##gff-version 3
Q13426	UniProtKB	Chain	1	336	.	.	.	ID=PRO_0000066047;Note=DNA repair protein XRCC4	
Q13426	UniProtKB	Chain	266	336	.	.	.	ID=PRO_0000453296;Note=Protein XRCC4%2C C-terminus;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:33725486;Dbxref=PMID:33725486	
Q13426	UniProtKB	Region	1	213	.	.	.	Note=Interaction with IFFO1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31548606;Dbxref=PMID:31548606	
Q13426	UniProtKB	Region	180	213	.	.	.	Note=Interaction with LIG4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11702069;Dbxref=PMID:11702069	
Q13426	UniProtKB	Region	212	249	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q13426	UniProtKB	Region	264	336	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q13426	UniProtKB	Coiled coil	131	165	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q13426	UniProtKB	Coiled coil	184	212	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q13426	UniProtKB	Motif	270	275	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25934149,ECO:0000269|PubMed:33725486;Dbxref=PMID:25934149,PMID:33725486	
Q13426	UniProtKB	Compositional bias	295	318	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q13426	UniProtKB	Site	265	266	.	.	.	Note=Cleavage%3B by caspase-3;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:33725486;Dbxref=PMID:33725486	
Q13426	UniProtKB	Modified residue	53	53	.	.	.	Note=Phosphoserine%3B by PRKDC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14599745;Dbxref=PMID:14599745	
Q13426	UniProtKB	Modified residue	193	193	.	.	.	Note=Phosphoserine%3B by PRKDC;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14599745,ECO:0000269|PubMed:22228831,ECO:0000269|PubMed:28500754;Dbxref=PMID:14599745,PMID:22228831,PMID:28500754	
Q13426	UniProtKB	Modified residue	229	229	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569	
Q13426	UniProtKB	Modified residue	232	232	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28453785;Dbxref=PMID:28453785	
Q13426	UniProtKB	Modified residue	233	233	.	.	.	Note=Phosphothreonine%3B by CK2;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:15385968,ECO:0000269|PubMed:20852255,ECO:0000269|PubMed:28453785,ECO:0007744|PubMed:24275569;Dbxref=PMID:15385968,PMID:20852255,PMID:24275569,PMID:28453785	
Q13426	UniProtKB	Modified residue	237	237	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569	
Q13426	UniProtKB	Modified residue	256	256	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:20068231;Dbxref=PMID:20068231	
Q13426	UniProtKB	Modified residue	260	260	.	.	.	Note=Phosphoserine%3B by PRKDC;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:14599745,ECO:0000269|PubMed:15177042,ECO:0000269|PubMed:22228831,ECO:0000269|PubMed:28500754,ECO:0000269|PubMed:30247612,ECO:0007744|PubMed:23186163;Dbxref=PMID:14599745,PMID:15177042,PMID:22228831,PMID:23186163,PMID:28500754,PMID:30247612	
Q13426	UniProtKB	Modified residue	303	303	.	.	.	Note=Phosphoserine%3B by PRKDC;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14599745,ECO:0000269|PubMed:22228831;Dbxref=PMID:14599745,PMID:22228831	
Q13426	UniProtKB	Modified residue	304	304	.	.	.	Note=Phosphoserine%3B by PRKDC;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:28500754,ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163,PMID:28500754	
Q13426	UniProtKB	Modified residue	315	315	.	.	.	Note=Phosphoserine%3B by PRKDC;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14599745,ECO:0000269|PubMed:22228831,ECO:0000269|PubMed:28500754;Dbxref=PMID:14599745,PMID:22228831,PMID:28500754	
Q13426	UniProtKB	Modified residue	320	320	.	.	.	Note=Phosphoserine%3B by PRKDC;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:14599745,ECO:0000269|PubMed:15177042,ECO:0000269|PubMed:22228831,ECO:0000269|PubMed:26666690,ECO:0000269|PubMed:28500754,ECO:0007744|PubMed:23186163;Dbxref=PMID:14599745,PMID:15177042,PMID:22228831,PMID:23186163,PMID:26666690,PMID:28500754	
Q13426	UniProtKB	Modified residue	323	323	.	.	.	Note=Phosphothreonine%3B by PRKDC;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14599745,ECO:0000269|PubMed:22228831,ECO:0000269|PubMed:28500754;Dbxref=PMID:14599745,PMID:22228831,PMID:28500754	
Q13426	UniProtKB	Modified residue	327	327	.	.	.	Note=Phosphoserine%3B by PRKDC;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:14599745,ECO:0000269|PubMed:22228831,ECO:0000269|PubMed:26774286,ECO:0000269|PubMed:28500754,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332;Dbxref=PMID:14599745,PMID:18669648,PMID:19690332,PMID:22228831,PMID:26774286,PMID:28500754	
Q13426	UniProtKB	Modified residue	328	328	.	.	.	Note=Phosphoserine%3B by PRKDC;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:14599745,ECO:0000269|PubMed:22228831,ECO:0000269|PubMed:26774286,ECO:0000269|PubMed:28500754,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332;Dbxref=PMID:14599745,PMID:18669648,PMID:19690332,PMID:22228831,PMID:26774286,PMID:28500754	
Q13426	UniProtKB	Cross-link	210	210	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16478998;Dbxref=PMID:16478998	
Q13426	UniProtKB	Cross-link	296	296	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26774286;Dbxref=PMID:26774286	
Q13426	UniProtKB	Alternative sequence	298	336	.	.	.	ID=VSP_009474;Note=In isoform 3. NSRPDSSLPETSKKEHISAENMSLETLRNSSPEDLFDEI->KGRKKETSEKEAV;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|Ref.4;Dbxref=PMID:15489334	
Q13426	UniProtKB	Alternative sequence	298	300	.	.	.	ID=VSP_009473;Note=In isoform 2. NSR->K;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:8548796;Dbxref=PMID:8548796	
Q13426	UniProtKB	Natural variant	12	12	.	.	.	ID=VAR_022310;Note=S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.6;Dbxref=dbSNP:rs28383138	
Q13426	UniProtKB	Natural variant	43	43	.	.	.	ID=VAR_075822;Note=In SSMED%3B impairs the protein function in DNA double-strand break repair. W->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24389050,ECO:0000269|PubMed:25728776,ECO:0000269|PubMed:26255102;Dbxref=dbSNP:rs587779351,PMID:24389050,PMID:25728776,PMID:26255102	
Q13426	UniProtKB	Natural variant	56	56	.	.	.	ID=VAR_022311;Note=A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.6;Dbxref=dbSNP:rs28383151	
Q13426	UniProtKB	Natural variant	82	82	.	.	.	ID=VAR_084965;Note=In SSMED%3B impaired ability to repair DNA double-strand breaks. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25742519;Dbxref=PMID:25742519	
Q13426	UniProtKB	Natural variant	134	134	.	.	.	ID=VAR_022312;Note=I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.6;Dbxref=dbSNP:rs28360135	
Q13426	UniProtKB	Natural variant	142	142	.	.	.	ID=VAR_022313;Note=E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.6;Dbxref=dbSNP:rs28360136	
Q13426	UniProtKB	Natural variant	161	336	.	.	.	ID=VAR_084966;Note=In SSMED. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25728776;Dbxref=PMID:25728776	
Q13426	UniProtKB	Natural variant	161	161	.	.	.	ID=VAR_075823;Note=In SSMED%3B no expression of the protein is observed%3B complete loss of function in DNA double-strand break repair. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25839420;Dbxref=dbSNP:rs797045017,PMID:25839420	
Q13426	UniProtKB	Natural variant	210	336	.	.	.	ID=VAR_084967;Note=In SSMED. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32524007;Dbxref=PMID:32524007	
Q13426	UniProtKB	Natural variant	225	336	.	.	.	ID=VAR_084968;Note=In SSMED. Missing;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25728776,ECO:0000269|PubMed:25872942,ECO:0000269|PubMed:26255102;Dbxref=PMID:25728776,PMID:25872942,PMID:26255102	
Q13426	UniProtKB	Natural variant	240	240	.	.	.	ID=VAR_017810;Note=Q->P;Dbxref=dbSNP:rs2974446	
Q13426	UniProtKB	Natural variant	247	247	.	.	.	ID=VAR_017811;Note=A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.6;Dbxref=dbSNP:rs3734091	
Q13426	UniProtKB	Natural variant	275	336	.	.	.	ID=VAR_084969;Note=In SSMED. Missing;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25728776,ECO:0000269|PubMed:25839420;Dbxref=PMID:25728776,PMID:25839420	
Q13426	UniProtKB	Mutagenesis	4	4	.	.	.	Note=Abolished interaction with NHEJ1/XLF%3B when associated with E-99. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18158905;Dbxref=PMID:18158905	
Q13426	UniProtKB	Mutagenesis	26	26	.	.	.	Note=Abolished interaction with NHEJ1/XLF%3B when associated with E-99. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18158905;Dbxref=PMID:18158905	
Q13426	UniProtKB	Mutagenesis	55	55	.	.	.	Note=Abolished interaction with NHEJ1/XLF. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21768349;Dbxref=PMID:21768349	
Q13426	UniProtKB	Mutagenesis	58	58	.	.	.	Note=Abolished interaction with NHEJ1/XLF. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21768349;Dbxref=PMID:21768349	
Q13426	UniProtKB	Mutagenesis	61	61	.	.	.	Note=Abolished interaction with NHEJ1/XLF. M->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21768349;Dbxref=PMID:21768349	
Q13426	UniProtKB	Mutagenesis	62	62	.	.	.	Note=Does not affect interaction with NHEJ1/XLF. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21768349;Dbxref=PMID:21768349	
Q13426	UniProtKB	Mutagenesis	65	65	.	.	.	Note=Strongly decreased interaction with NHEJ1/XLF. Abolished interaction with NHEJ1/XLF%3B when associated with E-99. Abolished ability to bridge DNA%3B when associated with E-99. Abolished interaction with NHEJ1/XLF%3B when associated with E-102. K->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18158905,ECO:0000269|PubMed:21768349,ECO:0000269|PubMed:22287571;Dbxref=PMID:18158905,PMID:21768349,PMID:22287571	
Q13426	UniProtKB	Mutagenesis	69	69	.	.	.	Note=Does not affect interaction with NHEJ1/XLF. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21768349;Dbxref=PMID:21768349	
Q13426	UniProtKB	Mutagenesis	71	71	.	.	.	Note=Abolished interaction with NHEJ1/XLF%3B when associated with E-99. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18158905;Dbxref=PMID:18158905	
Q13426	UniProtKB	Mutagenesis	72	72	.	.	.	Note=Abolished interaction with NHEJ1/XLF%3B when associated with E-99. Abolished ability to bridge DNA%3B when associated with E-90 and E-99. K->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18158905,ECO:0000269|PubMed:22287571;Dbxref=PMID:18158905,PMID:22287571	
Q13426	UniProtKB	Mutagenesis	90	90	.	.	.	Note=Abolished ability to bridge DNA%3B when associated with E-72 and E-99. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22287571;Dbxref=PMID:22287571	
Q13426	UniProtKB	Mutagenesis	99	99	.	.	.	Note=Abolished interaction with NHEJ1/XLF%3B when associated with E-4 or E-26 or E-65 or E-71 or E-72. Abolished ability to bridge DNA%3B when associated with E-65. Abolished ability to bridge DNA%3B when associated with E-72 and E-90. K->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18158905,ECO:0000269|PubMed:22287571;Dbxref=PMID:18158905,PMID:22287571	
Q13426	UniProtKB	Mutagenesis	102	102	.	.	.	Note=Abolished interaction with NHEJ1/XLF%3B when associated with E-65. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18158905;Dbxref=PMID:18158905	
Q13426	UniProtKB	Mutagenesis	106	106	.	.	.	Note=Abolished interaction with NHEJ1/XLF. F->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21768349;Dbxref=PMID:21768349	
Q13426	UniProtKB	Mutagenesis	140	140	.	.	.	Note=No change in sumoylation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16478998;Dbxref=PMID:16478998	
Q13426	UniProtKB	Mutagenesis	170	170	.	.	.	Note=Abolished DNA-binding. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22287571;Dbxref=PMID:22287571	
Q13426	UniProtKB	Mutagenesis	192	192	.	.	.	Note=Abolished DNA-binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22287571;Dbxref=PMID:22287571	
Q13426	UniProtKB	Mutagenesis	193	193	.	.	.	Note=In XRCC4-Ala mutant%3B abolished phosphorylation by PRKDC%3B does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant%3B when associated with A-260%2C A-304%2C A-315%2C A-320%2C A-323%2C A-327 and A-328. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28500754;Dbxref=PMID:28500754	
Q13426	UniProtKB	Mutagenesis	193	193	.	.	.	Note=In XRCC4-Asp mutant%3B phospho-mimetic mutant%3B abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant%3B when associated with D-260%2C D-304%2C D-315%2C D-320%2C D-323%2C D-327 and D-328. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28500754;Dbxref=PMID:28500754	
Q13426	UniProtKB	Mutagenesis	210	210	.	.	.	Note=Abolishes sumoylation. 5-fold decrease in recombination efficiency. Does not affect nuclear localization of XRCC4 and LIG4. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16478998,ECO:0000269|PubMed:25934149;Dbxref=PMID:16478998,PMID:25934149	
Q13426	UniProtKB	Mutagenesis	233	233	.	.	.	Note=Abolished phosphorylation by CK2%2C leading to strongly reduced interaction with PNKP. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15385968;Dbxref=PMID:15385968	
Q13426	UniProtKB	Mutagenesis	235	235	.	.	.	Note=Impaired ability mediate double-strand break repair. E->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25597996;Dbxref=PMID:25597996	
Q13426	UniProtKB	Mutagenesis	260	260	.	.	.	Note=Reduced phosphorylation by PRKDC. In XRCC4-Ala mutant%3B abolished phosphorylation by PRKDC%3B does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant%3B when associated with A-193%2C A-304%2C A-315%2C A-320%2C A-323%2C A-327 and A-328. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14599745,ECO:0000269|PubMed:28500754,ECO:0000269|PubMed:30247612;Dbxref=PMID:14599745,PMID:28500754,PMID:30247612	
Q13426	UniProtKB	Mutagenesis	260	260	.	.	.	Note=In XRCC4-Asp mutant%3B phospho-mimetic mutant%3B abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant%3B when associated with D-193%2C D-304%2C D-315%2C D-320%2C D-323%2C D-327 and D-328. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28500754;Dbxref=PMID:28500754	
Q13426	UniProtKB	Mutagenesis	262	265	.	.	.	Note=In 2DA%3B abolished cleavage by caspase and ability to regulate phospholipid scramblase activity. DVTD->AVTA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33725486;Dbxref=PMID:33725486	
Q13426	UniProtKB	Mutagenesis	264	264	.	.	.	Note=Does not affect phosphorylation by CK2. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15385968;Dbxref=PMID:15385968	
Q13426	UniProtKB	Mutagenesis	266	266	.	.	.	Note=Abolished cleavage by caspase and ability to regulate phospholipid scramblase activity. I->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33725486;Dbxref=PMID:33725486	
Q13426	UniProtKB	Mutagenesis	270	270	.	.	.	Note=Impaired ability to localize in the nucleus. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33725486;Dbxref=PMID:33725486	
Q13426	UniProtKB	Mutagenesis	271	271	.	.	.	Note=Impaired ability to localize in the nucleus%2C without affecting ability to activate phospholipid scramblase activity of XKR4. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33725486;Dbxref=PMID:33725486	
Q13426	UniProtKB	Mutagenesis	271	271	.	.	.	Note=Abolished nuclear localization of XRCC4 and LIG4. Impaired ability to repair DNA double-strand breaks (DSBs). Reduced ubiquitination by the SCF(FBXW7) complex caused by impaired localization to the nucleus. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25934149,ECO:0000269|PubMed:26774286;Dbxref=PMID:25934149,PMID:26774286	
Q13426	UniProtKB	Mutagenesis	272	272	.	.	.	Note=Impaired ability to localize in the nucleus%2C without affecting ability to activate phospholipid scramblase activity of XKR4. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33725486;Dbxref=PMID:33725486	
Q13426	UniProtKB	Mutagenesis	273	273	.	.	.	Note=Impaired ability to localize in the nucleus%2C without affecting ability to activate phospholipid scramblase activity of XKR4. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33725486;Dbxref=PMID:33725486	
Q13426	UniProtKB	Mutagenesis	275	275	.	.	.	Note=Does not affect ability to localize into the nucleus. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33725486;Dbxref=PMID:33725486	
Q13426	UniProtKB	Mutagenesis	282	282	.	.	.	Note=Does not affect phosphorylation by CK2. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15385968;Dbxref=PMID:15385968	
Q13426	UniProtKB	Mutagenesis	285	285	.	.	.	Note=Does not affect ubiquitination by the SCF(FBXW7) complex. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26774286;Dbxref=PMID:26774286	
Q13426	UniProtKB	Mutagenesis	296	296	.	.	.	Note=Abolished ubiquitination by the SCF(FBXW7) complex. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26774286;Dbxref=PMID:26774286	
Q13426	UniProtKB	Mutagenesis	304	304	.	.	.	Note=In XRCC4-Ala mutant%3B abolished phosphorylation by PRKDC%3B does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant%3B when associated with A-193%2C A-260%2C A-315%2C A-320%2C A-323%2C A-327 and A-328. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28500754;Dbxref=PMID:28500754	
Q13426	UniProtKB	Mutagenesis	304	304	.	.	.	Note=In XRCC4-Asp mutant%3B phospho-mimetic mutant%3B abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant%3B when associated with D-193%2C D-260%2C D-315%2C D-320%2C D-323%2C D-327 and D-328. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28500754;Dbxref=PMID:28500754	
Q13426	UniProtKB	Mutagenesis	308	308	.	.	.	Note=Does not affect phosphorylation by CK2. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15385968;Dbxref=PMID:15385968	
Q13426	UniProtKB	Mutagenesis	308	308	.	.	.	Note=Does not affect ubiquitination by the SCF(FBXW7) complex. T->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26774286;Dbxref=PMID:26774286	
Q13426	UniProtKB	Mutagenesis	315	315	.	.	.	Note=In XRCC4-Ala mutant%3B abolished phosphorylation by PRKDC%3B does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant%3B when associated with A-193%2C A-260%2C A-304%2C A-320%2C A-323%2C A-327 and A-328. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28500754;Dbxref=PMID:28500754	
Q13426	UniProtKB	Mutagenesis	315	315	.	.	.	Note=In XRCC4-Asp mutant%3B phospho-mimetic mutant%3B abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant%3B when associated with D-193%2C D-260%2C D-304%2C D-320%2C D-323%2C D-327 and D-328. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28500754;Dbxref=PMID:28500754	
Q13426	UniProtKB	Mutagenesis	320	320	.	.	.	Note=Slightly reduced phosphorylation by PRKDC. In XRCC4-Ala mutant%3B abolished phosphorylation by PRKDC%3B does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant%3B when associated with A-193%2C A-260%2C A-304%2C A-315%2C A-323%2C A-327 and A-328. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14599745,ECO:0000269|PubMed:28500754;Dbxref=PMID:14599745,PMID:28500754	
Q13426	UniProtKB	Mutagenesis	320	320	.	.	.	Note=In XRCC4-Asp mutant%3B phospho-mimetic mutant%3B abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant%3B when associated with D-193%2C D-260%2C D-304%2C D-315%2C D-323%2C D-327 and D-328. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28500754;Dbxref=PMID:28500754	
Q13426	UniProtKB	Mutagenesis	322	322	.	.	.	Note=Does not affect ability mediate double-strand break repair. E->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25597996;Dbxref=PMID:25597996	
Q13426	UniProtKB	Mutagenesis	323	323	.	.	.	Note=In XRCC4-Ala mutant%3B abolished phosphorylation by PRKDC%3B does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant%3B when associated with A-193%2C A-260%2C A-304%2C A-315%2C A-320%2C A-327 and A-328. Does not affect phosphorylation by CK2. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15385968,ECO:0000269|PubMed:28500754;Dbxref=PMID:15385968,PMID:28500754	
Q13426	UniProtKB	Mutagenesis	323	323	.	.	.	Note=Does not affect ability mediate double-strand break repair. In XRCC4-Asp mutant%3B phospho-mimetic mutant%3B abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant%3B when associated with D-193%2C D-260%2C D-304%2C D-315%2C D-320%2C D-327 and D-328. T->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25597996,ECO:0000269|PubMed:28500754;Dbxref=PMID:25597996,PMID:28500754	
Q13426	UniProtKB	Mutagenesis	324	324	.	.	.	Note=Does not affect ability mediate double-strand break repair. L->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25597996;Dbxref=PMID:25597996	
Q13426	UniProtKB	Mutagenesis	326	326	.	.	.	Note=Abolished ability mediate double-strand break repair%3B impaired nuclear localization. N->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25597996;Dbxref=PMID:25597996	
Q13426	UniProtKB	Mutagenesis	327	328	.	.	.	Note=Reduced ubiquitination by the SCF(FBXW7) complex. SS->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26774286;Dbxref=PMID:26774286	
Q13426	UniProtKB	Mutagenesis	327	327	.	.	.	Note=In XRCC4-Ala mutant%3B abolished phosphorylation by PRKDC%3B does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant%3B when associated with A-193%2C A-260%2C A-304%2C A-315%2C A-320%2C A-323 and A-328. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28500754;Dbxref=PMID:28500754	
Q13426	UniProtKB	Mutagenesis	327	327	.	.	.	Note=Does not affect ability mediate double-strand break repair. In XRCC4-Asp mutant%3B phospho-mimetic mutant%3B abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant%3B when associated with D-193%2C D-260%2C D-304%2C D-315%2C D-320%2C D-323 and D-328. S->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25597996,ECO:0000269|PubMed:28500754;Dbxref=PMID:25597996,PMID:28500754	
Q13426	UniProtKB	Mutagenesis	328	328	.	.	.	Note=In XRCC4-Ala mutant%3B abolished phosphorylation by PRKDC%3B does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant%3B when associated with A-193%2C A-260%2C A-304%2C A-315%2C A-320%2C A-323 and A-327. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28500754;Dbxref=PMID:28500754	
Q13426	UniProtKB	Mutagenesis	328	328	.	.	.	Note=Does not affect ability mediate double-strand break repair. In XRCC4-Asp mutant%3B phospho-mimetic mutant%3B abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant%3B when associated with D-193%2C D-260%2C D-304%2C D-315%2C D-320%2C D-323 and D-327. S->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25597996,ECO:0000269|PubMed:28500754;Dbxref=PMID:25597996,PMID:28500754	
Q13426	UniProtKB	Mutagenesis	329	329	.	.	.	Note=Does not affect ability mediate double-strand break repair. P->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25597996;Dbxref=PMID:25597996	
Q13426	UniProtKB	Mutagenesis	330	330	.	.	.	Note=Does not affect ability mediate double-strand break repair. E->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25597996;Dbxref=PMID:25597996	
Q13426	UniProtKB	Mutagenesis	331	331	.	.	.	Note=Does not affect ability mediate double-strand break repair. D->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25597996;Dbxref=PMID:25597996	
Q13426	UniProtKB	Mutagenesis	332	332	.	.	.	Note=Does not affect ability mediate double-strand break repair. L->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25597996;Dbxref=PMID:25597996	
Q13426	UniProtKB	Mutagenesis	333	333	.	.	.	Note=Does not affect ability mediate double-strand break repair. F->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25597996;Dbxref=PMID:25597996	
Q13426	UniProtKB	Mutagenesis	334	334	.	.	.	Note=Does not affect ability mediate double-strand break repair. D->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25597996;Dbxref=PMID:25597996	
Q13426	UniProtKB	Beta strand	2	10	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7M3P	
Q13426	UniProtKB	Beta strand	13	26	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7M3P	
Q13426	UniProtKB	Helix	28	30	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7M3P	
Q13426	UniProtKB	Beta strand	31	37	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7M3P	
Q13426	UniProtKB	Beta strand	42	48	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7M3P	
Q13426	UniProtKB	Helix	49	58	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7M3P	
Q13426	UniProtKB	Helix	63	74	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7M3P	
Q13426	UniProtKB	Turn	79	81	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WJ7	
Q13426	UniProtKB	Beta strand	84	89	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7M3P	
Q13426	UniProtKB	Turn	90	93	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7M3P	
Q13426	UniProtKB	Beta strand	94	101	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7M3P	
Q13426	UniProtKB	Beta strand	104	112	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7M3P	
Q13426	UniProtKB	Helix	119	132	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7M3P	
Q13426	UniProtKB	Helix	142	145	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5CJ4	
Q13426	UniProtKB	Turn	173	176	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FU1	
Q13426	UniProtKB	Helix	179	201	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1FU1