PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
16401076-5	2006	The mtMCM structure was successfully used to analyze a Saccharomyces cerevisiae MCM5 mutant, called BOB1, which contains a single residue change from Pro to Leu and bypasses a kinase normally required for initiation of DNA replication.	Leucine	157-160	MCM DNA helicase complex subunit MCM5	Saccharomyces cerevisiae S288C	80-84
18321994-3	2008	Mutation to alanine of these five sites (mcm4-5A) abolishes phosphorylation and decreases replication origin firing efficiency at 22 degrees C. Surprisingly, the loss of function mcm4-5A mutation confers cold and hydroxyurea sensitivity to DDK gain of function conditions (mcm5/bob1 mutation or DDK overexpression), implying that phosphorylation of Mcm4 by CDK somehow counteracts negative effects produced by ectopic DDK activation.	Alanine	12-19	MCM DNA helicase complex subunit MCM5	Saccharomyces cerevisiae S288C	273-277
18321994-3	2008	Mutation to alanine of these five sites (mcm4-5A) abolishes phosphorylation and decreases replication origin firing efficiency at 22 degrees C. Surprisingly, the loss of function mcm4-5A mutation confers cold and hydroxyurea sensitivity to DDK gain of function conditions (mcm5/bob1 mutation or DDK overexpression), implying that phosphorylation of Mcm4 by CDK somehow counteracts negative effects produced by ectopic DDK activation.	Alanine	12-19	MCM DNA helicase complex subunit MCM5	Saccharomyces cerevisiae S288C	278-282
16401076-5	2006	The mtMCM structure was successfully used to analyze a Saccharomyces cerevisiae MCM5 mutant, called BOB1, which contains a single residue change from Pro to Leu and bypasses a kinase normally required for initiation of DNA replication.	Proline	150-153	MCM DNA helicase complex subunit MCM5	Saccharomyces cerevisiae S288C	80-84
17895243-0	2007	Differences in the single-stranded DNA binding activities of MCM2-7 and MCM467: MCM2 and MCM5 define a slow ATP-dependent step.	Adenosine Triphosphate	108-111	MCM DNA helicase complex subunit MCM5	Saccharomyces cerevisiae S288C	89-93
16401076-5	2006	The mtMCM structure was successfully used to analyze a Saccharomyces cerevisiae MCM5 mutant, called BOB1, which contains a single residue change from Pro to Leu and bypasses a kinase normally required for initiation of DNA replication.	Leucine	157-160	MCM DNA helicase complex subunit MCM5	Saccharomyces cerevisiae S288C	100-104
33125801-4	2021	Here, we report the characterization of a non-natural mcm5isoC ribonucleoside in S. cerevisiae total tRNA hydrolysate.	Ribonucleosides	63-77	MCM DNA helicase complex subunit MCM5	Saccharomyces cerevisiae S288C	54-58
10945234-0	2000	Loss control of Mcm5 interaction with chromatin in cdc6-1 mutated in CDC-NTP motif.	ntp	73-76	MCM DNA helicase complex subunit MCM5	Saccharomyces cerevisiae S288C	16-20
34700328-6	2021	Our structures show that the leucine-rich repeat (LRR) domains of Dia2 and LRR1 are structurally distinct, but bind to a common site on CMG, including the MCM3 and MCM5 zinc finger domains.	Leucine	29-36	MCM DNA helicase complex subunit MCM5	Saccharomyces cerevisiae S288C	164-168
34411701-8	2021	MCM5-AID was able to improve beta-carotene production of S. cerevisiae 4742crt by 75.4% following eight rounds of editing.	beta Carotene	29-42	MCM DNA helicase complex subunit MCM5	Saccharomyces cerevisiae S288C	0-4
16401076-5	2006	The mtMCM structure was successfully used to analyze a Saccharomyces cerevisiae MCM5 mutant, called BOB1, which contains a single residue change from Pro to Leu and bypasses a kinase normally required for initiation of DNA replication.	Proline	150-153	MCM DNA helicase complex subunit MCM5	Saccharomyces cerevisiae S288C	100-104
31758251-3	2020	tRNA wobble uridines are chemically modified at the 2- and 5- positions, with a thiol (s2), and (commonly) a methoxycarbonylmethyl (mcm5) modification, respectively.	Uridine	12-20	MCM DNA helicase complex subunit MCM5	Saccharomyces cerevisiae S288C	132-136
30060218-8	2018	Both mcm5 and s2 modification of wobble uridine strongly stabilizes G2 U35 mismatches when ${\rm{tRNA} }^{\rm Glu}_{\rm UUC}$ misreads the GGA Gly codon but has weaker effects on other mismatches.	Glycine	143-146	MCM DNA helicase complex subunit MCM5	Saccharomyces cerevisiae S288C	5-9
31776648-2	2020	The Elongator complex promotes the first step in the formation of 5-methoxycarbonylmethyl (mcm5), 5-methoxycarbonylhydroxymethyl (mchm5), and 5-carbamoylmethyl (ncm5) groups on wobble uridine residues in eukaryotic cytosolic tRNAs.	5-methoxycarbonylmethyl	66-89	MCM DNA helicase complex subunit MCM5	Saccharomyces cerevisiae S288C	91-95
31776648-2	2020	The Elongator complex promotes the first step in the formation of 5-methoxycarbonylmethyl (mcm5), 5-methoxycarbonylhydroxymethyl (mchm5), and 5-carbamoylmethyl (ncm5) groups on wobble uridine residues in eukaryotic cytosolic tRNAs.	ncm5	161-165	MCM DNA helicase complex subunit MCM5	Saccharomyces cerevisiae S288C	91-95
31776648-2	2020	The Elongator complex promotes the first step in the formation of 5-methoxycarbonylmethyl (mcm5), 5-methoxycarbonylhydroxymethyl (mchm5), and 5-carbamoylmethyl (ncm5) groups on wobble uridine residues in eukaryotic cytosolic tRNAs.	Uridine	184-191	MCM DNA helicase complex subunit MCM5	Saccharomyces cerevisiae S288C	91-95
31465447-1	2019	The Elongator complex promotes formation of 5-methoxycarbonylmethyl (mcm5) and 5-carbamoylmethyl (ncm5) side-chains on uridines at the wobble position of cytosolic eukaryotic tRNAs.	5-methoxycarbonylmethyl	44-67	MCM DNA helicase complex subunit MCM5	Saccharomyces cerevisiae S288C	69-73
31465447-1	2019	The Elongator complex promotes formation of 5-methoxycarbonylmethyl (mcm5) and 5-carbamoylmethyl (ncm5) side-chains on uridines at the wobble position of cytosolic eukaryotic tRNAs.	Uridine	119-127	MCM DNA helicase complex subunit MCM5	Saccharomyces cerevisiae S288C	69-73
31465447-7	2019	The difference at the SSD1 locus also partially explains why the simultaneous lack of mcm5 and 2-thio groups at wobble uridines is lethal in the W303 but not in the S288C background.	Uridine	119-127	MCM DNA helicase complex subunit MCM5	Saccharomyces cerevisiae S288C	86-96
28368583-1	2017	Uridine 34 (U34) at the wobble position of the tRNA anticodon is post-transcriptionally modified, usually to mcm5s2, mcm5, or mnm5.	Uridine	0-7	MCM DNA helicase complex subunit MCM5	Saccharomyces cerevisiae S288C	109-113
26670883-3	2015	Here we use quantitative proteomics to show a direct link between wobble uridine 5-methoxycarbonylmethyl (mcm5) and 5-methoxy-carbonyl-methyl-2-thio (mcm5s2) modifications catalyzed by tRNA methyltransferase 9 (Trm9) in tRNAArg(UCU) and tRNAGlu(UUC) and selective translation of proteins from genes enriched with their cognate codons.	Uridine	73-80	MCM DNA helicase complex subunit MCM5	Saccharomyces cerevisiae S288C	106-110
27738410-0	2016	Loss of ncm5 and mcm5 wobble uridine side chains results in an altered metabolic profile.	Uridine	29-36	MCM DNA helicase complex subunit MCM5	Saccharomyces cerevisiae S288C	17-21
27738410-1	2016	INTRODUCTION: The Elongator complex, comprising six subunits (Elp1p-Elp6p), is required for formation of 5-carbamoylmethyl (ncm5) and 5-methoxycarbonylmethyl (mcm5) side chains on wobble uridines in 11 out of 42 tRNA species in Saccharomyces cerevisiae.	Uridine	187-195	MCM DNA helicase complex subunit MCM5	Saccharomyces cerevisiae S288C	159-163
27738410-9	2016	CONCLUSION: Our results suggest that the presence of ncm5- and mcm5-side chains on wobble uridines in tRNA are important for metabolic homeostasis.	Uridine	90-98	MCM DNA helicase complex subunit MCM5	Saccharomyces cerevisiae S288C	63-67