Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Neurofibromin (Neurofibromatosis-related protein NF-1) [Cleaved into: Neurofibromin truncated]

 NF1_HUMAN               Reviewed;        2839 AA.
P21359; O00662; Q14284; Q14930; Q14931; Q9UMK3;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 2.
25-OCT-2017, entry version 213.
RecName: Full=Neurofibromin;
AltName: Full=Neurofibromatosis-related protein NF-1;
Contains:
RecName: Full=Neurofibromin truncated;
Name=NF1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
PubMed=1457041; DOI=10.1089/dna.1992.11.727;
Bernards A., Haase V.H., Murthy A.E., Menon A., Hannigan G.E.,
Gusella J.F.;
"Complete human NF1 cDNA sequence: two alternatively spliced mRNAs and
absence of expression in a neuroblastoma line.";
DNA Cell Biol. 11:727-734(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2134734; DOI=10.1126/science.2134734;
Wallace M.R., Marchuk D.A., Andersen L.B., Letcher R., Odeh H.M.,
Saulino A.M., Fountain J.W., Brereton A., Nicholson J., Mitchell A.L.,
Brownstein B.H., Collins F.S.;
"Type 1 neurofibromatosis gene: identification of a large transcript
disrupted in three NF1 patients.";
Science 249:181-186(1990).
[3]
ERRATUM.
PubMed=2125369;
Wallace M.R., Marchuk D.A., Andersen L.B., Letcher R., Odeh H.M.,
Saulino A.M., Fountain J.W., Brereton A., Nicholson J., Mitchell A.L.,
Brownstein B.H., Collins F.S.;
Science 250:1749-1749(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1783401; DOI=10.1016/0888-7543(91)90017-9;
Marchuk D.A., Saulino A.M., Tavakkol R., Swaroop M., Wallace M.R.,
Andersen L.B., Mitchell A.L., Gutmann D.H., Boguski M.S.,
Collins F.S.;
"cDNA cloning of the type 1 neurofibromatosis gene: complete sequence
of the NF1 gene product.";
Genomics 11:931-940(1991).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND ALTERNATIVE SPLICING.
TISSUE=Placenta;
PubMed=1339276; DOI=10.1016/0006-291X(92)91294-Z;
Suzuki H., Takahashi K., Kubota Y., Shibahara S.;
"Molecular cloning of a cDNA coding for neurofibromatosis type 1
protein isoform lacking the domain related to ras GTPase-activating
protein.";
Biochem. Biophys. Res. Commun. 187:984-990(1992).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
TISSUE=Kidney;
PubMed=7570581; DOI=10.1620/tjem.175.225;
Suzuki H., Takahashi K., Shibahara S.;
"Evidence for the presence of two amino-terminal isoforms of
neurofibromin, a gene product responsible for neurofibromatosis type
1.";
Tohoku J. Exp. Med. 175:225-233(1995).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-80; LEU-678;
HIS-1422 AND LEU-2511.
NIEHS SNPs program;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 335-2839 (ISOFORM 1), AND
VARIANT NF1 PRO-1953.
PubMed=2114220; DOI=10.1016/0092-8674(90)90253-B;
Cawthon R.M., Weiss R., Xu G., Viskochil D., Culver M., Stevens J.,
Robertson M., Dunn D., Gesteland R., O'Connell P., White R.;
"A major segment of the neurofibromatosis type 1 gene: cDNA sequence,
genomic structure, and point mutations.";
Cell 62:193-201(1990).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 335-2839 (ISOFORMS 1 AND 6).
PubMed=2116237; DOI=10.1016/0092-8674(90)90024-9;
Xu G., O'Connell P., Viskochil D., Cawthon R.M., Robertson M.,
Culver M., Dunn D., Stevens J., Gesteland R., White R., Weiss R.;
"The neurofibromatosis type 1 gene encodes a protein related to GAP.";
Cell 62:599-608(1990).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 707-782.
PubMed=9002664; DOI=10.1093/hmg/6.1.9;
Regnier V., Meddeb M., Lecointre G., Richard F., Duverger A.,
Nguyen V.C., Dutrillaux B., Bernheim A., Danglot G.;
"Emergence and scattering of multiple neurofibromatosis (NF1)-related
sequences during hominoid evolution suggest a process of
pericentromeric interchromosomal transposition.";
Hum. Mol. Genet. 6:9-16(1997).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 751-1611 (ISOFORMS 1 AND 2).
PubMed=7774960; DOI=10.1016/0888-7543(95)80104-T;
Li Y., O'Connell P., Breidenbach H.H., Cawthon R.M., Stevens J.,
Xu G., Neil S., Robertson M., White R., Viskochil D.;
"Genomic organization of the neurofibromatosis 1 gene (NF1).";
Genomics 25:9-18(1995).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 1090-1598 (ISOFORM 4).
PubMed=2121370; DOI=10.1016/0092-8674(90)90150-D;
Martin G.A., Viskochil D., Bollag G., McCabe P.C., Crosier W.J.,
Haubruck H., Conroy L., Clark R., O'Connell P., Cawthon R.M.,
Innis M., McCormick F.;
"The GAP-related domain of the neurofibromatosis type 1 gene product
interacts with ras p21.";
Cell 63:843-849(1990).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 1168-1566 (ISOFORMS 1 AND 2).
PubMed=1923522;
Nishi T., Lee P.S., Oka K., Levin V.A., Tanase S., Morino Y., Saya H.;
"Differential expression of two types of the neurofibromatosis type 1
(NF1) gene transcripts related to neuronal differentiation.";
Oncogene 6:1555-1559(1991).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 1371-1391 (ISOFORM 2), FUNCTION, AND
TISSUE SPECIFICITY.
PubMed=8417346; DOI=10.1128/MCB.13.1.487;
Andersen L.B., Ballester R., Marchuk D.A., Chang E., Gutmann D.H.,
Saulino A.M., Camonis J., Wigler M., Collins F.S.;
"A conserved alternative splice in the von Recklinghausen
neurofibromatosis (NF1) gene produces two neurofibromin isoforms, both
of which have GTPase-activating protein activity.";
Mol. Cell. Biol. 13:487-495(1993).
[17]
NUCLEOTIDE SEQUENCE [MRNA] OF 1371-1391 (ISOFORM 2).
PubMed=1662505; DOI=10.1016/0006-291X(91)92029-J;
Suzuki Y., Suzuki H., Kayama T., Yoshimoto T., Shibahara S.;
"Brain tumors predominantly express the neurofibromatosis type 1 gene
transcripts containing the 63 base insert in the region coding for
GTPase activating protein-related domain.";
Biochem. Biophys. Res. Commun. 181:955-961(1991).
[18]
FUNCTION.
PubMed=2121371; DOI=10.1016/0092-8674(90)90151-4;
Ballester R., Marchuk D.A., Boguski M.S., Saulino A.M., Letcher R.,
Wigler M., Collins F.S.;
"The NF1 locus encodes a protein functionally related to mammalian GAP
and yeast IRA proteins.";
Cell 63:851-859(1990).
[19]
RNA EDITING.
PubMed=8602361; DOI=10.1093/nar/24.3.478;
Skuse G.R., Cappione A.J., Sowden M., Metheny L.J., Smith H.C.;
"The neurofibromatosis type I messenger RNA undergoes base-
modification RNA editing.";
Nucleic Acids Res. 24:478-485(1996).
[20]
RNA EDITING.
PubMed=11727199; DOI=10.1086/337952;
Mukhopadhyay D., Anant S., Lee R.M., Kennedy S., Viskochil D.,
Davidson N.O.;
"C-->U editing of neurofibromatosis 1 mRNA occurs in tumors that
express both the type II transcript and apobec-1, the catalytic
subunit of the apolipoprotein B mRNA-editing enzyme.";
Am. J. Hum. Genet. 70:38-50(2002).
[21]
REVIEW ON VARIANTS.
PubMed=7981724; DOI=10.1002/humu.1380040202;
Upadhyaya M., Shaw D.J., Harper P.S.;
"Molecular basis of neurofibromatosis type 1 (NF1): mutation analysis
and polymorphisms in the NF1 gene.";
Hum. Mutat. 4:83-101(1994).
[22]
REVIEW ON VARIANTS.
PubMed=8825042; DOI=10.1136/jmg.33.1.2;
Shen M.H., Harper P.S., Upadhyaya M.;
"Molecular genetics of neurofibromatosis type 1 (NF1).";
J. Med. Genet. 33:2-17(1996).
[23]
SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNAL.
PubMed=14988005; DOI=10.1016/S0014-5793(04)00078-X;
Vandenbroucke I., Van Oostveldt P., Coene E., De Paepe A.,
Messiaen L.;
"Neurofibromin is actively transported to the nucleus.";
FEBS Lett. 560:98-102(2004).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
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).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-864; SER-2188; SER-2515;
SER-2521 AND SER-2543, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-864; SER-876 AND
SER-2515, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-864 AND SER-2817, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2543 AND SER-2817, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[33]
INTERACTION WITH HTR6.
PubMed=23027611; DOI=10.1002/emmm.201201410;
Meffre J., Chaumont-Dubel S., Mannoury la Cour C., Loiseau F.,
Watson D.J., Dekeyne A., Seveno M., Rivet J.M., Gaven F., Deleris P.,
Herve D., Fone K.C., Bockaert J., Millan M.J., Marin P.;
"5-HT(6) receptor recruitment of mTOR as a mechanism for perturbed
cognition in schizophrenia.";
EMBO Mol. Med. 4:1043-1056(2012).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-864; SER-876; SER-2188;
SER-2515; SER-2521; SER-2523; SER-2543; THR-2565; SER-2597 AND
SER-2802, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2543 AND SER-2817, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[36]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1198-1551.
PubMed=9687500; DOI=10.1093/emboj/17.15.4313;
Scheffzek K., Ahmadian M.R., Wiesmuller L., Kabsch W., Stege P.,
Schmitz F., Wittinghofer A.;
"Structural analysis of the GAP-related domain from neurofibromin and
its implications.";
EMBO J. 17:4313-4327(1998).
[37]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1581-1837, LIPID-BINDING,
DOMAIN, AND MUTAGENESIS OF LYS-1691; ARG-1695; ARG-1769 AND LYS-1771.
PubMed=16397625; DOI=10.1038/sj.embor.7400602;
D'Angelo I., Welti S., Bonneau F., Scheffzek K.;
"A novel bipartite phospholipid-binding module in the
neurofibromatosis type 1 protein.";
EMBO Rep. 7:174-179(2006).
[38]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1566-1837 IN COMPLEX WITH
PHOSPHOLIPID, LIPID-BINDING, AND DOMAIN.
PubMed=17187824; DOI=10.1016/j.jmb.2006.11.055;
Welti S., Fraterman S., D'Angelo I., Wilm M., Scheffzek K.;
"The sec14 homology module of neurofibromin binds cellular
glycerophospholipids: mass spectrometry and structure of a lipid
complex.";
J. Mol. Biol. 366:551-562(2007).
[39]
X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 1581-1837 OF VARIANT NF1
VAL-1605 AND MUTANT LYS-1771 DEL IN COMPLEX WITH LIPID,
CHARACTERIZATION OF VARIANT NF1 VAL-1605, MUTAGENESIS OF LYS-1771,
LIPID-BINDING, AND DOMAIN.
PubMed=21089070; DOI=10.1002/humu.21405;
Welti S., Kuhn S., D'Angelo I., Brugger B., Kaufmann D., Scheffzek K.;
"Structural and biochemical consequences of NF1 associated
nontruncating mutations in the Sec14-PH module of neurofibromin.";
Hum. Mutat. 32:191-197(2011).
[40]
VARIANT GLU-1444.
PubMed=1568247; DOI=10.1016/0092-8674(92)90408-5;
Li Y., Bollag G., Clark R., Stevens J., Conroy L., Fults D., Ward K.,
Friedman E., Samowitz W., Robertson M., Bradley P., McCormick F.,
White R., Cawthon R.M.;
"Somatic mutations in the neurofibromatosis 1 gene in human tumors.";
Cell 69:275-281(1992).
[41]
VARIANTS NF1 MET-2164 AND ASN-2192.
PubMed=1302608; DOI=10.1093/hmg/1.9.735;
Upadhyaya M., Shen M.H., Cherryson A., Farnham J., Maynard J.,
Huson S.M., Harper P.S.;
"Analysis of mutations at the neurofibromatosis 1 (NF1) locus.";
Hum. Mol. Genet. 1:735-740(1992).
[42]
VARIANT GLY-HIS-GLU-GLN-GLN-LYS-LEU-PRO-ALA-ALA-THR-LEU-ALA-LEU-1733
INS.
PubMed=8317503;
Tassabehji M., Strachan T., Sharland M., Colley A., Donnai D.,
Harris R., Thakker N.;
"Tandem duplication within a neurofibromatosis type 1 (NF1) gene exon
in a family with features of Watson syndrome and Noonan syndrome.";
Am. J. Hum. Genet. 53:90-95(1993).
[43]
VARIANT MET-991 DEL.
PubMed=7904209; DOI=10.1093/hmg/2.11.1861;
Shen M.H., Harper P.S., Upadhyaya M.;
"Neurofibromatosis type 1 (NF1): the search for mutations by PCR-
heteroduplex analysis on Hydrolink gels.";
Hum. Mol. Genet. 2:1861-1864(1993).
[44]
VARIANTS NF1 ASP-1166 AND ARG-1440.
PubMed=7981679; DOI=10.1093/hmg/3.7.1109;
Purandare S.M., Lanyon W.G., Connor J.M.;
"Characterisation of inherited and sporadic mutations in
neurofibromatosis type-1.";
Hum. Mol. Genet. 3:1109-1115(1994).
[45]
VARIANT NF1 2387-ASN-PHE-2388 DEL.
PubMed=8081387; DOI=10.1002/humu.1380030404;
Abernathy C.R., Colman S.D., Kousseff B.G., Wallace M.R.;
"Two NF1 mutations: frameshift in the GAP-related domain, and loss of
two codons toward the 3' end of the gene.";
Hum. Mutat. 3:347-352(1994).
[46]
VARIANT NF1 ALA-2631.
PubMed=8544190; DOI=10.1136/jmg.32.9.706;
Upadhyaya M., Maynard J., Osborn M.J., Huson S.M., Ponder M.,
Ponder B.A.J., Harper P.S.;
"Characterisation of germline mutations in the neurofibromatosis type
1 (NF1) gene.";
J. Med. Genet. 32:706-710(1995).
[47]
VARIANT NF1 ARG-629.
PubMed=8834249; DOI=10.1007/BF02267073;
Gasparini P., D'Agruma L., de Cillis G.P., Balestrazzi P.,
Mingarelli R., Zelante L.;
"Scanning the first part of the neurofibromatosis type 1 gene by RNA-
SSCP: identification of three novel mutations and of two new
polymorphisms.";
Hum. Genet. 97:492-495(1996).
[48]
VARIANT NF1 ARG-1035.
PubMed=8807336;
DOI=10.1002/(SICI)1098-1004(1996)8:1<51::AID-HUMU7>3.0.CO;2-S;
Wu R., Legius E., Robberecht W., Dumoulin M., Cassiman J.-J.,
Fryns J.-P.;
"Neurofibromatosis type I gene mutation in a patient with features of
LEOPARD syndrome.";
Hum. Mutat. 8:51-56(1996).
[49]
VARIANTS NF1 SER-1412; GLN-1440; GLU-1444 AND GLY-1489.
PubMed=9003501; DOI=10.1007/s004390050317;
Upadhyaya M., Osborn M.J., Maynard J., Kim M.R., Tamanoi F.,
Cooper D.N.;
"Mutational and functional analysis of the neurofibromatosis type 1
(NF1) gene.";
Hum. Genet. 99:88-92(1997).
[50]
VARIANTS NF1 ARG-844 AND PRO-898.
PubMed=9150739; DOI=10.1007/s004390050427;
Maynard J., Krawczak M., Upadhyaya M.;
"Characterization and significance of nine novel mutations in exon 16
of the neurofibromatosis type 1 (NF1) gene.";
Hum. Genet. 99:674-676(1997).
[51]
VARIANT NF1 ARG-1952.
PubMed=9101300;
DOI=10.1002/(SICI)1098-1004(1997)9:4<366::AID-HUMU12>3.0.CO;2-0;
Hudson J., Wu C.L., Tassabehji M., Summers E.M., Simon S., Super M.,
Donnai D., Thakker N.;
"Novel and recurrent mutations in the neurofibromatosis type 1 (NF1)
gene.";
Hum. Mutat. 9:366-367(1997).
[52]
VARIANTS NF1 GLY-338 AND TRP-1611.
PubMed=9298829;
DOI=10.1002/(SICI)1098-1004(1997)10:3<248::AID-HUMU14>3.3.CO;2-D;
Upadhyaya M., Maynard J., Osborn M.J., Harper P.S.;
"Six novel mutations in the neurofibromatosis type 1 (NF1) gene.";
Hum. Mutat. 10:248-250(1997).
[53]
VARIANT NF1 PRO-1276.
PubMed=9668168; DOI=10.1093/hmg/7.8.1261;
Klose A., Ahmadian M.R., Schuelke M., Scheffzek K., Hoffmeyer S.,
Gewies A., Schmitz F., Kaufmann D., Peters H., Wittinghofer A.,
Nuernberg P.;
"Selective disactivation of neurofibromin GAP activity in
neurofibromatosis type 1 (NF1).";
Hum. Mol. Genet. 7:1261-1268(1998).
[54]
VARIANT NF1 GLY-1204, AND VARIANT HIS-765.
PubMed=10336779;
DOI=10.1002/(SICI)1098-1004(1998)11:5<411::AID-HUMU11>3.0.CO;2-2;
Krkljus S., Abernathy C.R., Johnson J.S., Williams C.A.,
Driscoll D.J., Zori R., Stalker H.J., Rasmussen S.A., Collins F.S.,
Kousseff B.G., Baumbach L., Wallace M.R.;
"Analysis of CpG C-to-T mutations in neurofibromatosis type 1.";
Hum. Mutat. 11:411-411(1998).
[55]
VARIANT NF1 PRO-508.
PubMed=11258625;
Messiaen L.M., Callens T., Roux K.J., Mortier G.R., De Paepe A.,
Abramowicz M., Pericak-Vance M.A., Vance J.M., Wallace M.R.;
"Exon 10b of the NF1 gene represents a mutational hotspot and harbors
a recurrent missense mutation Y489C associated with aberrant
splicing.";
Genet. Med. 1:248-253(1999).
[56]
VARIANT NF1 PRO-1446.
PubMed=10220149;
DOI=10.1002/(SICI)1098-1004(1999)13:4<337::AID-HUMU12>3.0.CO;2-F;
Peters H., Hess D., Fahsold R., Schuelke M.;
"A novel mutation L1425P in the GAP-region of the NF1 gene detected by
temperature gradient gel electrophoresis (TGGE).";
Hum. Mutat. 13:337-337(1999).
[57]
VARIANTS NF1 PRO-216; PRO-357; CYS-491; PRO-549; THR-581; ARG-583;
PHE-665; PRO-695; PRO-763; SER-777; LYS-780; PRO-781; PRO-847;
SER-1156; PRO-1250; GLN-1276; PRO-1276; PRO-1446; VAL-1605 AND
ILE-2507, AND VARIANT GLU-176.
PubMed=10712197; DOI=10.1086/302809;
Fahsold R., Hoffmeyer S., Mischung C., Gille C., Ehlers C.,
Kuecuekceylan N., Abdel-Nour M., Gewies A., Peters H., Kaufmann D.,
Buske A., Tinschert S., Nuernberg P.;
"Minor lesion mutational spectrum of the entire NF1 gene does not
explain its high mutability but points to a functional domain upstream
of the GAP-related domain.";
Am. J. Hum. Genet. 66:790-818(2000).
[58]
VARIANTS NF1 SER-117; TRP-1204; PRO-1446 AND 2387-ASN-PHE-2388 DEL.
PubMed=10607834; DOI=10.1093/hmg/9.2.237;
Ars E., Serra E., Garcia J., Kruyer H., Gaona A., Lazaro C.,
Estivill X.;
"Mutations affecting mRNA splicing are the most common molecular
defects in patients with neurofibromatosis type 1.";
Hum. Mol. Genet. 9:237-247(2000).
[59]
ERRATUM.
Ars E., Serra E., Garcia J., Kruyer H., Gaona A., Lazaro C.,
Estivill X.;
Hum. Mol. Genet. 9:659-659(2000).
[60]
VARIANT NF1 PHE-844.
PubMed=10980545;
DOI=10.1002/1098-1004(200009)16:3<274::AID-HUMU21>3.3.CO;2-6;
Boulandet E.G., Pantel J., Cazeneuve C., Van Gijn M., Vidaud D.,
Lemay S., Martin J., Zeller J., Revuz J., Goossens M., Amselem S.,
Wolkenstein P.;
"NF1 gene analysis focused on CpG-rich exons in a cohort of 93
patients with neurofibromatosis type 1.";
Hum. Mutat. 16:274-275(2000).
[61]
VARIANT SPINAL FSNF PRO-2088.
PubMed=11704931; DOI=10.1086/324648;
Kaufmann D., Mueller R., Bartelt B., Wolf M., Kunzi-Rapp K.,
Hanemann C.O., Fahsold R., Hein C., Vogel W., Assum G.;
"Spinal neurofibromatosis without cafe-au-lait macules in two families
with null mutations of the NF1 gene.";
Am. J. Hum. Genet. 69:1395-1400(2001).
[62]
VARIANTS NF1 LYS-780; CYS-784; PRO-1147; CYS-1193; ARG-1444; SER-1785;
ASN-2012 AND LYS-2357.
PubMed=11735023; DOI=10.1007/s004390100594;
Han S.S., Cooper D.N., Upadhyaya M.N.;
"Evaluation of denaturing high performance liquid chromatography
(DHPLC) for the mutational analysis of the neurofibromatosis type 1 (
NF1) gene.";
Hum. Genet. 109:487-497(2001).
[63]
VARIANTS NF1 PHE-82; ARG-784 AND GLU-1444.
PubMed=11857752; DOI=10.1002/humu.9018;
Kluwe L., Friedrich R.E., Korf B., Fahsold R., Mautner V.-F.;
"NF1 mutations in neurofibromatosis 1 patients with plexiform
neurofibromas.";
Hum. Mutat. 19:309-309(2002).
[64]
VARIANT NFNS GLU-1459 DEL.
PubMed=12707950; DOI=10.1002/ajmg.a.20023;
Baralle D., Mattocks C., Kalidas K., Elmslie F., Whittaker J.,
Lees M., Ragge N., Patton M.A., Winter R.M., ffrench-Constant C.;
"Different mutations in the NF1 gene are associated with
neurofibromatosis-Noonan syndrome (NFNS).";
Am. J. Med. Genet. A 119:1-8(2003).
[65]
VARIANTS NF1 TYR-93; VAL-604; ARG-844 AND PRO-898, AND VARIANTS
ASP-74; GLU-176; ARG-712 AND GLN-1276.
PubMed=12522551; DOI=10.1007/s00439-002-0858-4;
Wang Q., Montmain G., Ruano E., Upadhyaya M., Dudley S., Liskay R.M.,
Thibodeau S.N., Puisieux A.;
"Neurofibromatosis type 1 gene as a mutational target in a mismatch
repair-deficient cell type.";
Hum. Genet. 112:117-123(2003).
[66]
VARIANTS NF1 LYS-780; PRO-847; GLU-848 AND ARG-968; ASN-1444; LEU-1953
DEL AND ARG-2001.
PubMed=12552569; DOI=10.1002/humu.9111;
De Luca A., Buccino A., Gianni D., Mangino M., Giustini S.,
Richetta A., Divona L., Calvieri S., Mingarelli R., Dallapiccola B.;
"NF1 gene analysis based on DHPLC.";
Hum. Mutat. 21:171-172(2003).
[67]
VARIANTS NF1 ARG-578; PRO-920 AND ALA-2221.
PubMed=12746402; DOI=10.1136/jmg.40.5.368;
Kluwe L., Tatagiba M., Fuensterer C., Mautner V.F.;
"NF1 mutations and clinical spectrum in patients with spinal
neurofibromas.";
J. Med. Genet. 40:368-371(2003).
[68]
VARIANT NF1 VAL-186, AND CHARACTERIZATION OF VARIANT NF1 VAL-186.
PubMed=15523642; DOI=10.1002/humu.20103;
Zatkova A., Messiaen L., Vandenbroucke I., Wieser R., Fonatsch C.,
Krainer A.R., Wimmer K.;
"Disruption of exonic splicing enhancer elements is the principal
cause of exon skipping associated with seven nonsense or missense
alleles of NF1.";
Hum. Mutat. 24:491-501(2004).
[69]
VARIANTS NF1 ASN-157; ARG-629; SER-777; LYS-780; ARG-784; PRO-847;
GLU-848; ARG-968; ASN-1444; LEU-1953 DEL AND ARG-2001, AND VARIANT
GLU-176.
PubMed=15146469; DOI=10.1002/humu.9245;
De Luca A., Schirinzi A., Buccino A., Bottillo I., Sinibaldi L.,
Torrente I., Ciavarella A., Dottorini T., Porciello R., Giustini S.,
Calvieri S., Dallapiccola B.;
"Novel and recurrent mutations in the NF1 gene in Italian patients
with neurofibromatosis type 1.";
Hum. Mutat. 23:629-629(2004).
[70]
VARIANTS NF1 ARG-31; PRO-145; ARG-324; VAL-337; CYS-489; PRO-532;
ARG-574; ARG-629; PHE-665; PHE-844; PRO-844; MET-991 DEL; VAL-1073;
ARG-1196; GLY-1276; GLN-1276; GLU-1430; GLU-1459 DEL AND GLY-1489, AND
VARIANTS GLU-176 AND CYS-873.
PubMed=15060124; DOI=10.1136/jmg.2003.011890;
Mattocks C., Baralle D., Tarpey P., ffrench-Constant C., Bobrow M.,
Whittaker J.;
"Automated comparative sequence analysis identifies mutations in 89%
of NF1 patients and confirms a mutation cluster in exons 11-17
distinct from the GAP related domain.";
J. Med. Genet. 41:E48-E48(2004).
[71]
VARIANT NF1 PRO-1243.
PubMed=15520408; DOI=10.1136/jmg.2004.021683;
Ferner R.E., Hughes R.A.C., Hall S.M., Upadhyaya M., Johnson M.R.;
"Neurofibromatous neuropathy in neurofibromatosis 1 (NF1).";
J. Med. Genet. 41:837-841(2004).
[72]
VARIANT NF1 ARG-844.
PubMed=15948193; DOI=10.1002/ajmg.a.30813;
Bertola D.R., Pereira A.C., Passetti F., de Oliveira P.S.L.,
Messiaen L., Gelb B.D., Kim C.A., Krieger J.E.;
"Neurofibromatosis-Noonan syndrome: molecular evidence of the
concurrence of both disorders in a patient.";
Am. J. Med. Genet. A 136:242-245(2005).
[73]
VARIANTS NFNS ARG-194; GLU-1444; THR-1451; LEU-1453 AND GLU-1459 DEL.
PubMed=16380919; DOI=10.1086/498454;
De Luca A., Bottillo I., Sarkozy A., Carta C., Neri C., Bellacchio E.,
Schirinzi A., Conti E., Zampino G., Battaglia A., Majore S.,
Rinaldi M.M., Carella M., Marino B., Pizzuti A., Digilio M.C.,
Tartaglia M., Dallapiccola B.;
"NF1 gene mutations represent the major molecular event underlying
neurofibromatosis-Noonan syndrome.";
Am. J. Hum. Genet. 77:1092-1101(2005).
[74]
VARIANTS [LARGE SCALE ANALYSIS] ILE-1187; LEU-1951 AND ARG-2745.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[75]
VARIANT NF1 MET-991 DEL.
PubMed=17160901; DOI=10.1086/510781;
Upadhyaya M., Huson S.M., Davies M., Thomas N., Chuzhanova N.,
Giovannini S., Evans D.G., Howard E., Kerr B., Griffiths S.,
Consoli C., Side L., Adams D., Pierpont M., Hachen R., Barnicoat A.,
Li H., Wallace P., Van Biervliet J.P., Stevenson D., Viskochil D.,
Baralle D., Haan E., Riccardi V., Turnpenny P., Lazaro C.,
Messiaen L.;
"An absence of cutaneous neurofibromas associated with a 3-bp inframe
deletion in exon 17 of the NF1 gene (c.2970-2972 delAAT): evidence of
a clinically significant NF1 genotype-phenotype correlation.";
Am. J. Hum. Genet. 80:140-151(2007).
[76]
VARIANT NFNS PHE-1411.
PubMed=19845691; DOI=10.1111/j.1399-0004.2009.01233.x;
Nystrom A.M., Ekvall S., Allanson J., Edeby C., Elinder M.,
Holmstrom G., Bondeson M.L., Anneren G.;
"Noonan syndrome and neurofibromatosis type I in a family with a novel
mutation in NF1.";
Clin. Genet. 76:524-534(2009).
[77]
VARIANT NF1 THR-160.
PubMed=21838856; DOI=10.1186/1897-4287-9-6;
Ponti G., Losi L., Martorana D., Priola M., Boni E., Pollio A.,
Neri T.M., Seidenari S.;
"Clinico-pathological and biomolecular findings in Italian patients
with multiple cutaneous neurofibromas.";
Hered. Cancer Clin. Pract. 9:6-6(2011).
[78]
VARIANTS GLU-176; THR-330; ASP-393; LEU-393; PRO-519; THR-776 AND
PHE-1484.
PubMed=22108604; DOI=10.1038/ejhg.2011.207;
Thomas L., Spurlock G., Eudall C., Thomas N.S., Mort M., Hamby S.E.,
Chuzhanova N., Brems H., Legius E., Cooper D.N., Upadhyaya M.;
"Exploring the somatic NF1 mutational spectrum associated with NF1
cutaneous neurofibromas.";
Eur. J. Hum. Genet. 20:411-419(2012).
[79]
VARIANTS NF1 TRP-93; ARG-1048; ARG-1189; ARG-1661 (ISOFORM 1) AND
THR-1918 (ISOFORM 1).
PubMed=23758643; DOI=10.1111/ahg.12026;
Nemethova M., Bolcekova A., Ilencikova D., Durovcikova D.,
Hlinkova K., Hlavata A., Kovacs L., Kadasi L., Zatkova A.;
"Thirty-nine novel neurofibromatosis 1 (NF1) gene mutations identified
in Slovak patients.";
Ann. Hum. Genet. 77:364-379(2013).
[80]
VARIANT NF1 PRO-2125.
PubMed=24413922; DOI=10.1007/s00381-013-2352-9;
Ben-Salem S., Al-Shamsi A.M., Ali B.R., Al-Gazali L.;
"The mutational spectrum of the NF1 gene in neurofibromatosis type I
patients from UAE.";
Childs Nerv. Syst. 30:1183-1189(2014).
-!- FUNCTION: Stimulates the GTPase activity of Ras. NF1 shows greater
affinity for Ras GAP, but lower specific activity. May be a
regulator of Ras activity. {ECO:0000269|PubMed:2121371,
ECO:0000269|PubMed:8417346}.
-!- SUBUNIT: Interacts with HTR6 (PubMed:23027611).
{ECO:0000269|PubMed:23027611}.
-!- INTERACTION:
P05067:APP; NbExp=3; IntAct=EBI-1172917, EBI-77613;
P34741:SDC2; NbExp=4; IntAct=EBI-1172917, EBI-1172957;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14988005}.
Nucleus, nucleolus {ECO:0000269|PubMed:14988005}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Comment=Experimental confirmation may be lacking for some
isoforms.;
Name=2; Synonyms=Type II;
IsoId=P21359-1; Sequence=Displayed;
Name=1; Synonyms=Type I;
IsoId=P21359-2; Sequence=VSP_001628;
Note=Variant in position: 1661:C->R (in NF1). Variant in
position: 1918:I->T (in NF1). {ECO:0000269|PubMed:23758643};
Name=3;
IsoId=P21359-3; Sequence=VSP_001629, VSP_001630;
Name=4;
IsoId=P21359-4; Sequence=VSP_001631, VSP_001632;
Name=5;
IsoId=P21359-5; Sequence=VSP_043467, VSP_043468;
Name=6;
IsoId=P21359-6; Sequence=VSP_001628, VSP_053587;
-!- TISSUE SPECIFICITY: Detected in brain, peripheral nerve, lung,
colon and muscle. {ECO:0000269|PubMed:8417346}.
-!- DOMAIN: Binds phospholipids via its C-terminal CRAL-TRIO domain.
Binds primarily glycerophospholipids with monounsaturated C18:1
and/or C16:1 fatty acid moieties and a phosphatidylethanolamine or
phosphatidylcholine headgroup. Has lesser affinity for lipids
containing phosphatidylserine and phosphatidylinositol.
{ECO:0000269|PubMed:16397625, ECO:0000269|PubMed:17187824,
ECO:0000269|PubMed:21089070}.
-!- RNA EDITING: Modified_positions=1306 {ECO:0000269|PubMed:11727199,
ECO:0000269|PubMed:8602361}; Note=The stop codon (UGA) at position
1306 is created by RNA editing. Various levels of RNA editing
occurs in peripheral nerve-sheath tumor samples (PNSTs) from
patients with NF1. Preferentially observed in transcripts
containing exon 23A.;
-!- DISEASE: Neurofibromatosis 1 (NF1) [MIM:162200]: A disease
characterized by patches of skin pigmentation (cafe-au-lait
spots), Lisch nodules of the iris, tumors in the peripheral
nervous system and fibromatous skin tumors. Individuals with the
disorder have increased susceptibility to the development of
benign and malignant tumors. {ECO:0000269|PubMed:10220149,
ECO:0000269|PubMed:10336779, ECO:0000269|PubMed:10607834,
ECO:0000269|PubMed:10712197, ECO:0000269|PubMed:10980545,
ECO:0000269|PubMed:11258625, ECO:0000269|PubMed:11735023,
ECO:0000269|PubMed:11857752, ECO:0000269|PubMed:12522551,
ECO:0000269|PubMed:12552569, ECO:0000269|PubMed:12746402,
ECO:0000269|PubMed:1302608, ECO:0000269|PubMed:15060124,
ECO:0000269|PubMed:15146469, ECO:0000269|PubMed:15520408,
ECO:0000269|PubMed:15523642, ECO:0000269|PubMed:15948193,
ECO:0000269|PubMed:17160901, ECO:0000269|PubMed:21089070,
ECO:0000269|PubMed:2114220, ECO:0000269|PubMed:21838856,
ECO:0000269|PubMed:23758643, ECO:0000269|PubMed:24413922,
ECO:0000269|PubMed:7981679, ECO:0000269|PubMed:8081387,
ECO:0000269|PubMed:8544190, ECO:0000269|PubMed:8807336,
ECO:0000269|PubMed:8834249, ECO:0000269|PubMed:9003501,
ECO:0000269|PubMed:9101300, ECO:0000269|PubMed:9150739,
ECO:0000269|PubMed:9298829, ECO:0000269|PubMed:9668168}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An
aggressive pediatric myelodysplastic syndrome/myeloproliferative
disorder characterized by malignant transformation in the
hematopoietic stem cell compartment with proliferation of
differentiated progeny. Patients have splenomegaly, enlarged lymph
nodes, rashes, and hemorrhages. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Watson syndrome (WTSN) [MIM:193520]: A syndrome
characterized by the presence of pulmonary stenosis, cafe-au-lait
spots, and mental retardation. It is considered as an atypical
form of neurofibromatosis. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- DISEASE: Familial spinal neurofibromatosis (FSNF) [MIM:162210]:
Considered to be an alternative form of neurofibromatosis, showing
multiple spinal tumors. {ECO:0000269|PubMed:11704931}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Neurofibromatosis-Noonan syndrome (NFNS) [MIM:601321]:
Characterized by manifestations of both NF1 and Noonan syndrome
(NS). NS is a disorder characterized by dysmorphic facial
features, short stature, hypertelorism, cardiac anomalies,
deafness, motor delay, and a bleeding diathesis.
{ECO:0000269|PubMed:12707950, ECO:0000269|PubMed:16380919,
ECO:0000269|PubMed:19845691}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Colorectal cancer (CRC) [MIM:114500]: A complex disease
characterized by malignant lesions arising from the inner wall of
the large intestine (the colon) and the rectum. Genetic
alterations are often associated with progression from
premalignant lesion (adenoma) to invasive adenocarcinoma. Risk
factors for cancer of the colon and rectum include colon polyps,
long-standing ulcerative colitis, and genetic family history.
Note=The gene represented in this entry may be involved in disease
pathogenesis.
-!- CAUTION: Was originally thought to be associated with LEOPARD
(LS), an autosomal dominant syndrome.
{ECO:0000305|PubMed:8807336}.
-!- SEQUENCE CAUTION:
Sequence=AAA59923.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/NF1ID134.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/nf1/";
-!- WEB RESOURCE: Name=Mendelian genes neurofibromin 1 (NF1);
Note=Leiden Open Variation Database (LOVD);
URL="http://www.lovd.nl/NF1";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M89914; AAA59925.1; -; mRNA.
EMBL; M82814; AAA59924.1; -; mRNA.
EMBL; M60496; AAA59928.1; -; mRNA.
EMBL; D12625; BAA02150.1; -; mRNA.
EMBL; M38106; AAA74897.1; -; mRNA.
EMBL; M38107; AAB59558.1; -; mRNA.
EMBL; D42072; BAA07669.1; -; mRNA.
EMBL; AY796305; AAV50004.1; -; Genomic_DNA.
EMBL; AC004222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC079915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC134669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC135724; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC138207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC139072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471147; EAW80272.1; -; Genomic_DNA.
EMBL; CH471147; EAW80275.1; -; Genomic_DNA.
EMBL; AH000834; AAA18483.1; -; Genomic_DNA.
EMBL; Y07853; CAA69179.1; -; Genomic_DNA.
EMBL; U17690; AAB48380.1; -; Genomic_DNA.
EMBL; U17680; AAB48380.1; JOINED; Genomic_DNA.
EMBL; U17681; AAB48380.1; JOINED; Genomic_DNA.
EMBL; U17682; AAB48380.1; JOINED; Genomic_DNA.
EMBL; U17683; AAB48380.1; JOINED; Genomic_DNA.
EMBL; U17684; AAB48380.1; JOINED; Genomic_DNA.
EMBL; U17685; AAB48380.1; JOINED; Genomic_DNA.
EMBL; U17686; AAB48380.1; JOINED; Genomic_DNA.
EMBL; U17687; AAB48380.1; JOINED; Genomic_DNA.
EMBL; U17688; AAB48380.1; JOINED; Genomic_DNA.
EMBL; U17689; AAB48380.1; JOINED; Genomic_DNA.
EMBL; U17690; AAB48379.1; -; Genomic_DNA.
EMBL; U17680; AAB48379.1; JOINED; Genomic_DNA.
EMBL; U17681; AAB48379.1; JOINED; Genomic_DNA.
EMBL; U17682; AAB48379.1; JOINED; Genomic_DNA.
EMBL; U17683; AAB48379.1; JOINED; Genomic_DNA.
EMBL; U17684; AAB48379.1; JOINED; Genomic_DNA.
EMBL; U17685; AAB48379.1; JOINED; Genomic_DNA.
EMBL; U17687; AAB48379.1; JOINED; Genomic_DNA.
EMBL; U17688; AAB48379.1; JOINED; Genomic_DNA.
EMBL; U17689; AAB48379.1; JOINED; Genomic_DNA.
EMBL; U17656; AAB48373.1; -; Genomic_DNA.
EMBL; U17659; AAB48374.1; -; Genomic_DNA.
EMBL; U17662; AAB48375.1; -; Genomic_DNA.
EMBL; U17668; AAB48376.1; -; Genomic_DNA.
EMBL; U17667; AAB48376.1; JOINED; Genomic_DNA.
EMBL; U17673; AAB48377.1; -; Genomic_DNA.
EMBL; U17677; AAB48378.1; -; Genomic_DNA.
EMBL; U17676; AAB48378.1; JOINED; Genomic_DNA.
EMBL; M60915; AAA59921.1; -; mRNA.
EMBL; M60915; AAA59922.1; -; mRNA.
EMBL; M61213; AAA59923.1; ALT_INIT; mRNA.
EMBL; S51751; AAB24636.1; -; mRNA.
EMBL; D10490; BAA01371.1; -; mRNA.
CCDS; CCDS11264.1; -. [P21359-2]
CCDS; CCDS42292.1; -. [P21359-1]
CCDS; CCDS45645.1; -. [P21359-5]
PIR; B55282; B55282.
PIR; I78852; I78852.
RefSeq; NP_000258.1; NM_000267.3. [P21359-2]
RefSeq; NP_001035957.1; NM_001042492.2. [P21359-1]
RefSeq; NP_001121619.1; NM_001128147.2. [P21359-5]
UniGene; Hs.113577; -.
PDB; 1NF1; X-ray; 2.50 A; A=1198-1551.
PDB; 2D4Q; X-ray; 2.30 A; A/B=1581-1837.
PDB; 2E2X; X-ray; 2.50 A; A/B=1566-1837.
PDB; 3P7Z; X-ray; 2.65 A; A/B=1566-1837.
PDB; 3PEG; X-ray; 2.52 A; A=1566-1837.
PDB; 3PG7; X-ray; 2.19 A; A/B=1581-1837.
PDBsum; 1NF1; -.
PDBsum; 2D4Q; -.
PDBsum; 2E2X; -.
PDBsum; 3P7Z; -.
PDBsum; 3PEG; -.
PDBsum; 3PG7; -.
ProteinModelPortal; P21359; -.
SMR; P21359; -.
BioGrid; 110836; 103.
IntAct; P21359; 12.
MINT; MINT-1504522; -.
STRING; 9606.ENSP00000351015; -.
iPTMnet; P21359; -.
PhosphoSitePlus; P21359; -.
BioMuta; NF1; -.
DMDM; 548350; -.
EPD; P21359; -.
MaxQB; P21359; -.
PaxDb; P21359; -.
PeptideAtlas; P21359; -.
PRIDE; P21359; -.
Ensembl; ENST00000356175; ENSP00000348498; ENSG00000196712. [P21359-2]
Ensembl; ENST00000358273; ENSP00000351015; ENSG00000196712. [P21359-1]
Ensembl; ENST00000431387; ENSP00000412921; ENSG00000196712. [P21359-5]
Ensembl; ENST00000487476; ENSP00000491589; ENSG00000196712. [P21359-3]
GeneID; 4763; -.
KEGG; hsa:4763; -.
UCSC; uc002hgf.3; human. [P21359-1]
CTD; 4763; -.
DisGeNET; 4763; -.
EuPathDB; HostDB:ENSG00000196712.16; -.
GeneCards; NF1; -.
GeneReviews; NF1; -.
HGNC; HGNC:7765; NF1.
HPA; HPA045502; -.
MalaCards; NF1; -.
MIM; 114500; phenotype.
MIM; 162200; phenotype.
MIM; 162210; phenotype.
MIM; 193520; phenotype.
MIM; 601321; phenotype.
MIM; 607785; phenotype.
MIM; 613113; gene.
neXtProt; NX_P21359; -.
OpenTargets; ENSG00000196712; -.
Orphanet; 97685; 17q11 microdeletion syndrome.
Orphanet; 139474; 17q11.2 microduplication syndrome.
Orphanet; 86834; Juvenile myelomonocytic leukemia.
Orphanet; 363700; Neurofibromatosis type 1 due to NF1mutation or intragenic deletion.
Orphanet; 638; Neurofibromatosis-Noonan syndrome.
PharmGKB; PA31572; -.
eggNOG; KOG1826; Eukaryota.
eggNOG; ENOG410XRPJ; LUCA.
GeneTree; ENSGT00550000074797; -.
HOGENOM; HOG000047020; -.
HOVERGEN; HBG006486; -.
InParanoid; P21359; -.
KO; K08052; -.
OMA; YYAKPYE; -.
OrthoDB; EOG091G03FI; -.
PhylomeDB; P21359; -.
TreeFam; TF300302; -.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-6802949; Signaling by RAS mutants.
Reactome; R-HSA-6802953; RAS signaling downstream of NF1 loss-of-function variants.
Reactome; R-HSA-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
SignaLink; P21359; -.
SIGNOR; P21359; -.
ChiTaRS; NF1; human.
EvolutionaryTrace; P21359; -.
GeneWiki; Neurofibromin_1; -.
GenomeRNAi; 4763; -.
PRO; PR:P21359; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000196712; -.
CleanEx; HS_NF1; -.
ExpressionAtlas; P21359; baseline and differential.
Genevisible; P21359; HS.
GO; GO:0030424; C:axon; IDA:HGNC.
GO; GO:0005737; C:cytoplasm; ISS:HGNC.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030425; C:dendrite; IDA:HGNC.
GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISS:HGNC.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
GO; GO:0031210; F:phosphatidylcholine binding; IDA:UniProtKB.
GO; GO:0008429; F:phosphatidylethanolamine binding; IDA:UniProtKB.
GO; GO:0030036; P:actin cytoskeleton organization; ISS:HGNC.
GO; GO:0030325; P:adrenal gland development; ISS:HGNC.
GO; GO:0021764; P:amygdala development; IEA:Ensembl.
GO; GO:0048844; P:artery morphogenesis; ISS:HGNC.
GO; GO:0007420; P:brain development; ISS:HGNC.
GO; GO:0048593; P:camera-type eye morphogenesis; ISS:HGNC.
GO; GO:0007154; P:cell communication; ISS:HGNC.
GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
GO; GO:0021987; P:cerebral cortex development; ISS:HGNC.
GO; GO:0050890; P:cognition; IMP:HGNC.
GO; GO:0030199; P:collagen fibril organization; ISS:HGNC.
GO; GO:0030198; P:extracellular matrix organization; ISS:HGNC.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
GO; GO:0021897; P:forebrain astrocyte development; ISS:HGNC.
GO; GO:0048853; P:forebrain morphogenesis; ISS:HGNC.
GO; GO:0061534; P:gamma-aminobutyric acid secretion, neurotransmission; IEA:Ensembl.
GO; GO:0061535; P:glutamate secretion, neurotransmission; IEA:Ensembl.
GO; GO:0048820; P:hair follicle maturation; IEA:Ensembl.
GO; GO:0007507; P:heart development; ISS:HGNC.
GO; GO:0001889; P:liver development; ISS:HGNC.
GO; GO:0000165; P:MAPK cascade; ISS:HGNC.
GO; GO:0001656; P:metanephros development; ISS:HGNC.
GO; GO:0022011; P:myelination in peripheral nervous system; ISS:HGNC.
GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
GO; GO:0048712; P:negative regulation of astrocyte differentiation; IEA:Ensembl.
GO; GO:0030336; P:negative regulation of cell migration; IMP:MGI.
GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IEA:Ensembl.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IMP:HGNC.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISS:UniProtKB.
GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:HGNC.
GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:MGI.
GO; GO:0007406; P:negative regulation of neuroblast proliferation; ISS:HGNC.
GO; GO:0046929; P:negative regulation of neurotransmitter secretion; IEA:Ensembl.
GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; ISS:HGNC.
GO; GO:0045671; P:negative regulation of osteoclast differentiation; IEA:Ensembl.
GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:HGNC.
GO; GO:0035021; P:negative regulation of Rac protein signal transduction; IEA:Ensembl.
GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IBA:GO_Central.
GO; GO:0042992; P:negative regulation of transcription factor import into nucleus; ISS:HGNC.
GO; GO:0021915; P:neural tube development; IEA:Ensembl.
GO; GO:0098597; P:observational learning; IEA:Ensembl.
GO; GO:0001649; P:osteoblast differentiation; ISS:HGNC.
GO; GO:0007422; P:peripheral nervous system development; ISS:HGNC.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISS:HGNC.
GO; GO:0043473; P:pigmentation; ISS:HGNC.
GO; GO:0045762; P:positive regulation of adenylate cyclase activity; ISS:HGNC.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:HGNC.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:HGNC.
GO; GO:0007265; P:Ras protein signal transduction; ISS:HGNC.
GO; GO:0045765; P:regulation of angiogenesis; IMP:HGNC.
GO; GO:0043535; P:regulation of blood vessel endothelial cell migration; IMP:HGNC.
GO; GO:0045124; P:regulation of bone resorption; ISS:HGNC.
GO; GO:0001952; P:regulation of cell-matrix adhesion; ISS:HGNC.
GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
GO; GO:0045685; P:regulation of glial cell differentiation; ISS:HGNC.
GO; GO:0043087; P:regulation of GTPase activity; IMP:HGNC.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
GO; GO:1900271; P:regulation of long-term synaptic potentiation; IEA:Ensembl.
GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; ISS:HGNC.
GO; GO:0014044; P:Schwann cell development; ISS:HGNC.
GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
GO; GO:0048745; P:smooth muscle tissue development; ISS:HGNC.
GO; GO:0021510; P:spinal cord development; ISS:HGNC.
GO; GO:0048485; P:sympathetic nervous system development; ISS:HGNC.
GO; GO:0008542; P:visual learning; ISS:HGNC.
GO; GO:0042060; P:wound healing; ISS:HGNC.
CDD; cd00170; SEC14; 1.
Gene3D; 1.25.10.10; -; 2.
Gene3D; 3.40.525.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR001251; CRAL-TRIO_dom.
InterPro; IPR036865; CRAL-TRIO_dom_sf.
InterPro; IPR023152; RasGAP_CS.
InterPro; IPR001936; RasGAP_dom.
InterPro; IPR008936; Rho_GTPase_activation_prot.
Pfam; PF13716; CRAL_TRIO_2; 1.
Pfam; PF00616; RasGAP; 1.
SMART; SM00323; RasGAP; 1.
SMART; SM00516; SEC14; 1.
SUPFAM; SSF48350; SSF48350; 1.
SUPFAM; SSF48371; SSF48371; 4.
PROSITE; PS50191; CRAL_TRIO; 1.
PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Disease mutation; GTPase activation; Lipid-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; RNA editing;
Tumor suppressor.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P97526}.
CHAIN 2 2839 Neurofibromin.
/FTId=PRO_0000010773.
CHAIN 2 1305 Neurofibromin truncated.
/FTId=PRO_0000010774.
DOMAIN 1235 1451 Ras-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00167}.
DOMAIN 1580 1738 CRAL-TRIO. {ECO:0000255|PROSITE-
ProRule:PRU00056}.
REGION 1580 1837 Lipid binding.
MOTIF 2555 2571 Bipartite nuclear localization signal.
COMPBIAS 1352 1355 Poly-Ser.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P97526}.
MOD_RES 864 864 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 876 876 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 2188 2188 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 2467 2467 Phosphoserine.
{ECO:0000250|UniProtKB:Q04690}.
MOD_RES 2514 2514 Phosphothreonine.
{ECO:0000250|UniProtKB:Q04690}.
MOD_RES 2515 2515 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 2521 2521 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 2523 2523 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2543 2543 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 2565 2565 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2597 2597 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2802 2802 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2817 2817 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 548 551 ALLV -> VRGK (in isoform 3).
{ECO:0000303|PubMed:1339276}.
/FTId=VSP_001629.
VAR_SEQ 552 2839 Missing (in isoform 3).
{ECO:0000303|PubMed:1339276}.
/FTId=VSP_001630.
VAR_SEQ 574 593 SSQMLFYICKKLTSHQMLSS -> RYMYFYFLNSTFKFYFV
FLS (in isoform 5).
{ECO:0000303|PubMed:7570581}.
/FTId=VSP_043467.
VAR_SEQ 594 2839 Missing (in isoform 5).
{ECO:0000303|PubMed:7570581}.
/FTId=VSP_043468.
VAR_SEQ 1371 1391 Missing (in isoform 1 and isoform 6).
{ECO:0000303|PubMed:1457041,
ECO:0000303|PubMed:1783401,
ECO:0000303|PubMed:1923522,
ECO:0000303|PubMed:2114220,
ECO:0000303|PubMed:2116237,
ECO:0000303|PubMed:2134734}.
/FTId=VSP_001628.
VAR_SEQ 1591 1598 SIFYQAGT -> TPPPEPET (in isoform 4).
{ECO:0000303|PubMed:2121370}.
/FTId=VSP_001631.
VAR_SEQ 1599 2839 Missing (in isoform 4).
{ECO:0000303|PubMed:2121370}.
/FTId=VSP_001632.
VAR_SEQ 2792 2792 P -> PASLPCSNSAVFMQLFPHQ (in isoform 6).
{ECO:0000303|PubMed:2116237}.
/FTId=VSP_053587.
VARIANT 31 31 H -> R (in NF1; dbSNP:rs199474725).
{ECO:0000269|PubMed:15060124}.
/FTId=VAR_032459.
VARIANT 74 74 A -> D (in mismatch repair deficient
cancer cells; dbSNP:rs199474726).
{ECO:0000269|PubMed:12522551}.
/FTId=VAR_017550.
VARIANT 80 80 Y -> C (in dbSNP:rs4795581).
{ECO:0000269|Ref.7}.
/FTId=VAR_022254.
VARIANT 80 80 Y -> S (in dbSNP:rs4795581).
/FTId=VAR_049135.
VARIANT 82 82 S -> F (in NF1; dbSNP:rs199474729).
{ECO:0000269|PubMed:11857752}.
/FTId=VAR_021730.
VARIANT 93 93 C -> W (in NF1).
{ECO:0000269|PubMed:23758643}.
/FTId=VAR_071668.
VARIANT 93 93 C -> Y (in NF1; dbSNP:rs199474728).
{ECO:0000269|PubMed:12522551}.
/FTId=VAR_017551.
VARIANT 117 117 I -> S (in NF1; dbSNP:rs199474731).
{ECO:0000269|PubMed:10607834}.
/FTId=VAR_010989.
VARIANT 145 145 L -> P (in NF1; dbSNP:rs199474734).
{ECO:0000269|PubMed:15060124}.
/FTId=VAR_032460.
VARIANT 157 157 I -> N (in NF1; dbSNP:rs199474744).
{ECO:0000269|PubMed:15146469}.
/FTId=VAR_021731.
VARIANT 160 160 R -> T (in NF1; dbSNP:rs199474752).
{ECO:0000269|PubMed:21838856}.
/FTId=VAR_065888.
VARIANT 176 176 D -> E (found in mismatch repair
deficient cancer cells; also found in a
cutaneous neurofibroma from a patient
with neurofibromatosis; somatic mutation;
dbSNP:rs112306990).
{ECO:0000269|PubMed:10712197,
ECO:0000269|PubMed:12522551,
ECO:0000269|PubMed:15060124,
ECO:0000269|PubMed:15146469,
ECO:0000269|PubMed:22108604}.
/FTId=VAR_017552.
VARIANT 186 186 D -> V (in NF1; reduced splicing
enhancement).
{ECO:0000269|PubMed:15523642}.
/FTId=VAR_032461.
VARIANT 194 194 L -> R (in NFNS; dbSNP:rs199474753).
{ECO:0000269|PubMed:16380919}.
/FTId=VAR_032462.
VARIANT 216 216 L -> P (in NF1; dbSNP:rs199474756).
{ECO:0000269|PubMed:10712197}.
/FTId=VAR_021732.
VARIANT 324 324 C -> R (in NF1; dbSNP:rs199474735).
{ECO:0000269|PubMed:15060124}.
/FTId=VAR_032463.
VARIANT 330 330 A -> T (in a cutaneous neurofibroma from
a patient with neurofibromatosis; somatic
mutation; dbSNP:rs199474767).
{ECO:0000269|PubMed:22108604}.
/FTId=VAR_067201.
VARIANT 337 337 E -> V (in NF1; dbSNP:rs199474736).
{ECO:0000269|PubMed:15060124}.
/FTId=VAR_032464.
VARIANT 338 338 D -> G (in NF1; dbSNP:rs199474773).
{ECO:0000269|PubMed:9298829}.
/FTId=VAR_010990.
VARIANT 357 357 L -> P (in NF1; dbSNP:rs137854563).
{ECO:0000269|PubMed:10712197}.
/FTId=VAR_021733.
VARIANT 393 393 H -> D (in a cutaneous neurofibroma from
a patient with neurofibromatosis; somatic
mutation; dbSNP:rs199474768).
{ECO:0000269|PubMed:22108604}.
/FTId=VAR_067202.
VARIANT 393 393 H -> L (in a cutaneous neurofibroma from
a patient with neurofibromatosis; somatic
mutation; dbSNP:rs199474769).
{ECO:0000269|PubMed:22108604}.
/FTId=VAR_067203.
VARIANT 489 489 Y -> C (in NF1; dbSNP:rs137854557).
{ECO:0000269|PubMed:15060124}.
/FTId=VAR_032465.
VARIANT 491 491 Y -> C (in NF1; dbSNP:rs199474757).
{ECO:0000269|PubMed:10712197}.
/FTId=VAR_021734.
VARIANT 508 508 L -> P (in NF1; dbSNP:rs137854558).
{ECO:0000269|PubMed:11258625}.
/FTId=VAR_010991.
VARIANT 519 519 Q -> P (in a cutaneous neurofibroma from
a patient with neurofibromatosis; somatic
mutation; dbSNP:rs199474770).
{ECO:0000269|PubMed:22108604}.
/FTId=VAR_067204.
VARIANT 532 532 L -> P (in NF1; dbSNP:rs199474737).
{ECO:0000269|PubMed:15060124}.
/FTId=VAR_032466.
VARIANT 549 549 L -> P (in NF1; dbSNP:rs199474758).
{ECO:0000269|PubMed:10712197}.
/FTId=VAR_021735.
VARIANT 574 574 S -> R (in NF1).
{ECO:0000269|PubMed:15060124}.
/FTId=VAR_032467.
VARIANT 578 578 L -> R (in NF1; dbSNP:rs199474774).
{ECO:0000269|PubMed:12746402}.
/FTId=VAR_021736.
VARIANT 581 581 I -> T (in NF1; dbSNP:rs199474759).
{ECO:0000269|PubMed:10712197}.
/FTId=VAR_021737.
VARIANT 583 583 K -> R (in NF1; dbSNP:rs199474760).
{ECO:0000269|PubMed:10712197}.
/FTId=VAR_021738.
VARIANT 604 604 L -> V (in NF1; dbSNP:rs142712751).
{ECO:0000269|PubMed:12522551}.
/FTId=VAR_017553.
VARIANT 629 629 G -> R (in NF1; affects splicing by
creating a novel splice acceptor site;
dbSNP:rs199474738).
{ECO:0000269|PubMed:15060124,
ECO:0000269|PubMed:15146469,
ECO:0000269|PubMed:8834249}.
/FTId=VAR_002653.
VARIANT 665 665 S -> F (in NF1; unknown pathological
significance; dbSNP:rs145891889).
{ECO:0000269|PubMed:10712197,
ECO:0000269|PubMed:15060124}.
/FTId=VAR_021739.
VARIANT 678 678 P -> L (in dbSNP:rs17881753).
{ECO:0000269|Ref.7}.
/FTId=VAR_022255.
VARIANT 695 695 L -> P (in NF1; dbSNP:rs199474761).
{ECO:0000269|PubMed:10712197}.
/FTId=VAR_021740.
VARIANT 712 712 H -> R (in mismatch repair deficient
cancer cells; dbSNP:rs199474727).
{ECO:0000269|PubMed:12522551}.
/FTId=VAR_017554.
VARIANT 763 763 L -> P (in NF1; dbSNP:rs199474762).
{ECO:0000269|PubMed:10712197}.
/FTId=VAR_021741.
VARIANT 765 765 R -> H (in dbSNP:rs199474777).
{ECO:0000269|PubMed:10336779}.
/FTId=VAR_021742.
VARIANT 776 776 A -> T (in a cutaneous neurofibroma from
a patient with neurofibromatosis; somatic
mutation; dbSNP:rs199474771).
{ECO:0000269|PubMed:22108604}.
/FTId=VAR_067205.
VARIANT 777 777 W -> S (in NF1; dbSNP:rs199474745).
{ECO:0000269|PubMed:10712197,
ECO:0000269|PubMed:15146469}.
/FTId=VAR_021743.
VARIANT 780 780 T -> K (in NF1; dbSNP:rs199474746).
{ECO:0000269|PubMed:10712197,
ECO:0000269|PubMed:11735023,
ECO:0000269|PubMed:12552569,
ECO:0000269|PubMed:15146469}.
/FTId=VAR_021744.
VARIANT 781 781 H -> P (in NF1; dbSNP:rs199474763).
{ECO:0000269|PubMed:10712197}.
/FTId=VAR_021745.
VARIANT 784 784 W -> C (in NF1; dbSNP:rs199474778).
{ECO:0000269|PubMed:11735023}.
/FTId=VAR_021746.
VARIANT 784 784 W -> R (in NF1; dbSNP:rs199474730).
{ECO:0000269|PubMed:11857752,
ECO:0000269|PubMed:15146469}.
/FTId=VAR_021747.
VARIANT 844 844 L -> F (in NF1; dbSNP:rs199474785).
{ECO:0000269|PubMed:10980545,
ECO:0000269|PubMed:15060124}.
/FTId=VAR_010992.
VARIANT 844 844 L -> P (in NF1; dbSNP:rs137854566).
{ECO:0000269|PubMed:15060124}.
/FTId=VAR_032468.
VARIANT 844 844 L -> R (in NF1; sporadic;
dbSNP:rs137854566).
{ECO:0000269|PubMed:12522551,
ECO:0000269|PubMed:15948193,
ECO:0000269|PubMed:9150739}.
/FTId=VAR_002654.
VARIANT 847 847 L -> P (in NF1; dbSNP:rs199474747).
{ECO:0000269|PubMed:10712197,
ECO:0000269|PubMed:12552569,
ECO:0000269|PubMed:15146469}.
/FTId=VAR_021748.
VARIANT 848 848 G -> E (in NF1; dbSNP:rs199474748).
{ECO:0000269|PubMed:12552569,
ECO:0000269|PubMed:15146469}.
/FTId=VAR_021749.
VARIANT 873 873 R -> C (in dbSNP:rs199474739).
{ECO:0000269|PubMed:15060124}.
/FTId=VAR_032469.
VARIANT 898 898 L -> P (in NF1; sporadic;
dbSNP:rs199474786).
{ECO:0000269|PubMed:12522551,
ECO:0000269|PubMed:9150739}.
/FTId=VAR_002655.
VARIANT 920 920 L -> P (in NF1; patient with cafe-au-lait
spots; may be a distinct form of NF1;
dbSNP:rs199474775).
{ECO:0000269|PubMed:12746402}.
/FTId=VAR_021750.
VARIANT 968 968 M -> R (in NF1; dbSNP:rs199474749).
{ECO:0000269|PubMed:12552569,
ECO:0000269|PubMed:15146469}.
/FTId=VAR_021751.
VARIANT 991 991 Missing (in NF1; most patients carrying
the mutation do not manifest cutaneous
neurofibromas).
{ECO:0000269|PubMed:15060124,
ECO:0000269|PubMed:17160901,
ECO:0000269|PubMed:7904209}.
/FTId=VAR_002656.
VARIANT 1035 1035 M -> R (in NF1; dbSNP:rs137854553).
{ECO:0000269|PubMed:8807336}.
/FTId=VAR_002657.
VARIANT 1048 1048 W -> R (in NF1).
{ECO:0000269|PubMed:23758643}.
/FTId=VAR_071669.
VARIANT 1073 1073 M -> V (in NF1; dbSNP:rs199474740).
{ECO:0000269|PubMed:15060124}.
/FTId=VAR_032470.
VARIANT 1147 1147 L -> P (in NF1; dbSNP:rs199474779).
{ECO:0000269|PubMed:11735023}.
/FTId=VAR_021752.
VARIANT 1156 1156 N -> S (in NF1; dbSNP:rs199474764).
{ECO:0000269|PubMed:10712197}.
/FTId=VAR_021753.
VARIANT 1166 1166 G -> D (in NF1; dbSNP:rs199474787).
{ECO:0000269|PubMed:7981679}.
/FTId=VAR_010993.
VARIANT 1187 1187 L -> I (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035543.
VARIANT 1189 1189 Q -> R (in NF1; dbSNP:rs752039618).
{ECO:0000269|PubMed:23758643}.
/FTId=VAR_071670.
VARIANT 1193 1193 F -> C (in NF1; dbSNP:rs199474780).
{ECO:0000269|PubMed:11735023}.
/FTId=VAR_021754.
VARIANT 1196 1196 L -> R (in NF1; dbSNP:rs199474741).
{ECO:0000269|PubMed:15060124}.
/FTId=VAR_032471.
VARIANT 1204 1204 R -> G (in NF1; dbSNP:rs199474732).
{ECO:0000269|PubMed:10336779}.
/FTId=VAR_021755.
VARIANT 1204 1204 R -> W (in NF1; dbSNP:rs199474732).
{ECO:0000269|PubMed:10607834}.
/FTId=VAR_010994.
VARIANT 1243 1243 L -> P (in NF1; with neurofibromatous
neuropathy; dbSNP:rs137854564).
{ECO:0000269|PubMed:15520408}.
/FTId=VAR_032472.
VARIANT 1250 1250 R -> P (in NF1; dbSNP:rs199474765).
{ECO:0000269|PubMed:10712197}.
/FTId=VAR_021756.
VARIANT 1276 1276 R -> G (in NF1; dbSNP:rs199474742).
{ECO:0000269|PubMed:15060124}.
/FTId=VAR_032473.
VARIANT 1276 1276 R -> P (in NF1; complete loss of GAP
activity; dbSNP:rs137854556).
{ECO:0000269|PubMed:10712197,
ECO:0000269|PubMed:9668168}.
/FTId=VAR_010995.
VARIANT 1276 1276 R -> Q (in NF1 and mismatch repair
deficient cancer cells;
dbSNP:rs137854556).
{ECO:0000269|PubMed:10712197,
ECO:0000269|PubMed:12522551,
ECO:0000269|PubMed:15060124}.
/FTId=VAR_017555.
VARIANT 1411 1411 L -> F (in NFNS; dbSNP:rs199474789).
{ECO:0000269|PubMed:19845691}.
/FTId=VAR_065236.
VARIANT 1412 1412 R -> S (in NF1; significant reduction of
GAP activity; dbSNP:rs137854554).
{ECO:0000269|PubMed:9003501}.
/FTId=VAR_010996.
VARIANT 1422 1422 Y -> H (in dbSNP:rs17884349).
{ECO:0000269|Ref.7}.
/FTId=VAR_022256.
VARIANT 1430 1430 K -> E (in NF1).
{ECO:0000269|PubMed:15060124}.
/FTId=VAR_032474.
VARIANT 1440 1440 K -> Q (in NF1; dbSNP:rs199474790).
{ECO:0000269|PubMed:9003501}.
/FTId=VAR_010997.
VARIANT 1440 1440 K -> R (in NF1; dbSNP:rs199474788).
{ECO:0000269|PubMed:7981679}.
/FTId=VAR_002658.
VARIANT 1444 1444 K -> E (in NF1 and NFNS; significant
reduction of intrinsic GAP activity;
dbSNP:rs137854550).
{ECO:0000269|PubMed:11857752,
ECO:0000269|PubMed:1568247,
ECO:0000269|PubMed:16380919,
ECO:0000269|PubMed:9003501}.
/FTId=VAR_002659.
VARIANT 1444 1444 K -> N (in NF1; dbSNP:rs199474750).
{ECO:0000269|PubMed:12552569,
ECO:0000269|PubMed:15146469}.
/FTId=VAR_021757.
VARIANT 1444 1444 K -> R (in NF1; dbSNP:rs199474781).
{ECO:0000269|PubMed:11735023}.
/FTId=VAR_021758.
VARIANT 1446 1446 L -> P (in NF1; dbSNP:rs199474733).
{ECO:0000269|PubMed:10220149,
ECO:0000269|PubMed:10607834,
ECO:0000269|PubMed:10712197}.
/FTId=VAR_008129.
VARIANT 1451 1451 N -> T (in NFNS; dbSNP:rs199474754).
{ECO:0000269|PubMed:16380919}.
/FTId=VAR_032475.
VARIANT 1453 1453 V -> L (in NFNS; dbSNP:rs199474755).
{ECO:0000269|PubMed:16380919}.
/FTId=VAR_032476.
VARIANT 1459 1459 Missing (in NFNS).
{ECO:0000269|PubMed:12707950,
ECO:0000269|PubMed:15060124,
ECO:0000269|PubMed:16380919}.
/FTId=VAR_032477.
VARIANT 1484 1484 S -> F (in a cutaneous neurofibroma from
a patient with neurofibromatosis; somatic
mutation; dbSNP:rs199474772).
{ECO:0000269|PubMed:22108604}.
/FTId=VAR_067206.
VARIANT 1489 1489 S -> G (in NF1; dbSNP:rs199474743).
{ECO:0000269|PubMed:15060124,
ECO:0000269|PubMed:9003501}.
/FTId=VAR_010998.
VARIANT 1605 1605 I -> V (in NF1; reduces protein
stability; dbSNP:rs199474766).
{ECO:0000269|PubMed:10712197,
ECO:0000269|PubMed:21089070}.
/FTId=VAR_021759.
VARIANT 1611 1611 R -> W (in NF1).
{ECO:0000269|PubMed:9298829}.
/FTId=VAR_002660.
VARIANT 1733 1733 L -> LGHEQQKLPAATLAL (in NF1).
{ECO:0000269|PubMed:8317503}.
/FTId=VAR_002661.
VARIANT 1785 1785 A -> S (in NF1; dbSNP:rs199474782).
{ECO:0000269|PubMed:11735023}.
/FTId=VAR_021760.
VARIANT 1951 1951 P -> L (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035544.
VARIANT 1952 1952 W -> R (in NF1; dbSNP:rs199474791).
{ECO:0000269|PubMed:9101300}.
/FTId=VAR_002662.
VARIANT 1953 1953 L -> P (in NF1; dbSNP:rs199474792).
{ECO:0000269|PubMed:2114220}.
/FTId=VAR_002663.
VARIANT 1953 1953 Missing (in NF1).
{ECO:0000269|PubMed:12552569,
ECO:0000269|PubMed:15146469}.
/FTId=VAR_021761.
VARIANT 2001 2001 G -> R (in NF1; dbSNP:rs199474751).
{ECO:0000269|PubMed:12552569,
ECO:0000269|PubMed:15146469}.
/FTId=VAR_021762.
VARIANT 2012 2012 D -> N (in NF1; dbSNP:rs199474783).
{ECO:0000269|PubMed:11735023}.
/FTId=VAR_021763.
VARIANT 2088 2088 L -> P (in FSNF; no cafe-au-lait macules;
null mutation; 50% reduction of protein
level; dbSNP:rs137854561).
{ECO:0000269|PubMed:11704931}.
/FTId=VAR_017669.
VARIANT 2125 2125 L -> P (in NF1).
{ECO:0000269|PubMed:24413922}.
/FTId=VAR_071671.
VARIANT 2164 2164 L -> M (in NF1; dbSNP:rs137854551).
{ECO:0000269|PubMed:1302608}.
/FTId=VAR_002664.
VARIANT 2192 2192 Y -> N (in NF1; dbSNP:rs267606598).
{ECO:0000269|PubMed:1302608}.
/FTId=VAR_002665.
VARIANT 2221 2221 P -> A (in NF1; dbSNP:rs199474776).
{ECO:0000269|PubMed:12746402}.
/FTId=VAR_021764.
VARIANT 2357 2357 E -> K (in NF1; dbSNP:rs199474784).
{ECO:0000269|PubMed:11735023}.
/FTId=VAR_021765.
VARIANT 2387 2388 Missing (in NF1).
{ECO:0000269|PubMed:10607834,
ECO:0000269|PubMed:8081387}.
/FTId=VAR_002666.
VARIANT 2507 2507 T -> I (in NF1; dbSNP:rs149055633).
{ECO:0000269|PubMed:10712197}.
/FTId=VAR_021766.
VARIANT 2511 2511 V -> L (in dbSNP:rs2230850).
{ECO:0000269|Ref.7}.
/FTId=VAR_022257.
VARIANT 2631 2631 T -> A (in NF1; dbSNP:rs199474793).
{ECO:0000269|PubMed:8544190}.
/FTId=VAR_002667.
VARIANT 2745 2745 G -> R (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035545.
MUTAGEN 1691 1691 K->A: Reduces phospholipid binding; when
associated with A-1695; A-1769 and A-
1771. {ECO:0000269|PubMed:16397625}.
MUTAGEN 1695 1695 R->A: Reduces phospholipid binding; when
associated with A-1691; A-1769 and A-
1771. {ECO:0000269|PubMed:16397625}.
MUTAGEN 1769 1769 R->A: Reduces phospholipid binding; when
associated with A-1691; A-1695 and A-
1771. {ECO:0000269|PubMed:16397625}.
MUTAGEN 1771 1771 K->A: Reduces phospholipid binding; when
associated with A-1691; A-169 and A-1769.
{ECO:0000269|PubMed:16397625,
ECO:0000269|PubMed:21089070}.
MUTAGEN 1771 1771 Missing: Reduces protein stability.
{ECO:0000269|PubMed:16397625,
ECO:0000269|PubMed:21089070}.
CONFLICT 496 496 M -> I (in Ref. 11; AAA74897/AAB59558).
{ECO:0000305}.
CONFLICT 1094 1095 EL -> ST (in Ref. 14; AAA59923).
{ECO:0000305}.
CONFLICT 1576 1576 H -> HH (in Ref. 11; AAA74897/AAB59558).
{ECO:0000305}.
HELIX 1208 1216 {ECO:0000244|PDB:1NF1}.
HELIX 1224 1228 {ECO:0000244|PDB:1NF1}.
HELIX 1233 1235 {ECO:0000244|PDB:1NF1}.
HELIX 1236 1248 {ECO:0000244|PDB:1NF1}.
TURN 1249 1251 {ECO:0000244|PDB:1NF1}.
HELIX 1253 1263 {ECO:0000244|PDB:1NF1}.
STRAND 1266 1270 {ECO:0000244|PDB:1NF1}.
HELIX 1282 1293 {ECO:0000244|PDB:1NF1}.
HELIX 1296 1299 {ECO:0000244|PDB:1NF1}.
STRAND 1300 1302 {ECO:0000244|PDB:1NF1}.
TURN 1335 1337 {ECO:0000244|PDB:1NF1}.
TURN 1339 1342 {ECO:0000244|PDB:1NF1}.
HELIX 1343 1352 {ECO:0000244|PDB:1NF1}.
TURN 1353 1356 {ECO:0000244|PDB:1NF1}.
HELIX 1361 1370 {ECO:0000244|PDB:1NF1}.
TURN 1394 1396 {ECO:0000244|PDB:1NF1}.
HELIX 1402 1412 {ECO:0000244|PDB:1NF1}.
HELIX 1414 1419 {ECO:0000244|PDB:1NF1}.
HELIX 1434 1440 {ECO:0000244|PDB:1NF1}.
HELIX 1442 1451 {ECO:0000244|PDB:1NF1}.
HELIX 1462 1464 {ECO:0000244|PDB:1NF1}.
HELIX 1465 1470 {ECO:0000244|PDB:1NF1}.
HELIX 1472 1481 {ECO:0000244|PDB:1NF1}.
HELIX 1510 1514 {ECO:0000244|PDB:1NF1}.
HELIX 1517 1520 {ECO:0000244|PDB:1NF1}.
HELIX 1535 1544 {ECO:0000244|PDB:1NF1}.
HELIX 1569 1578 {ECO:0000244|PDB:3P7Z}.
TURN 1582 1586 {ECO:0000244|PDB:3PG7}.
HELIX 1587 1590 {ECO:0000244|PDB:3PG7}.
STRAND 1592 1598 {ECO:0000244|PDB:3PG7}.
STRAND 1604 1609 {ECO:0000244|PDB:3PG7}.
HELIX 1610 1612 {ECO:0000244|PDB:3PG7}.
TURN 1615 1617 {ECO:0000244|PDB:2D4Q}.
HELIX 1620 1631 {ECO:0000244|PDB:3PG7}.
TURN 1632 1636 {ECO:0000244|PDB:3PG7}.
STRAND 1639 1644 {ECO:0000244|PDB:3PG7}.
HELIX 1650 1652 {ECO:0000244|PDB:3PG7}.
HELIX 1656 1661 {ECO:0000244|PDB:3PG7}.
TURN 1662 1664 {ECO:0000244|PDB:3PG7}.
HELIX 1668 1672 {ECO:0000244|PDB:3PG7}.
STRAND 1674 1681 {ECO:0000244|PDB:3PG7}.
HELIX 1684 1692 {ECO:0000244|PDB:3PG7}.
HELIX 1694 1697 {ECO:0000244|PDB:3PG7}.
TURN 1698 1702 {ECO:0000244|PDB:3PG7}.
STRAND 1706 1711 {ECO:0000244|PDB:3PG7}.
HELIX 1714 1717 {ECO:0000244|PDB:3PG7}.
HELIX 1721 1723 {ECO:0000244|PDB:3PG7}.
HELIX 1728 1732 {ECO:0000244|PDB:3PG7}.
STRAND 1738 1749 {ECO:0000244|PDB:3PG7}.
STRAND 1751 1757 {ECO:0000244|PDB:3PG7}.
STRAND 1759 1767 {ECO:0000244|PDB:3PG7}.
STRAND 1770 1772 {ECO:0000244|PDB:2D4Q}.
STRAND 1775 1777 {ECO:0000244|PDB:3PG7}.
STRAND 1780 1784 {ECO:0000244|PDB:3PG7}.
HELIX 1785 1787 {ECO:0000244|PDB:3PG7}.
STRAND 1788 1795 {ECO:0000244|PDB:3PG7}.
STRAND 1798 1803 {ECO:0000244|PDB:3PG7}.
STRAND 1810 1813 {ECO:0000244|PDB:3PG7}.
HELIX 1817 1833 {ECO:0000244|PDB:3PG7}.
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


Related products :

Catalog number Product name Quantity
18-272-196659 Neurofibromin - Rabbit polyclonal to Neurofibromin; Neurofibromatosis-related protein NF-1 Polyclonal 0.05 mg
EIAAB27014 Neurofibromatosis-related protein NF-1,Neurofibromin,Nf1,Rat,Rattus norvegicus
EIAAB27013 Mouse,Mus musculus,Neurofibromatosis-related protein NF-1,Neurofibromin,Nf1
EIAAB27015 Homo sapiens,Human,Neurofibromatosis-related protein NF-1,Neurofibromin,NF1
EIAAB27012 Chicken,Gallus gallus,Neurofibromatosis-related protein NF-1,Neurofibromin,NF1
PR-223 NF1-333 (RasGAP) Neurofibromin, GTPase Activating Protein of Ras human, recombinant, E. coli 50
PR-223 NF1-333 (RasGAP) Neurofibromin, GTPase Activating Protein of Rashuman, recombinant, E. coli 50
PR-223 NF1_333 (RasGAP) Neurofibromin, GTPase Activating Protein of Ras human, recombinant, E. coli 50 µg
PR-223 NF1_333 (RasGAP) Neurofibromin, GTPase Activating Protein of Ras human, recombinant, E. coli 50µg
PR-223 Proteins: NF1-333 (RasGAP) Neurofibromin, GTPase Activating Protein of Rashuman, recombinant, E. coli 50
18-785-210276 Merlin (Ab-518) - Moesin-ezrin-radixin-like protein; Neurofibromin-2; Schwannomin; Schwannomerlin Polyclonal 0.05 mg
18-785-210276 Merlin (Ab-518) - Moesin-ezrin-radixin-like protein; Neurofibromin-2; Schwannomin; Schwannomerlin Polyclonal 0.1 mg
PC-187 Neurofibromin 200 uL
PC-187 Neurofibromin 200 uL
18-785-210275 Merlin (Phospho-Ser518) - Moesin-ezrin-radixin-like protein; Neurofibromin-2; Schwannomin; Schwannomerlin Polyclonal 0.05 mg
18-785-210275 Merlin (Phospho-Ser518) - Moesin-ezrin-radixin-like protein; Neurofibromin-2; Schwannomin; Schwannomerlin Polyclonal 0.1 mg
PC-187 Neurofibromin Polyclonal 200 uL
GTX77638 Neurofibromin 50 µg
24950002 Neurofibromin 100 µg
GTX77638 Neurofibromin 50 µg
NB300-153 Neurofibromin 0.2 ml
GTX28131 Neurofibromin 50 µl
SP2067P Neurofibromin 50 µg
AP10397PU-N Neurofibromin 0.2 ml
GTX17963 Neurofibromin 50 µg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur