##gff-version 3 P05771 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12665801;Dbxref=PMID:12665801 P05771 UniProtKB Chain 2 671 . . . ID=PRO_0000055684;Note=Protein kinase C beta type P05771 UniProtKB Domain 158 275 . . . Note=C2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P05771 UniProtKB Domain 342 600 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P05771 UniProtKB Domain 601 671 . . . Note=AGC-kinase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00618 P05771 UniProtKB Zinc finger 36 86 . . . Note=Phorbol-ester/DAG-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00226 P05771 UniProtKB Zinc finger 101 151 . . . Note=Phorbol-ester/DAG-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00226 P05771 UniProtKB Region 311 330 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P05771 UniProtKB Region 614 635 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P05771 UniProtKB Compositional bias 315 330 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P05771 UniProtKB Compositional bias 614 633 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P05771 UniProtKB Active site 466 466 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 P05771 UniProtKB Binding site 186 186 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68403 P05771 UniProtKB Binding site 187 187 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68403 P05771 UniProtKB Binding site 187 187 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68403 P05771 UniProtKB Binding site 193 193 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68403 P05771 UniProtKB Binding site 246 246 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68403 P05771 UniProtKB Binding site 246 246 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68403 P05771 UniProtKB Binding site 247 247 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68403 P05771 UniProtKB Binding site 248 248 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68403 P05771 UniProtKB Binding site 248 248 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68403 P05771 UniProtKB Binding site 248 248 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68403 P05771 UniProtKB Binding site 251 251 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68403 P05771 UniProtKB Binding site 252 252 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68403 P05771 UniProtKB Binding site 254 254 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68403 P05771 UniProtKB Binding site 254 254 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68403 P05771 UniProtKB Binding site 348 356 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P05771 UniProtKB Binding site 371 371 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P05771 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12665801;Dbxref=PMID:12665801 P05771 UniProtKB Modified residue 11 11 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P05771 UniProtKB Modified residue 16 16 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P68403,ECO:0000255 P05771 UniProtKB Modified residue 17 17 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P05771 UniProtKB Modified residue 206 206 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P05771 UniProtKB Modified residue 250 250 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 P05771 UniProtKB Modified residue 311 311 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P05771 UniProtKB Modified residue 314 314 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P05771 UniProtKB Modified residue 324 324 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P68403,ECO:0000255 P05771 UniProtKB Modified residue 500 500 . . . Note=Phosphothreonine%3B by PDPK1;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:17115692;Dbxref=PMID:17115692 P05771 UniProtKB Modified residue 504 504 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19369195;Dbxref=PMID:19369195 P05771 UniProtKB Modified residue 635 635 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68403 P05771 UniProtKB Modified residue 642 642 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:17115692,ECO:0007744|PubMed:23186163;Dbxref=PMID:17115692,PMID:23186163 P05771 UniProtKB Modified residue 661 661 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17115692;Dbxref=PMID:17115692 P05771 UniProtKB Modified residue 662 662 . . . Note=Phosphotyrosine%3B by SYK;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P68404 P05771 UniProtKB Alternative sequence 622 671 . . . ID=VSP_004738;Note=In isoform Beta-II. RDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV->CGRNAENFDRFFTRHPPVLTPPDQEVIRNIDQSEFEGFSFVNSEFLKPEVKS;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:3666134,ECO:0000303|PubMed:3755548;Dbxref=PMID:3666134,PMID:3755548 P05771 UniProtKB Natural variant 144 144 . . . ID=VAR_042304;Note=In a colorectal adenocarcinoma sample%3B somatic mutation. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs764534677,PMID:17344846 P05771 UniProtKB Natural variant 496 496 . . . ID=VAR_042305;Note=In a glioblastoma multiforme sample%3B somatic mutation. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs1466858740,PMID:17344846 P05771 UniProtKB Natural variant 588 588 . . . ID=VAR_042306;Note=P->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs35631544,PMID:17344846 P05771 UniProtKB Sequence conflict 69 69 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 P05771 UniProtKB Beta strand 342 351 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I0E P05771 UniProtKB Beta strand 354 361 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I0E P05771 UniProtKB Beta strand 364 374 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I0E P05771 UniProtKB Helix 375 380 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I0E P05771 UniProtKB Helix 384 394 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I0E P05771 UniProtKB Beta strand 406 411 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I0E P05771 UniProtKB Beta strand 413 421 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I0E P05771 UniProtKB Helix 428 435 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I0E P05771 UniProtKB Helix 440 459 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I0E P05771 UniProtKB Helix 469 471 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I0E P05771 UniProtKB Beta strand 472 474 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I0E P05771 UniProtKB Beta strand 480 482 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I0E P05771 UniProtKB Helix 505 507 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I0E P05771 UniProtKB Helix 510 513 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I0E P05771 UniProtKB Helix 521 536 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I0E P05771 UniProtKB Helix 546 555 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I0E P05771 UniProtKB Helix 566 575 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I0E P05771 UniProtKB Helix 590 595 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I0E P05771 UniProtKB Helix 598 600 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I0E P05771 UniProtKB Helix 605 609 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I0E P05771 UniProtKB Helix 629 636 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I0E P05771 UniProtKB Helix 646 651 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I0E P05771 UniProtKB Turn 654 657 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2I0E P05771 UniProtKB Modified residue 641 641 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19369195,ECO:0007744|PubMed:24275569;Dbxref=PMID:19369195,PMID:24275569 P05771 UniProtKB Modified residue 660 660 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19369195,ECO:0007744|PubMed:24275569;Dbxref=PMID:19369195,PMID:24275569