##gff-version 3 P51610 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19413330,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:22223895,ECO:0007744|PubMed:22814378;Dbxref=PMID:19413330,PMID:20068231,PMID:21406692,PMID:22223895,PMID:22814378 P51610 UniProtKB Chain 2 1423 . . . ID=PRO_0000016611;Note=HCF N-terminal chain 6;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Chain 2 1323 . . . ID=PRO_0000016612;Note=HCF N-terminal chain 5;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Chain 2 1295 . . . ID=PRO_0000016613;Note=HCF N-terminal chain 4;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Chain 2 1110 . . . ID=PRO_0000016614;Note=HCF N-terminal chain 3;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Chain 2 1081 . . . ID=PRO_0000016615;Note=HCF N-terminal chain 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Chain 2 1019 . . . ID=PRO_0000016616;Note=HCF N-terminal chain 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Chain 1020 2035 . . . ID=PRO_0000016617;Note=HCF C-terminal chain 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Chain 1082 2035 . . . ID=PRO_0000016618;Note=HCF C-terminal chain 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Chain 1111 2035 . . . ID=PRO_0000016619;Note=HCF C-terminal chain 3;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Chain 1296 2035 . . . ID=PRO_0000016620;Note=HCF C-terminal chain 4;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Chain 1324 2035 . . . ID=PRO_0000016621;Note=HCF C-terminal chain 5;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Chain 1424 2035 . . . ID=PRO_0000016622;Note=HCF C-terminal chain 6;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Repeat 44 89 . . . Note=Kelch 1;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51610 UniProtKB Repeat 93 140 . . . Note=Kelch 2;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51610 UniProtKB Repeat 148 194 . . . Note=Kelch 3;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51610 UniProtKB Repeat 217 265 . . . Note=Kelch 4;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51610 UniProtKB Repeat 266 313 . . . Note=Kelch 5;Ontology_term=ECO:0000255;evidence=ECO:0000255 P51610 UniProtKB Domain 366 466 . . . Note=Fibronectin type-III 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 P51610 UniProtKB Repeat 1010 1035 . . . Note=HCF repeat 1;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Repeat 1072 1097 . . . Note=HCF repeat 2;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Repeat 1101 1126 . . . Note=HCF repeat 3;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Repeat 1158 1183 . . . Note=HCF repeat 4%3B degenerate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Repeat 1286 1311 . . . Note=HCF repeat 5;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Repeat 1314 1339 . . . Note=HCF repeat 6;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Repeat 1349 1374 . . . Note=HCF repeat 7%3B degenerate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Repeat 1414 1439 . . . Note=HCF repeat 8;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Domain 1797 1888 . . . Note=Fibronectin type-III 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 P51610 UniProtKB Domain 1890 2006 . . . Note=Fibronectin type-III 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 P51610 UniProtKB Region 407 434 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P51610 UniProtKB Region 500 550 . . . Note=Required for interaction with OGT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21285374;Dbxref=PMID:21285374 P51610 UniProtKB Region 610 722 . . . Note=Interaction with SIN3A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12670868;Dbxref=PMID:12670868 P51610 UniProtKB Region 750 902 . . . Note=Interaction with ZBTB17;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12244100;Dbxref=PMID:12244100 P51610 UniProtKB Region 813 912 . . . Note=Interaction with GABP2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10675337;Dbxref=PMID:10675337 P51610 UniProtKB Region 1292 1371 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P51610 UniProtKB Region 1435 1470 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P51610 UniProtKB Region 1487 1515 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P51610 UniProtKB Region 1994 2035 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P51610 UniProtKB Compositional bias 414 432 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P51610 UniProtKB Compositional bias 1292 1346 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P51610 UniProtKB Compositional bias 1355 1371 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P51610 UniProtKB Compositional bias 1997 2015 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P51610 UniProtKB Site 1019 1020 . . . Note=Cleavage%3B by autolysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Site 1081 1082 . . . Note=Cleavage%3B by autolysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Site 1110 1111 . . . Note=Cleavage%3B by autolysis;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Site 1295 1296 . . . Note=Cleavage%3B by autolysis;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Site 1323 1324 . . . Note=Cleavage%3B by autolysis;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:10920196,ECO:0000305|PubMed:7590226;Dbxref=PMID:10920196,PMID:7590226 P51610 UniProtKB Site 1423 1424 . . . Note=Cleavage%3B by autolysis;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:10920196,ECO:0000305|PubMed:7590226;Dbxref=PMID:10920196,PMID:7590226 P51610 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19413330,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:22223895,ECO:0007744|PubMed:22814378;Dbxref=PMID:19413330,PMID:20068231,PMID:21406692,PMID:22223895,PMID:22814378 P51610 UniProtKB Modified residue 6 6 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163;Dbxref=PMID:20068231,PMID:21406692,PMID:23186163 P51610 UniProtKB Modified residue 288 288 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P51610 UniProtKB Modified residue 411 411 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19690332;Dbxref=PMID:19690332 P51610 UniProtKB Modified residue 504 504 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 P51610 UniProtKB Modified residue 524 524 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 P51610 UniProtKB Modified residue 598 598 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P51610 UniProtKB Modified residue 666 666 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:16964243,ECO:0007744|PubMed:17924679,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163;Dbxref=PMID:16964243,PMID:17924679,PMID:18669648,PMID:20068231,PMID:21406692,PMID:23186163 P51610 UniProtKB Modified residue 669 669 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:20068231;Dbxref=PMID:20068231 P51610 UniProtKB Modified residue 813 813 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P51610 UniProtKB Modified residue 1205 1205 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:23186163 P51610 UniProtKB Modified residue 1219 1219 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 P51610 UniProtKB Modified residue 1224 1224 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P51610 UniProtKB Modified residue 1491 1491 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:16964243;Dbxref=PMID:16964243 P51610 UniProtKB Modified residue 1497 1497 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 P51610 UniProtKB Modified residue 1507 1507 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,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:21406692,ECO:0007744|PubMed:24275569;Dbxref=PMID:16964243,PMID:18669648,PMID:19690332,PMID:20068231,PMID:21406692,PMID:24275569 P51610 UniProtKB Modified residue 1771 1771 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 P51610 UniProtKB Modified residue 1838 1838 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q61191 P51610 UniProtKB Modified residue 2005 2005 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P51610 UniProtKB Cross-link 105 105 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19815555;Dbxref=PMID:19815555 P51610 UniProtKB Cross-link 163 163 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19815555;Dbxref=PMID:19815555 P51610 UniProtKB Cross-link 244 244 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19815555;Dbxref=PMID:19815555 P51610 UniProtKB Cross-link 282 282 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 P51610 UniProtKB Cross-link 363 363 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19815555;Dbxref=PMID:19815555 P51610 UniProtKB Cross-link 1807 1807 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19188440;Dbxref=PMID:19188440 P51610 UniProtKB Cross-link 1808 1808 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19188440;Dbxref=PMID:19188440 P51610 UniProtKB Cross-link 2024 2024 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 P51610 UniProtKB Alternative sequence 382 450 . . . ID=VSP_002815;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:8392914;Dbxref=PMID:8392914 P51610 UniProtKB Alternative sequence 428 428 . . . ID=VSP_012984;Note=In isoform 3. P->L;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 P51610 UniProtKB Alternative sequence 429 2035 . . . ID=VSP_012985;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 P51610 UniProtKB Alternative sequence 1499 1499 . . . ID=VSP_047138;Note=In isoform 4. P->PKISSMTETAPRALTTEVPIPAKITVTIANTETSDMPFSAVDILQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 P51610 UniProtKB Natural variant 225 225 . . . ID=VAR_069098;Note=In MAHCX%3B uncertain significance. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23000143;Dbxref=dbSNP:rs318240758,PMID:23000143 P51610 UniProtKB Natural variant 1164 1164 . . . ID=VAR_019813;Note=S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7829097;Dbxref=dbSNP:rs1051152,PMID:7829097 P51610 UniProtKB Natural variant 2004 2004 . . . ID=VAR_050043;Note=S->I;Dbxref=dbSNP:rs6643651 P51610 UniProtKB Mutagenesis 30 30 . . . Note=Severely reduces VP16-induced complex (VIC) formation%2C but retains association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. Abolishes interaction with CREB3. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10629049;Dbxref=PMID:10629049 P51610 UniProtKB Mutagenesis 79 79 . . . Note=Severely reduces VIC formation%2C but retains association with VP16. Severely reduces association with CREB3. Unable to rescue proliferation in temperature-sensitive arrested cells. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10629049;Dbxref=PMID:10629049 P51610 UniProtKB Mutagenesis 82 82 . . . Note=Moderately reduces VIC formation and association with VP16 and CREB3. Unable to rescue proliferation in temperature-sensitive arrested cells. C->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10629049;Dbxref=PMID:10629049 P51610 UniProtKB Mutagenesis 105 105 . . . Note=Minor reduction in VIC formation and association with VP16 and CREB3. Able to rescue proliferation in temperature-sensitive arrested cells. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10629049;Dbxref=PMID:10629049 P51610 UniProtKB Mutagenesis 134 134 . . . Note=Eliminates VIC formation and association with VP16. Weak association with POU2F1. Unable to associate with CREBZF and BAP1. Unable to rescue proliferation in temperature-sensitive arrested cells. P->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10629049,ECO:0000269|PubMed:19815555,ECO:0000269|PubMed:9271389;Dbxref=PMID:10629049,PMID:19815555,PMID:9271389 P51610 UniProtKB Mutagenesis 137 137 . . . Note=Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10629049;Dbxref=PMID:10629049 P51610 UniProtKB Mutagenesis 197 197 . . . Note=Eliminates VIC formation and association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10629049;Dbxref=PMID:10629049 P51610 UniProtKB Mutagenesis 200 200 . . . Note=Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10629049;Dbxref=PMID:10629049 P51610 UniProtKB Mutagenesis 228 228 . . . Note=Eliminates VIC formation and association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10629049;Dbxref=PMID:10629049 P51610 UniProtKB Mutagenesis 252 252 . . . Note=Minor reduction in VIC formation%2C but retains association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10629049;Dbxref=PMID:10629049 P51610 UniProtKB Mutagenesis 255 255 . . . Note=Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10629049;Dbxref=PMID:10629049 P51610 UniProtKB Mutagenesis 289 291 . . . Note=Minor reduction in VIC formation and association with VP16. Weak association with POU2F1. Severely reduces association with CREB3. Able to rescue proliferation in temperature-sensitive arrested cells. EWK->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10629049;Dbxref=PMID:10629049 P51610 UniProtKB Mutagenesis 319 319 . . . Note=Eliminates VIC formation and association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10629049;Dbxref=PMID:10629049 P51610 UniProtKB Mutagenesis 322 322 . . . Note=Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells. R->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10629049;Dbxref=PMID:10629049 P51610 UniProtKB Mutagenesis 338 338 . . . Note=Moderately reduces association with VP16 and CREB3. Able to rescue proliferation in temperature-sensitive arrested cells. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10629049;Dbxref=PMID:10629049 P51610 UniProtKB Mutagenesis 344 345 . . . Note=Eliminates VIC formation%2C but only minor reduction in association with VP16. Unable to associate with POU2F1%2C but only minor reduction in association with CREB3. Able to rescue proliferation in temperature-sensitive arrested cells. RK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10629049;Dbxref=PMID:10629049 P51610 UniProtKB Mutagenesis 1017 1021 . . . Note=Reduces and disrupts cleavage at HCF repeat. PCETH->AAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7590226;Dbxref=PMID:7590226 P51610 UniProtKB Mutagenesis 1072 1072 . . . Note=No effect on cleavage at HCF repeat. V->A P51610 UniProtKB Mutagenesis 1073 1073 . . . Note=No effect on cleavage at HCF repeat. R->A P51610 UniProtKB Mutagenesis 1074 1074 . . . Note=No effect on cleavage at HCF repeat. V->A P51610 UniProtKB Mutagenesis 1075 1075 . . . Note=No effect on cleavage at HCF repeat. C->A P51610 UniProtKB Mutagenesis 1076 1076 . . . Note=No effect on cleavage at HCF repeat. S->A P51610 UniProtKB Mutagenesis 1077 1077 . . . Note=No effect on cleavage at HCF repeat. N->A P51610 UniProtKB Mutagenesis 1078 1078 . . . Note=Inactivates cleavage at HCF repeat. P->A P51610 UniProtKB Mutagenesis 1079 1083 . . . Note=Reduces and disrupts cleavage at HCF repeat. PCETH->AAAAA P51610 UniProtKB Mutagenesis 1079 1079 . . . Note=Inactivates cleavage at HCF repeat. P->A P51610 UniProtKB Mutagenesis 1080 1080 . . . Note=Inactivates cleavage at HCF repeat. C->A P51610 UniProtKB Mutagenesis 1081 1081 . . . Note=Inactivates cleavage at HCF repeat. E->A P51610 UniProtKB Mutagenesis 1081 1081 . . . Note=Inactivates cleavage at HCF repeat. E->D P51610 UniProtKB Mutagenesis 1082 1082 . . . Note=Inactivates cleavage at HCF repeat. T->A P51610 UniProtKB Mutagenesis 1082 1082 . . . Note=Reduces cleavage at HCF repeat. T->F P51610 UniProtKB Mutagenesis 1082 1082 . . . Note=Reduces cleavage at HCF repeat. T->S P51610 UniProtKB Mutagenesis 1083 1083 . . . Note=Reduces cleavage at HCF repeat. H->A P51610 UniProtKB Mutagenesis 1084 1084 . . . Note=No effect on cleavage at HCF repeat. E->A P51610 UniProtKB Mutagenesis 1085 1085 . . . Note=Inactivates cleavage at HCF repeat. T->A P51610 UniProtKB Mutagenesis 1086 1086 . . . Note=No effect on cleavage at HCF repeat. G->A P51610 UniProtKB Mutagenesis 1087 1087 . . . Note=Inactivates cleavage at HCF repeat. T->A P51610 UniProtKB Mutagenesis 1088 1088 . . . Note=Inactivates cleavage at HCF repeat. T->A P51610 UniProtKB Mutagenesis 1089 1089 . . . Note=Reduces cleavage at HCF repeat. N->A P51610 UniProtKB Mutagenesis 1090 1090 . . . Note=Inactivates cleavage at HCF repeat. T->A P51610 UniProtKB Mutagenesis 1092 1092 . . . Note=Inactivates cleavage at HCF repeat. T->A P51610 UniProtKB Mutagenesis 1093 1093 . . . Note=Inactivates cleavage at HCF repeat. T->A P51610 UniProtKB Mutagenesis 1095 1095 . . . Note=Reduces cleavage at HCF repeat. T->A P51610 UniProtKB Mutagenesis 1096 1096 . . . Note=No effect on cleavage at HCF repeat. S->A P51610 UniProtKB Mutagenesis 1097 1097 . . . Note=No effect on cleavage at HCF repeat. N->A P51610 UniProtKB Sequence conflict 564 564 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 P51610 UniProtKB Sequence conflict 603 603 . . . Note=S->SVS;Ontology_term=ECO:0000305;evidence=ECO:0000305 P51610 UniProtKB Sequence conflict 665 665 . . . Note=K->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 P51610 UniProtKB Sequence conflict 1638 1638 . . . Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 P51610 UniProtKB Sequence conflict 1685 1685 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P51610 UniProtKB Sequence conflict 1735 1735 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 P51610 UniProtKB Sequence conflict 1873 1873 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P51610 UniProtKB Beta strand 368 375 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GO6 P51610 UniProtKB Beta strand 380 385 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GO6 P51610 UniProtKB Beta strand 391 399 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GO6 P51610 UniProtKB Beta strand 1813 1825 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GO6 P51610 UniProtKB Beta strand 1827 1829 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GO6 P51610 UniProtKB Beta strand 1853 1855 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GO6 P51610 UniProtKB Beta strand 1861 1870 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GO6 P51610 UniProtKB Beta strand 1873 1877 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GO6 P51610 UniProtKB Beta strand 1881 1884 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GO6 P51610 UniProtKB Beta strand 1895 1902 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GO6 P51610 UniProtKB Beta strand 1905 1911 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GO6 P51610 UniProtKB Beta strand 1922 1929 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GO6 P51610 UniProtKB Beta strand 1935 1937 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GO6 P51610 UniProtKB Beta strand 1946 1962 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GO6 P51610 UniProtKB Helix 1963 1966 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GO6 P51610 UniProtKB Beta strand 1971 1986 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GO6 P51610 UniProtKB Beta strand 1995 2000 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GO6