NF1_HUMAN
ID NF1_HUMAN Reviewed; 2839 AA.
AC P21359; O00662; Q14284; Q14930; Q14931; Q9UMK3;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 245.
DE RecName: Full=Neurofibromin;
DE AltName: Full=Neurofibromatosis-related protein NF-1;
DE Contains:
DE RecName: Full=Neurofibromin truncated;
GN Name=NF1;
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] (ISOFORMS I AND II).
RX PubMed=1457041; DOI=10.1089/dna.1992.11.727;
RA Bernards A., Haase V.H., Murthy A.E., Menon A., Hannigan G.E.,
RA Gusella J.F.;
RT "Complete human NF1 cDNA sequence: two alternatively spliced mRNAs and
RT absence of expression in a neuroblastoma line.";
RL DNA Cell Biol. 11:727-734(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I).
RX PubMed=2134734; DOI=10.1126/science.2134734;
RA Wallace M.R., Marchuk D.A., Andersen L.B., Letcher R., Odeh H.M.,
RA Saulino A.M., Fountain J.W., Brereton A., Nicholson J., Mitchell A.L.,
RA Brownstein B.H., Collins F.S.;
RT "Type 1 neurofibromatosis gene: identification of a large transcript
RT disrupted in three NF1 patients.";
RL Science 249:181-186(1990).
RN [3]
RP ERRATUM OF PUBMED:2134734.
RX PubMed=2125369;
RA Wallace M.R., Marchuk D.A., Andersen L.B., Letcher R., Odeh H.M.,
RA Saulino A.M., Fountain J.W., Brereton A., Nicholson J., Mitchell A.L.,
RA Brownstein B.H., Collins F.S.;
RL Science 250:1749-1749(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I).
RX PubMed=1783401; DOI=10.1016/0888-7543(91)90017-9;
RA Marchuk D.A., Saulino A.M., Tavakkol R., Swaroop M., Wallace M.R.,
RA Andersen L.B., Mitchell A.L., Gutmann D.H., Boguski M.S., Collins F.S.;
RT "cDNA cloning of the type 1 neurofibromatosis gene: complete sequence of
RT the NF1 gene product.";
RL Genomics 11:931-940(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND ALTERNATIVE SPLICING.
RC TISSUE=Placenta;
RX PubMed=1339276; DOI=10.1016/0006-291x(92)91294-z;
RA Suzuki H., Takahashi K., Kubota Y., Shibahara S.;
RT "Molecular cloning of a cDNA coding for neurofibromatosis type 1 protein
RT isoform lacking the domain related to ras GTPase-activating protein.";
RL Biochem. Biophys. Res. Commun. 187:984-990(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RC TISSUE=Kidney;
RX PubMed=7570581; DOI=10.1620/tjem.175.225;
RA Suzuki H., Takahashi K., Shibahara S.;
RT "Evidence for the presence of two amino-terminal isoforms of neurofibromin,
RT a gene product responsible for neurofibromatosis type 1.";
RL Tohoku J. Exp. Med. 175:225-233(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-80; LEU-678; HIS-1422
RP AND LEU-2511.
RG NIEHS SNPs program;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 335-2839 (ISOFORM I), AND
RP VARIANT NF1 PRO-1953.
RX PubMed=2114220; DOI=10.1016/0092-8674(90)90253-b;
RA Cawthon R.M., Weiss R., Xu G., Viskochil D., Culver M., Stevens J.,
RA Robertson M., Dunn D., Gesteland R., O'Connell P., White R.;
RT "A major segment of the neurofibromatosis type 1 gene: cDNA sequence,
RT genomic structure, and point mutations.";
RL Cell 62:193-201(1990).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 335-2839 (ISOFORMS I AND 6).
RX PubMed=2116237; DOI=10.1016/0092-8674(90)90024-9;
RA Xu G., O'Connell P., Viskochil D., Cawthon R.M., Robertson M., Culver M.,
RA Dunn D., Stevens J., Gesteland R., White R., Weiss R.;
RT "The neurofibromatosis type 1 gene encodes a protein related to GAP.";
RL Cell 62:599-608(1990).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 707-782.
RX PubMed=9002664; DOI=10.1093/hmg/6.1.9;
RA Regnier V., Meddeb M., Lecointre G., Richard F., Duverger A., Nguyen V.C.,
RA Dutrillaux B., Bernheim A., Danglot G.;
RT "Emergence and scattering of multiple neurofibromatosis (NF1)-related
RT sequences during hominoid evolution suggest a process of pericentromeric
RT interchromosomal transposition.";
RL Hum. Mol. Genet. 6:9-16(1997).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 751-1611 (ISOFORMS I AND II).
RX PubMed=7774960; DOI=10.1016/0888-7543(95)80104-t;
RA Li Y., O'Connell P., Breidenbach H.H., Cawthon R.M., Stevens J., Xu G.,
RA Neil S., Robertson M., White R., Viskochil D.;
RT "Genomic organization of the neurofibromatosis 1 gene (NF1).";
RL Genomics 25:9-18(1995).
RN [14]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1090-1598 (ISOFORM 4).
RX PubMed=2121370; DOI=10.1016/0092-8674(90)90150-d;
RA Martin G.A., Viskochil D., Bollag G., McCabe P.C., Crosier W.J.,
RA Haubruck H., Conroy L., Clark R., O'Connell P., Cawthon R.M., Innis M.,
RA McCormick F.;
RT "The GAP-related domain of the neurofibromatosis type 1 gene product
RT interacts with ras p21.";
RL Cell 63:843-849(1990).
RN [15]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1168-1566 (ISOFORMS I AND II).
RX PubMed=1923522;
RA Nishi T., Lee P.S., Oka K., Levin V.A., Tanase S., Morino Y., Saya H.;
RT "Differential expression of two types of the neurofibromatosis type 1 (NF1)
RT gene transcripts related to neuronal differentiation.";
RL Oncogene 6:1555-1559(1991).
RN [16]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1371-1391 (ISOFORM II), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=8417346; DOI=10.1128/mcb.13.1.487-495.1993;
RA Andersen L.B., Ballester R., Marchuk D.A., Chang E., Gutmann D.H.,
RA Saulino A.M., Camonis J., Wigler M., Collins F.S.;
RT "A conserved alternative splice in the von Recklinghausen neurofibromatosis
RT (NF1) gene produces two neurofibromin isoforms, both of which have GTPase-
RT activating protein activity.";
RL Mol. Cell. Biol. 13:487-495(1993).
RN [17]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1371-1391 (ISOFORM II).
RX PubMed=1662505; DOI=10.1016/0006-291x(91)92029-j;
RA Suzuki Y., Suzuki H., Kayama T., Yoshimoto T., Shibahara S.;
RT "Brain tumors predominantly express the neurofibromatosis type 1 gene
RT transcripts containing the 63 base insert in the region coding for GTPase
RT activating protein-related domain.";
RL Biochem. Biophys. Res. Commun. 181:955-961(1991).
RN [18]
RP FUNCTION.
RX PubMed=2121371; DOI=10.1016/0092-8674(90)90151-4;
RA Ballester R., Marchuk D.A., Boguski M.S., Saulino A.M., Letcher R.,
RA Wigler M., Collins F.S.;
RT "The NF1 locus encodes a protein functionally related to mammalian GAP and
RT yeast IRA proteins.";
RL Cell 63:851-859(1990).
RN [19]
RP RNA EDITING.
RX PubMed=8602361; DOI=10.1093/nar/24.3.478;
RA Skuse G.R., Cappione A.J., Sowden M., Metheny L.J., Smith H.C.;
RT "The neurofibromatosis type I messenger RNA undergoes base-modification RNA
RT editing.";
RL Nucleic Acids Res. 24:478-485(1996).
RN [20]
RP RNA EDITING.
RX PubMed=11727199; DOI=10.1086/337952;
RA Mukhopadhyay D., Anant S., Lee R.M., Kennedy S., Viskochil D.,
RA Davidson N.O.;
RT "C-->U editing of neurofibromatosis 1 mRNA occurs in tumors that express
RT both the type II transcript and apobec-1, the catalytic subunit of the
RT apolipoprotein B mRNA-editing enzyme.";
RL Am. J. Hum. Genet. 70:38-50(2002).
RN [21]
RP REVIEW ON VARIANTS.
RX PubMed=7981724; DOI=10.1002/humu.1380040202;
RA Upadhyaya M., Shaw D.J., Harper P.S.;
RT "Molecular basis of neurofibromatosis type 1 (NF1): mutation analysis and
RT polymorphisms in the NF1 gene.";
RL Hum. Mutat. 4:83-101(1994).
RN [22]
RP REVIEW ON VARIANTS.
RX PubMed=8825042; DOI=10.1136/jmg.33.1.2;
RA Shen M.H., Harper P.S., Upadhyaya M.;
RT "Molecular genetics of neurofibromatosis type 1 (NF1).";
RL J. Med. Genet. 33:2-17(1996).
RN [23]
RP SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=14988005; DOI=10.1016/s0014-5793(04)00078-x;
RA Vandenbroucke I., Van Oostveldt P., Coene E., De Paepe A., Messiaen L.;
RT "Neurofibromin is actively transported to the nucleus.";
RL FEBS Lett. 560:98-102(2004).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [25]
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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-864; SER-2188; SER-2515;
RP SER-2521 AND SER-2543, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-864; SER-876 AND SER-2515,
RP AND 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 [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-864 AND SER-2817, AND
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 [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2543 AND SER-2817, AND
RP IDENTIFICATION BY 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 [33]
RP INTERACTION WITH HTR6.
RX PubMed=23027611; DOI=10.1002/emmm.201201410;
RA Meffre J., Chaumont-Dubel S., Mannoury la Cour C., Loiseau F., Watson D.J.,
RA Dekeyne A., Seveno M., Rivet J.M., Gaven F., Deleris P., Herve D.,
RA Fone K.C., Bockaert J., Millan M.J., Marin P.;
RT "5-HT(6) receptor recruitment of mTOR as a mechanism for perturbed
RT cognition in schizophrenia.";
RL EMBO Mol. Med. 4:1043-1056(2012).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-864; SER-876; SER-2188;
RP SER-2515; SER-2521; SER-2523; SER-2543; THR-2565; SER-2597 AND SER-2802,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2543 AND SER-2817, AND
RP IDENTIFICATION BY 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 [36]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1198-1551.
RX PubMed=9687500; DOI=10.1093/emboj/17.15.4313;
RA Scheffzek K., Ahmadian M.R., Wiesmuller L., Kabsch W., Stege P.,
RA Schmitz F., Wittinghofer A.;
RT "Structural analysis of the GAP-related domain from neurofibromin and its
RT implications.";
RL EMBO J. 17:4313-4327(1998).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1581-1837, LIPID-BINDING, DOMAIN,
RP AND MUTAGENESIS OF LYS-1691; ARG-1695; ARG-1769 AND LYS-1771.
RX PubMed=16397625; DOI=10.1038/sj.embor.7400602;
RA D'Angelo I., Welti S., Bonneau F., Scheffzek K.;
RT "A novel bipartite phospholipid-binding module in the neurofibromatosis
RT type 1 protein.";
RL EMBO Rep. 7:174-179(2006).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1566-1837 IN COMPLEX WITH
RP PHOSPHOLIPID, LIPID-BINDING, AND DOMAIN.
RX PubMed=17187824; DOI=10.1016/j.jmb.2006.11.055;
RA Welti S., Fraterman S., D'Angelo I., Wilm M., Scheffzek K.;
RT "The sec14 homology module of neurofibromin binds cellular
RT glycerophospholipids: mass spectrometry and structure of a lipid complex.";
RL J. Mol. Biol. 366:551-562(2007).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 1581-1837 OF VARIANT NF1 VAL-1605
RP AND MUTANT LYS-1771 DEL IN COMPLEX WITH LIPID, CHARACTERIZATION OF VARIANT
RP NF1 VAL-1605, MUTAGENESIS OF LYS-1771, LIPID-BINDING, AND DOMAIN.
RX PubMed=21089070; DOI=10.1002/humu.21405;
RA Welti S., Kuhn S., D'Angelo I., Brugger B., Kaufmann D., Scheffzek K.;
RT "Structural and biochemical consequences of NF1 associated nontruncating
RT mutations in the Sec14-PH module of neurofibromin.";
RL Hum. Mutat. 32:191-197(2011).
RN [40]
RP VARIANT GLU-1444.
RX PubMed=1568247; DOI=10.1016/0092-8674(92)90408-5;
RA Li Y., Bollag G., Clark R., Stevens J., Conroy L., Fults D., Ward K.,
RA Friedman E., Samowitz W., Robertson M., Bradley P., McCormick F., White R.,
RA Cawthon R.M.;
RT "Somatic mutations in the neurofibromatosis 1 gene in human tumors.";
RL Cell 69:275-281(1992).
RN [41]
RP VARIANTS NF1 MET-2164 AND ASN-2192.
RX PubMed=1302608; DOI=10.1093/hmg/1.9.735;
RA Upadhyaya M., Shen M.H., Cherryson A., Farnham J., Maynard J., Huson S.M.,
RA Harper P.S.;
RT "Analysis of mutations at the neurofibromatosis 1 (NF1) locus.";
RL Hum. Mol. Genet. 1:735-740(1992).
RN [42]
RP VARIANT GLY-HIS-GLU-GLN-GLN-LYS-LEU-PRO-ALA-ALA-THR-LEU-ALA-LEU-1733 INS.
RX PubMed=8317503;
RA Tassabehji M., Strachan T., Sharland M., Colley A., Donnai D., Harris R.,
RA Thakker N.;
RT "Tandem duplication within a neurofibromatosis type 1 (NF1) gene exon in a
RT family with features of Watson syndrome and Noonan syndrome.";
RL Am. J. Hum. Genet. 53:90-95(1993).
RN [43]
RP VARIANT MET-991 DEL.
RX PubMed=7904209; DOI=10.1093/hmg/2.11.1861;
RA Shen M.H., Harper P.S., Upadhyaya M.;
RT "Neurofibromatosis type 1 (NF1): the search for mutations by PCR-
RT heteroduplex analysis on Hydrolink gels.";
RL Hum. Mol. Genet. 2:1861-1864(1993).
RN [44]
RP VARIANTS NF1 ASP-1166 AND ARG-1440.
RX PubMed=7981679; DOI=10.1093/hmg/3.7.1109;
RA Purandare S.M., Lanyon W.G., Connor J.M.;
RT "Characterisation of inherited and sporadic mutations in neurofibromatosis
RT type-1.";
RL Hum. Mol. Genet. 3:1109-1115(1994).
RN [45]
RP VARIANT NF1 2387-ASN-PHE-2388 DEL.
RX PubMed=8081387; DOI=10.1002/humu.1380030404;
RA Abernathy C.R., Colman S.D., Kousseff B.G., Wallace M.R.;
RT "Two NF1 mutations: frameshift in the GAP-related domain, and loss of two
RT codons toward the 3' end of the gene.";
RL Hum. Mutat. 3:347-352(1994).
RN [46]
RP VARIANT NF1 ALA-2631.
RX PubMed=8544190; DOI=10.1136/jmg.32.9.706;
RA Upadhyaya M., Maynard J., Osborn M.J., Huson S.M., Ponder M.,
RA Ponder B.A.J., Harper P.S.;
RT "Characterisation of germline mutations in the neurofibromatosis type 1
RT (NF1) gene.";
RL J. Med. Genet. 32:706-710(1995).
RN [47]
RP VARIANT NF1 ARG-629.
RX PubMed=8834249; DOI=10.1007/bf02267073;
RA Gasparini P., D'Agruma L., de Cillis G.P., Balestrazzi P., Mingarelli R.,
RA Zelante L.;
RT "Scanning the first part of the neurofibromatosis type 1 gene by RNA-SSCP:
RT identification of three novel mutations and of two new polymorphisms.";
RL Hum. Genet. 97:492-495(1996).
RN [48]
RP VARIANT NF1 ARG-1035.
RX PubMed=8807336;
RX DOI=10.1002/(sici)1098-1004(1996)8:1<51::aid-humu7>3.0.co;2-s;
RA Wu R., Legius E., Robberecht W., Dumoulin M., Cassiman J.-J., Fryns J.-P.;
RT "Neurofibromatosis type I gene mutation in a patient with features of
RT LEOPARD syndrome.";
RL Hum. Mutat. 8:51-56(1996).
RN [49]
RP VARIANTS NF1 SER-1412; GLN-1440; GLU-1444 AND GLY-1489.
RX PubMed=9003501; DOI=10.1007/s004390050317;
RA Upadhyaya M., Osborn M.J., Maynard J., Kim M.R., Tamanoi F., Cooper D.N.;
RT "Mutational and functional analysis of the neurofibromatosis type 1 (NF1)
RT gene.";
RL Hum. Genet. 99:88-92(1997).
RN [50]
RP VARIANTS NF1 ARG-844 AND PRO-898.
RX PubMed=9150739; DOI=10.1007/s004390050427;
RA Maynard J., Krawczak M., Upadhyaya M.;
RT "Characterization and significance of nine novel mutations in exon 16 of
RT the neurofibromatosis type 1 (NF1) gene.";
RL Hum. Genet. 99:674-676(1997).
RN [51]
RP VARIANT NF1 ARG-1952.
RX PubMed=9101300;
RX DOI=10.1002/(sici)1098-1004(1997)9:4<366::aid-humu12>3.0.co;2-0;
RA Hudson J., Wu C.L., Tassabehji M., Summers E.M., Simon S., Super M.,
RA Donnai D., Thakker N.;
RT "Novel and recurrent mutations in the neurofibromatosis type 1 (NF1)
RT gene.";
RL Hum. Mutat. 9:366-367(1997).
RN [52]
RP VARIANTS NF1 GLY-338 AND TRP-1611.
RX PubMed=9298829;
RX DOI=10.1002/(sici)1098-1004(1997)10:3<248::aid-humu14>3.0.co;2-#;
RA Upadhyaya M., Maynard J., Osborn M.J., Harper P.S.;
RT "Six novel mutations in the neurofibromatosis type 1 (NF1) gene.";
RL Hum. Mutat. 10:248-250(1997).
RN [53]
RP VARIANT NF1 PRO-1276.
RX PubMed=9668168; DOI=10.1093/hmg/7.8.1261;
RA Klose A., Ahmadian M.R., Schuelke M., Scheffzek K., Hoffmeyer S.,
RA Gewies A., Schmitz F., Kaufmann D., Peters H., Wittinghofer A.,
RA Nuernberg P.;
RT "Selective disactivation of neurofibromin GAP activity in neurofibromatosis
RT type 1 (NF1).";
RL Hum. Mol. Genet. 7:1261-1268(1998).
RN [54]
RP VARIANTS NF1 HIS-765 AND GLY-1204.
RX PubMed=10336779;
RX DOI=10.1002/(sici)1098-1004(1998)11:5<411::aid-humu11>3.0.co;2-2;
RA Krkljus S., Abernathy C.R., Johnson J.S., Williams C.A., Driscoll D.J.,
RA Zori R., Stalker H.J., Rasmussen S.A., Collins F.S., Kousseff B.G.,
RA Baumbach L., Wallace M.R.;
RT "Analysis of CpG C-to-T mutations in neurofibromatosis type 1.";
RL Hum. Mutat. 11:411-411(1998).
RN [55]
RP VARIANT NF1 PRO-508.
RX PubMed=11258625; DOI=10.1097/00125817-199909000-00002;
RA Messiaen L.M., Callens T., Roux K.J., Mortier G.R., De Paepe A.,
RA Abramowicz M., Pericak-Vance M.A., Vance J.M., Wallace M.R.;
RT "Exon 10b of the NF1 gene represents a mutational hotspot and harbors a
RT recurrent missense mutation Y489C associated with aberrant splicing.";
RL Genet. Med. 1:248-253(1999).
RN [56]
RP VARIANT NF1 PRO-1446.
RX PubMed=10220149;
RX DOI=10.1002/(sici)1098-1004(1999)13:4<337::aid-humu12>3.0.co;2-f;
RA Peters H., Hess D., Fahsold R., Schuelke M.;
RT "A novel mutation L1425P in the GAP-region of the NF1 gene detected by
RT temperature gradient gel electrophoresis (TGGE).";
RL Hum. Mutat. 13:337-337(1999).
RN [57]
RP VARIANTS NF1 PRO-216; PRO-357; CYS-491; PRO-549; THR-581; ARG-583; PHE-665;
RP PRO-695; PRO-763; SER-777; LYS-780; PRO-781; PRO-847; SER-1156; PRO-1250;
RP GLN-1276; PRO-1276; PRO-1446; VAL-1605 AND ILE-2507, AND VARIANT GLU-176.
RX PubMed=10712197; DOI=10.1086/302809;
RA Fahsold R., Hoffmeyer S., Mischung C., Gille C., Ehlers C.,
RA Kuecuekceylan N., Abdel-Nour M., Gewies A., Peters H., Kaufmann D.,
RA Buske A., Tinschert S., Nuernberg P.;
RT "Minor lesion mutational spectrum of the entire NF1 gene does not explain
RT its high mutability but points to a functional domain upstream of the GAP-
RT related domain.";
RL Am. J. Hum. Genet. 66:790-818(2000).
RN [58]
RP VARIANTS NF1 SER-117; TRP-1204; PRO-1446 AND 2387-ASN-PHE-2388 DEL.
RX PubMed=10607834; DOI=10.1093/hmg/9.2.237;
RA Ars E., Serra E., Garcia J., Kruyer H., Gaona A., Lazaro C., Estivill X.;
RT "Mutations affecting mRNA splicing are the most common molecular defects in
RT patients with neurofibromatosis type 1.";
RL Hum. Mol. Genet. 9:237-247(2000).
RN [59]
RP ERRATUM OF PUBMED:10607834.
RA Ars E., Serra E., Garcia J., Kruyer H., Gaona A., Lazaro C., Estivill X.;
RL Hum. Mol. Genet. 9:659-659(2000).
RN [60]
RP VARIANT NF1 PHE-844.
RX PubMed=10980545;
RX DOI=10.1002/1098-1004(200009)16:3<274::aid-humu21>3.3.co;2-6;
RA Boulandet E.G., Pantel J., Cazeneuve C., Van Gijn M., Vidaud D., Lemay S.,
RA Martin J., Zeller J., Revuz J., Goossens M., Amselem S., Wolkenstein P.;
RT "NF1 gene analysis focused on CpG-rich exons in a cohort of 93 patients
RT with neurofibromatosis type 1.";
RL Hum. Mutat. 16:274-275(2000).
RN [61]
RP VARIANT SPINAL FSNF PRO-2088.
RX PubMed=11704931; DOI=10.1086/324648;
RA Kaufmann D., Mueller R., Bartelt B., Wolf M., Kunzi-Rapp K., Hanemann C.O.,
RA Fahsold R., Hein C., Vogel W., Assum G.;
RT "Spinal neurofibromatosis without cafe-au-lait macules in two families with
RT null mutations of the NF1 gene.";
RL Am. J. Hum. Genet. 69:1395-1400(2001).
RN [62]
RP VARIANTS NF1 LYS-780; CYS-784; PRO-1147; CYS-1193; ARG-1444; SER-1785;
RP ASN-2012 AND LYS-2357.
RX PubMed=11735023; DOI=10.1007/s004390100594;
RA Han S.S., Cooper D.N., Upadhyaya M.N.;
RT "Evaluation of denaturing high performance liquid chromatography (DHPLC)
RT for the mutational analysis of the neurofibromatosis type 1 (NF1) gene.";
RL Hum. Genet. 109:487-497(2001).
RN [63]
RP VARIANTS NF1 PHE-82; ARG-784 AND GLU-1444.
RX PubMed=11857752; DOI=10.1002/humu.9018;
RA Kluwe L., Friedrich R.E., Korf B., Fahsold R., Mautner V.-F.;
RT "NF1 mutations in neurofibromatosis 1 patients with plexiform
RT neurofibromas.";
RL Hum. Mutat. 19:309-309(2002).
RN [64]
RP VARIANT NFNS GLU-1459 DEL.
RX PubMed=12707950; DOI=10.1002/ajmg.a.20023;
RA Baralle D., Mattocks C., Kalidas K., Elmslie F., Whittaker J., Lees M.,
RA Ragge N., Patton M.A., Winter R.M., ffrench-Constant C.;
RT "Different mutations in the NF1 gene are associated with neurofibromatosis-
RT Noonan syndrome (NFNS).";
RL Am. J. Med. Genet. A 119:1-8(2003).
RN [65]
RP VARIANTS NF1 TYR-93; VAL-604; ARG-844 AND PRO-898, AND VARIANTS ASP-74;
RP GLU-176; ARG-712 AND GLN-1276.
RX PubMed=12522551; DOI=10.1007/s00439-002-0858-4;
RA Wang Q., Montmain G., Ruano E., Upadhyaya M., Dudley S., Liskay R.M.,
RA Thibodeau S.N., Puisieux A.;
RT "Neurofibromatosis type 1 gene as a mutational target in a mismatch repair-
RT deficient cell type.";
RL Hum. Genet. 112:117-123(2003).
RN [66]
RP VARIANTS NF1 LYS-780; PRO-847; GLU-848 AND ARG-968; ASN-1444; LEU-1953 DEL
RP AND ARG-2001.
RX PubMed=12552569; DOI=10.1002/humu.9111;
RA De Luca A., Buccino A., Gianni D., Mangino M., Giustini S., Richetta A.,
RA Divona L., Calvieri S., Mingarelli R., Dallapiccola B.;
RT "NF1 gene analysis based on DHPLC.";
RL Hum. Mutat. 21:171-172(2003).
RN [67]
RP VARIANTS NF1 ARG-578; PRO-920 AND ALA-2221.
RX PubMed=12746402; DOI=10.1136/jmg.40.5.368;
RA Kluwe L., Tatagiba M., Fuensterer C., Mautner V.F.;
RT "NF1 mutations and clinical spectrum in patients with spinal
RT neurofibromas.";
RL J. Med. Genet. 40:368-371(2003).
RN [68]
RP VARIANT NF1 VAL-186, AND CHARACTERIZATION OF VARIANT NF1 VAL-186.
RX PubMed=15523642; DOI=10.1002/humu.20103;
RA Zatkova A., Messiaen L., Vandenbroucke I., Wieser R., Fonatsch C.,
RA Krainer A.R., Wimmer K.;
RT "Disruption of exonic splicing enhancer elements is the principal cause of
RT exon skipping associated with seven nonsense or missense alleles of NF1.";
RL Hum. Mutat. 24:491-501(2004).
RN [69]
RP VARIANTS NF1 ASN-157; ARG-629; SER-777; LYS-780; ARG-784; PRO-847; GLU-848;
RP ARG-968; ASN-1444; LEU-1953 DEL AND ARG-2001, AND VARIANT GLU-176.
RX PubMed=15146469; DOI=10.1002/humu.9245;
RA De Luca A., Schirinzi A., Buccino A., Bottillo I., Sinibaldi L.,
RA Torrente I., Ciavarella A., Dottorini T., Porciello R., Giustini S.,
RA Calvieri S., Dallapiccola B.;
RT "Novel and recurrent mutations in the NF1 gene in Italian patients with
RT neurofibromatosis type 1.";
RL Hum. Mutat. 23:629-629(2004).
RN [70]
RP VARIANTS NF1 ARG-31; PRO-145; ARG-324; VAL-337; CYS-489; PRO-532; ARG-574;
RP ARG-629; PHE-665; PHE-844; PRO-844; MET-991 DEL; VAL-1073; ARG-1196;
RP GLY-1276; GLN-1276; GLU-1430; GLU-1459 DEL AND GLY-1489, AND VARIANTS
RP GLU-176 AND CYS-873.
RX PubMed=15060124; DOI=10.1136/jmg.2003.011890;
RA Mattocks C., Baralle D., Tarpey P., ffrench-Constant C., Bobrow M.,
RA Whittaker J.;
RT "Automated comparative sequence analysis identifies mutations in 89% of NF1
RT patients and confirms a mutation cluster in exons 11-17 distinct from the
RT GAP related domain.";
RL J. Med. Genet. 41:E48-E48(2004).
RN [71]
RP VARIANT NF1 PRO-1243.
RX PubMed=15520408; DOI=10.1136/jmg.2004.021683;
RA Ferner R.E., Hughes R.A.C., Hall S.M., Upadhyaya M., Johnson M.R.;
RT "Neurofibromatous neuropathy in neurofibromatosis 1 (NF1).";
RL J. Med. Genet. 41:837-841(2004).
RN [72]
RP VARIANT NF1 ARG-844.
RX PubMed=15948193; DOI=10.1002/ajmg.a.30813;
RA Bertola D.R., Pereira A.C., Passetti F., de Oliveira P.S.L., Messiaen L.,
RA Gelb B.D., Kim C.A., Krieger J.E.;
RT "Neurofibromatosis-Noonan syndrome: molecular evidence of the concurrence
RT of both disorders in a patient.";
RL Am. J. Med. Genet. A 136:242-245(2005).
RN [73]
RP VARIANTS NFNS ARG-194; GLU-1444; THR-1451; LEU-1453 AND GLU-1459 DEL.
RX PubMed=16380919; DOI=10.1086/498454;
RA De Luca A., Bottillo I., Sarkozy A., Carta C., Neri C., Bellacchio E.,
RA Schirinzi A., Conti E., Zampino G., Battaglia A., Majore S., Rinaldi M.M.,
RA Carella M., Marino B., Pizzuti A., Digilio M.C., Tartaglia M.,
RA Dallapiccola B.;
RT "NF1 gene mutations represent the major molecular event underlying
RT neurofibromatosis-Noonan syndrome.";
RL Am. J. Hum. Genet. 77:1092-1101(2005).
RN [74]
RP VARIANTS [LARGE SCALE ANALYSIS] ILE-1187; LEU-1951 AND ARG-2745.
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 [75]
RP VARIANT NF1 MET-991 DEL.
RX PubMed=17160901; DOI=10.1086/510781;
RA Upadhyaya M., Huson S.M., Davies M., Thomas N., Chuzhanova N.,
RA Giovannini S., Evans D.G., Howard E., Kerr B., Griffiths S., Consoli C.,
RA Side L., Adams D., Pierpont M., Hachen R., Barnicoat A., Li H., Wallace P.,
RA Van Biervliet J.P., Stevenson D., Viskochil D., Baralle D., Haan E.,
RA Riccardi V., Turnpenny P., Lazaro C., Messiaen L.;
RT "An absence of cutaneous neurofibromas associated with a 3-bp inframe
RT deletion in exon 17 of the NF1 gene (c.2970-2972 delAAT): evidence of a
RT clinically significant NF1 genotype-phenotype correlation.";
RL Am. J. Hum. Genet. 80:140-151(2007).
RN [76]
RP VARIANT NFNS PHE-1411.
RX PubMed=19845691; DOI=10.1111/j.1399-0004.2009.01233.x;
RA Nystrom A.M., Ekvall S., Allanson J., Edeby C., Elinder M., Holmstrom G.,
RA Bondeson M.L., Anneren G.;
RT "Noonan syndrome and neurofibromatosis type I in a family with a novel
RT mutation in NF1.";
RL Clin. Genet. 76:524-534(2009).
RN [77]
RP VARIANT NF1 THR-160.
RX PubMed=21838856; DOI=10.1186/1897-4287-9-6;
RA Ponti G., Losi L., Martorana D., Priola M., Boni E., Pollio A., Neri T.M.,
RA Seidenari S.;
RT "Clinico-pathological and biomolecular findings in Italian patients with
RT multiple cutaneous neurofibromas.";
RL Hered. Cancer Clin. Pract. 9:6-6(2011).
RN [78]
RP VARIANTS GLU-176; THR-330; ASP-393; LEU-393; PRO-519; THR-776 AND PHE-1484.
RX PubMed=22108604; DOI=10.1038/ejhg.2011.207;
RA Thomas L., Spurlock G., Eudall C., Thomas N.S., Mort M., Hamby S.E.,
RA Chuzhanova N., Brems H., Legius E., Cooper D.N., Upadhyaya M.;
RT "Exploring the somatic NF1 mutational spectrum associated with NF1
RT cutaneous neurofibromas.";
RL Eur. J. Hum. Genet. 20:411-419(2012).
RN [79]
RP VARIANTS NF1 TRP-93; ARG-1048; ARG-1189; ARG-1661 (ISOFORM I) AND THR-1918
RP (ISOFORM I).
RX PubMed=23758643; DOI=10.1111/ahg.12026;
RA Nemethova M., Bolcekova A., Ilencikova D., Durovcikova D., Hlinkova K.,
RA Hlavata A., Kovacs L., Kadasi L., Zatkova A.;
RT "Thirty-nine novel neurofibromatosis 1 (NF1) gene mutations identified in
RT Slovak patients.";
RL Ann. Hum. Genet. 77:364-379(2013).
RN [80]
RP VARIANT NF1 PRO-2125.
RX PubMed=24413922; DOI=10.1007/s00381-013-2352-9;
RA Ben-Salem S., Al-Shamsi A.M., Ali B.R., Al-Gazali L.;
RT "The mutational spectrum of the NF1 gene in neurofibromatosis type I
RT patients from UAE.";
RL Childs Nerv. Syst. 30:1183-1189(2014).
CC -!- FUNCTION: Stimulates the GTPase activity of Ras. NF1 shows greater
CC affinity for Ras GAP, but lower specific activity. May be a regulator
CC of Ras activity. {ECO:0000269|PubMed:2121371,
CC ECO:0000269|PubMed:8417346}.
CC -!- SUBUNIT: Interacts with HTR6 (PubMed:23027611).
CC {ECO:0000269|PubMed:23027611}.
CC -!- INTERACTION:
CC P21359; P05067: APP; NbExp=3; IntAct=EBI-1172917, EBI-77613;
CC P21359; P01112: HRAS; NbExp=3; IntAct=EBI-1172917, EBI-350145;
CC P21359; P34741: SDC2; NbExp=4; IntAct=EBI-1172917, EBI-1172957;
CC P21359; Q7Z699: SPRED1; NbExp=6; IntAct=EBI-1172917, EBI-5235340;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14988005}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:14988005}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=II {ECO:0000303|PubMed:1923522};
CC IsoId=P21359-1; Sequence=Displayed;
CC Name=I {ECO:0000303|PubMed:1923522};
CC IsoId=P21359-2; Sequence=VSP_001628;
CC Name=3;
CC IsoId=P21359-3; Sequence=VSP_001629, VSP_001630;
CC Name=4;
CC IsoId=P21359-4; Sequence=VSP_001631, VSP_001632;
CC Name=5;
CC IsoId=P21359-5; Sequence=VSP_043467, VSP_043468;
CC Name=6;
CC IsoId=P21359-6; Sequence=VSP_001628, VSP_053587;
CC -!- TISSUE SPECIFICITY: Detected in brain, peripheral nerve, lung, colon
CC and muscle. {ECO:0000269|PubMed:8417346}.
CC -!- DOMAIN: Binds phospholipids via its C-terminal CRAL-TRIO domain. Binds
CC primarily glycerophospholipids with monounsaturated C18:1 and/or C16:1
CC fatty acid moieties and a phosphatidylethanolamine or
CC phosphatidylcholine headgroup. Has lesser affinity for lipids
CC containing phosphatidylserine and phosphatidylinositol.
CC {ECO:0000269|PubMed:16397625, ECO:0000269|PubMed:17187824,
CC ECO:0000269|PubMed:21089070}.
CC -!- RNA EDITING: Modified_positions=1306 {ECO:0000269|PubMed:11727199,
CC ECO:0000269|PubMed:8602361}; Note=The stop codon (UGA) at position 1306
CC is created by RNA editing. Various levels of RNA editing occurs in
CC peripheral nerve-sheath tumor samples (PNSTs) from patients with NF1.
CC Preferentially observed in transcripts containing exon 23A.;
CC -!- DISEASE: Neurofibromatosis 1 (NF1) [MIM:162200]: A disease
CC characterized by patches of skin pigmentation (cafe-au-lait spots),
CC Lisch nodules of the iris, tumors in the peripheral nervous system and
CC fibromatous skin tumors. Individuals with the disorder have increased
CC susceptibility to the development of benign and malignant tumors.
CC {ECO:0000269|PubMed:10220149, ECO:0000269|PubMed:10336779,
CC ECO:0000269|PubMed:10607834, ECO:0000269|PubMed:10712197,
CC ECO:0000269|PubMed:10980545, ECO:0000269|PubMed:11258625,
CC ECO:0000269|PubMed:11735023, ECO:0000269|PubMed:11857752,
CC ECO:0000269|PubMed:12522551, ECO:0000269|PubMed:12552569,
CC ECO:0000269|PubMed:12746402, ECO:0000269|PubMed:1302608,
CC ECO:0000269|PubMed:15060124, ECO:0000269|PubMed:15146469,
CC ECO:0000269|PubMed:15520408, ECO:0000269|PubMed:15523642,
CC ECO:0000269|PubMed:15948193, ECO:0000269|PubMed:17160901,
CC ECO:0000269|PubMed:21089070, ECO:0000269|PubMed:2114220,
CC ECO:0000269|PubMed:21838856, ECO:0000269|PubMed:23758643,
CC ECO:0000269|PubMed:24413922, ECO:0000269|PubMed:7981679,
CC ECO:0000269|PubMed:8081387, ECO:0000269|PubMed:8544190,
CC ECO:0000269|PubMed:8807336, ECO:0000269|PubMed:8834249,
CC ECO:0000269|PubMed:9003501, ECO:0000269|PubMed:9101300,
CC ECO:0000269|PubMed:9150739, ECO:0000269|PubMed:9298829,
CC ECO:0000269|PubMed:9668168}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An
CC aggressive pediatric myelodysplastic syndrome/myeloproliferative
CC disorder characterized by malignant transformation in the hematopoietic
CC stem cell compartment with proliferation of differentiated progeny.
CC Patients have splenomegaly, enlarged lymph nodes, rashes, and
CC hemorrhages. Note=The disease is caused by variants affecting the gene
CC represented in this entry.
CC -!- DISEASE: Watson syndrome (WTSN) [MIM:193520]: A syndrome characterized
CC by the presence of pulmonary stenosis, cafe-au-lait spots, and
CC intellectual disability. It is considered as an atypical form of
CC neurofibromatosis. Note=The disease is caused by variants affecting the
CC gene represented in this entry.
CC -!- DISEASE: Familial spinal neurofibromatosis (FSNF) [MIM:162210]:
CC Considered to be an alternative form of neurofibromatosis, showing
CC multiple spinal tumors. {ECO:0000269|PubMed:11704931}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Neurofibromatosis-Noonan syndrome (NFNS) [MIM:601321]:
CC Characterized by manifestations of both NF1 and Noonan syndrome (NS).
CC NS is a disorder characterized by dysmorphic facial features, short
CC stature, hypertelorism, cardiac anomalies, deafness, motor delay, and a
CC bleeding diathesis. {ECO:0000269|PubMed:12707950,
CC ECO:0000269|PubMed:16380919, ECO:0000269|PubMed:19845691}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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. Note=The gene represented in this entry may be
CC involved in disease pathogenesis.
CC -!- CAUTION: Was originally thought to be associated with LEOPARD (LS), an
CC autosomal dominant syndrome. {ECO:0000305|PubMed:8807336}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA59923.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/NF1ID134.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/nf1/";
CC -!- WEB RESOURCE: Name=Mendelian genes neurofibromin 1 (NF1); Note=Leiden
CC Open Variation Database (LOVD);
CC URL="https://databases.lovd.nl/shared/genes/NF1";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M89914; AAA59925.1; -; mRNA.
DR EMBL; M82814; AAA59924.1; -; mRNA.
DR EMBL; M60496; AAA59928.1; -; mRNA.
DR EMBL; D12625; BAA02150.1; -; mRNA.
DR EMBL; M38106; AAA74897.1; -; mRNA.
DR EMBL; M38107; AAB59558.1; -; mRNA.
DR EMBL; D42072; BAA07669.1; -; mRNA.
DR EMBL; AY796305; AAV50004.1; -; Genomic_DNA.
DR EMBL; AC004222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC134669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC135724; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC138207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC139072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471147; EAW80272.1; -; Genomic_DNA.
DR EMBL; CH471147; EAW80275.1; -; Genomic_DNA.
DR EMBL; AH000834; AAA18483.1; -; Genomic_DNA.
DR EMBL; Y07853; CAA69179.1; -; Genomic_DNA.
DR EMBL; U17690; AAB48380.1; -; Genomic_DNA.
DR EMBL; U17680; AAB48380.1; JOINED; Genomic_DNA.
DR EMBL; U17681; AAB48380.1; JOINED; Genomic_DNA.
DR EMBL; U17682; AAB48380.1; JOINED; Genomic_DNA.
DR EMBL; U17683; AAB48380.1; JOINED; Genomic_DNA.
DR EMBL; U17684; AAB48380.1; JOINED; Genomic_DNA.
DR EMBL; U17685; AAB48380.1; JOINED; Genomic_DNA.
DR EMBL; U17686; AAB48380.1; JOINED; Genomic_DNA.
DR EMBL; U17687; AAB48380.1; JOINED; Genomic_DNA.
DR EMBL; U17688; AAB48380.1; JOINED; Genomic_DNA.
DR EMBL; U17689; AAB48380.1; JOINED; Genomic_DNA.
DR EMBL; U17690; AAB48379.1; -; Genomic_DNA.
DR EMBL; U17680; AAB48379.1; JOINED; Genomic_DNA.
DR EMBL; U17681; AAB48379.1; JOINED; Genomic_DNA.
DR EMBL; U17682; AAB48379.1; JOINED; Genomic_DNA.
DR EMBL; U17683; AAB48379.1; JOINED; Genomic_DNA.
DR EMBL; U17684; AAB48379.1; JOINED; Genomic_DNA.
DR EMBL; U17685; AAB48379.1; JOINED; Genomic_DNA.
DR EMBL; U17687; AAB48379.1; JOINED; Genomic_DNA.
DR EMBL; U17688; AAB48379.1; JOINED; Genomic_DNA.
DR EMBL; U17689; AAB48379.1; JOINED; Genomic_DNA.
DR EMBL; U17656; AAB48373.1; -; Genomic_DNA.
DR EMBL; U17659; AAB48374.1; -; Genomic_DNA.
DR EMBL; U17662; AAB48375.1; -; Genomic_DNA.
DR EMBL; U17668; AAB48376.1; -; Genomic_DNA.
DR EMBL; U17667; AAB48376.1; JOINED; Genomic_DNA.
DR EMBL; U17673; AAB48377.1; -; Genomic_DNA.
DR EMBL; U17677; AAB48378.1; -; Genomic_DNA.
DR EMBL; U17676; AAB48378.1; JOINED; Genomic_DNA.
DR EMBL; M60915; AAA59921.1; -; mRNA.
DR EMBL; M60915; AAA59922.1; -; mRNA.
DR EMBL; M61213; AAA59923.1; ALT_INIT; mRNA.
DR EMBL; S51751; AAB24636.1; -; mRNA.
DR EMBL; D10490; BAA01371.1; -; mRNA.
DR CCDS; CCDS11264.1; -. [P21359-2]
DR CCDS; CCDS42292.1; -. [P21359-1]
DR CCDS; CCDS45645.1; -. [P21359-5]
DR PIR; B55282; B55282.
DR PIR; I78852; I78852.
DR RefSeq; NP_000258.1; NM_000267.3. [P21359-2]
DR RefSeq; NP_001035957.1; NM_001042492.2. [P21359-1]
DR RefSeq; NP_001121619.1; NM_001128147.2. [P21359-5]
DR PDB; 1NF1; X-ray; 2.50 A; A=1198-1551.
DR PDB; 2D4Q; X-ray; 2.30 A; A/B=1581-1837.
DR PDB; 2E2X; X-ray; 2.50 A; A/B=1566-1837.
DR PDB; 3P7Z; X-ray; 2.65 A; A/B=1566-1837.
DR PDB; 3PEG; X-ray; 2.52 A; A=1566-1837.
DR PDB; 3PG7; X-ray; 2.19 A; A/B=1581-1837.
DR PDB; 6OB2; X-ray; 2.85 A; B/D=1209-1484.
DR PDB; 6OB3; X-ray; 2.10 A; B/D=1209-1484.
DR PDB; 6V65; X-ray; 2.76 A; B=1203-1551.
DR PDB; 6V6F; X-ray; 2.54 A; B=1203-1551.
DR PDB; 7MOC; EM; 4.56 A; A/B=2-2839.
DR PDB; 7MP5; EM; 5.60 A; A/B=2-2839.
DR PDB; 7MP6; EM; 6.25 A; A/B=2-2839.
DR PDB; 7PGR; EM; 4.00 A; F/N=1-2839.
DR PDB; 7PGS; EM; 3.40 A; F/N=1-2839.
DR PDB; 7PGT; EM; 4.80 A; F/N=1-2839.
DR PDB; 7PGU; EM; 3.30 A; F/N=1-2839.
DR PDB; 7R03; EM; 3.60 A; A/B=1-2839.
DR PDB; 7R04; EM; 3.70 A; A/B=1-2839.
DR PDBsum; 1NF1; -.
DR PDBsum; 2D4Q; -.
DR PDBsum; 2E2X; -.
DR PDBsum; 3P7Z; -.
DR PDBsum; 3PEG; -.
DR PDBsum; 3PG7; -.
DR PDBsum; 6OB2; -.
DR PDBsum; 6OB3; -.
DR PDBsum; 6V65; -.
DR PDBsum; 6V6F; -.
DR PDBsum; 7MOC; -.
DR PDBsum; 7MP5; -.
DR PDBsum; 7MP6; -.
DR PDBsum; 7PGR; -.
DR PDBsum; 7PGS; -.
DR PDBsum; 7PGT; -.
DR PDBsum; 7PGU; -.
DR PDBsum; 7R03; -.
DR PDBsum; 7R04; -.
DR SMR; P21359; -.
DR BioGRID; 110836; 157.
DR IntAct; P21359; 36.
DR MINT; P21359; -.
DR STRING; 9606.ENSP00000351015; -.
DR iPTMnet; P21359; -.
DR PhosphoSitePlus; P21359; -.
DR BioMuta; NF1; -.
DR DMDM; 548350; -.
DR CPTAC; CPTAC-1622; -.
DR EPD; P21359; -.
DR jPOST; P21359; -.
DR MassIVE; P21359; -.
DR MaxQB; P21359; -.
DR PaxDb; P21359; -.
DR PeptideAtlas; P21359; -.
DR PRIDE; P21359; -.
DR ProteomicsDB; 53861; -. [P21359-1]
DR ProteomicsDB; 53862; -. [P21359-2]
DR ProteomicsDB; 53863; -. [P21359-3]
DR ProteomicsDB; 53864; -. [P21359-4]
DR ProteomicsDB; 53865; -. [P21359-5]
DR Antibodypedia; 3471; 487 antibodies from 39 providers.
DR CPTC; P21359; 3 antibodies.
DR DNASU; 4763; -.
DR Ensembl; ENST00000356175.7; ENSP00000348498.3; ENSG00000196712.19. [P21359-2]
DR Ensembl; ENST00000358273.9; ENSP00000351015.4; ENSG00000196712.19. [P21359-1]
DR Ensembl; ENST00000431387.8; ENSP00000412921.4; ENSG00000196712.19. [P21359-5]
DR Ensembl; ENST00000487476.5; ENSP00000491589.1; ENSG00000196712.19. [P21359-3]
DR GeneID; 4763; -.
DR KEGG; hsa:4763; -.
DR MANE-Select; ENST00000358273.9; ENSP00000351015.4; NM_001042492.3; NP_001035957.1.
DR UCSC; uc002hgf.3; human. [P21359-1]
DR CTD; 4763; -.
DR DisGeNET; 4763; -.
DR GeneCards; NF1; -.
DR GeneReviews; NF1; -.
DR HGNC; HGNC:7765; NF1.
DR HPA; ENSG00000196712; Low tissue specificity.
DR MalaCards; NF1; -.
DR MIM; 114500; phenotype.
DR MIM; 162200; phenotype.
DR MIM; 162210; phenotype.
DR MIM; 193520; phenotype.
DR MIM; 601321; phenotype.
DR MIM; 607785; phenotype.
DR MIM; 613113; gene.
DR neXtProt; NX_P21359; -.
DR OpenTargets; ENSG00000196712; -.
DR Orphanet; 97685; 17q11 microdeletion syndrome.
DR Orphanet; 139474; 17q11.2 microduplication syndrome.
DR Orphanet; 29072; Hereditary pheochromocytoma-paraganglioma.
DR Orphanet; 86834; Juvenile myelomonocytic leukemia.
DR Orphanet; 363700; Neurofibromatosis type 1 due to NF1 mutation or intragenic deletion.
DR Orphanet; 638; Neurofibromatosis-Noonan syndrome.
DR PharmGKB; PA31572; -.
DR VEuPathDB; HostDB:ENSG00000196712; -.
DR eggNOG; KOG1826; Eukaryota.
DR GeneTree; ENSGT00550000074797; -.
DR HOGENOM; CLU_036305_0_0_1; -.
DR InParanoid; P21359; -.
DR OMA; WSIDMEA; -.
DR OrthoDB; 9686at2759; -.
DR PhylomeDB; P21359; -.
DR TreeFam; TF300302; -.
DR PathwayCommons; P21359; -.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR Reactome; R-HSA-6802953; RAS signaling downstream of NF1 loss-of-function variants.
DR SignaLink; P21359; -.
DR SIGNOR; P21359; -.
DR BioGRID-ORCS; 4763; 55 hits in 1104 CRISPR screens.
DR ChiTaRS; NF1; human.
DR EvolutionaryTrace; P21359; -.
DR GeneWiki; Neurofibromin_1; -.
DR GenomeRNAi; 4763; -.
DR Pharos; P21359; Tbio.
DR PRO; PR:P21359; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P21359; protein.
DR Bgee; ENSG00000196712; Expressed in colonic epithelium and 200 other tissues.
DR ExpressionAtlas; P21359; baseline and differential.
DR Genevisible; P21359; HS.
DR GO; GO:0030424; C:axon; IDA:HGNC-UCL.
DR GO; GO:0005737; C:cytoplasm; ISS:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IDA:HGNC-UCL.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:HGNC-UCL.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0031210; F:phosphatidylcholine binding; IDA:UniProtKB.
DR GO; GO:0008429; F:phosphatidylethanolamine binding; IDA:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:HGNC-UCL.
DR GO; GO:0030325; P:adrenal gland development; ISS:HGNC-UCL.
DR GO; GO:0021764; P:amygdala development; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0048844; P:artery morphogenesis; ISS:HGNC-UCL.
DR GO; GO:0007420; P:brain development; ISS:HGNC-UCL.
DR GO; GO:0048593; P:camera-type eye morphogenesis; ISS:HGNC-UCL.
DR GO; GO:0007154; P:cell communication; ISS:HGNC-UCL.
DR GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
DR GO; GO:0021987; P:cerebral cortex development; ISS:HGNC-UCL.
DR GO; GO:0050890; P:cognition; IMP:HGNC-UCL.
DR GO; GO:0030199; P:collagen fibril organization; ISS:HGNC-UCL.
DR GO; GO:0001935; P:endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; ISS:HGNC-UCL.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0021897; P:forebrain astrocyte development; ISS:HGNC-UCL.
DR GO; GO:0048853; P:forebrain morphogenesis; ISS:HGNC-UCL.
DR GO; GO:0061534; P:gamma-aminobutyric acid secretion, neurotransmission; IEA:Ensembl.
DR GO; GO:0061535; P:glutamate secretion, neurotransmission; IEA:Ensembl.
DR GO; GO:0048820; P:hair follicle maturation; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; ISS:HGNC-UCL.
DR GO; GO:0001889; P:liver development; ISS:HGNC-UCL.
DR GO; GO:0000165; P:MAPK cascade; ISS:HGNC-UCL.
DR GO; GO:0033024; P:mast cell apoptotic process; IEA:Ensembl.
DR GO; GO:0070662; P:mast cell proliferation; IEA:Ensembl.
DR GO; GO:0001656; P:metanephros development; ISS:HGNC-UCL.
DR GO; GO:0022011; P:myelination in peripheral nervous system; ISS:HGNC-UCL.
DR GO; GO:0097529; P:myeloid leukocyte migration; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0048712; P:negative regulation of astrocyte differentiation; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:MGI.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IMP:HGNC-UCL.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISS:UniProtKB.
DR GO; GO:0002686; P:negative regulation of leukocyte migration; IEA:Ensembl.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:HGNC-UCL.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:MGI.
DR GO; GO:0070667; P:negative regulation of mast cell proliferation; IEA:Ensembl.
DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; ISS:HGNC-UCL.
DR GO; GO:0046929; P:negative regulation of neurotransmitter secretion; IEA:Ensembl.
DR GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; ISS:HGNC-UCL.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; IEA:Ensembl.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:HGNC-UCL.
DR GO; GO:0035021; P:negative regulation of Rac protein signal transduction; IEA:Ensembl.
DR GO; GO:1900148; P:negative regulation of Schwann cell migration; IEA:Ensembl.
DR GO; GO:0010626; P:negative regulation of Schwann cell proliferation; IEA:Ensembl.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IEA:Ensembl.
DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; IEA:Ensembl.
DR GO; GO:0021915; P:neural tube development; IEA:Ensembl.
DR GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0098597; P:observational learning; IEA:Ensembl.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; ISS:HGNC-UCL.
DR GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0007422; P:peripheral nervous system development; ISS:HGNC-UCL.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISS:HGNC-UCL.
DR GO; GO:0043473; P:pigmentation; ISS:HGNC-UCL.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; ISS:HGNC-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:HGNC-UCL.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0033027; P:positive regulation of mast cell apoptotic process; IEA:Ensembl.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:HGNC-UCL.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR GO; GO:0016601; P:Rac protein signal transduction; IEA:Ensembl.
DR GO; GO:0007265; P:Ras protein signal transduction; ISS:HGNC-UCL.
DR GO; GO:0045765; P:regulation of angiogenesis; IMP:HGNC-UCL.
DR GO; GO:0043535; P:regulation of blood vessel endothelial cell migration; IMP:HGNC-UCL.
DR GO; GO:0045124; P:regulation of bone resorption; ISS:HGNC-UCL.
DR GO; GO:0001952; P:regulation of cell-matrix adhesion; ISS:HGNC-UCL.
DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR GO; GO:0045685; P:regulation of glial cell differentiation; ISS:HGNC-UCL.
DR GO; GO:0043087; P:regulation of GTPase activity; IMP:HGNC-UCL.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
DR GO; GO:1900271; P:regulation of long-term synaptic potentiation; IEA:Ensembl.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; ISS:HGNC-UCL.
DR GO; GO:0014044; P:Schwann cell development; ISS:HGNC-UCL.
DR GO; GO:0036135; P:Schwann cell migration; IEA:Ensembl.
DR GO; GO:0014010; P:Schwann cell proliferation; IEA:Ensembl.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR GO; GO:0048745; P:smooth muscle tissue development; ISS:HGNC-UCL.
DR GO; GO:0021510; P:spinal cord development; ISS:HGNC-UCL.
DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR GO; GO:0048485; P:sympathetic nervous system development; ISS:HGNC-UCL.
DR GO; GO:1904738; P:vascular associated smooth muscle cell migration; IEA:Ensembl.
DR GO; GO:1990874; P:vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0008542; P:visual learning; ISS:HGNC-UCL.
DR GO; GO:0042060; P:wound healing; ISS:HGNC-UCL.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 1.10.506.10; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR039360; Ras_GTPase.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR PANTHER; PTHR10194; PTHR10194; 2.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00616; RasGAP; 1.
DR SMART; SM00323; RasGAP; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Disease variant;
KW GTPase activation; Lipid-binding; Nucleus; Phosphoprotein;
KW Reference proteome; RNA editing; Tumor suppressor.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P97526"
FT CHAIN 2..2839
FT /note="Neurofibromin"
FT /id="PRO_0000010773"
FT CHAIN 2..1305
FT /note="Neurofibromin truncated"
FT /id="PRO_0000010774"
FT DOMAIN 1235..1451
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT DOMAIN 1580..1738
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REGION 1580..1837
FT /note="Lipid binding"
FT REGION 2787..2839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2555..2571
FT /note="Bipartite nuclear localization signal"
FT COMPBIAS 2802..2831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P97526"
FT MOD_RES 864
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 876
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04690"
FT MOD_RES 2514
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04690"
FT MOD_RES 2515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 2521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2543
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2565
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2597
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2802
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2817
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 548..551
FT /note="ALLV -> VRGK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:1339276"
FT /id="VSP_001629"
FT VAR_SEQ 552..2839
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:1339276"
FT /id="VSP_001630"
FT VAR_SEQ 574..593
FT /note="SSQMLFYICKKLTSHQMLSS -> RYMYFYFLNSTFKFYFVFLS (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:7570581"
FT /id="VSP_043467"
FT VAR_SEQ 594..2839
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:7570581"
FT /id="VSP_043468"
FT VAR_SEQ 1371..1391
FT /note="Missing (in isoform I and isoform 6)"
FT /evidence="ECO:0000303|PubMed:1457041,
FT ECO:0000303|PubMed:1783401, ECO:0000303|PubMed:1923522,
FT ECO:0000303|PubMed:2114220, ECO:0000303|PubMed:2116237,
FT ECO:0000303|PubMed:2134734"
FT /id="VSP_001628"
FT VAR_SEQ 1591..1598
FT /note="SIFYQAGT -> TPPPEPET (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:2121370"
FT /id="VSP_001631"
FT VAR_SEQ 1599..2839
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:2121370"
FT /id="VSP_001632"
FT VAR_SEQ 2792
FT /note="P -> PASLPCSNSAVFMQLFPHQ (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:2116237"
FT /id="VSP_053587"
FT VARIANT 31
FT /note="H -> R (in NF1; dbSNP:rs199474725)"
FT /evidence="ECO:0000269|PubMed:15060124"
FT /id="VAR_032459"
FT VARIANT 74
FT /note="A -> D (in mismatch repair deficient cancer cells;
FT dbSNP:rs199474726)"
FT /evidence="ECO:0000269|PubMed:12522551"
FT /id="VAR_017550"
FT VARIANT 80
FT /note="Y -> C (in dbSNP:rs4795581)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_022254"
FT VARIANT 80
FT /note="Y -> S (in dbSNP:rs4795581)"
FT /id="VAR_049135"
FT VARIANT 82
FT /note="S -> F (in NF1; dbSNP:rs199474729)"
FT /evidence="ECO:0000269|PubMed:11857752"
FT /id="VAR_021730"
FT VARIANT 93
FT /note="C -> W (in NF1)"
FT /evidence="ECO:0000269|PubMed:23758643"
FT /id="VAR_071668"
FT VARIANT 93
FT /note="C -> Y (in NF1; dbSNP:rs199474728)"
FT /evidence="ECO:0000269|PubMed:12522551"
FT /id="VAR_017551"
FT VARIANT 117
FT /note="I -> S (in NF1; dbSNP:rs199474731)"
FT /evidence="ECO:0000269|PubMed:10607834"
FT /id="VAR_010989"
FT VARIANT 145
FT /note="L -> P (in NF1; dbSNP:rs199474734)"
FT /evidence="ECO:0000269|PubMed:15060124"
FT /id="VAR_032460"
FT VARIANT 157
FT /note="I -> N (in NF1; dbSNP:rs199474744)"
FT /evidence="ECO:0000269|PubMed:15146469"
FT /id="VAR_021731"
FT VARIANT 160
FT /note="R -> T (in NF1; dbSNP:rs199474752)"
FT /evidence="ECO:0000269|PubMed:21838856"
FT /id="VAR_065888"
FT VARIANT 176
FT /note="D -> E (found in mismatch repair deficient cancer
FT cells; also found in a cutaneous neurofibroma from a
FT patient with neurofibromatosis; somatic mutation;
FT dbSNP:rs112306990)"
FT /evidence="ECO:0000269|PubMed:10712197,
FT ECO:0000269|PubMed:12522551, ECO:0000269|PubMed:15060124,
FT ECO:0000269|PubMed:15146469, ECO:0000269|PubMed:22108604"
FT /id="VAR_017552"
FT VARIANT 186
FT /note="D -> V (in NF1; reduced splicing enhancement;
FT dbSNP:rs1567820771)"
FT /evidence="ECO:0000269|PubMed:15523642"
FT /id="VAR_032461"
FT VARIANT 194
FT /note="L -> R (in NFNS; dbSNP:rs199474753)"
FT /evidence="ECO:0000269|PubMed:16380919"
FT /id="VAR_032462"
FT VARIANT 216
FT /note="L -> P (in NF1; dbSNP:rs199474756)"
FT /evidence="ECO:0000269|PubMed:10712197"
FT /id="VAR_021732"
FT VARIANT 324
FT /note="C -> R (in NF1; dbSNP:rs199474735)"
FT /evidence="ECO:0000269|PubMed:15060124"
FT /id="VAR_032463"
FT VARIANT 330
FT /note="A -> T (in a cutaneous neurofibroma from a patient
FT with neurofibromatosis; somatic mutation;
FT dbSNP:rs199474767)"
FT /evidence="ECO:0000269|PubMed:22108604"
FT /id="VAR_067201"
FT VARIANT 337
FT /note="E -> V (in NF1; dbSNP:rs199474736)"
FT /evidence="ECO:0000269|PubMed:15060124"
FT /id="VAR_032464"
FT VARIANT 338
FT /note="D -> G (in NF1; dbSNP:rs199474773)"
FT /evidence="ECO:0000269|PubMed:9298829"
FT /id="VAR_010990"
FT VARIANT 357
FT /note="L -> P (in NF1; dbSNP:rs137854563)"
FT /evidence="ECO:0000269|PubMed:10712197"
FT /id="VAR_021733"
FT VARIANT 393
FT /note="H -> D (in a cutaneous neurofibroma from a patient
FT with neurofibromatosis; somatic mutation;
FT dbSNP:rs199474768)"
FT /evidence="ECO:0000269|PubMed:22108604"
FT /id="VAR_067202"
FT VARIANT 393
FT /note="H -> L (in a cutaneous neurofibroma from a patient
FT with neurofibromatosis; somatic mutation;
FT dbSNP:rs199474769)"
FT /evidence="ECO:0000269|PubMed:22108604"
FT /id="VAR_067203"
FT VARIANT 489
FT /note="Y -> C (in NF1; dbSNP:rs137854557)"
FT /evidence="ECO:0000269|PubMed:15060124"
FT /id="VAR_032465"
FT VARIANT 491
FT /note="Y -> C (in NF1; dbSNP:rs199474757)"
FT /evidence="ECO:0000269|PubMed:10712197"
FT /id="VAR_021734"
FT VARIANT 508
FT /note="L -> P (in NF1; dbSNP:rs137854558)"
FT /evidence="ECO:0000269|PubMed:11258625"
FT /id="VAR_010991"
FT VARIANT 519
FT /note="Q -> P (in a cutaneous neurofibroma from a patient
FT with neurofibromatosis; somatic mutation;
FT dbSNP:rs199474770)"
FT /evidence="ECO:0000269|PubMed:22108604"
FT /id="VAR_067204"
FT VARIANT 532
FT /note="L -> P (in NF1; dbSNP:rs199474737)"
FT /evidence="ECO:0000269|PubMed:15060124"
FT /id="VAR_032466"
FT VARIANT 549
FT /note="L -> P (in NF1; dbSNP:rs199474758)"
FT /evidence="ECO:0000269|PubMed:10712197"
FT /id="VAR_021735"
FT VARIANT 574
FT /note="S -> R (in NF1)"
FT /evidence="ECO:0000269|PubMed:15060124"
FT /id="VAR_032467"
FT VARIANT 578
FT /note="L -> R (in NF1; dbSNP:rs199474774)"
FT /evidence="ECO:0000269|PubMed:12746402"
FT /id="VAR_021736"
FT VARIANT 581
FT /note="I -> T (in NF1; dbSNP:rs199474759)"
FT /evidence="ECO:0000269|PubMed:10712197"
FT /id="VAR_021737"
FT VARIANT 583
FT /note="K -> R (in NF1; dbSNP:rs199474760)"
FT /evidence="ECO:0000269|PubMed:10712197"
FT /id="VAR_021738"
FT VARIANT 604
FT /note="L -> V (in NF1; dbSNP:rs142712751)"
FT /evidence="ECO:0000269|PubMed:12522551"
FT /id="VAR_017553"
FT VARIANT 629
FT /note="G -> R (in NF1; affects splicing by creating a novel
FT splice acceptor site; dbSNP:rs199474738)"
FT /evidence="ECO:0000269|PubMed:15060124,
FT ECO:0000269|PubMed:15146469, ECO:0000269|PubMed:8834249"
FT /id="VAR_002653"
FT VARIANT 665
FT /note="S -> F (in NF1; unknown pathological significance;
FT dbSNP:rs145891889)"
FT /evidence="ECO:0000269|PubMed:10712197,
FT ECO:0000269|PubMed:15060124"
FT /id="VAR_021739"
FT VARIANT 678
FT /note="P -> L (in dbSNP:rs17881753)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_022255"
FT VARIANT 695
FT /note="L -> P (in NF1; dbSNP:rs199474761)"
FT /evidence="ECO:0000269|PubMed:10712197"
FT /id="VAR_021740"
FT VARIANT 712
FT /note="H -> R (in mismatch repair deficient cancer cells;
FT dbSNP:rs199474727)"
FT /evidence="ECO:0000269|PubMed:12522551"
FT /id="VAR_017554"
FT VARIANT 763
FT /note="L -> P (in NF1; dbSNP:rs199474762)"
FT /evidence="ECO:0000269|PubMed:10712197"
FT /id="VAR_021741"
FT VARIANT 765
FT /note="R -> H (in NF1; unknown pathological significance;
FT dbSNP:rs199474777)"
FT /evidence="ECO:0000269|PubMed:10336779"
FT /id="VAR_021742"
FT VARIANT 776
FT /note="A -> T (in a cutaneous neurofibroma from a patient
FT with neurofibromatosis; somatic mutation;
FT dbSNP:rs199474771)"
FT /evidence="ECO:0000269|PubMed:22108604"
FT /id="VAR_067205"
FT VARIANT 777
FT /note="W -> S (in NF1; dbSNP:rs199474745)"
FT /evidence="ECO:0000269|PubMed:10712197,
FT ECO:0000269|PubMed:15146469"
FT /id="VAR_021743"
FT VARIANT 780
FT /note="T -> K (in NF1; dbSNP:rs199474746)"
FT /evidence="ECO:0000269|PubMed:10712197,
FT ECO:0000269|PubMed:11735023, ECO:0000269|PubMed:12552569,
FT ECO:0000269|PubMed:15146469"
FT /id="VAR_021744"
FT VARIANT 781
FT /note="H -> P (in NF1; dbSNP:rs199474763)"
FT /evidence="ECO:0000269|PubMed:10712197"
FT /id="VAR_021745"
FT VARIANT 784
FT /note="W -> C (in NF1; dbSNP:rs199474778)"
FT /evidence="ECO:0000269|PubMed:11735023"
FT /id="VAR_021746"
FT VARIANT 784
FT /note="W -> R (in NF1; dbSNP:rs199474730)"
FT /evidence="ECO:0000269|PubMed:11857752,
FT ECO:0000269|PubMed:15146469"
FT /id="VAR_021747"
FT VARIANT 844
FT /note="L -> F (in NF1; dbSNP:rs199474785)"
FT /evidence="ECO:0000269|PubMed:10980545,
FT ECO:0000269|PubMed:15060124"
FT /id="VAR_010992"
FT VARIANT 844
FT /note="L -> P (in NF1; dbSNP:rs137854566)"
FT /evidence="ECO:0000269|PubMed:15060124"
FT /id="VAR_032468"
FT VARIANT 844
FT /note="L -> R (in NF1; sporadic; dbSNP:rs137854566)"
FT /evidence="ECO:0000269|PubMed:12522551,
FT ECO:0000269|PubMed:15948193, ECO:0000269|PubMed:9150739"
FT /id="VAR_002654"
FT VARIANT 847
FT /note="L -> P (in NF1; dbSNP:rs199474747)"
FT /evidence="ECO:0000269|PubMed:10712197,
FT ECO:0000269|PubMed:12552569, ECO:0000269|PubMed:15146469"
FT /id="VAR_021748"
FT VARIANT 848
FT /note="G -> E (in NF1; dbSNP:rs199474748)"
FT /evidence="ECO:0000269|PubMed:12552569,
FT ECO:0000269|PubMed:15146469"
FT /id="VAR_021749"
FT VARIANT 873
FT /note="R -> C (in dbSNP:rs199474739)"
FT /evidence="ECO:0000269|PubMed:15060124"
FT /id="VAR_032469"
FT VARIANT 898
FT /note="L -> P (in NF1; sporadic; dbSNP:rs199474786)"
FT /evidence="ECO:0000269|PubMed:12522551,
FT ECO:0000269|PubMed:9150739"
FT /id="VAR_002655"
FT VARIANT 920
FT /note="L -> P (in NF1; patient with cafe-au-lait spots; may
FT be a distinct form of NF1; dbSNP:rs199474775)"
FT /evidence="ECO:0000269|PubMed:12746402"
FT /id="VAR_021750"
FT VARIANT 968
FT /note="M -> R (in NF1; dbSNP:rs199474749)"
FT /evidence="ECO:0000269|PubMed:12552569,
FT ECO:0000269|PubMed:15146469"
FT /id="VAR_021751"
FT VARIANT 991
FT /note="Missing (in NF1; most patients carrying the mutation
FT do not manifest cutaneous neurofibromas)"
FT /evidence="ECO:0000269|PubMed:15060124,
FT ECO:0000269|PubMed:17160901, ECO:0000269|PubMed:7904209"
FT /id="VAR_002656"
FT VARIANT 1035
FT /note="M -> R (in NF1; dbSNP:rs137854553)"
FT /evidence="ECO:0000269|PubMed:8807336"
FT /id="VAR_002657"
FT VARIANT 1048
FT /note="W -> R (in NF1)"
FT /evidence="ECO:0000269|PubMed:23758643"
FT /id="VAR_071669"
FT VARIANT 1073
FT /note="M -> V (in NF1; dbSNP:rs199474740)"
FT /evidence="ECO:0000269|PubMed:15060124"
FT /id="VAR_032470"
FT VARIANT 1147
FT /note="L -> P (in NF1; dbSNP:rs199474779)"
FT /evidence="ECO:0000269|PubMed:11735023"
FT /id="VAR_021752"
FT VARIANT 1156
FT /note="N -> S (in NF1; dbSNP:rs199474764)"
FT /evidence="ECO:0000269|PubMed:10712197"
FT /id="VAR_021753"
FT VARIANT 1166
FT /note="G -> D (in NF1; dbSNP:rs199474787)"
FT /evidence="ECO:0000269|PubMed:7981679"
FT /id="VAR_010993"
FT VARIANT 1187
FT /note="L -> I (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035543"
FT VARIANT 1189
FT /note="Q -> R (in NF1; dbSNP:rs752039618)"
FT /evidence="ECO:0000269|PubMed:23758643"
FT /id="VAR_071670"
FT VARIANT 1193
FT /note="F -> C (in NF1; dbSNP:rs199474780)"
FT /evidence="ECO:0000269|PubMed:11735023"
FT /id="VAR_021754"
FT VARIANT 1196
FT /note="L -> R (in NF1; dbSNP:rs199474741)"
FT /evidence="ECO:0000269|PubMed:15060124"
FT /id="VAR_032471"
FT VARIANT 1204
FT /note="R -> G (in NF1; dbSNP:rs199474732)"
FT /evidence="ECO:0000269|PubMed:10336779"
FT /id="VAR_021755"
FT VARIANT 1204
FT /note="R -> W (in NF1; dbSNP:rs199474732)"
FT /evidence="ECO:0000269|PubMed:10607834"
FT /id="VAR_010994"
FT VARIANT 1243
FT /note="L -> P (in NF1; with neurofibromatous neuropathy;
FT dbSNP:rs137854564)"
FT /evidence="ECO:0000269|PubMed:15520408"
FT /id="VAR_032472"
FT VARIANT 1250
FT /note="R -> P (in NF1; dbSNP:rs199474765)"
FT /evidence="ECO:0000269|PubMed:10712197"
FT /id="VAR_021756"
FT VARIANT 1276
FT /note="R -> G (in NF1; dbSNP:rs199474742)"
FT /evidence="ECO:0000269|PubMed:15060124"
FT /id="VAR_032473"
FT VARIANT 1276
FT /note="R -> P (in NF1; complete loss of GAP activity;
FT dbSNP:rs137854556)"
FT /evidence="ECO:0000269|PubMed:10712197,
FT ECO:0000269|PubMed:9668168"
FT /id="VAR_010995"
FT VARIANT 1276
FT /note="R -> Q (in NF1 and mismatch repair deficient cancer
FT cells; dbSNP:rs137854556)"
FT /evidence="ECO:0000269|PubMed:10712197,
FT ECO:0000269|PubMed:12522551, ECO:0000269|PubMed:15060124"
FT /id="VAR_017555"
FT VARIANT 1411
FT /note="L -> F (in NFNS; dbSNP:rs199474789)"
FT /evidence="ECO:0000269|PubMed:19845691"
FT /id="VAR_065236"
FT VARIANT 1412
FT /note="R -> S (in NF1; significant reduction of GAP
FT activity; dbSNP:rs137854554)"
FT /evidence="ECO:0000269|PubMed:9003501"
FT /id="VAR_010996"
FT VARIANT 1422
FT /note="Y -> H (in dbSNP:rs17884349)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_022256"
FT VARIANT 1430
FT /note="K -> E (in NF1)"
FT /evidence="ECO:0000269|PubMed:15060124"
FT /id="VAR_032474"
FT VARIANT 1440
FT /note="K -> Q (in NF1; dbSNP:rs199474790)"
FT /evidence="ECO:0000269|PubMed:9003501"
FT /id="VAR_010997"
FT VARIANT 1440
FT /note="K -> R (in NF1; dbSNP:rs199474788)"
FT /evidence="ECO:0000269|PubMed:7981679"
FT /id="VAR_002658"
FT VARIANT 1444
FT /note="K -> E (in NF1 and NFNS; significant reduction of
FT intrinsic GAP activity; dbSNP:rs137854550)"
FT /evidence="ECO:0000269|PubMed:11857752,
FT ECO:0000269|PubMed:1568247, ECO:0000269|PubMed:16380919,
FT ECO:0000269|PubMed:9003501"
FT /id="VAR_002659"
FT VARIANT 1444
FT /note="K -> N (in NF1; dbSNP:rs199474750)"
FT /evidence="ECO:0000269|PubMed:12552569,
FT ECO:0000269|PubMed:15146469"
FT /id="VAR_021757"
FT VARIANT 1444
FT /note="K -> R (in NF1; dbSNP:rs199474781)"
FT /evidence="ECO:0000269|PubMed:11735023"
FT /id="VAR_021758"
FT VARIANT 1446
FT /note="L -> P (in NF1; dbSNP:rs199474733)"
FT /evidence="ECO:0000269|PubMed:10220149,
FT ECO:0000269|PubMed:10607834, ECO:0000269|PubMed:10712197"
FT /id="VAR_008129"
FT VARIANT 1451
FT /note="N -> T (in NFNS; dbSNP:rs199474754)"
FT /evidence="ECO:0000269|PubMed:16380919"
FT /id="VAR_032475"
FT VARIANT 1453
FT /note="V -> L (in NFNS; dbSNP:rs199474755)"
FT /evidence="ECO:0000269|PubMed:16380919"
FT /id="VAR_032476"
FT VARIANT 1459
FT /note="Missing (in NFNS; dbSNP:rs267606607)"
FT /evidence="ECO:0000269|PubMed:12707950,
FT ECO:0000269|PubMed:15060124, ECO:0000269|PubMed:16380919"
FT /id="VAR_032477"
FT VARIANT 1484
FT /note="S -> F (in a cutaneous neurofibroma from a patient
FT with neurofibromatosis; somatic mutation;
FT dbSNP:rs199474772)"
FT /evidence="ECO:0000269|PubMed:22108604"
FT /id="VAR_067206"
FT VARIANT 1489
FT /note="S -> G (in NF1; dbSNP:rs199474743)"
FT /evidence="ECO:0000269|PubMed:15060124,
FT ECO:0000269|PubMed:9003501"
FT /id="VAR_010998"
FT VARIANT 1605
FT /note="I -> V (in NF1; reduces protein stability;
FT dbSNP:rs199474766)"
FT /evidence="ECO:0000269|PubMed:10712197,
FT ECO:0000269|PubMed:21089070"
FT /id="VAR_021759"
FT VARIANT 1611
FT /note="R -> W (in NF1; dbSNP:rs1060500316)"
FT /evidence="ECO:0000269|PubMed:9298829"
FT /id="VAR_002660"
FT VARIANT 1733
FT /note="L -> LGHEQQKLPAATLAL (in NF1)"
FT /evidence="ECO:0000269|PubMed:8317503"
FT /id="VAR_002661"
FT VARIANT 1785
FT /note="A -> S (in NF1; dbSNP:rs199474782)"
FT /evidence="ECO:0000269|PubMed:11735023"
FT /id="VAR_021760"
FT VARIANT 1951
FT /note="P -> L (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035544"
FT VARIANT 1952
FT /note="W -> R (in NF1; dbSNP:rs199474791)"
FT /evidence="ECO:0000269|PubMed:9101300"
FT /id="VAR_002662"
FT VARIANT 1953
FT /note="L -> P (in NF1; dbSNP:rs199474792)"
FT /evidence="ECO:0000269|PubMed:2114220"
FT /id="VAR_002663"
FT VARIANT 1953
FT /note="Missing (in NF1)"
FT /evidence="ECO:0000269|PubMed:12552569,
FT ECO:0000269|PubMed:15146469"
FT /id="VAR_021761"
FT VARIANT 2001
FT /note="G -> R (in NF1; dbSNP:rs199474751)"
FT /evidence="ECO:0000269|PubMed:12552569,
FT ECO:0000269|PubMed:15146469"
FT /id="VAR_021762"
FT VARIANT 2012
FT /note="D -> N (in NF1; dbSNP:rs199474783)"
FT /evidence="ECO:0000269|PubMed:11735023"
FT /id="VAR_021763"
FT VARIANT 2088
FT /note="L -> P (in FSNF; no cafe-au-lait macules; null
FT mutation; 50% reduction of protein level;
FT dbSNP:rs137854561)"
FT /evidence="ECO:0000269|PubMed:11704931"
FT /id="VAR_017669"
FT VARIANT 2125
FT /note="L -> P (in NF1; dbSNP:rs1597843129)"
FT /evidence="ECO:0000269|PubMed:24413922"
FT /id="VAR_071671"
FT VARIANT 2164
FT /note="L -> M (in NF1; dbSNP:rs137854551)"
FT /evidence="ECO:0000269|PubMed:1302608"
FT /id="VAR_002664"
FT VARIANT 2192
FT /note="Y -> N (in NF1; dbSNP:rs267606598)"
FT /evidence="ECO:0000269|PubMed:1302608"
FT /id="VAR_002665"
FT VARIANT 2221
FT /note="P -> A (in NF1; dbSNP:rs199474776)"
FT /evidence="ECO:0000269|PubMed:12746402"
FT /id="VAR_021764"
FT VARIANT 2357
FT /note="E -> K (in NF1; dbSNP:rs199474784)"
FT /evidence="ECO:0000269|PubMed:11735023"
FT /id="VAR_021765"
FT VARIANT 2387..2388
FT /note="Missing (in NF1)"
FT /evidence="ECO:0000269|PubMed:10607834,
FT ECO:0000269|PubMed:8081387"
FT /id="VAR_002666"
FT VARIANT 2507
FT /note="T -> I (in NF1; dbSNP:rs149055633)"
FT /evidence="ECO:0000269|PubMed:10712197"
FT /id="VAR_021766"
FT VARIANT 2511
FT /note="V -> L (in dbSNP:rs2230850)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_022257"
FT VARIANT 2631
FT /note="T -> A (in NF1; dbSNP:rs199474793)"
FT /evidence="ECO:0000269|PubMed:8544190"
FT /id="VAR_002667"
FT VARIANT 2745
FT /note="G -> R (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035545"
FT MUTAGEN 1691
FT /note="K->A: Reduces phospholipid binding; when associated
FT with A-1695; A-1769 and A-1771."
FT /evidence="ECO:0000269|PubMed:16397625"
FT MUTAGEN 1695
FT /note="R->A: Reduces phospholipid binding; when associated
FT with A-1691; A-1769 and A-1771."
FT /evidence="ECO:0000269|PubMed:16397625"
FT MUTAGEN 1769
FT /note="R->A: Reduces phospholipid binding; when associated
FT with A-1691; A-1695 and A-1771."
FT /evidence="ECO:0000269|PubMed:16397625"
FT MUTAGEN 1771
FT /note="K->A: Reduces phospholipid binding; when associated
FT with A-1691; A-169 and A-1769."
FT /evidence="ECO:0000269|PubMed:16397625,
FT ECO:0000269|PubMed:21089070"
FT MUTAGEN 1771
FT /note="Missing: Reduces protein stability."
FT /evidence="ECO:0000269|PubMed:16397625,
FT ECO:0000269|PubMed:21089070"
FT CONFLICT 496
FT /note="M -> I (in Ref. 11; AAA74897/AAB59558)"
FT /evidence="ECO:0000305"
FT CONFLICT 1094..1095
FT /note="EL -> ST (in Ref. 14; AAA59923)"
FT /evidence="ECO:0000305"
FT CONFLICT 1576
FT /note="H -> HH (in Ref. 11; AAA74897/AAB59558)"
FT /evidence="ECO:0000305"
FT HELIX 5..18
FT /evidence="ECO:0007829|PDB:7PGU"
FT TURN 29..33
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 34..47
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 51..66
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 73..95
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 130..144
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 150..166
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 177..181
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 187..200
FT /evidence="ECO:0007829|PDB:7PGU"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 206..226
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 228..236
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 240..256
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 260..274
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 278..285
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 294..308
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 314..331
FT /evidence="ECO:0007829|PDB:7PGU"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 341..357
FT /evidence="ECO:0007829|PDB:7PGU"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:7PGS"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 373..386
FT /evidence="ECO:0007829|PDB:7PGU"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 394..398
FT /evidence="ECO:0007829|PDB:7PGU"
FT STRAND 399..402
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 404..419
FT /evidence="ECO:0007829|PDB:7PGU"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 429..435
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 436..454
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 483..502
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 504..506
FT /evidence="ECO:0007829|PDB:7PGU"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:7PGU"
FT STRAND 516..518
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 521..530
FT /evidence="ECO:0007829|PDB:7PGU"
FT TURN 531..534
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 539..551
FT /evidence="ECO:0007829|PDB:7PGU"
FT TURN 555..557
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 559..561
FT /evidence="ECO:0007829|PDB:7PGS"
FT HELIX 566..585
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 593..617
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 678..686
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 688..692
FT /evidence="ECO:0007829|PDB:7PGU"
FT TURN 693..696
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 700..720
FT /evidence="ECO:0007829|PDB:7PGU"
FT TURN 724..727
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 728..731
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 735..745
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 752..763
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 771..792
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 832..846
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 849..851
FT /evidence="ECO:0007829|PDB:7PGS"
FT HELIX 890..901
FT /evidence="ECO:0007829|PDB:7PGU"
FT TURN 907..909
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 910..923
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 927..929
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 930..941
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 942..944
FT /evidence="ECO:0007829|PDB:7PGU"
FT TURN 947..949
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 957..972
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 980..983
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 989..999
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1008..1024
FT /evidence="ECO:0007829|PDB:7PGU"
FT TURN 1025..1028
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1034..1045
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1053..1057
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1061..1063
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1064..1079
FT /evidence="ECO:0007829|PDB:7PGU"
FT STRAND 1091..1093
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1095..1115
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1137..1154
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1157..1160
FT /evidence="ECO:0007829|PDB:7PGU"
FT TURN 1162..1164
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1165..1169
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1173..1188
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1197..1200
FT /evidence="ECO:0007829|PDB:7PGU"
FT TURN 1201..1204
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1208..1216
FT /evidence="ECO:0007829|PDB:1NF1"
FT TURN 1217..1219
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1220..1228
FT /evidence="ECO:0007829|PDB:6OB3"
FT HELIX 1233..1235
FT /evidence="ECO:0007829|PDB:6OB3"
FT HELIX 1236..1249
FT /evidence="ECO:0007829|PDB:6OB3"
FT HELIX 1253..1267
FT /evidence="ECO:0007829|PDB:6OB3"
FT HELIX 1271..1273
FT /evidence="ECO:0007829|PDB:6OB3"
FT STRAND 1277..1279
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1280..1309
FT /evidence="ECO:0007829|PDB:6OB3"
FT TURN 1310..1312
FT /evidence="ECO:0007829|PDB:6V6F"
FT HELIX 1315..1317
FT /evidence="ECO:0007829|PDB:6OB3"
FT HELIX 1323..1325
FT /evidence="ECO:0007829|PDB:6OB3"
FT STRAND 1328..1330
FT /evidence="ECO:0007829|PDB:6V65"
FT HELIX 1332..1351
FT /evidence="ECO:0007829|PDB:6OB3"
FT HELIX 1354..1356
FT /evidence="ECO:0007829|PDB:6OB3"
FT HELIX 1359..1370
FT /evidence="ECO:0007829|PDB:6OB3"
FT HELIX 1392..1394
FT /evidence="ECO:0007829|PDB:6OB3"
FT HELIX 1398..1400
FT /evidence="ECO:0007829|PDB:6OB3"
FT HELIX 1401..1411
FT /evidence="ECO:0007829|PDB:6OB3"
FT HELIX 1414..1419
FT /evidence="ECO:0007829|PDB:6OB3"
FT TURN 1421..1425
FT /evidence="ECO:0007829|PDB:6OB3"
FT STRAND 1426..1429
FT /evidence="ECO:0007829|PDB:6V6F"
FT HELIX 1433..1451
FT /evidence="ECO:0007829|PDB:6OB3"
FT HELIX 1459..1464
FT /evidence="ECO:0007829|PDB:6OB3"
FT HELIX 1465..1483
FT /evidence="ECO:0007829|PDB:6OB3"
FT STRAND 1490..1492
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1510..1514
FT /evidence="ECO:0007829|PDB:1NF1"
FT HELIX 1517..1520
FT /evidence="ECO:0007829|PDB:1NF1"
FT HELIX 1531..1533
FT /evidence="ECO:0007829|PDB:7PGS"
FT HELIX 1535..1544
FT /evidence="ECO:0007829|PDB:1NF1"
FT HELIX 1569..1578
FT /evidence="ECO:0007829|PDB:3P7Z"
FT TURN 1582..1586
FT /evidence="ECO:0007829|PDB:3PG7"
FT HELIX 1587..1590
FT /evidence="ECO:0007829|PDB:3PG7"
FT STRAND 1592..1598
FT /evidence="ECO:0007829|PDB:3PG7"
FT STRAND 1604..1609
FT /evidence="ECO:0007829|PDB:3PG7"
FT HELIX 1610..1612
FT /evidence="ECO:0007829|PDB:3PG7"
FT TURN 1615..1617
FT /evidence="ECO:0007829|PDB:2D4Q"
FT HELIX 1620..1631
FT /evidence="ECO:0007829|PDB:3PG7"
FT TURN 1632..1636
FT /evidence="ECO:0007829|PDB:3PG7"
FT STRAND 1639..1644
FT /evidence="ECO:0007829|PDB:3PG7"
FT HELIX 1650..1652
FT /evidence="ECO:0007829|PDB:3PG7"
FT HELIX 1656..1661
FT /evidence="ECO:0007829|PDB:3PG7"
FT TURN 1662..1664
FT /evidence="ECO:0007829|PDB:3PG7"
FT HELIX 1668..1672
FT /evidence="ECO:0007829|PDB:3PG7"
FT STRAND 1674..1681
FT /evidence="ECO:0007829|PDB:3PG7"
FT HELIX 1684..1692
FT /evidence="ECO:0007829|PDB:3PG7"
FT HELIX 1694..1697
FT /evidence="ECO:0007829|PDB:3PG7"
FT TURN 1698..1702
FT /evidence="ECO:0007829|PDB:3PG7"
FT STRAND 1706..1711
FT /evidence="ECO:0007829|PDB:3PG7"
FT HELIX 1714..1717
FT /evidence="ECO:0007829|PDB:3PG7"
FT HELIX 1721..1723
FT /evidence="ECO:0007829|PDB:3PG7"
FT HELIX 1728..1732
FT /evidence="ECO:0007829|PDB:3PG7"
FT STRAND 1738..1749
FT /evidence="ECO:0007829|PDB:3PG7"
FT STRAND 1751..1757
FT /evidence="ECO:0007829|PDB:3PG7"
FT STRAND 1759..1767
FT /evidence="ECO:0007829|PDB:3PG7"
FT STRAND 1770..1772
FT /evidence="ECO:0007829|PDB:2D4Q"
FT STRAND 1775..1777
FT /evidence="ECO:0007829|PDB:3PG7"
FT STRAND 1780..1784
FT /evidence="ECO:0007829|PDB:3PG7"
FT HELIX 1785..1787
FT /evidence="ECO:0007829|PDB:3PG7"
FT STRAND 1788..1795
FT /evidence="ECO:0007829|PDB:3PG7"
FT STRAND 1798..1803
FT /evidence="ECO:0007829|PDB:3PG7"
FT STRAND 1810..1813
FT /evidence="ECO:0007829|PDB:3PG7"
FT HELIX 1817..1833
FT /evidence="ECO:0007829|PDB:3PG7"
FT HELIX 1847..1849
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1851..1861
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1867..1883
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1905..1917
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1920..1922
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1923..1934
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1939..1949
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1950..1956
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1957..1960
FT /evidence="ECO:0007829|PDB:7PGU"
FT STRAND 1965..1967
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1968..1984
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 1989..2000
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2004..2006
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2007..2021
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2026..2041
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2043..2059
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2060..2062
FT /evidence="ECO:0007829|PDB:7PGU"
FT STRAND 2067..2069
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2075..2089
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2090..2092
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2096..2110
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2116..2134
FT /evidence="ECO:0007829|PDB:7PGU"
FT STRAND 2137..2139
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2143..2155
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2159..2164
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2173..2177
FT /evidence="ECO:0007829|PDB:7PGU"
FT TURN 2180..2184
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2199..2218
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2225..2237
FT /evidence="ECO:0007829|PDB:7PGU"
FT TURN 2242..2244
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2245..2255
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2261..2280
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2284..2301
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2302..2304
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2311..2323
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2328..2347
FT /evidence="ECO:0007829|PDB:7PGU"
FT STRAND 2350..2354
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2356..2363
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2365..2367
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2368..2378
FT /evidence="ECO:0007829|PDB:7PGU"
FT TURN 2382..2384
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2386..2394
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2396..2399
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2403..2424
FT /evidence="ECO:0007829|PDB:7PGU"
FT TURN 2427..2429
FT /evidence="ECO:0007829|PDB:7PGU"
FT TURN 2433..2435
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2436..2442
FT /evidence="ECO:0007829|PDB:7PGU"
FT TURN 2443..2445
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2447..2452
FT /evidence="ECO:0007829|PDB:7PGU"
FT TURN 2607..2609
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2613..2629
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2633..2649
FT /evidence="ECO:0007829|PDB:7PGU"
FT TURN 2651..2653
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2654..2657
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2658..2671
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2675..2691
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2702..2705
FT /evidence="ECO:0007829|PDB:7PGU"
FT TURN 2706..2709
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2711..2714
FT /evidence="ECO:0007829|PDB:7PGU"
FT HELIX 2728..2742
FT /evidence="ECO:0007829|PDB:7PGU"
FT VARIANT P21359-2:1661
FT /note="C -> R (in NF1; dbSNP:rs1597829901)"
FT /evidence="ECO:0000269|PubMed:23758643"
FT /id="VAR_082822"
FT VARIANT P21359-2:1918
FT /note="I -> T (in NF1; dbSNP:rs1304057833)"
FT /evidence="ECO:0000269|PubMed:23758643"
FT /id="VAR_082823"
SQ SEQUENCE 2839 AA; 319372 MW; C079475139DBD51E CRC64;
MAAHRPVEWV QAVVSRFDEQ LPIKTGQQNT HTKVSTEHNK ECLINISKYK FSLVISGLTT
ILKNVNNMRI FGEAAEKNLY LSQLIILDTL EKCLAGQPKD TMRLDETMLV KQLLPEICHF
LHTCREGNQH AAELRNSASG VLFSLSCNNF NAVFSRISTR LQELTVCSED NVDVHDIELL
QYINVDCAKL KRLLKETAFK FKALKKVAQL AVINSLEKAF WNWVENYPDE FTKLYQIPQT
DMAECAEKLF DLVDGFAEST KRKAAVWPLQ IILLILCPEI IQDISKDVVD ENNMNKKLFL
DSLRKALAGH GGSRQLTESA AIACVKLCKA STYINWEDNS VIFLLVQSMV VDLKNLLFNP
SKPFSRGSQP ADVDLMIDCL VSCFRISPHN NQHFKICLAQ NSPSTFHYVL VNSLHRIITN
SALDWWPKID AVYCHSVELR NMFGETLHKA VQGCGAHPAI RMAPSLTFKE KVTSLKFKEK
PTDLETRSYK YLLLSMVKLI HADPKLLLCN PRKQGPETQG STAELITGLV QLVPQSHMPE
IAQEAMEALL VLHQLDSIDL WNPDAPVETF WEISSQMLFY ICKKLTSHQM LSSTEILKWL
REILICRNKF LLKNKQADRS SCHFLLFYGV GCDIPSSGNT SQMSMDHEEL LRTPGASLRK
GKGNSSMDSA AGCSGTPPIC RQAQTKLEVA LYMFLWNPDT EAVLVAMSCF RHLCEEADIR
CGVDEVSVHN LLPNYNTFME FASVSNMMST GRAALQKRVM ALLRRIEHPT AGNTEAWEDT
HAKWEQATKL ILNYPKAKME DGQAAESLHK TIVKRRMSHV SGGGSIDLSD TDSLQEWINM
TGFLCALGGV CLQQRSNSGL ATYSPPMGPV SERKGSMISV MSSEGNADTP VSKFMDRLLS
LMVCNHEKVG LQIRTNVKDL VGLELSPALY PMLFNKLKNT ISKFFDSQGQ VLLTDTNTQF
VEQTIAIMKN LLDNHTEGSS EHLGQASIET MMLNLVRYVR VLGNMVHAIQ IKTKLCQLVE
VMMARRDDLS FCQEMKFRNK MVEYLTDWVM GTSNQAADDD VKCLTRDLDQ ASMEAVVSLL
AGLPLQPEEG DGVELMEAKS QLFLKYFTLF MNLLNDCSEV EDESAQTGGR KRGMSRRLAS
LRHCTVLAMS NLLNANVDSG LMHSIGLGYH KDLQTRATFM EVLTKILQQG TEFDTLAETV
LADRFERLVE LVTMMGDQGE LPIAMALANV VPCSQWDELA RVLVTLFDSR HLLYQLLWNM
FSKEVELADS MQTLFRGNSL ASKIMTFCFK VYGATYLQKL LDPLLRIVIT SSDWQHVSFE
VDPTRLEPSE SLEENQRNLL QMTEKFFHAI ISSSSEFPPQ LRSVCHCLYQ ATCHSLLNKA
TVKEKKENKK SVVSQRFPQN SIGAVGSAMF LRFINPAIVS PYEAGILDKK PPPRIERGLK
LMSKILQSIA NHVLFTKEEH MRPFNDFVKS NFDAARRFFL DIASDCPTSD AVNHSLSFIS
DGNVLALHRL LWNNQEKIGQ YLSSNRDHKA VGRRPFDKMA TLLAYLGPPE HKPVADTHWS
SLNLTSSKFE EFMTRHQVHE KEEFKALKTL SIFYQAGTSK AGNPIFYYVA RRFKTGQING
DLLIYHVLLT LKPYYAKPYE IVVDLTHTGP SNRFKTDFLS KWFVVFPGFA YDNVSAVYIY
NCNSWVREYT KYHERLLTGL KGSKRLVFID CPGKLAEHIE HEQQKLPAAT LALEEDLKVF
HNALKLAHKD TKVSIKVGST AVQVTSAERT KVLGQSVFLN DIYYASEIEE ICLVDENQFT
LTIANQGTPL TFMHQECEAI VQSIIHIRTR WELSQPDSIP QHTKIRPKDV PGTLLNIALL
NLGSSDPSLR SAAYNLLCAL TCTFNLKIEG QLLETSGLCI PANNTLFIVS ISKTLAANEP
HLTLEFLEEC ISGFSKSSIE LKHLCLEYMT PWLSNLVRFC KHNDDAKRQR VTAILDKLIT
MTINEKQMYP SIQAKIWGSL GQITDLLDVV LDSFIKTSAT GGLGSIKAEV MADTAVALAS
GNVKLVSSKV IGRMCKIIDK TCLSPTPTLE QHLMWDDIAI LARYMLMLSF NNSLDVAAHL
PYLFHVVTFL VATGPLSLRA STHGLVINII HSLCTCSQLH FSEETKQVLR LSLTEFSLPK
FYLLFGISKV KSAAVIAFRS SYRDRSFSPG SYERETFALT SLETVTEALL EIMEACMRDI
PTCKWLDQWT ELAQRFAFQY NPSLQPRALV VFGCISKRVS HGQIKQIIRI LSKALESCLK
GPDTYNSQVL IEATVIALTK LQPLLNKDSP LHKALFWVAV AVLQLDEVNL YSAGTALLEQ
NLHTLDSLRI FNDKSPEEVF MAIRNPLEWH CKQMDHFVGL NFNSNFNFAL VGHLLKGYRH
PSPAIVARTV RILHTLLTLV NKHRNCDKFE VNTQSVAYLA ALLTVSEEVR SRCSLKHRKS
LLLTDISMEN VPMDTYPIHH GDPSYRTLKE TQPWSSPKGS EGYLAATYPT VGQTSPRARK
SMSLDMGQPS QANTKKLLGT RKSFDHLISD TKAPKRQEME SGITTPPKMR RVAETDYEME
TQRISSSQQH PHLRKVSVSE SNVLLDEEVL TDPKIQALLL TVLATLVKYT TDEFDQRILY
EYLAEASVVF PKVFPVVHNL LDSKINTLLS LCQDPNLLNP IHGIVQSVVY HEESPPQYQT
SYLQSFGFNG LWRFAGPFSK QTQIPDYAEL IVKFLDALID TYLPGIDEET SEESLLTPTS
PYPPALQSQL SITANLNLSN SMTSLATSQH SPGIDKENVE LSPTTGHCNS GRTRHGSASQ
VQKQRSAGSF KRNSIKKIV
