serum proteome analysis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proteomics (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/pmic.200401309"}], "href": "https://doi.org/10.1002/pmic.200401309"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16240287"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16240287"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "X Sun, Z Ou, M Xie, et al. "}, {"type": "b", "children": [{"type": "t", "text": "HSPB1 as a novel regulator of ferroptotic cancer cell death."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/onc.2015.32"}], "href": "https://doi.org/10.1038/onc.2015.32"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25728673"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25728673"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Claudia Cosentino, Domenico Grieco, Vincenzo Costanzo "}, {"type": "b", "children": [{"type": "t", "text": "ATM activates the pentose phosphate pathway promoting anti-oxidant defence and DNA repair."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "EMBO J (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/emboj.2010.330"}], "href": "https://doi.org/10.1038/emboj.2010.330"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21157431"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21157431"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Madhavi J Rane, Yong Pan, Saurabh Singh, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Heat shock protein 27 controls apoptosis by regulating Akt activation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M303417200"}], "href": "https://doi.org/10.1074/jbc.M303417200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12740362"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12740362"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "DaoHai Zhang, Lee Kian Tai, Lee Lee Wong, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Proteomic study reveals that proteins involved in metabolic and detoxification pathways are highly expressed in HER-2/neu-positive breast cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Proteomics (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/mcp.M400221-MCP200"}], "href": "https://doi.org/10.1074/mcp.M400221-MCP200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16048908"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16048908"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Amina Zoubeidi, Anousheh Zardan, Eliana Beraldi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cooperative interactions between androgen receptor (AR) and heat-shock protein 27 facilitate AR transcriptional activity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Res (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1158/0008-5472.CAN-07-2057"}], "href": "https://doi.org/10.1158/0008-5472.CAN-07-2057"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17974989"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17974989"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Masaki Shiota, Jennifer L Bishop, Ka Mun Nip, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Hsp27 regulates epithelial mesenchymal transition, metastasis, and circulating tumor cells in prostate cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Res (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1158/0008-5472.CAN-12-3979"}], "href": "https://doi.org/10.1158/0008-5472.CAN-12-3979"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23492367"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23492367"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Jasper J Saris, Peter A C 't Hoen, Ingrid M Garrelds, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Prorenin induces intracellular signaling in cardiomyocytes independently of angiotensin II."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hypertension (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1161/01.HYP.0000240064.19301.1b"}], "href": "https://doi.org/10.1161/01.HYP.0000240064.19301.1b"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16940215"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16940215"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Rachel K Wolfson, Eddie T Chiang, Joe G N Garcia "}, {"type": "b", "children": [{"type": "t", "text": "HMGB1 induces human lung endothelial cell cytoskeletal rearrangement and barrier disruption."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Microvasc Res (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.mvr.2010.11.010"}], "href": "https://doi.org/10.1016/j.mvr.2010.11.010"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21146549"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21146549"}]}]}]}
Synonyms	HSP25, HSP27, CMT2F, HEL-S-102, HMN2B, HS.76067, HSP28, SRP27
Proteins	HSPB1_HUMAN
NCBI Gene ID	3315
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

HSPB1 has 23,819 functional associations with biological entities spanning 8 categories (molecular profile, organism, functional term, phrase or reference, chemical, disease, phenotype or trait, structural feature, cell line, cell type or tissue, gene, protein or microRNA) extracted from 146 datasets.

Click the + buttons to view associations for HSPB1 from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

HSPB1 Gene

Functional Associations

Please acknowledge the Harmonizome in your publications by citing the following reference(s):

	Dataset	Summary
	Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of HSPB1 gene relative to other tissues from the Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles dataset.
	Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles	tissues with high or low expression of HSPB1 gene relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.
	Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles	tissue samples with high or low expression of HSPB1 gene relative to other tissue samples from the Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles dataset.
	Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by Microarray	tissue samples with high or low expression of HSPB1 gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by Microarray dataset.
	Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq	tissue samples with high or low expression of HSPB1 gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq dataset.
	Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of HSPB1 gene relative to other tissues from the Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles dataset.
	Biocarta Pathways	pathways involving HSPB1 protein from the Biocarta Pathways dataset.
	BioGPS Cell Line Gene Expression Profiles	cell lines with high or low expression of HSPB1 gene relative to other cell lines from the BioGPS Cell Line Gene Expression Profiles dataset.
	BioGPS Human Cell Type and Tissue Gene Expression Profiles	cell types and tissues with high or low expression of HSPB1 gene relative to other cell types and tissues from the BioGPS Human Cell Type and Tissue Gene Expression Profiles dataset.
	BioGPS Mouse Cell Type and Tissue Gene Expression Profiles	cell types and tissues with high or low expression of HSPB1 gene relative to other cell types and tissues from the BioGPS Mouse Cell Type and Tissue Gene Expression Profiles dataset.
	Carcinogenome Chemical Perturbation Carcinogenicity Signatures	small molecule perturbations changing expression of HSPB1 gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of HSPB1 gene relative to other cell lines from the CCLE Cell Line Gene CNV Profiles dataset.
	CCLE Cell Line Gene Mutation Profiles	cell lines with HSPB1 gene mutations from the CCLE Cell Line Gene Mutation Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with HSPB1 protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with HSPB1 gene from the CellMarker Gene-Cell Type Associations dataset.
	ChEA Transcription Factor Binding Site Profiles	transcription factor binding site profiles with transcription factor binding evidence at the promoter of HSPB1 gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of HSPB1 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets dataset.
	ChEA Transcription Factor Targets 2022	transcription factors binding the promoter of HSPB1 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset.
	ClinVar Gene-Phenotype Associations	phenotypes associated with HSPB1 gene from the curated ClinVar Gene-Phenotype Associations dataset.
	ClinVar Gene-Phenotype Associations 2025	phenotypes associated with HSPB1 gene from the curated ClinVar Gene-Phenotype Associations 2025 dataset.
	CM4AI U2OS Cell Map Protein Localization Assemblies	assemblies containing HSPB1 protein from integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.
	CMAP Signatures of Differentially Expressed Genes for Small Molecules	small molecule perturbations changing expression of HSPB1 gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing HSPB1 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing HSPB1 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores	cellular components containing HSPB1 protein in low- or high-throughput protein localization assays from the COMPARTMENTS Experimental Protein Localization Evidence Scores dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores 2025	cellular components containing HSPB1 protein in low- or high-throughput protein localization assays from the COMPARTMENTS Experimental Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores	cellular components co-occuring with HSPB1 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025	cellular components co-occuring with HSPB1 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.
	CORUM Protein Complexes	protein complexs containing HSPB1 protein from the CORUM Protein Complexes dataset.
	COSMIC Cell Line Gene CNV Profiles	cell lines with high or low copy number of HSPB1 gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with HSPB1 gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with HSPB1 gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with HSPB1 gene/protein from the curated CTD Gene-Disease Associations dataset.
	DeepCoverMOA Drug Mechanisms of Action	small molecule perturbations with high or low expression of HSPB1 protein relative to other small molecule perturbations from the DeepCoverMOA Drug Mechanisms of Action dataset.
	DepMap CRISPR Gene Dependency	cell lines with fitness changed by HSPB1 gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DEPOD Substrates of Phosphatases	phosphatases that dephosphorylate HSPB1 protein from the curated DEPOD Substrates of Phosphatases dataset.
	DISEASES Curated Gene-Disease Association Evidence Scores	diseases involving HSPB1 gene from the DISEASES Curated Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Curated Gene-Disease Association Evidence Scores 2025	diseases involving HSPB1 gene from the DISEASES Curated Gene-Disease Association Evidence Scores 2025 dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with HSPB1 gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores 2025	diseases co-occuring with HSPB1 gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.