AliasesSERPINH1, AsTP3, CBP1, CBP2, HSP47, OI10, PIG14, PPROM, RA-A47, SERPINH2, gp46, serpin family H member 1
External IDsOMIM: 600943; MGI: 88283; HomoloGene: 20331; GeneCards: SERPINH1; OMA:SERPINH1 - orthologs
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC)Chr 11: 75.56 – 75.57 MbChr 7: 98.99 – 99 Mb
PubMed search[3][4]
View/Edit HumanView/Edit Mouse

Heat shock protein 47, also known as SERPINH1 is a serpin which serves as a human chaperone protein for collagen.[5][6]


This protein is a member of the serpin superfamily of serine proteinase inhibitors. Its expression is induced by heat shock. HSP47 is expressed in the endoplasmic reticulum. These cells synthesize and secrete type I and type II collagen. [7] The protein localizes to the endoplasmic reticulum lumen and binds collagen; thus it is thought to be a molecular chaperone involved in the maturation of collagen molecules. HSP47 is essential for the correct folding of procollagen. Antibodies directed to this protein have been found in patients with rheumatoid arthritis.[5]


HSP47 contains 3 beta sheets and 9 alpha helices. After binding with collagen no conformation change is observed.[8]


Heat shock protein 47 has been shown to interact with collagens I, II, III, IV and V.[9] It is involved in the secretion of collagen as well as the processing, assembly, and folding of collagen proteins. Hsp 47 binds specifically to procollagen and collagen only. The protein recognizes the triple helix of procollagen, two HSP47 proteins will bind to the leading and trailing strands of procollagen.[8]

Research on role in preventing deep vein thrombosis

Research published in 2023 indicates a potential role of HSP47 regarding deep vein thrombosis.[10] [11] This initial research will be followed by additional studies.

Role in Fibrosis

Fibrosis is the scarring of connective tissue, one attribute is the excess deposition of collagen in the extracellular matrix of tissue. Research has shown that HSPs have a role in fibrotic diseases.[12] HSP47 has been shown to be pro-fibrosis in various fibrotic diseases. During the process of fibrosis, HSP47 is expressed and is involved in the production of collagen.[13] HSP47 could be a potential therapeutic agent for fibrotic disease, a down-regulation of HSP47 leads to decreased fibrotic progression.[14]


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000149257Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000070436Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b "Entrez Gene: SERPINH1 serpin peptidase inhibitor, clade H (heat shock protein 47), member 1, (collagen binding protein 1)".
  6. ^ Dafforn TR, Della M, Miller AD (December 2001). "The molecular interactions of heat shock protein 47 (Hsp47) and their implications for collagen biosynthesis". The Journal of Biological Chemistry. 276 (52): 49310–9. doi:10.1074/jbc.M108896200. PMID 11592970.
  7. ^ Williams RS (21 March 2000). "Heat Shock Protein 47: A Chaperone for the Fibrous Cap?". Circulation. 101 (11): 1227–1228. doi:10.1161/01.CIR.101.11.1227. PMID 10725278. Retrieved 11 December 2017.
  8. ^ a b Widmer C, Gebauer J, Baumann U (2013-01-09). "Molecular basis for the action of the collagen-specific chaperone Hsp47 SERPINH1 and its structure-specific client recognition". Proceedings of the National Academy of Sciences of the United States of America. 109 (33): 13243–13247. doi:10.2210/pdb3zha/pdb. PMC 3421173. PMID 22847422. Retrieved 2023-11-26.
  9. ^ Mala JG, Rose C (November 2010). "Interactions of heat shock protein 47 with collagen and the stress response: an unconventional chaperone model?". Life Sciences. 87 (19–22): 579–86. doi:10.1016/j.lfs.2010.09.024. PMID 20888348.
  10. ^ Schattner, Mirta, Sleep like a bear, Science, April 13, 2023
  11. ^ Garcia de Jesús, Erin, Hibernating bears don’t get blood clots. Now scientists know why, Science News, April 13, 2023
  12. ^ Balasubramaniam B, Balamurugan K (2020), "Role of Heat Shock Factors in Diseases and Immunity", Heat Shock Proteins in Human Diseases, Cham: Springer International Publishing, pp. 197–210, doi:10.1007/7515_2020_21, ISBN 978-3-030-62288-6, S2CID 226465376, retrieved 2023-11-26
  13. ^ Kim HJ, Park JH, Shin JM, Yang HW, Lee HM, Park IH (2020-06-09). "Author Correction: TGF-β1-induced HSP47 regulates extracellular matrix accumulation via Smad2/3 signaling pathways in nasal fibroblasts". Scientific Reports. 10 (1): 9585. Bibcode:2020NatSR..10.9585K. doi:10.1038/s41598-020-66547-z. ISSN 2045-2322. PMC 7280506. PMID 32514115.
  14. ^ Sakamoto N, Okuno D, Tokito T, Yura H, Kido T, Ishimoto H, Tanaka Y, Mukae H (2023-08-25). "HSP47: A Therapeutic Target in Pulmonary Fibrosis". Biomedicines. 11 (9): 2387. doi:10.3390/biomedicines11092387. ISSN 2227-9059. PMC 10525413. PMID 37760828.

Further reading