HSPA2

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
Gene location (Human)
Chr.	Chromosome 14 (human)[1]
End	64,546,173 bp[1]
Gene location (Mouse)
Chr.	Chromosome 12 (mouse)[2]
End	76,406,938 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• nucleotide binding; • unfolded protein binding; • GO:0001948 protein binding; • enzyme binding; • ATP binding; • disordered domain specific binding; • glycolipid binding; • ATPase activity; • heat shock protein binding; • protein binding involved in protein folding; • tau protein binding; • chaperone binding; • misfolded protein binding;
Cellular component	• cytoplasm; • cytosol; • blood microparticle; • membrane; • spindle; • extracellular exosome; • cytoskeleton; • cell nucleus; • synaptonemal complex; • male germ cell nucleus; • mitochondrion; • cell surface; • CatSper complex; • myelin; • meiotic spindle; • cell 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 ATPase activity; • synaptonemal complex disassembly; • positive regulation of calcium-transporting ATPase activity; • positive regulation of G2/M transition of mitotic cell cycle; • vesicle-mediated transport; • cellular response to heat; • cellular response to unfolded protein; • chaperone mediated protein folding requiring cofactor;
	Sources:Amigo / QuickGO
Orthologs
	3306
	15512
	ENSG00000126803
	ENSMUSG00000059970
	P54652
	P17156
	NM_021979
	NM_001002012; NM_008301
	NP_068814
	NP_001002012; NP_032327
	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.[5]

References

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

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.
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. 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. 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. 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. 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.
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.
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.
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. doi:10.1038/nature04209. PMID 16189514.

External links

HSPA2+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)

This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000126803 - Ensembl, May 2017

[refGRCm38Ensembl-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.

[entrez-5] "Entrez Gene: HSPA2 heat shock 70kDa protein 2".

HSPA2

References

Further reading

External links