HSPB2

HSPB2

Identifiers

HSPB2, HSP27, Hs.78846, LOH11CR1K, MKBP, heat shock protein family B (small) member 2

External IDs

OMIM: 602179; MGI: 1916503; GeneCards: HSPB2

Gene location (Human)

Chr.	Chromosome 11 (human)

Band	11q23.1	Start	111,912,734 bp
Band	11q23.1	End	111,914,093 bp

Gene location (Mouse)

Chr.	Chromosome 9 (mouse)

Band	9 A5.3\|9 27.75 cM	Start	50,662,378 bp
Band	9 A5.3\|9 27.75 cM	End	50,663,654 bp

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

right auricle of heart

apex of heart

muscle of thigh

left ventricle

gastrocnemius muscle

Descending thoracic aorta

ascending aorta

popliteal artery

tibial arteries

gastric mucosa

Top expressed in

interventricular septum

extraocular muscle

plantaris muscle

cardiac muscle tissue of left ventricle

extensor digitorum longus muscle

right ventricle

muscle of thigh

soleus muscle

temporal muscle

ankle

More reference expression data


More reference expression data

Gene ontology
Molecular function	enzyme activator activity protein binding
Cellular component	cytoplasm cytosol nucleus
Biological process	response to unfolded protein positive regulation of catalytic activity
Sources:Amigo / QuickGO

Databases

NCBI: entry; OMA: entry

Species

Human

Mouse


3316


69253


ENSG00000170276


ENSMUSG00000038086


Q16082


Q99PR8

RefSeq (mRNA)


NM_001541


NM_001164708 NM_024441

RefSeq (protein)


NP_001532


NP_001158180.1 NP_077761.3

Location (UCSC)

Chr 11: 111.91 – 111.91 Mb

Chr 9: 50.66 – 50.66 Mb

PubMed search

View/Edit Human

View/Edit Mouse

Heat shock protein beta-2 is a protein that in humans is encoded by the HSPB2 gene.

Interactions

HSPB2 has been shown to interact with:

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000170276 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000038086 – 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.

Further reading

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. Bibcode:2003FEBSL.546..307W. 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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