##gff-version 3 Q9UKT4 UniProtKB Chain 1 447 . . . ID=PRO_0000119881;Note=F-box only protein 5 Q9UKT4 UniProtKB Domain 250 296 . . . Note=F-box Q9UKT4 UniProtKB Zinc finger 374 422 . . . Note=ZBR-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01220 Q9UKT4 UniProtKB Region 135 244 . . . Note=Interaction with EVI5;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16439210;Dbxref=PMID:16439210 Q9UKT4 UniProtKB Region 261 409 . . . Note=Requires for efficient binding to CDC20;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q7TSG3 Q9UKT4 UniProtKB Region 261 339 . . . Note=Sufficient for interaction with RPS6KA2%3B Prevents association of CDC20 with RPS6KA2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q7TSG3 Q9UKT4 UniProtKB Region 305 447 . . . Note=Inhibits APC ubiquitin ligase activity;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23708605;Dbxref=PMID:23708605 Q9UKT4 UniProtKB Region 322 325 . . . Note=Competitively blocks access of APC substrates to the D-box coreceptor formed by FZR1 and ANAPC10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23708001;Dbxref=PMID:23708001 Q9UKT4 UniProtKB Region 337 358 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9UKT4 UniProtKB Region 378 420 . . . Note=Allows a rapid multiple mono-ubiquitination of the APC substrate%2C but strongly inhibits the slow ubiquitin chain elongation catalyzed by UBCH10;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23708001;Dbxref=PMID:23708001 Q9UKT4 UniProtKB Region 437 447 . . . Note=Sufficient to suppress UBE2S activity%3B essential for interaction with UBE2S%3B competitively inhibits the rapide ubiquitin chain elongation by UBE2D1 which blocks UBE2D1 with APC%3B indispensable for recruitment and position of FBXO5 to the catalytic site of APC%3B abrogates the inhibition of ubiquitin chain assembly primarily catalyzed by UBE2S%3B inhibits the ubiquitination by either UBE2C or UBE2D1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23708001;Dbxref=PMID:23708001 Q9UKT4 UniProtKB Compositional bias 343 357 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9UKT4 UniProtKB Binding site 378 378 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01220 Q9UKT4 UniProtKB Binding site 381 381 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01220 Q9UKT4 UniProtKB Binding site 396 396 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01220 Q9UKT4 UniProtKB Binding site 401 401 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01220 Q9UKT4 UniProtKB Binding site 406 406 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01220 Q9UKT4 UniProtKB Binding site 409 409 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01220 Q9UKT4 UniProtKB Binding site 414 414 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01220 Q9UKT4 UniProtKB Binding site 419 419 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01220 Q9UKT4 UniProtKB Modified residue 94 94 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q7TSG3 Q9UKT4 UniProtKB Modified residue 102 102 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q9UKT4 UniProtKB Alternative sequence 1 46 . . . ID=VSP_041362;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q9UKT4 UniProtKB Natural variant 107 107 . . . ID=VAR_024440;Note=Q->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14702039,ECO:0000269|PubMed:15489334;Dbxref=dbSNP:rs2073260,PMID:14702039,PMID:15489334 Q9UKT4 UniProtKB Natural variant 164 164 . . . ID=VAR_049038;Note=L->F;Dbxref=dbSNP:rs7763565 Q9UKT4 UniProtKB Mutagenesis 143 143 . . . Note=Delays degradation. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15469984;Dbxref=PMID:15469984 Q9UKT4 UniProtKB Mutagenesis 144 144 . . . Note=Does not affect protein stability. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17485488;Dbxref=PMID:17485488 Q9UKT4 UniProtKB Mutagenesis 145 145 . . . Note=Does not affect protein stability%3B when associated with A-149. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17485488;Dbxref=PMID:17485488 Q9UKT4 UniProtKB Mutagenesis 145 145 . . . Note=Degraded in similar manner to wild-type. S->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12791267,ECO:0000269|PubMed:15148369,ECO:0000269|PubMed:15469984;Dbxref=PMID:12791267,PMID:15148369,PMID:15469984 Q9UKT4 UniProtKB Mutagenesis 145 145 . . . Note=Not mitotically degraded. Shows impaired interaction with BTRC and reduced phosphate incorporation%3B when associated with N-149. S->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12791267,ECO:0000269|PubMed:15148369,ECO:0000269|PubMed:15469984;Dbxref=PMID:12791267,PMID:15148369,PMID:15469984 Q9UKT4 UniProtKB Mutagenesis 146 146 . . . Note=Does not affect protein stability. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17485488;Dbxref=PMID:17485488 Q9UKT4 UniProtKB Mutagenesis 148 148 . . . Note=Degraded in similar manner to wild-type. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15469984;Dbxref=PMID:15469984 Q9UKT4 UniProtKB Mutagenesis 149 149 . . . Note=Does not affect protein stability%3B when associated with A-145. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17485488;Dbxref=PMID:17485488 Q9UKT4 UniProtKB Mutagenesis 149 149 . . . Note=Degraded in similar manner to wild-type. S->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12791267,ECO:0000269|PubMed:15148369,ECO:0000269|PubMed:15469984;Dbxref=PMID:12791267,PMID:15148369,PMID:15469984 Q9UKT4 UniProtKB Mutagenesis 149 149 . . . Note=Not mitotically degraded. Shows impaired interaction with BTRC and reduced phosphate incorporation%3B when associated with N-145. S->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12791267,ECO:0000269|PubMed:15148369,ECO:0000269|PubMed:15469984;Dbxref=PMID:12791267,PMID:15148369,PMID:15469984 Q9UKT4 UniProtKB Mutagenesis 182 182 . . . Note=Shows impaired interaction with BTRC. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12791267;Dbxref=PMID:12791267 Q9UKT4 UniProtKB Mutagenesis 210 216 . . . Note=Loss of interaction with EVI5. KRNPKVD->AAAAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16439210;Dbxref=PMID:16439210 Q9UKT4 UniProtKB Mutagenesis 322 325 . . . Note=Does not affect inhibition of UBE2S-catalyzed chain elongation. Efficiently inhibits the degradation of PTTG1 at relatively high concentration. Reduces the competitive ability of FBXO5 to inhibit the association of PTTG1 to APC. Cannot compete with the APC substrate for APC binding. Decreases inhibition of CCNB1 ubiquitination by UBE2C. RTPL->ATPA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23708001,ECO:0000269|PubMed:23708605;Dbxref=PMID:23708001,PMID:23708605 Q9UKT4 UniProtKB Mutagenesis 339 345 . . . Note=Impairs CCNB1 ubiquitination by UBE2C%3B when associated with 356-Y--R-358 del. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23708605;Dbxref=PMID:23708605 Q9UKT4 UniProtKB Mutagenesis 345 345 . . . Note=Substantially impairs inhibition of CCNB1 ubiquitination by UBE2C%3B when associated with 346-S--T-355 del. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23708605;Dbxref=PMID:23708605 Q9UKT4 UniProtKB Mutagenesis 346 355 . . . Note=Inhibits CCNB1 ubiquitination by UBE2C. Substantially impairs inhibition of CCNB1 ubiquitination by UBE2C%3B when associated with A-345%3B A-356 and A-358. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23708605;Dbxref=PMID:23708605 Q9UKT4 UniProtKB Mutagenesis 356 358 . . . Note=Impairs CCNB1 ubiquitination by UBE2C%3B when associated with 339-K--L-345 del. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23708605;Dbxref=PMID:23708605 Q9UKT4 UniProtKB Mutagenesis 356 356 . . . Note=Substantially impairs inhibition of CCNB1 ubiquitination by UBE2C%3B when associated with 346-S--T-355 del. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23708605;Dbxref=PMID:23708605 Q9UKT4 UniProtKB Mutagenesis 358 358 . . . Note=Substantially impairs inhibition of CCNB1 ubiquitination by UBE2C%3B when associated with 346-S--T-355 del. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23708605;Dbxref=PMID:23708605 Q9UKT4 UniProtKB Mutagenesis 375 375 . . . Note=Decreases UBE2C-mediated ubiquitination. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23708605;Dbxref=PMID:23708605 Q9UKT4 UniProtKB Mutagenesis 376 376 . . . Note=Decreases UBE2C-mediated ubiquitination. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23708605;Dbxref=PMID:23708605 Q9UKT4 UniProtKB Mutagenesis 393 393 . . . Note=Decreases UBE2C-mediated ubiquitination. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23708605;Dbxref=PMID:23708605 Q9UKT4 UniProtKB Mutagenesis 401 401 . . . Note=Reduced inhibition of APC. Does not affect the FBXO5-mediated inhibitory activity against ubiquitin chain assembly. Does not affect the FBXO5-mediated inhibitory activity against ubiquitin chain assembly%3B when associated with S-401. Does not affect inhibition of UBE2S-catalyzed chain elongation. Reduces the competitive ability of FBXO5 to inhibit the association of securin to APC. Can still compete with the APC substrate for APC binding. Fails to inhibit ubiquitin chain assembly by UBE2C or mono-ubiquitination by UBE2D1. Largely abolishes the inhibitory activity against protein degradation. Fails to inactivate APC-FZR1 complex. Allows FBXO5 degradation in the absence of CDK4 inhibitor. C->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16921029,ECO:0000269|PubMed:23708001,ECO:0000269|PubMed:29875408;Dbxref=PMID:16921029,PMID:23708001,PMID:29875408 Q9UKT4 UniProtKB Mutagenesis 406 406 . . . Note=Does not affect the inhibitory activity against chain assembly%3B when associated with S-401. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23708001;Dbxref=PMID:23708001 Q9UKT4 UniProtKB Mutagenesis 409 409 . . . Note=Decreases UBE2C-mediated ubiquitination. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23708605;Dbxref=PMID:23708605 Q9UKT4 UniProtKB Mutagenesis 444 445 . . . Note=Loses inhibitory activity on UBE2S-catalyzed chain elongation. LR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23708001;Dbxref=PMID:23708001 Q9UKT4 UniProtKB Sequence conflict 212 212 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9UKT4 UniProtKB Turn 118 120 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:9GAW Q9UKT4 UniProtKB Beta strand 324 327 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:9GAW Q9UKT4 UniProtKB Helix 359 366 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:9GAW Q9UKT4 UniProtKB Beta strand 374 377 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:9GAW Q9UKT4 UniProtKB Turn 379 381 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:9GAW Q9UKT4 UniProtKB Beta strand 384 388 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:9GAW Q9UKT4 UniProtKB Turn 389 392 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:9GAW Q9UKT4 UniProtKB Beta strand 393 396 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:9GAW Q9UKT4 UniProtKB Turn 399 401 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:9GAW Q9UKT4 UniProtKB Beta strand 404 406 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:9GAW Q9UKT4 UniProtKB Turn 407 409 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:9GAW Q9UKT4 UniProtKB Beta strand 410 412 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:9GAW Q9UKT4 UniProtKB Helix 438 446 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:9GAW