ID BRAF_HUMAN Reviewed; 766 AA.
AC P15056; A4D1T4; B6HY61; B6HY62; B6HY63; B6HY64; B6HY65; B6HY66; Q13878;
AC Q3MIN6; Q9UDP8; Q9Y6T3;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 4.
DT 27-MAR-2024, entry version 259.
DE RecName: Full=Serine/threonine-protein kinase B-raf {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:21441910, ECO:0000269|PubMed:29433126};
DE AltName: Full=Proto-oncogene B-Raf;
DE AltName: Full=p94;
DE AltName: Full=v-Raf murine sarcoma viral oncogene homolog B1;
GN Name=BRAF {ECO:0000312|HGNC:HGNC:1097}; Synonyms=BRAF1, RAFB1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP PHOSPHORYLATION AT THR-373.
RC TISSUE=Testis;
RX PubMed=1508179; DOI=10.1128/mcb.12.9.3733-3742.1992;
RA Stephens R.M., Sithanandam G., Copeland T.D., Kaplan D.R., Rapp U.R.,
RA Morrison D.K.;
RT "95-kilodalton B-Raf serine/threonine kinase: identification of the protein
RT and its major autophosphorylation site.";
RL Mol. Cell. Biol. 12:3733-3742(1992).
RN [2]
RP SEQUENCE REVISION TO 31-33.
RA Albert S., Wixler L., Rapp U.R.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-200.
RC TISSUE=Placenta;
RX PubMed=1630826;
RA Eychene A., Barnier J.V., Apiou F., Dutrillaux B., Calothy G.;
RT "Chromosomal assignment of two human B-raf(Rmil) proto-oncogene loci: B-
RT raf-1 encoding the p94Braf/Rmil and B-raf-2, a processed pseudogene.";
RL Oncogene 7:1657-1660(1992).
RN [8]
RP PROTEIN SEQUENCE OF 2-51; 56-95; 151-158; 189-199; 253-260; 294-354;
RP 361-424; 444-507; 510-522; 559-570; 579-626; 663-680; 692-698; 702-719;
RP 727-735 AND 753-766, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, PHOSPHORYLATION AT SER-365; THR-396; SER-399; THR-401 AND SER-729,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma, and Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Zebisch A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 117-766.
RC TISSUE=Testis;
RX PubMed=2284096;
RA Sithanandam G., Kolch W., Duh F.-M., Rapp U.R.;
RT "Complete coding sequence of a human B-raf cDNA and detection of B-raf
RT protein kinase with isozyme specific antibodies.";
RL Oncogene 5:1775-1780(1990).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 381-766, DISEASE, AND CHROMOSOMAL
RP REARRANGEMENT.
RC TISSUE=Brain;
RX PubMed=18974108; DOI=10.1158/0008-5472.can-08-2097;
RA Jones D.T.W., Kocialkowski S., Liu L., Pearson D.M., Backlund L.M.,
RA Ichimura K., Collins V.P.;
RT "Tandem duplication producing a novel oncogenic BRAF fusion gene defines
RT the majority of pilocytic astrocytomas.";
RL Cancer Res. 68:8673-8677(2008).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 439-766.
RX PubMed=3043188; DOI=10.1128/mcb.8.6.2651-2654.1988;
RA Ikawa S., Fukui M., Ueyama Y., Tamaoki N., Yamamoto T., Toyoshima K.;
RT "B-raf, a new member of the raf family, is activated by DNA
RT rearrangement.";
RL Mol. Cell. Biol. 8:2651-2654(1988).
RN [12]
RP PHOSPHORYLATION AT SER-365 BY SGK1.
RX PubMed=11410590; DOI=10.1074/jbc.m102808200;
RA Zhang B.H., Tang E.D., Zhu T., Greenberg M.E., Vojtek A.B., Guan K.L.;
RT "Serum- and glucocorticoid-inducible kinase SGK phosphorylates and
RT negatively regulates B-Raf.";
RL J. Biol. Chem. 276:31620-31626(2001).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401; SER-446; SER-447 AND
RP SER-729, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP SUBUNIT, INTERACTION WITH DGKH, SUBCELLULAR LOCATION, AND PHOSPHORYLATION
RP AT THR-753 BY MAPK1.
RX PubMed=19710016; DOI=10.1074/jbc.m109.043604;
RA Yasuda S., Kai M., Imai S., Takeishi K., Taketomi A., Toyota M., Kanoh H.,
RA Sakane F.;
RT "Diacylglycerol kinase eta augments C-Raf activity and B-Raf/C-Raf
RT heterodimerization.";
RL J. Biol. Chem. 284:29559-29570(2009).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [18]
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 [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
RP INTERACTION WITH KSR2, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION, AND
RP MUTAGENESIS OF LYS-483.
RX PubMed=21441910; DOI=10.1038/nature09860;
RA Brennan D.F., Dar A.C., Hertz N.T., Chao W.C., Burlingame A.L.,
RA Shokat K.M., Barford D.;
RT "A Raf-induced allosteric transition of KSR stimulates phosphorylation of
RT MEK.";
RL Nature 472:366-369(2011).
RN [21]
RP INTERACTION WITH PRMT5, METHYLATION AT ARG-671, CHARACTERIZATION OF VARIANT
RP CRC GLU-600, AND MUTAGENESIS OF ARG-671.
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).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [23]
RP UBIQUITINATION BY RNF149.
RX PubMed=22628551; DOI=10.1074/jbc.m111.319822;
RA Hong S.W., Jin D.H., Shin J.S., Moon J.H., Na Y.S., Jung K.A., Kim S.M.,
RA Kim J.C., Kim K.P., Hong Y.S., Lee J.L., Choi E.K., Lee J.S., Kim T.W.;
RT "Ring finger protein 149 is an E3 ubiquitin ligase active on wild-type v-
RT Raf murine sarcoma viral oncogene homolog B1 (BRAF).";
RL J. Biol. Chem. 287:24017-24025(2012).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151; SER-365; THR-401;
RP SER-446 AND SER-729, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [25]
RP UBIQUITINATION AT LYS-578, AND MUTAGENESIS OF LYS-578.
RX PubMed=23907581; DOI=10.1038/srep02344;
RA An L., Jia W., Yu Y., Zou N., Liang L., Zhao Y., Fan Y., Cheng J., Shi Z.,
RA Xu G., Li G., Yang J., Zhang H.;
RT "Lys63-linked polyubiquitination of BRAF at lysine 578 is required for
RT BRAF-mediated signaling.";
RL Sci. Rep. 3:2344-2344(2013).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [27]
RP INTERACTION WITH FNIP1 AND FNIP2.
RX PubMed=27353360; DOI=10.1038/ncomms12037;
RA Woodford M.R., Dunn D.M., Blanden A.R., Capriotti D., Loiselle D.,
RA Prodromou C., Panaretou B., Hughes P.F., Smith A., Ackerman W.,
RA Haystead T.A., Loh S.N., Bourboulia D., Schmidt L.S., Marston Linehan W.,
RA Bratslavsky G., Mollapour M.;
RT "The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance
RT drug binding.";
RL Nat. Commun. 7:12037-12037(2016).
RN [28]
RP INTERACTION WITH YWHAZ.
RX PubMed=31024343; DOI=10.3389/fphys.2019.00388;
RA Popov I.K., Hiatt S.M., Whalen S., Keren B., Ruivenkamp C.,
RA van Haeringen A., Chen M.J., Cooper G.M., Korf B.R., Chang C.;
RT "A YWHAZ variant associated with cardiofaciocutaneous syndrome activates
RT the RAF-ERK pathway.";
RL Front. Physiol. 10:388-388(2019).
RN [29]
RP FUNCTION, AND SUBUNIT.
RX PubMed=36402789; DOI=10.1038/s41467-022-34907-0;
RA McGrail K., Granado-Martinez P., Esteve-Puig R., Garcia-Ortega S., Ding Y.,
RA Sanchez-Redondo S., Ferrer B., Hernandez-Losa J., Canals F., Manzano A.,
RA Navarro-Sabate A., Bartrons R., Yanes O., Perez-Alea M., Munoz-Couselo E.,
RA Garcia-Patos V., Recio J.A.;
RT "BRAF activation by metabolic stress promotes glycolysis sensitizing
RT NRASQ61-mutated melanomas to targeted therapy.";
RL Nat. Commun. 13:7113-7113(2022).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 444-719 IN COMPLEX WITH
RP INHIBITOR.
RX PubMed=18287029; DOI=10.1073/pnas.0711741105;
RA Tsai J., Lee J.T., Wang W., Zhang J., Cho H., Mamo S., Bremer R.,
RA Gillette S., Kong J., Haass N.K., Sproesser K., Li L., Smalley K.S.,
RA Fong D., Zhu Y.L., Marimuthu A., Nguyen H., Lam B., Liu J., Cheung I.,
RA Rice J., Suzuki Y., Luu C., Settachatgul C., Shellooe R., Cantwell J.,
RA Kim S.H., Schlessinger J., Zhang K.Y., West B.L., Powell B., Habets G.,
RA Zhang C., Ibrahim P.N., Hirth P., Artis D.R., Herlyn M., Bollag G.;
RT "Discovery of a selective inhibitor of oncogenic B-Raf kinase with potent
RT antimelanoma activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:3041-3046(2008).
RN [31] {ECO:0007744|PDB:5VR3, ECO:0007744|PDB:5VYK}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 36-110, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH KSR1; KSR2; MAP2K1 AND
RP MAP2K2, AND MUTAGENESIS OF MET-53; LYS-88; ARG-509 AND ILE-666.
RX PubMed=29433126; DOI=10.1038/nature25478;
RA Lavoie H., Sahmi M., Maisonneuve P., Marullo S.A., Thevakumaran N., Jin T.,
RA Kurinov I., Sicheri F., Therrien M.;
RT "MEK drives BRAF activation through allosteric control of KSR proteins.";
RL Nature 554:549-553(2018).
RN [32]
RP VARIANTS LNCR VAL-466 AND ARG-597.
RX PubMed=12460919;
RA Naoki K., Chen T.-H., Richards W.G., Sugarbaker D.J., Meyerson M.;
RT "Missense mutations of the BRAF gene in human lung adenocarcinoma.";
RL Cancer Res. 62:7001-7003(2002).
RN [33]
RP VARIANTS CANCER GLU-464; VAL-464; ALA-466; GLU-466; VAL-466; ALA-469;
RP GLU-469; LYS-586; LEU-595; ARG-596; ARG-597; VAL-597; GLU-600 AND ASP-600,
RP AND CHARACTERIZATION OF VARIANTS CANCER VAL-464; ALA-469; VAL-597 AND
RP GLU-600.
RX PubMed=12068308; DOI=10.1038/nature00766;
RA Davies H., Bignell G.R., Cox C., Stephens P., Edkins S., Clegg S.,
RA Teague J., Woffendin H., Garnett M.J., Bottomley W., Davis N., Dicks E.,
RA Ewing R., Floyd Y., Gray K., Hall S., Hawes R., Hughes J., Kosmidou V.,
RA Menzies A., Mould C., Parker A., Stevens C., Watt S., Hooper S., Wilson R.,
RA Jayatilake H., Gusterson B.A., Cooper C., Shipley J., Hargrave D.,
RA Pritchard-Jones K., Maitland N., Chenevix-Trench G., Riggins G.J.,
RA Bigner D.D., Palmieri G., Cossu A., Flanagan A., Nicholson A., Ho J.W.C.,
RA Leung S.Y., Yuen S.T., Weber B.L., Seigler H.F., Darrow T.L., Paterson H.,
RA Marais R., Marshall C.J., Wooster R., Stratton M.R., Futreal P.A.;
RT "Mutations of the BRAF gene in human cancer.";
RL Nature 417:949-954(2002).
RN [34]
RP VARIANTS CRC ILE-462; SER-463; GLU-464; GLU-600 AND GLU-601.
RX PubMed=12198537; DOI=10.1038/418934a;
RA Rajagopalan H., Bardelli A., Lengauer C., Kinzler K.W., Vogelstein B.,
RA Velculescu V.E.;
RT "Tumorigenesis: RAF/RAS oncogenes and mismatch-repair status.";
RL Nature 418:934-934(2002).
RN [35]
RP VARIANTS NHL ALA-469; ARG-469 AND GLY-594.
RX PubMed=14612909; DOI=10.1038/sj.bjc.6601371;
RA Lee J.W., Yoo N.J., Soung Ark W.S., Kim S.Y., Lee J.H., Park J.Y.,
RA Cho Y.G., Kim C.J., Ko Y.H., Kim S.H., Nam S.W., Lee J.Y., Lee S.H.;
RT "BRAF mutations in non-Hodgkin's lymphoma.";
RL Br. J. Cancer 89:1958-1960(2003).
RN [36]
RP CHARACTERIZATION OF VARIANT MELANOMA GLU-600.
RX PubMed=14500344;
RA Hingorani S.R., Jacobetz M.A., Robertson G.P., Herlyn M., Tuveson D.A.;
RT "Suppression of BRAF(V599E) in human melanoma abrogates transformation.";
RL Cancer Res. 63:5198-5202(2003).
RN [37]
RP VARIANTS CFC1 PRO-246; ARG-257; GLU-469; PHE-485; GLU-499; LYS-501; GLY-501
RP AND ASP-581.
RX PubMed=16474404; DOI=10.1038/ng1749;
RA Niihori T., Aoki Y., Narumi Y., Neri G., Cave H., Verloes A., Okamoto N.,
RA Hennekam R.C.M., Gillessen-Kaesbach G., Wieczorek D., Kavamura M.I.,
RA Kurosawa K., Ohashi H., Wilson L., Heron D., Bonneau D., Corona G.,
RA Kaname T., Naritomi K., Baumann C., Matsumoto N., Kato K., Kure S.,
RA Matsubara Y.;
RT "Germline KRAS and BRAF mutations in cardio-facio-cutaneous syndrome.";
RL Nat. Genet. 38:294-296(2006).
RN [38]
RP VARIANT [LARGE SCALE ANALYSIS] GLU-600.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [39]
RP VARIANTS CFC1 ARG-257; ALA-467; SER-468; GLU-469; PHE-485; GLU-499;
RP LYS-501; GLY-501; ASP-581; LEU-595 AND VAL-596.
RX PubMed=16439621; DOI=10.1126/science.1124642;
RA Rodriguez-Viciana P., Tetsu O., Tidyman W.E., Estep A.L., Conger B.A.,
RA Cruz M.S., McCormick F., Rauen K.A.;
RT "Germline mutations in genes within the MAPK pathway cause cardio-facio-
RT cutaneous syndrome.";
RL Science 311:1287-1290(2006).
RN [40]
RP VARIANTS [LARGE SCALE ANALYSIS] SER-301; ALA-469; VAL-469; SER-581;
RP ARG-596; ARG-597; VAL-597 AND GLU-600.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [41]
RP VARIANTS CFC1 PRO-241; PRO-244; PRO-246; ARG-257; LYS-262; SER-468;
RP GLU-469; GLU-499; ASN-499; ASP-580; ASP-581 AND LEU-595.
RX PubMed=18042262; DOI=10.1111/j.1399-0004.2007.00931.x;
RA Schulz A.L., Albrecht B., Arici C., van der Burgt I., Buske A.,
RA Gillessen-Kaesbach G., Heller R., Horn D., Hubner C.A., Korenke G.C.,
RA Konig R., Kress W., Kruger G., Meinecke P., Mucke J., Plecko B.,
RA Rossier E., Schinzel A., Schulze A., Seemanova E., Seidel H., Spranger S.,
RA Tuysuz B., Uhrig S., Wieczorek D., Kutsche K., Zenker M.;
RT "Mutation and phenotypic spectrum in patients with cardio-facio-cutaneous
RT and Costello syndrome.";
RL Clin. Genet. 73:62-70(2008).
RN [42]
RP VARIANT LPRD3 PRO-241, VARIANTS NS7 ARG-241; MET-241; CYS-531 AND VAL-597,
RP AND VARIANTS CFC1 PHE-245; PRO-246; ARG-257; LYS-275; GLU-469; PHE-485;
RP ASN-499; LYS-501; PRO-525; LEU-595; ARG-599; GLN-601; GLU-638 AND ARG-709.
RX PubMed=19206169; DOI=10.1002/humu.20955;
RA Sarkozy A., Carta C., Moretti S., Zampino G., Digilio M.C., Pantaleoni F.,
RA Scioletti A.P., Esposito G., Cordeddu V., Lepri F., Petrangeli V.,
RA Dentici M.L., Mancini G.M., Selicorni A., Rossi C., Mazzanti L., Marino B.,
RA Ferrero G.B., Silengo M.C., Memo L., Stanzial F., Faravelli F., Stuppia L.,
RA Puxeddu E., Gelb B.D., Dallapiccola B., Tartaglia M.;
RT "Germline BRAF mutations in Noonan, LEOPARD, and cardiofaciocutaneous
RT syndromes: molecular diversity and associated phenotypic spectrum.";
RL Hum. Mutat. 30:695-702(2009).
RN [43]
RP VARIANT CRC GLU-600.
RX PubMed=23263490; DOI=10.1038/ng.2503;
RG CORGI Consortium;
RG WGS500 Consortium;
RA Palles C., Cazier J.B., Howarth K.M., Domingo E., Jones A.M., Broderick P.,
RA Kemp Z., Spain S.L., Guarino Almeida E., Salguero I., Sherborne A.,
RA Chubb D., Carvajal-Carmona L.G., Ma Y., Kaur K., Dobbins S., Barclay E.,
RA Gorman M., Martin L., Kovac M.B., Humphray S., Lucassen A., Holmes C.C.,
RA Bentley D., Donnelly P., Taylor J., Petridis C., Roylance R., Sawyer E.J.,
RA Kerr D.J., Clark S., Grimes J., Kearsey S.E., Thomas H.J., McVean G.,
RA Houlston R.S., Tomlinson I.;
RT "Germline mutations affecting the proofreading domains of POLE and POLD1
RT predispose to colorectal adenomas and carcinomas.";
RL Nat. Genet. 45:136-144(2013).
RN [44]
RP VARIANT CRC GLU-600.
RX PubMed=24455489; DOI=10.3389/fonc.2013.00333;
RA D'mello S.A., Flanagan J.U., Green T.N., Leung E.Y., Askarian-Amiri M.E.,
RA Joseph W.R., McCrystal M.R., Isaacs R.J., Shaw J.H., Furneaux C.E.,
RA During M.J., Finlay G.J., Baguley B.C., Kalev-Zylinska M.L.;
RT "Evidence that GRIN2A mutations in melanoma correlate with decreased
RT survival.";
RL Front. Oncol. 3:333-333(2014).
CC -!- FUNCTION: Protein kinase involved in the transduction of mitogenic
CC signals from the cell membrane to the nucleus (Probable).
CC Phosphorylates MAP2K1, and thereby activates the MAP kinase signal
CC transduction pathway (PubMed:21441910, PubMed:29433126). Phosphorylates
CC PFKFB2 (PubMed:36402789). May play a role in the postsynaptic responses
CC of hippocampal neurons (PubMed:1508179). {ECO:0000269|PubMed:1508179,
CC ECO:0000269|PubMed:21441910, ECO:0000269|PubMed:29433126,
CC ECO:0000269|PubMed:36402789, ECO:0000305}.
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:0000269|PubMed:21441910, ECO:0000269|PubMed:29433126};
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:0000269|PubMed:21441910};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
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:0000269|PubMed:29433126}.
CC -!- SUBUNIT: Monomer (PubMed:19710016). Homodimer (PubMed:19710016,
CC PubMed:36402789). Heterodimerizes with RAF1, and the heterodimer
CC possesses a highly increased kinase activity compared to the respective
CC homodimers or monomers (PubMed:19710016). Heterodimerization is
CC mitogen-regulated and enhanced by 14-3-3 proteins. MAPK1/ERK2
CC activation can induce a negative feedback that promotes the
CC dissociation of the heterodimer by phosphorylating BRAF at Thr-753.
CC Heterodimerizes (via N-terminus) with KSR1 (via N-terminus) or KSR2
CC (via N-terminus) in a MAP2K1-dependent manner (PubMed:29433126).
CC Interacts with MAP2K1 and MAP2K2 (PubMed:29433126). Found in a complex
CC with at least BRAF, HRAS, MAP2K1, MAPK3 and RGS14. Interacts with RIT1.
CC Interacts (via N-terminus) with RGS14 (via RBD domains); the
CC interaction mediates the formation of a ternary complex with RAF1, a
CC ternary complex inhibited by GNAI1 (By similarity). Interacts with DGKH
CC (PubMed:19710016). Interacts with PRMT5 (PubMed:21917714). Interacts
CC with KSR2 (PubMed:21441910). Interacts with AKAP13, MAP2K1 and KSR1.
CC Identified in a complex with AKAP13, MAP2K1 and KSR1 (PubMed:21102438).
CC Interacts with FNIP1 and FNIP2 (PubMed:27353360). {ECO:0000250,
CC ECO:0000269|PubMed:18287029, ECO:0000269|PubMed:19710016,
CC ECO:0000269|PubMed:21102438, ECO:0000269|PubMed:21441910,
CC ECO:0000269|PubMed:21917714, ECO:0000269|PubMed:27353360,
CC ECO:0000269|PubMed:29433126, ECO:0000269|PubMed:36402789}.
CC -!- INTERACTION:
CC P15056; P15056: BRAF; NbExp=13; IntAct=EBI-365980, EBI-365980;
CC P15056; P01112: HRAS; NbExp=7; IntAct=EBI-365980, EBI-350145;
CC P15056; P08238: HSP90AB1; NbExp=4; IntAct=EBI-365980, EBI-352572;
CC P15056; P46940: IQGAP1; NbExp=4; IntAct=EBI-365980, EBI-297509;
CC P15056; Q02750: MAP2K1; NbExp=62; IntAct=EBI-365980, EBI-492564;
CC P15056; P36507: MAP2K2; NbExp=11; IntAct=EBI-365980, EBI-1056930;
CC P15056; Q13233: MAP3K1; NbExp=2; IntAct=EBI-365980, EBI-49776;
CC P15056; P01111: NRAS; NbExp=6; IntAct=EBI-365980, EBI-721993;
CC P15056; Q02156: PRKCE; NbExp=3; IntAct=EBI-365980, EBI-706254;
CC P15056; P04049: RAF1; NbExp=71; IntAct=EBI-365980, EBI-365996;
CC P15056; Q15349: RPS6KA2; NbExp=2; IntAct=EBI-365980, EBI-1384149;
CC P15056; P31947: SFN; NbExp=5; IntAct=EBI-365980, EBI-476295;
CC P15056; Q13114: TRAF3; NbExp=2; IntAct=EBI-365980, EBI-357631;
CC P15056; P31946: YWHAB; NbExp=8; IntAct=EBI-365980, EBI-359815;
CC P15056; P62258: YWHAE; NbExp=9; IntAct=EBI-365980, EBI-356498;
CC P15056; P63104: YWHAZ; NbExp=10; IntAct=EBI-365980, EBI-347088;
CC P15056; Q61097: Ksr1; Xeno; NbExp=3; IntAct=EBI-365980, EBI-1536336;
CC P15056; P29678: MAP2K1; Xeno; NbExp=2; IntAct=EBI-365980, EBI-1631983;
CC P15056; Q99N57: Raf1; Xeno; NbExp=3; IntAct=EBI-365980, EBI-397757;
CC P15056; Q8CGE9: Rgs12; Xeno; NbExp=2; IntAct=EBI-365980, EBI-7340552;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
CC {ECO:0000269|PubMed:19710016}. Cell membrane
CC {ECO:0000269|PubMed:19710016}. Note=Colocalizes with RGS14 and RAF1 in
CC both the cytoplasm and membranes. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Brain and testis.
CC -!- PTM: Phosphorylation at Ser-365 by SGK1 inhibits its activity.
CC {ECO:0000269|PubMed:11410590, ECO:0000269|PubMed:1508179,
CC ECO:0000269|PubMed:19710016, ECO:0000269|Ref.8}.
CC -!- PTM: Methylation at Arg-671 decreases stability and kinase activity.
CC {ECO:0000269|PubMed:21917714}.
CC -!- PTM: Ubiquitinated by RNF149; which leads to proteasomal degradation.
CC Polyubiquitinated at Lys-578 in response to EGF.
CC {ECO:0000269|PubMed:22628551, ECO:0000269|PubMed:23907581}.
CC -!- DISEASE: Note=Defects in BRAF are found in a wide range of cancers.
CC {ECO:0000269|PubMed:18974108}.
CC -!- DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease
CC characterized by malignant lesions arising from the inner wall of the
CC large intestine (the colon) and the rectum. Genetic alterations are
CC often associated with progression from premalignant lesion (adenoma) to
CC invasive adenocarcinoma. Risk factors for cancer of the colon and
CC rectum include colon polyps, long-standing ulcerative colitis, and
CC genetic family history. {ECO:0000269|PubMed:12198537,
CC ECO:0000269|PubMed:21917714, ECO:0000269|PubMed:23263490,
CC ECO:0000269|PubMed:24455489}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Lung cancer (LNCR) [MIM:211980]: A common malignancy affecting
CC tissues of the lung. The most common form of lung cancer is non-small
CC cell lung cancer (NSCLC) that can be divided into 3 major histologic
CC subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung
CC cancer. NSCLC is often diagnosed at an advanced stage and has a poor
CC prognosis. {ECO:0000269|PubMed:12460919}. Note=The gene represented in
CC this entry is involved in disease pathogenesis.
CC -!- DISEASE: Familial non-Hodgkin lymphoma (NHL) [MIM:605027]: Cancer that
CC starts in cells of the lymph system, which is part of the body's immune
CC system. NHLs can occur at any age and are often marked by enlarged
CC lymph nodes, fever and weight loss. {ECO:0000269|PubMed:14612909}.
CC Note=The gene represented in this entry is involved in disease
CC pathogenesis.
CC -!- DISEASE: Cardiofaciocutaneous syndrome 1 (CFC1) [MIM:115150]: A
CC multiple congenital anomaly disorder characterized by a distinctive
CC facial appearance, heart defects and intellectual disability. Heart
CC defects include pulmonic stenosis, atrial septal defects and
CC hypertrophic cardiomyopathy. Some affected individuals present with
CC ectodermal abnormalities such as sparse, friable hair, hyperkeratotic
CC skin lesions and a generalized ichthyosis-like condition. Typical
CC facial features are similar to Noonan syndrome. They include high
CC forehead with bitemporal constriction, hypoplastic supraorbital ridges,
CC downslanting palpebral fissures, a depressed nasal bridge, and
CC posteriorly angulated ears with prominent helices.
CC {ECO:0000269|PubMed:16439621, ECO:0000269|PubMed:16474404,
CC ECO:0000269|PubMed:18042262, ECO:0000269|PubMed:19206169}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Noonan syndrome 7 (NS7) [MIM:613706]: A form of Noonan
CC syndrome, a disease characterized by short stature, facial dysmorphic
CC features such as hypertelorism, a downward eyeslant and low-set
CC posteriorly rotated ears, and a high incidence of congenital heart
CC defects and hypertrophic cardiomyopathy. Other features can include a
CC short neck with webbing or redundancy of skin, deafness, motor delay,
CC variable intellectual deficits, multiple skeletal defects,
CC cryptorchidism, and bleeding diathesis. Individuals with Noonan
CC syndrome are at risk of juvenile myelomonocytic leukemia, a
CC myeloproliferative disorder characterized by excessive production of
CC myelomonocytic cells. {ECO:0000269|PubMed:19206169}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: LEOPARD syndrome 3 (LPRD3) [MIM:613707]: A disorder
CC characterized by lentigines, electrocardiographic conduction
CC abnormalities, ocular hypertelorism, pulmonic stenosis, abnormalities
CC of genitalia, retardation of growth, and sensorineural deafness.
CC {ECO:0000269|PubMed:19206169}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=A chromosomal aberration involving BRAF is found in
CC pilocytic astrocytomas. A tandem duplication of 2 Mb at 7q34 leads to
CC the expression of a KIAA1549-BRAF fusion protein with a constitutive
CC kinase activity and inducing cell transformation.
CC {ECO:0000269|PubMed:18974108}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. RAF subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD43193.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAQ43111.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAQ43112.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAQ43113.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAQ43114.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAQ43115.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAQ43116.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/828/BRAF";
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DR EMBL; M95712; AAA35609.2; -; mRNA.
DR EMBL; AC006344; AAD43193.1; ALT_SEQ; Genomic_DNA.
DR EMBL; EU600171; ACD11489.1; -; Genomic_DNA.
DR EMBL; AC006347; AAD15551.1; -; Genomic_DNA.
DR EMBL; CH236950; EAL24023.1; -; Genomic_DNA.
DR EMBL; BC101757; AAI01758.1; -; mRNA.
DR EMBL; BC112079; AAI12080.1; -; mRNA.
DR EMBL; X65187; CAA46301.1; -; Genomic_DNA.
DR EMBL; M21001; AAA96495.1; -; mRNA.
DR EMBL; AM989472; CAQ43111.1; ALT_INIT; mRNA.
DR EMBL; AM989473; CAQ43112.1; ALT_INIT; mRNA.
DR EMBL; AM989474; CAQ43113.1; ALT_INIT; mRNA.
DR EMBL; AM989475; CAQ43114.1; ALT_INIT; mRNA.
DR EMBL; AM989476; CAQ43115.1; ALT_INIT; mRNA.
DR EMBL; AM989477; CAQ43116.1; ALT_INIT; mRNA.
DR CCDS; CCDS5863.1; -.
DR PIR; A57977; TVHUBF.
DR RefSeq; NP_004324.2; NM_004333.4.
DR PDB; 1UWH; X-ray; 2.95 A; A/B=448-723.
DR PDB; 1UWJ; X-ray; 3.50 A; A/B=448-723.
DR PDB; 2FB8; X-ray; 2.90 A; A/B=445-723.
DR PDB; 2L05; NMR; -; A=149-232.
DR PDB; 3C4C; X-ray; 2.57 A; A/B=444-721.
DR PDB; 3D4Q; X-ray; 2.80 A; A/B=433-726.
DR PDB; 3IDP; X-ray; 2.70 A; A/B=434-727.
DR PDB; 3II5; X-ray; 2.79 A; A/B=432-726.
DR PDB; 3NY5; X-ray; 1.99 A; A/B/C/D=153-237.
DR PDB; 3OG7; X-ray; 2.45 A; A/B=448-720.
DR PDB; 3PPJ; X-ray; 3.70 A; A/B=432-726.
DR PDB; 3PPK; X-ray; 3.00 A; A/B=432-726.
DR PDB; 3PRF; X-ray; 2.90 A; A/B=432-726.
DR PDB; 3PRI; X-ray; 3.50 A; A/B=432-726.
DR PDB; 3PSB; X-ray; 3.40 A; A/B=433-726.
DR PDB; 3PSD; X-ray; 3.60 A; A/B=433-726.
DR PDB; 3Q4C; X-ray; 3.20 A; A/B=432-726.
DR PDB; 3Q96; X-ray; 3.10 A; A/B=446-727.
DR PDB; 3SKC; X-ray; 3.20 A; A/B=432-726.
DR PDB; 3TV4; X-ray; 3.40 A; A/B=432-726.
DR PDB; 3TV6; X-ray; 3.30 A; A/B=432-726.
DR PDB; 4CQE; X-ray; 2.30 A; A/B=448-723.
DR PDB; 4DBN; X-ray; 3.15 A; A/B=445-726.
DR PDB; 4E26; X-ray; 2.55 A; A/B=432-726.
DR PDB; 4E4X; X-ray; 3.60 A; A/B=432-726.
DR PDB; 4EHE; X-ray; 3.30 A; A/B=432-726.
DR PDB; 4EHG; X-ray; 3.50 A; A/B=432-726.
DR PDB; 4FC0; X-ray; 2.95 A; A/B=445-726.
DR PDB; 4FK3; X-ray; 2.65 A; A/B=444-723.
DR PDB; 4G9C; X-ray; 3.50 A; A/B=432-726.
DR PDB; 4G9R; X-ray; 3.20 A; A/B=432-726.
DR PDB; 4H58; X-ray; 3.10 A; A/B/C=448-722.
DR PDB; 4JVG; X-ray; 3.09 A; A/B/C/D=444-723.
DR PDB; 4KSP; X-ray; 2.93 A; A/B=445-726.
DR PDB; 4KSQ; X-ray; 3.30 A; A/B=445-726.
DR PDB; 4MBJ; X-ray; 3.60 A; A/B=432-723.
DR PDB; 4MNE; X-ray; 2.85 A; B/C/F/G=432-726.
DR PDB; 4MNF; X-ray; 2.80 A; A/B=432-736.
DR PDB; 4PP7; X-ray; 3.40 A; A/B=432-726.
DR PDB; 4R5Y; X-ray; 3.50 A; A/B=444-723.
DR PDB; 4RZV; X-ray; 2.99 A; A/B=443-723.
DR PDB; 4RZW; X-ray; 3.49 A; A/B=443-723.
DR PDB; 4WO5; X-ray; 2.83 A; A/B=444-723.
DR PDB; 4XV1; X-ray; 2.47 A; A/B=444-705.
DR PDB; 4XV2; X-ray; 2.50 A; A/B=444-705.
DR PDB; 4XV3; X-ray; 2.80 A; A/B=444-705.
DR PDB; 4XV9; X-ray; 2.00 A; A=442-705.
DR PDB; 4YHT; X-ray; 3.05 A; A/B=449-720.
DR PDB; 5C9C; X-ray; 2.70 A; A/B=432-726.
DR PDB; 5CSW; X-ray; 2.66 A; A/B=442-721.
DR PDB; 5CSX; X-ray; 2.51 A; A=442-721.
DR PDB; 5CT7; X-ray; 3.17 A; A/B=445-723.
DR PDB; 5FD2; X-ray; 2.89 A; A/B=433-726.
DR PDB; 5HI2; X-ray; 2.51 A; A=444-737.
DR PDB; 5HID; X-ray; 2.50 A; A/B=444-737.
DR PDB; 5HIE; X-ray; 3.00 A; A/B/C/D=432-726.
DR PDB; 5ITA; X-ray; 1.95 A; A/B=448-723.
DR PDB; 5J17; NMR; -; A=151-232.
DR PDB; 5J18; NMR; -; A=151-232.
DR PDB; 5J2R; NMR; -; A=151-232.
DR PDB; 5JRQ; X-ray; 2.29 A; A/B=448-723.
DR PDB; 5JSM; X-ray; 2.19 A; A/B/C/D=448-723.
DR PDB; 5JT2; X-ray; 2.70 A; A/B/C/D=448-723.
DR PDB; 5VAL; X-ray; 2.26 A; A/B=445-723.
DR PDB; 5VAM; X-ray; 2.10 A; A/B=445-723.
DR PDB; 5VR3; X-ray; 2.10 A; A=36-114.
DR PDB; 5VYK; X-ray; 1.75 A; A/C=36-110.
DR PDB; 6B8U; X-ray; 2.68 A; A/B=445-723.
DR PDB; 6CAD; X-ray; 2.55 A; A/B=444-723.
DR PDB; 6N0P; X-ray; 2.37 A; A/B=449-721.
DR PDB; 6N0Q; X-ray; 2.04 A; A/B=445-723.
DR PDB; 6NSQ; X-ray; 3.05 A; A/B=444-723.
DR PDB; 6NYB; EM; 4.10 A; A=1-766.
DR PDB; 6P3D; X-ray; 2.11 A; A=448-721.
DR PDB; 6P7G; X-ray; 2.65 A; A/B/C/D=448-723.
DR PDB; 6PP9; X-ray; 2.59 A; A=445-723.
DR PDB; 6Q0J; EM; 4.90 A; A/B=1-766.
DR PDB; 6Q0K; EM; 6.80 A; A/B=1-766.
DR PDB; 6Q0T; EM; 5.70 A; A/B=1-766.
DR PDB; 6U2G; X-ray; 2.89 A; B=432-726.
DR PDB; 6U2H; X-ray; 2.50 A; C/D=447-735.
DR PDB; 6UAN; EM; 3.90 A; B/C=1-766.
DR PDB; 6UUO; X-ray; 3.29 A; A/B=444-723.
DR PDB; 6V2U; X-ray; 3.78 A; A/B=445-723.
DR PDB; 6V2W; X-ray; 3.12 A; A=445-723.
DR PDB; 6V34; X-ray; 3.15 A; A/B=448-721.
DR PDB; 6XAG; X-ray; 3.30 A; C/D=447-735.
DR PDB; 6XFP; X-ray; 2.00 A; A=442-721.
DR PDB; 6XLO; X-ray; 2.49 A; A/B=442-721.
DR PDB; 7K0V; X-ray; 1.93 A; A/B/C/D=444-723.
DR PDB; 7M0T; X-ray; 3.19 A; A=445-723.
DR PDB; 7M0U; X-ray; 3.09 A; A=445-723.
DR PDB; 7M0V; X-ray; 3.16 A; A=445-723.
DR PDB; 7M0W; X-ray; 3.09 A; A=445-723.
DR PDB; 7M0X; X-ray; 2.47 A; A=445-723.
DR PDB; 7M0Y; X-ray; 3.45 A; A=445-723.
DR PDB; 7M0Z; X-ray; 3.12 A; A=445-723.
DR PDB; 7MFD; EM; 3.66 A; A=1-766.
DR PDB; 7MFE; EM; 4.07 A; A=1-766.
DR PDB; 7MFF; EM; 3.89 A; A/B=1-766.
DR PDB; 7P3V; X-ray; 2.37 A; A/B=448-719.
DR PDB; 7SHV; X-ray; 2.88 A; A/B=432-726.
DR PDB; 7ZR0; EM; 3.40 A; K=1-766.
DR PDB; 7ZR5; EM; 3.90 A; K=1-766.
DR PDB; 7ZR6; EM; 4.20 A; K=1-766.
DR PDB; 8C7X; X-ray; 1.65 A; A/B=444-721.
DR PDB; 8C7Y; X-ray; 1.65 A; A/B=444-721.
DR PDB; 8DGS; EM; 4.30 A; A=1-766.
DR PDB; 8DGT; EM; 3.90 A; A=1-766.
DR PDB; 8F7O; X-ray; 3.54 A; A/B=441-723.
DR PDB; 8F7P; X-ray; 2.74 A; A/B=441-723.
DR PDBsum; 1UWH; -.
DR PDBsum; 1UWJ; -.
DR PDBsum; 2FB8; -.
DR PDBsum; 2L05; -.
DR PDBsum; 3C4C; -.
DR PDBsum; 3D4Q; -.
DR PDBsum; 3IDP; -.
DR PDBsum; 3II5; -.
DR PDBsum; 3NY5; -.
DR PDBsum; 3OG7; -.
DR PDBsum; 3PPJ; -.
DR PDBsum; 3PPK; -.
DR PDBsum; 3PRF; -.
DR PDBsum; 3PRI; -.
DR PDBsum; 3PSB; -.
DR PDBsum; 3PSD; -.
DR PDBsum; 3Q4C; -.
DR PDBsum; 3Q96; -.
DR PDBsum; 3SKC; -.
DR PDBsum; 3TV4; -.
DR PDBsum; 3TV6; -.
DR PDBsum; 4CQE; -.
DR PDBsum; 4DBN; -.
DR PDBsum; 4E26; -.
DR PDBsum; 4E4X; -.
DR PDBsum; 4EHE; -.
DR PDBsum; 4EHG; -.
DR PDBsum; 4FC0; -.
DR PDBsum; 4FK3; -.
DR PDBsum; 4G9C; -.
DR PDBsum; 4G9R; -.
DR PDBsum; 4H58; -.
DR PDBsum; 4JVG; -.
DR PDBsum; 4KSP; -.
DR PDBsum; 4KSQ; -.
DR PDBsum; 4MBJ; -.
DR PDBsum; 4MNE; -.
DR PDBsum; 4MNF; -.
DR PDBsum; 4PP7; -.
DR PDBsum; 4R5Y; -.
DR PDBsum; 4RZV; -.
DR PDBsum; 4RZW; -.
DR PDBsum; 4WO5; -.
DR PDBsum; 4XV1; -.
DR PDBsum; 4XV2; -.
DR PDBsum; 4XV3; -.
DR PDBsum; 4XV9; -.
DR PDBsum; 4YHT; -.
DR PDBsum; 5C9C; -.
DR PDBsum; 5CSW; -.
DR PDBsum; 5CSX; -.
DR PDBsum; 5CT7; -.
DR PDBsum; 5FD2; -.
DR PDBsum; 5HI2; -.
DR PDBsum; 5HID; -.
DR PDBsum; 5HIE; -.
DR PDBsum; 5ITA; -.
DR PDBsum; 5J17; -.
DR PDBsum; 5J18; -.
DR PDBsum; 5J2R; -.
DR PDBsum; 5JRQ; -.
DR PDBsum; 5JSM; -.
DR PDBsum; 5JT2; -.
DR PDBsum; 5VAL; -.
DR PDBsum; 5VAM; -.
DR PDBsum; 5VR3; -.
DR PDBsum; 5VYK; -.
DR PDBsum; 6B8U; -.
DR PDBsum; 6CAD; -.
DR PDBsum; 6N0P; -.
DR PDBsum; 6N0Q; -.
DR PDBsum; 6NSQ; -.
DR PDBsum; 6NYB; -.
DR PDBsum; 6P3D; -.
DR PDBsum; 6P7G; -.
DR PDBsum; 6PP9; -.
DR PDBsum; 6Q0J; -.
DR PDBsum; 6Q0K; -.
DR PDBsum; 6Q0T; -.
DR PDBsum; 6U2G; -.
DR PDBsum; 6U2H; -.
DR PDBsum; 6UAN; -.
DR PDBsum; 6UUO; -.
DR PDBsum; 6V2U; -.
DR PDBsum; 6V2W; -.
DR PDBsum; 6V34; -.
DR PDBsum; 6XAG; -.
DR PDBsum; 6XFP; -.
DR PDBsum; 6XLO; -.
DR PDBsum; 7K0V; -.
DR PDBsum; 7M0T; -.
DR PDBsum; 7M0U; -.
DR PDBsum; 7M0V; -.
DR PDBsum; 7M0W; -.
DR PDBsum; 7M0X; -.
DR PDBsum; 7M0Y; -.
DR PDBsum; 7M0Z; -.
DR PDBsum; 7MFD; -.
DR PDBsum; 7MFE; -.
DR PDBsum; 7MFF; -.
DR PDBsum; 7P3V; -.
DR PDBsum; 7SHV; -.
DR PDBsum; 7ZR0; -.
DR PDBsum; 7ZR5; -.
DR PDBsum; 7ZR6; -.
DR PDBsum; 8C7X; -.
DR PDBsum; 8C7Y; -.
DR PDBsum; 8DGS; -.
DR PDBsum; 8DGT; -.
DR PDBsum; 8F7O; -.
DR PDBsum; 8F7P; -.
DR AlphaFoldDB; P15056; -.
DR BMRB; P15056; -.
DR EMDB; EMD-0541; -.
DR EMDB; EMD-20550; -.
DR EMDB; EMD-20551; -.
DR EMDB; EMD-20552; -.
DR EMDB; EMD-20708; -.
DR EMDB; EMD-23813; -.
DR EMDB; EMD-23814; -.
DR EMDB; EMD-23815; -.
DR EMDB; EMD-27428; -.
DR EMDB; EMD-27429; -.
DR SMR; P15056; -.
DR BioGRID; 107141; 183.
DR CORUM; P15056; -.
DR DIP; DIP-1045N; -.
DR IntAct; P15056; 91.
DR MINT; P15056; -.
DR STRING; 9606.ENSP00000419060; -.
DR BindingDB; P15056; -.
DR ChEMBL; CHEMBL5145; -.
DR DrugBank; DB08553; (1E)-5-(1-piperidin-4-yl-3-pyridin-4-yl-1H-pyrazol-4-yl)-2,3-dihydro-1H-inden-1-one oxime.
DR DrugBank; DB08912; Dabrafenib.
DR DrugBank; DB11718; Encorafenib.
DR DrugBank; DB12010; Fostamatinib.
DR DrugBank; DB07000; N-{2,4-difluoro-3-[(5-pyridin-3-yl-1H-pyrrolo[2,3-b]pyridin-3-yl)carbonyl]phenyl}ethanesulfonamide.
DR DrugBank; DB06999; PLX-4720.
DR DrugBank; DB05984; RAF-265.
DR DrugBank; DB08896; Regorafenib.
DR DrugBank; DB14840; Ripretinib.
DR DrugBank; DB00398; Sorafenib.
DR DrugBank; DB08881; Vemurafenib.
DR DrugBank; DB05190; XL281.
DR DrugCentral; P15056; -.
DR GuidetoPHARMACOLOGY; 1943; -.
DR TCDB; 8.A.23.1.48; the basigin (basigin) family.
DR iPTMnet; P15056; -.
DR PhosphoSitePlus; P15056; -.
DR BioMuta; BRAF; -.
DR DMDM; 50403720; -.
DR CPTAC; CPTAC-3112; -.
DR CPTAC; CPTAC-3113; -.
DR CPTAC; CPTAC-5771; -.
DR CPTAC; CPTAC-5817; -.
DR CPTAC; CPTAC-5818; -.
DR CPTAC; CPTAC-5819; -.
DR CPTAC; CPTAC-5820; -.
DR CPTAC; CPTAC-5821; -.
DR CPTAC; CPTAC-5822; -.
DR CPTAC; non-CPTAC-5352; -.
DR CPTAC; non-CPTAC-5353; -.
DR CPTAC; non-CPTAC-5354; -.
DR CPTAC; non-CPTAC-5355; -.
DR CPTAC; non-CPTAC-5356; -.
DR CPTAC; non-CPTAC-5357; -.
DR CPTAC; non-CPTAC-5727; -.
DR CPTAC; non-CPTAC-5728; -.
DR CPTAC; non-CPTAC-5729; -.
DR EPD; P15056; -.
DR jPOST; P15056; -.
DR MassIVE; P15056; -.
DR MaxQB; P15056; -.
DR PaxDb; 9606-ENSP00000288602; -.
DR PeptideAtlas; P15056; -.
DR ProteomicsDB; 53102; -.
DR Pumba; P15056; -.
DR Antibodypedia; 751; 2663 antibodies from 51 providers.
DR CPTC; P15056; 7 antibodies.
DR DNASU; 673; -.
DR Ensembl; ENST00000646891.2; ENSP00000493543.1; ENSG00000157764.14.
DR GeneID; 673; -.
DR KEGG; hsa:673; -.
DR MANE-Select; ENST00000646891.2; ENSP00000493543.1; NM_004333.6; NP_004324.2.
DR UCSC; uc003vwc.5; human.
DR AGR; HGNC:1097; -.
DR CTD; 673; -.
DR DisGeNET; 673; -.
DR GeneCards; BRAF; -.
DR GeneReviews; BRAF; -.
DR HGNC; HGNC:1097; BRAF.
DR HPA; ENSG00000157764; Low tissue specificity.
DR MalaCards; BRAF; -.
DR MIM; 114500; phenotype.
DR MIM; 115150; phenotype.
DR MIM; 164757; gene.
DR MIM; 211980; phenotype.
DR MIM; 605027; phenotype.
DR MIM; 613706; phenotype.
DR MIM; 613707; phenotype.
DR neXtProt; NX_P15056; -.
DR OpenTargets; ENSG00000157764; -.
DR Orphanet; 1340; Cardiofaciocutaneous syndrome.
DR Orphanet; 58017; Classic hairy cell leukemia.
DR Orphanet; 54595; Craniopharyngioma.
DR Orphanet; 96253; Cushing disease.
DR Orphanet; 146; Differentiated thyroid carcinoma.
DR Orphanet; 389; Langerhans cell histiocytosis.
DR Orphanet; 626; Large congenital melanocytic nevus.
DR Orphanet; 411533; NON RARE IN EUROPE: Melanoma.
DR Orphanet; 500; Noonan syndrome with multiple lentigines.
DR Orphanet; 251615; Pilomyxoid astrocytoma.
DR Orphanet; 840; Syringocystadenoma papilliferum.
DR PharmGKB; PA25408; -.
DR VEuPathDB; HostDB:ENSG00000157764; -.
DR eggNOG; KOG0193; Eukaryota.
DR GeneTree; ENSGT00940000156154; -.
DR HOGENOM; CLU_023684_1_0_1; -.
DR InParanoid; P15056; -.
DR OrthoDB; 4560496at2759; -.
DR PhylomeDB; P15056; -.
DR TreeFam; TF317006; -.
DR BRENDA; 2.7.10.2; 2681.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; P15056; -.
DR Reactome; R-HSA-1295596; Spry regulation of FGF signaling.
DR Reactome; R-HSA-170968; Frs2-mediated activation.
DR Reactome; R-HSA-170984; ARMS-mediated activation.
DR Reactome; R-HSA-187706; Signalling to p38 via RIT and RIN.
DR Reactome; R-HSA-5673000; RAF activation.
DR Reactome; R-HSA-5674135; MAP2K and MAPK activation.
DR Reactome; R-HSA-5674499; Negative feedback regulation of MAPK pathway.
DR Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
DR Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions.
DR Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
DR Reactome; R-HSA-9649948; Signaling downstream of RAS mutants.
DR Reactome; R-HSA-9656223; Signaling by RAF1 mutants.
DR Reactome; R-HSA-9726840; SHOC2 M1731 mutant abolishes MRAS complex function.
DR Reactome; R-HSA-9726842; Gain-of-function MRAS complexes activate RAF signaling.
DR SignaLink; P15056; -.
DR SIGNOR; P15056; -.
DR BioGRID-ORCS; 673; 88 hits in 1213 CRISPR screens.
DR ChiTaRS; BRAF; human.
DR EvolutionaryTrace; P15056; -.
DR GeneWiki; BRAF_(gene); -.
DR GenomeRNAi; 673; -.
DR Pharos; P15056; Tclin.
DR PRO; PR:P15056; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P15056; Protein.
DR Bgee; ENSG00000157764; Expressed in buccal mucosa cell and 183 other cell types or tissues.
DR ExpressionAtlas; P15056; baseline and differential.
DR Genevisible; P15056; HS.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004708; F:MAP kinase kinase activity; IMP:UniProtKB.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IBA:GO_Central.
DR GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IEA:Ensembl.
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; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
DR GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
DR GO; GO:0043369; P:CD4-positive or CD8-positive, alpha-beta T cell lineage commitment; IEA:Ensembl.
DR GO; GO:0043367; P:CD4-positive, alpha-beta T cell differentiation; IEA:Ensembl.
DR GO; GO:0071277; P:cellular response to calcium ion; IDA:BHF-UCL.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0072577; P:endothelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0090150; P:establishment of protein localization to membrane; IDA:CACAO.
DR GO; GO:0060324; P:face development; IEA:Ensembl.
DR GO; GO:0060323; P:head morphogenesis; IEA:Ensembl.
DR GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
DR GO; GO:0000165; P:MAPK cascade; IDA:UniProtKB.
DR GO; GO:0002318; P:myeloid progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:0010764; P:negative regulation of fibroblast migration; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:2000301; P:negative regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0048680; P:positive regulation of axon regeneration; IEA:Ensembl.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0010828; P:positive regulation of glucose transmembrane transport; IDA:CACAO.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:UniProtKB.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IDA:BHF-UCL.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0045580; P:regulation of T cell differentiation; IEA:Ensembl.
DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0043149; P:stress fiber assembly; IEA:Ensembl.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR GO; GO:0030878; P:thyroid gland development; IEA:Ensembl.
DR GO; GO:0070413; P:trehalose metabolism in response to stress; IMP:SGD.
DR GO; GO:0008542; P:visual learning; IEA:Ensembl.
DR CDD; cd20871; C1_B-Raf; 1.
DR CDD; cd17134; RBD_BRAF; 1.
DR CDD; cd14062; STKc_Raf; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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 PANTHER; PTHR23257:SF731; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
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; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 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 3D-structure; Acetylation; Allosteric enzyme; ATP-binding; Cardiomyopathy;
KW Cell membrane; Chromosomal rearrangement; Cytoplasm; Deafness;
KW Direct protein sequencing; Disease variant; Ectodermal dysplasia;
KW Intellectual disability; Isopeptide bond; Kinase; Membrane; Metal-binding;
KW Methylation; Nucleotide-binding; Nucleus; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.8"
FT CHAIN 2..766
FT /note="Serine/threonine-protein kinase B-raf"
FT /id="PRO_0000085665"
FT DOMAIN 155..227
FT /note="RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00262"
FT DOMAIN 457..717
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ZN_FING 234..280
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 576
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 235
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="2"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 463..471
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 483
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 380..381
FT /note="Breakpoint for translocation to form KIAA1549-BRAF
FT fusion protein"
FT SITE 438..439
FT /note="Breakpoint for translocation to form KIAA1549-BRAF
FT fusion protein"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.8"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28028"
FT MOD_RES 365
FT /note="Phosphoserine; by SGK1"
FT /evidence="ECO:0000269|PubMed:11410590, ECO:0000269|Ref.8,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 373
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:1508179"
FT MOD_RES 396
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|Ref.8"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.8"
FT MOD_RES 401
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 671
FT /note="Omega-N-methylarginine; by PRMT5"
FT /evidence="ECO:0000269|PubMed:21917714"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 750
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28028"
FT MOD_RES 753
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000269|PubMed:19710016"
FT CROSSLNK 578
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23907581"
FT VARIANT 241
FT /note="T -> M (in NS7; dbSNP:rs387906660)"
FT /evidence="ECO:0000269|PubMed:19206169"
FT /id="VAR_058620"
FT VARIANT 241
FT /note="T -> P (in CFC1 and LPRD3; dbSNP:rs387906661)"
FT /evidence="ECO:0000269|PubMed:18042262,
FT ECO:0000269|PubMed:19206169"
FT /id="VAR_058621"
FT VARIANT 241
FT /note="T -> R (in NS7; dbSNP:rs387906660)"
FT /evidence="ECO:0000269|PubMed:19206169"
FT /id="VAR_058622"
FT VARIANT 244
FT /note="T -> P (in CFC1; dbSNP:rs397507465)"
FT /evidence="ECO:0000269|PubMed:18042262"
FT /id="VAR_065171"
FT VARIANT 245
FT /note="L -> F (in CFC1; dbSNP:rs397507466)"
FT /evidence="ECO:0000269|PubMed:19206169"
FT /id="VAR_058623"
FT VARIANT 246
FT /note="A -> P (in CFC1; dbSNP:rs180177034)"
FT /evidence="ECO:0000269|PubMed:16474404,
FT ECO:0000269|PubMed:18042262, ECO:0000269|PubMed:19206169"
FT /id="VAR_026113"
FT VARIANT 257
FT /note="Q -> R (in CFC1; dbSNP:rs180177035)"
FT /evidence="ECO:0000269|PubMed:16439621,
FT ECO:0000269|PubMed:16474404, ECO:0000269|PubMed:18042262,
FT ECO:0000269|PubMed:19206169"
FT /id="VAR_026114"
FT VARIANT 262
FT /note="Q -> K (in CFC1; dbSNP:rs397507470)"
FT /evidence="ECO:0000269|PubMed:18042262"
FT /id="VAR_065172"
FT VARIANT 275
FT /note="E -> K (in CFC1)"
FT /evidence="ECO:0000269|PubMed:19206169"
FT /id="VAR_058624"
FT VARIANT 301
FT /note="P -> S (in dbSNP:rs34776339)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040391"
FT VARIANT 462
FT /note="R -> I (in CRC; dbSNP:rs180177032)"
FT /evidence="ECO:0000269|PubMed:12198537"
FT /id="VAR_018613"
FT VARIANT 463
FT /note="I -> S (in CRC; dbSNP:rs180177033)"
FT /evidence="ECO:0000269|PubMed:12198537"
FT /id="VAR_018614"
FT VARIANT 464
FT /note="G -> E (in CRC; dbSNP:rs121913348)"
FT /evidence="ECO:0000269|PubMed:12068308,
FT ECO:0000269|PubMed:12198537"
FT /id="VAR_018615"
FT VARIANT 464
FT /note="G -> V (in a colorectal cancer cell line; elevated
FT kinase activity; efficiently induces cell transformation;
FT dbSNP:rs121913348)"
FT /evidence="ECO:0000269|PubMed:12068308"
FT /id="VAR_018616"
FT VARIANT 466
FT /note="G -> A (in melanoma; dbSNP:rs121913351)"
FT /evidence="ECO:0000269|PubMed:12068308"
FT /id="VAR_018617"
FT VARIANT 466
FT /note="G -> E (in melanoma; dbSNP:rs121913351)"
FT /evidence="ECO:0000269|PubMed:12068308"
FT /id="VAR_018618"
FT VARIANT 466
FT /note="G -> V (in LNCR; dbSNP:rs121913351)"
FT /evidence="ECO:0000269|PubMed:12068308,
FT ECO:0000269|PubMed:12460919"
FT /id="VAR_018512"
FT VARIANT 467
FT /note="S -> A (in CFC1; dbSNP:rs869025606)"
FT /evidence="ECO:0000269|PubMed:16439621"
FT /id="VAR_035096"
FT VARIANT 468
FT /note="F -> S (in CFC1; dbSNP:rs397507473)"
FT /evidence="ECO:0000269|PubMed:16439621,
FT ECO:0000269|PubMed:18042262"
FT /id="VAR_035097"
FT VARIANT 469
FT /note="G -> A (in NHL; also in a lung adenocarcinoma
FT sample; somatic mutation; elevated kinase activity;
FT efficiently induces cell transformation;
FT dbSNP:rs121913355)"
FT /evidence="ECO:0000269|PubMed:12068308,
FT ECO:0000269|PubMed:14612909, ECO:0000269|PubMed:17344846"
FT /id="VAR_018620"
FT VARIANT 469
FT /note="G -> E (in CFC1 and colon cancer;
FT dbSNP:rs121913355)"
FT /evidence="ECO:0000269|PubMed:12068308,
FT ECO:0000269|PubMed:16439621, ECO:0000269|PubMed:16474404,
FT ECO:0000269|PubMed:18042262, ECO:0000269|PubMed:19206169"
FT /id="VAR_018621"
FT VARIANT 469
FT /note="G -> R (in NHL; dbSNP:rs121913357)"
FT /evidence="ECO:0000269|PubMed:14612909"
FT /id="VAR_018622"
FT VARIANT 469
FT /note="G -> V (in a colorectal adenocarcinoma sample;
FT somatic mutation; dbSNP:rs121913355)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040392"
FT VARIANT 485
FT /note="L -> F (in CFC1; dbSNP:rs180177036)"
FT /evidence="ECO:0000269|PubMed:16439621,
FT ECO:0000269|PubMed:16474404, ECO:0000269|PubMed:19206169"
FT /id="VAR_026115"
FT VARIANT 499
FT /note="K -> E (in CFC1; dbSNP:rs180177037)"
FT /evidence="ECO:0000269|PubMed:16439621,
FT ECO:0000269|PubMed:16474404, ECO:0000269|PubMed:18042262"
FT /id="VAR_026116"
FT VARIANT 499
FT /note="K -> N (in CFC1; dbSNP:rs397507476)"
FT /evidence="ECO:0000269|PubMed:18042262,
FT ECO:0000269|PubMed:19206169"
FT /id="VAR_058625"
FT VARIANT 501
FT /note="E -> G (in CFC1; dbSNP:rs180177039)"
FT /evidence="ECO:0000269|PubMed:16439621,
FT ECO:0000269|PubMed:16474404"
FT /id="VAR_026117"
FT VARIANT 501
FT /note="E -> K (in CFC1; dbSNP:rs180177038)"
FT /evidence="ECO:0000269|PubMed:16439621,
FT ECO:0000269|PubMed:16474404, ECO:0000269|PubMed:19206169"
FT /id="VAR_026118"
FT VARIANT 525
FT /note="L -> P (in CFC1; dbSNP:rs869025340)"
FT /evidence="ECO:0000269|PubMed:19206169"
FT /id="VAR_058626"
FT VARIANT 531
FT /note="W -> C (in NS7; dbSNP:rs606231228)"
FT /evidence="ECO:0000269|PubMed:19206169"
FT /id="VAR_058627"
FT VARIANT 580
FT /note="N -> D (in CFC1)"
FT /evidence="ECO:0000269|PubMed:18042262"
FT /id="VAR_065173"
FT VARIANT 581
FT /note="N -> D (in CFC1; dbSNP:rs180177040)"
FT /evidence="ECO:0000269|PubMed:16439621,
FT ECO:0000269|PubMed:16474404, ECO:0000269|PubMed:18042262"
FT /id="VAR_026119"
FT VARIANT 581
FT /note="N -> S (in a colorectal adenocarcinoma sample;
FT somatic mutation; dbSNP:rs121913370)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040393"
FT VARIANT 586
FT /note="E -> K (in ovarian cancer; dbSNP:rs121913340)"
FT /evidence="ECO:0000269|PubMed:12068308"
FT /id="VAR_018623"
FT VARIANT 594
FT /note="D -> G (in NHL; dbSNP:rs121913338)"
FT /evidence="ECO:0000269|PubMed:14612909"
FT /id="VAR_018624"
FT VARIANT 595
FT /note="F -> L (in CFC1; also found in colon cancer;
FT dbSNP:rs121913341)"
FT /evidence="ECO:0000269|PubMed:12068308,
FT ECO:0000269|PubMed:16439621, ECO:0000269|PubMed:18042262,
FT ECO:0000269|PubMed:19206169"
FT /id="VAR_018625"
FT VARIANT 596
FT /note="G -> R (in a colorectal adenocarcinoma sample;
FT somatic mutation; dbSNP:rs121913361)"
FT /evidence="ECO:0000269|PubMed:12068308,
FT ECO:0000269|PubMed:17344846"
FT /id="VAR_018626"
FT VARIANT 596
FT /note="G -> V (in CFC1; dbSNP:rs397507483)"
FT /evidence="ECO:0000269|PubMed:16439621"
FT /id="VAR_035098"
FT VARIANT 597
FT /note="L -> R (in LNCR; also found in an ovarian serous
FT carcinoma sample; somatic mutation; dbSNP:rs121913366)"
FT /evidence="ECO:0000269|PubMed:12068308,
FT ECO:0000269|PubMed:12460919, ECO:0000269|PubMed:17344846"
FT /id="VAR_018513"
FT VARIANT 597
FT /note="L -> V (in NS7; also in a lung adenocarcinoma
FT sample; somatic mutation; elevated kinase activity;
FT efficiently induces cell transformation;
FT dbSNP:rs121913369)"
FT /evidence="ECO:0000269|PubMed:12068308,
FT ECO:0000269|PubMed:17344846, ECO:0000269|PubMed:19206169"
FT /id="VAR_018627"
FT VARIANT 599
FT /note="T -> R (in CFC1; dbSNP:rs121913375)"
FT /evidence="ECO:0000269|PubMed:19206169"
FT /id="VAR_058628"
FT VARIANT 600
FT /note="V -> D (in a melanoma cell line; requires 2
FT nucleotide substitutions; dbSNP:rs121913377)"
FT /evidence="ECO:0000269|PubMed:12068308"
FT /id="VAR_018628"
FT VARIANT 600
FT /note="V -> E (in CRC; also found in sarcoma, metastatic
FT melanoma, ovarian serous carcinoma, pilocytic astrocytoma;
FT somatic mutation; most common mutation; constitutive and
FT elevated kinase activity; efficiently induces cell
FT transformation; suppression of mutation in melanoma causes
FT growth arrest and promotes apoptosis; loss of regulation by
FT PMRT5; dbSNP:rs113488022)"
FT /evidence="ECO:0000269|PubMed:12068308,
FT ECO:0000269|PubMed:12198537, ECO:0000269|PubMed:14500344,
FT ECO:0000269|PubMed:16959974, ECO:0000269|PubMed:17344846,
FT ECO:0000269|PubMed:21917714, ECO:0000269|PubMed:23263490,
FT ECO:0000269|PubMed:24455489"
FT /id="VAR_018629"
FT VARIANT 601
FT /note="K -> E (in CRC; dbSNP:rs121913364)"
FT /evidence="ECO:0000269|PubMed:12198537"
FT /id="VAR_018630"
FT VARIANT 601
FT /note="K -> Q (in CFC1; dbSNP:rs121913364)"
FT /evidence="ECO:0000269|PubMed:19206169"
FT /id="VAR_058629"
FT VARIANT 638
FT /note="D -> E (in CFC1; dbSNP:rs180177042)"
FT /evidence="ECO:0000269|PubMed:19206169"
FT /id="VAR_058630"
FT VARIANT 709
FT /note="Q -> R (in CFC1; dbSNP:rs397507486)"
FT /evidence="ECO:0000269|PubMed:19206169"
FT /id="VAR_058631"
FT MUTAGEN 53
FT /note="M->D: Reduces interaction with KSR1 and MAP2K1 and
FT thus phosphorylation of MAP2K1."
FT /evidence="ECO:0000269|PubMed:29433126"
FT MUTAGEN 88
FT /note="K->E: Reduces interaction with KSR1 and MAP2K1 and
FT thus phosphorylation of MAP2K1."
FT /evidence="ECO:0000269|PubMed:29433126"
FT MUTAGEN 483
FT /note="K->S: Reduces kinase activity with MAP2K1."
FT /evidence="ECO:0000269|PubMed:21441910"
FT MUTAGEN 509
FT /note="R->H: Loss of MAP2K1-mediated-BRAF-KSR1
FT dimerization."
FT /evidence="ECO:0000269|PubMed:29433126"
FT MUTAGEN 578
FT /note="K->R: Blocks EGF-induced ubiquitination and ERK
FT activation."
FT /evidence="ECO:0000269|PubMed:23907581"
FT MUTAGEN 666
FT /note="I->R: No effect on MAP2K1-mediated-BRAF-KSR1
FT dimerization, however loss of BRAF-mediated phosphorylation
FT of MAP2K1."
FT /evidence="ECO:0000269|PubMed:29433126"
FT MUTAGEN 671
FT /note="R->K: Increased kinase activity and stability in
FT response to EGF treatment."
FT /evidence="ECO:0000269|PubMed:21917714"
FT CONFLICT 766
FT /note="H -> D (in Ref. 11; AAA96495)"
FT /evidence="ECO:0000305"
FT HELIX 43..68
FT /evidence="ECO:0007829|PDB:5VYK"
FT HELIX 76..103
FT /evidence="ECO:0007829|PDB:5VYK"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:3NY5"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:3NY5"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:3NY5"
FT HELIX 177..186
FT /evidence="ECO:0007829|PDB:3NY5"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:3NY5"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:3NY5"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:3NY5"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:3NY5"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:3NY5"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:3NY5"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:6P3D"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:5JRQ"
FT STRAND 458..466
FT /evidence="ECO:0007829|PDB:8C7X"
FT STRAND 469..484
FT /evidence="ECO:0007829|PDB:8C7X"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:8C7X"
FT HELIX 492..505
FT /evidence="ECO:0007829|PDB:8C7X"
FT STRAND 516..520
FT /evidence="ECO:0007829|PDB:8C7X"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:8C7X"
FT STRAND 526..530
FT /evidence="ECO:0007829|PDB:8C7X"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:8C7X"
FT HELIX 537..542
FT /evidence="ECO:0007829|PDB:8C7X"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:6P3D"
FT HELIX 550..569
FT /evidence="ECO:0007829|PDB:8C7X"
FT HELIX 579..581
FT /evidence="ECO:0007829|PDB:8C7X"
FT STRAND 582..585
FT /evidence="ECO:0007829|PDB:8C7X"
FT TURN 586..588
FT /evidence="ECO:0007829|PDB:8C7X"
FT STRAND 589..592
FT /evidence="ECO:0007829|PDB:8C7X"
FT TURN 598..600
FT /evidence="ECO:0007829|PDB:6XFP"
FT TURN 602..605
FT /evidence="ECO:0007829|PDB:4RZV"
FT HELIX 609..612
FT /evidence="ECO:0007829|PDB:8C7X"
FT HELIX 614..619
FT /evidence="ECO:0007829|PDB:8C7X"
FT HELIX 622..626
FT /evidence="ECO:0007829|PDB:8C7X"
FT STRAND 629..631
FT /evidence="ECO:0007829|PDB:8C7X"
FT HELIX 635..651
FT /evidence="ECO:0007829|PDB:8C7X"
FT TURN 655..658
FT /evidence="ECO:0007829|PDB:8C7X"
FT HELIX 662..671
FT /evidence="ECO:0007829|PDB:8C7X"
FT HELIX 678..680
FT /evidence="ECO:0007829|PDB:8C7X"
FT STRAND 683..685
FT /evidence="ECO:0007829|PDB:5JRQ"
FT HELIX 687..696
FT /evidence="ECO:0007829|PDB:8C7X"
FT HELIX 701..703
FT /evidence="ECO:0007829|PDB:8C7X"
FT HELIX 707..721
FT /evidence="ECO:0007829|PDB:8C7X"
FT STRAND 723..726
FT /evidence="ECO:0007829|PDB:6U2H"
SQ SEQUENCE 766 AA; 84437 MW; 0798C2AAB487E813 CRC64;
MAALSGGGGG GAEPGQALFN GDMEPEAGAG AGAAASSAAD PAIPEEVWNI KQMIKLTQEH
IEALLDKFGG EHNPPSIYLE AYEEYTSKLD ALQQREQQLL ESLGNGTDFS VSSSASMDTV
TSSSSSSLSV LPSSLSVFQN PTDVARSNPK SPQKPIVRVF LPNKQRTVVP ARCGVTVRDS
LKKALMMRGL IPECCAVYRI QDGEKKPIGW DTDISWLTGE ELHVEVLENV PLTTHNFVRK
TFFTLAFCDF CRKLLFQGFR CQTCGYKFHQ RCSTEVPLMC VNYDQLDLLF VSKFFEHHPI
PQEEASLAET ALTSGSSPSA PASDSIGPQI LTSPSPSKSI PIPQPFRPAD EDHRNQFGQR
DRSSSAPNVH INTIEPVNID DLIRDQGFRG DGGSTTGLSA TPPASLPGSL TNVKALQKSP
GPQRERKSSS SSEDRNRMKT LGRRDSSDDW EIPDGQITVG QRIGSGSFGT VYKGKWHGDV
AVKMLNVTAP TPQQLQAFKN EVGVLRKTRH VNILLFMGYS TKPQLAIVTQ WCEGSSLYHH
LHIIETKFEM IKLIDIARQT AQGMDYLHAK SIIHRDLKSN NIFLHEDLTV KIGDFGLATV
KSRWSGSHQF EQLSGSILWM APEVIRMQDK NPYSFQSDVY AFGIVLYELM TGQLPYSNIN
NRDQIIFMVG RGYLSPDLSK VRSNCPKAMK RLMAECLKKK RDERPLFPQI LASIELLARS
LPKIHRSASE PSLNRAGFQT EDFSLYACAS PKTPIQAGGY GAFPVH
//
