##gff-version 3 Q02156 UniProtKB Chain 1 737 . . . ID=PRO_0000055697;Note=Protein kinase C epsilon type Q02156 UniProtKB Domain 1 117 . . . Note=C2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 Q02156 UniProtKB Domain 408 668 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q02156 UniProtKB Domain 669 737 . . . Note=AGC-kinase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00618 Q02156 UniProtKB Zinc finger 169 220 . . . Note=Phorbol-ester/DAG-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00226 Q02156 UniProtKB Zinc finger 242 292 . . . Note=Phorbol-ester/DAG-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00226 Q02156 UniProtKB Region 325 356 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q02156 UniProtKB Region 370 398 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q02156 UniProtKB Motif 223 228 . . . Note=Interaction with actin;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q02156 UniProtKB Compositional bias 330 351 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q02156 UniProtKB Active site 532 532 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 Q02156 UniProtKB Binding site 414 422 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q02156 UniProtKB Binding site 437 437 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q02156 UniProtKB Modified residue 62 62 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16054 Q02156 UniProtKB Modified residue 228 228 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18691976;Dbxref=PMID:18691976 Q02156 UniProtKB Modified residue 234 234 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16054 Q02156 UniProtKB Modified residue 309 309 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:18691976;Dbxref=PMID:18669648,PMID:18691976 Q02156 UniProtKB Modified residue 316 316 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q02156 UniProtKB Modified residue 329 329 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18691976;Dbxref=PMID:18691976 Q02156 UniProtKB Modified residue 337 337 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16054 Q02156 UniProtKB Modified residue 346 346 . . . Note=Phosphoserine%3B by GSK3-beta;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:19662078;Dbxref=PMID:19662078 Q02156 UniProtKB Modified residue 349 349 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16054 Q02156 UniProtKB Modified residue 350 350 . . . Note=Phosphoserine%3B by MAPK11 and MAPK14;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:P16054,ECO:0000305 Q02156 UniProtKB Modified residue 368 368 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000305,ECO:0007744;evidence=ECO:0000305|PubMed:19662078,ECO:0007744|PubMed:23186163;Dbxref=PMID:19662078,PMID:23186163 Q02156 UniProtKB Modified residue 388 388 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18691976;Dbxref=PMID:18691976 Q02156 UniProtKB Modified residue 566 566 . . . Note=Phosphothreonine%3B by PDPK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11964154;Dbxref=PMID:11964154 Q02156 UniProtKB Modified residue 703 703 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q02156 UniProtKB Modified residue 710 710 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18691976;Dbxref=PMID:18691976 Q02156 UniProtKB Modified residue 729 729 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11964154;Dbxref=PMID:11964154 Q02156 UniProtKB Natural variant 143 143 . . . ID=VAR_035466;Note=In a colorectal cancer sample%3B somatic mutation. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16959974;Dbxref=dbSNP:rs772834505,PMID:16959974 Q02156 UniProtKB Natural variant 333 333 . . . ID=VAR_042307;Note=A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs55989965,PMID:17344846 Q02156 UniProtKB Natural variant 389 389 . . . ID=VAR_042308;Note=P->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs55767130,PMID:17344846 Q02156 UniProtKB Natural variant 563 563 . . . ID=VAR_042309;Note=T->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs34077350,PMID:17344846 Q02156 UniProtKB Natural variant 654 654 . . . ID=VAR_050559;Note=A->T;Dbxref=dbSNP:rs35777875 Q02156 UniProtKB Mutagenesis 437 437 . . . Note=Abolishes activity and S-729 phosphorylation. K->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11964154;Dbxref=PMID:11964154 Q02156 UniProtKB Mutagenesis 566 566 . . . Note=Abolishes phosphorylation by PDK1%2C and S-729 phosphorylation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11964154;Dbxref=PMID:11964154 Q02156 UniProtKB Mutagenesis 566 566 . . . Note=No effect on S-729 phosphorylation. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11964154;Dbxref=PMID:11964154 Q02156 UniProtKB Mutagenesis 710 710 . . . Note=No effect on activity%3B no effect on S-729 phosphorylation. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11964154;Dbxref=PMID:11964154 Q02156 UniProtKB Mutagenesis 729 729 . . . Note=Enhances T-566 dephosphorylation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11964154;Dbxref=PMID:11964154