Species	Reference gene ID	Possible function	Papers / DOI
Arabidopsis	At3g12580	In cooperation with other chaperones, Hsp70s are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions (Probable).	Comprehensive expression profile analysis of the Arabidopsis Hsp70 gene family.; 2001; DOI: 10.1104/pp.126.2.789; PMID: 11402207; https://pubmed.ncbi.nlm.nih.gov/11402207/ | Heat shock protein cognate 70-4 and an E3 ubiquitin ligase, CHIP, mediate plastid-destined precursor degradation through the ubiquitin-26S proteasome system in Arabidopsis.; 2009; DOI: 10.1105/tpc.109.071548; PMID: 20028838; https://pubmed.ncbi.nlm.nih.gov/20028838/
Arabidopsis	At5g02500	In cooperation with other chaperones, Hsp70s are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions (Probable).	Physiological and molecular assessment of altered expression of Hsc70-1 in Arabidopsis. Evidence for pleiotropic consequences.; 2003; DOI: 10.1104/pp.102.019398; PMID: 12805626; https://pubmed.ncbi.nlm.nih.gov/12805626/ | Interaction between SGT1 and cytosolic/nuclear HSC70 chaperones regulates Arabidopsis immune responses.; 2007; DOI: 10.1105/tpc.107.051896; PMID: 18065690; https://pubmed.ncbi.nlm.nih.gov/18065690/ | WPP-domain proteins mimic the activity of the HSC70-1 chaperone in preventing mistargeting of RanGAP1-anchoring protein WIT1.; 2009; DOI: 10.1104/pp.109.143404; PMID: 19617588; https://pubmed.ncbi.nlm.nih.gov/19617588/ | The cytosolic/nuclear HSC70 and HSP90 molecular chaperones are important for stomatal closure and modulate abscisic acid-dependent physiological responses in Arabidopsis.; 2011; DOI: 10.1104/pp.111.174425; PMID: 21586649; https://pubmed.ncbi.nlm.nih.gov/21586649/