HSPA14

Heat shock 70 kDa protein 14 also known as HSP70-like protein 1 or heat shock protein HSP60 is a protein that in humans is encoded by the HSPA14 gene.[4][5]

For GroEL/60 kDa heat shock protein with the same symbol, see GroEL.

HSPA14
Identifiers
Aliases	HSPA14, HSP70-4, HSP70L1, heat shock protein family A (Hsp70) member 14
External IDs	OMIM: 610369 MGI: 1354164 HomoloGene: 74307 GeneCards: HSPA14
Gene location (Mouse) Chr. Chromosome 2 (mouse)[1] Band 2|2 A1 Start 3,488,850 bp[1] End 3,512,814 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • nucleotide binding • GO:0001948 protein binding • ATP binding • ATPase activity • heat shock protein binding • protein binding involved in protein folding • unfolded protein binding • misfolded protein binding Cellular component • cytoplasm • cytosol • ribosome • membrane • polysome Biological process • 'de novo' cotranslational protein folding • cytoplasmic translation • regulation of translational fidelity • response to unfolded protein • cellular response to heat • cellular response to unfolded protein • protein refolding • chaperone mediated protein folding requiring cofactor Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	51182	50497
Ensembl	n/a	ENSMUSG00000109865
UniProt	Q0VDF9 Q8TAQ0	Q99M31
RefSeq (mRNA)	NM_001037538 NM_001278205 NM_016299	NM_001037542 NM_015765 NM_001355397
RefSeq (protein)	NP_057383 NP_001265134.1	NP_056580 NP_001342326
Location (UCSC)	n/a	Chr 2: 3.49 – 3.51 Mb
PubMed search	[2]	[3]
Wikidata
View/Edit Human View/Edit Mouse

References

1. GRCm38: Ensembl release 89: ENSMUSG00000109865 - 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.
4. Wan T, Zhou X, Chen G, An H, Chen T, Zhang W, Liu S, Jiang Y, Yang F, Wu Y, Cao X (March 2004). "Novel heat shock protein Hsp70L1 activates dendritic cells and acts as a Th1 polarizing adjuvant". Blood. 103 (5): 1747–54. doi:10.1182/blood-2003-08-2828. PMID 14592822.
5. "Entrez Gene: HSPA14 heat shock 70kDa protein 14".

Further reading

• 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" (PDF). J. Gen. Virol. 75 (1): 193–9. doi:10.1099/0022-1317-75-1-193. PMID 7906708.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Scheufler C, Brinker A, Bourenkov G, et al. (2000). "Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine". Cell. 101 (2): 199–210. doi:10.1016/S0092-8674(00)80830-2. PMID 10786835.
• 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.
• 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.

External links

• HSPA14+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)