##gff-version 3 Q9Z1T6 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2I7 Q9Z1T6 UniProtKB Chain 2 2097 . . . ID=PRO_0000185453;Note=1-phosphatidylinositol 3-phosphate 5-kinase Q9Z1T6 UniProtKB Domain 365 440 . . . Note=DEP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00066 Q9Z1T6 UniProtKB Domain 1757 2083 . . . Note=PIPK;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00781 Q9Z1T6 UniProtKB Zinc finger 158 218 . . . Note=FYVE-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091 Q9Z1T6 UniProtKB Region 1 44 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z1T6 UniProtKB Region 56 122 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z1T6 UniProtKB Region 442 469 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z1T6 UniProtKB Region 484 505 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z1T6 UniProtKB Region 616 868 . . . Note=Chaperonin-like domain;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14530284;Dbxref=PMID:14530284 Q9Z1T6 UniProtKB Region 895 928 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z1T6 UniProtKB Region 989 1022 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z1T6 UniProtKB Region 1171 1194 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z1T6 UniProtKB Region 1511 1555 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z1T6 UniProtKB Region 1697 1742 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z1T6 UniProtKB Region 1781 1800 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z1T6 UniProtKB Region 1841 2097 . . . Note=Catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2I7 Q9Z1T6 UniProtKB Compositional bias 1 22 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z1T6 UniProtKB Compositional bias 62 91 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z1T6 UniProtKB Compositional bias 94 118 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z1T6 UniProtKB Compositional bias 442 461 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z1T6 UniProtKB Compositional bias 990 1007 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z1T6 UniProtKB Compositional bias 1717 1733 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Z1T6 UniProtKB Binding site 164 164 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091 Q9Z1T6 UniProtKB Binding site 167 167 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091 Q9Z1T6 UniProtKB Binding site 180 180 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091 Q9Z1T6 UniProtKB Binding site 183 183 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091 Q9Z1T6 UniProtKB Binding site 188 188 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091 Q9Z1T6 UniProtKB Binding site 191 191 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091 Q9Z1T6 UniProtKB Binding site 210 210 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091 Q9Z1T6 UniProtKB Binding site 213 213 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00091 Q9Z1T6 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2I7 Q9Z1T6 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2I7 Q9Z1T6 UniProtKB Modified residue 48 48 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2I7 Q9Z1T6 UniProtKB Modified residue 88 88 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2I7 Q9Z1T6 UniProtKB Modified residue 299 299 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q9Z1T6 UniProtKB Modified residue 307 307 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2I7 Q9Z1T6 UniProtKB Modified residue 312 312 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q9Z1T6 UniProtKB Modified residue 318 318 . . . Note=Phosphoserine%3B by PKB/AKT1 or PKB/AKT2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2I7 Q9Z1T6 UniProtKB Modified residue 329 329 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2I7 Q9Z1T6 UniProtKB Modified residue 475 475 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q9Z1T6 UniProtKB Modified residue 1543 1543 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2I7 Q9Z1T6 UniProtKB Modified residue 1548 1548 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2I7 Q9Z1T6 UniProtKB Modified residue 1668 1668 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2I7 Q9Z1T6 UniProtKB Modified residue 1753 1753 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q9Z1T6 UniProtKB Modified residue 1968 1968 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2I7 Q9Z1T6 UniProtKB Modified residue 2052 2052 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Y2I7 Q9Z1T6 UniProtKB Alternative sequence 107 107 . . . ID=VSP_034953;Note=In isoform 2. L->LENTLPHPQEST;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:9858586;Dbxref=PMID:9858586 Q9Z1T6 UniProtKB Alternative sequence 490 545 . . . ID=VSP_034954;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:9858586;Dbxref=PMID:9858586 Q9Z1T6 UniProtKB Alternative sequence 490 497 . . . ID=VSP_034955;Note=In isoform 3. NSASPSKR->SKFGFLML;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:16141072;Dbxref=PMID:16141072 Q9Z1T6 UniProtKB Alternative sequence 498 2097 . . . ID=VSP_034956;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:16141072;Dbxref=PMID:16141072 Q9Z1T6 UniProtKB Mutagenesis 1831 1831 . . . Note=Loss of kinase activity. Decreases RABEPK location to membranes. Abolishes EGFR translocation to the nucleus. K->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11123925,ECO:0000269|PubMed:14530284,ECO:0000269|PubMed:17909029;Dbxref=PMID:11123925,PMID:14530284,PMID:17909029 Q9Z1T6 UniProtKB Sequence conflict 546 546 . . . Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Z1T6 UniProtKB Sequence conflict 944 944 . . . Note=K->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Z1T6 UniProtKB Sequence conflict 994 995 . . . Note=QP->HR;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Z1T6 UniProtKB Sequence conflict 1107 1107 . . . Note=R->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Z1T6 UniProtKB Sequence conflict 1141 1141 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Z1T6 UniProtKB Sequence conflict 1264 1264 . . . Note=S->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Z1T6 UniProtKB Sequence conflict 1996 1996 . . . Note=V->E;Ontology_term=ECO:0000305;evidence=ECO:0000305