##gff-version 3 Q9NQB0 UniProtKB Chain 1 619 . . . ID=PRO_0000048623;Note=Transcription factor 7-like 2 Q9NQB0 UniProtKB DNA binding 350 418 . . . Note=HMG box;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00267 Q9NQB0 UniProtKB Region 1 96 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9NQB0 UniProtKB Region 1 53 . . . Note=CTNNB1-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9NQB0 UniProtKB Region 201 395 . . . Note=Mediates interaction with MAD2L2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19443654;Dbxref=PMID:19443654 Q9NQB0 UniProtKB Region 318 350 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9NQB0 UniProtKB Region 420 441 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9NQB0 UniProtKB Region 459 505 . . . Note=Promoter-specific activation domain Q9NQB0 UniProtKB Region 496 547 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9NQB0 UniProtKB Region 574 619 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9NQB0 UniProtKB Motif 425 430 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9NQB0 UniProtKB Compositional bias 16 46 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9NQB0 UniProtKB Compositional bias 47 63 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9NQB0 UniProtKB Compositional bias 64 91 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9NQB0 UniProtKB Compositional bias 318 332 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9NQB0 UniProtKB Compositional bias 333 350 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9NQB0 UniProtKB Compositional bias 520 537 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9NQB0 UniProtKB Compositional bias 584 619 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9NQB0 UniProtKB Modified residue 201 201 . . . Note=Phosphothreonine%3B by NLK;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12556497;Dbxref=PMID:12556497 Q9NQB0 UniProtKB Modified residue 212 212 . . . Note=Phosphothreonine%3B by NLK;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12556497;Dbxref=PMID:12556497 Q9NQB0 UniProtKB Cross-link 22 22 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q9NQB0 UniProtKB Cross-link 320 320 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12727872;Dbxref=PMID:12727872 Q9NQB0 UniProtKB Cross-link 539 539 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q9NQB0 UniProtKB Alternative sequence 1 6 . . . ID=VSP_053748;Note=In isoform 17. MPQLNG->MSSFLS;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:21256126;Dbxref=PMID:21256126 Q9NQB0 UniProtKB Alternative sequence 7 290 . . . ID=VSP_053749;Note=In isoform 17. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:21256126;Dbxref=PMID:21256126 Q9NQB0 UniProtKB Alternative sequence 128 150 . . . ID=VSP_006962;Note=In isoform 8%2C isoform 10%2C isoform 11%2C isoform 12%2C isoform 13%2C isoform 14%2C isoform 15 and isoform 16. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:14702039,ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:19602480,ECO:0000303|PubMed:21256126,ECO:0000303|PubMed:9065401;Dbxref=PMID:14702039,PMID:15489334,PMID:19602480,PMID:21256126,PMID:9065401 Q9NQB0 UniProtKB Alternative sequence 184 184 . . . ID=VSP_045821;Note=In isoform 11. V->VSPLPCCTQGHDCQHFYPPSDFTVSTQVFRDMKRSHSLQKVGEPWCIE;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NQB0 UniProtKB Alternative sequence 260 263 . . . ID=VSP_006963;Note=In isoform 10. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 Q9NQB0 UniProtKB Alternative sequence 290 290 . . . ID=VSP_053750;Note=In isoform 15 and isoform 16. M->MSSFLS;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:21256126;Dbxref=PMID:21256126 Q9NQB0 UniProtKB Alternative sequence 440 465 . . . ID=VSP_006965;Note=In isoform 9%2C isoform 11%2C isoform 14 and isoform 15. EHSECFLNPCLSLPPITDLSAPKKCR->GEKKSAFATYKVKAAASAHPLQMEAY;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:14702039,ECO:0000303|PubMed:19602480,ECO:0000303|PubMed:21256126,ECO:0000303|PubMed:9065401,ECO:0000303|Ref.5;Dbxref=PMID:14702039,PMID:19602480,PMID:21256126,PMID:9065401 Q9NQB0 UniProtKB Alternative sequence 440 456 . . . ID=VSP_006964;Note=In isoform 4%2C isoform 5%2C isoform 7%2C isoform 13 and isoform 16. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:19602480,ECO:0000303|PubMed:21256126;Dbxref=PMID:19602480,PMID:21256126 Q9NQB0 UniProtKB Alternative sequence 457 619 . . . ID=VSP_006967;Note=In isoform 6. DLSAPKKCRARFGLDQQNNWCGPCRRKKKCVRYIQGEGSCLSPPSSDGSLLDSPPPSPNLLGSPPRDAKSQTEQTQPLSLSLKPDPLAHLSMMPPPPALLLAEATHKASALCPNGALDLPPAALQPAAPSSSIAQPSTSSLHSHSSLAGTQPQPLSLVTKSLE->GEKKSAFATYKVKAAASAHPLQMEAY;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:21256126;Dbxref=PMID:21256126 Q9NQB0 UniProtKB Alternative sequence 457 482 . . . ID=VSP_006968;Note=In isoform 10. DLSAPKKCRARFGLDQQNNWCGPCRR->GEKKSAFATYKVKAAASAHPLQMEAY;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 Q9NQB0 UniProtKB Alternative sequence 457 478 . . . ID=VSP_006966;Note=In isoform 3%2C isoform 7 and isoform 13. DLSAPKKCRARFGLDQQNNWCG->DANTPKKCRALFGLDRQTLWCK;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:19602480,ECO:0000303|PubMed:21256126;Dbxref=PMID:19602480,PMID:21256126 Q9NQB0 UniProtKB Alternative sequence 466 619 . . . ID=VSP_006969;Note=In isoform 9%2C isoform 11%2C isoform 14 and isoform 15. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:14702039,ECO:0000303|PubMed:19602480,ECO:0000303|PubMed:21256126,ECO:0000303|PubMed:9065401,ECO:0000303|Ref.5;Dbxref=PMID:14702039,PMID:19602480,PMID:21256126,PMID:9065401 Q9NQB0 UniProtKB Alternative sequence 481 619 . . . ID=VSP_045822;Note=In isoform 12. RRKKKCVRYIQGEGSCLSPPSSDGSLLDSPPPSPNLLGSPPRDAKSQTEQTQPLSLSLKPDPLAHLSMMPPPPALLLAEATHKASALCPNGALDLPPAALQPAAPSSSIAQPSTSSLHSHSSLAGTQPQPLSLVTKSLE->SL;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:19602480;Dbxref=PMID:19602480 Q9NQB0 UniProtKB Alternative sequence 482 494 . . . ID=VSP_006970;Note=In isoform 2 and isoform 4. RKKKCVRYIQGEG->CKYSKEVSGTVRA;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NQB0 UniProtKB Alternative sequence 483 619 . . . ID=VSP_006971;Note=In isoform 10. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 Q9NQB0 UniProtKB Alternative sequence 495 619 . . . ID=VSP_006972;Note=In isoform 2 and isoform 4. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NQB0 UniProtKB Natural variant 346 346 . . . ID=VAR_047126;Note=K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10919662;Dbxref=dbSNP:rs2757884,PMID:10919662 Q9NQB0 UniProtKB Natural variant 465 465 . . . ID=VAR_035939;Note=In a colorectal cancer sample%3B somatic mutation. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16959974;Dbxref=PMID:16959974 Q9NQB0 UniProtKB Mutagenesis 10 11 . . . Note=Reduces CTNNB1 binding. DD->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10080941;Dbxref=PMID:10080941 Q9NQB0 UniProtKB Mutagenesis 16 16 . . . Note=Abolishes CTNNB1 binding. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10080941;Dbxref=PMID:10080941 Q9NQB0 UniProtKB Mutagenesis 17 17 . . . Note=Reduces CTNNB1 binding. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10080941;Dbxref=PMID:10080941 Q9NQB0 UniProtKB Mutagenesis 19 19 . . . Note=Reduces transcription activation. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11713476;Dbxref=PMID:11713476 Q9NQB0 UniProtKB Mutagenesis 21 21 . . . Note=Reduces transcription activation. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11713476;Dbxref=PMID:11713476 Q9NQB0 UniProtKB Mutagenesis 23 24 . . . Note=Reduces CTNNB1 binding. DE->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10080941;Dbxref=PMID:10080941 Q9NQB0 UniProtKB Mutagenesis 24 24 . . . Note=Reduces CTNNB1 binding%2C and abolishes CTNNB1 binding%3B when associated with A-26%3B A-28 and A-29. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11713475;Dbxref=PMID:11713475 Q9NQB0 UniProtKB Mutagenesis 26 26 . . . Note=Abolishes CTNNB1 binding%3B when associated with A-24%3B A-28 and A-29. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11713475;Dbxref=PMID:11713475 Q9NQB0 UniProtKB Mutagenesis 28 28 . . . Note=Abolishes CTNNB1 binding%3B when associated with A-24%3B A-26 and A-29. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11713475;Dbxref=PMID:11713475 Q9NQB0 UniProtKB Mutagenesis 29 29 . . . Note=Reduces CTNNB1 binding%2C and abolishes CTNNB1 binding%3B when associated with A-24%3B A-26 and A-28. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11713475;Dbxref=PMID:11713475 Q9NQB0 UniProtKB Mutagenesis 48 48 . . . Note=Abolishes CTNNB1 binding. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10080941;Dbxref=PMID:10080941 Q9NQB0 UniProtKB Mutagenesis 201 201 . . . Note=Reduced phosphorylation by NLK and enhanced DNA-binding%3B when associated with V-212. T->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12556497;Dbxref=PMID:12556497 Q9NQB0 UniProtKB Mutagenesis 212 212 . . . Note=Reduced phosphorylation by NLK and enhanced DNA-binding%3B when associated with V-201. T->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12556497;Dbxref=PMID:12556497 Q9NQB0 UniProtKB Mutagenesis 320 320 . . . Note=Loss of sumoylation. No effect on localization to nuclear bodies. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12727872;Dbxref=PMID:12727872 Q9NQB0 UniProtKB Mutagenesis 322 322 . . . Note=Loss of sumoylation. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12727872;Dbxref=PMID:12727872 Q9NQB0 UniProtKB Sequence conflict 118 121 . . . Note=NGSL->KRSV;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NQB0 UniProtKB Sequence conflict 167 167 . . . Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NQB0 UniProtKB Sequence conflict 226 226 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NQB0 UniProtKB Sequence conflict 290 290 . . . Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NQB0 UniProtKB Sequence conflict 331 331 . . . Note=L->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NQB0 UniProtKB Sequence conflict 596 596 . . . Note=S->W;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NQB0 UniProtKB Helix 22 31 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1JDH Q9NQB0 UniProtKB Helix 38 48 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1JDH