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Serine/threonine-protein kinase B-raf (EC 2.7.11.1) (Proto-oncogene B-Raf) (p94) (v-Raf murine sarcoma viral oncogene homolog B1)

 BRAF_HUMAN              Reviewed;         766 AA.
P15056; A4D1T4; B6HY61; B6HY62; B6HY63; B6HY64; B6HY65; B6HY66;
Q13878; Q3MIN6; Q9UDP8; Q9Y6T3;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 4.
30-AUG-2017, entry version 214.
RecName: Full=Serine/threonine-protein kinase B-raf;
EC=2.7.11.1;
AltName: Full=Proto-oncogene B-Raf;
AltName: Full=p94;
AltName: Full=v-Raf murine sarcoma viral oncogene homolog B1;
Name=BRAF; Synonyms=BRAF1, RAFB1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND
PHOSPHORYLATION AT THR-373.
TISSUE=Testis;
PubMed=1508179; DOI=10.1128/MCB.12.9.3733;
Stephens R.M., Sithanandam G., Copeland T.D., Kaplan D.R., Rapp U.R.,
Morrison D.K.;
"95-kilodalton B-Raf serine/threonine kinase: identification of the
protein and its major autophosphorylation site.";
Mol. Cell. Biol. 12:3733-3742(1992).
[2]
SEQUENCE REVISION TO 31-33.
Albert S., Wixler L., Rapp U.R.;
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-200.
TISSUE=Placenta;
PubMed=1630826;
Eychene A., Barnier J.V., Apiou F., Dutrillaux B., Calothy G.;
"Chromosomal assignment of two human B-raf(Rmil) proto-oncogene loci:
B-raf-1 encoding the p94Braf/Rmil and B-raf-2, a processed
pseudogene.";
Oncogene 7:1657-1660(1992).
[8]
PROTEIN SEQUENCE OF 2-51; 56-95; 151-158; 189-199; 253-260; 294-354;
361-424; 444-507; 510-522; 559-570; 579-626; 663-680; 692-698;
702-719; 727-735 AND 753-766, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-365; THR-396; SER-399;
THR-401 AND SER-729, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Colon carcinoma, and Hepatoma;
Bienvenut W.V., Boldt K., von Kriegsheim A.F., Zebisch A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 117-766.
TISSUE=Testis;
PubMed=2284096;
Sithanandam G., Kolch W., Duh F.-M., Rapp U.R.;
"Complete coding sequence of a human B-raf cDNA and detection of B-raf
protein kinase with isozyme specific antibodies.";
Oncogene 5:1775-1780(1990).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 381-766, DISEASE, AND CHROMOSOMAL
REARRANGEMENT.
TISSUE=Brain;
PubMed=18974108; DOI=10.1158/0008-5472.CAN-08-2097;
Jones D.T.W., Kocialkowski S., Liu L., Pearson D.M., Backlund L.M.,
Ichimura K., Collins V.P.;
"Tandem duplication producing a novel oncogenic BRAF fusion gene
defines the majority of pilocytic astrocytomas.";
Cancer Res. 68:8673-8677(2008).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 439-766.
PubMed=3043188; DOI=10.1128/MCB.8.6.2651;
Ikawa S., Fukui M., Ueyama Y., Tamaoki N., Yamamoto T., Toyoshima K.;
"B-raf, a new member of the raf family, is activated by DNA
rearrangement.";
Mol. Cell. Biol. 8:2651-2654(1988).
[12]
PHOSPHORYLATION AT SER-365 BY SGK1.
PubMed=11410590; DOI=10.1074/jbc.M102808200;
Zhang B.H., Tang E.D., Zhu T., Greenberg M.E., Vojtek A.B., Guan K.L.;
"Serum- and glucocorticoid-inducible kinase SGK phosphorylates and
negatively regulates B-Raf.";
J. Biol. Chem. 276:31620-31626(2001).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401; SER-446; SER-447
AND SER-729, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
SUBUNIT, INTERACTION WITH DGKH, AND PHOSPHORYLATION AT THR-753 BY
MAPK1.
PubMed=19710016; DOI=10.1074/jbc.M109.043604;
Yasuda S., Kai M., Imai S., Takeishi K., Taketomi A., Toyota M.,
Kanoh H., Sakane F.;
"Diacylglycerol kinase eta augments C-Raf activity and B-Raf/C-Raf
heterodimerization.";
J. Biol. Chem. 284:29559-29570(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
INTERACTION WITH AKAP13; MAP2K1 AND KSR1.
PubMed=21102438; DOI=10.1038/ncb2130;
Smith F.D., Langeberg L.K., Cellurale C., Pawson T., Morrison D.K.,
Davis R.J., Scott J.D.;
"AKAP-Lbc enhances cyclic AMP control of the ERK1/2 cascade.";
Nat. Cell Biol. 12:1242-1249(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[20]
INTERACTION WITH KSR2, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION, AND
MUTAGENESIS OF LYS-483.
PubMed=21441910; DOI=10.1038/nature09860;
Brennan D.F., Dar A.C., Hertz N.T., Chao W.C., Burlingame A.L.,
Shokat K.M., Barford D.;
"A Raf-induced allosteric transition of KSR stimulates phosphorylation
of MEK.";
Nature 472:366-369(2011).
[21]
INTERACTION WITH PRMT5, METHYLATION AT ARG-671, CHARACTERIZATION OF
VARIANT CRC GLU-600, AND MUTAGENESIS OF ARG-671.
PubMed=21917714; DOI=10.1126/scisignal.2001936;
Andreu-Perez P., Esteve-Puig R., de Torre-Minguela C.,
Lopez-Fauqued M., Bech-Serra J.J., Tenbaum S., Garcia-Trevijano E.R.,
Canals F., Merlino G., Avila M.A., Recio J.A.;
"Protein arginine methyltransferase 5 regulates ERK1/2 signal
transduction amplitude and cell fate through CRAF.";
Sci. Signal. 4:RA58-RA58(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[23]
UBIQUITINATION BY RNF149.
PubMed=22628551; DOI=10.1074/jbc.M111.319822;
Hong S.W., Jin D.H., Shin J.S., Moon J.H., Na Y.S., Jung K.A.,
Kim S.M., Kim J.C., Kim K.P., Hong Y.S., Lee J.L., Choi E.K.,
Lee J.S., Kim T.W.;
"Ring finger protein 149 is an E3 ubiquitin ligase active on wild-type
v-Raf murine sarcoma viral oncogene homolog B1 (BRAF).";
J. Biol. Chem. 287:24017-24025(2012).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151; SER-365; THR-401;
SER-446 AND SER-729, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
UBIQUITINATION AT LYS-578, AND MUTAGENESIS OF LYS-578.
PubMed=23907581; DOI=10.1038/srep02344;
An L., Jia W., Yu Y., Zou N., Liang L., Zhao Y., Fan Y., Cheng J.,
Shi Z., Xu G., Li G., Yang J., Zhang H.;
"Lys63-linked polyubiquitination of BRAF at lysine 578 is required for
BRAF-mediated signaling.";
Sci. Rep. 3:2344-2344(2013).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[27]
INTERACTION WITH FNIP1 AND FNIP2.
PubMed=27353360; DOI=10.1038/ncomms12037;
Woodford M.R., Dunn D.M., Blanden A.R., Capriotti D., Loiselle D.,
Prodromou C., Panaretou B., Hughes P.F., Smith A., Ackerman W.,
Haystead T.A., Loh S.N., Bourboulia D., Schmidt L.S.,
Marston Linehan W., Bratslavsky G., Mollapour M.;
"The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and
enhance drug binding.";
Nat. Commun. 7:12037-12037(2016).
[28]
X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 444-719 IN COMPLEX WITH
INHIBITOR.
PubMed=18287029; DOI=10.1073/pnas.0711741105;
Tsai J., Lee J.T., Wang W., Zhang J., Cho H., Mamo S., Bremer R.,
Gillette S., Kong J., Haass N.K., Sproesser K., Li L., Smalley K.S.,
Fong D., Zhu Y.L., Marimuthu A., Nguyen H., Lam B., Liu J., Cheung I.,
Rice J., Suzuki Y., Luu C., Settachatgul C., Shellooe R., Cantwell J.,
Kim S.H., Schlessinger J., Zhang K.Y., West B.L., Powell B.,
Habets G., Zhang C., Ibrahim P.N., Hirth P., Artis D.R., Herlyn M.,
Bollag G.;
"Discovery of a selective inhibitor of oncogenic B-Raf kinase with
potent antimelanoma activity.";
Proc. Natl. Acad. Sci. U.S.A. 105:3041-3046(2008).
[29]
VARIANTS LNCR VAL-466 AND ARG-597.
PubMed=12460919;
Naoki K., Chen T.-H., Richards W.G., Sugarbaker D.J., Meyerson M.;
"Missense mutations of the BRAF gene in human lung adenocarcinoma.";
Cancer Res. 62:7001-7003(2002).
[30]
VARIANTS CANCER GLU-464; VAL-464; ALA-466; GLU-466; VAL-466; ALA-469;
GLU-469; LYS-586; LEU-595; ARG-596; ARG-597; VAL-597; GLU-600 AND
ASP-600, AND CHARACTERIZATION OF VARIANTS CANCER VAL-464; ALA-469;
VAL-597 AND GLU-600.
PubMed=12068308; DOI=10.1038/nature00766;
Davies H., Bignell G.R., Cox C., Stephens P., Edkins S., Clegg S.,
Teague J., Woffendin H., Garnett M.J., Bottomley W., Davis N.,
Dicks E., Ewing R., Floyd Y., Gray K., Hall S., Hawes R., Hughes J.,
Kosmidou V., Menzies A., Mould C., Parker A., Stevens C., Watt S.,
Hooper S., Wilson R., Jayatilake H., Gusterson B.A., Cooper C.,
Shipley J., Hargrave D., Pritchard-Jones K., Maitland N.,
Chenevix-Trench G., Riggins G.J., Bigner D.D., Palmieri G., Cossu A.,
Flanagan A., Nicholson A., Ho J.W.C., Leung S.Y., Yuen S.T.,
Weber B.L., Seigler H.F., Darrow T.L., Paterson H., Marais R.,
Marshall C.J., Wooster R., Stratton M.R., Futreal P.A.;
"Mutations of the BRAF gene in human cancer.";
Nature 417:949-954(2002).
[31]
VARIANTS CRC ILE-462; SER-463; GLU-464; GLU-600 AND GLU-601.
PubMed=12198537; DOI=10.1038/418934a;
Rajagopalan H., Bardelli A., Lengauer C., Kinzler K.W., Vogelstein B.,
Velculescu V.E.;
"Tumorigenesis: RAF/RAS oncogenes and mismatch-repair status.";
Nature 418:934-934(2002).
[32]
VARIANTS NHL ALA-469; ARG-469 AND GLY-594.
PubMed=14612909; DOI=10.1038/sj.bjc.6601371;
Lee J.W., Yoo N.J., Soung Ark W.S., Kim S.Y., Lee J.H., Park J.Y.,
Cho Y.G., Kim C.J., Ko Y.H., Kim S.H., Nam S.W., Lee J.Y., Lee S.H.;
"BRAF mutations in non-Hodgkin's lymphoma.";
Br. J. Cancer 89:1958-1960(2003).
[33]
CHARACTERIZATION OF VARIANT MELANOMA GLU-600.
PubMed=14500344;
Hingorani S.R., Jacobetz M.A., Robertson G.P., Herlyn M.,
Tuveson D.A.;
"Suppression of BRAF(V599E) in human melanoma abrogates
transformation.";
Cancer Res. 63:5198-5202(2003).
[34]
VARIANTS CFC1 PRO-246; ARG-257; GLU-469; PHE-485; GLU-499; LYS-501;
GLY-501 AND ASP-581.
PubMed=16474404; DOI=10.1038/ng1749;
Niihori T., Aoki Y., Narumi Y., Neri G., Cave H., Verloes A.,
Okamoto N., Hennekam R.C.M., Gillessen-Kaesbach G., Wieczorek D.,
Kavamura M.I., Kurosawa K., Ohashi H., Wilson L., Heron D.,
Bonneau D., Corona G., Kaname T., Naritomi K., Baumann C.,
Matsumoto N., Kato K., Kure S., Matsubara Y.;
"Germline KRAS and BRAF mutations in cardio-facio-cutaneous
syndrome.";
Nat. Genet. 38:294-296(2006).
[35]
VARIANT [LARGE SCALE ANALYSIS] GLU-600.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[36]
VARIANTS CFC1 ARG-257; ALA-467; SER-468; GLU-469; PHE-485; GLU-499;
LYS-501; GLY-501; ASP-581; LEU-595 AND VAL-596.
PubMed=16439621; DOI=10.1126/science.1124642;
Rodriguez-Viciana P., Tetsu O., Tidyman W.E., Estep A.L., Conger B.A.,
Cruz M.S., McCormick F., Rauen K.A.;
"Germline mutations in genes within the MAPK pathway cause cardio-
facio-cutaneous syndrome.";
Science 311:1287-1290(2006).
[37]
VARIANTS [LARGE SCALE ANALYSIS] SER-301; ALA-469; VAL-469; SER-581;
ARG-596; ARG-597; VAL-597 AND GLU-600.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[38]
VARIANTS CFC1 PRO-241; PRO-244; PRO-246; ARG-257; LYS-262; SER-468;
GLU-469; GLU-499; ASN-499; ASP-580; ASP-581 AND LEU-595.
PubMed=18042262; DOI=10.1111/j.1399-0004.2007.00931.x;
Schulz A.L., Albrecht B., Arici C., van der Burgt I., Buske A.,
Gillessen-Kaesbach G., Heller R., Horn D., Hubner C.A., Korenke G.C.,
Konig R., Kress W., Kruger G., Meinecke P., Mucke J., Plecko B.,
Rossier E., Schinzel A., Schulze A., Seemanova E., Seidel H.,
Spranger S., Tuysuz B., Uhrig S., Wieczorek D., Kutsche K., Zenker M.;
"Mutation and phenotypic spectrum in patients with cardio-facio-
cutaneous and Costello syndrome.";
Clin. Genet. 73:62-70(2008).
[39]
VARIANT LPRD3 PRO-241, VARIANTS NS7 CYS-531 AND VAL-597, VARIANTS CFC1
PHE-245; PRO-246; ARG-257; LYS-275; GLU-469; PHE-485; ASN-499;
LYS-501; PRO-525; LEU-595; ARG-599; GLN-601; GLU-638 AND ARG-709, AND
VARIANTS ARG-241 AND MET-241.
PubMed=19206169; DOI=10.1002/humu.20955;
Sarkozy A., Carta C., Moretti S., Zampino G., Digilio M.C.,
Pantaleoni F., Scioletti A.P., Esposito G., Cordeddu V., Lepri F.,
Petrangeli V., Dentici M.L., Mancini G.M., Selicorni A., Rossi C.,
Mazzanti L., Marino B., Ferrero G.B., Silengo M.C., Memo L.,
Stanzial F., Faravelli F., Stuppia L., Puxeddu E., Gelb B.D.,
Dallapiccola B., Tartaglia M.;
"Germline BRAF mutations in Noonan, LEOPARD, and cardiofaciocutaneous
syndromes: molecular diversity and associated phenotypic spectrum.";
Hum. Mutat. 30:695-702(2009).
[40]
VARIANT CRC GLU-600.
PubMed=23263490; DOI=10.1038/ng.2503;
CORGI Consortium;
WGS500 Consortium;
Palles C., Cazier J.B., Howarth K.M., Domingo E., Jones A.M.,
Broderick P., Kemp Z., Spain S.L., Guarino Almeida E., Salguero I.,
Sherborne A., Chubb D., Carvajal-Carmona L.G., Ma Y., Kaur K.,
Dobbins S., Barclay E., Gorman M., Martin L., Kovac M.B., Humphray S.,
Lucassen A., Holmes C.C., Bentley D., Donnelly P., Taylor J.,
Petridis C., Roylance R., Sawyer E.J., Kerr D.J., Clark S., Grimes J.,
Kearsey S.E., Thomas H.J., McVean G., Houlston R.S., Tomlinson I.;
"Germline mutations affecting the proofreading domains of POLE and
POLD1 predispose to colorectal adenomas and carcinomas.";
Nat. Genet. 45:136-144(2013).
[41]
VARIANT CRC GLU-600.
PubMed=24455489; DOI=10.3389/fonc.2013.00333;
D'mello S.A., Flanagan J.U., Green T.N., Leung E.Y.,
Askarian-Amiri M.E., Joseph W.R., McCrystal M.R., Isaacs R.J.,
Shaw J.H., Furneaux C.E., During M.J., Finlay G.J., Baguley B.C.,
Kalev-Zylinska M.L.;
"Evidence that GRIN2A mutations in melanoma correlate with decreased
survival.";
Front. Oncol. 3:333-333(2014).
-!- FUNCTION: Protein kinase involved in the transduction of mitogenic
signals from the cell membrane to the nucleus. May play a role in
the postsynaptic responses of hippocampal neuron. Phosphorylates
MAP2K1, and thereby contributes to the MAP kinase signal
transduction pathway. {ECO:0000269|PubMed:21441910}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:21441910}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Activity is increased by EGF and HGF.
-!- SUBUNIT: Monomer. Homodimer. Heterodimerizes with RAF1, and the
heterodimer possesses a highly increased kinase activity compared
to the respective homodimers or monomers. Heterodimerization is
mitogen-regulated and enhanced by 14-3-3 proteins. MAPK1/ERK2
activation can induce a negative feedback that promotes the
dissociation of the heterodimer by phosphorylating BRAF at Thr-
753. Found in a complex with at least BRAF, HRAS, MAP2K1, MAPK3
and RGS14. Interacts with RIT1. Interacts (via N-terminus) with
RGS14 (via RBD domains); the interaction mediates the formation of
a ternary complex with RAF1, a ternary complex inhibited by GNAI1
(By similarity). Interacts with DGKH (PubMed:19710016). Interacts
with PRMT5 (PubMed:21917714). Interacts with KSR2
(PubMed:21441910). Interacts with AKAP13, MAP2K1 and KSR1.
Identified in a complex with AKAP13, MAP2K1 and KSR1
(PubMed:21102438). Interacts with FNIP1 and FNIP2
(PubMed:27353360). {ECO:0000250, ECO:0000269|PubMed:18287029,
ECO:0000269|PubMed:19710016, ECO:0000269|PubMed:21102438,
ECO:0000269|PubMed:21441910, ECO:0000269|PubMed:21917714,
ECO:0000269|PubMed:27353360}.
-!- INTERACTION:
Self; NbExp=9; IntAct=EBI-365980, EBI-365980;
P10398:ARAF; NbExp=2; IntAct=EBI-365980, EBI-365961;
P08238:HSP90AB1; NbExp=2; IntAct=EBI-365980, EBI-352572;
Q61097:Ksr1 (xeno); NbExp=3; IntAct=EBI-365980, EBI-1536336;
Q02750:MAP2K1; NbExp=54; IntAct=EBI-365980, EBI-492564;
P36507:MAP2K2; NbExp=6; IntAct=EBI-365980, EBI-1056930;
Q13233:MAP3K1; NbExp=2; IntAct=EBI-365980, EBI-49776;
P04049:RAF1; NbExp=46; IntAct=EBI-365980, EBI-365996;
Q99N57:Raf1 (xeno); NbExp=3; IntAct=EBI-365980, EBI-397757;
Q8CGE9:Rgs12 (xeno); NbExp=2; IntAct=EBI-365980, EBI-7340552;
Q15349:RPS6KA2; NbExp=2; IntAct=EBI-365980, EBI-1384149;
Q13114:TRAF3; NbExp=2; IntAct=EBI-365980, EBI-357631;
P31946:YWHAB; NbExp=3; IntAct=EBI-365980, EBI-359815;
P63104:YWHAZ; NbExp=4; IntAct=EBI-365980, EBI-347088;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm. Cell
membrane {ECO:0000250}. Note=Colocalizes with RGS14 and RAF1 in
both the cytoplasm and membranes. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Brain and testis.
-!- PTM: Phosphorylation at Ser-365 by SGK1 inhibits its activity.
{ECO:0000269|PubMed:11410590, ECO:0000269|PubMed:1508179,
ECO:0000269|PubMed:19710016, ECO:0000269|Ref.8}.
-!- PTM: Methylation at Arg-671 decreases stability and kinase
activity. {ECO:0000269|PubMed:21917714}.
-!- PTM: Ubiquitinated by RNF149; which leads to proteasomal
degradation. Polyubiquitinated at Lys-578 in response to EGF.
{ECO:0000269|PubMed:22628551, ECO:0000269|PubMed:23907581}.
-!- DISEASE: Note=Defects in BRAF are found in a wide range of
cancers. {ECO:0000269|PubMed:18974108}.
-!- DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease
characterized by malignant lesions arising from the inner wall of
the large intestine (the colon) and the rectum. Genetic
alterations are often associated with progression from
premalignant lesion (adenoma) to invasive adenocarcinoma. Risk
factors for cancer of the colon and rectum include colon polyps,
long-standing ulcerative colitis, and genetic family history.
{ECO:0000269|PubMed:12198537, ECO:0000269|PubMed:21917714,
ECO:0000269|PubMed:23263490, ECO:0000269|PubMed:24455489}.
Note=The disease may be caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Lung cancer (LNCR) [MIM:211980]: A common malignancy
affecting tissues of the lung. The most common form of lung cancer
is non-small cell lung cancer (NSCLC) that can be divided into 3
major histologic subtypes: squamous cell carcinoma,
adenocarcinoma, and large cell lung cancer. NSCLC is often
diagnosed at an advanced stage and has a poor prognosis.
{ECO:0000269|PubMed:12460919}. Note=The gene represented in this
entry is involved in disease pathogenesis.
-!- DISEASE: Familial non-Hodgkin lymphoma (NHL) [MIM:605027]: Cancer
that starts in cells of the lymph system, which is part of the
body's immune system. NHLs can occur at any age and are often
marked by enlarged lymph nodes, fever and weight loss.
{ECO:0000269|PubMed:14612909}. Note=The gene represented in this
entry is involved in disease pathogenesis.
-!- DISEASE: Cardiofaciocutaneous syndrome 1 (CFC1) [MIM:115150]: A
multiple congenital anomaly disorder characterized by a
distinctive facial appearance, heart defects and mental
retardation. Heart defects include pulmonic stenosis, atrial
septal defects and hypertrophic cardiomyopathy. Some affected
individuals present with ectodermal abnormalities such as sparse,
friable hair, hyperkeratotic skin lesions and a generalized
ichthyosis-like condition. Typical facial features are similar to
Noonan syndrome. They include high forehead with bitemporal
constriction, hypoplastic supraorbital ridges, downslanting
palpebral fissures, a depressed nasal bridge, and posteriorly
angulated ears with prominent helices.
{ECO:0000269|PubMed:16439621, ECO:0000269|PubMed:16474404,
ECO:0000269|PubMed:18042262, ECO:0000269|PubMed:19206169}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Noonan syndrome 7 (NS7) [MIM:613706]: A form of Noonan
syndrome, a disease characterized by short stature, facial
dysmorphic features such as hypertelorism, a downward eyeslant and
low-set posteriorly rotated ears, and a high incidence of
congenital heart defects and hypertrophic cardiomyopathy. Other
features can include a short neck with webbing or redundancy of
skin, deafness, motor delay, variable intellectual deficits,
multiple skeletal defects, cryptorchidism, and bleeding diathesis.
Individuals with Noonan syndrome are at risk of juvenile
myelomonocytic leukemia, a myeloproliferative disorder
characterized by excessive production of myelomonocytic cells.
{ECO:0000269|PubMed:19206169}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: LEOPARD syndrome 3 (LPRD3) [MIM:613707]: A disorder
characterized by lentigines, electrocardiographic conduction
abnormalities, ocular hypertelorism, pulmonic stenosis,
abnormalities of genitalia, retardation of growth, and
sensorineural deafness. {ECO:0000269|PubMed:19206169}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Note=A chromosomal aberration involving BRAF is found in
pilocytic astrocytomas. A tandem duplication of 2 Mb at 7q34 leads
to the expression of a KIAA1549-BRAF fusion protein with a
constitutive kinase activity and inducing cell transformation.
{ECO:0000269|PubMed:18974108}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. RAF subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD43193.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAQ43111.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAQ43112.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAQ43113.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAQ43114.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAQ43115.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAQ43116.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BRAFID828.html";
-----------------------------------------------------------------------
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EMBL; M95712; AAA35609.2; -; mRNA.
EMBL; AC006344; AAD43193.1; ALT_SEQ; Genomic_DNA.
EMBL; EU600171; ACD11489.1; -; Genomic_DNA.
EMBL; AC006347; AAD15551.1; -; Genomic_DNA.
EMBL; CH236950; EAL24023.1; -; Genomic_DNA.
EMBL; BC101757; AAI01758.1; -; mRNA.
EMBL; BC112079; AAI12080.1; -; mRNA.
EMBL; X65187; CAA46301.1; -; Genomic_DNA.
EMBL; M21001; AAA96495.1; -; mRNA.
EMBL; AM989472; CAQ43111.1; ALT_INIT; mRNA.
EMBL; AM989473; CAQ43112.1; ALT_INIT; mRNA.
EMBL; AM989474; CAQ43113.1; ALT_INIT; mRNA.
EMBL; AM989475; CAQ43114.1; ALT_INIT; mRNA.
EMBL; AM989476; CAQ43115.1; ALT_INIT; mRNA.
EMBL; AM989477; CAQ43116.1; ALT_INIT; mRNA.
CCDS; CCDS5863.1; -.
PIR; A57977; TVHUBF.
RefSeq; NP_004324.2; NM_004333.4.
UniGene; Hs.550061; -.
UniGene; Hs.600998; -.
UniGene; Hs.605380; -.
UniGene; Hs.659507; -.
UniGene; Hs.684552; -.
PDB; 1UWH; X-ray; 2.95 A; A/B=448-723.
PDB; 1UWJ; X-ray; 3.50 A; A/B=448-723.
PDB; 2FB8; X-ray; 2.90 A; A/B=445-723.
PDB; 2L05; NMR; -; A=149-232.
PDB; 3C4C; X-ray; 2.57 A; A/B=444-721.
PDB; 3D4Q; X-ray; 2.80 A; A/B=433-726.
PDB; 3IDP; X-ray; 2.70 A; A/B=434-727.
PDB; 3II5; X-ray; 2.79 A; A/B=432-726.
PDB; 3NY5; X-ray; 1.99 A; A/B/C/D=153-237.
PDB; 3OG7; X-ray; 2.45 A; A/B=448-720.
PDB; 3PPJ; X-ray; 3.70 A; A/B=432-726.
PDB; 3PPK; X-ray; 3.00 A; A/B=432-726.
PDB; 3PRF; X-ray; 2.90 A; A/B=432-726.
PDB; 3PRI; X-ray; 3.50 A; A/B=432-726.
PDB; 3PSB; X-ray; 3.40 A; A/B=433-726.
PDB; 3PSD; X-ray; 3.60 A; A/B=433-726.
PDB; 3Q4C; X-ray; 3.20 A; A/B=432-726.
PDB; 3Q96; X-ray; 3.10 A; A/B=446-727.
PDB; 3SKC; X-ray; 3.20 A; A/B=432-726.
PDB; 3TV4; X-ray; 3.40 A; A/B=432-726.
PDB; 3TV6; X-ray; 3.30 A; A/B=432-726.
PDB; 4CQE; X-ray; 2.30 A; A/B=448-723.
PDB; 4DBN; X-ray; 3.15 A; A/B=445-726.
PDB; 4E26; X-ray; 2.55 A; A/B=432-726.
PDB; 4E4X; X-ray; 3.60 A; A/B=432-726.
PDB; 4EHE; X-ray; 3.30 A; A/B=432-726.
PDB; 4EHG; X-ray; 3.50 A; A/B=432-726.
PDB; 4FC0; X-ray; 2.95 A; A/B=445-726.
PDB; 4FK3; X-ray; 2.65 A; A/B=444-723.
PDB; 4G9C; X-ray; 3.50 A; A/B=432-726.
PDB; 4G9R; X-ray; 3.20 A; A/B=432-726.
PDB; 4H58; X-ray; 3.10 A; A/B/C=448-722.
PDB; 4JVG; X-ray; 3.09 A; A/B/C/D=444-723.
PDB; 4KSP; X-ray; 2.93 A; A/B=445-726.
PDB; 4KSQ; X-ray; 3.30 A; A/B=445-726.
PDB; 4MBJ; X-ray; 3.60 A; A/B=432-723.
PDB; 4MNE; X-ray; 2.85 A; B/C/F/G=432-726.
PDB; 4MNF; X-ray; 2.80 A; A/B=432-736.
PDB; 4PP7; X-ray; 3.40 A; A/B=432-726.
PDB; 4R5Y; X-ray; 3.50 A; A/B=444-723.
PDB; 4RZV; X-ray; 2.99 A; A/B=443-723.
PDB; 4RZW; X-ray; 3.49 A; A/B=443-723.
PDB; 4WO5; X-ray; 2.83 A; A/B=444-723.
PDB; 4XV1; X-ray; 2.47 A; A/B=444-705.
PDB; 4XV2; X-ray; 2.50 A; A/B=444-705.
PDB; 4XV3; X-ray; 2.80 A; A/B=444-705.
PDB; 4XV9; X-ray; 2.00 A; A=442-705.
PDB; 4YHT; X-ray; 3.05 A; A/B=449-720.
PDB; 5C9C; X-ray; 2.70 A; A/B=432-726.
PDB; 5CSW; X-ray; 2.66 A; A/B=442-721.
PDB; 5CSX; X-ray; 2.51 A; A=442-721.
PDB; 5CT7; X-ray; 3.17 A; A/B=445-723.
PDB; 5FD2; X-ray; 2.89 A; A/B=433-726.
PDB; 5HI2; X-ray; 2.51 A; A=444-737.
PDB; 5HID; X-ray; 2.50 A; A/B=444-737.
PDB; 5HIE; X-ray; 3.00 A; A/B/C/D=432-726.
PDB; 5ITA; X-ray; 1.95 A; A/B=448-723.
PDB; 5J17; NMR; -; A=151-232.
PDB; 5J18; NMR; -; A=151-232.
PDB; 5J2R; NMR; -; A=151-232.
PDB; 5JRQ; X-ray; 2.29 A; A/B=448-723.
PDB; 5JSM; X-ray; 2.19 A; A/B/C/D=448-723.
PDB; 5JT2; X-ray; 2.70 A; A/B/C/D=448-723.
PDBsum; 1UWH; -.
PDBsum; 1UWJ; -.
PDBsum; 2FB8; -.
PDBsum; 2L05; -.
PDBsum; 3C4C; -.
PDBsum; 3D4Q; -.
PDBsum; 3IDP; -.
PDBsum; 3II5; -.
PDBsum; 3NY5; -.
PDBsum; 3OG7; -.
PDBsum; 3PPJ; -.
PDBsum; 3PPK; -.
PDBsum; 3PRF; -.
PDBsum; 3PRI; -.
PDBsum; 3PSB; -.
PDBsum; 3PSD; -.
PDBsum; 3Q4C; -.
PDBsum; 3Q96; -.
PDBsum; 3SKC; -.
PDBsum; 3TV4; -.
PDBsum; 3TV6; -.
PDBsum; 4CQE; -.
PDBsum; 4DBN; -.
PDBsum; 4E26; -.
PDBsum; 4E4X; -.
PDBsum; 4EHE; -.
PDBsum; 4EHG; -.
PDBsum; 4FC0; -.
PDBsum; 4FK3; -.
PDBsum; 4G9C; -.
PDBsum; 4G9R; -.
PDBsum; 4H58; -.
PDBsum; 4JVG; -.
PDBsum; 4KSP; -.
PDBsum; 4KSQ; -.
PDBsum; 4MBJ; -.
PDBsum; 4MNE; -.
PDBsum; 4MNF; -.
PDBsum; 4PP7; -.
PDBsum; 4R5Y; -.
PDBsum; 4RZV; -.
PDBsum; 4RZW; -.
PDBsum; 4WO5; -.
PDBsum; 4XV1; -.
PDBsum; 4XV2; -.
PDBsum; 4XV3; -.
PDBsum; 4XV9; -.
PDBsum; 4YHT; -.
PDBsum; 5C9C; -.
PDBsum; 5CSW; -.
PDBsum; 5CSX; -.
PDBsum; 5CT7; -.
PDBsum; 5FD2; -.
PDBsum; 5HI2; -.
PDBsum; 5HID; -.
PDBsum; 5HIE; -.
PDBsum; 5ITA; -.
PDBsum; 5J17; -.
PDBsum; 5J18; -.
PDBsum; 5J2R; -.
PDBsum; 5JRQ; -.
PDBsum; 5JSM; -.
PDBsum; 5JT2; -.
ProteinModelPortal; P15056; -.
SMR; P15056; -.
BioGrid; 107141; 63.
DIP; DIP-1045N; -.
IntAct; P15056; 45.
MINT; MINT-1574728; -.
STRING; 9606.ENSP00000288602; -.
BindingDB; P15056; -.
ChEMBL; CHEMBL5145; -.
DrugBank; DB08912; Dabrafenib.
DrugBank; DB05238; PLX4032.
DrugBank; DB08896; Regorafenib.
DrugBank; DB00398; Sorafenib.
DrugBank; DB08881; Vemurafenib.
DrugBank; DB05190; XL281.
GuidetoPHARMACOLOGY; 1943; -.
iPTMnet; P15056; -.
PhosphoSitePlus; P15056; -.
BioMuta; BRAF; -.
DMDM; 50403720; -.
EPD; P15056; -.
MaxQB; P15056; -.
PaxDb; P15056; -.
PeptideAtlas; P15056; -.
PRIDE; P15056; -.
DNASU; 673; -.
Ensembl; ENST00000288602; ENSP00000288602; ENSG00000157764.
GeneID; 673; -.
KEGG; hsa:673; -.
UCSC; uc003vwc.5; human.
CTD; 673; -.
DisGeNET; 673; -.
GeneCards; BRAF; -.
GeneReviews; BRAF; -.
H-InvDB; HIX0167822; -.
HGNC; HGNC:1097; BRAF.
HPA; CAB004552; -.
HPA; HPA001328; -.
HPA; HPA071048; -.
MalaCards; BRAF; -.
MIM; 114500; phenotype.
MIM; 115150; phenotype.
MIM; 164757; gene.
MIM; 211980; phenotype.
MIM; 605027; phenotype.
MIM; 613706; phenotype.
MIM; 613707; phenotype.
neXtProt; NX_P15056; -.
OpenTargets; ENSG00000157764; -.
Orphanet; 1340; Cardiofaciocutaneous syndrome.
Orphanet; 54595; Craniopharyngioma.
Orphanet; 58017; Hairy cell leukemia.
Orphanet; 99872; Hashimoto-Pritzker syndrome.
Orphanet; 500; LEOPARD syndrome.
Orphanet; 648; Noonan syndrome.
Orphanet; 251612; Pilocytic astrocytoma.
PharmGKB; PA25408; -.
eggNOG; KOG0193; Eukaryota.
eggNOG; ENOG410Y4UP; LUCA.
GeneTree; ENSGT00760000118807; -.
HOVERGEN; HBG001886; -.
InParanoid; P15056; -.
KO; K04365; -.
OMA; IVFDFEP; -.
OrthoDB; EOG091G09SB; -.
PhylomeDB; P15056; -.
TreeFam; TF317006; -.
BRENDA; 2.7.10.2; 2681.
Reactome; R-HSA-1295596; Spry regulation of FGF signaling.
Reactome; R-HSA-170968; Frs2-mediated activation.
Reactome; R-HSA-170984; ARMS-mediated activation.
Reactome; R-HSA-187706; Signalling to p38 via RIT and RIN.
Reactome; R-HSA-442742; CREB phosphorylation through the activation of Ras.
Reactome; R-HSA-5673000; RAF activation.
Reactome; R-HSA-5674135; MAP2K and MAPK activation.
Reactome; R-HSA-5674499; Negative feedback regulation of MAPK pathway.
Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
Reactome; R-HSA-6802949; Signaling by RAS mutants.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
SignaLink; P15056; -.
SIGNOR; P15056; -.
ChiTaRS; BRAF; human.
EvolutionaryTrace; P15056; -.
GeneWiki; BRAF_(gene); -.
GenomeRNAi; 673; -.
PMAP-CutDB; P15056; -.
PRO; PR:P15056; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000157764; -.
CleanEx; HS_BRAF; -.
ExpressionAtlas; P15056; baseline and differential.
Genevisible; P15056; HS.
GO; GO:0044297; C:cell body; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005622; C:intracellular; IBA:GO_Central.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004709; F:MAP kinase kinase kinase activity; IBA:GO_Central.
GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IBA:GO_Central.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0004672; F:protein kinase activity; IDA:BHF-UCL.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
GO; GO:0043369; P:CD4-positive or CD8-positive, alpha-beta T cell lineage commitment; IEA:Ensembl.
GO; GO:0043367; P:CD4-positive, alpha-beta T cell differentiation; IEA:Ensembl.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0071277; P:cellular response to calcium ion; IDA:BHF-UCL.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
GO; GO:0090150; P:establishment of protein localization to membrane; IDA:CACAO.
GO; GO:0060324; P:face development; IEA:Ensembl.
GO; GO:0015758; P:glucose transport; IDA:CACAO.
GO; GO:0060323; P:head morphogenesis; IEA:Ensembl.
GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0002318; P:myeloid progenitor cell differentiation; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IEA:Ensembl.
GO; GO:0010764; P:negative regulation of fibroblast migration; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0009968; P:negative regulation of signal transduction; IBA:GO_Central.
GO; GO:2000301; P:negative regulation of synaptic vesicle exocytosis; IEA:Ensembl.
GO; GO:0048680; P:positive regulation of axon regeneration; IEA:Ensembl.
GO; GO:0050772; P:positive regulation of axonogenesis; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:UniProtKB.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IDA:BHF-UCL.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
GO; GO:0045580; P:regulation of T cell differentiation; IEA:Ensembl.
GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
GO; GO:0048538; P:thymus development; IEA:Ensembl.
GO; GO:0030878; P:thyroid gland development; IEA:Ensembl.
GO; GO:0008542; P:visual learning; IEA:Ensembl.
CDD; cd00029; C1; 1.
InterPro; IPR020454; DAG/PE-bd.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR003116; RBD_dom.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR029071; Ubiquitin-rel_dom.
Pfam; PF00130; C1_1; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF02196; RBD; 1.
PRINTS; PR00008; DAGPEDOMAIN.
SMART; SM00109; C1; 1.
SMART; SM00455; RBD; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF54236; SSF54236; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS50898; RBD; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Cardiomyopathy; Cell membrane;
Chromosomal rearrangement; Complete proteome; Cytoplasm; Deafness;
Direct protein sequencing; Disease mutation; Ectodermal dysplasia;
Isopeptide bond; Kinase; Membrane; Mental retardation; Metal-binding;
Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Proto-oncogene; Reference proteome;
Serine/threonine-protein kinase; Transferase; Ubl conjugation; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.8}.
CHAIN 2 766 Serine/threonine-protein kinase B-raf.
/FTId=PRO_0000085665.
DOMAIN 155 227 RBD. {ECO:0000255|PROSITE-
ProRule:PRU00262}.
DOMAIN 457 717 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ZN_FING 234 280 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
NP_BIND 463 471 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 6 11 Poly-Gly.
COMPBIAS 122 129 Poly-Ser.
COMPBIAS 428 432 Poly-Ser.
ACT_SITE 576 576 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
METAL 235 235 Zinc 1. {ECO:0000250}.
METAL 248 248 Zinc 2. {ECO:0000250}.
METAL 251 251 Zinc 2. {ECO:0000250}.
METAL 261 261 Zinc 1. {ECO:0000250}.
METAL 264 264 Zinc 1. {ECO:0000250}.
METAL 269 269 Zinc 2. {ECO:0000250}.
METAL 272 272 Zinc 2. {ECO:0000250}.
METAL 280 280 Zinc 1. {ECO:0000250}.
BINDING 483 483 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 380 381 Breakpoint for translocation to form
KIAA1549-BRAF fusion protein.
SITE 438 439 Breakpoint for translocation to form
KIAA1549-BRAF fusion protein.
MOD_RES 2 2 N-acetylalanine. {ECO:0000269|Ref.8}.
MOD_RES 151 151 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 333 333 Phosphoserine.
{ECO:0000250|UniProtKB:P28028}.
MOD_RES 365 365 Phosphoserine; by SGK1.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:11410590,
ECO:0000269|Ref.8}.
MOD_RES 373 373 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:1508179}.
MOD_RES 396 396 Phosphothreonine. {ECO:0000269|Ref.8}.
MOD_RES 399 399 Phosphoserine. {ECO:0000269|Ref.8}.
MOD_RES 401 401 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|Ref.8}.
MOD_RES 446 446 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 447 447 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 671 671 Omega-N-methylarginine; by PRMT5.
{ECO:0000269|PubMed:21917714}.
MOD_RES 729 729 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|Ref.8}.
MOD_RES 750 750 Phosphoserine.
{ECO:0000250|UniProtKB:P28028}.
MOD_RES 753 753 Phosphothreonine; by MAPK1.
{ECO:0000269|PubMed:19710016}.
CROSSLNK 578 578 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:23907581}.
VARIANT 241 241 T -> M (in a patient with Noonan
syndrome; dbSNP:rs387906660).
{ECO:0000269|PubMed:19206169}.
/FTId=VAR_058620.
VARIANT 241 241 T -> P (in CFC1 and LPRD3;
dbSNP:rs387906661).
{ECO:0000269|PubMed:18042262,
ECO:0000269|PubMed:19206169}.
/FTId=VAR_058621.
VARIANT 241 241 T -> R (in a patient with Noonan
syndrome; dbSNP:rs387906660).
{ECO:0000269|PubMed:19206169}.
/FTId=VAR_058622.
VARIANT 244 244 T -> P (in CFC1; dbSNP:rs397507465).
{ECO:0000269|PubMed:18042262}.
/FTId=VAR_065171.
VARIANT 245 245 L -> F (in CFC1; dbSNP:rs397507466).
{ECO:0000269|PubMed:19206169}.
/FTId=VAR_058623.
VARIANT 246 246 A -> P (in CFC1; dbSNP:rs180177034).
{ECO:0000269|PubMed:16474404,
ECO:0000269|PubMed:18042262,
ECO:0000269|PubMed:19206169}.
/FTId=VAR_026113.
VARIANT 257 257 Q -> R (in CFC1; dbSNP:rs180177035).
{ECO:0000269|PubMed:16439621,
ECO:0000269|PubMed:16474404,
ECO:0000269|PubMed:18042262,
ECO:0000269|PubMed:19206169}.
/FTId=VAR_026114.
VARIANT 262 262 Q -> K (in CFC1; dbSNP:rs397507470).
{ECO:0000269|PubMed:18042262}.
/FTId=VAR_065172.
VARIANT 275 275 E -> K (in CFC1).
{ECO:0000269|PubMed:19206169}.
/FTId=VAR_058624.
VARIANT 301 301 P -> S (in dbSNP:rs34776339).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040391.
VARIANT 462 462 R -> I (in CRC; dbSNP:rs180177032).
{ECO:0000269|PubMed:12198537}.
/FTId=VAR_018613.
VARIANT 463 463 I -> S (in CRC; dbSNP:rs180177033).
{ECO:0000269|PubMed:12198537}.
/FTId=VAR_018614.
VARIANT 464 464 G -> E (in CRC; dbSNP:rs121913348).
{ECO:0000269|PubMed:12068308,
ECO:0000269|PubMed:12198537}.
/FTId=VAR_018615.
VARIANT 464 464 G -> V (in a colorectal cancer cell line;
elevated kinase activity; efficiently
induces cell transformation;
dbSNP:rs121913348).
{ECO:0000269|PubMed:12068308}.
/FTId=VAR_018616.
VARIANT 466 466 G -> A (in melanoma; dbSNP:rs121913351).
{ECO:0000269|PubMed:12068308}.
/FTId=VAR_018617.
VARIANT 466 466 G -> E (in melanoma; dbSNP:rs121913351).
{ECO:0000269|PubMed:12068308}.
/FTId=VAR_018618.
VARIANT 466 466 G -> V (in LNCR; dbSNP:rs121913351).
{ECO:0000269|PubMed:12068308,
ECO:0000269|PubMed:12460919}.
/FTId=VAR_018512.
VARIANT 467 467 S -> A (in CFC1; dbSNP:rs869025606).
{ECO:0000269|PubMed:16439621}.
/FTId=VAR_035096.
VARIANT 468 468 F -> S (in CFC1; dbSNP:rs397507473).
{ECO:0000269|PubMed:16439621,
ECO:0000269|PubMed:18042262}.
/FTId=VAR_035097.
VARIANT 469 469 G -> A (in NHL; also in a lung
adenocarcinoma sample; somatic mutation;
elevated kinase activity; efficiently
induces cell transformation;
dbSNP:rs121913355).
{ECO:0000269|PubMed:12068308,
ECO:0000269|PubMed:14612909,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_018620.
VARIANT 469 469 G -> E (in CFC1 and colon cancer;
dbSNP:rs121913355).
{ECO:0000269|PubMed:12068308,
ECO:0000269|PubMed:16439621,
ECO:0000269|PubMed:16474404,
ECO:0000269|PubMed:18042262,
ECO:0000269|PubMed:19206169}.
/FTId=VAR_018621.
VARIANT 469 469 G -> R (in NHL; dbSNP:rs121913357).
{ECO:0000269|PubMed:14612909}.
/FTId=VAR_018622.
VARIANT 469 469 G -> V (in a colorectal adenocarcinoma
sample; somatic mutation;
dbSNP:rs121913355).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040392.
VARIANT 485 485 L -> F (in CFC1; dbSNP:rs180177036).
{ECO:0000269|PubMed:16439621,
ECO:0000269|PubMed:16474404,
ECO:0000269|PubMed:19206169}.
/FTId=VAR_026115.
VARIANT 499 499 K -> E (in CFC1; dbSNP:rs180177037).
{ECO:0000269|PubMed:16439621,
ECO:0000269|PubMed:16474404,
ECO:0000269|PubMed:18042262}.
/FTId=VAR_026116.
VARIANT 499 499 K -> N (in CFC1; dbSNP:rs397507476).
{ECO:0000269|PubMed:18042262,
ECO:0000269|PubMed:19206169}.
/FTId=VAR_058625.
VARIANT 501 501 E -> G (in CFC1; dbSNP:rs180177039).
{ECO:0000269|PubMed:16439621,
ECO:0000269|PubMed:16474404}.
/FTId=VAR_026117.
VARIANT 501 501 E -> K (in CFC1; dbSNP:rs180177038).
{ECO:0000269|PubMed:16439621,
ECO:0000269|PubMed:16474404,
ECO:0000269|PubMed:19206169}.
/FTId=VAR_026118.
VARIANT 525 525 L -> P (in CFC1; dbSNP:rs869025340).
{ECO:0000269|PubMed:19206169}.
/FTId=VAR_058626.
VARIANT 531 531 W -> C (in NS7; dbSNP:rs606231228).
{ECO:0000269|PubMed:19206169}.
/FTId=VAR_058627.
VARIANT 580 580 N -> D (in CFC1).
{ECO:0000269|PubMed:18042262}.
/FTId=VAR_065173.
VARIANT 581 581 N -> D (in CFC1; dbSNP:rs180177040).
{ECO:0000269|PubMed:16439621,
ECO:0000269|PubMed:16474404,
ECO:0000269|PubMed:18042262}.
/FTId=VAR_026119.
VARIANT 581 581 N -> S (in a colorectal adenocarcinoma
sample; somatic mutation;
dbSNP:rs121913370).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040393.
VARIANT 586 586 E -> K (in ovarian cancer;
dbSNP:rs121913340).
{ECO:0000269|PubMed:12068308}.
/FTId=VAR_018623.
VARIANT 594 594 D -> G (in NHL; dbSNP:rs121913338).
{ECO:0000269|PubMed:14612909}.
/FTId=VAR_018624.
VARIANT 595 595 F -> L (in colon cancer and CFC1;
dbSNP:rs121913341).
{ECO:0000269|PubMed:12068308,
ECO:0000269|PubMed:16439621,
ECO:0000269|PubMed:18042262,
ECO:0000269|PubMed:19206169}.
/FTId=VAR_018625.
VARIANT 596 596 G -> R (in a colorectal adenocarcinoma
sample; somatic mutation;
dbSNP:rs121913361).
{ECO:0000269|PubMed:12068308,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_018626.
VARIANT 596 596 G -> V (in CFC1; dbSNP:rs397507483).
{ECO:0000269|PubMed:16439621}.
/FTId=VAR_035098.
VARIANT 597 597 L -> R (in LNCR; also found in an ovarian
serous carcinoma sample; somatic
mutation; dbSNP:rs121913366).
{ECO:0000269|PubMed:12068308,
ECO:0000269|PubMed:12460919,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_018513.
VARIANT 597 597 L -> V (in NS7; also in a lung
adenocarcinoma sample; somatic mutation;
elevated kinase activity; efficiently
induces cell transformation;
dbSNP:rs121913369).
{ECO:0000269|PubMed:12068308,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:19206169}.
/FTId=VAR_018627.
VARIANT 599 599 T -> R (in CFC1).
{ECO:0000269|PubMed:19206169}.
/FTId=VAR_058628.
VARIANT 600 600 V -> D (in a melanoma cell line; requires
2 nucleotide substitutions;
dbSNP:rs121913377).
{ECO:0000269|PubMed:12068308}.
/FTId=VAR_018628.
VARIANT 600 600 V -> E (in CRC; also found in sarcoma,
metastatic melanoma, ovarian serous
carcinoma, pilocytic astrocytoma; somatic
mutation; most common mutation;
constitutive and elevated kinase
activity; efficiently induces cell
transformation; suppression of mutation
in melanoma causes growth arrest and
promotes apoptosis; loss of regulation by
PMRT5; dbSNP:rs113488022).
{ECO:0000269|PubMed:12068308,
ECO:0000269|PubMed:12198537,
ECO:0000269|PubMed:14500344,
ECO:0000269|PubMed:16959974,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:21917714,
ECO:0000269|PubMed:23263490,
ECO:0000269|PubMed:24455489}.
/FTId=VAR_018629.
VARIANT 601 601 K -> E (in CRC; dbSNP:rs121913364).
{ECO:0000269|PubMed:12198537}.
/FTId=VAR_018630.
VARIANT 601 601 K -> Q (in CFC1; dbSNP:rs121913364).
{ECO:0000269|PubMed:19206169}.
/FTId=VAR_058629.
VARIANT 638 638 D -> E (in CFC1; dbSNP:rs180177042).
{ECO:0000269|PubMed:19206169}.
/FTId=VAR_058630.
VARIANT 709 709 Q -> R (in CFC1; dbSNP:rs397507486).
{ECO:0000269|PubMed:19206169}.
/FTId=VAR_058631.
MUTAGEN 483 483 K->S: Reduces kinase activity with
MAP2K1. {ECO:0000269|PubMed:21441910}.
MUTAGEN 578 578 K->R: Blocks EGF-induced ubiquitination
and ERK activation.
{ECO:0000269|PubMed:23907581}.
MUTAGEN 671 671 R->K: Increased kinase activity and
stability in response to EGF treatment.
{ECO:0000269|PubMed:21917714}.
CONFLICT 766 766 H -> D (in Ref. 11; AAA96495).
{ECO:0000305}.
STRAND 156 161 {ECO:0000244|PDB:3NY5}.
TURN 162 164 {ECO:0000244|PDB:3NY5}.
STRAND 165 170 {ECO:0000244|PDB:3NY5}.
HELIX 177 186 {ECO:0000244|PDB:3NY5}.
TURN 187 189 {ECO:0000244|PDB:3NY5}.
HELIX 192 194 {ECO:0000244|PDB:3NY5}.
STRAND 195 199 {ECO:0000244|PDB:3NY5}.
STRAND 206 208 {ECO:0000244|PDB:3NY5}.
HELIX 214 217 {ECO:0000244|PDB:3NY5}.
STRAND 221 226 {ECO:0000244|PDB:3NY5}.
HELIX 448 450 {ECO:0000244|PDB:5JRQ}.
HELIX 454 456 {ECO:0000244|PDB:5JRQ}.
STRAND 458 466 {ECO:0000244|PDB:5ITA}.
STRAND 469 486 {ECO:0000244|PDB:5ITA}.
STRAND 487 489 {ECO:0000244|PDB:4E26}.
HELIX 492 506 {ECO:0000244|PDB:5ITA}.
STRAND 516 520 {ECO:0000244|PDB:5ITA}.
STRAND 522 524 {ECO:0000244|PDB:5ITA}.
STRAND 526 530 {ECO:0000244|PDB:5ITA}.
STRAND 534 536 {ECO:0000244|PDB:3OG7}.
HELIX 537 542 {ECO:0000244|PDB:5ITA}.
STRAND 543 545 {ECO:0000244|PDB:4RZW}.
HELIX 550 569 {ECO:0000244|PDB:5ITA}.
HELIX 579 581 {ECO:0000244|PDB:5ITA}.
STRAND 582 585 {ECO:0000244|PDB:5ITA}.
TURN 586 588 {ECO:0000244|PDB:5ITA}.
STRAND 589 592 {ECO:0000244|PDB:5ITA}.
TURN 598 600 {ECO:0000244|PDB:5JSM}.
TURN 602 605 {ECO:0000244|PDB:4RZV}.
HELIX 611 613 {ECO:0000244|PDB:4WO5}.
TURN 614 616 {ECO:0000244|PDB:5HID}.
HELIX 617 619 {ECO:0000244|PDB:5ITA}.
HELIX 622 625 {ECO:0000244|PDB:5ITA}.
TURN 626 629 {ECO:0000244|PDB:5HID}.
HELIX 635 651 {ECO:0000244|PDB:5ITA}.
TURN 655 659 {ECO:0000244|PDB:5ITA}.
HELIX 662 670 {ECO:0000244|PDB:5ITA}.
HELIX 678 680 {ECO:0000244|PDB:5ITA}.
STRAND 683 685 {ECO:0000244|PDB:5JRQ}.
HELIX 687 696 {ECO:0000244|PDB:5ITA}.
HELIX 701 703 {ECO:0000244|PDB:5ITA}.
HELIX 707 717 {ECO:0000244|PDB:5ITA}.
TURN 718 720 {ECO:0000244|PDB:4RZV}.
HELIX 723 726 {ECO:0000244|PDB:5HID}.
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


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18-785-210091 c-Jun (Ab-243) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.05 mg
18-785-210089 c-Jun (Ab-93) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.05 mg
18-785-210090 c-Jun (Ab-170) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.1 mg
18-785-210088 c-Jun (Ab-91) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.05 mg
18-785-210090 c-Jun (Ab-170) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.05 mg
18-785-210088 c-Jun (Ab-91) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.1 mg
G4693 Proto-oncogene serine threonine-protein kinase mos (MOS), Pig, ELISA Kit 96T
G4694 Proto-oncogene serine threonine-protein kinase mos (MOS), Rat, ELISA Kit 96T
10-782-55042 Transcription factor AP-1 - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 N_A 0.05 mg
10-782-55042 Transcription factor AP-1 - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 N_A 0.2 mg
18-785-210085 c-Jun (Phospho-Ser243) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.05 mg
18-785-210084 c-Jun (Phospho-Tyr170) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.1 mg
18-785-210084 c-Jun (Phospho-Tyr170) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.05 mg
18-003-43188 Transcription factor AP-1 - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.1 mg Protein A
18-785-210092 c-Jun (Phospho-Thr239) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.1 mg
18-785-210092 c-Jun (Phospho-Thr239) - Activator protein 1; AP1; Proto-oncogene c-jun; V-jun avian sarcoma virus 17 oncogene homolog; p39 Polyclonal 0.05 mg


 

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