HSPB2

HSPB2
Identifiers
Aliases	HSPB2 , HSP27, Hs.78846, LOH11CR1K, MKBP, heat shock protein family B (small) member 2
External IDs	OMIM: 602179 MGI: 1916503 HomoloGene: 68189 GeneCards: HSPB2
Gene location (Human)
Chr.	Chromosome 11 (human)
End	111,914,093 bp
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• GO:0010577 enzyme activator activity ; • GO:0001948 protein binding ;
Cellular component	• cytoplasm ; • cytosol ; • cell nucleus ;
Biological process	• response to unfolded protein ; • GO:0048554 positive regulation of catalytic activity ;
	Sources:Amigo / QuickGO
Orthologs
	3316
	69253
	ENSG00000170276
	ENSMUSG00000038086
	Q16082
	Q99PR8
	NM_001541
	NM_001164708 ; NM_024441
	NP_001532
	NP_001158180.1 ; NP_077761.3
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated December 31, 2020

Heat shock protein beta-2 is a protein that in humans is encoded by the HSPB2 gene.^[4]^[5]^[6]

Interactions

HSPB2 has been shown to interact with:

CRYAB,^[7]
HSPB8,^[8]^[9]
Myotonic dystrophy protein kinase ^[5]^[7] and
TRAF6.^[10]

Related Research Articles

Heat shock proteins (HSP) are a family of proteins that are produced by cells in response to exposure to stressful conditions. They were first described in relation to heat shock, but are now known to also be expressed during other stresses including exposure to cold, UV light and during wound healing or tissue remodeling. Many members of this group perform chaperone functions by stabilizing new proteins to ensure correct folding or by helping to refold proteins that were damaged by the cell stress. This increase in expression is transcriptionally regulated. The dramatic upregulation of the heat shock proteins is a key part of the heat shock response and is induced primarily by heat shock factor (HSF). HSPs are found in virtually all living organisms, from bacteria to humans.

Hsp90 Heat shock proteins with a molecular mass around 90kDa

Hsp90 is a chaperone protein that assists other proteins to fold properly, stabilizes proteins against heat stress, and aids in protein degradation. It also stabilizes a number of proteins required for tumor growth, which is why Hsp90 inhibitors are investigated as anti-cancer drugs.

Heat shock protein 27 (Hsp27) also known as heat shock protein beta-1 (HSPB1) is a protein that in humans is encoded by the HSPB1 gene.

BAG family molecular chaperone regulator 1 is a protein that in humans is encoded by the BAG1 gene.

MAP kinase-activated protein kinase 2 is an enzyme that in humans is encoded by the MAPKAPK2 gene.

Hsp90 co-chaperone Cdc37 is a protein that in humans is encoded by the CDC37 gene.

Cyclic AMP-dependent transcription factor ATF-1 is a protein that in humans is encoded by the ATF1 gene.

Alpha-crystallin B chain is a protein that in humans is encoded by the CRYAB gene. It is part of the small heat shock protein family and functions as molecular chaperone that primarily binds misfolded proteins to prevent protein aggregation, as well as inhibit apoptosis and contribute to intracellular architecture. Post-translational modifications decrease the ability to chaperone. Mutations in CRYAB cause different cardiomyopathies and skeletal myopathies. In addition, defects in this gene/protein have been associated with cancer and neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease.

Heat shock protein beta-8 is a protein that in humans is encoded by the HSPB8 gene.

Prostaglandin E synthase 3 (cytosolic) is an enzyme that in humans is encoded by the PTGES3 gene.

DnaJ homolog subfamily A member 3, mitochondrial, also known as Tumorous imaginal disc 1 (TID1), is a protein that in humans is encoded by the DNAJA3 gene on chromosome 16. This protein belongs to the DNAJ/Hsp40 protein family, which is known for binding and activating Hsp70 chaperone proteins to perform protein folding, degradation, and complex assembly. As a mitochondrial protein, it is involved in maintaining membrane potential and mitochondrial DNA (mtDNA) integrity, as well as cellular processes such as cell movement, growth, and death. Furthermore, it is associated with a broad range of diseases, including neurodegenerative diseases, inflammatory diseases, and cancers.

Scaffold attachment factor B, also known as SAFB, is a gene with homologs that have been studied in humans and mice.

DnaJ homolog subfamily B member 1 is a protein that in humans is encoded by the DNAJB1 gene.

MAP kinase-interacting serine/threonine-protein kinase 1 is an enzyme that in humans is encoded by the MKNK1 gene.

Heat shock factor protein 2 is a protein that in humans is encoded by the HSF2 gene.

Heat shock protein 75 kDa, mitochondrial is a protein that in humans is encoded by the TRAP1 gene.

MAP kinase-activated protein kinase 5 is an enzyme that in humans is encoded by the MAPKAPK5 gene. The protein encoded by this gene is a member of the serine/threonine kinase family. In response to cellular stress and proinflammatory cytokines, this kinase is activated through its phosphorylation by MAP kinases, including MAPK1/ERK, MAPK14/p38-alpha, and MAPK11/p38-beta. In vitro, this kinase phosphorylates heat shock protein HSP27 at its physiologically relevant sites. Two alternately-spliced transcript variants of this gene encoding distinct isoforms have been reported.

Heat shock protein beta-6 is a protein that in humans is encoded by the HSPB6 gene.

The heat shock protein Hsp20 family, also known as small heat shock proteins (sHSPs), is a family of heat shock proteins.

Heat shock protein beta-3 (HspB3) also known as heat shock 27kDa protein 3 is a protein that in humans is encoded by the HSPB3 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000170276 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Iwaki A, Nagano T, Nakagawa M, Iwaki T, Fukumaki Y (February 1998). "Identification and characterization of the gene encoding a new member of the alpha-crystallin/small hsp family, closely linked to the alphaB-crystallin gene in a head-to-head manner". Genomics. 45 (2): 386–94. doi:10.1006/geno.1997.4956. PMID 9344664.
1 2 Suzuki A, Sugiyama Y, Hayashi Y, Nyu-i N, Yoshida M, Nonaka I, Ishiura S, Arahata K, Ohno S (April 1998). "MKBP, a novel member of the small heat shock protein family, binds and activates the myotonic dystrophy protein kinase". J Cell Biol. 140 (5): 1113–24. doi:10.1083/jcb.140.5.1113. PMC 2132705 . PMID 9490724.
↑ "Entrez Gene: HSPB2 heat shock 27kDa protein 2".
1 2 Sugiyama Y, Suzuki A, Kishikawa M, Akutsu R, Hirose T, Waye MM, Tsui SK, Yoshida S, Ohno S (January 2000). "Muscle develops a specific form of small heat shock protein complex composed of MKBP/HSPB2 and HSPB3 during myogenic differentiation". J. Biol. Chem. 275 (2): 1095–104. doi: 10.1074/jbc.275.2.1095 . PMID 10625651.
↑ Sun X, Fontaine JM, Rest JS, Shelden EA, Welsh MJ, Benndorf R (January 2004). "Interaction of human HSP22 (HSPB8) with other small heat shock proteins". J. Biol. Chem. 279 (4): 2394–402. doi: 10.1074/jbc.M311324200 . PMID 14594798.
↑ Benndorf R, Sun X, Gilmont RR, Biederman KJ, Molloy MP, Goodmurphy CW, Cheng H, Andrews PC, Welsh MJ (July 2001). "HSP22, a new member of the small heat shock protein superfamily, interacts with mimic of phosphorylated HSP27 ((3D)HSP27)". J. Biol. Chem. 276 (29): 26753–61. doi: 10.1074/jbc.M103001200 . PMID 11342557.
↑ Wu Y, Liu J, Zhang Z, Huang H, Shen J, Zhang S, Jiang Y, Luo L, Yin Z (January 2009). "HSP27 regulates IL-1 stimulated IKK activation through interacting with TRAF6 and affecting its ubiquitination". Cell. Signal. 21 (1): 143–50. doi:10.1016/j.cellsig.2008.10.001. PMID 18950704.

Concannon CG, Gorman AM, Samali A (2003). "On the role of Hsp27 in regulating apoptosis". Apoptosis. 8 (1): 61–70. doi:10.1023/A:1021601103096. PMID 12510153. S2CID 18464958.
Elisei R, Weightman D, Kendall-Taylor P, Vassart G, Ludgate M (1993). "Muscle autoantigens in thyroid associated ophthalmopathy: the limits of molecular genetics". J. Endocrinol. Invest. 16 (7): 533–40. doi:10.1007/bf03348900. PMID 8227983. S2CID 23857370.
Deak M, Clifton AD, Lucocq LM, Alessi DR (1998). "Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB". EMBO J. 17 (15): 4426–41. doi:10.1093/emboj/17.15.4426. PMC 1170775 . PMID 9687510.
Sugiyama Y, Suzuki A, Kishikawa M, Akutsu R, Hirose T, Waye MM, Tsui SK, Yoshida S, Ohno S (2000). "Muscle develops a specific form of small heat shock protein complex composed of MKBP/HSPB2 and HSPB3 during myogenic differentiation". J. Biol. Chem. 275 (2): 1095–104. doi: 10.1074/jbc.275.2.1095 . PMID 10625651.
Baysal BE, Willett-Brozick JE, Taschner PE, Dauwerse JG, Devilee P, Devlin B (2001). "A high-resolution integrated map spanning the SDHD gene at 11q23: a 1.1-Mb BAC contig, a partial transcript map and 15 new repeat polymorphisms in a tumour-suppressor region". Eur. J. Hum. Genet. 9 (2): 121–9. doi: 10.1038/sj.ejhg.5200585 . PMID 11313745.
Nakagawa M, Tsujimoto N, Nakagawa H, Iwaki T, Fukumaki Y, Iwaki A (2001). "Association of HSPB2, a member of the small heat shock protein family, with mitochondria". Exp. Cell Res. 271 (1): 161–8. doi:10.1006/excr.2001.5362. PMID 11697892.
Ito H, Kamei K, Iwamoto I, Inaguma Y, García-Mata R, Sztul E, Kato K (2002). "Inhibition of proteasomes induces accumulation, phosphorylation, and recruitment of HSP27 and alphaB-crystallin to aggresomes". J. Biochem. 131 (4): 593–603. doi:10.1093/oxfordjournals.jbchem.a003139. PMID 11926998.
Boxman IL, Kempenaar J, de Haas E, Ponec M (2003). "Induction of HSP27 nuclear immunoreactivity during stress is modulated by vitamin C.". Exp. Dermatol. 11 (6): 509–17. doi:10.1034/j.1600-0625.2002.110603.x. PMID 12473058. S2CID 25384331.
Patel VM, Heinel LA, Provencio JJ, Vinall PE, Kramer MS, Rosenwasser RH (2003). "Validation of image analysis for enzyme histochemical and immunocytochemical staining". Biotechnic & Histochemistry. 77 (4): 213–21. doi:10.1080/714028196. PMID 12503731.
Mao H, Li F, Ruchalski K, Mosser DD, Schwartz JH, Wang Y, Borkan SC (2003). "hsp72 inhibits focal adhesion kinase degradation in ATP-depleted renal epithelial cells". J. Biol. Chem. 278 (20): 18214–20. doi: 10.1074/jbc.M300126200 . PMID 12611892.
Yonekura N, Yokota S, Yonekura K, Dehari H, Arata S, Kohama G, Fujii N (2003). "Interferon-gamma downregulates Hsp27 expression and suppresses the negative regulation of cell death in oral squamous cell carcinoma lines". Cell Death Differ. 10 (3): 313–22. doi: 10.1038/sj.cdd.4401169 . PMID 12700631.
Kantham L, Kerr-Bayles L, Godde N, Quick M, Webb R, Sunderland T, Bond J, Walder K, Augert G, Collier G (2003). "Beacon interacts with cdc2/cdc28-like kinases". Biochem. Biophys. Res. Commun. 304 (1): 125–9. doi:10.1016/S0006-291X(03)00549-7. PMID 12705895.
Yaglom J, O'Callaghan-Sunol C, Gabai V, Sherman MY (2003). "Inactivation of dual-specificity phosphatases is involved in the regulation of extracellular signal-regulated kinases by heat shock and hsp72". Mol. Cell. Biol. 23 (11): 3813–24. doi:10.1128/MCB.23.11.3813-3824.2003. PMC 155207 . PMID 12748284.
Park KJ, Gaynor RB, Kwak YT (2003). "Heat shock protein 27 association with the I kappa B kinase complex regulates tumor necrosis factor alpha-induced NF-kappa B activation". J. Biol. Chem. 278 (37): 35272–8. doi: 10.1074/jbc.M305095200 . PMID 12829720.
Wen FC, Li YH, Tsai HF, Lin CH, Li C, Liu CS, Lii CK, Nukina N, Hsieh M (2003). "Down-regulation of heat shock protein 27 in neuronal cells and non-neuronal cells expressing mutant ataxin-3". FEBS Lett. 546 (2–3): 307–14. doi: 10.1016/S0014-5793(03)00605-7 . PMID 12832059. S2CID 35025906.
Parcellier A, Schmitt E, Gurbuxani S, Seigneurin-Berny D, Pance A, Chantôme A, Plenchette S, Khochbin S, Solary E, Garrido C (2003). "HSP27 is a ubiquitin-binding protein involved in I-kappaBalpha proteasomal degradation". Mol. Cell. Biol. 23 (16): 5790–802. doi:10.1128/MCB.23.16.5790-5802.2003. PMC 166315 . PMID 12897149.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000170276 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9344664-4] Iwaki A, Nagano T, Nakagawa M, Iwaki T, Fukumaki Y (February 1998). "Identification and characterization of the gene encoding a new member of the alpha-crystallin/small hsp family, closely linked to the alphaB-crystallin gene in a head-to-head manner". Genomics. 45 (2): 386–94. doi:10.1006/geno.1997.4956. PMID 9344664.

[pmid9490724-5] 1 2 Suzuki A, Sugiyama Y, Hayashi Y, Nyu-i N, Yoshida M, Nonaka I, Ishiura S, Arahata K, Ohno S (April 1998). "MKBP, a novel member of the small heat shock protein family, binds and activates the myotonic dystrophy protein kinase". J Cell Biol. 140 (5): 1113–24. doi:10.1083/jcb.140.5.1113. PMC 2132705 . PMID 9490724.

[entrez-6] "Entrez Gene: HSPB2 heat shock 27kDa protein 2".

[pmid10625651-7] 1 2 Sugiyama Y, Suzuki A, Kishikawa M, Akutsu R, Hirose T, Waye MM, Tsui SK, Yoshida S, Ohno S (January 2000). "Muscle develops a specific form of small heat shock protein complex composed of MKBP/HSPB2 and HSPB3 during myogenic differentiation". J. Biol. Chem. 275 (2): 1095–104. doi: 10.1074/jbc.275.2.1095 . PMID 10625651.

[pmid14594798-8] Sun X, Fontaine JM, Rest JS, Shelden EA, Welsh MJ, Benndorf R (January 2004). "Interaction of human HSP22 (HSPB8) with other small heat shock proteins". J. Biol. Chem. 279 (4): 2394–402. doi: 10.1074/jbc.M311324200 . PMID 14594798.

[pmid11342557-9] Benndorf R, Sun X, Gilmont RR, Biederman KJ, Molloy MP, Goodmurphy CW, Cheng H, Andrews PC, Welsh MJ (July 2001). "HSP22, a new member of the small heat shock protein superfamily, interacts with mimic of phosphorylated HSP27 ((3D)HSP27)". J. Biol. Chem. 276 (29): 26753–61. doi: 10.1074/jbc.M103001200 . PMID 11342557.

[pmid18950704-10] Wu Y, Liu J, Zhang Z, Huang H, Shen J, Zhang S, Jiang Y, Luo L, Yin Z (January 2009). "HSP27 regulates IL-1 stimulated IKK activation through interacting with TRAF6 and affecting its ubiquitination". Cell. Signal. 21 (1): 143–50. doi:10.1016/j.cellsig.2008.10.001. PMID 18950704.

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HSPB2

Contents

Interactions

Related Research Articles

References

Further reading