##gff-version 3 Q80UE6 UniProtKB Chain 1 1222 . . . ID=PRO_0000086825;Note=Serine/threonine-protein kinase WNK4 Q80UE6 UniProtKB Domain 171 429 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q80UE6 UniProtKB Region 1 165 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q80UE6 UniProtKB Region 525 562 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q80UE6 UniProtKB Region 554 564 . . . Note=Interaction with KLHL3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96J92 Q80UE6 UniProtKB Region 626 659 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q80UE6 UniProtKB Region 747 809 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q80UE6 UniProtKB Region 877 896 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q80UE6 UniProtKB Region 927 976 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q80UE6 UniProtKB Region 1000 1087 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q80UE6 UniProtKB Region 1166 1222 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q80UE6 UniProtKB Motif 996 999 . . . Note=RFXV motif;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96J92 Q80UE6 UniProtKB Compositional bias 44 60 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q80UE6 UniProtKB Compositional bias 61 78 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q80UE6 UniProtKB Compositional bias 79 99 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q80UE6 UniProtKB Compositional bias 139 160 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q80UE6 UniProtKB Compositional bias 531 555 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q80UE6 UniProtKB Compositional bias 779 800 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q80UE6 UniProtKB Compositional bias 931 945 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q80UE6 UniProtKB Compositional bias 949 971 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q80UE6 UniProtKB Compositional bias 1000 1039 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q80UE6 UniProtKB Compositional bias 1047 1073 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q80UE6 UniProtKB Compositional bias 1168 1183 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q80UE6 UniProtKB Compositional bias 1194 1211 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q80UE6 UniProtKB Active site 318 318 . . . Note=Proton acceptor;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:17360470;Dbxref=PMID:17360470 Q80UE6 UniProtKB Binding site 181 181 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H4A3 Q80UE6 UniProtKB Binding site 251 254 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H4A3 Q80UE6 UniProtKB Binding site 301 301 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H4A3 Q80UE6 UniProtKB Modified residue 95 95 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96J92 Q80UE6 UniProtKB Modified residue 328 328 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9JIH7 Q80UE6 UniProtKB Modified residue 332 332 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9JIH7 Q80UE6 UniProtKB Modified residue 572 572 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96J92 Q80UE6 UniProtKB Modified residue 1014 1014 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q7TPK6 Q80UE6 UniProtKB Modified residue 1196 1196 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q80UE6 UniProtKB Cross-link 154 154 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96J92 Q80UE6 UniProtKB Cross-link 172 172 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96J92 Q80UE6 UniProtKB Cross-link 183 183 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96J92 Q80UE6 UniProtKB Cross-link 223 223 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96J92 Q80UE6 UniProtKB Cross-link 238 238 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96J92 Q80UE6 UniProtKB Cross-link 325 325 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96J92 Q80UE6 UniProtKB Cross-link 384 384 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96J92 Q80UE6 UniProtKB Cross-link 390 390 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96J92 Q80UE6 UniProtKB Cross-link 447 447 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96J92 Q80UE6 UniProtKB Cross-link 451 451 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96J92 Q80UE6 UniProtKB Cross-link 990 990 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96J92 Q80UE6 UniProtKB Cross-link 1123 1123 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96J92 Q80UE6 UniProtKB Cross-link 1136 1136 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96J92 Q80UE6 UniProtKB Cross-link 1137 1137 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q96J92 Q80UE6 UniProtKB Mutagenesis 183 183 . . . Note=Abolished serine/threonine-protein kinase activity without affecting ability to regulate localization of TRPV4 and SLC12A9. K->M;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16403833,ECO:0000269|PubMed:17673510;Dbxref=PMID:16403833,PMID:17673510 Q80UE6 UniProtKB Mutagenesis 318 318 . . . Note=Loss of serine/threonine-protein kinase activity. No effect on inhibition of KCNJ1%2C SCNN1A%2C SCNN1B or SCNN1D. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14608358,ECO:0000269|PubMed:17360470;Dbxref=PMID:14608358,PMID:17360470 Q80UE6 UniProtKB Mutagenesis 318 318 . . . Note=No effect on inhibition of SLC4A4. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21317537;Dbxref=PMID:21317537 Q80UE6 UniProtKB Mutagenesis 559 559 . . . Note=No effect on inhibition of SLC12A3. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12671053;Dbxref=PMID:12671053 Q80UE6 UniProtKB Mutagenesis 561 561 . . . Note=Increased protein level%2C probably due to defects in ubiquitination. Knockin mice display higher blood pressure%2C hyperkalemia%2C hypercalciuria and marked hyperplasia of the distal convoluted tubule cells of kidney. Increased phosphorylation of OXSR1/OSR1 and STK39/SPAK is observed%2C leading to phosphorylation and activation of SLC12A3/NCC. D->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12671053,ECO:0000269|PubMed:17488636,ECO:0000269|PubMed:21486947,ECO:0000269|PubMed:23453970;Dbxref=PMID:12671053,PMID:17488636,PMID:21486947,PMID:23453970 Q80UE6 UniProtKB Mutagenesis 562 562 . . . Note=Increased protein level%2C probably due to defects in ubiquitination. Knockin mice display higher blood pressure%2C hyperkalemia%2C hypercalciuria and marked hyperplasia of the distal convoluted tubule cells of kidney. Q->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12671053,ECO:0000269|PubMed:16964266,ECO:0000269|PubMed:17360470,ECO:0000269|PubMed:23576762;Dbxref=PMID:12671053,PMID:16964266,PMID:17360470,PMID:23576762 Q80UE6 UniProtKB Sequence conflict 179 179 . . . Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q80UE6 UniProtKB Sequence conflict 607 607 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305