##gff-version 3 Q99708 UniProtKB Chain 1 897 . . . ID=PRO_0000097179;Note=DNA endonuclease RBBP8 Q99708 UniProtKB Region 22 45 . . . Note=Essential for binding to the MRN complex and for RPA focus formation on DNA damage Q99708 UniProtKB Region 45 160 . . . Note=Required for interaction with LMO4%2C probably by stabilizing the interaction through RPPB8 dimerization;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23353824;Dbxref=PMID:23353824 Q99708 UniProtKB Region 292 325 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q99708 UniProtKB Region 419 464 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q99708 UniProtKB Region 509 557 . . . Note=Damage-recruitment motif Q99708 UniProtKB Region 641 685 . . . Note=Required for interaction with LMO4%2C probably by making physical contact with LMO4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23353824;Dbxref=PMID:23353824 Q99708 UniProtKB Region 704 723 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q99708 UniProtKB Region 873 897 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q99708 UniProtKB Coiled coil 35 84 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34129781;Dbxref=PMID:34129781 Q99708 UniProtKB Coiled coil 117 138 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34129781;Dbxref=PMID:34129781 Q99708 UniProtKB Motif 490 494 . . . Note=PXDLS motif Q99708 UniProtKB Motif 840 842 . . . Note=KLHL15-binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27561354;Dbxref=PMID:27561354 Q99708 UniProtKB Compositional bias 305 325 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q99708 UniProtKB Compositional bias 420 462 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q99708 UniProtKB Modified residue 233 233 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q99708 UniProtKB Modified residue 276 276 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23623683;Dbxref=PMID:23623683 Q99708 UniProtKB Modified residue 315 315 . . . Note=Phosphothreonine%3B by CDK2;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:23623683,ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163,PMID:23623683 Q99708 UniProtKB Modified residue 326 326 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17965729;Dbxref=PMID:17965729 Q99708 UniProtKB Modified residue 327 327 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:15485915,ECO:0007744|PubMed:23186163;Dbxref=PMID:15485915,PMID:23186163 Q99708 UniProtKB Modified residue 349 349 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17965729;Dbxref=PMID:17965729 Q99708 UniProtKB Modified residue 379 379 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q99708 UniProtKB Modified residue 664 664 . . . Note=Phosphoserine%3B by ATM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10910365;Dbxref=PMID:10910365 Q99708 UniProtKB Modified residue 679 679 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17965729;Dbxref=PMID:17965729 Q99708 UniProtKB Modified residue 723 723 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:20068231,PMID:23186163 Q99708 UniProtKB Modified residue 745 745 . . . Note=Phosphoserine%3B by ATM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10910365;Dbxref=PMID:10910365 Q99708 UniProtKB Modified residue 847 847 . . . Note=Phosphothreonine%3B by CDK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19202191;Dbxref=PMID:19202191 Q99708 UniProtKB Cross-link 62 62 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q99708 UniProtKB Cross-link 115 115 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q99708 UniProtKB Cross-link 193 193 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25755297,ECO:0007744|PubMed:28112733;Dbxref=PMID:25755297,PMID:28112733 Q99708 UniProtKB Cross-link 360 360 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q99708 UniProtKB Cross-link 378 378 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25755297,ECO:0007744|PubMed:28112733;Dbxref=PMID:25755297,PMID:28112733 Q99708 UniProtKB Cross-link 396 396 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q99708 UniProtKB Cross-link 404 404 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q99708 UniProtKB Cross-link 410 410 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q99708 UniProtKB Cross-link 438 438 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q99708 UniProtKB Cross-link 449 449 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q99708 UniProtKB Cross-link 526 526 . . . 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 Q99708 UniProtKB Cross-link 530 530 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q99708 UniProtKB Cross-link 572 572 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q99708 UniProtKB Cross-link 578 578 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q99708 UniProtKB Cross-link 604 604 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)%3B alternate;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25755297,ECO:0007744|PubMed:28112733;Dbxref=PMID:25755297,PMID:28112733 Q99708 UniProtKB Cross-link 613 613 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25755297,ECO:0007744|PubMed:28112733;Dbxref=PMID:25755297,PMID:28112733 Q99708 UniProtKB Cross-link 638 638 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q99708 UniProtKB Cross-link 640 640 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q99708 UniProtKB Cross-link 676 676 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q99708 UniProtKB Cross-link 719 719 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q99708 UniProtKB Cross-link 782 782 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q99708 UniProtKB Cross-link 869 869 . . . 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:25755297,ECO:0007744|PubMed:28112733;Dbxref=PMID:25218447,PMID:25755297,PMID:28112733 Q99708 UniProtKB Alternative sequence 714 714 . . . ID=VSP_043220;Note=In isoform 2. S->SMLFYI;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 Q99708 UniProtKB Alternative sequence 786 867 . . . ID=VSP_045247;Note=In isoform 3. RETSLQNFPHIEVVRKKEERRKLLGHTCKECEIYYADMPAEEREKKLASCSRHRFRYIPPNTPENFWEVGFPSTQTCMERGY->SIMQICQQKKEKRNWLPAQDTDSATFHPTHQRIFGKLVFLPLRLVWKEVILRKILILVLVQKDVSLTTQYFLQKARSRRHRR;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:17974005;Dbxref=PMID:17974005 Q99708 UniProtKB Alternative sequence 868 897 . . . ID=VSP_045248;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:17974005;Dbxref=PMID:17974005 Q99708 UniProtKB Natural variant 100 100 . . . ID=VAR_075824;Note=In SCKL2. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24389050;Dbxref=dbSNP:rs373804633,PMID:24389050 Q99708 UniProtKB Natural variant 357 357 . . . ID=VAR_051308;Note=K->N;Dbxref=dbSNP:rs34678569 Q99708 UniProtKB Natural variant 387 387 . . . ID=VAR_028308;Note=H->Y;Dbxref=dbSNP:rs1804732 Q99708 UniProtKB Mutagenesis 27 27 . . . Note=Can form homodimers but not homotetramers. Abolishes ability to promote homologous recombination and DNA resection. Defective binding to DNA. Defective in localizing to sites of DNA damage. Does not affect interaction with MRN complex components MRE11%2C NBN or RAD50. L->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25558984,ECO:0000269|PubMed:30601117;Dbxref=PMID:25558984,PMID:30601117 Q99708 UniProtKB Mutagenesis 31 31 . . . Note=No effect on RPA focus formation on DNA damage. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19759395;Dbxref=PMID:19759395 Q99708 UniProtKB Mutagenesis 35 35 . . . Note=No effect on RPA focus formation on DNA damage. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19759395;Dbxref=PMID:19759395 Q99708 UniProtKB Mutagenesis 41 41 . . . Note=No effect on RPA focus formation on DNA damage. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19759395;Dbxref=PMID:19759395 Q99708 UniProtKB Mutagenesis 45 45 . . . Note=No effect on RPA focus formation on DNA damage. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19759395;Dbxref=PMID:19759395 Q99708 UniProtKB Mutagenesis 62 62 . . . Note=In K12R%3B defects in ability to promoting DNA resection and homologous recombination%3B when associated with R-78%3B R-115%3B R-132%3B R-133%3B R-404%3B R-572%3B R-578%3B R-640%3B R-759%3B R-760 and R-782. In K5R%3B defects in ability to promoting DNA resection and homologous recombination%3B when associated with R-78%3B R-115%3B R-132 and R-133. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26502057;Dbxref=PMID:26502057 Q99708 UniProtKB Mutagenesis 78 78 . . . Note=In K12R%3B defects in ability to promoting DNA resection and homologous recombination%3B when associated with R-62%3B R-115%3B R-132%3B R-133%3B R-404%3B R-572%3B R-578%3B R-640%3B R-759%3B R-760 and R-782. In K5R%3B defects in ability to promoting DNA resection and homologous recombination%3B when associated with R-62%3B R-115%3B R-132 and R-133. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26502057;Dbxref=PMID:26502057 Q99708 UniProtKB Mutagenesis 89 89 . . . Note=Reduces Zn(2+) content%3B when associated with A-92. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25558984;Dbxref=PMID:25558984 Q99708 UniProtKB Mutagenesis 92 92 . . . Note=Reduces Zn(2+) content%3B when associated with A-89. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25558984;Dbxref=PMID:25558984 Q99708 UniProtKB Mutagenesis 115 115 . . . Note=In K12R%3B defects in ability to promoting DNA resection and homologous recombination%3B when associated with R-62%3B R-78%3B R-132%3B R-133%3B R-404%3B R-572%3B R-578%3B R-640%3B R-759%3B R-760 and R-782. In K5R%3B defects in ability to promoting DNA resection and homologous recombination%3B when associated with R-62%3B R-78%3B R-132 and R-133. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26502057;Dbxref=PMID:26502057 Q99708 UniProtKB Mutagenesis 132 132 . . . Note=In K12R%3B defects in ability to promoting DNA resection and homologous recombination%3B when associated with R-62%3B R-78%3B R-115%3B R-133%3B R-404%3B R-572%3B R-578%3B R-640%3B R-759%3B R-760 and R-782. In K5R%3B defects in ability to promoting DNA resection and homologous recombination%3B when associated with R-62%3B R-78%3B R-115 and R-133. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26502057;Dbxref=PMID:26502057 Q99708 UniProtKB Mutagenesis 133 133 . . . Note=In K12R%3B defects in ability to promoting DNA resection and homologous recombination%3B when associated with R-62%3B R-78%3B R-115%3B R-133%3B R-404%3B R-572%3B R-578%3B R-640%3B R-759%3B R-760 and R-782. In K5R%3B defects in ability to promoting DNA resection and homologous recombination%3B when associated with R-62%3B R-78%3B R-115 and R-132. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26502057;Dbxref=PMID:26502057 Q99708 UniProtKB Mutagenesis 179 179 . . . Note=No effect on FZR1-binding. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25349192;Dbxref=PMID:25349192 Q99708 UniProtKB Mutagenesis 276 276 . . . Note=No effect on PIN1-binding. Impaired PIN1-binding%2C partially decreased CUL3/KLHL15-mediated proteasomal degradation%2C no effect on BRCA1-%2C MRE11-%2C nor on KLHL15-binding%3B when associated with A-315. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23623683,ECO:0000269|PubMed:27561354;Dbxref=PMID:23623683,PMID:27561354 Q99708 UniProtKB Mutagenesis 315 315 . . . Note=Decreased PIN1-binding. Impaired PIN1-binding%2C partially decreased CUL3/KLHL15-mediated proteasomal degradation%2C no effect on BRCA1-%2C MRE11-%2C nor on KLHL15-binding%3B when associated with A-276. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23623683,ECO:0000269|PubMed:27561354;Dbxref=PMID:23623683,PMID:27561354 Q99708 UniProtKB Mutagenesis 327 327 . . . Note=Abolishes BRCA1 interaction and ubiquitination. No activation of CHEK1 after DNA damage. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15485915,ECO:0000269|PubMed:16818604;Dbxref=PMID:15485915,PMID:16818604 Q99708 UniProtKB Mutagenesis 404 404 . . . Note=In K12R%3B defects in ability to promoting DNA resection and homologous recombination%3B when associated with R-62%3B R-78%3B R-115%3B R-132%3B R-133%3B R-572%3B R-578%3B R-640%3B R-759%3B R-760 and R-782. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26502057;Dbxref=PMID:26502057 Q99708 UniProtKB Mutagenesis 467 467 . . . Note=Impaired FZR1-binding and APC/C-mediated polyubiquitination. Increased stability. No effect on MRE11-binding%2C nor on CUL3/KLHL15-mediated proteasomal degradation. No effect on DNA-en resection activity. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25349192,ECO:0000269|PubMed:27561354;Dbxref=PMID:25349192,PMID:27561354 Q99708 UniProtKB Mutagenesis 513 513 . . . Note=Abolishes damage recruitment capability. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20064462;Dbxref=PMID:20064462 Q99708 UniProtKB Mutagenesis 515 515 . . . Note=Abolishes damage recruitment capability. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20064462;Dbxref=PMID:20064462 Q99708 UniProtKB Mutagenesis 572 572 . . . Note=In K12R%3B defects in ability to promoting DNA resection and homologous recombination%3B when associated with R-62%3B R-78%3B R-115%3B R-132%3B R-133%3B R-404%3B R-578%3B R-640%3B R-759%3B R-760 and R-782. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26502057;Dbxref=PMID:26502057 Q99708 UniProtKB Mutagenesis 578 578 . . . Note=In K12R%3B defects in ability to promoting DNA resection and homologous recombination%3B when associated with R-62%3B R-78%3B R-115%3B R-132%3B R-133%3B R-404%3B R-572%3B R-640%3B R-759%3B R-760 and R-782. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26502057;Dbxref=PMID:26502057 Q99708 UniProtKB Mutagenesis 640 640 . . . Note=In K12R%3B defects in ability to promoting DNA resection and homologous recombination%3B when associated with R-62%3B R-78%3B R-115%3B R-132%3B R-133%3B R-404%3B R-572%3B R-578%3B R-759%3B R-760 and R-782. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26502057;Dbxref=PMID:26502057 Q99708 UniProtKB Mutagenesis 664 664 . . . Note=Abrogates dissociation of BRCA1. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10910365;Dbxref=PMID:10910365 Q99708 UniProtKB Mutagenesis 745 745 . . . Note=Abrogates dissociation of BRCA1. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10910365;Dbxref=PMID:10910365 Q99708 UniProtKB Mutagenesis 759 759 . . . Note=In K12R%3B defects in ability to promoting DNA resection and homologous recombination%3B when associated with R-62%3B R-78%3B R-115%3B R-132%3B R-133%3B R-404%3B R-572%3B R-578%3B R-640%3B R-760 and R-782. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26502057;Dbxref=PMID:26502057 Q99708 UniProtKB Mutagenesis 760 760 . . . Note=In K12R%3B defects in ability to promoting DNA resection and homologous recombination%3B when associated with R-62%3B R-78%3B R-115%3B R-132%3B R-133%3B R-404%3B R-572%3B R-578%3B R-640%3B R-759 and R-782. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26502057;Dbxref=PMID:26502057 Q99708 UniProtKB Mutagenesis 782 782 . . . Note=In K12R%3B defects in ability to promoting DNA resection and homologous recombination%3B when associated with R-62%3B R-78%3B R-115%3B R-132%3B R-133%3B R-404%3B R-572%3B R-578%3B R-640%3B R-759 and R-760. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26502057;Dbxref=PMID:26502057 Q99708 UniProtKB Mutagenesis 839 839 . . . Note=Defective binding to DNA. No effect on CUL3/KLHL15-mediated proteasomal degradation. Does not affect tetramerization. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:27561354,ECO:0000269|PubMed:30601117;Dbxref=PMID:27561354,PMID:30601117 Q99708 UniProtKB Mutagenesis 840 840 . . . Note=Decreased CUL3/KLHL15-mediated proteasomal degradation. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27561354;Dbxref=PMID:27561354 Q99708 UniProtKB Mutagenesis 842 842 . . . Note=Decreased interaction with KLHL15%2C decreased polyubiquitination and CUL3/KLHL15-mediated proteasomal degradation. No effect on DNA-end resection activity. Y->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:27561354,ECO:0000269|PubMed:35219381;Dbxref=PMID:27561354,PMID:35219381 Q99708 UniProtKB Mutagenesis 842 842 . . . Note=No effect on KLHL15-binding%2C nor on CUL3/KLHL15-mediated proteasomal degradation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27561354;Dbxref=PMID:27561354 Q99708 UniProtKB Mutagenesis 847 847 . . . Note=Impairs DNA resection. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19202191;Dbxref=PMID:19202191 Q99708 UniProtKB Mutagenesis 847 847 . . . Note=Mimics constitutive phosphorylation. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19202191;Dbxref=PMID:19202191 Q99708 UniProtKB Sequence conflict 4 4 . . . Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q99708 UniProtKB Sequence conflict 74 74 . . . Note=H->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q99708 UniProtKB Sequence conflict 92 92 . . . Note=C->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q99708 UniProtKB Sequence conflict 123 123 . . . Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q99708 UniProtKB Sequence conflict 341 341 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q99708 UniProtKB Sequence conflict 515 515 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q99708 UniProtKB Sequence conflict 521 521 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q99708 UniProtKB Sequence conflict 642 642 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q99708 UniProtKB Helix 18 50 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4D2H Q99708 UniProtKB Sequence conflict 862 862 . . . Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305