##gff-version 3 P63318 UniProtKB Chain 1 697 . . . ID=PRO_0000055690;Note=Protein kinase C gamma type P63318 UniProtKB Domain 157 275 . . . Note=C2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P63318 UniProtKB Domain 351 614 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P63318 UniProtKB Domain 615 685 . . . Note=AGC-kinase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00618 P63318 UniProtKB Zinc finger 35 85 . . . Note=Phorbol-ester/DAG-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00226 P63318 UniProtKB Zinc finger 100 150 . . . Note=Phorbol-ester/DAG-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00226 P63318 UniProtKB Active site 480 480 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 P63318 UniProtKB Binding site 186 186 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05129 P63318 UniProtKB Binding site 187 187 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05129 P63318 UniProtKB Binding site 187 187 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05129 P63318 UniProtKB Binding site 193 193 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05129 P63318 UniProtKB Binding site 246 246 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05129 P63318 UniProtKB Binding site 246 246 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05129 P63318 UniProtKB Binding site 247 247 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05129 P63318 UniProtKB Binding site 248 248 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05129 P63318 UniProtKB Binding site 248 248 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05129 P63318 UniProtKB Binding site 248 248 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05129 P63318 UniProtKB Binding site 251 251 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05129 P63318 UniProtKB Binding site 252 252 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05129 P63318 UniProtKB Binding site 254 254 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05129 P63318 UniProtKB Binding site 254 254 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05129 P63318 UniProtKB Binding site 357 365 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P63318 UniProtKB Binding site 380 380 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P63318 UniProtKB Modified residue 250 250 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 P63318 UniProtKB Modified residue 320 320 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P63318 UniProtKB Modified residue 322 322 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P63318 UniProtKB Modified residue 326 326 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P63318 UniProtKB Modified residue 328 328 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P63318 UniProtKB Modified residue 330 330 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P63318 UniProtKB Modified residue 332 332 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P63318 UniProtKB Modified residue 373 373 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P63318 UniProtKB Modified residue 514 514 . . . Note=Phosphothreonine%3B by PDPK1;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:17904530;Dbxref=PMID:17904530 P63318 UniProtKB Modified residue 648 648 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000255;evidence=ECO:0000255 P63318 UniProtKB Modified residue 655 655 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17904530,ECO:0000269|PubMed:23185022;Dbxref=PMID:17904530,PMID:23185022 P63318 UniProtKB Modified residue 674 674 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17904530;Dbxref=PMID:17904530 P63318 UniProtKB Modified residue 675 675 . . . Note=Phosphotyrosine%3B by SYK;Ontology_term=ECO:0000250;evidence=ECO:0000250 P63318 UniProtKB Modified residue 687 687 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63319