##gff-version 3 P42224 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22223895;Dbxref=PMID:22223895 P42224 UniProtKB Chain 2 750 . . . ID=PRO_0000182410;Note=Signal transducer and activator of transcription 1-alpha/beta P42224 UniProtKB Domain 573 670 . . . Note=SH2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00191 P42224 UniProtKB Coiled coil 136 317 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9630226;Dbxref=PMID:9630226 P42224 UniProtKB Site 724 724 . . . Note=Required for recruitment of EP300/p300;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16257975;Dbxref=PMID:16257975 P42224 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22223895;Dbxref=PMID:22223895 P42224 UniProtKB Modified residue 114 114 . . . Note=N6-methyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28753426;Dbxref=PMID:28753426 P42224 UniProtKB Modified residue 175 175 . . . Note=N6-methyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28753426;Dbxref=PMID:28753426 P42224 UniProtKB Modified residue 296 296 . . . Note=N6-methyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28753426;Dbxref=PMID:28753426 P42224 UniProtKB Modified residue 366 366 . . . Note=N6-methyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28753426;Dbxref=PMID:28753426 P42224 UniProtKB Modified residue 525 525 . . . Note=N6-methyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28753426;Dbxref=PMID:28753426 P42224 UniProtKB Modified residue 637 637 . . . Note=N6-methyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28753426;Dbxref=PMID:28753426 P42224 UniProtKB Modified residue 657 657 . . . Note=ADP-ribosyl glutamic acid%3B by PARP14;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27796300;Dbxref=PMID:27796300 P42224 UniProtKB Modified residue 665 665 . . . Note=N6-methyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28753426;Dbxref=PMID:28753426 P42224 UniProtKB Modified residue 701 701 . . . Note=Phosphotyrosine%3B by JAK1%2C JAK2 or TYK2;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17561467,ECO:0000269|PubMed:19088846,ECO:0000269|PubMed:21135090,ECO:0000269|PubMed:22065572,ECO:0000269|PubMed:26479788,ECO:0000269|PubMed:27796300,ECO:0000269|PubMed:28753426,ECO:0000269|PubMed:7657660;Dbxref=PMID:17561467,PMID:19088846,PMID:21135090,PMID:22065572,PMID:26479788,PMID:27796300,PMID:28753426,PMID:7657660 P42224 UniProtKB Modified residue 705 705 . . . Note=ADP-ribosyl glutamic acid%3B by PARP14;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27796300;Dbxref=PMID:27796300 P42224 UniProtKB Modified residue 708 708 . . . Note=Phosphoserine%3B by IKKE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22065572;Dbxref=PMID:22065572 P42224 UniProtKB Modified residue 727 727 . . . Note=Phosphoserine%3B by CAMK2 and MAPK14;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:11972023,ECO:0000269|PubMed:15322115,ECO:0000269|PubMed:16257975,ECO:0000269|PubMed:17897103,ECO:0000269|PubMed:21135090,ECO:0000269|PubMed:22065572,ECO:0000269|PubMed:26479788,ECO:0000269|PubMed:7543024,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:18691976,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:11972023,PMID:15322115,PMID:16257975,PMID:17897103,PMID:18669648,PMID:18691976,PMID:19690332,PMID:20068231,PMID:21135090,PMID:22065572,PMID:23186163,PMID:26479788,PMID:7543024 P42224 UniProtKB Modified residue 745 745 . . . Note=Phosphoserine%3B by IKKE;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P42225 P42224 UniProtKB Cross-link 703 703 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:25114211;Dbxref=PMID:25114211 P42224 UniProtKB Cross-link 703 703 . . . 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 P42224 UniProtKB Alternative sequence 713 750 . . . ID=VSP_006282;Note=In isoform Beta. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|Ref.6;Dbxref=PMID:15489334 P42224 UniProtKB Natural variant 30 30 . . . ID=VAR_034521;Note=I->T;Dbxref=dbSNP:rs34255470 P42224 UniProtKB Natural variant 165 165 . . . ID=VAR_065934;Note=In IMD31C%3B gain of function mutation associated with increased STAT1 phosphorylation due to impaired nuclear dephosphorylation. D->G;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21727188,ECO:0000269|PubMed:23709754;Dbxref=dbSNP:rs387906764,PMID:21727188,PMID:23709754 P42224 UniProtKB Natural variant 165 165 . . . ID=VAR_065935;Note=In IMD31C. D->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21727188;Dbxref=dbSNP:rs387906767,PMID:21727188 P42224 UniProtKB Natural variant 170 170 . . . ID=VAR_065936;Note=In IMD31C. Y->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21727188;Dbxref=dbSNP:rs387906766,PMID:21727188 P42224 UniProtKB Natural variant 174 174 . . . ID=VAR_065937;Note=In IMD31C. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21727188;Dbxref=dbSNP:rs387906763,PMID:21727188 P42224 UniProtKB Natural variant 179 179 . . . ID=VAR_075494;Note=In IMD31C%3B gain of function%3B increases transactivation activity in response to IFNG. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23709754;Dbxref=dbSNP:rs587777628,PMID:23709754 P42224 UniProtKB Natural variant 201 201 . . . ID=VAR_065815;Note=In IMD31B%3B not deleterious in terms of most STAT1 functions%3B causes abnormal splicing out of exon 8 from most mRNAs thereby decreasing protein levels by approximately 70%25. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20841510;Dbxref=dbSNP:rs587776870,PMID:20841510 P42224 UniProtKB Natural variant 202 202 . . . ID=VAR_065938;Note=In IMD31C. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21727188;Dbxref=PMID:21727188 P42224 UniProtKB Natural variant 202 202 . . . ID=VAR_065939;Note=In IMD31C. M->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21727188;Dbxref=dbSNP:rs387906762,PMID:21727188 P42224 UniProtKB Natural variant 267 267 . . . ID=VAR_065940;Note=In IMD31C. A->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21714643,ECO:0000269|PubMed:21727188;Dbxref=dbSNP:rs387906759,PMID:21714643,PMID:21727188 P42224 UniProtKB Natural variant 271 271 . . . ID=VAR_065941;Note=In IMD31C. Q->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21727188;Dbxref=dbSNP:rs387906768,PMID:21727188 P42224 UniProtKB Natural variant 274 274 . . . ID=VAR_065942;Note=In IMD31C%3B gain of function%3B increases STAT1 phosphorylation due to impaired nuclear dephosphorylation%3B increases transactivation activity in response to IFNG. R->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21727188,ECO:0000269|PubMed:23709754;Dbxref=dbSNP:rs387906760,PMID:21727188,PMID:23709754 P42224 UniProtKB Natural variant 274 274 . . . ID=VAR_065943;Note=In IMD31C%3B gain of function%3B increases phosphorylation in response to IFNG%2C IFNA and IL27 due to a loss of dephosphorylation. R->W;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21714643,ECO:0000269|PubMed:21727188,ECO:0000269|PubMed:23709754;Dbxref=dbSNP:rs387906758,PMID:21714643,PMID:21727188,PMID:23709754 P42224 UniProtKB Natural variant 278 278 . . . ID=VAR_075495;Note=In IMD31C%3B gain of function%3B increases phosphorylation in response to IFNG and IFNA due to a loss of dephosphorylation. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25288569;Dbxref=dbSNP:rs863223398,PMID:25288569 P42224 UniProtKB Natural variant 285 285 . . . ID=VAR_075496;Note=In IMD31C%3B gain of function%3B increases transactivation activity in response to IFNG. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23709754;Dbxref=dbSNP:rs587777629,PMID:23709754 P42224 UniProtKB Natural variant 286 286 . . . ID=VAR_065944;Note=In IMD31C. K->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21727188;Dbxref=dbSNP:rs387906761,PMID:21727188 P42224 UniProtKB Natural variant 288 288 . . . ID=VAR_065945;Note=In IMD31C. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21727188;Dbxref=dbSNP:rs387906765,PMID:21727188 P42224 UniProtKB Natural variant 298 298 . . . ID=VAR_075497;Note=In IMD31C%3B gain of function%3B increases basal STAT1 phosphorylation levels which are 10-20 fold higher than controls after IFNG stimulation. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26514428;Dbxref=PMID:26514428 P42224 UniProtKB Natural variant 320 320 . . . ID=VAR_065816;Note=In IMD31A%3B affects the DNA-binding activity of the protein. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16934001;Dbxref=dbSNP:rs137852680,PMID:16934001 P42224 UniProtKB Natural variant 384 384 . . . ID=VAR_075498;Note=In IMD31C%3B gain of function%3B increases phosphorylation in response to IFNG and IFNA due to a loss of dephosphorylation. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25288569;Dbxref=dbSNP:rs796065052,PMID:25288569 P42224 UniProtKB Natural variant 385 385 . . . ID=VAR_075499;Note=In IMD31C%3B gain of function%3B increases phosphorylation in response to IFNG%2C IFNA and IL27 due to a loss of dephosphorylation. T->M;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23709754,ECO:0000269|PubMed:25288569;Dbxref=dbSNP:rs587777630,PMID:23709754,PMID:25288569 P42224 UniProtKB Natural variant 463 463 . . . ID=VAR_065817;Note=In IMD31A%3B affects the DNA-binding activity of the protein. Q->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16934001;Dbxref=dbSNP:rs137852679,PMID:16934001 P42224 UniProtKB Natural variant 491 491 . . . ID=VAR_036001;Note=In a breast cancer sample%3B somatic mutation. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16959974;Dbxref=PMID:16959974 P42224 UniProtKB Natural variant 600 600 . . . ID=VAR_018265;Note=In IMD31B%3B found in an infant who died of a viral-like illness associated with complete STAT1 deficiency. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12590259;Dbxref=dbSNP:rs137852678,PMID:12590259 P42224 UniProtKB Natural variant 637 637 . . . ID=VAR_068713;Note=In IMD31A%3B affects both phosphorylation and DNA-binding activity%3B results in impaired STAT1-mediated cellular response to IFN-gamma and interleukin-27. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22573496;Dbxref=dbSNP:rs587777705,PMID:22573496 P42224 UniProtKB Natural variant 673 673 . . . ID=VAR_068714;Note=In IMD31A%3B impairs tyrosine phosphorylation%3B results in impaired STAT1-mediated cellular response to IFN-gamma and interleukin-27. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22573496;Dbxref=dbSNP:rs587777704,PMID:22573496 P42224 UniProtKB Natural variant 701 701 . . . ID=VAR_075500;Note=In IMD31B%3B disrupts transactivation activity in response to IFNG. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23709754;Dbxref=PMID:23709754 P42224 UniProtKB Natural variant 706 706 . . . ID=VAR_018266;Note=In IMD31A%3B loss of GAF and ISGF3 activation%3B impairs the nuclear accumulation of GAF but not of ISGF3 in heterozygous cells stimulated by IFNs%3B affects phosphorylation of the protein. L->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11452125,ECO:0000269|PubMed:16934001;Dbxref=dbSNP:rs137852677,PMID:11452125,PMID:16934001 P42224 UniProtKB Mutagenesis 110 110 . . . Note=Sumoylated. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12764129;Dbxref=PMID:12764129 P42224 UniProtKB Mutagenesis 114 114 . . . Note=No effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28753426;Dbxref=PMID:28753426 P42224 UniProtKB Mutagenesis 175 175 . . . Note=No effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28753426;Dbxref=PMID:28753426 P42224 UniProtKB Mutagenesis 296 296 . . . Note=No effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28753426;Dbxref=PMID:28753426 P42224 UniProtKB Mutagenesis 366 366 . . . Note=No effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28753426;Dbxref=PMID:28753426 P42224 UniProtKB Mutagenesis 525 525 . . . Note=Strongly reduced IFN-alpha-induced STAT1 phosphorylation and nuclear translocation. Does not affect ability to homodimerize. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28753426;Dbxref=PMID:28753426 P42224 UniProtKB Mutagenesis 636 637 . . . Note=No effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation. KK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28753426;Dbxref=PMID:28753426 P42224 UniProtKB Mutagenesis 656 658 . . . Note=Enhances STAT1 nuclear translocation and interferon (IFN)-stimulated gene (ISG) expression in response to IFN-beta stimulation. Reduces viral load in infected cultured cells. AEN->CEC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26479788;Dbxref=PMID:26479788 P42224 UniProtKB Mutagenesis 657 657 . . . Note=Loss of ADP-ribosylation and increased Tyr-701 phosphorylation%3B when associated with Q-705. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27796300;Dbxref=PMID:27796300 P42224 UniProtKB Mutagenesis 665 665 . . . Note=No effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28753426;Dbxref=PMID:28753426 P42224 UniProtKB Mutagenesis 701 701 . . . Note=Not phosphorylated at S-708 upon IFNB induction. Y->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17897103,ECO:0000269|PubMed:22065572;Dbxref=PMID:17897103,PMID:22065572 P42224 UniProtKB Mutagenesis 701 701 . . . Note=No effect on basal sumoylation. Enhances sumoylation in the presence of MAPK stimulation. Phosphorylated at S-708 upon IFNB induction. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17897103,ECO:0000269|PubMed:22065572;Dbxref=PMID:17897103,PMID:22065572 P42224 UniProtKB Mutagenesis 703 703 . . . Note=Abolishes sumoylation by SUMO1. Increased IFN-gamma-mediated transactivation. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12764129,ECO:0000269|PubMed:12855578;Dbxref=PMID:12764129,PMID:12855578 P42224 UniProtKB Mutagenesis 705 705 . . . Note=Loss of ADP-ribosylation and increased Tyr-701 phosphorylation%3B when associated with Q-657. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27796300;Dbxref=PMID:27796300 P42224 UniProtKB Mutagenesis 708 708 . . . Note=Phosphorylated at Y-701 upon IFNB induction. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22065572;Dbxref=PMID:22065572 P42224 UniProtKB Mutagenesis 708 708 . . . Note=Not phosphorylated at Y-701 upon IFNB induction. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22065572;Dbxref=PMID:22065572 P42224 UniProtKB Mutagenesis 724 724 . . . Note=Impaired phosphorylation at S-727. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16257975;Dbxref=PMID:16257975 P42224 UniProtKB Mutagenesis 727 727 . . . Note=Decreased transcriptional activation. No effect on basal sumoylation. No enhancement of sumoylation on MAPK stimulation. No PRKCD-induced apoptosis. Upon IFNB induction%2C phosphorylated at Y-701 but not at S-708. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15322115,ECO:0000269|PubMed:17897103,ECO:0000269|PubMed:22065572;Dbxref=PMID:15322115,PMID:17897103,PMID:22065572 P42224 UniProtKB Mutagenesis 727 727 . . . Note=No change in enhancement of MAPK-induced sumoylation. Basal interaction with PIAS1. Interaction with PIAS1 increased on MAPK stimulation. S->D;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15322115,ECO:0000269|PubMed:17897103,ECO:0000269|PubMed:22065572;Dbxref=PMID:15322115,PMID:17897103,PMID:22065572 P42224 UniProtKB Mutagenesis 727 727 . . . Note=No change in enhancement of MAPK-induced sumoylation. S->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15322115,ECO:0000269|PubMed:17897103,ECO:0000269|PubMed:22065572;Dbxref=PMID:15322115,PMID:17897103,PMID:22065572 P42224 UniProtKB Sequence conflict 46 46 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 P42224 UniProtKB Sequence conflict 307 307 . . . Note=S->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 P42224 UniProtKB Sequence conflict 718 718 . . . Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 P42224 UniProtKB Helix 3 8 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3WWT P42224 UniProtKB Helix 12 21 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3WWT P42224 UniProtKB Beta strand 23 26 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3WWT P42224 UniProtKB Helix 28 33 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3WWT P42224 UniProtKB Helix 35 40 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3WWT P42224 UniProtKB Helix 43 46 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3WWT P42224 UniProtKB Helix 50 73 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3WWT P42224 UniProtKB Helix 77 94 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3WWT P42224 UniProtKB Helix 99 122 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3WWT P42224 UniProtKB Helix 134 175 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Turn 176 179 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Helix 192 233 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Helix 235 247 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Helix 257 286 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Helix 293 315 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Beta strand 317 324 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Beta strand 334 336 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Beta strand 341 349 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Helix 352 354 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Turn 355 357 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Beta strand 359 365 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Helix 370 373 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Beta strand 374 376 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1BF5 P42224 UniProtKB Beta strand 380 384 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Beta strand 387 389 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Beta strand 391 395 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1BF5 P42224 UniProtKB Turn 396 398 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1BF5 P42224 UniProtKB Beta strand 401 411 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Beta strand 421 425 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1BF5 P42224 UniProtKB Helix 426 428 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Beta strand 433 441 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Beta strand 444 451 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Beta strand 455 460 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Helix 461 463 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Helix 464 477 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Turn 484 488 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Helix 495 509 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Helix 516 527 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Helix 539 542 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Beta strand 550 552 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1BF5 P42224 UniProtKB Helix 554 568 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Helix 570 574 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Helix 584 591 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Beta strand 592 594 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1YVL P42224 UniProtKB Beta strand 598 603 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Beta strand 612 618 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Beta strand 621 624 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1BF5 P42224 UniProtKB Beta strand 627 631 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Helix 636 641 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Helix 644 650 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Beta strand 652 654 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8D3F P42224 UniProtKB Beta strand 657 659 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1BF5 P42224 UniProtKB Turn 668 670 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Helix 673 677 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Turn 678 680 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NUF P42224 UniProtKB Beta strand 709 711 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8D3F P42224 UniProtKB Helix 728 738 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KA6 P42224 UniProtKB Turn 739 742 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KA6 P42224 UniProtKB Helix 743 745 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KA6 P42224 UniProtKB Turn 746 748 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KA6