##gff-version 3 Q99N57 UniProtKB Chain 1 648 . . . ID=PRO_0000086597;Note=RAF proto-oncogene serine/threonine-protein kinase Q99N57 UniProtKB Domain 56 131 . . . Note=RBD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00262 Q99N57 UniProtKB Domain 349 609 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q99N57 UniProtKB Zinc finger 138 184 . . . Note=Phorbol-ester/DAG-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00226 Q99N57 UniProtKB Region 205 265 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q99N57 UniProtKB Region 281 335 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q99N57 UniProtKB Region 331 349 . . . Note=Interaction with PEBP1/RKIP;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q99N57 UniProtKB Compositional bias 222 265 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q99N57 UniProtKB Compositional bias 284 310 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q99N57 UniProtKB Active site 468 468 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 Q99N57 UniProtKB Binding site 139 139 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q99N57 UniProtKB Binding site 152 152 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q99N57 UniProtKB Binding site 155 155 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q99N57 UniProtKB Binding site 165 165 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q99N57 UniProtKB Binding site 168 168 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q99N57 UniProtKB Binding site 173 173 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q99N57 UniProtKB Binding site 176 176 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q99N57 UniProtKB Binding site 184 184 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q99N57 UniProtKB Binding site 355 363 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q99N57 UniProtKB Binding site 375 375 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q99N57 UniProtKB Modified residue 29 29 . . . Note=Phosphoserine%3B by MAPK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15664191;Dbxref=PMID:15664191 Q99N57 UniProtKB Modified residue 43 43 . . . Note=Phosphoserine%3B by PKA and MAPK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15664191;Dbxref=PMID:15664191 Q99N57 UniProtKB Modified residue 233 233 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04049 Q99N57 UniProtKB Modified residue 252 252 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04049 Q99N57 UniProtKB Modified residue 259 259 . . . Note=Phosphoserine%3B by PKA%2C PKC and PKB/AKT1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04049 Q99N57 UniProtKB Modified residue 268 268 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04049 Q99N57 UniProtKB Modified residue 269 269 . . . Note=Phosphothreonine%3B by PKA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04049 Q99N57 UniProtKB Modified residue 289 289 . . . Note=Phosphoserine%3B by MAPK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15664191;Dbxref=PMID:15664191 Q99N57 UniProtKB Modified residue 296 296 . . . Note=Phosphoserine%3B by MAPK1;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:15664191,ECO:0007744|PubMed:21183079;Dbxref=PMID:15664191,PMID:21183079 Q99N57 UniProtKB Modified residue 301 301 . . . Note=Phosphoserine%3B by MAPK1;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:15664191,ECO:0007744|PubMed:21183079;Dbxref=PMID:15664191,PMID:21183079 Q99N57 UniProtKB Modified residue 338 338 . . . Note=Phosphoserine%3B by PAK1%2C PAK2%2C PAK3 and PAK5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04049 Q99N57 UniProtKB Modified residue 339 339 . . . Note=Phosphoserine%3B by PAK1%2C PAK2 and PAK3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04049 Q99N57 UniProtKB Modified residue 340 340 . . . Note=Phosphotyrosine%3B by SRC;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04049 Q99N57 UniProtKB Modified residue 341 341 . . . Note=Phosphotyrosine%3B by SRC;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04049 Q99N57 UniProtKB Modified residue 471 471 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04049 Q99N57 UniProtKB Modified residue 491 491 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04049 Q99N57 UniProtKB Modified residue 494 494 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04049 Q99N57 UniProtKB Modified residue 497 497 . . . Note=Phosphoserine%3B by PKC;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04049 Q99N57 UniProtKB Modified residue 499 499 . . . Note=Phosphoserine%3B by PKC;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04049 Q99N57 UniProtKB Modified residue 563 563 . . . Note=Symmetric dimethylarginine%3B by PRMT5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04049 Q99N57 UniProtKB Modified residue 621 621 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15664191;Dbxref=PMID:15664191 Q99N57 UniProtKB Modified residue 642 642 . . . Note=Phosphoserine%3B by MAPK1;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:15664191,ECO:0007744|PubMed:21183079;Dbxref=PMID:15664191,PMID:21183079 Q99N57 UniProtKB Alternative sequence 278 278 . . . ID=VSP_034629;Note=In isoform 2. E->ESNSLNASPRACSRRFCLRGR;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q99N57 UniProtKB Sequence conflict 522 522 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q99N57 UniProtKB Sequence conflict 543 543 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305