##gff-version 3
O70161	UniProtKB	Chain	1	661	.	.	.	ID=PRO_0000185463;Note=Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma	
O70161	UniProtKB	Domain	75	443	.	.	.	Note=PIPK;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00781	
O70161	UniProtKB	Region	44	69	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O70161	UniProtKB	Region	525	572	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O70161	UniProtKB	Region	605	661	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O70161	UniProtKB	Region	636	661	.	.	.	Note=Mediates interaction with TLN2	
O70161	UniProtKB	Compositional bias	525	541	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O70161	UniProtKB	Compositional bias	542	571	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O70161	UniProtKB	Compositional bias	613	627	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O70161	UniProtKB	Modified residue	265	265	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60331	
O70161	UniProtKB	Modified residue	268	268	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60331	
O70161	UniProtKB	Modified residue	459	459	.	.	.	Note=Asymmetric dimethylarginine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315	
O70161	UniProtKB	Modified residue	459	459	.	.	.	Note=Omega-N-methylarginine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315	
O70161	UniProtKB	Modified residue	554	554	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5I6B8	
O70161	UniProtKB	Modified residue	634	634	.	.	.	Note=Phosphotyrosine%3B by EGFR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17635937;Dbxref=PMID:17635937	
O70161	UniProtKB	Modified residue	644	644	.	.	.	Note=Phosphotyrosine%3B by CSK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14691141;Dbxref=PMID:14691141	
O70161	UniProtKB	Modified residue	645	645	.	.	.	Note=Phosphoserine%3B by CDK5%2C MAPK1 and CDK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O60331	
O70161	UniProtKB	Modified residue	655	655	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
O70161	UniProtKB	Modified residue	659	659	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5I6B8	
O70161	UniProtKB	Modified residue	661	661	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5I6B8	
O70161	UniProtKB	Alternative sequence	343	402	.	.	.	ID=VSP_016013;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:12693553;Dbxref=PMID:12693553	
O70161	UniProtKB	Alternative sequence	635	635	.	.	.	ID=VSP_016014;Note=In isoform 2. F->FFAHGRYWLFSPRRRQLRAVTPNHTGT;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:12693553;Dbxref=PMID:12693553	
O70161	UniProtKB	Alternative sequence	636	661	.	.	.	ID=VSP_016015;Note=In isoform 3. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:16141072;Dbxref=PMID:15489334,PMID:16141072	
O70161	UniProtKB	Mutagenesis	253	253	.	.	.	Note=Abolishes lipid kinase activity. Does not affect targeting of TLN1 to plasma membrane. Affects assembly of TLN1 into focal adhesions. Affects uropodium formation and retraction of the cell rear. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12422220,ECO:0000269|PubMed:17928408;Dbxref=PMID:12422220,PMID:17928408	
O70161	UniProtKB	Mutagenesis	634	634	.	.	.	Note=Cannot rescue the effect PIP5K1C knockdown on EGF-stimulated cell migration. Does not affect lipid kinase activity. Does not alter binding to tailin. Decreased tailin assembly into focal adhesions. Increased interaction with PLCG1. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17635937;Dbxref=PMID:17635937	
O70161	UniProtKB	Mutagenesis	635	635	.	.	.	Note=Abolishes interaction with AP2B1. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19287005;Dbxref=PMID:19287005	
O70161	UniProtKB	Mutagenesis	642	642	.	.	.	Note=Abolishes interaction with AP2B1. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19287005;Dbxref=PMID:19287005	
O70161	UniProtKB	Mutagenesis	644	644	.	.	.	Note=Loss of phosphorylation by CSK. Abolishes interaction with AP-2 complex. Cannot rescue the effect PIP5K1C knockdown on EGF-stimulated cell migration. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14691141,ECO:0000269|PubMed:16707488,ECO:0000269|PubMed:17635937,ECO:0000269|PubMed:19287005;Dbxref=PMID:14691141,PMID:16707488,PMID:17635937,PMID:19287005	
O70161	UniProtKB	Mutagenesis	645	645	.	.	.	Note=Cannot rescue the effect PIP5K1C knockdown on EGF-stimulated cell migration. Decreased tailin assembly into focal adhesions. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17635937;Dbxref=PMID:17635937	
O70161	UniProtKB	Mutagenesis	646	646	.	.	.	Note=Abolishes interaction with AP-2 complex. P->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16707488;Dbxref=PMID:16707488	
O70161	UniProtKB	Mutagenesis	647	647	.	.	.	Note=Abolishes interaction with AP-2 complex. L->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16707488;Dbxref=PMID:16707488	
O70161	UniProtKB	Sequence conflict	110	110	.	.	.	Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
O70161	UniProtKB	Sequence conflict	122	122	.	.	.	Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305	
O70161	UniProtKB	Beta strand	642	644	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Y19	
O70161	UniProtKB	Helix	646	648	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Y19