##gff-version 3 Q9Y6D9 UniProtKB Chain 1 718 . . . ID=PRO_0000213800;Note=Mitotic spindle assembly checkpoint protein MAD1 Q9Y6D9 UniProtKB Region 301 340 . . . Note=Important for interaction with IK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22351768;Dbxref=PMID:22351768 Q9Y6D9 UniProtKB Region 380 532 . . . Note=Necessary for interaction with NEK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14978040;Dbxref=PMID:14978040 Q9Y6D9 UniProtKB Region 439 480 . . . Note=Important for interaction with IK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22351768;Dbxref=PMID:22351768 Q9Y6D9 UniProtKB Region 540 551 . . . Note=Necessary for interaction with MAD2L1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19010891;Dbxref=PMID:19010891 Q9Y6D9 UniProtKB Coiled coil 46 632 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y6D9 UniProtKB Motif 79 82 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19010891;Dbxref=PMID:19010891 Q9Y6D9 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:22223895,ECO:0007744|PubMed:22814378;Dbxref=PMID:22223895,PMID:22814378 Q9Y6D9 UniProtKB Modified residue 16 16 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:23186163 Q9Y6D9 UniProtKB Modified residue 61 61 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 Q9Y6D9 UniProtKB Modified residue 214 214 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:17525332;Dbxref=PMID:17525332 Q9Y6D9 UniProtKB Modified residue 428 428 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:16964243,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:16964243,PMID:18669648,PMID:20068231,PMID:23186163 Q9Y6D9 UniProtKB Modified residue 598 598 . . . Note=Phosphoserine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:29162720;Dbxref=PMID:29162720 Q9Y6D9 UniProtKB Modified residue 610 610 . . . Note=Phosphoserine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:29162720;Dbxref=PMID:29162720 Q9Y6D9 UniProtKB Modified residue 634 634 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:29162720;Dbxref=PMID:29162720 Q9Y6D9 UniProtKB Modified residue 716 716 . . . Note=Phosphothreonine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:29162720;Dbxref=PMID:29162720 Q9Y6D9 UniProtKB Cross-link 61 61 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)%3B alternate;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25218447,ECO:0007744|PubMed:28112733;Dbxref=PMID:25218447,PMID:28112733 Q9Y6D9 UniProtKB Alternative sequence 1 65 . . . ID=VSP_056160;Note=In isoform 2. MEDLGENTMVLSTLRSLNNFISQRVEGGSGLDISTSAPGSLQMQYQQSMQLEERAEQIRSKSHLI->MLPARGCVRKRTVWPRLARVLIVTLLTLELSYAPLPCQLSGVPYNTGDPVGRWARPCIWPCPWHT;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q9Y6D9 UniProtKB Alternative sequence 51 97 . . . ID=VSP_061075;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:19010891;Dbxref=PMID:19010891 Q9Y6D9 UniProtKB Alternative sequence 66 157 . . . ID=VSP_056161;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q9Y6D9 UniProtKB Natural variant 29 29 . . . ID=VAR_019707;Note=In a lymphoid cancer cell line%3B somatic mutation. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11423979;Dbxref=PMID:11423979 Q9Y6D9 UniProtKB Natural variant 59 59 . . . ID=VAR_019708;Note=In a prostate cancer cell line%3B somatic mutation. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11423979;Dbxref=dbSNP:rs121908982,PMID:11423979 Q9Y6D9 UniProtKB Natural variant 66 718 . . . ID=VAR_087991;Note=In MVA7%3B decreased protein abundance in cells from the patient and from his heterozygous parents. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36322655;Dbxref=PMID:36322655 Q9Y6D9 UniProtKB Natural variant 160 160 . . . ID=VAR_019709;Note=N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10597320;Dbxref=dbSNP:rs550573452,PMID:10597320 Q9Y6D9 UniProtKB Natural variant 299 299 . . . ID=VAR_019710;Note=In lung cancer cell line%3B somatic mutation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10597320;Dbxref=PMID:10597320 Q9Y6D9 UniProtKB Natural variant 360 360 . . . ID=VAR_019711;Note=In a prostate cancer cell line%3B somatic mutation. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11423979;Dbxref=dbSNP:rs769418574,PMID:11423979 Q9Y6D9 UniProtKB Natural variant 500 500 . . . ID=VAR_019712;Note=T->M;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10597320,ECO:0000269|PubMed:11423979;Dbxref=dbSNP:rs193231481,PMID:10597320,PMID:11423979 Q9Y6D9 UniProtKB Natural variant 511 511 . . . ID=VAR_019713;Note=E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10597320;Dbxref=dbSNP:rs377555260,PMID:10597320 Q9Y6D9 UniProtKB Natural variant 516 516 . . . ID=VAR_019714;Note=In a breast cancer cell line%3B somatic mutation. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11423979;Dbxref=PMID:11423979 Q9Y6D9 UniProtKB Natural variant 556 556 . . . ID=VAR_019715;Note=In a prostate cancer cell line%3B somatic mutation. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11423979;Dbxref=dbSNP:rs371561369,PMID:11423979 Q9Y6D9 UniProtKB Natural variant 556 556 . . . ID=VAR_019716;Note=In one individual with lung cancer. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10597320;Dbxref=dbSNP:rs755012008,PMID:10597320 Q9Y6D9 UniProtKB Natural variant 558 558 . . . ID=VAR_019717;Note=In a cancer cell line. R->H;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10366450,ECO:0000269|PubMed:10597320,ECO:0000269|PubMed:11423979;Dbxref=dbSNP:rs1801368,PMID:10366450,PMID:10597320,PMID:11423979 Q9Y6D9 UniProtKB Natural variant 569 569 . . . ID=VAR_019718;Note=In a breast cancer cell line%3B somatic mutation. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11423979;Dbxref=dbSNP:rs201951163,PMID:11423979 Q9Y6D9 UniProtKB Natural variant 572 572 . . . ID=VAR_019719;Note=In a cancer cell line. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10366450;Dbxref=dbSNP:rs1801500,PMID:10366450 Q9Y6D9 UniProtKB Natural variant 628 718 . . . ID=VAR_087992;Note=In MVA7%3B decreased protein abundance in cells from the patient and from his heterozygous parents. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:36322655;Dbxref=PMID:36322655 Q9Y6D9 UniProtKB Mutagenesis 1 485 . . . Note=Defective dimerization. Abolishes binding to the closed and open conformations of MAD2L1. Impairs mitotic checkpoint signaling abolishing mitotic arrest%2C and shortens the duration of mitosis. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29162720;Dbxref=PMID:29162720 Q9Y6D9 UniProtKB Mutagenesis 79 82 . . . Note=Loss of nuclear localization. KRAR->LLAL;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19010891;Dbxref=PMID:19010891 Q9Y6D9 UniProtKB Mutagenesis 540 551 . . . Note=Loss of interaction with MAD2L1. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19010891;Dbxref=PMID:19010891 Q9Y6D9 UniProtKB Mutagenesis 541 541 . . . Note=Abolishes binding to closed and open conformations of MAD2L1 and impairs mitotic checkpint signaling abolishing mitotic arrest%2C and shortens the duration of mitosis%3B in association with A-543. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29162720;Dbxref=PMID:29162720 Q9Y6D9 UniProtKB Mutagenesis 543 543 . . . Note=Abolishes binding to closed and open conformations of MAD2L1 and impairs mitotic checkpoint signaling abolishing mitotic arrest%2C and shortens the duration of mitosis%3B in association with A-541. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29162720;Dbxref=PMID:29162720 Q9Y6D9 UniProtKB Mutagenesis 597 718 . . . Note=Defective dimerization. Reduces binding to the closed and open conformations of MAD2L1. Impairs mitotic checkpoint signaling abolishing mitotic arrest%2C and shortens the duration of mitosis. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29162720;Dbxref=PMID:29162720 Q9Y6D9 UniProtKB Mutagenesis 598 598 . . . Note=Does not impact the duration of mitosis. S->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29162720;Dbxref=PMID:29162720 Q9Y6D9 UniProtKB Mutagenesis 610 610 . . . Note=Impairs mitotic checkpoint signaling and shortens the duration of mitosis. S->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29162720;Dbxref=PMID:29162720 Q9Y6D9 UniProtKB Mutagenesis 634 634 . . . Note=Reduces binding to closed and open conformations of MAD2L1. Impairs mitotic checkpoint signaling abolishing mitotic arrest%2C and shortens the duration of mitosis. Y->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29162720;Dbxref=PMID:29162720 Q9Y6D9 UniProtKB Mutagenesis 634 634 . . . Note=Reduces binding to closed and open conformations of MAD2L1. Does not impact the duration of mitosis. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29162720;Dbxref=PMID:29162720 Q9Y6D9 UniProtKB Mutagenesis 716 716 . . . Note=Reduces binding to closed and open conformations of MAD2L1. Impairs mitotic checkpoint signaling and shortens the duration of mitosis. T->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29162720;Dbxref=PMID:29162720 Q9Y6D9 UniProtKB Sequence conflict 189 190 . . . Note=EL->DV;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Y6D9 UniProtKB Sequence conflict 260 260 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Y6D9 UniProtKB Sequence conflict 268 268 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Y6D9 UniProtKB Helix 487 492 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GO4 Q9Y6D9 UniProtKB Helix 494 528 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GO4 Q9Y6D9 UniProtKB Turn 537 539 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GO4 Q9Y6D9 UniProtKB Beta strand 540 547 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GO4 Q9Y6D9 UniProtKB Helix 549 575 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GO4 Q9Y6D9 UniProtKB Turn 580 582 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1GO4 Q9Y6D9 UniProtKB Helix 598 637 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7B1F Q9Y6D9 UniProtKB Beta strand 638 643 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7B1F Q9Y6D9 UniProtKB Beta strand 647 653 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7B1F Q9Y6D9 UniProtKB Beta strand 657 660 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7B1J Q9Y6D9 UniProtKB Beta strand 663 667 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7B1F Q9Y6D9 UniProtKB Beta strand 670 672 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7B1H Q9Y6D9 UniProtKB Beta strand 675 677 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7B1F Q9Y6D9 UniProtKB Helix 681 685 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7B1F Q9Y6D9 UniProtKB Helix 687 693 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7B1F Q9Y6D9 UniProtKB Turn 694 696 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7B1F Q9Y6D9 UniProtKB Helix 700 715 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7B1F