##gff-version 3 Q13873 UniProtKB Signal peptide 1 26 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q13873 UniProtKB Chain 27 1038 . . . ID=PRO_0000024415;Note=Bone morphogenetic protein receptor type-2 Q13873 UniProtKB Topological domain 27 150 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q13873 UniProtKB Transmembrane 151 171 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q13873 UniProtKB Topological domain 172 1038 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q13873 UniProtKB Domain 203 504 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q13873 UniProtKB Region 593 626 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13873 UniProtKB Region 746 770 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13873 UniProtKB Region 872 972 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13873 UniProtKB Compositional bias 746 768 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13873 UniProtKB Compositional bias 872 897 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13873 UniProtKB Compositional bias 898 918 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13873 UniProtKB Compositional bias 937 964 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q13873 UniProtKB Active site 333 333 . . . Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q13873 UniProtKB Binding site 209 217 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305|Ref.16 Q13873 UniProtKB Binding site 230 230 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305|Ref.16 Q13873 UniProtKB Binding site 280 282 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305|Ref.16 Q13873 UniProtKB Binding site 337 338 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305|Ref.16 Q13873 UniProtKB Binding site 351 351 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305|Ref.16 Q13873 UniProtKB Modified residue 379 379 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19369195;Dbxref=PMID:19369195 Q13873 UniProtKB Modified residue 586 586 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18691976;Dbxref=PMID:18691976 Q13873 UniProtKB Modified residue 680 680 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35607 Q13873 UniProtKB Modified residue 681 681 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35607 Q13873 UniProtKB Glycosylation 55 55 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q13873 UniProtKB Glycosylation 110 110 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q13873 UniProtKB Glycosylation 126 126 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q13873 UniProtKB Disulfide bond 34 66 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:17094948,ECO:0007744|PDB:2HLQ;Dbxref=PMID:17094948 Q13873 UniProtKB Disulfide bond 60 84 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:17094948,ECO:0007744|PDB:2HLQ;Dbxref=PMID:17094948 Q13873 UniProtKB Disulfide bond 94 117 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:17094948,ECO:0007744|PDB:2HLQ;Dbxref=PMID:17094948 Q13873 UniProtKB Disulfide bond 99 116 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:17094948,ECO:0007744|PDB:2HLQ;Dbxref=PMID:17094948 Q13873 UniProtKB Disulfide bond 118 123 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:17094948,ECO:0007744|PDB:2HLQ;Dbxref=PMID:17094948 Q13873 UniProtKB Alternative sequence 530 530 . . . ID=VSP_054441;Note=In isoform 2. N->R;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:7791754;Dbxref=PMID:15489334,PMID:7791754 Q13873 UniProtKB Alternative sequence 531 1038 . . . ID=VSP_054442;Note=In isoform 2. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:7791754;Dbxref=PMID:15489334,PMID:7791754 Q13873 UniProtKB Natural variant 60 60 . . . ID=VAR_013670;Note=In PPH1%3B loss of function in BMP signaling pathway via SMAD proteins activation%3B does not localize to the cell surface%3B when transfected in epithelial cells it results in constitutive p38MAPK phosphorylation consistent with a gain of function in the activation of p38MAPK cascade. C->Y;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11015450,ECO:0000269|PubMed:12045205;Dbxref=dbSNP:rs1085307172,PMID:11015450,PMID:12045205 Q13873 UniProtKB Natural variant 64 64 . . . ID=VAR_079588;Note=In PPH1%3B uncertain significance%3B unchanged subcellular localization. S->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28507310;Dbxref=PMID:28507310 Q13873 UniProtKB Natural variant 67 67 . . . ID=VAR_073041;Note=In PPH1%3B significant decrease in nitric oxide synthesis by endothelial cells. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25187962;Dbxref=dbSNP:rs1085307177,PMID:25187962 Q13873 UniProtKB Natural variant 77 77 . . . ID=VAR_079589;Note=In PPH1%3B uncertain significance%3B unchanged subcellular localization. I->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24936649,ECO:0000269|PubMed:28507310;Dbxref=PMID:24936649,PMID:28507310 Q13873 UniProtKB Natural variant 82 82 . . . ID=VAR_033109;Note=In PPH1. Q->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12358323;Dbxref=dbSNP:rs1085307185,PMID:12358323 Q13873 UniProtKB Natural variant 84 84 . . . ID=VAR_079590;Note=In PPH1%3B alters alternative splicing of BMPR2. C->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24936649,ECO:0000269|PubMed:28507310;Dbxref=dbSNP:rs1085307197,PMID:24936649,PMID:28507310 Q13873 UniProtKB Natural variant 87 87 . . . ID=VAR_079591;Note=In PPH1%3B uncertain significance%3B unchanged subcellular localization. H->Y;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24936649,ECO:0000269|PubMed:28507310;Dbxref=PMID:24936649,PMID:28507310 Q13873 UniProtKB Natural variant 92 92 . . . ID=VAR_079592;Note=In PPH1%3B uncertain significance%3B unchanged subcellular localization. Q->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24936649,ECO:0000269|PubMed:28507310;Dbxref=PMID:24936649,PMID:28507310 Q13873 UniProtKB Natural variant 109 109 . . . ID=VAR_079593;Note=In PPH1%3B uncertain significance%3B unchanged subcellular localization. Q->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28507310;Dbxref=PMID:28507310 Q13873 UniProtKB Natural variant 117 117 . . . ID=VAR_013671;Note=In PPH1%3B loss of function in BMP signaling pathway%3B does not localize to the cell surface. C->Y;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11015450,ECO:0000269|PubMed:12045205;Dbxref=dbSNP:rs1085307215,PMID:11015450,PMID:12045205 Q13873 UniProtKB Natural variant 118 118 . . . ID=VAR_013672;Note=In PPH1%3B loss of function in BMP signaling pathway%3B does not localize to the cell surface. C->W;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10973254,ECO:0000269|PubMed:12045205;Dbxref=dbSNP:rs137852743,PMID:10973254,PMID:12045205 Q13873 UniProtKB Natural variant 123 123 . . . ID=VAR_013673;Note=In PPH1%3B loss of function in BMP signaling pathway%3B does not localize to the cell surface. C->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11115378,ECO:0000269|PubMed:12045205;Dbxref=dbSNP:rs137852750,PMID:11115378,PMID:12045205 Q13873 UniProtKB Natural variant 123 123 . . . ID=VAR_013674;Note=In PPH1%3B loss of function in BMP signaling pathway%3B does not localize to the cell surface. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11115378,ECO:0000269|PubMed:12045205;Dbxref=dbSNP:rs137852750,PMID:11115378,PMID:12045205 Q13873 UniProtKB Natural variant 138 138 . . . ID=VAR_079594;Note=In PPH1%3B uncertain significance%3B unchanged subcellular localization. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28507310;Dbxref=PMID:28507310 Q13873 UniProtKB Natural variant 162 162 . . . ID=VAR_079595;Note=In PPH1%3B uncertain significance%3B unchanged subcellular localization. A->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24936649,ECO:0000269|PubMed:28507310;Dbxref=PMID:24936649,PMID:28507310 Q13873 UniProtKB Natural variant 182 182 . . . ID=VAR_033110;Note=In PPH1. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12358323;Dbxref=dbSNP:rs137852754,PMID:12358323 Q13873 UniProtKB Natural variant 218 1038 . . . ID=VAR_079596;Note=In PPH1%3B changed localization to the plasma membrane. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28507310;Dbxref=PMID:28507310 Q13873 UniProtKB Natural variant 224 224 . . . ID=VAR_013675;Note=E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11115378;Dbxref=dbSNP:rs754343081,PMID:11115378 Q13873 UniProtKB Natural variant 248 248 . . . ID=VAR_079597;Note=In PPH1%3B uncertain significance%3B unchanged subcellular localization. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28507310;Dbxref=PMID:28507310 Q13873 UniProtKB Natural variant 264 264 . . . ID=VAR_079598;Note=In PPH1%3B uncertain significance%3B unchanged subcellular localization. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24936649,ECO:0000269|PubMed:28507310;Dbxref=PMID:24936649,PMID:28507310 Q13873 UniProtKB Natural variant 298 1038 . . . ID=VAR_079599;Note=In PPH1%3B loss of localization to the plasma membrane%3B localized to the cytoplasm. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28507310;Dbxref=PMID:28507310 Q13873 UniProtKB Natural variant 341 341 . . . ID=VAR_079600;Note=In PPH1%3B uncertain significance%3B unchanged subcellular localization. V->M;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24936649,ECO:0000269|PubMed:28507310;Dbxref=dbSNP:rs767882551,PMID:24936649,PMID:28507310 Q13873 UniProtKB Natural variant 347 347 . . . ID=VAR_013676;Note=In PPH1%3B does not localize to the cell surface. C->Y;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10973254,ECO:0000269|PubMed:12045205;Dbxref=dbSNP:rs137852744,PMID:10973254,PMID:12045205 Q13873 UniProtKB Natural variant 420 420 . . . ID=VAR_013677;Note=In PPH1%3B loss of function in BMP signaling pathway%3B does not localize to the cell surface. C->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11115378,ECO:0000269|PubMed:12045205;Dbxref=dbSNP:rs1085307324,PMID:11115378,PMID:12045205 Q13873 UniProtKB Natural variant 467 467 . . . ID=VAR_079601;Note=In PPH1%3B uncertain significance%3B unchanged subcellular localization. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28507310;Dbxref=PMID:28507310 Q13873 UniProtKB Natural variant 483 483 . . . ID=VAR_013678;Note=In PPH1%3B sporadic%3B loss of function in BMP signaling pathway via SMAD proteins activation%3B does not localize to the cell surface%3B when transfected in epithelial cells it results in constitutive p38MAPK phosphorylation consistent with a gain of function in the activation of p38MAPK cascade. C->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11015450,ECO:0000269|PubMed:12045205,ECO:0000269|PubMed:12358323;Dbxref=dbSNP:rs1085307354,PMID:11015450,PMID:12045205,PMID:12358323 Q13873 UniProtKB Natural variant 485 485 . . . ID=VAR_013679;Note=In PPH1%3B complete loss of function%3B no effect on localization to the cell surface%3B no effect on BMP4 binding. D->G;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10973254,ECO:0000269|PubMed:11115378,ECO:0000269|PubMed:12045205;Dbxref=dbSNP:rs137852745,PMID:10973254,PMID:11115378,PMID:12045205 Q13873 UniProtKB Natural variant 491 491 . . . ID=VAR_013680;Note=In PPH1%3B sporadic%3B no effect on localization to the cell surface. R->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10903931,ECO:0000269|PubMed:12045205;Dbxref=dbSNP:rs137852749,PMID:10903931,PMID:12045205 Q13873 UniProtKB Natural variant 491 491 . . . ID=VAR_013681;Note=In PPH1%3B loss of function in BMP signaling pathway via SMAD proteins activation%3B no effect on localization to the cell surface%3B no effect on BMP4 binding%3B when transfected in epithelial cells it results in constitutive p38MAPK phosphorylation consistent with a gain of function in the activation of p38MAPK cascade. R->W;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10903931,ECO:0000269|PubMed:12045205;Dbxref=dbSNP:rs137852746,PMID:10903931,PMID:12045205 Q13873 UniProtKB Natural variant 512 512 . . . ID=VAR_013682;Note=In PPH1%3B no effect on localization to the cell surface%3B no effect on BMP4 binding%3B when transfected in epithelial cells it results in constitutive p38MAPK phosphorylation consistent with a gain of function in the activation of p38MAPK cascade. K->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11115378,ECO:0000269|PubMed:12045205;Dbxref=dbSNP:rs1085307364,PMID:11115378,PMID:12045205 Q13873 UniProtKB Natural variant 519 519 . . . ID=VAR_013683;Note=In PPH1%3B no effect on localization to the cell surface. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12045205;Dbxref=dbSNP:rs1085307365,PMID:12045205 Q13873 UniProtKB Natural variant 775 775 . . . ID=VAR_019996;Note=Unchanged subcellular localization. S->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17344846,ECO:0000269|PubMed:24936649,ECO:0000269|PubMed:28507310;Dbxref=dbSNP:rs2228545,PMID:17344846,PMID:24936649,PMID:28507310 Q13873 UniProtKB Natural variant 863 863 . . . ID=VAR_073042;Note=In PPH1%3B abnormal subcellular localization%3B significant increase in apoptosis of endothelial cells%3B significant decrease in proliferation of endothelial cells%3B significant decrease in nitric oxide synthesis by endothelial cells%3B significant increase in endothelin 1 synthesis by endothelial cells. S->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25187962;Dbxref=dbSNP:rs1006246556,PMID:25187962 Q13873 UniProtKB Natural variant 899 899 . . . ID=VAR_033111;Note=In PPH1%3B leads to constitutive activation of the MAPK14 pathway. R->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15965979;Dbxref=dbSNP:rs137852752,PMID:15965979 Q13873 UniProtKB Sequence conflict 828 828 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q13873 UniProtKB Turn 27 30 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7PPA Q13873 UniProtKB Beta strand 33 35 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HLQ Q13873 UniProtKB Turn 42 47 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HLQ Q13873 UniProtKB Helix 48 50 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HLQ Q13873 UniProtKB Turn 53 56 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HLQ Q13873 UniProtKB Beta strand 57 59 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HLQ Q13873 UniProtKB Beta strand 66 73 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HLQ Q13873 UniProtKB Beta strand 76 84 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HLQ Q13873 UniProtKB Beta strand 90 92 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HLQ Q13873 UniProtKB Turn 105 109 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HLQ Q13873 UniProtKB Beta strand 113 118 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HLQ Q13873 UniProtKB Helix 123 125 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HLQ Q13873 UniProtKB Helix 200 202 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UNP Q13873 UniProtKB Beta strand 203 211 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UNP Q13873 UniProtKB Beta strand 216 222 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UNP Q13873 UniProtKB Beta strand 225 233 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UNP Q13873 UniProtKB Helix 234 236 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UNP Q13873 UniProtKB Helix 237 247 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UNP Q13873 UniProtKB Beta strand 260 267 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UNP Q13873 UniProtKB Beta strand 273 279 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UNP Q13873 UniProtKB Helix 287 293 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UNP Q13873 UniProtKB Helix 298 315 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UNP Q13873 UniProtKB Helix 322 324 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UNP Q13873 UniProtKB Beta strand 338 341 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UNP Q13873 UniProtKB Beta strand 347 349 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UNP Q13873 UniProtKB Beta strand 359 362 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UNP Q13873 UniProtKB Helix 380 382 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UNP Q13873 UniProtKB Helix 385 388 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UNP Q13873 UniProtKB Helix 394 396 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UNP Q13873 UniProtKB Helix 397 417 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UNP Q13873 UniProtKB Helix 421 423 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UNP Q13873 UniProtKB Helix 437 440 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UNP Q13873 UniProtKB Helix 446 453 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UNP Q13873 UniProtKB Helix 471 481 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UNP Q13873 UniProtKB Helix 488 490 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UNP Q13873 UniProtKB Helix 494 506 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6UNP