PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
30412706-5	2019	The crystal structures of the UBA5 long isoform bound to ATP with and without UFM1 show that the N-terminus not only is directly involved in ATP binding but also affects how the adenylation domain interacts with ATP.	Adenosine Triphosphate	141-144	ubiquitin fold modifier 1	Homo sapiens	78-82	
30412706-5	2019	The crystal structures of the UBA5 long isoform bound to ATP with and without UFM1 show that the N-terminus not only is directly involved in ATP binding but also affects how the adenylation domain interacts with ATP.	Adenosine Triphosphate	141-144	ubiquitin fold modifier 1	Homo sapiens	78-82	
29295865-0	2018	Trans-binding of UFM1 to UBA5 stimulates UBA5 homodimerization and ATP binding.	Adenosine Triphosphate	67-70	ubiquitin fold modifier 1	Homo sapiens	17-21	
29295865-5	2018	Dimerization of UBA5 is required for ATP binding; therefore, stabilization of the dimer by UFM1 enhances ATP binding.	Adenosine Triphosphate	37-40	ubiquitin fold modifier 1	Homo sapiens	91-95	
29295865-5	2018	Dimerization of UBA5 is required for ATP binding; therefore, stabilization of the dimer by UFM1 enhances ATP binding.	Adenosine Triphosphate	105-108	ubiquitin fold modifier 1	Homo sapiens	91-95	
29295865-6	2018	Our results make a connection between the binding of UFM1 to UBA5 and the latter"s affinity to ATP, so we propose a novel mechanism for the regulation of ATP"s binding to E1.-Mashahreh, B., Hassouna, F., Soudah, N., Cohen-Kfir, E., Strulovich, R., Haitin, Y., Wiener, R. Trans-binding of UFM1 to UBA5 stimulates UBA5 homodimerization and ATP binding.	Adenosine Triphosphate	95-98	ubiquitin fold modifier 1	Homo sapiens	53-57	
29295865-6	2018	Our results make a connection between the binding of UFM1 to UBA5 and the latter"s affinity to ATP, so we propose a novel mechanism for the regulation of ATP"s binding to E1.-Mashahreh, B., Hassouna, F., Soudah, N., Cohen-Kfir, E., Strulovich, R., Haitin, Y., Wiener, R. Trans-binding of UFM1 to UBA5 stimulates UBA5 homodimerization and ATP binding.	Adenosine Triphosphate	95-98	ubiquitin fold modifier 1	Homo sapiens	288-292	
29295865-6	2018	Our results make a connection between the binding of UFM1 to UBA5 and the latter"s affinity to ATP, so we propose a novel mechanism for the regulation of ATP"s binding to E1.-Mashahreh, B., Hassouna, F., Soudah, N., Cohen-Kfir, E., Strulovich, R., Haitin, Y., Wiener, R. Trans-binding of UFM1 to UBA5 stimulates UBA5 homodimerization and ATP binding.	Adenosine Triphosphate	154-157	ubiquitin fold modifier 1	Homo sapiens	53-57	
29295865-6	2018	Our results make a connection between the binding of UFM1 to UBA5 and the latter"s affinity to ATP, so we propose a novel mechanism for the regulation of ATP"s binding to E1.-Mashahreh, B., Hassouna, F., Soudah, N., Cohen-Kfir, E., Strulovich, R., Haitin, Y., Wiener, R. Trans-binding of UFM1 to UBA5 stimulates UBA5 homodimerization and ATP binding.	Adenosine Triphosphate	154-157	ubiquitin fold modifier 1	Homo sapiens	288-292	
29295865-6	2018	Our results make a connection between the binding of UFM1 to UBA5 and the latter"s affinity to ATP, so we propose a novel mechanism for the regulation of ATP"s binding to E1.-Mashahreh, B., Hassouna, F., Soudah, N., Cohen-Kfir, E., Strulovich, R., Haitin, Y., Wiener, R. Trans-binding of UFM1 to UBA5 stimulates UBA5 homodimerization and ATP binding.	Adenosine Triphosphate	154-157	ubiquitin fold modifier 1	Homo sapiens	53-57	
29295865-6	2018	Our results make a connection between the binding of UFM1 to UBA5 and the latter"s affinity to ATP, so we propose a novel mechanism for the regulation of ATP"s binding to E1.-Mashahreh, B., Hassouna, F., Soudah, N., Cohen-Kfir, E., Strulovich, R., Haitin, Y., Wiener, R. Trans-binding of UFM1 to UBA5 stimulates UBA5 homodimerization and ATP binding.	Adenosine Triphosphate	154-157	ubiquitin fold modifier 1	Homo sapiens	288-292	
24966333-8	2014	Furthermore, binding of ATP to Uba5~Ufm1 thioester was required for efficient transfer of Ufm1 from Uba5 to Ufc1 via transthiolation.	Adenosine Triphosphate	24-27	ubiquitin fold modifier 1	Homo sapiens	36-40	
20368332-4	2010	We have determined the crystal structure of the human UFM1 (ubiquitin-fold modifier 1) E1-activating enzyme UBA5, bound to ATP, revealing a structure that shares similarities with both large canonical E1 enzymes and smaller ancestral E1-like enzymes.	Adenosine Triphosphate	123-126	ubiquitin fold modifier 1	Homo sapiens	54-58	
20368332-4	2010	We have determined the crystal structure of the human UFM1 (ubiquitin-fold modifier 1) E1-activating enzyme UBA5, bound to ATP, revealing a structure that shares similarities with both large canonical E1 enzymes and smaller ancestral E1-like enzymes.	Adenosine Triphosphate	123-126	ubiquitin fold modifier 1	Homo sapiens	60-85