BRAF_MOUSE
ID BRAF_MOUSE Reviewed; 751 AA.
AC P28028; E9QNG9; F6SZ47; Q3USE9;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 4.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Serine/threonine-protein kinase B-raf {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P15056};
DE AltName: Full=Proto-oncogene B-Raf;
GN Name=Braf {ECO:0000312|MGI:MGI:88190}; Synonyms=B-raf;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 424-751 (ISOFORM 3).
RX PubMed=2052597; DOI=10.1073/pnas.88.12.5167;
RA Miki T., Fleming T.P., Crescenzi M., Molloy C.J., Blam S.B., Reynolds S.H.,
RA Aaronson S.A.;
RT "Development of a highly efficient expression cDNA cloning system:
RT application to oncogene isolation.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:5167-5171(1991).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316; SER-348; SER-431;
RP SER-432 AND SER-735, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP INTERACTION WITH AKAP13; MAP2K1 AND KSR1.
RX PubMed=21102438; DOI=10.1038/ncb2130;
RA Smith F.D., Langeberg L.K., Cellurale C., Pawson T., Morrison D.K.,
RA Davis R.J., Scott J.D.;
RT "AKAP-Lbc enhances cyclic AMP control of the ERK1/2 cascade.";
RL Nat. Cell Biol. 12:1242-1249(2010).
RN [7]
RP METHYLATION.
RX PubMed=21917714; DOI=10.1126/scisignal.2001936;
RA Andreu-Perez P., Esteve-Puig R., de Torre-Minguela C., Lopez-Fauqued M.,
RA Bech-Serra J.J., Tenbaum S., Garcia-Trevijano E.R., Canals F., Merlino G.,
RA Avila M.A., Recio J.A.;
RT "Protein arginine methyltransferase 5 regulates ERK1/2 signal transduction
RT amplitude and cell fate through CRAF.";
RL Sci. Signal. 4:RA58-RA58(2011).
CC -!- FUNCTION: Involved in the transduction of mitogenic signals from the
CC cell membrane to the nucleus. Phosphorylates MAP2K1, and thereby
CC activates the MAP kinase signal transduction pathway. May play a role
CC in the postsynaptic responses of hippocampal neurons.
CC {ECO:0000250|UniProtKB:P15056}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:P15056};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P15056};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000305};
CC -!- ACTIVITY REGULATION: In quiescent cells, maintained in an inactive
CC state via an intramolecular interaction between the protein kinase and
CC N-terminal domains. Following mitogen-mediated cell activation, binds
CC via its RGB domain to active HRAS (GTP-bound) which releases the
CC inhibitory intramolecular interaction between the two domains. This
CC allows the MAP2K1-mediated dimerization of KSR1 or KSR2, and BRAF which
CC activates BRAF. {ECO:0000250|UniProtKB:P15056}.
CC -!- SUBUNIT: Monomer. Homodimer. Heterodimerizes with RAF1, and the
CC heterodimer possesses a highly increased kinase activity compared to
CC the respective homodimers or monomers. Heterodimerization is mitogen-
CC regulated and enhanced by 14-3-3 proteins. MAPK1/ERK2 activation can
CC induce a negative feedback that promotes the dissociation of the
CC heterodimer by phosphorylating BRAF at Thr-738. Heterodimerizes (via N-
CC terminus) with KSR1 (via N-terminus) or KSR2 (via N-terminus) in a
CC MAP2K1-dependent manner (By similarity). Interacts with MAP2K1 and
CC MAP2K2 (By similarity). Found in a complex with at least BRAF, HRAS,
CC MAP2K1, MAPK3 and RGS14. Interacts with RIT1. Interacts (via N-
CC terminus) with RGS14 (via RBD domains); the interaction mediates the
CC formation of a ternary complex with RAF1, a ternary complex inhibited
CC by GNAI1 (By similarity). Interacts with DGKH (By similarity).
CC Interacts with PRMT5 (By similarity). Interacts with AKAP13, MAP2K1 and
CC KSR1. Identified in a complex with AKAP13, KSR1 and MAP2K1
CC (PubMed:21102438). Interacts with FNIP1 and FNIP2 (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P15056,
CC ECO:0000269|PubMed:21102438}.
CC -!- INTERACTION:
CC P28028; Q99N57: Raf1; NbExp=2; IntAct=EBI-2584830, EBI-397757;
CC P28028; P01111: NRAS; Xeno; NbExp=2; IntAct=EBI-2584830, EBI-721993;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cell membrane {ECO:0000250}. Note=Colocalizes with RGS14 and RAF1 in
CC both the cytoplasm and membranes. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=3;
CC IsoId=P28028-3; Sequence=Displayed;
CC Name=1;
CC IsoId=P28028-1; Sequence=VSP_060878, VSP_060879, VSP_060880;
CC -!- PTM: Phosphorylation at Ser-348 by SGK1 inhibits its activity.
CC {ECO:0000250}.
CC -!- PTM: Methylation by PRMT5 decreases stability and kinase activity.
CC {ECO:0000269|PubMed:21917714}.
CC -!- PTM: Ubiquitinated by RNF149; which leads to proteasomal degradation.
CC Polyubiquitinated at Lys-615 in response to EGF (By similarity).
CC {ECO:0000250}.
CC -!- DISEASE: Note=Participates in a chromosomal translocation that produces
CC a Tif1a-BRAF (T18) oncogene originally isolated from a furfural-induced
CC hepatoma.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. RAF subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA37320.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK140431; BAE24384.1; -; mRNA.
DR EMBL; AC122345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC163109; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M64429; AAA37320.1; ALT_SEQ; mRNA.
DR CCDS; CCDS39463.1; -. [P28028-1]
DR PIR; A40951; TVMSBF.
DR RefSeq; NP_647455.3; NM_139294.5. [P28028-1]
DR AlphaFoldDB; P28028; -.
DR BMRB; P28028; -.
DR SMR; P28028; -.
DR BioGRID; 225124; 77.
DR CORUM; P28028; -.
DR DIP; DIP-57050N; -.
DR IntAct; P28028; 10.
DR MINT; P28028; -.
DR STRING; 10090.ENSMUSP00000002487; -.
DR BindingDB; P28028; -.
DR ChEMBL; CHEMBL2331061; -.
DR iPTMnet; P28028; -.
DR PhosphoSitePlus; P28028; -.
DR SwissPalm; P28028; -.
DR EPD; P28028; -.
DR jPOST; P28028; -.
DR MaxQB; P28028; -.
DR PaxDb; P28028; -.
DR PeptideAtlas; P28028; -.
DR PRIDE; P28028; -.
DR ProteomicsDB; 273625; -. [P28028-3]
DR ProteomicsDB; 320910; -.
DR Antibodypedia; 751; 2292 antibodies from 51 providers.
DR DNASU; 109880; -.
DR Ensembl; ENSMUST00000002487; ENSMUSP00000002487; ENSMUSG00000002413. [P28028-1]
DR GeneID; 109880; -.
DR KEGG; mmu:109880; -.
DR UCSC; uc009bme.2; mouse. [P28028-3]
DR UCSC; uc009bmg.1; mouse.
DR CTD; 673; -.
DR MGI; MGI:88190; Braf.
DR VEuPathDB; HostDB:ENSMUSG00000002413; -.
DR eggNOG; KOG0193; Eukaryota.
DR GeneTree; ENSGT00940000156154; -.
DR HOGENOM; CLU_023684_1_0_1; -.
DR InParanoid; P28028; -.
DR OMA; MYLMEYQ; -.
DR OrthoDB; 243095at2759; -.
DR PhylomeDB; P28028; -.
DR TreeFam; TF317006; -.
DR Reactome; R-MMU-1295596; Spry regulation of FGF signaling.
DR Reactome; R-MMU-170968; Frs2-mediated activation.
DR Reactome; R-MMU-5673000; RAF activation.
DR Reactome; R-MMU-5674135; MAP2K and MAPK activation.
DR Reactome; R-MMU-5674499; Negative feedback regulation of MAPK pathway.
DR Reactome; R-MMU-5675221; Negative regulation of MAPK pathway.
DR BioGRID-ORCS; 109880; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Braf; mouse.
DR PRO; PR:P28028; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P28028; protein.
DR Bgee; ENSMUSG00000002413; Expressed in embryonic post-anal tail and 220 other tissues.
DR ExpressionAtlas; P28028; baseline and differential.
DR Genevisible; P28028; MM.
DR GO; GO:0044297; C:cell body; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004708; F:MAP kinase kinase activity; ISO:MGI.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IDA:BHF-UCL.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0046632; P:alpha-beta T cell differentiation; IMP:MGI.
DR GO; GO:0043369; P:CD4-positive or CD8-positive, alpha-beta T cell lineage commitment; IMP:MGI.
DR GO; GO:0043367; P:CD4-positive, alpha-beta T cell differentiation; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IGI:MGI.
DR GO; GO:0071277; P:cellular response to calcium ion; ISO:MGI.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:MGI.
DR GO; GO:0072577; P:endothelial cell apoptotic process; IMP:MGI.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IMP:MGI.
DR GO; GO:0090150; P:establishment of protein localization to membrane; ISO:MGI.
DR GO; GO:0060324; P:face development; IGI:MGI.
DR GO; GO:0060323; P:head morphogenesis; IMP:MGI.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
DR GO; GO:0000165; P:MAPK cascade; ISO:MGI.
DR GO; GO:0002318; P:myeloid progenitor cell differentiation; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IMP:MGI.
DR GO; GO:0010764; P:negative regulation of fibroblast migration; IMP:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR GO; GO:2000301; P:negative regulation of synaptic vesicle exocytosis; IMP:MGI.
DR GO; GO:0048680; P:positive regulation of axon regeneration; IDA:MGI.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IMP:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:MGI.
DR GO; GO:0010828; P:positive regulation of glucose transmembrane transport; ISO:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:MGI.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:MGI.
DR GO; GO:0043368; P:positive T cell selection; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:BHF-UCL.
DR GO; GO:0048679; P:regulation of axon regeneration; IGI:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0045580; P:regulation of T cell differentiation; IMP:MGI.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IGI:MGI.
DR GO; GO:0043149; P:stress fiber assembly; IMP:MGI.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:MGI.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IMP:MGI.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IDA:MGI.
DR GO; GO:0048538; P:thymus development; IGI:MGI.
DR GO; GO:0030878; P:thyroid gland development; IGI:MGI.
DR GO; GO:0070413; P:trehalose metabolism in response to stress; ISO:MGI.
DR GO; GO:0008542; P:visual learning; IMP:MGI.
DR CDD; cd00029; C1; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR003116; RBD_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF02196; RBD; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00455; RBD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50898; RBD; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Allosteric enzyme; Alternative splicing; ATP-binding;
KW Cell membrane; Chromosomal rearrangement; Cytoplasm; Isopeptide bond;
KW Kinase; Membrane; Metal-binding; Methylation; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Proto-oncogene; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P15056"
FT CHAIN 2..751
FT /note="Serine/threonine-protein kinase B-raf"
FT /id="PRO_0000085666"
FT DOMAIN 139..211
FT /note="RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00262"
FT DOMAIN 442..702
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 561
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 448..456
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 468
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P15056"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15056"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 356
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P15056"
FT MOD_RES 379
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15056"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15056"
FT MOD_RES 384
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15056"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 656
FT /note="Omega-N-methylarginine; by PRMT5"
FT /evidence="ECO:0000250|UniProtKB:P15056"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15056"
FT MOD_RES 735
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 738
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:P15056"
FT CROSSLNK 563
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P15056"
FT VAR_SEQ 363
FT /note="D -> DEKFPEVELQDQR (in isoform 1)"
FT /id="VSP_060878"
FT VAR_SEQ 375
FT /note="G -> GAPLNQLMRCLRKYQSRTPSPLLHSVPSEIVFDFEPGPVFR (in
FT isoform 1)"
FT /id="VSP_060879"
FT VAR_SEQ 747..751
FT /note="GFPVH -> EFAAFK (in isoform 1)"
FT /id="VSP_060880"
FT CONFLICT 10..11
FT /note="SS -> RR (in Ref. 1; BAE24384)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 751 AA; 82515 MW; 0643D7F6C44A9A05 CRC64;
MAALSGGGGS SSGGGGGGGG GGGGGDGGGG AEQGQALFNG DMEPEAGAGA AASSAADPAI
PEEVWNIKQM IKLTQEHIEA LLDKFGGEHN PPSIYLEAYE EYTSKLDALQ QREQQLLESL
VFQTPTDASR NNPKSPQKPI VRVFLPNKQR TVVPARCGVT VRDSLKKALM MRGLIPECCA
VYRIQDGEKK PIGWDTDISW LTGEELHVEV LENVPLTTHN FVRKTFFTLA FCDFCRKLLF
QGFRCQTCGY KFHQRCSTEV PLMCVNYDQL DLLFVSKFFE HHPVPQEEAS FPETALPSGS
SSAPPSDSTG PQILTSPSPS KSIPIPQPFR PADEDHRNQF GQRDRSSSAP NVHINTIEPV
NIDDLIRDQG FRGDGGSTTG LSATPPASLP GSLTNVKALQ KSPGPQRERK SSSSSSSEDR
SRMKTLGRRD SSDDWEIPDG QITVGQRIGS GSFGTVYKGK WHGDVAVKML NVTAPTPQQL
QAFKNEVGVL RKTRHVNILL FMGYSTKPQL AIVTQWCEGS SLYHHLHIIE TKFEMIKLID
IARQTAQGMD YLHAKSIIHR DLKSNNIFLH EDLTVKIGDF GLATVKSRWS GSHQFEQLSG
SILWMAPEVI RMQDKNPYSF QSDVYAFGIV LYELMTGQLP YSNINNRDQI IFMVGRGYLS
PDLSKVRSNC PKAMKRLMAE CLKKKRDERP LFPQILASIE LLARSLPKIH RSASEPSLNR
AGFQTEDFSL YACASPKTPI QAGGYGGFPV H
