# HSPB6

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{{Short description|Protein-coding gene in the species Homo sapiens}}
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'''Heat shock protein beta-6''' (HSPB6) is a [protein](/source/protein) that in humans is encoded by the ''HSPB6'' [gene](/source/gene).<ref name="pmid12820654">{{cite journal |vauthors=Kappe G, Franck E, Verschuure P, Boelens WC, Leunissen JA, de Jong WW | title = The human genome encodes 10 alpha-crystallin-related small heat shock proteins: HspB1-10 | journal = Cell Stress & Chaperones | volume = 8 | issue = 1 | pages = 53–61 |date=Jun 2003 | doi = 10.1379/1466-1268(2003)8<53:thgecs>2.0.co;2 | doi-broken-date = 12 July 2025 | pmid = 12820654 | pmc = 514853 }}</ref><ref name="pmid14717697">{{cite journal |vauthors=Bukach OV, Seit-Nebi AS, Marston SB, Gusev NB | title = Some properties of human small heat shock protein Hsp20 (HspB6) | journal = Eur J Biochem | volume = 271 | issue = 2 | pages = 291–302 |date=Jan 2004 | pmid = 14717697 | doi =10.1046/j.1432-1033.2003.03928.x  | doi-access =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: HSPB6 heat shock protein, alpha-crystallin-related, B6| url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=126393}}</ref>

HSPB6 is a 17-kDa member of the [heat shock](/source/heat_shock_protein) family of proteins. HSPB6 was first identified in 1994 when it was isolated from rat and human skeletal muscle as a complex with [HSPB1](/source/HSPB1) (also known as [HSP27](/source/HSP27)) and [HSPB5](/source/HSPB5) (also known as αB-crystallin).<ref name="pmid8195168">{{cite journal |vauthors=Kato K, Goto S, Inaguma Y, Hasegawa K, Morishita R, Asano T | title = Purification and characterization of a 20-kDa protein that is highly homologous to alpha B crystallin | journal = J. Biol. Chem. | volume = 269 | issue = 21 | pages = 15302–9 |date=May 1994 | doi = 10.1016/S0021-9258(17)36606-1 | pmid = 8195168 | doi-access = free }}</ref>

HSPB6 is expressed in multiple tissues; however, HSPB6 is most highly and constitutively expressed in vascular, airway, colonic, bladder, uterine smooth muscle, cardiac muscle and skeletal muscle. HSPB6 has specific functions for [vasodilation](/source/vasodilation), platelet function, and [insulin resistance](/source/insulin_resistance)<ref name="PMC2866971">{{cite journal |vauthors=Dreiza CM, Komalavilas P, Furnish EJ, Flynn CR, Sheller MR, Smoke CC, Lopes LB, Brophy CM | title = The small heat shock protein, HSPB6, in muscle function and disease | journal = Cell Stress & Chaperones | volume = 15 | issue = 1 | pages = 1–11 |date=Jan 2010 | pmid =  19568960| pmc = 2866971  | doi =10.1007/s12192-009-0127-8  }}</ref> and in smooth and cardiac muscle.<ref name="pmid18579210">{{cite journal |vauthors=Salinthone S, Tyagi M, Gerthoffer WT | title = Small heat shock proteins in smooth muscle | journal = Pharmacol. Ther. | volume = 119 | issue = 1 | pages = 44–54 |date=July 2008 | pmid = 18579210 | pmc = 2581864 | doi = 10.1016/j.pharmthera.2008.04.005 }}</ref><ref name="pmid16099377">{{cite journal |vauthors=Fan GC, Chu G, Kranias EG | title = Hsp20 and its cardioprotection | journal = Trends Cardiovasc. Med. | volume = 15 | issue = 4 | pages = 138–41 |date=May 2005 | pmid = 16099377 | doi = 10.1016/j.tcm.2005.05.004 }}</ref>

==References==
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==Further reading==
{{refbegin | 2}}
*{{cite journal  |vauthors=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317–20 |year= 1992 |pmid= 1602151 |doi=10.1016/S0163-4453(05)80037-4  }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |bibcode=2002PNAS...9916899M |doi-access=free }}
*{{cite journal   |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |doi-access= free }}
*{{cite journal   |vauthors=Grimwood J, Gordon LA, Olsen A, etal |title=The DNA sequence and biology of human chromosome 19. |journal=Nature |volume=428 |issue= 6982 |pages= 529–35 |year= 2004 |pmid= 15057824 |doi= 10.1038/nature02399 |bibcode=2004Natur.428..529G |doi-access= free }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 }}
*{{cite journal  |vauthors=Fontaine JM, Sun X, Benndorf R, Welsh MJ |title=Interactions of HSP22 (HSPB8) with HSP20, alphaB-crystallin, and HSPB3. |journal=Biochem. Biophys. Res. Commun. |volume=337 |issue= 3 |pages= 1006–11 |year= 2005 |pmid= 16225851 |doi= 10.1016/j.bbrc.2005.09.148 |bibcode=2005BBRC..337.1006F }}
*{{cite journal   |vauthors=Flynn CR, Smoke CC, Furnish E, etal |title=Phosphorylation and activation of a transducible recombinant form of human HSP20 in Escherichia coli. |journal=Protein Expr. Purif. |volume=52 |issue= 1 |pages= 50–8 |year= 2007 |pmid= 17084643 |doi= 10.1016/j.pep.2006.08.015  | pmc=1839877 }}
*{{cite journal  |vauthors=Chernik IS, Seit-Nebi AS, Marston SB, Gusev NB |title=Small heat shock protein Hsp20 (HspB6) as a partner of 14-3-3gamma. |journal=Mol. Cell. Biochem. |volume=295 |issue= 1–2 |pages= 9–17 |year= 2007 |pmid= 17109079 |doi= 10.1007/s11010-006-9266-8 |s2cid=6389210 }}
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== External links ==
* {{PDBe-KB2|O14558|Heat shock protein beta-6}}

Category:Heat shock proteins

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Adapted from the Wikipedia article [HSPB6](https://en.wikipedia.org/wiki/HSPB6) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/HSPB6?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.