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GTPase NRas (Transforming protein N-Ras)

 RASN_HUMAN              Reviewed;         189 AA.
P01111; Q14971; Q15104; Q15282;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
05-JUN-2019, entry version 222.
RecName: Full=GTPase NRas;
AltName: Full=Transforming protein N-Ras;
Flags: Precursor;
Name=NRAS; Synonyms=HRAS1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6616621; DOI=10.1016/0092-8674(83)90390-2;
Taparowsky E., Shimizu K., Goldfarb M., Wigler M.;
"Structure and activation of the human N-ras gene.";
Cell 34:581-586(1983).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2991860; DOI=10.1093/nar/13.14.5255;
Hall A., Brown R.;
"Human N-ras: cDNA cloning and gene structure.";
Nucleic Acids Res. 13:5255-5268(1985).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Fibrosarcoma;
PubMed=6086315;
Brown R., Marshall C.J., Pennie S.G., Hall A.;
"Mechanism of activation of an N-ras gene in the human fibrosarcoma
cell line HT1080.";
EMBO J. 3:1321-1326(1984).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Lung carcinoma;
PubMed=6587382; DOI=10.1073/pnas.81.12.3670;
Yuasa Y., Gol R.A., Chang A., Chiu I.-M., Reddy E.P., Tronick S.R.,
Aaronson S.A.;
"Mechanism of activation of an N-ras oncogene of SW-1271 human lung
carcinoma cells.";
Proc. Natl. Acad. Sci. U.S.A. 81:3670-3674(1984).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE OF 1-96, AND VARIANT CYS-12.
TISSUE=Leukemia;
PubMed=2998510;
Hirai H., Tanaka S., Azuma M., Anraku Y., Kobayashi Y., Fujisawa M.,
Okabe T., Urabe A., Takaku F.;
"Transforming genes in human leukemia cells.";
Blood 66:1371-1378(1985).
[9]
NUCLEOTIDE SEQUENCE OF 1-29 AND 43-78.
PubMed=1970154;
Yuasa Y., Kamiyama T., Kato M., Iwama T., Ikeuchi T., Tonomura A.;
"Transforming genes from familial adenomatous polyposis patient cells
detected by a tumorigenicity assay.";
Oncogene 5:589-596(1990).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-96.
PubMed=3856237; DOI=10.1073/pnas.82.3.879;
Gambke C., Hall A., Moroni C.;
"Activation of an N-ras gene in acute myeloblastic leukemia through
somatic mutation in the first exon.";
Proc. Natl. Acad. Sci. U.S.A. 82:879-882(1985).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-96.
TISSUE=Bone marrow;
PubMed=3295562; DOI=10.1038/327430a0;
Hirai H., Kobayashi Y., Mano H., Hagiwara K., Maru Y., Omine M.,
Mizoguchi H., Nishida J., Takaku F.;
"A point mutation at codon 13 of the N-ras oncogene in myelodysplastic
syndrome.";
Nature 327:430-432(1987).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-96, AND VARIANT ARG-61.
PubMed=3276402;
Raybaud F., Noguchi T., Marics I., Adelaide J., Planche J., Batoz M.,
Aubet C., de Lapeyriere O., Birnbaum D.;
"Detection of a low frequency of activated ras genes in human
melanomas using a tumorigenicity assay.";
Cancer Res. 48:950-953(1988).
[13]
PALMITOYLATION AT CYS-181, AND ISOPRENYLATION AT CYS-186.
PubMed=2661017; DOI=10.1016/0092-8674(89)90054-8;
Hancock J.F., Magee A.I., Childs J.E., Marshall C.J.;
"All ras proteins are polyisoprenylated but only some are
palmitoylated.";
Cell 57:1167-1177(1989).
[14]
INVOLVEMENT IN NMTC2, AND VARIANT NMTC2 ARG-61.
PubMed=12727991; DOI=10.1210/jc.2002-021907;
Nikiforova M.N., Lynch R.A., Biddinger P.W., Alexander E.K.,
Dorn G.W. II, Tallini G., Kroll T.G., Nikiforov Y.E.;
"RAS point mutations and PAX8-PPAR gamma rearrangement in thyroid
tumors: evidence for distinct molecular pathways in thyroid follicular
carcinoma.";
J. Clin. Endocrinol. Metab. 88:2318-2326(2003).
[15]
PALMITOYLATION AT CYS-181.
PubMed=16000296; DOI=10.1074/jbc.M504113200;
Swarthout J.T., Lobo S., Farh L., Croke M.R., Greentree W.K.,
Deschenes R.J., Linder M.E.;
"DHHC9 and GCP16 constitute a human protein fatty acyltransferase with
specificity for H- and N-Ras.";
J. Biol. Chem. 280:31141-31148(2005).
[16]
PALMITOYLATION, AND SUBCELLULAR LOCATION.
PubMed=15705808; DOI=10.1126/science.1105654;
Rocks O., Peyker A., Kahms M., Verveer P.J., Koerner C.,
Lumbierres M., Kuhlmann J., Waldmann H., Wittinghofer A.,
Bastiaens P.I.H.;
"An acylation cycle regulates localization and activity of
palmitoylated Ras isoforms.";
Science 307:1746-1752(2005).
[17]
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).
[18]
INTERACTION WITH RASSF7.
PubMed=21278800; DOI=10.1038/cdd.2010.137;
Takahashi S., Ebihara A., Kajiho H., Kontani K., Nishina H.,
Katada T.;
"RASSF7 negatively regulates pro-apoptotic JNK signaling by inhibiting
the activity of phosphorylated-MKK7.";
Cell Death Differ. 18:645-655(2011).
[19]
SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-181, AND MUTAGENESIS OF
CYS-181.
PubMed=26701913; DOI=10.7554/eLife.11306;
Lin D.T., Conibear E.;
"ABHD17 proteins are novel protein depalmitoylases that regulate N-Ras
palmitate turnover and subcellular localization.";
Elife 4:E11306-E11306(2015).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[21]
UBIQUITINATION AT LYS-170.
PubMed=30442762; DOI=10.1126/science.aap7607;
Steklov M., Pandolfi S., Baietti M.F., Batiuk A., Carai P., Najm P.,
Zhang M., Jang H., Renzi F., Cai Y., Abbasi Asbagh L., Pastor T.,
De Troyer M., Simicek M., Radaelli E., Brems H., Legius E.,
Tavernier J., Gevaert K., Impens F., Messiaen L., Nussinov R.,
Heymans S., Eyckerman S., Sablina A.A.;
"Mutations in LZTR1 drive human disease by dysregulating RAS
ubiquitination.";
Science 362:1177-1182(2018).
[22]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-89, MUTAGENESIS
OF SER-89, VARIANT ARG-61, AND CHARACTERIZATION OF VARIANT ARG-61.
PubMed=30712867; DOI=10.1016/j.cell.2019.01.002;
Yin C., Zhu B., Zhang T., Liu T., Chen S., Liu Y., Li X., Miao X.,
Li S., Mi X., Zhang J., Li L., Wei G., Xu Z.X., Gao X., Huang C.,
Wei Z., Goding C.R., Wang P., Deng X., Cui R.;
"Pharmacological targeting of STK19 inhibits oncogenic NRAS-driven
melanomagenesis.";
Cell 176:1113-1127(2019).
[23]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-172 IN COMPLEX WITH GDP.
Nedyalkova L., Tong Y., Tempel W., Shen L., Loppnau P.,
Arrowsmith C.H., Edwards A.M., Bountra C., Weigelt J., Bochkarev A.,
Park H.;
"Crystal structure of the human NRAS GTPase bound with GDP.";
Submitted (MAR-2008) to the PDB data bank.
[24]
VARIANT COLORECTAL CANCER ARG-13.
PubMed=3102434;
Nitta N., Ochiai M., Nagao M., Sugimura T.;
"Amino-acid substitution at codon 13 of the N-ras oncogene in rectal
cancer in a Japanese patient.";
Jpn. J. Cancer Res. 78:21-26(1987).
[25]
VARIANTS JMML ASP-12 AND ASP-13.
PubMed=17332249; DOI=10.1182/blood-2006-09-046649;
Matsuda K., Shimada A., Yoshida N., Ogawa A., Watanabe A., Yajima S.,
Iizuka S., Koike K., Yanai F., Kawasaki K., Yanagimachi M.,
Kikuchi A., Ohtsuka Y., Hidaka E., Yamauchi K., Tanaka M.,
Yanagisawa R., Nakazawa Y., Shiohara M., Manabe A., Kojima S.,
Koike K.;
"Spontaneous improvement of hematologic abnormalities in patients
having juvenile myelomonocytic leukemia with specific RAS mutations.";
Blood 109:5477-5480(2007).
[26]
VARIANT RALD ASP-13.
PubMed=17517660; DOI=10.1073/pnas.0702975104;
Oliveira J.B., Bidere N., Niemela J.E., Zheng L., Sakai K., Nix C.P.,
Danner R.L., Barb J., Munson P.J., Puck J.M., Dale J., Straus S.E.,
Fleisher T.A., Lenardo M.J.;
"NRAS mutation causes a human autoimmune lymphoproliferative
syndrome.";
Proc. Natl. Acad. Sci. U.S.A. 104:8953-8958(2007).
[27]
VARIANTS CMNS ARG-13 AND ARG-61.
PubMed=18633438; DOI=10.1038/jid.2008.203;
Dessars B., De Raeve L.E., Morandini R., Lefort A., El Housni H.,
Ghanem G.E., Van den Eynde B.J., Ma W., Roseeuw D., Vassart G.,
Libert F., Heimann P.;
"Genotypic and gene expression studies in congenital melanocytic nevi:
insight into initial steps of melanotumorigenesis.";
J. Invest. Dermatol. 129:139-147(2009).
[28]
VARIANTS NS6 ILE-50 AND GLU-60, AND CHARACTERIZATION OF VARIANTS NS6
ILE-50 AND GLU-60.
PubMed=19966803; DOI=10.1038/ng.497;
Cirstea I.C., Kutsche K., Dvorsky R., Gremer L., Carta C., Horn D.,
Roberts A.E., Lepri F., Merbitz-Zahradnik T., Konig R., Kratz C.P.,
Pantaleoni F., Dentici M.L., Joshi V.A., Kucherlapati R.S.,
Mazzanti L., Mundlos S., Patton M.A., Silengo M.C., Rossi C.,
Zampino G., Digilio C., Stuppia L., Seemanova E., Pennacchio L.A.,
Gelb B.D., Dallapiccola B., Wittinghofer A., Ahmadian M.R.,
Tartaglia M., Zenker M.;
"A restricted spectrum of NRAS mutations causes Noonan syndrome.";
Nat. Genet. 42:27-29(2010).
[29]
VARIANTS KNEN ASP-12; LEU-34 AND ARG-61.
PubMed=22499344; DOI=10.1136/jmedgenet-2011-100637;
Hafner C., Toll A., Gantner S., Mauerer A., Lurkin I., Acquadro F.,
Fernandez-Casado A., Zwarthoff E.C., Dietmaier W., Baselga E.,
Parera E., Vicente A., Casanova A., Cigudosa J., Mentzel T.,
Pujol R.M., Landthaler M., Real F.X.;
"Keratinocytic epidermal nevi are associated with mosaic RAS
mutations.";
J. Med. Genet. 49:249-253(2012).
[30]
VARIANTS CMNS ARG-61 AND LYS-61, AND VARIANTS NCMS ARG-61 AND LYS-61.
PubMed=23392294; DOI=10.1038/jid.2013.70;
Kinsler V.A., Thomas A.C., Ishida M., Bulstrode N.W., Loughlin S.,
Hing S., Chalker J., McKenzie K., Abu-Amero S., Slater O.,
Chanudet E., Palmer R., Morrogh D., Stanier P., Healy E., Sebire N.J.,
Moore G.E.;
"Multiple congenital melanocytic nevi and neurocutaneous melanosis are
caused by postzygotic mutations in codon 61 of NRAS.";
J. Invest. Dermatol. 133:2229-2236(2013).
-!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
activity. {ECO:0000269|PubMed:30712867}.
-!- ACTIVITY REGULATION: Alternates between an inactive form bound to
GDP and an active form bound to GTP. Activated by a guanine
nucleotide-exchange factor (GEF) and inactivated by a GTPase-
activating protein (GAP).
-!- SUBUNIT: Interacts (active GTP-bound form preferentially) with
RGS14 (By similarity). Interacts (active GTP-bound form) with
RASSF7 (PubMed:21278800). {ECO:0000250|UniProtKB:Q04970,
ECO:0000269|PubMed:21278800}.
-!- INTERACTION:
P15056:BRAF; NbExp=3; IntAct=EBI-721993, EBI-365980;
P28028:Braf (xeno); NbExp=2; IntAct=EBI-721993, EBI-2584830;
P04049:RAF1; NbExp=5; IntAct=EBI-721993, EBI-365996;
Q99N57:Raf1 (xeno); NbExp=2; IntAct=EBI-721993, EBI-397757;
P52306-5:RAP1GDS1; NbExp=4; IntAct=EBI-721993, EBI-12832744;
Q13671:RIN1; NbExp=4; IntAct=EBI-721993, EBI-366017;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15705808,
ECO:0000269|PubMed:26701913}; Lipid-anchor
{ECO:0000269|PubMed:15705808, ECO:0000269|PubMed:26701913};
Cytoplasmic side {ECO:0000269|PubMed:15705808,
ECO:0000269|PubMed:26701913}. Golgi apparatus membrane
{ECO:0000269|PubMed:15705808, ECO:0000269|PubMed:26701913}; Lipid-
anchor {ECO:0000269|PubMed:15705808, ECO:0000269|PubMed:26701913}.
Note=Shuttles between the plasma membrane and the Golgi apparatus.
{ECO:0000269|PubMed:15705808, ECO:0000269|PubMed:26701913}.
-!- PTM: Palmitoylated by the ZDHHC9-GOLGA7 complex (PubMed:16000296).
Depalmitoylated by ABHD17A, ABHD17B and ABHD17C (PubMed:26701913).
A continuous cycle of de- and re-palmitoylation regulates rapid
exchange between plasma membrane and Golgi (PubMed:16000296,
PubMed:15705808, PubMed:2661017, PubMed:26701913).
{ECO:0000269|PubMed:15705808, ECO:0000269|PubMed:16000296,
ECO:0000269|PubMed:2661017, ECO:0000269|PubMed:26701913}.
-!- PTM: Acetylation at Lys-104 prevents interaction with guanine
nucleotide exchange factors (GEFs).
{ECO:0000250|UniProtKB:P01116}.
-!- PTM: Ubiquitinated by the BCR(LZTR1) E3 ubiquitin ligase complex
at Lys-170 in a non-degradative manner, leading to inhibit Ras
signaling by decreasing Ras association with membranes.
{ECO:0000305|PubMed:30442762}.
-!- PTM: Phosphorylation at Ser-89 by STK19 enhances NRAS-association
with its downstream effectors. {ECO:0000269|PubMed:30712867}.
-!- 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. {ECO:0000269|PubMed:17332249}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Noonan syndrome 6 (NS6) [MIM:613224]: A form of Noonan
syndrome, a disease characterized by short stature, facial
dysmorphic features such as hypertelorism, a downward eyeslant and
low-set posteriorly rotated ears, and a high incidence of
congenital heart defects and hypertrophic cardiomyopathy. Other
features can include a short neck with webbing or redundancy of
skin, deafness, motor delay, variable intellectual deficits,
multiple skeletal defects, cryptorchidism, and bleeding diathesis.
Individuals with Noonan syndrome are at risk of juvenile
myelomonocytic leukemia, a myeloproliferative disorder
characterized by excessive production of myelomonocytic cells.
{ECO:0000269|PubMed:19966803}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: RAS-associated autoimmune leukoproliferative disorder
(RALD) [MIM:614470]: A disorder of apoptosis, characterized by
chronic accumulation of non-malignant lymphocytes, defective
lymphocyte apoptosis, and an increased risk for the development of
hematologic malignancies. {ECO:0000269|PubMed:17517660}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Melanocytic nevus syndrome, congenital (CMNS)
[MIM:137550]: A syndrome characterized by congenital pigmentary
skin lesions which can occur at any site and can cover most of the
body surface. These lesions may or may not be hairy. Congenital
melanocytic nevi are associated with neuromelanosis (the presence
of melanin-producing cells within the brain parenchyma or
leptomeninges). Less commonly they are associated with malignant
melanoma in childhood, both in the skin and the central nervous
system. CMNS patients also tend to have a characteristic facial
appearance, including wide or prominent forehead, periorbital
fullness, small short nose with narrow nasal bridge, round face,
full cheeks, prominent premaxilla, and everted lower lip.
{ECO:0000269|PubMed:18633438, ECO:0000269|PubMed:23392294}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Melanosis, neurocutaneous (NCMS) [MIM:249400]: A rare
congenital disease characterized by the presence of giant or
multiple melanocytic nevi on the skin, foci of melanin-producing
cells within the brain parenchyma, and infiltration of
leptomeninges by abnormal melanin deposits. Neurologic
abnormalities include seizures, hydrocephalus, arachnoid cysts,
tumors, and syringomyelia. Some patients may develop malignant
melanoma. {ECO:0000269|PubMed:23392294}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Keratinocytic non-epidermolytic nevus (KNEN)
[MIM:162900]: Epidermal nevi of the common, non-organoid and non-
epidermolytic type are benign skin lesions and may vary in their
extent from a single (usually linear) lesion to widespread and
systematized involvement. They may be present at birth or develop
early during childhood. {ECO:0000269|PubMed:22499344}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Thyroid cancer, non-medullary, 2 (NMTC2) [MIM:188470]: A
form of non-medullary thyroid cancer (NMTC), a cancer
characterized by tumors originating from the thyroid follicular
cells. NMTCs represent approximately 95% of all cases of thyroid
cancer and are classified into papillary, follicular, Hurthle
cell, and anaplastic neoplasms. {ECO:0000269|PubMed:12727991}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- MISCELLANEOUS: Mutations which change AA 12, 13 or 61 activate the
potential of Ras to transform cultured cells and are implicated in
a variety of human tumors.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/NRASID92.html";
-!- WEB RESOURCE: Name=NRASbase; Note=NRAS mutation db;
URL="http://structure.bmc.lu.se/idbase/NRASbase/";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/nras/";
-!- WEB RESOURCE: Name=Wikipedia; Note=RAS proteins entry;
URL="https://en.wikipedia.org/wiki/RAS_proteins";
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EMBL; X02751; CAA26529.1; -; mRNA.
EMBL; X00642; CAA25269.1; -; Genomic_DNA.
EMBL; X00643; CAA25270.1; -; Genomic_DNA.
EMBL; X00644; CAA25271.1; -; Genomic_DNA.
EMBL; X00645; CAA25272.1; -; Genomic_DNA.
EMBL; L00043; AAA60255.1; -; Genomic_DNA.
EMBL; L00040; AAA60255.1; JOINED; Genomic_DNA.
EMBL; L00041; AAA60255.1; JOINED; Genomic_DNA.
EMBL; L00042; AAA60255.1; JOINED; Genomic_DNA.
EMBL; AF493919; AAM12633.1; -; mRNA.
EMBL; AY428630; AAQ94397.1; -; Genomic_DNA.
EMBL; BC005219; AAH05219.1; -; mRNA.
EMBL; M25898; AAA36548.1; -; Genomic_DNA.
EMBL; X53291; CAA37384.1; -; Genomic_DNA.
EMBL; X53292; CAA37384.1; JOINED; Genomic_DNA.
EMBL; K03211; AAA36556.1; -; Genomic_DNA.
EMBL; M10055; AAA36556.1; JOINED; Genomic_DNA.
EMBL; X05565; CAA29079.1; -; Genomic_DNA.
EMBL; X07440; CAA30320.1; -; Genomic_DNA.
CCDS; CCDS877.1; -.
PIR; A90839; TVHURA.
PIR; I38149; I38149.
RefSeq; NP_002515.1; NM_002524.4.
PDB; 2N9C; NMR; -; A=1-17.
PDB; 3CON; X-ray; 1.65 A; A=1-172.
PDB; 5UHV; X-ray; 1.67 A; A=1-166.
PDBsum; 2N9C; -.
PDBsum; 3CON; -.
PDBsum; 5UHV; -.
SMR; P01111; -.
BioGrid; 110952; 169.
DIP; DIP-1058N; -.
ELM; P01111; -.
IntAct; P01111; 43.
MINT; P01111; -.
STRING; 9606.ENSP00000358548; -.
BindingDB; P01111; -.
ChEMBL; CHEMBL2079845; -.
GuidetoPHARMACOLOGY; 2823; -.
iPTMnet; P01111; -.
PhosphoSitePlus; P01111; -.
SwissPalm; P01111; -.
BioMuta; NRAS; -.
DMDM; 131883; -.
OGP; P01111; -.
EPD; P01111; -.
jPOST; P01111; -.
PaxDb; P01111; -.
PeptideAtlas; P01111; -.
PRIDE; P01111; -.
ProteomicsDB; 51320; -.
DNASU; 4893; -.
Ensembl; ENST00000369535; ENSP00000358548; ENSG00000213281.
GeneID; 4893; -.
KEGG; hsa:4893; -.
CTD; 4893; -.
DisGeNET; 4893; -.
GeneCards; NRAS; -.
GeneReviews; NRAS; -.
HGNC; HGNC:7989; NRAS.
HPA; CAB010157; -.
HPA; HPA049830; -.
MalaCards; NRAS; -.
MIM; 137550; phenotype.
MIM; 162900; phenotype.
MIM; 164790; gene.
MIM; 188470; phenotype.
MIM; 249400; phenotype.
MIM; 607785; phenotype.
MIM; 613224; phenotype.
MIM; 614470; phenotype.
neXtProt; NX_P01111; -.
OpenTargets; ENSG00000213281; -.
Orphanet; 146; Differentiated thyroid carcinoma.
Orphanet; 86834; Juvenile myelomonocytic leukemia.
Orphanet; 626; Large congenital melanocytic nevus.
Orphanet; 2612; Linear nevus sebaceus syndrome.
Orphanet; 411533; NON RARE IN EUROPE: Melanoma.
Orphanet; 648; Noonan syndrome.
Orphanet; 268114; RAS-associated autoimmune leukoproliferative disease.
Orphanet; 357194; Selection of therapeutic option in colorectal cancer.
PharmGKB; PA31768; -.
eggNOG; KOG0395; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00940000158947; -.
HOGENOM; HOG000233973; -.
InParanoid; P01111; -.
KO; K07828; -.
OMA; DIHLYRE; -.
OrthoDB; 1344247at2759; -.
PhylomeDB; P01111; -.
TreeFam; TF312796; -.
Reactome; R-HSA-112412; SOS-mediated signalling.
Reactome; R-HSA-1169092; Activation of RAS in B cells.
Reactome; R-HSA-1236382; Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
Reactome; R-HSA-1250196; SHC1 events in ERBB2 signaling.
Reactome; R-HSA-1250347; SHC1 events in ERBB4 signaling.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-167044; Signalling to RAS.
Reactome; R-HSA-171007; p38MAPK events.
Reactome; R-HSA-179812; GRB2 events in EGFR signaling.
Reactome; R-HSA-180336; SHC1 events in EGFR signaling.
Reactome; R-HSA-186763; Downstream signal transduction.
Reactome; R-HSA-1963640; GRB2 events in ERBB2 signaling.
Reactome; R-HSA-210993; Tie2 Signaling.
Reactome; R-HSA-2179392; EGFR Transactivation by Gastrin.
Reactome; R-HSA-2424491; DAP12 signaling.
Reactome; R-HSA-2428933; SHC-related events triggered by IGF1R.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-375165; NCAM signaling for neurite out-growth.
Reactome; R-HSA-442982; Ras activation upon Ca2+ influx through NMDA receptor.
Reactome; R-HSA-5218921; VEGFR2 mediated cell proliferation.
Reactome; R-HSA-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-HSA-5637810; Constitutive Signaling by EGFRvIII.
Reactome; R-HSA-5654688; SHC-mediated cascade:FGFR1.
Reactome; R-HSA-5654693; FRS-mediated FGFR1 signaling.
Reactome; R-HSA-5654699; SHC-mediated cascade:FGFR2.
Reactome; R-HSA-5654700; FRS-mediated FGFR2 signaling.
Reactome; R-HSA-5654704; SHC-mediated cascade:FGFR3.
Reactome; R-HSA-5654706; FRS-mediated FGFR3 signaling.
Reactome; R-HSA-5654712; FRS-mediated FGFR4 signaling.
Reactome; R-HSA-5654719; SHC-mediated cascade:FGFR4.
Reactome; R-HSA-5655253; Signaling by FGFR2 in disease.
Reactome; R-HSA-5655291; Signaling by FGFR4 in disease.
Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-5673000; RAF activation.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-5674135; MAP2K and MAPK activation.
Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
Reactome; R-HSA-6802949; Signaling by RAS mutants.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
Reactome; R-HSA-6802953; RAS signaling downstream of NF1 loss-of-function variants.
Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
Reactome; R-HSA-74751; Insulin receptor signalling cascade.
Reactome; R-HSA-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
Reactome; R-HSA-8851805; MET activates RAS signaling.
Reactome; R-HSA-8853334; Signaling by FGFR3 fusions in cancer.
Reactome; R-HSA-8853338; Signaling by FGFR3 point mutants in cancer.
Reactome; R-HSA-9026519; Activated NTRK2 signals through RAS.
Reactome; R-HSA-9027284; Erythropoietin activates RAS.
Reactome; R-HSA-9028731; Activated NTRK2 signals through FRS2 and FRS3.
Reactome; R-HSA-9034864; Activated NTRK3 signals through RAS.
Reactome; R-HSA-9634635; Estrogen-stimulated signaling through PRKCZ.
SignaLink; P01111; -.
SIGNOR; P01111; -.
ChiTaRS; NRAS; human.
EvolutionaryTrace; P01111; -.
GeneWiki; Neuroblastoma_RAS_viral_oncogene_homolog; -.
GenomeRNAi; 4893; -.
PRO; PR:P01111; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000213281; Expressed in 217 organ(s), highest expression level in testis.
ExpressionAtlas; P01111; baseline and differential.
Genevisible; P01111; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:CACAO.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
GO; GO:0019003; F:GDP binding; IBA:GO_Central.
GO; GO:0005525; F:GTP binding; IBA:GO_Central.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:BHF-UCL.
GO; GO:0007265; P:Ras protein signal transduction; IDA:UniProtKB.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR020849; Small_GTPase_Ras-type.
PANTHER; PTHR24070; PTHR24070; 1.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51421; RAS; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cell membrane; Complete proteome;
Disease mutation; Golgi apparatus; GTP-binding; Isopeptide bond;
Lipoprotein; Membrane; Methylation; Nucleotide-binding; Palmitate;
Phosphoprotein; Prenylation; Proto-oncogene; Reference proteome;
Ubl conjugation.
CHAIN 1 186 GTPase NRas.
/FTId=PRO_0000043006.
PROPEP 187 189 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000043007.
NP_BIND 10 18 GTP. {ECO:0000269|Ref.23}.
NP_BIND 29 30 GTP. {ECO:0000269|Ref.23}.
NP_BIND 57 61 GTP. {ECO:0000255}.
NP_BIND 116 119 GTP. {ECO:0000269|Ref.23}.
REGION 166 185 Hypervariable region.
MOTIF 32 40 Effector region.
MOD_RES 89 89 Phosphoserine; by STK19.
{ECO:0000269|PubMed:30712867}.
LIPID 181 181 S-palmitoyl cysteine.
{ECO:0000269|PubMed:16000296,
ECO:0000269|PubMed:2661017,
ECO:0000269|PubMed:26701913}.
LIPID 186 186 S-farnesyl cysteine.
{ECO:0000269|PubMed:2661017}.
CROSSLNK 170 170 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000305|PubMed:30442762}.
VARIANT 12 12 G -> C (in leukemia; dbSNP:rs121913250).
{ECO:0000269|PubMed:2998510}.
/FTId=VAR_021194.
VARIANT 12 12 G -> D (in KNEN and JMML;
dbSNP:rs121913237).
{ECO:0000269|PubMed:17332249,
ECO:0000269|PubMed:22499344}.
/FTId=VAR_071129.
VARIANT 13 13 G -> D (in RALD and JMML;
dbSNP:rs121434596).
{ECO:0000269|PubMed:17332249,
ECO:0000269|PubMed:17517660}.
/FTId=VAR_063084.
VARIANT 13 13 G -> R (in CMNS and colorectal cancer;
somatic mutation; dbSNP:rs121434595).
{ECO:0000269|PubMed:18633438,
ECO:0000269|PubMed:3102434}.
/FTId=VAR_006845.
VARIANT 34 34 P -> L (in KNEN; dbSNP:rs397514553).
{ECO:0000269|PubMed:22499344}.
/FTId=VAR_071130.
VARIANT 50 50 T -> I (in NS6; hypermorphic mutation;
dbSNP:rs267606921).
{ECO:0000269|PubMed:19966803}.
/FTId=VAR_063085.
VARIANT 60 60 G -> E (in NS6; hypermorphic mutation;
dbSNP:rs267606920).
{ECO:0000269|PubMed:19966803}.
/FTId=VAR_063086.
VARIANT 61 61 Q -> K (in CMNS and NCMS; somatic
mutation; dbSNP:rs121913254).
{ECO:0000269|PubMed:23392294}.
/FTId=VAR_006846.
VARIANT 61 61 Q -> R (in CMNS, NCMS, KNEN and NMTC2;
also found in lung carcinoma cell and
melanoma; impaired GTP hydrolysis
activity, trapping NRAS in a constitutive
GTP-bound active conformation; promotes
melanomagenesis; dbSNP:rs11554290).
{ECO:0000269|PubMed:12727991,
ECO:0000269|PubMed:18633438,
ECO:0000269|PubMed:22499344,
ECO:0000269|PubMed:23392294,
ECO:0000269|PubMed:30712867,
ECO:0000269|PubMed:3276402}.
/FTId=VAR_006847.
MUTAGEN 89 89 S->A: Abolished phosphorylation by STK19.
{ECO:0000269|PubMed:30712867}.
MUTAGEN 164 164 R->A: Loss of GTP-binding activity.
MUTAGEN 181 181 C->S: Loss of plasma membrane
localization.
{ECO:0000269|PubMed:26701913}.
STRAND 2 9 {ECO:0000244|PDB:3CON}.
HELIX 16 25 {ECO:0000244|PDB:3CON}.
STRAND 38 46 {ECO:0000244|PDB:3CON}.
STRAND 49 57 {ECO:0000244|PDB:3CON}.
HELIX 62 64 {ECO:0000244|PDB:5UHV}.
HELIX 65 71 {ECO:0000244|PDB:5UHV}.
TURN 72 74 {ECO:0000244|PDB:5UHV}.
STRAND 76 83 {ECO:0000244|PDB:3CON}.
HELIX 87 104 {ECO:0000244|PDB:3CON}.
STRAND 111 116 {ECO:0000244|PDB:3CON}.
HELIX 127 137 {ECO:0000244|PDB:3CON}.
STRAND 141 143 {ECO:0000244|PDB:3CON}.
TURN 146 148 {ECO:0000244|PDB:3CON}.
HELIX 152 166 {ECO:0000244|PDB:3CON}.
SEQUENCE 189 AA; 21229 MW; 6898D3F6815B1EC7 CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLC VFAINNSKSF ADINLYREQI KRVKDSDDVP MVLVGNKCDL
PTRTVDTKQA HELAKSYGIP FIETSAKTRQ GVEDAFYTLV REIRQYRMKK LNSSDDGTQG
CMGLPCVVM


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Related Genes :
[NRAS HRAS1] GTPase NRas (Transforming protein N-Ras)
[HRAS HRAS1] GTPase HRas (H-Ras-1) (Ha-Ras) (Transforming protein p21) (c-H-ras) (p21ras) [Cleaved into: GTPase HRas, N-terminally processed]
[KRAS KRAS2 RASK2] GTPase KRas (K-Ras 2) (Ki-Ras) (c-K-ras) (c-Ki-ras) [Cleaved into: GTPase KRas, N-terminally processed]
[nras] GTPase NRas (Transforming protein N-Ras)
[Ran Rasl2-8] GTP-binding nuclear protein Ran (GTPase Ran) (Ras-like protein TC4) (Ras-related nuclear protein)
[Rhoa Arha Arha2] Transforming protein RhoA (EC 3.6.5.2)
[rab-11.1 F53G12.1] Ras-related protein rab-11.1 (Rab GTPase rab-11.1)
[Shc1 Shc ShcA] SHC-transforming protein 1 (SHC-transforming protein A) (Src homology 2 domain-containing-transforming protein C1) (SH2 domain protein C1)
[Khdrbs1] KH domain-containing, RNA-binding, signal transduction-associated protein 1 (GAP-associated tyrosine phosphoprotein p62) (Src-associated in mitosis 68 kDa protein) (Sam68) (p21 Ras GTPase-activating protein-associated p62) (p68)
[SYNGAP1 KIAA1938] Ras/Rap GTPase-activating protein SynGAP (Neuronal RasGAP) (Synaptic Ras GTPase-activating protein 1) (Synaptic Ras-GAP 1)
[Syngap1] Ras/Rap GTPase-activating protein SynGAP (Neuronal RasGAP) (Synaptic Ras GTPase-activating protein 1) (Synaptic Ras-GAP 1) (p135 SynGAP)
[RASA1 GAP RASA] Ras GTPase-activating protein 1 (GAP) (GTPase-activating protein) (RasGAP) (Ras p21 protein activator) (p120GAP)
[Syngap1] Ras/Rap GTPase-activating protein SynGAP (Neuronal RasGAP) (Synaptic Ras GTPase-activating protein 1) (Synaptic Ras-GAP 1)
[SHC3 NSHC SHCC] SHC-transforming protein 3 (Neuronal Shc) (N-Shc) (Protein Rai) (SHC-transforming protein C) (Src homology 2 domain-containing-transforming protein C3) (SH2 domain protein C3)
[RASA4 CAPRI GAPL KIAA0538] Ras GTPase-activating protein 4 (Calcium-promoted Ras inactivator) (Ras p21 protein activator 4) (RasGAP-activating-like protein 2)
[Rragc] Ras-related GTP-binding protein C (Rag C) (RagC) (GTPase-interacting protein 2) (TIB929)
[Arhgap32 Grit Kiaa0712 Rics] Rho GTPase-activating protein 32 (Brain-specific Rho GTPase-activating protein) (GAB-associated Cdc42/Rac GTPase-activating protein) (GC-GAP) (Rho-type GTPase-activating protein 32) (Rho/Cdc42/Rac GTPase-activating protein RICS) (RhoGAP involved in the beta-catenin-N-cadherin and NMDA receptor signaling) (p200RhoGAP) (p250GAP)
[RAN ARA24 OK/SW-cl.81] GTP-binding nuclear protein Ran (Androgen receptor-associated protein 24) (GTPase Ran) (Ras-like protein TC4) (Ras-related nuclear protein)
[RAN] GTP-binding nuclear protein Ran (GTPase Ran) (Ras-like protein TC4) (Ras-related nuclear protein)
[Ran] GTP-binding nuclear protein Ran (GTPase Ran) (Ras-like protein TC4) (Ras-related nuclear protein)
[SHC1 SHC SHCA] SHC-transforming protein 1 (SHC-transforming protein 3) (SHC-transforming protein A) (Src homology 2 domain-containing-transforming protein C1) (SH2 domain protein C1)
[RHOA ARH12 ARHA RHO12] Transforming protein RhoA (EC 3.6.5.2) (Rho cDNA clone 12) (h12)
[ced-10 rac-1 C09G12.8] Ras-related protein ced-10 (CErac1) (Cell death protein 10) (Cell-corpse engulfment protein ced-10) (Ras-related protein rac-1)
[G3BP1 G3BP] Ras GTPase-activating protein-binding protein 1 (G3BP-1) (EC 3.6.4.12) (EC 3.6.4.13) (ATP-dependent DNA helicase VIII) (hDH VIII) (GAP SH3 domain-binding protein 1)
[rgaA DG1029 rasGAP1 DDB_G0287585] Ras GTPase-activating-like protein rgaA (DGAP1) (Developmental gene 1029 protein)
[Rin1] Ras and Rab interactor 1 (Ras interaction/interference protein 1)
[Rasgrp1 Rasgrp] RAS guanyl-releasing protein 1 (Calcium and DAG-regulated guanine nucleotide exchange factor II) (CalDAG-GEFII) (Ras guanyl-releasing protein)
[IQGAP1 KIAA0051] Ras GTPase-activating-like protein IQGAP1 (p195)
[G3bp1 G3bp] Ras GTPase-activating protein-binding protein 1 (G3BP-1) (EC 3.6.4.12) (EC 3.6.4.13) (ATP-dependent DNA helicase VIII) (GAP SH3 domain-binding protein 1) (HDH-VIII)
[ran] GTP-binding nuclear protein Ran (GTPase Ran) (Ras-like protein TC4) (Ras-related nuclear protein)

Bibliography :
[23733505] Dominant role of oncogene dosage and absence of tumor suppressor activity in Nras-driven hematopoietic transformation.
[23240926] Evidence of a low prevalence of RAS mutations in a large medullary thyroid cancer series.
[19075190] High-throughput sequencing screen reveals novel, transforming RAS mutations in myeloid leukemia patients.