[1]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
DOI=10.1093/nar/14.2.1009; PubMed=3003687 [NCBI, ExPASy, EBI, Israel, Japan]
Bonner T.I.,
Oppermann H.,
Seeburg P.,
Kerby S.B.,
Gunnell M.A.,
Young A.C.,
Rapp U.R.;
"The complete coding sequence of the human raf oncogene and the corresponding structure of the c-raf-1 gene.";
Nucleic Acids Res. 14:1009-1015(1986).
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[2]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-308.
NIEHS SNPs program;
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J.,
Istrail S.,
Sutton G.G.,
Florea L.,
Halpern A.L.,
Mobarry C.M.,
Lippert R.,
Walenz B.,
Shatkay H.,
Dew I.,
Miller J.R.,
Flanigan M.J.,
Edwards N.J.,
Bolanos R.,
Fasulo D.,
Halldorsson B.V.,
Hannenhalli S.,
Turner R.,
Yooseph S., ![]()
Lu F.,
Nusskern D.R.,
Shue B.C.,
Zheng X.H.,
Zhong F.,
Delcher A.L.,
Huson D.H.,
Kravitz S.A.,
Mouchard L.,
Reinert K.,
Remington K.A.,
Clark A.G.,
Waterman M.S.,
Eichler E.E.,
Adams M.D.,
Hunkapiller M.W.,
Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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[4]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pancreas;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[5]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 228-648.
PubMed=2993863 [NCBI, ExPASy, EBI, Israel, Japan]
Bonner T.I.,
Kerby S.B.,
Sutrave P.,
Gunnell M.A.,
Mark G.,
Rapp U.R.;
"Structure and biological activity of human homologs of the raf/mil oncogene.";
Mol. Cell. Biol. 5:1400-1407(1985).
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[6]
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PROTEIN SEQUENCE OF 254-278, AND PHOSPHORYLATION AT THR-269.
DOI=10.1038/378307a0; PubMed=7477354 [NCBI, ExPASy, EBI, Israel, Japan]
Yao B.,
Zhang Y.,
Delikat S.,
Mathias S.,
Basu S.,
Kolesnick R.;
"Phosphorylation of Raf by ceramide-activated protein kinase.";
Nature 378:307-310(1995).
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[7]
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PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
TISSUE=Placenta;
PubMed=1886707 [NCBI, ExPASy, EBI, Israel, Japan]
Dozier C.,
Ansieau S.,
Ferreira E.,
Coll J.,
Stehelin D.;
"An alternatively spliced c-mil/raf mRNA is predominantly expressed in chicken muscular tissues and conserved among vertebrate species.";
Oncogene 6:1307-1311(1991).
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[8]
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PHOSPHORYLATION AT SER-43; SER-259; THR-268; SER-499 AND SER-621.
PubMed=8349614 [NCBI, ExPASy, EBI, Israel, Japan]
Morrison D.K.,
Heidecker G.,
Rapp U.R.,
Copeland T.D.;
"Identification of the major phosphorylation sites of the Raf-1 kinase.";
J. Biol. Chem. 268:17309-17316(1993).
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[9]
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PHOSPHORYLATION.
DOI=10.1038/24184; PubMed=9823899 [NCBI, ExPASy, EBI, Israel, Japan]
King A.J.,
Sun H.,
Diaz B.,
Barnard D.,
Miao W.,
Bagrodia S.,
Marshall M.S.;
"The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338.";
Nature 396:180-183(1998).
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[10]
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ERRATUM.
King A.J.,
Sun H.,
Diaz B.,
Barnard D.,
Miao W.,
Bagrodia S.,
Marshall M.S.;
Nature 406:439-439(2000).
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[11]
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COMPETITION WITH RIN1.
DOI=10.1128/MCB.22.13.4638-4651.2002; PubMed=11784866 [NCBI, ExPASy, EBI, Israel, Japan]
Wang Y.,
Waldron R.T.,
Dhaka A.,
Patel A.,
Riley M.M.,
Rozengurt E.,
Colicelli J.;
"The RAS effector RIN1 directly competes with RAF and is regulated by 14-3-3 proteins.";
Mol. Cell. Biol. 22:916-926(2002).
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[12]
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INTERACTION WITH STK3, AND FUNCTION.
DOI=10.1126/science.1103233; PubMed=15618521 [NCBI, ExPASy, EBI, Israel, Japan]
O'Neill E.,
Rushworth L.,
Baccarini M.,
Kolch W.;
"Role of the kinase MST2 in suppression of apoptosis by the proto-oncogene product Raf-1.";
Science 306:2267-2270(2004).
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[13]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294 AND SER-301, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V.,
Blagoev B.,
Gnad F.,
Macek B.,
Kumar C.,
Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
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[14]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuoka S.,
Ballif B.A.,
Smogorzewska A.,
McDonald E.R. III,
Hurov K.E.,
Luo J.,
Bakalarski C.E.,
Zhao Z.,
Solimini N.,
Lerenthal Y.,
Shiloh Y.,
Gygi S.P.,
Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
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[15]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257 AND THR-258, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T.,
Yi W.,
Lu B.,
Park S.K.,
Xu T.,
Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
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[16]
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X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 51-131.
DOI=10.1038/375554a0; PubMed=7791872 [NCBI, ExPASy, EBI, Israel, Japan]
Nassar N.,
Horn G.,
Herrmann C.,
Scherer A.,
McCormick F.,
Wittinghofer A.;
"The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue.";
Nature 375:554-560(1995).
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[17]
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X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 56-131.
DOI=10.1038/nsb0896-723; PubMed=8756332 [NCBI, ExPASy, EBI, Israel, Japan]
Nassar N.,
Horn G.,
Herrmann C.,
Block C.,
Janknecht R.,
Wittinghofer A.;
"Ras/Rap effector specificity determined by charge reversal.";
Nat. Struct. Biol. 3:723-729(1996).
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[18]
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STRUCTURE BY NMR OF 55-132.
DOI=10.1021/bi00021a001; PubMed=7766599 [NCBI, ExPASy, EBI, Israel, Japan]
Emerson S.D.,
Madison V.S.,
Palermo R.E.,
Waugh D.S.,
Scheffler J.E.,
Tsao K.L.,
Kiefer S.E.,
Liu S.P.,
Fry D.C.;
"Solution structure of the Ras-binding domain of c-Raf-1 and identification of its Ras interaction surface.";
Biochemistry 34:6911-6918(1995).
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[19]
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STRUCTURE BY NMR OF 136-187.
DOI=10.1073/pnas.93.16.8312; PubMed=8710867 [NCBI, ExPASy, EBI, Israel, Japan]
Mott H.R.,
Carpenter J.W.,
Zhong S.,
Ghosh S.,
Bell R.M.,
Campbell S.L.;
"The solution structure of the Raf-1 cysteine-rich domain: a novel ras and phospholipid binding site.";
Proc. Natl. Acad. Sci. U.S.A. 93:8312-8317(1996).
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[20]
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VARIANTS NS5 SER-256; PHE-259; ARG-260; LEU-261; SER-261; ASN-486; GLY-486; ILE-491; ARG-491 AND THR-612, VARIANT HYPERTROPHIC CARDIOMYOPATHY ILE-260, VARIANT LEOPARD SYNDROME-2 VAL-613, VARIANT NS5/LEOPARD SYNDROME-2 LEU-257, CHARACTERIZATION OF VARIANTS NS5 SER-261; ASN-486 AND ILE-491, AND CHARACTERIZATION OF VARIANT LEOPARD SYNDROME-2 VAL-613.
DOI=10.1038/ng2073; PubMed=17603483 [NCBI, ExPASy, EBI, Israel, Japan]
Pandit B.,
Sarkozy A.,
Pennacchio L.A.,
Carta C.,
Oishi K.,
Martinelli S.,
Pogna E.A.,
Schackwitz W.,
Ustaszewska A.,
Landstrom A.,
Bos J.M.,
Ommen S.R.,
Esposito G.,
Lepri F.,
Faul C.,
Mundel P.,
Lopez Siguero J.P.,
Tenconi R.,
Selicorni A., ![]()
Rossi C.,
Mazzanti L.,
Torrente I.,
Marino B.,
Digilio M.C.,
Zampino G.,
Ackerman M.J.,
Dallapiccola B.,
Tartaglia M.,
Gelb B.D.;
"Gain-of-function RAF1 mutations cause Noonan and LEOPARD syndromes with hypertrophic cardiomyopathy.";
Nat. Genet. 39:1007-1012(2007).
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[21]
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VARIANTS NS5 LEU-257; ALA-261; SER-261; ALA-263 AND VAL-613, AND CHARACTERIZATION OF VARIANTS NS5 LEU-257; ALA-261; SER-261; ALA-263 AND VAL-613.
DOI=10.1038/ng2078; PubMed=17603482 [NCBI, ExPASy, EBI, Israel, Japan]
Razzaque M.A.,
Nishizawa T.,
Komoike Y.,
Yagi H.,
Furutani M.,
Amo R.,
Kamisago M.,
Momma K.,
Katayama H.,
Nakagawa M.,
Fujiwara Y.,
Matsushima M.,
Mizuno K.,
Tokuyama M.,
Hirota H.,
Muneuchi J.,
Higashinakagawa T.,
Matsuoka R.;
"Germline gain-of-function mutations in RAF1 cause Noonan syndrome.";
Nat. Genet. 39:1013-1017(2007).
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[22]
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VARIANTS [LARGE SCALE ANALYSIS] ALA-259 AND HIS-335.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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