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HSPA2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3I33, 4FSV, 5FPM, 5FPN, 5FPD, 5FPE
Identifiers
Aliases	HSPA2, HSP70-2, HSP70-3, heat shock protein family A (Hsp70) member 2
External IDs	OMIM: 140560; MGI: 96243; HomoloGene: 68564; GeneCards: HSPA2; OMA:HSPA2 - orthologs
Gene location (Human) Chr. Chromosome 14 (human) Band 14q23.3 Start 64,535,905 bp End 64,546,173 bp
Gene location (Mouse) Chr. Chromosome 12 (mouse) Band 12 C3|12 33.73 cM Start 76,450,950 bp End 76,453,712 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in inferior ganglion of vagus nerve middle frontal gyrus subthalamic nucleus external globus pallidus Medulla Oblongata pars reticulata internal globus pallidus superior vestibular nucleus Skeletal muscle tissue of rectus abdominis corpus callosum Top expressed in seminiferous tubule spermatocyte spermatid ascending aorta aortic valve dentate gyrus of hippocampal formation granule cell piriform cortex hippocampus proper supraoptic nucleus olfactory epithelium More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleotide binding unfolded protein binding protein binding enzyme binding ATP binding disordered domain specific binding glycolipid binding ATPase activity heat shock protein binding protein folding chaperone activity tau protein binding chaperone binding misfolded protein binding Cellular component cytoplasm cytosol blood microparticle membrane spindle extracellular exosome cytoskeleton nucleus synaptonemal complex male germ cell nucleus mitochondrion cell surface CatSper complex myelin sheath meiotic spindle plasma membrane Biological process cell differentiation negative regulation of inclusion body assembly response to heat response to unfolded protein protein refolding spermatogenesis response to cold positive regulation of protein phosphorylation male meiotic nuclear division male meiosis I spermatid development positive regulation of ATP-dependent activity synaptonemal complex disassembly positive regulation of ATPase-coupled calcium transmembrane transporter activity positive regulation of G2/M transition of mitotic cell cycle vesicle-mediated transport cellular response to heat Unfolded Protein Response chaperone cofactor-dependent protein refolding Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3306 15512 Ensembl ENSG00000126803 ENSMUSG00000059970 UniProt P54652 P17156 RefSeq (mRNA) NM_021979 NM_001387931 NM_001002012 NM_008301 RefSeq (protein) NP_068814 NP_001002012 NP_032327 Location (UCSC) Chr 14: 64.54 – 64.55 Mb Chr 12: 76.45 – 76.45 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Heat shock-related 70 kDa protein 2 is a protein that in humans is encoded by the HSPA2 gene.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000126803 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000059970 – Ensembl, 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. "Entrez Gene: HSPA2 heat shock 70kDa protein 2".

Further reading

• Schwab CG, Bozak CK, Whitehouse NL, Olson VM (1993). "Amino acid limitation and flow to the duodenum at four stages of lactation. 2. Extent of lysine limitation". J. Dairy Sci. 75 (12): 3503–18. doi:10.3168/jds.S0022-0302(92)78126-0. PMID 1474216.
• Dworniczak B, Mirault ME (1987). "Structure and expression of a human gene coding for a 71 kd heat shock 'cognate' protein". Nucleic Acids Res. 15 (13): 5181–97. doi:10.1093/nar/15.13.5181. PMC 305955. PMID 3037489.
• Bonnycastle LL, Yu CE, Hunt CR, et al. (1995). "Cloning, sequencing, and mapping of the human chromosome 14 heat shock protein gene (HSPA2)". Genomics. 23 (1): 85–93. doi:10.1006/geno.1994.1462. PMID 7829106.
• Roux AF, Nguyen VT, Squire JA, Cox DW (1995). "A heat shock gene at 14q22: mapping and expression". Hum. Mol. Genet. 3 (10): 1819–22. doi:10.1093/hmg/3.10.1819. PMID 7849706.
• Furlini G, Vignoli M, Re MC, et al. (1994). "Human immunodeficiency virus type 1 interaction with the membrane of CD4+ cells induces the synthesis and nuclear translocation of 70K heat shock protein". J. Gen. Virol. 75 (1): 193–9. doi:10.1099/0022-1317-75-1-193. PMID 7906708.
• Allen JW, Dix DJ, Collins BW, et al. (1996). "HSP70-2 is part of the synaptonemal complex in mouse and hamster spermatocytes". Chromosoma. 104 (6): 414–21. doi:10.1007/BF00352265. PMID 8601336. S2CID 7244472.
• Dix DJ, Allen JW, Collins BW, et al. (1996). "Targeted gene disruption of Hsp70-2 results in failed meiosis, germ cell apoptosis, and male infertility". Proc. Natl. Acad. Sci. U.S.A. 93 (8): 3264–8. Bibcode:1996PNAS...93.3264D. doi:10.1073/pnas.93.8.3264. PMC 39594. PMID 8622925.
• Zhu D, Dix DJ, Eddy EM (1997). "HSP70-2 is required for CDC2 kinase activity in meiosis I of mouse spermatocytes". Development. 124 (15): 3007–14. doi:10.1242/dev.124.15.3007. PMID 9247342.
• O'Keeffe B, Fong Y, Chen D, et al. (2000). "Requirement for a kinase-specific chaperone pathway in the production of a Cdk9/cyclin T1 heterodimer responsible for P-TEFb-mediated tat stimulation of HIV-1 transcription". J. Biol. Chem. 275 (1): 279–87. doi:10.1074/jbc.275.1.279. PMID 10617616.
• Agostini I, Popov S, Li J, et al. (2000). "Heat-shock protein 70 can replace viral protein R of HIV-1 during nuclear import of the viral preintegration complex". Exp. Cell Res. 259 (2): 398–403. doi:10.1006/excr.2000.4992. PMID 10964507.
• Andersen JS, Lyon CE, Fox AH, et al. (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. Bibcode:2002CBio...12....1A. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
• Gurer C, Cimarelli A, Luban J (2002). "Specific incorporation of heat shock protein 70 family members into primate lentiviral virions". J. Virol. 76 (9): 4666–70. doi:10.1128/JVI.76.9.4666-4670.2002. PMC 155079. PMID 11932435.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Shin BK, Wang H, Yim AM, et al. (2003). "Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function". J. Biol. Chem. 278 (9): 7607–16. doi:10.1074/jbc.M210455200. PMID 12493773.
• Lim MC, Brooke SM, Sapolsky RM (2003). "gp120 neurotoxicity fails to induce heat shock defenses, while the over expression of hsp70 protects against gp120". Brain Res. Bull. 61 (2): 183–8. doi:10.1016/S0361-9230(03)00113-8. PMID 12832005. S2CID 35451084.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.
• Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197. S2CID 27764390.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

External links

• HSPA2+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

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