##gff-version 3
Q12888	UniProtKB	Chain	1	1972	.	.	.	ID=PRO_0000072643;Note=TP53-binding protein 1	
Q12888	UniProtKB	Domain	1724	1848	.	.	.	Note=BRCT 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033	
Q12888	UniProtKB	Domain	1864	1964	.	.	.	Note=BRCT 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00033	
Q12888	UniProtKB	Region	24	273	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Region	290	332	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Region	346	507	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Region	520	556	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Region	568	595	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Region	649	687	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Region	742	911	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Region	997	1028	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Region	1045	1103	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Region	1127	1148	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Region	1188	1232	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Region	1269	1478	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Region	1484	1603	.	.	.	Note=Tudor-like;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:17190600;Dbxref=PMID:17190600	
Q12888	UniProtKB	Region	1495	1523	.	.	.	Note=Interaction with dimethylated histone H4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17190600;Dbxref=PMID:17190600	
Q12888	UniProtKB	Region	1622	1719	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Region	1745	1768	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Motif	1396	1403	.	.	.	Note=GAR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16294045;Dbxref=PMID:16294045	
Q12888	UniProtKB	Motif	1604	1631	.	.	.	Note=UDR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23760478;Dbxref=PMID:23760478	
Q12888	UniProtKB	Compositional bias	31	63	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Compositional bias	76	92	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Compositional bias	93	124	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Compositional bias	130	152	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Compositional bias	153	209	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Compositional bias	346	366	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Compositional bias	424	441	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Compositional bias	452	469	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Compositional bias	580	595	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Compositional bias	794	822	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Compositional bias	848	878	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Compositional bias	887	905	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Compositional bias	1068	1082	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Compositional bias	1188	1202	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Compositional bias	1216	1232	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Compositional bias	1284	1329	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Compositional bias	1632	1655	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Compositional bias	1669	1683	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q12888	UniProtKB	Modified residue	25	25	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19176521;Dbxref=PMID:19176521	
Q12888	UniProtKB	Modified residue	63	63	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
Q12888	UniProtKB	Modified residue	105	105	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:17525332;Dbxref=PMID:17525332	
Q12888	UniProtKB	Modified residue	124	124	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:20068231,PMID:23186163	
Q12888	UniProtKB	Modified residue	166	166	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17553757;Dbxref=PMID:17553757	
Q12888	UniProtKB	Modified residue	176	176	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:17553757;Dbxref=PMID:17553757	
Q12888	UniProtKB	Modified residue	178	178	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:17553757;Dbxref=PMID:17553757	
Q12888	UniProtKB	Modified residue	222	222	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163;Dbxref=PMID:17081983,PMID:18669648,PMID:21406692,PMID:23186163	
Q12888	UniProtKB	Modified residue	265	265	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:23186163	
Q12888	UniProtKB	Modified residue	294	294	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:17553757,ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:17081983,PMID:17553757,PMID:19690332,PMID:20068231,PMID:21406692,PMID:23186163,PMID:24275569	
Q12888	UniProtKB	Modified residue	302	302	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:17553757,ECO:0007744|PubMed:17525332;Dbxref=PMID:17525332,PMID:17553757	
Q12888	UniProtKB	Modified residue	366	366	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:31135337,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:23186163;Dbxref=PMID:19690332,PMID:23186163,PMID:31135337	
Q12888	UniProtKB	Modified residue	380	380	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:17553757,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:23186163;Dbxref=PMID:17553757,PMID:19690332,PMID:23186163	
Q12888	UniProtKB	Modified residue	395	395	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648	
Q12888	UniProtKB	Modified residue	398	398	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:23186163	
Q12888	UniProtKB	Modified residue	429	429	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P70399	
Q12888	UniProtKB	Modified residue	452	452	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17553757;Dbxref=PMID:17553757	
Q12888	UniProtKB	Modified residue	464	464	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P70399	
Q12888	UniProtKB	Modified residue	500	500	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:17081983,PMID:18669648,PMID:19690332,PMID:20068231,PMID:21406692,PMID:23186163,PMID:24275569	
Q12888	UniProtKB	Modified residue	507	507	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
Q12888	UniProtKB	Modified residue	518	518	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
Q12888	UniProtKB	Modified residue	523	523	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:17553757,ECO:0007744|PubMed:17525332,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:23186163;Dbxref=PMID:17525332,PMID:17553757,PMID:18669648,PMID:19690332,PMID:23186163	
Q12888	UniProtKB	Modified residue	525	525	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:19690332,PMID:20068231,PMID:21406692,PMID:23186163	
Q12888	UniProtKB	Modified residue	543	543	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17525332,ECO:0007744|PubMed:19690332;Dbxref=PMID:17525332,PMID:19690332	
Q12888	UniProtKB	Modified residue	548	548	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:17525332;Dbxref=PMID:17525332	
Q12888	UniProtKB	Modified residue	552	552	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:17553757,ECO:0007744|PubMed:17525332,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:17525332,PMID:17553757,PMID:18669648,PMID:19690332,PMID:20068231,PMID:21406692,PMID:23186163,PMID:24275569	
Q12888	UniProtKB	Modified residue	566	566	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:20068231;Dbxref=PMID:20068231	
Q12888	UniProtKB	Modified residue	580	580	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:20068231,PMID:23186163	
Q12888	UniProtKB	Modified residue	630	630	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569	
Q12888	UniProtKB	Modified residue	635	635	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:17081983;Dbxref=PMID:17081983	
Q12888	UniProtKB	Modified residue	639	639	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:20068231;Dbxref=PMID:17081983,PMID:20068231	
Q12888	UniProtKB	Modified residue	640	640	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:20068231;Dbxref=PMID:17081983,PMID:20068231	
Q12888	UniProtKB	Modified residue	670	670	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31135337;Dbxref=PMID:31135337	
Q12888	UniProtKB	Modified residue	692	692	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569	
Q12888	UniProtKB	Modified residue	724	724	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P70399	
Q12888	UniProtKB	Modified residue	727	727	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569	
Q12888	UniProtKB	Modified residue	771	771	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
Q12888	UniProtKB	Modified residue	809	809	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:20068231,PMID:21406692,PMID:23186163	
Q12888	UniProtKB	Modified residue	830	830	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P70399	
Q12888	UniProtKB	Modified residue	831	831	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:17553757,ECO:0007744|PubMed:17525332,ECO:0007744|PubMed:18669648;Dbxref=PMID:17525332,PMID:17553757,PMID:18669648	
Q12888	UniProtKB	Modified residue	834	834	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:16964243,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:23186163;Dbxref=PMID:16964243,PMID:19690332,PMID:23186163	
Q12888	UniProtKB	Modified residue	855	855	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:17525332;Dbxref=PMID:17525332	
Q12888	UniProtKB	Modified residue	922	922	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:20068231,PMID:23186163	
Q12888	UniProtKB	Modified residue	970	970	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:20068231;Dbxref=PMID:20068231	
Q12888	UniProtKB	Modified residue	975	975	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:20068231;Dbxref=PMID:20068231	
Q12888	UniProtKB	Modified residue	1028	1028	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:17553757,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163;Dbxref=PMID:17553757,PMID:18669648,PMID:19690332,PMID:20068231,PMID:21406692,PMID:23186163	
Q12888	UniProtKB	Modified residue	1056	1056	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
Q12888	UniProtKB	Modified residue	1068	1068	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:20068231,PMID:23186163	
Q12888	UniProtKB	Modified residue	1086	1086	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17553757;Dbxref=PMID:17553757	
Q12888	UniProtKB	Modified residue	1094	1094	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:17081983,PMID:18669648,PMID:23186163	
Q12888	UniProtKB	Modified residue	1101	1101	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21406692;Dbxref=PMID:21406692	
Q12888	UniProtKB	Modified residue	1114	1114	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:17553757,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:17553757,PMID:19690332,PMID:20068231,PMID:21406692,PMID:23186163,PMID:24275569	
Q12888	UniProtKB	Modified residue	1148	1148	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
Q12888	UniProtKB	Modified residue	1214	1214	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:17525332;Dbxref=PMID:17525332	
Q12888	UniProtKB	Modified residue	1216	1216	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17525332,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:17525332,PMID:18669648,PMID:23186163,PMID:24275569	
Q12888	UniProtKB	Modified residue	1219	1219	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:17553757,ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:17525332,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:17081983,PMID:17525332,PMID:17553757,PMID:18669648,PMID:23186163	
Q12888	UniProtKB	Modified residue	1317	1317	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
Q12888	UniProtKB	Modified residue	1342	1342	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
Q12888	UniProtKB	Modified residue	1355	1355	.	.	.	Note=Omega-N-methylarginine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P70399	
Q12888	UniProtKB	Modified residue	1362	1362	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:17081983,PMID:20068231,PMID:21406692,PMID:23186163,PMID:24275569	
Q12888	UniProtKB	Modified residue	1368	1368	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648	
Q12888	UniProtKB	Modified residue	1372	1372	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648	
Q12888	UniProtKB	Modified residue	1426	1426	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:16964243,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:16964243,PMID:18669648,PMID:19690332,PMID:20068231,PMID:23186163	
Q12888	UniProtKB	Modified residue	1430	1430	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:19690332,PMID:20068231,PMID:21406692,PMID:23186163	
Q12888	UniProtKB	Modified residue	1460	1460	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19690332;Dbxref=PMID:19690332	
Q12888	UniProtKB	Modified residue	1462	1462	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:19690332,PMID:23186163	
Q12888	UniProtKB	Modified residue	1474	1474	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19690332;Dbxref=PMID:19690332	
Q12888	UniProtKB	Modified residue	1609	1609	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:24703952,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:20068231,PMID:23186163,PMID:24703952	
Q12888	UniProtKB	Modified residue	1618	1618	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:24703952,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163;Dbxref=PMID:20068231,PMID:21406692,PMID:23186163,PMID:24703952	
Q12888	UniProtKB	Modified residue	1631	1631	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P70399	
Q12888	UniProtKB	Modified residue	1635	1635	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
Q12888	UniProtKB	Modified residue	1638	1638	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
Q12888	UniProtKB	Modified residue	1648	1648	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
Q12888	UniProtKB	Modified residue	1656	1656	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
Q12888	UniProtKB	Modified residue	1673	1673	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
Q12888	UniProtKB	Modified residue	1678	1678	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163;Dbxref=PMID:17081983,PMID:20068231,PMID:21406692,PMID:23186163	
Q12888	UniProtKB	Modified residue	1701	1701	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:23186163	
Q12888	UniProtKB	Modified residue	1759	1759	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648	
Q12888	UniProtKB	Modified residue	1778	1778	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19176521,ECO:0000269|PubMed:21144835;Dbxref=PMID:19176521,PMID:21144835	
Q12888	UniProtKB	Cross-link	217	217	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:25114211;Dbxref=PMID:25114211	
Q12888	UniProtKB	Cross-link	217	217	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)%3B alternate;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25114211,ECO:0007744|PubMed:28112733;Dbxref=PMID:25114211,PMID:28112733	
Q12888	UniProtKB	Cross-link	868	868	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:25114211;Dbxref=PMID:25114211	
Q12888	UniProtKB	Cross-link	868	868	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733	
Q12888	UniProtKB	Cross-link	930	930	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25218447,ECO:0007744|PubMed:25772364,ECO:0007744|PubMed:28112733;Dbxref=PMID:25218447,PMID:25772364,PMID:28112733	
Q12888	UniProtKB	Cross-link	984	984	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733	
Q12888	UniProtKB	Cross-link	1365	1365	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733	
Q12888	UniProtKB	Cross-link	1434	1434	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:25114211;Dbxref=PMID:25114211	
Q12888	UniProtKB	Cross-link	1434	1434	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)%3B alternate;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25114211,ECO:0007744|PubMed:28112733;Dbxref=PMID:25114211,PMID:28112733	
Q12888	UniProtKB	Cross-link	1563	1563	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:25114211;Dbxref=PMID:25114211	
Q12888	UniProtKB	Cross-link	1563	1563	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)%3B alternate;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25114211,ECO:0007744|PubMed:25218447,ECO:0007744|PubMed:25755297,ECO:0007744|PubMed:28112733;Dbxref=PMID:25114211,PMID:25218447,PMID:25755297,PMID:28112733	
Q12888	UniProtKB	Alternative sequence	1	1	.	.	.	ID=VSP_018390;Note=In isoform 2 and isoform 3. M->MPGEQM;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:17974005,ECO:0000303|Ref.2;Dbxref=PMID:17974005	
Q12888	UniProtKB	Alternative sequence	1692	1693	.	.	.	ID=VSP_055062;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.2	
Q12888	UniProtKB	Natural variant	353	353	.	.	.	ID=VAR_022172;Note=D->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17974005,ECO:0000269|Ref.4;Dbxref=dbSNP:rs560191,PMID:17974005	
Q12888	UniProtKB	Natural variant	412	412	.	.	.	ID=VAR_022173;Note=G->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17974005,ECO:0000269|Ref.4;Dbxref=dbSNP:rs689647,PMID:17974005	
Q12888	UniProtKB	Natural variant	648	648	.	.	.	ID=VAR_022174;Note=M->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4;Dbxref=dbSNP:rs45443496	
Q12888	UniProtKB	Natural variant	699	699	.	.	.	ID=VAR_022175;Note=Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4;Dbxref=dbSNP:rs34823068	
Q12888	UniProtKB	Natural variant	841	841	.	.	.	ID=VAR_034558;Note=D->G;Dbxref=dbSNP:rs34185035	
Q12888	UniProtKB	Natural variant	1014	1014	.	.	.	ID=VAR_022176;Note=E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4;Dbxref=dbSNP:rs45470395	
Q12888	UniProtKB	Natural variant	1026	1026	.	.	.	ID=VAR_022177;Note=V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4;Dbxref=dbSNP:rs45482998	
Q12888	UniProtKB	Natural variant	1136	1136	.	.	.	ID=VAR_022178;Note=K->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17974005,ECO:0000269|Ref.4;Dbxref=dbSNP:rs2602141,PMID:17974005	
Q12888	UniProtKB	Natural variant	1137	1137	.	.	.	ID=VAR_034559;Note=E->K;Dbxref=dbSNP:rs34740611	
Q12888	UniProtKB	Natural variant	1170	1170	.	.	.	ID=VAR_022179;Note=A->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4;Dbxref=dbSNP:rs45500399	
Q12888	UniProtKB	Natural variant	1174	1174	.	.	.	ID=VAR_022180;Note=I->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4;Dbxref=dbSNP:rs3803339	
Q12888	UniProtKB	Natural variant	1442	1442	.	.	.	ID=VAR_034560;Note=R->Q;Dbxref=dbSNP:rs2230449	
Q12888	UniProtKB	Natural variant	1488	1488	.	.	.	ID=VAR_038689;Note=G->W;Dbxref=dbSNP:rs11554564	
Q12888	UniProtKB	Mutagenesis	6	6	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-13%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176%3B A-178%3B A-302%3B A-437%3B A-452%3B A-523%3B A-543%3B A-580%3B A-625%3B A-674%3B A-696%3B A-698%3B A-784%3B A-831%3B A-855%3B A-892%3B A-1068%3B A-1086%3B A-1104%3B A-1148%3B A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR)%2C but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres%3B when associated with A-13%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176 and A-178. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425,ECO:0000269|PubMed:23727112;Dbxref=PMID:23333306,PMID:23345425,PMID:23727112	
Q12888	UniProtKB	Mutagenesis	13	13	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176%3B A-178%3B A-302%3B A-437%3B A-452%3B A-523%3B A-543%3B A-580%3B A-625%3B A-674%3B A-696%3B A-698%3B A-784%3B A-831%3B A-855%3B A-892%3B A-1068%3B A-1086%3B A-1104%3B A-1148%3B A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR)%2C but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres%3B when associated with A-6%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176 and A-178. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425,ECO:0000269|PubMed:23727112;Dbxref=PMID:23333306,PMID:23345425,PMID:23727112	
Q12888	UniProtKB	Mutagenesis	25	25	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-29%3B A-105%3B A-166%3B A-176%3B A-178%3B A-302%3B A-437%3B A-452%3B A-523%3B A-543%3B A-580%3B A-625%3B A-674%3B A-696%3B A-698%3B A-784%3B A-831%3B A-855%3B A-892%3B A-1068%3B A-1086%3B A-1104%3B A-1148%3B A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR)%2C but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres%3B when associated with A-6%3B A-13%3B A-29%3B A-105%3B A-166%3B A-176 and A-178. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425,ECO:0000269|PubMed:23727112;Dbxref=PMID:23333306,PMID:23345425,PMID:23727112	
Q12888	UniProtKB	Mutagenesis	29	29	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-105%3B A-166%3B A-176%3B A-178%3B A-302%3B A-437%3B A-452%3B A-523%3B A-543%3B A-580%3B A-625%3B A-674%3B A-696%3B A-698%3B A-784%3B A-831%3B A-855%3B A-892%3B A-1068%3B A-1086%3B A-1104%3B A-1148%3B A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR)%2C but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres%3B when associated with A-6%3B A-13%3B A-25%3B A-105%3B A-166%3B A-176 and A-178. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425,ECO:0000269|PubMed:23727112;Dbxref=PMID:23333306,PMID:23345425,PMID:23727112	
Q12888	UniProtKB	Mutagenesis	105	105	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-166%3B A-176%3B A-178%3B A-302%3B A-437%3B A-452%3B A-523%3B A-543%3B A-580%3B A-625%3B A-674%3B A-696%3B A-698%3B A-784%3B A-831%3B A-855%3B A-892%3B A-1068%3B A-1086%3B A-1104%3B A-1148%3B A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR)%2C but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-166%3B A-176 and A-178. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425,ECO:0000269|PubMed:23727112;Dbxref=PMID:23333306,PMID:23345425,PMID:23727112	
Q12888	UniProtKB	Mutagenesis	166	166	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-176%3B A-178%3B A-302%3B A-437%3B A-452%3B A-523%3B A-543%3B A-580%3B A-625%3B A-674%3B A-696%3B A-698%3B A-784%3B A-831%3B A-855%3B A-892%3B A-1068%3B A-1086%3B A-1104%3B A-1148%3B A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR)%2C but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-176 and A-178. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425,ECO:0000269|PubMed:23727112;Dbxref=PMID:23333306,PMID:23345425,PMID:23727112	
Q12888	UniProtKB	Mutagenesis	176	178	.	.	.	Note=Loss of phosphorylation site. SQS->AQA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17553757;Dbxref=PMID:17553757	
Q12888	UniProtKB	Mutagenesis	176	176	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-166%3B A-178%3B A-302%3B A-437%3B A-452%3B A-523%3B A-543%3B A-580%3B A-625%3B A-674%3B A-696%3B A-698%3B A-784%3B A-831%3B A-855%3B A-892%3B A-1068%3B A-1086%3B A-1104%3B A-1148%3B A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR)%2C but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-166 and A-178. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425,ECO:0000269|PubMed:23727112;Dbxref=PMID:23333306,PMID:23345425,PMID:23727112	
Q12888	UniProtKB	Mutagenesis	178	178	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176%3B A-302%3B A-437%3B A-452%3B A-523%3B A-543%3B A-580%3B A-625%3B A-674%3B A-696%3B A-698%3B A-784%3B A-831%3B A-855%3B A-892%3B A-1068%3B A-1086%3B A-1104%3B A-1148%3B A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR)%2C but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-166 and A-176. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425,ECO:0000269|PubMed:23727112;Dbxref=PMID:23333306,PMID:23345425,PMID:23727112	
Q12888	UniProtKB	Mutagenesis	302	302	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176%3B A-178%3B A-437%3B A-452%3B A-523%3B A-543%3B A-580%3B A-625%3B A-674%3B A-696%3B A-698%3B A-784%3B A-831%3B A-855%3B A-892%3B A-1068%3B A-1086%3B A-1104%3B A-1148%3B A-1171 and A-1219. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425;Dbxref=PMID:23333306,PMID:23345425	
Q12888	UniProtKB	Mutagenesis	366	366	.	.	.	Note=Decreased interaction with TOPBP1. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31135337;Dbxref=PMID:31135337	
Q12888	UniProtKB	Mutagenesis	437	437	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176%3B A-178%3B A-302%3B A-452%3B A-523%3B A-543%3B A-580%3B A-625%3B A-674%3B A-696%3B A-698%3B A-784%3B A-831%3B A-855%3B A-892%3B A-1068%3B A-1086%3B A-1104%3B A-1148%3B A-1171 and A-1219. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425;Dbxref=PMID:23333306,PMID:23345425	
Q12888	UniProtKB	Mutagenesis	452	452	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176%3B A-178%3B A-302%3B A-437%3B A-523%3B A-543%3B A-580%3B A-625%3B A-674%3B A-696%3B A-698%3B A-784%3B A-831%3B A-855%3B A-892%3B A-1068%3B A-1086%3B A-1104%3B A-1148%3B A-1171 and A-1219. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425;Dbxref=PMID:23333306,PMID:23345425	
Q12888	UniProtKB	Mutagenesis	523	523	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176%3B A-178%3B A-302%3B A-437%3B A-452%3B A-543%3B A-580%3B A-625%3B A-674%3B A-696%3B A-698%3B A-784%3B A-831%3B A-855%3B A-892%3B A-1068%3B A-1086%3B A-1104%3B A-1148%3B A-1171 and A-1219. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425;Dbxref=PMID:23333306,PMID:23345425	
Q12888	UniProtKB	Mutagenesis	543	543	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176%3B A-178%3B A-302%3B A-437%3B A-452%3B A-523%3B A-580%3B A-625%3B A-674%3B A-696%3B A-698%3B A-784%3B A-831%3B A-855%3B A-892%3B A-1068%3B A-1086%3B A-1104%3B A-1148%3B A-1171 and A-1219. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425;Dbxref=PMID:23333306,PMID:23345425	
Q12888	UniProtKB	Mutagenesis	580	580	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176%3B A-178%3B A-302%3B A-437%3B A-452%3B A-523%3B A-543%3B A-625%3B A-674%3B A-696%3B A-698%3B A-784%3B A-831%3B A-855%3B A-892%3B A-1068%3B A-1086%3B A-1104%3B A-1148%3B A-1171 and A-1219. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425;Dbxref=PMID:23333306,PMID:23345425	
Q12888	UniProtKB	Mutagenesis	625	625	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176%3B A-178%3B A-302%3B A-437%3B A-452%3B A-523%3B A-543%3B A-580%3B A-674%3B A-696%3B A-698%3B A-784%3B A-831%3B A-855%3B A-892%3B A-1068%3B A-1086%3B A-1104%3B A-1148%3B A-1171 and A-1219. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425;Dbxref=PMID:23333306,PMID:23345425	
Q12888	UniProtKB	Mutagenesis	670	670	.	.	.	Note=Decreased interaction with TOPBP1. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31135337;Dbxref=PMID:31135337	
Q12888	UniProtKB	Mutagenesis	674	674	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176%3B A-178%3B A-302%3B A-437%3B A-452%3B A-523%3B A-543%3B A-580%3B A-625%3B A-696%3B A-698%3B A-784%3B A-831%3B A-855%3B A-892%3B A-1068%3B A-1086%3B A-1104%3B A-1148%3B A-1171 and A-1219. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425;Dbxref=PMID:23333306,PMID:23345425	
Q12888	UniProtKB	Mutagenesis	696	696	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176%3B A-178%3B A-302%3B A-437%3B A-452%3B A-523%3B A-543%3B A-580%3B A-625%3B A-674%3B A-698%3B A-784%3B A-831%3B A-855%3B A-892%3B A-1068%3B A-1086%3B A-1104%3B A-1148%3B A-1171 and A-1219. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425;Dbxref=PMID:23333306,PMID:23345425	
Q12888	UniProtKB	Mutagenesis	698	698	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176%3B A-178%3B A-302%3B A-437%3B A-452%3B A-523%3B A-543%3B A-580%3B A-625%3B A-674%3B A-696%3B A-784%3B A-831%3B A-855%3B A-892%3B A-1068%3B A-1086%3B A-1104%3B A-1148%3B A-1171 and A-1219. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425;Dbxref=PMID:23333306,PMID:23345425	
Q12888	UniProtKB	Mutagenesis	784	784	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176%3B A-178%3B A-302%3B A-437%3B A-452%3B A-523%3B A-543%3B A-580%3B A-625%3B A-674%3B A-696%3B A-698%3B A-831%3B A-855%3B A-892%3B A-1068%3B A-1086%3B A-1104%3B A-1148%3B A-1171 and A-1219. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425;Dbxref=PMID:23333306,PMID:23345425	
Q12888	UniProtKB	Mutagenesis	831	831	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176%3B A-178%3B A-302%3B A-437%3B A-452%3B A-523%3B A-543%3B A-580%3B A-625%3B A-674%3B A-696%3B A-698%3B A-784%3B A-855%3B A-892%3B A-1068%3B A-1086%3B A-1104%3B A-1148%3B A-1171 and A-1219. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425;Dbxref=PMID:23333306,PMID:23345425	
Q12888	UniProtKB	Mutagenesis	855	855	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176%3B A-178%3B A-302%3B A-437%3B A-452%3B A-523%3B A-543%3B A-580%3B A-625%3B A-674%3B A-696%3B A-698%3B A-784%3B A-831%3B A-892%3B A-1068%3B A-1086%3B A-1104%3B A-1148%3B A-1171 and A-1219. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425;Dbxref=PMID:23333306,PMID:23345425	
Q12888	UniProtKB	Mutagenesis	892	892	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176%3B A-178%3B A-302%3B A-437%3B A-452%3B A-523%3B A-543%3B A-580%3B A-625%3B A-674%3B A-696%3B A-698%3B A-784%3B A-831%3B A-855%3B A-1068%3B A-1086%3B A-1104%3B A-1148%3B A-1171 and A-1219. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425;Dbxref=PMID:23333306,PMID:23345425	
Q12888	UniProtKB	Mutagenesis	1068	1068	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176%3B A-178%3B A-302%3B A-437%3B A-452%3B A-523%3B A-543%3B A-580%3B A-625%3B A-674%3B A-696%3B A-698%3B A-784%3B A-831%3B A-855%3B A-892%3B A-1086%3B A-1104%3B A-1148%3B A-1171 and A-1219. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425;Dbxref=PMID:23333306,PMID:23345425	
Q12888	UniProtKB	Mutagenesis	1086	1086	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176%3B A-178%3B A-302%3B A-437%3B A-452%3B A-523%3B A-543%3B A-580%3B A-625%3B A-674%3B A-696%3B A-698%3B A-784%3B A-831%3B A-855%3B A-892%3B A-1068%3B A-1104%3B A-1148%3B A-1171 and A-1219. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425;Dbxref=PMID:23333306,PMID:23345425	
Q12888	UniProtKB	Mutagenesis	1104	1104	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176%3B A-178%3B A-302%3B A-437%3B A-452%3B A-523%3B A-543%3B A-580%3B A-625%3B A-674%3B A-696%3B A-698%3B A-784%3B A-831%3B A-855%3B A-892%3B A-1068%3B A-1086%3B A-1148%3B A-1171 and A-1219. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425;Dbxref=PMID:23333306,PMID:23345425	
Q12888	UniProtKB	Mutagenesis	1148	1148	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176%3B A-178%3B A-302%3B A-437%3B A-452%3B A-523%3B A-543%3B A-580%3B A-625%3B A-674%3B A-696%3B A-698%3B A-784%3B A-831%3B A-855%3B A-892%3B A-1068%3B A-1086%3B A-1104%3B A-1171 and A-1219. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425;Dbxref=PMID:23333306,PMID:23345425	
Q12888	UniProtKB	Mutagenesis	1171	1171	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176%3B A-178%3B A-302%3B A-437%3B A-452%3B A-523%3B A-543%3B A-580%3B A-625%3B A-674%3B A-696%3B A-698%3B A-784%3B A-831%3B A-855%3B A-892%3B A-1068%3B A-1086%3B A-1104%3B A-1148 and A-1219. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425;Dbxref=PMID:23333306,PMID:23345425	
Q12888	UniProtKB	Mutagenesis	1219	1219	.	.	.	Note=In 28A: Defects in recruitment to double strand breaks (DSBs)%2C abolished interaction with RIF1 and abolished ability to repair DSBs%3B when associated with A-6%3B A-13%3B A-25%3B A-29%3B A-105%3B A-166%3B A-176%3B A-178%3B A-302%3B A-437%3B A-452%3B A-523%3B A-543%3B A-580%3B A-625%3B A-674%3B A-696%3B A-698%3B A-784%3B A-831%3B A-855%3B A-892%3B A-1068%3B A-1086%3B A-1104%3B A-1148 and A-1171. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23333306,ECO:0000269|PubMed:23345425;Dbxref=PMID:23333306,PMID:23345425	
Q12888	UniProtKB	Mutagenesis	1396	1396	.	.	.	Note=No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation%3B when associated with A-1398%3B A-1400%3B A-1401 and A-1403. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16294045,ECO:0000269|PubMed:16294047;Dbxref=PMID:16294045,PMID:16294047	
Q12888	UniProtKB	Mutagenesis	1396	1396	.	.	.	Note=No detectable effect on methylation by PRMT1 (in vitro). R->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16294045,ECO:0000269|PubMed:16294047;Dbxref=PMID:16294045,PMID:16294047	
Q12888	UniProtKB	Mutagenesis	1398	1401	.	.	.	Note=No effect on in class-switch recombination (CSR). RGRR->AGAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23345425;Dbxref=PMID:23345425	
Q12888	UniProtKB	Mutagenesis	1398	1398	.	.	.	Note=No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation%3B when associated with A-1396%3B A-1400%3B A-1401 and A-1403. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16294045,ECO:0000269|PubMed:16294047;Dbxref=PMID:16294045,PMID:16294047	
Q12888	UniProtKB	Mutagenesis	1398	1398	.	.	.	Note=Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation%3B when associated with K-1400. Strongly reduced methylation%3B when associated with K-1401. R->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16294045,ECO:0000269|PubMed:16294047;Dbxref=PMID:16294045,PMID:16294047	
Q12888	UniProtKB	Mutagenesis	1400	1400	.	.	.	Note=No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation%3B when associated with A-1396%3B A-1398%3B A-1401 and A-1403. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16294045,ECO:0000269|PubMed:16294047;Dbxref=PMID:16294045,PMID:16294047	
Q12888	UniProtKB	Mutagenesis	1400	1400	.	.	.	Note=Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation%3B when associated with K-1398. Strongly reduced methylation%3B when associated with K-1401. R->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16294045,ECO:0000269|PubMed:16294047;Dbxref=PMID:16294045,PMID:16294047	
Q12888	UniProtKB	Mutagenesis	1401	1401	.	.	.	Note=No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation%3B when associated with A-1396%3B A-1398%3B A-1400 and A-1403. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16294045,ECO:0000269|PubMed:16294047;Dbxref=PMID:16294045,PMID:16294047	
Q12888	UniProtKB	Mutagenesis	1401	1401	.	.	.	Note=Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation%3B when associated with K-1398. Strongly reduced methylation%3B when associated with K-1400. R->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16294045,ECO:0000269|PubMed:16294047;Dbxref=PMID:16294045,PMID:16294047	
Q12888	UniProtKB	Mutagenesis	1403	1403	.	.	.	Note=No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation%3B when associated with A-1396%3B A-1398%3B A-1400 and A-1401. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16294045,ECO:0000269|PubMed:16294047;Dbxref=PMID:16294045,PMID:16294047	
Q12888	UniProtKB	Mutagenesis	1403	1403	.	.	.	Note=No detectable effect on methylation by PRMT1 (in vitro). R->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16294045,ECO:0000269|PubMed:16294047;Dbxref=PMID:16294045,PMID:16294047	
Q12888	UniProtKB	Mutagenesis	1495	1495	.	.	.	Note=Loss of interaction with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2). Abolishes recruitment to double strand breaks. Loss of interaction with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2). Abolishes recruitment to double strand breaks%3B when associated with A-1521. W->A%2CH;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15525939,ECO:0000269|PubMed:17190600,ECO:0000269|PubMed:28241136;Dbxref=PMID:15525939,PMID:17190600,PMID:28241136	
Q12888	UniProtKB	Mutagenesis	1495	1495	.	.	.	Note=No effect on recruitment to double strand breaks. W->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15525939,ECO:0000269|PubMed:17190600;Dbxref=PMID:15525939,PMID:17190600	
Q12888	UniProtKB	Mutagenesis	1495	1495	.	.	.	Note=Reduces recruitment to double strand breaks. W->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15525939,ECO:0000269|PubMed:17190600;Dbxref=PMID:15525939,PMID:17190600	
Q12888	UniProtKB	Mutagenesis	1500	1500	.	.	.	Note=Reduces affinity for histone H4 that has been dimethylated at 'Lys-20'. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17190600;Dbxref=PMID:17190600	
Q12888	UniProtKB	Mutagenesis	1502	1502	.	.	.	Note=Reduces affinity for histone H4 that has been dimethylated at 'Lys-20'. Y->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15525939,ECO:0000269|PubMed:17190600;Dbxref=PMID:15525939,PMID:17190600	
Q12888	UniProtKB	Mutagenesis	1502	1502	.	.	.	Note=Abolishes recruitment to double strand breaks. Y->L%2CQ;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15525939,ECO:0000269|PubMed:17190600;Dbxref=PMID:15525939,PMID:17190600	
Q12888	UniProtKB	Mutagenesis	1521	1521	.	.	.	Note=Loss of interaction with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2). Abolishes recruitment to double strand breaks. Loss of interaction with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2). Abolishes recruitment to double strand breaks%3B when associated with A-1495. D->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15525939,ECO:0000269|PubMed:17190600,ECO:0000269|PubMed:28241136;Dbxref=PMID:15525939,PMID:17190600,PMID:28241136	
Q12888	UniProtKB	Mutagenesis	1521	1521	.	.	.	Note=Abolishes recruitment to double strand breaks and induces defects in class-switch recombination (CSR). D->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15525939,ECO:0000269|PubMed:17190600,ECO:0000269|PubMed:23345425,ECO:0000269|PubMed:23760478;Dbxref=PMID:15525939,PMID:17190600,PMID:23345425,PMID:23760478	
Q12888	UniProtKB	Mutagenesis	1523	1523	.	.	.	Note=Increases affinity for histone H4 that has been dimethylated at 'Lys-20'. No effect on recruitment to double strand breaks. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17190600;Dbxref=PMID:17190600	
Q12888	UniProtKB	Mutagenesis	1523	1523	.	.	.	Note=Decreases affinity for histone H4 that has been dimethylated at 'Lys-20'. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17190600;Dbxref=PMID:17190600	
Q12888	UniProtKB	Mutagenesis	1609	1609	.	.	.	Note=Constitutive recruitment to mitotic DNA lesions%2C leading to mitotic defects%3B when associated with A-1618. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24703952;Dbxref=PMID:24703952	
Q12888	UniProtKB	Mutagenesis	1609	1609	.	.	.	Note=Phosphomimetic mutant that abolishes recruitment to double strand breaks%3B when associated with D-1618. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24703952;Dbxref=PMID:24703952	
Q12888	UniProtKB	Mutagenesis	1613	1613	.	.	.	Note=Does not affect recruitment to double strand breaks. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23760478;Dbxref=PMID:23760478	
Q12888	UniProtKB	Mutagenesis	1616	1616	.	.	.	Note=Does not affect recruitment to double strand breaks. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23760478;Dbxref=PMID:23760478	
Q12888	UniProtKB	Mutagenesis	1617	1617	.	.	.	Note=Strongly reduced recruitment to double strand breaks. Defects in class-switch recombination (CSR). I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23760478;Dbxref=PMID:23760478	
Q12888	UniProtKB	Mutagenesis	1618	1618	.	.	.	Note=Constitutive recruitment to mitotic DNA lesions%2C leading to mitotic defects%3B when associated with A-1609. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24703952;Dbxref=PMID:24703952	
Q12888	UniProtKB	Mutagenesis	1618	1618	.	.	.	Note=Phosphomimetic mutant that abolishes recruitment to double strand breaks%3B when associated with E-1609. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24703952;Dbxref=PMID:24703952	
Q12888	UniProtKB	Mutagenesis	1619	1619	.	.	.	Note=Strongly reduced recruitment to double strand breaks. Defects in class-switch recombination (CSR). Does not affect interaction with histone H4 dimethylated at 'Lys-20' (H4K20me2). Impaired interaction with histone H2A monoubiquitinated at 'Lys-15' (H2AK15ub). L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23760478;Dbxref=PMID:23760478	
Q12888	UniProtKB	Mutagenesis	1621	1621	.	.	.	Note=Reduced recruitment to double strand breaks. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23760478;Dbxref=PMID:23760478	
Q12888	UniProtKB	Mutagenesis	1622	1622	.	.	.	Note=Reduced recruitment to double strand breaks. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23760478;Dbxref=PMID:23760478	
Q12888	UniProtKB	Mutagenesis	1624	1624	.	.	.	Note=Does not affect recruitment to double strand breaks. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23760478;Dbxref=PMID:23760478	
Q12888	UniProtKB	Mutagenesis	1627	1627	.	.	.	Note=Reduced recruitment to double strand breaks. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23760478;Dbxref=PMID:23760478	
Q12888	UniProtKB	Sequence conflict	796	796	.	.	.	Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q12888	UniProtKB	Sequence conflict	1600	1600	.	.	.	Note=Y->C;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q12888	UniProtKB	Sequence conflict	1958	1958	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q12888	UniProtKB	Beta strand	1490	1494	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2G3R	
Q12888	UniProtKB	Turn	1496	1498	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2G3R	
Q12888	UniProtKB	Beta strand	1501	1511	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2G3R	
Q12888	UniProtKB	Beta strand	1514	1519	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2G3R	
Q12888	UniProtKB	Beta strand	1524	1528	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2G3R	
Q12888	UniProtKB	Helix	1529	1531	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2G3R	
Q12888	UniProtKB	Beta strand	1532	1535	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LVM	
Q12888	UniProtKB	Beta strand	1543	1547	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2G3R	
Q12888	UniProtKB	Turn	1549	1551	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6VA5	
Q12888	UniProtKB	Beta strand	1553	1564	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2G3R	
Q12888	UniProtKB	Beta strand	1567	1574	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2G3R	
Q12888	UniProtKB	Beta strand	1577	1582	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2G3R	
Q12888	UniProtKB	Helix	1583	1585	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2G3R	
Q12888	UniProtKB	Beta strand	1586	1588	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2G3R	
Q12888	UniProtKB	Helix	1590	1594	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2G3R	
Q12888	UniProtKB	Helix	1597	1600	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2G3R	
Q12888	UniProtKB	Beta strand	1615	1617	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7YQK	
Q12888	UniProtKB	Turn	1674	1676	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6IUA	
Q12888	UniProtKB	Helix	1715	1719	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KZY	
Q12888	UniProtKB	Turn	1726	1731	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KZY	
Q12888	UniProtKB	Beta strand	1732	1736	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KZY	
Q12888	UniProtKB	Helix	1741	1745	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GZH	
Q12888	UniProtKB	Helix	1773	1781	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KZY	
Q12888	UniProtKB	Turn	1782	1784	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KZY	
Q12888	UniProtKB	Turn	1793	1799	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KZY	
Q12888	UniProtKB	Beta strand	1801	1808	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KZY	
Q12888	UniProtKB	Helix	1813	1821	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KZY	
Q12888	UniProtKB	Beta strand	1825	1827	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KZY	
Q12888	UniProtKB	Helix	1829	1837	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KZY	
Q12888	UniProtKB	Helix	1843	1845	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KZY	
Q12888	UniProtKB	Beta strand	1851	1853	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KZY	
Q12888	UniProtKB	Turn	1854	1857	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KZY	
Q12888	UniProtKB	Beta strand	1858	1860	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KZY	
Q12888	UniProtKB	Turn	1868	1871	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KZY	
Q12888	UniProtKB	Beta strand	1873	1879	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KZY	
Q12888	UniProtKB	Turn	1881	1884	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KZY	
Q12888	UniProtKB	Helix	1885	1894	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KZY	
Q12888	UniProtKB	Beta strand	1898	1908	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KZY	
Q12888	UniProtKB	Helix	1914	1916	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KZY	
Q12888	UniProtKB	Beta strand	1918	1922	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KZY	
Q12888	UniProtKB	Helix	1928	1937	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KZY	
Q12888	UniProtKB	Helix	1944	1953	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KZY	
Q12888	UniProtKB	Helix	1963	1965	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1KZY