query	query_gene_id	query_protein_id	source_reference	hit_rank	swissprot_acc	swissprot_entry	database_section	target_gene_id	description	organism	homolog_gene_name	percent_identity	alignment_length	query_coverage	evalue	bitscore	confidence	evidence_type	source_db	reference_gene_id	reference_function_zh	reference_function_en	reference_papers_json
LXL04_038062	gene-LXL04_038062	KAL4555443.1	OH-1004	1	O65719	HSP7C_ARATH	Swiss-Prot		Heat shock 70 kDa protein 3 OS=Arabidopsis thaliana OX=3702 GN=HSP70-3 PE=1 SV=1	Arabidopsis thaliana	HSP70-3	67.0	100	68.027	1.24e-38	140.0	moderate_database_homology	BLASTP to reviewed UniProt Swiss-Prot	UniProt Swiss-Prot current_release 2026-06-10	At3g09440	在其他分子伴侣的协作下，Hsp70s 是促进新合成蛋白折叠、协助前体蛋白转运到细胞器，并在应激条件下负责损伤蛋白降解的关键成分。	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.	[]
LXL04_038062	gene-LXL04_038062	KAL4555443.1	OH-1004	3	Q9LHA8	HS704_ARATH	Swiss-Prot		Heat shock 70 kDa protein 4 OS=Arabidopsis thaliana OX=3702 GN=HSP70-4 PE=1 SV=1	Arabidopsis thaliana	HSP70-4	66.0	100	68.027	1.53e-38	140.0	moderate_database_homology	BLASTP to reviewed UniProt Swiss-Prot	UniProt Swiss-Prot current_release 2026-06-10	At3g12580	与其他伴侣蛋白合作，Hsp70 是关键组分，可促进新合成蛋白的折叠，协助前体蛋白转运进入细胞器，并负责在应激条件下降解受损蛋白（可能）。	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).	"[{""pmid"":""11402207"",""title"":""Comprehensive expression profile analysis of the Arabidopsis Hsp70 gene family."",""doi"":""10.1104/pp.126.2.789"",""url"":""https://pubmed.ncbi.nlm.nih.gov/11402207/"",""year"":""2001"",""journal"":""Plant physiology"",""authors"":""Sung DY; Vierling E; Guy CL"",""matched_aliases"":[""HSP70""],""evidence"":""UniProt FUNCTION; UniProt/PubMed metadata and gene/species abstract checks; EuropePMC cross-check where available"",""metadata_sources"":[""UniProt"",""PubMed""],""fulltext_reviewed"":false},{""pmid"":""20028838"",""title"":""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."",""doi"":""10.1105/tpc.109.071548"",""url"":""https://pubmed.ncbi.nlm.nih.gov/20028838/"",""year"":""2009"",""journal"":""The Plant cell"",""authors"":""Lee S, Lee DW, Lee Y, Mayer U, Stierhof YD, Lee S, Jürgens G, Hwang I."",""matched_aliases"":[""HSC70-4""],""evidence"":""UniProt FUNCTION; UniProt/PubMed metadata and gene/species abstract checks; EuropePMC cross-check where available"",""metadata_sources"":[""UniProt"",""PubMed"",""EuropePMC""],""fulltext_reviewed"":false}]"
LXL04_038062	gene-LXL04_038062	KAL4555443.1	OH-1004	5	P22953	HS701_ARATH	Swiss-Prot		Heat shock 70 kDa protein 1 OS=Arabidopsis thaliana OX=3702 GN=HSP70-1 PE=1 SV=3	Arabidopsis thaliana	HSP70-1	65.0	100	68.027	4.78e-38	139.0	moderate_database_homology	BLASTP to reviewed UniProt Swiss-Prot	UniProt Swiss-Prot current_release 2026-06-10	At5g02500	与其他伴侣蛋白合作，Hsp70 是关键组分，可促进新合成蛋白的折叠，协助前体蛋白转运进入细胞器，并负责在应激条件下降解受损蛋白（可能）。	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).	"[{""pmid"":""12805626"",""title"":""Physiological and molecular assessment of altered expression of Hsc70-1 in Arabidopsis. Evidence for pleiotropic consequences."",""doi"":""10.1104/pp.102.019398"",""url"":""https://pubmed.ncbi.nlm.nih.gov/12805626/"",""year"":""2003"",""journal"":""Plant physiology"",""authors"":""Sung DY; Guy CL"",""matched_aliases"":[""HSC70-1""],""evidence"":""UniProt FUNCTION; UniProt/PubMed metadata and gene/species abstract checks; EuropePMC cross-check where available"",""metadata_sources"":[""UniProt"",""PubMed""],""fulltext_reviewed"":false},{""pmid"":""18065690"",""title"":""Interaction between SGT1 and cytosolic/nuclear HSC70 chaperones regulates Arabidopsis immune responses."",""doi"":""10.1105/tpc.107.051896"",""url"":""https://pubmed.ncbi.nlm.nih.gov/18065690/"",""year"":""2007"",""journal"":""The Plant cell"",""authors"":""Noël LD, Cagna G, Stuttmann J, Wirthmüller L, Betsuyaku S, Witte CP, Bhat R, Pochon N, Colby T, Parker JE."",""matched_aliases"":[""HSC70-1""],""evidence"":""UniProt FUNCTION; UniProt/PubMed metadata and gene/species abstract checks; EuropePMC cross-check where available"",""metadata_sources"":[""UniProt"",""PubMed"",""EuropePMC""],""fulltext_reviewed"":false},{""pmid"":""19617588"",""title"":""WPP-domain proteins mimic the activity of the HSC70-1 chaperone in preventing mistargeting of RanGAP1-anchoring protein WIT1."",""doi"":""10.1104/pp.109.143404"",""url"":""https://pubmed.ncbi.nlm.nih.gov/19617588/"",""year"":""2009"",""journal"":""Plant physiology"",""authors"":""Brkljacic J, Zhao Q, Meier I."",""matched_aliases"":[""HSC70-1""],""evidence"":""UniProt FUNCTION; UniProt/PubMed metadata and gene/species abstract checks; EuropePMC cross-check where available"",""metadata_sources"":[""UniProt"",""PubMed"",""EuropePMC""],""fulltext_reviewed"":false},{""pmid"":""21586649"",""title"":""The cytosolic/nuclear HSC70 and HSP90 molecular chaperones are important for stomatal closure and modulate abscisic acid-dependent physiological responses in Arabidopsis."",""doi"":""10.1104/pp.111.174425"",""url"":""https://pubmed.ncbi.nlm.nih.gov/21586649/"",""year"":""2011"",""journal"":""Plant physiology"",""authors"":""Clément M, Leonhardt N, Droillard MJ, Reiter I, Montillet JL, Genty B, Laurière C, Nussaume L, Noël LD."",""matched_aliases"":[""HSC70-1""],""evidence"":""UniProt FUNCTION; UniProt/PubMed metadata and gene/species abstract checks; EuropePMC cross-check where available"",""metadata_sources"":[""UniProt"",""PubMed"",""EuropePMC""],""fulltext_reviewed"":false}]"