PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
29689452-0	2018	Role of the HSPA9/HSC20 chaperone pair in promoting directional human iron-sulfur cluster exchange involving monothiol glutaredoxin 5.	Iron	70-74	heat shock protein family A (Hsp70) member 9	Homo sapiens	12-17	
30933555-1	2019	HSPA9, the gene coding for the mitochondrial chaperone mortalin, is involved in various cellular roles such as mitochondrial protein import, folding, degradation, Fe-S cluster biogenesis, mitochondrial homeostasis, and regulation of the antiapoptotic protein p53.	Iron	163-167	heat shock protein family A (Hsp70) member 9	Homo sapiens	0-5	
28380382-3	2017	Here we report that a transient subcomplex involved in CIII assembly, composed of LYRM7 bound to UQCRFS1, interacts with components of an Fe-S transfer complex, consisting of HSC20, its cognate chaperone HSPA9, and the holo-scaffold ISCU.	Iron	138-140	heat shock protein family A (Hsp70) member 9	Homo sapiens	204-209	
28848044-9	2017	The formation of this subcomplex was critical for conferring stability to the NEFs, helped fine-tune mitochondrial protein quality control, and regulated crucial mtHsp70 functions, such as import of preproteins and biogenesis of Fe-S clusters.	Iron	229-233	heat shock protein family A (Hsp70) member 9	Homo sapiens	162-169	
26749241-3	2016	SDHAF1 transiently binds to aromatic peptides of SDHB through an arginine-rich region in its C terminus and specifically engages a Fe-S donor complex, consisting of the scaffold, holo-ISCU, and the co-chaperone-chaperone pair, HSC20-HSPA9, through an LYR motif near its N-terminal domain.	Iron	131-135	heat shock protein family A (Hsp70) member 9	Homo sapiens	233-238	
27714045-3	2016	The delivery of assembled Fe-S clusters to recipient proteins is a crucial step in the biogenesis of Fe-S proteins, and, in mammals, it relies on the activity of a multiprotein transfer complex that contains the chaperone HSPA9, the co-chaperone HSC20 and the scaffold ISCU.	Iron	26-30	heat shock protein family A (Hsp70) member 9	Homo sapiens	222-227	
27714045-3	2016	The delivery of assembled Fe-S clusters to recipient proteins is a crucial step in the biogenesis of Fe-S proteins, and, in mammals, it relies on the activity of a multiprotein transfer complex that contains the chaperone HSPA9, the co-chaperone HSC20 and the scaffold ISCU.	Iron	101-105	heat shock protein family A (Hsp70) member 9	Homo sapiens	222-227	
24606901-4	2014	In succinate dehydrogenase B, two LYR motifs engage the ISCU-HSC20-HSPA9 complex to aid incorporation of three Fe-S clusters within the final structure of complex II.	Iron	111-115	heat shock protein family A (Hsp70) member 9	Homo sapiens	67-72	
26702583-0	2016	Mitochondrial Hspa9/Mortalin regulates erythroid differentiation via iron-sulfur cluster assembly.	Iron	69-73	heat shock protein family A (Hsp70) member 9	Homo sapiens	14-19	
26491070-2	2015	Here we demonstrate that mutations in HSPA9, a mitochondrial HSP70 homolog located in the chromosome 5q deletion syndrome 5q33 critical deletion interval and involved in mitochondrial Fe-S biogenesis, result in CSA inherited as an autosomal recessive trait.	Iron	184-188	heat shock protein family A (Hsp70) member 9	Homo sapiens	38-43	
23940031-0	2013	Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU).	Iron	197-201	heat shock protein family A (Hsp70) member 9	Homo sapiens	31-38