HSPA14

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; OMA:HSPA14 - orthologs
Gene location (Human) Chr. Chromosome 10 (human) Band 10p13 Start 14,838,306 bp End 14,871,741 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2|2 A1 Start 3,489,887 bp End 3,513,851 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in secondary oocyte middle temporal gyrus right testis rectum deltoid muscle left testis gastrocnemius muscle mucosa of sigmoid colon vastus lateralis muscle Skeletal muscle tissue of biceps brachii Top expressed in primitive streak epiblast otic placode abdominal wall otic vesicle yolk sac dermis morula morula embryo More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleotide binding protein binding ATP binding ATPase activity heat shock protein binding protein folding chaperone activity 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 Unfolded Protein Response protein refolding chaperone cofactor-dependent protein refolding Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 51182 50497 Ensembl ENSG00000187522 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) Chr 10: 14.84 – 14.87 Mb Chr 2: 3.49 – 3.51 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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.

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. S2CID 18200460.
• 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.
• 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.

External links

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