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GTPase HRas (H-Ras-1) (Ha-Ras) (Transforming protein p21) (c-H-ras) (p21ras) [Cleaved into: GTPase HRas, N-terminally processed]

 RASH_HUMAN              Reviewed;         189 AA.
P01112; B5BUA0; Q14080; Q6FHV9; Q9BR65; Q9UCE2;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
30-AUG-2017, entry version 225.
RecName: Full=GTPase HRas;
AltName: Full=H-Ras-1;
AltName: Full=Ha-Ras;
AltName: Full=Transforming protein p21;
AltName: Full=c-H-ras;
AltName: Full=p21ras;
Contains:
RecName: Full=GTPase HRas, N-terminally processed;
Flags: Precursor;
Name=HRAS; 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], AND INVOLVEMENT IN BLADDER CANCER.
PubMed=6298635; DOI=10.1038/302033a0;
Capon D.J., Chen E.Y., Levinson A.D., Seeburg P.H., Goeddel D.V.;
"Complete nucleotide sequences of the T24 human bladder carcinoma
oncogene and its normal homologue.";
Nature 302:33-37(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INVOLVEMENT IN BLADDER CANCER.
PubMed=6844927; DOI=10.1126/science.6844927;
Reddy E.P.;
"Nucleotide sequence analysis of the T24 human bladder carcinoma
oncogene.";
Science 220:1061-1063(1983).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6087347; DOI=10.1073/pnas.81.15.4771;
Sekiya T., Fushimi M., Hori H., Hirohashi S., Nishimura S.,
Sugimura T.;
"Molecular cloning and the total nucleotide sequence of the human c-
Ha-ras-1 gene activated in a melanoma from a Japanese patient.";
Proc. Natl. Acad. Sci. U.S.A. 81:4771-4775(1984).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH
RACK1, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY,
AND MUTAGENESIS OF SER-17.
PubMed=14500341;
Guil S., de La Iglesia N., Fernandez-Larrea J., Cifuentes D.,
Ferrer J.C., Guinovart J.J., Bach-Elias M.;
"Alternative splicing of the human proto-oncogene c-H-ras renders a
new Ras family protein that trafficks to cytoplasm and nucleus.";
Cancer Res. 63:5178-5187(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [LARGE SCALE MRNA] (ISOFORM 1).
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Lung carcinoma;
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).
[12]
PROTEIN SEQUENCE OF 1-41; 43-117; 129-161 AND 170-185, CLEAVAGE OF
INITIATOR METHIONINE, ACETYLATION AT MET-1 AND THR-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Cervix carcinoma;
Bienvenut W.V., Calvo F., Kolch W.;
Submitted (FEB-2008) to UniProtKB.
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
PubMed=6290897; DOI=10.1038/300143a0;
Tabin C.J., Bradley S.M., Bargmann C.I., Weinberg R.A.,
Papageorge A.G., Scolnick E.M., Dhar R., Lowy D.R., Chang E.H.;
"Mechanism of activation of a human oncogene.";
Nature 300:143-149(1982).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
PubMed=3670300; DOI=10.1128/MCB.7.8.2933;
Honkawa H., Masahashi W., Hashimoto S., Hashimoto-Gotoh T.;
"Identification of the principal promoter sequence of the c-H-ras
transforming oncogene: deletion analysis of the 5'-flanking region by
focus formation assay.";
Mol. Cell. Biol. 7:2933-2940(1987).
[15]
PROTEIN SEQUENCE OF 108-117 AND 132-153.
PubMed=8393791; DOI=10.1111/j.1432-1033.1993.tb18056.x;
Loew A., Sprinzl M., Faulhammer H.G.;
"Affinity labeling of c-H-ras p21 consensus elements with periodate-
oxidized GDP and GTP.";
Eur. J. Biochem. 215:473-479(1993).
[16]
MUTAGENESIS OF ALA-83; ASP-119 AND THR-144.
PubMed=3088563; DOI=10.1073/pnas.83.13.4607;
Feig L.A., Pan B.-T., Roberts T.M., Cooper G.M.;
"Isolation of ras GTP-binding mutants using an in situ colony-binding
assay.";
Proc. Natl. Acad. Sci. U.S.A. 83:4607-4611(1986).
[17]
MUTAGENESIS OF 164-ARG-GLN-165.
PubMed=3011420;
Lacal J.C., Anderson P.S., Aaronson S.A.;
"Deletion mutants of Harvey ras p21 protein reveal the absolute
requirement of at least two distant regions for GTP-binding and
transforming activities.";
EMBO J. 5:679-687(1986).
[18]
PALMITOYLATION AT CYS-181 AND CYS-184.
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).
[19]
PALMITOYLATION AT CYS-181 AND CYS-184, ISOPRENYLATION AT CYS-186,
METHYLATION AT CYS-186, AND MUTAGENESIS OF CYS-181 AND CYS-184.
PubMed=8626715; DOI=10.1074/jbc.271.19.11541;
Dudler T., Gelb M.H.;
"Palmitoylation of Ha-Ras facilitates membrane binding, activation of
downstream effectors, and meiotic maturation in Xenopus oocytes.";
J. Biol. Chem. 271:11541-11547(1996).
[20]
S-NITROSYLATION AT CYS-118, FUNCTION, MASS SPECTROMETRY, AND
MUTAGENESIS OF CYS-118.
PubMed=9020151; DOI=10.1074/jbc.272.7.4323;
Lander H.M., Hajjar D.P., Hempstead B.L., Mirza U.A., Chait B.T.,
Campbell S., Quilliam L.A.;
"A molecular redox switch on p21(ras). Structural basis for the nitric
oxide-p21(ras) interaction.";
J. Biol. Chem. 272:4323-4326(1997).
[21]
INTERACTION WITH IKZF3.
PubMed=10369681; DOI=10.1093/emboj/18.12.3419;
Romero F., Martinez-A C., Camonis J., Rebollo A.;
"Aiolos transcription factor controls cell death in T cells by
regulating Bcl-2 expression and its cellular localization.";
EMBO J. 18:3419-3430(1999).
[22]
INTERACTION WITH RAPGEF2.
PubMed=10608844; DOI=10.1074/jbc.274.53.37815;
Liao Y., Kariya K., Hu C.-D., Shibatohge M., Goshima M., Okada T.,
Watari Y., Gao X., Jin T.-G., Yamawaki-Kataoka Y., Kataoka T.;
"RA-GEF, a novel Rap1A guanine nucleotide exchange factor containing a
Ras/Rap1A-associating domain, is conserved between nematode and
humans.";
J. Biol. Chem. 274:37815-37820(1999).
[23]
INTERACTION WITH PLCE1, CHARACTERIZATION OF VARIANT VAL-12, AND
MUTAGENESIS OF SER-17; ASN-26; VAL-29; TYR-32; PRO-34; THR-35; GLU-37;
ASP-38 AND SER-39.
PubMed=11022048; DOI=10.1074/jbc.M008324200;
Song C., Hu C.-D., Masago M., Kariya K., Yamawaki-Kataoka Y.,
Shibatohge M., Wu D., Satoh T., Kataoka T.;
"Regulation of a novel human phospholipase C, PLCepsilon, through
membrane targeting by Ras.";
J. Biol. Chem. 276:2752-2757(2001).
[24]
INTERACTION WITH RAPGEF2.
PubMed=11598133; DOI=10.1074/jbc.M108373200;
Pham N., Rotin D.;
"Nedd4 regulates ubiquitination and stability of the guanine-
nucleotide exchange factor CNrasGEF.";
J. Biol. Chem. 276:46995-47003(2001).
[25]
IDENTIFICATION IN A COMPLEX WITH RASGRP1 AND DGKZ.
PubMed=11257115; DOI=10.1083/jcb.152.6.1135;
Topham M.K., Prescott S.M.;
"Diacylglycerol kinase zeta regulates Ras activation by a novel
mechanism.";
J. Cell Biol. 152:1135-1143(2001).
[26]
INTERACTION WITH PDE6D.
PubMed=11980706; DOI=10.1093/emboj/21.9.2095;
Hanzal-Bayer M., Renault L., Roversi P., Wittinghofer A., Hillig R.C.;
"The complex of Arl2-GTP and PDE delta: from structure to function.";
EMBO J. 21:2095-2106(2002).
[27]
LIPIDATION AT CYS-184, AND MUTAGENESIS OF CYS-184.
PubMed=12684535; DOI=10.1073/pnas.0735842100;
Oliva J.L., Perez-Sala D., Castrillo A., Martinez N., Canada F.J.,
Bosca L., Rojas J.M.;
"The cyclopentenone 15-deoxy-delta 12,14-prostaglandin J2 binds to and
activates H-Ras.";
Proc. Natl. Acad. Sci. U.S.A. 100:4772-4777(2003).
[28]
FUNCTION, VARIANT CYS-89, AND CHARACTERIZATION OF VARIANT CYS-89.
PubMed=22821884; DOI=10.1002/ajmg.a.35449;
Gripp K.W., Bifeld E., Stabley D.L., Hopkins E., Meien S., Vinette K.,
Sol-Church K., Rosenberger G.;
"A novel HRAS substitution (c.266C>G; p.S89C) resulting in decreased
downstream signaling suggests a new dimension of RAS pathway
dysregulation in human development.";
Am. J. Med. Genet. A 158A:2106-2118(2012).
[29]
CHARACTERIZATION OF CSTLO VARIANT VAL-12.
PubMed=15546861; DOI=10.1074/jbc.M410775200;
Liu F., Iqbal K., Grundke-Iqbal I., Rossie S., Gong C.X.;
"Dephosphorylation of tau by protein phosphatase 5: impairment in
Alzheimer's disease.";
J. Biol. Chem. 280:1790-1796(2005).
[30]
PALMITOYLATION AT CYS-181 AND CYS-184.
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).
[31]
PALMITOYLATION AT CYS-181 AND CYS-184, MUTAGENESIS OF CYS-181 AND
CYS-184, 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).
[32]
INTERACTION WITH TBC1D10C.
PubMed=17230191; DOI=10.1038/nature05476;
Pan F., Sun L., Kardian D.B., Whartenby K.A., Pardoll D.M., Liu J.O.;
"Feedback inhibition of calcineurin and Ras by a dual inhibitory
protein Carabin.";
Nature 445:433-436(2007).
[33]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed=2448879; DOI=10.1126/science.2448879;
de Vos A.M., Tong L., Milburn M.V., Matias P.M., Jancarik J.,
Noguchi S., Nishimura S., Miura K., Ohtsuka E., Kim S.-H.;
"Three-dimensional structure of an oncogene protein: catalytic domain
of human c-H-ras p21.";
Science 239:888-893(1988).
[34]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
PubMed=2476675; DOI=10.1038/341209a0;
Pai E.F., Kabsch W., Krengel U., Holmes K.C., John J.,
Wittinghofer A.;
"Structure of the guanine-nucleotide-binding domain of the Ha-ras
oncogene product p21 in the triphosphate conformation.";
Nature 341:209-214(1989).
[35]
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
PubMed=2196171;
Pai E.F., Krengel U., Petsko G.A., Goody R.S., Kabsch W.,
Wittinghofer A.;
"Refined crystal structure of the triphosphate conformation of H-ras
p21 at 1.35-A resolution: implications for the mechanism of GTP
hydrolysis.";
EMBO J. 9:2351-2359(1990).
[36]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed=1899707; DOI=10.1016/0022-2836(91)90753-S;
Tong L.A., de Vos A.M., Milburn M.V., Kim S.H.;
"Crystal structures at 2.2-A resolution of the catalytic domains of
normal ras protein and an oncogenic mutant complexed with GDP.";
J. Mol. Biol. 217:503-516(1991).
[37]
STRUCTURE BY NMR OF 1-166.
PubMed=8142349; DOI=10.1021/bi00178a008;
Kraulis P.J., Domaille P.J., Campbell-Burk S.L., van Aken T.,
Laue E.D.;
"Solution structure and dynamics of ras p21.GDP determined by
heteronuclear three- and four-dimensional NMR spectroscopy.";
Biochemistry 33:3515-3531(1994).
[38]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-166 IN COMPLEX WITH RASGAP.
PubMed=9219684; DOI=10.1126/science.277.5324.333;
Scheffzek K., Ahmadian M.R., Kabsch W., Wiesmuller L., Lautwein A.,
Schmitz F., Wittinghofer A.;
"The Ras-RasGAP complex: structural basis for GTPase activation and
its loss in oncogenic Ras mutants.";
Science 277:333-338(1997).
[39]
X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS).
PubMed=10574788; DOI=10.1016/S0969-2126(00)80021-0;
Scheidig A.J., Burmester C., Goody R.S.;
"The pre-hydrolysis state of p21(ras) in complex with GTP: new
insights into the role of water molecules in the GTP hydrolysis
reaction of ras-like proteins.";
Structure 7:1311-1324(1999).
[40]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-166 IN COMPLEXES WITH GTP
ANALOGS.
PubMed=12213964; DOI=10.1073/pnas.192453199;
Hall B.E., Bar-Sagi D., Nassar N.;
"The structural basis for the transition from Ras-GTP to Ras-GDP.";
Proc. Natl. Acad. Sci. U.S.A. 99:12138-12142(2002).
[41]
STRUCTURE BY NMR OF 1-166, S-NITROSYLATION, FUNCTION, MUTAGENESIS OF
CYS-118, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12740440; DOI=10.1073/pnas.1037299100;
Williams J.G., Pappu K., Campbell S.L.;
"Structural and biochemical studies of p21Ras S-nitrosylation and
nitric oxide-mediated guanine nucleotide exchange.";
Proc. Natl. Acad. Sci. U.S.A. 100:6376-6381(2003).
[42]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-166 IN COMPLEXES WITH GTP
ANALOG, CHARACTERIZATION OF VARIANTS LEU-61 AND LYS-61, AND
MUTAGENESIS OF GLN-61.
PubMed=18073111; DOI=10.1016/j.str.2007.10.011;
Buhrman G., Wink G., Mattos C.;
"Transformation efficiency of RasQ61 mutants linked to structural
features of the switch regions in the presence of Raf.";
Structure 15:1618-1629(2007).
[43]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-166 IN COMPLEX WITH RASSF5.
PubMed=18596699; DOI=10.1038/emboj.2008.125;
Stieglitz B., Bee C., Schwarz D., Yildiz O., Moshnikova A.,
Khokhlatchev A., Herrmann C.;
"Novel type of Ras effector interaction established between tumour
suppressor NORE1A and Ras switch II.";
EMBO J. 27:1995-2005(2008).
[44]
VARIANT SER-12.
PubMed=1459726; DOI=10.1002/ijc.2910520606;
Sakai E., Rikimaru K., Ueda M., Matsumoto Y., Ishii N., Enomoto S.,
Yamamoto H., Tsuchida N.;
"The p53 tumor-suppressor gene and ras oncogene mutations in oral
squamous-cell carcinoma.";
Int. J. Cancer 52:867-872(1992).
[45]
INVOLVEMENT IN NMTC2, AND VARIANT NMTC2 LYS-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).
[46]
VARIANTS CSTLO ALA-12; SER-12; VAL-12 AND ASP-13.
PubMed=16170316; DOI=10.1038/ng1641;
Aoki Y., Niihori T., Kawame H., Kurosawa K., Ohashi H., Tanaka Y.,
Filocamo M., Kato K., Suzuki Y., Kure S., Matsubara Y.;
"Germline mutations in HRAS proto-oncogene cause Costello syndrome.";
Nat. Genet. 37:1038-1040(2005).
[47]
VARIANTS CSTLO ALA-12; SER-12 AND CYS-13.
PubMed=16329078; DOI=10.1002/ajmg.a.31047;
Gripp K.W., Lin A.E., Stabley D.L., Nicholson L., Scott C.I. Jr.,
Doyle D., Aoki Y., Matsubara Y., Zackai E.H., Lapunzina P.,
Gonzalez-Meneses A., Holbrook J., Agresta C.A., Gonzalez I.L.,
Sol-Church K.;
"HRAS mutation analysis in Costello syndrome: genotype and phenotype
correlation.";
Am. J. Med. Genet. A 140:1-7(2006).
[48]
VARIANTS CSTLO SER-12; CYS-12; GLU-12; ALA-12 AND ARG-117.
PubMed=16443854; DOI=10.1136/jmg.2005.040352;
Kerr B., Delrue M.-A., Sigaudy S., Perveen R., Marche M., Burgelin I.,
Stef M., Tang B., Eden O.B., O'Sullivan J., De Sandre-Giovannoli A.,
Reardon W., Brewer C., Bennett C., Quarell O., M'Cann E., Donnai D.,
Stewart F., Hennekam R., Cave H., Verloes A., Philip N., Lacombe D.,
Levy N., Arveiler B., Black G.;
"Genotype-phenotype correlation in Costello syndrome: HRAS mutation
analysis in 43 cases.";
J. Med. Genet. 43:401-405(2006).
[49]
VARIANTS CSTLO SER-12 AND THR-146.
PubMed=17054105; DOI=10.1002/humu.20431;
Zampino G., Pantaleoni F., Carta C., Cobellis G., Vasta I., Neri C.,
Pogna E.A., De Feo E., Delogu A., Sarkozy A., Atzeri F., Selicorni A.,
Rauen K.A., Cytrynbaum C.S., Weksberg R., Dallapiccola B.,
Ballabio A., Gelb B.D., Neri G., Tartaglia M.;
"Diversity, parental germline origin, and phenotypic spectrum of de
novo HRAS missense changes in Costello syndrome.";
Hum. Mutat. 28:265-272(2007).
[50]
VARIANTS CMEMS VAL-12; SER-12; LYS-22 AND LYS-63.
PubMed=17412879; DOI=10.1136/jmg.2007.049270;
van der Burgt I., Kupsky W., Stassou S., Nadroo A., Barroso C.,
Diem A., Kratz C.P., Dvorsky R., Ahmadian M.R., Zenker M.;
"Myopathy caused by HRAS germline mutations: implications for
disturbed myogenic differentiation in the presence of constitutive
HRas activation.";
J. Med. Genet. 44:459-462(2007).
[51]
VARIANTS CSTLO ILE-58 AND VAL-146.
PubMed=18247425; DOI=10.1002/ajmg.a.32227;
Gripp K.W., Innes A.M., Axelrad M.E., Gillan T.L., Parboosingh J.S.,
Davies C., Leonard N.J., Lapointe M., Doyle D., Catalano S.,
Nicholson L., Stabley D.L., Sol-Church K.;
"Costello syndrome associated with novel germline HRAS mutations: an
attenuated phenotype?";
Am. J. Med. Genet. A 146:683-690(2008).
[52]
VARIANTS CSTLO ASP-12 AND CYS-12.
PubMed=18039947; DOI=10.1136/jmg.2007.054411;
Lo I.F., Brewer C., Shannon N., Shorto J., Tang B., Black G.,
Soo M.T., Ng D.K., Lam S.T., Kerr B.;
"Severe neonatal manifestations of Costello syndrome.";
J. Med. Genet. 45:167-171(2008).
[53]
VARIANT CSTLO GLU-37 INS.
PubMed=19995790; DOI=10.1093/hmg/ddp548;
Gremer L., De Luca A., Merbitz-Zahradnik T., Dallapiccola B.,
Morlot S., Tartaglia M., Kutsche K., Ahmadian M.R., Rosenberger G.;
"Duplication of Glu37 in the switch I region of HRAS impairs
effector/GAP binding and underlies Costello syndrome by promoting
enhanced growth factor-dependent MAPK and AKT activation.";
Hum. Mol. Genet. 19:790-802(2010).
[54]
VARIANT SFM ARG-13, AND CHARACTERIZATION OF VARIANT SFM ARG-13.
PubMed=22683711; DOI=10.1038/ng.2316;
Groesser L., Herschberger E., Ruetten A., Ruivenkamp C., Lopriore E.,
Zutt M., Langmann T., Singer S., Klingseisen L.,
Schneider-Brachert W., Toll A., Real F.X., Landthaler M., Hafner C.;
"Postzygotic HRAS and KRAS mutations cause nevus sebaceous and
Schimmelpenning syndrome.";
Nat. Genet. 44:783-787(2012).
-!- FUNCTION: Involved in the activation of Ras protein signal
transduction (PubMed:22821884). Ras proteins bind GDP/GTP and
possess intrinsic GTPase activity (PubMed:12740440,
PubMed:14500341, PubMed:9020151). {ECO:0000269|PubMed:12740440,
ECO:0000269|PubMed:14500341, ECO:0000269|PubMed:22821884,
ECO:0000269|PubMed:9020151}.
-!- ENZYME 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: In its GTP-bound form interacts with PLCE1
(PubMed:11022048). Interacts with TBC1D10C (PubMed:17230191).
Interacts with RGL3 (By similarity). Interacts with HSPD1 (By
similarity). Found in a complex with at least BRAF, HRAS, MAP2K1,
MAPK3 and RGS14 (By similarity). Interacts (active GTP-bound form)
with RGS14 (via RBD 1 domain) (By similarity). Forms a signaling
complex with RASGRP1 and DGKZ (PubMed:11257115). Interacts with
RASSF5 (PubMed:18596699). Interacts with PDE6D (PubMed:11980706).
Interacts with IKZF3 (PubMed:10369681). Interacts with RACK1
(PubMed:14500341). Interacts with PIK3CG; the interaction is
required for membrane recruitment and beta-gamma G protein dimer-
dependent activation of the PI3K gamma complex PIK3CG:PIK3R6 (By
similarity). Interacts with RAPGEF2 (PubMed:10608844,
PubMed:11598133). {ECO:0000250|UniProtKB:P20171,
ECO:0000250|UniProtKB:Q61411, ECO:0000269|PubMed:10369681,
ECO:0000269|PubMed:10608844, ECO:0000269|PubMed:11022048,
ECO:0000269|PubMed:11257115, ECO:0000269|PubMed:11598133,
ECO:0000269|PubMed:11980706, ECO:0000269|PubMed:14500341,
ECO:0000269|PubMed:17230191, ECO:0000269|PubMed:18596699,
ECO:0000269|PubMed:9219684}.
-!- INTERACTION:
Q7Z569:BRAP; NbExp=3; IntAct=EBI-350145, EBI-349900;
P42337:Pik3ca (xeno); NbExp=2; IntAct=EBI-350145, EBI-641748;
O00329:PIK3CD; NbExp=2; IntAct=EBI-350145, EBI-718309;
O00329-2:PIK3CD; NbExp=2; IntAct=EBI-350145, EBI-6470902;
Q9Z0S9:Rabac1 (xeno); NbExp=4; IntAct=EBI-350145, EBI-476965;
P04049:RAF1; NbExp=14; IntAct=EBI-350145, EBI-365996;
Q12967:RALGDS; NbExp=2; IntAct=EBI-350145, EBI-365861;
Q9EQZ6:Rapgef4 (xeno); NbExp=3; IntAct=EBI-350145, EBI-772212;
Q9NS23-2:RASSF1; NbExp=2; IntAct=EBI-350145, EBI-438698;
Q8WWW0:RASSF5; NbExp=2; IntAct=EBI-350145, EBI-367390;
Q5EBH1:Rassf5 (xeno); NbExp=11; IntAct=EBI-350145, EBI-960530;
Q5EBH1-2:Rassf5 (xeno); NbExp=3; IntAct=EBI-350145, EBI-960547;
Q13671:RIN1; NbExp=5; IntAct=EBI-350145, EBI-366017;
Q07889:SOS1; NbExp=8; IntAct=EBI-350145, EBI-297487;
-!- SUBCELLULAR LOCATION: Cell membrane. Cell membrane; Lipid-anchor;
Cytoplasmic side. Golgi apparatus. Golgi apparatus membrane;
Lipid-anchor. Note=The active GTP-bound form is localized most
strongly to membranes than the inactive GDP-bound form (By
similarity). Shuttles between the plasma membrane and the Golgi
apparatus. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus. Cytoplasm. Cytoplasm,
perinuclear region. Note=Colocalizes with RACK1 to the perinuclear
region.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=H-Ras4A, p21;
IsoId=P01112-1; Sequence=Displayed;
Name=2; Synonyms=H-RasIDX, p19;
IsoId=P01112-2; Sequence=VSP_041597;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:14500341}.
-!- PTM: Palmitoylated by the ZDHHC9-GOLGA7 complex. A continuous
cycle of de- and re-palmitoylation regulates rapid exchange
between plasma membrane and Golgi.
-!- PTM: S-nitrosylated; critical for redox regulation. Important for
stimulating guanine nucleotide exchange. No structural
perturbation on nitrosylation.
-!- PTM: The covalent modification of cysteine by 15-deoxy-Delta12,14-
prostaglandin-J2 is autocatalytic and reversible. It may occur as
an alternative to other cysteine modifications, such as S-
nitrosylation and S-palmitoylation.
-!- PTM: Acetylation at Lys-104 prevents interaction with guanine
nucleotide exchange factors (GEFs). {ECO:0000250}.
-!- MASS SPECTROMETRY: Mass=6223; Mass_error=2; Method=Electrospray;
Range=112-166; Evidence={ECO:0000269|PubMed:9020151};
-!- MASS SPECTROMETRY: Mass=6253; Mass_error=2; Method=Electrospray;
Range=112-166; Note=Includes one nitric oxide molecule.;
Evidence={ECO:0000269|PubMed:9020151};
-!- DISEASE: Costello syndrome (CSTLO) [MIM:218040]: A rare condition
characterized by prenatally increased growth, postnatal growth
deficiency, mental retardation, distinctive facial appearance,
cardiovascular abnormalities (typically pulmonic stenosis,
hypertrophic cardiomyopathy and/or atrial tachycardia), tumor
predisposition, skin and musculoskeletal abnormalities.
{ECO:0000269|PubMed:16170316, ECO:0000269|PubMed:16329078,
ECO:0000269|PubMed:16443854, ECO:0000269|PubMed:17054105,
ECO:0000269|PubMed:18039947, ECO:0000269|PubMed:18247425,
ECO:0000269|PubMed:19995790}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Congenital myopathy with excess of muscle spindles
(CMEMS) [MIM:218040]: Variant of Costello syndrome.
{ECO:0000269|PubMed:17412879}. 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.
-!- DISEASE: Note=Mutations which change positions 12, 13 or 61
activate the potential of HRAS to transform cultured cells and are
implicated in a variety of human tumors.
{ECO:0000269|PubMed:3670300}.
-!- DISEASE: Bladder cancer (BLC) [MIM:109800]: A malignancy
originating in tissues of the urinary bladder. It often presents
with multiple tumors appearing at different times and at different
sites in the bladder. Most bladder cancers are transitional cell
carcinomas that begin in cells that normally make up the inner
lining of the bladder. Other types of bladder cancer include
squamous cell carcinoma (cancer that begins in thin, flat cells)
and adenocarcinoma (cancer that begins in cells that make and
release mucus and other fluids). Bladder cancer is a complex
disorder with both genetic and environmental influences.
{ECO:0000269|PubMed:6298635, ECO:0000269|PubMed:6844927}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Schimmelpenning-Feuerstein-Mims syndrome (SFM)
[MIM:163200]: A disease characterized by sebaceous nevi, often on
the face, associated with variable ipsilateral abnormalities of
the central nervous system, ocular anomalies, and skeletal
defects. Many oral manifestations have been reported, not only
including hypoplastic and malformed teeth, and mucosal
papillomatosis, but also ankyloglossia, hemihyperplastic tongue,
intraoral nevus, giant cell granuloma, ameloblastoma, bone cysts,
follicular cysts, oligodontia, and odontodysplasia. Sebaceous nevi
follow the lines of Blaschko and these can continue as linear
intraoral lesions, as in mucosal papillomatosis.
{ECO:0000269|PubMed:22683711}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- 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/HRASID108.html";
-----------------------------------------------------------------------
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EMBL; J00277; AAB02605.1; -; Genomic_DNA.
EMBL; AJ437024; CAD24594.1; -; mRNA.
EMBL; AF493916; AAM12630.1; -; mRNA.
EMBL; CR536579; CAG38816.1; -; mRNA.
EMBL; CR542271; CAG47067.1; -; mRNA.
EMBL; BT019421; AAV38228.1; -; mRNA.
EMBL; EF015887; ABI97389.1; -; Genomic_DNA.
EMBL; AB451336; BAG70150.1; -; mRNA.
EMBL; AB451485; BAG70299.1; -; mRNA.
EMBL; CH471158; EAX02337.1; -; Genomic_DNA.
EMBL; CH471158; EAX02338.1; -; Genomic_DNA.
EMBL; BC006499; AAH06499.1; -; mRNA.
EMBL; BC095471; AAH95471.1; -; mRNA.
EMBL; M17232; AAA35685.1; -; Genomic_DNA.
CCDS; CCDS7698.1; -. [P01112-1]
CCDS; CCDS7699.1; -. [P01112-2]
PIR; A93299; TVHUH.
RefSeq; NP_001123914.1; NM_001130442.2. [P01112-1]
RefSeq; NP_001304983.1; NM_001318054.1.
RefSeq; NP_005334.1; NM_005343.3. [P01112-1]
RefSeq; NP_789765.1; NM_176795.4. [P01112-2]
UniGene; Hs.37003; -.
PDB; 121P; X-ray; 1.54 A; A=1-166.
PDB; 1AA9; NMR; -; A=1-171.
PDB; 1AGP; X-ray; 2.30 A; A=1-166.
PDB; 1BKD; X-ray; 2.80 A; R=1-166.
PDB; 1CLU; X-ray; 1.70 A; A=1-166.
PDB; 1CRP; NMR; -; A=1-166.
PDB; 1CRQ; NMR; -; A=1-166.
PDB; 1CRR; NMR; -; A=1-166.
PDB; 1CTQ; X-ray; 1.26 A; A=1-166.
PDB; 1GNP; X-ray; 2.70 A; A=1-166.
PDB; 1GNQ; X-ray; 2.50 A; A=1-166.
PDB; 1GNR; X-ray; 1.85 A; A=1-166.
PDB; 1HE8; X-ray; 3.00 A; B=1-166.
PDB; 1IAQ; X-ray; 2.90 A; A/B/C=1-166.
PDB; 1IOZ; X-ray; 2.00 A; A=1-171.
PDB; 1JAH; X-ray; 1.80 A; A=1-166.
PDB; 1JAI; X-ray; 1.80 A; A=1-166.
PDB; 1K8R; X-ray; 3.00 A; A=1-166.
PDB; 1LF0; X-ray; 1.70 A; A=1-166.
PDB; 1LF5; X-ray; 1.70 A; A=1-166.
PDB; 1LFD; X-ray; 2.10 A; B/D=1-167.
PDB; 1NVU; X-ray; 2.20 A; Q/R=1-166.
PDB; 1NVV; X-ray; 2.18 A; Q/R=1-166.
PDB; 1NVW; X-ray; 2.70 A; Q/R=1-166.
PDB; 1NVX; X-ray; 3.20 A; Q/R=1-166.
PDB; 1P2S; X-ray; 2.45 A; A=1-166.
PDB; 1P2T; X-ray; 2.00 A; A=1-166.
PDB; 1P2U; X-ray; 2.00 A; A=1-166.
PDB; 1P2V; X-ray; 2.30 A; A=1-166.
PDB; 1PLJ; X-ray; 2.80 A; A=1-166.
PDB; 1PLK; X-ray; 2.80 A; A=1-166.
PDB; 1PLL; X-ray; 2.80 A; A=1-166.
PDB; 1Q21; X-ray; 2.20 A; A=1-171.
PDB; 1QRA; X-ray; 1.60 A; A=1-166.
PDB; 1RVD; X-ray; 1.90 A; A=1-166.
PDB; 1WQ1; X-ray; 2.50 A; R=1-166.
PDB; 1XCM; X-ray; 1.84 A; A=1-167.
PDB; 1XD2; X-ray; 2.70 A; A/B=1-166.
PDB; 1XJ0; X-ray; 1.70 A; A=1-166.
PDB; 1ZVQ; X-ray; 2.00 A; A=1-166.
PDB; 1ZW6; X-ray; 1.50 A; A=1-166.
PDB; 221P; X-ray; 2.30 A; A=1-166.
PDB; 2C5L; X-ray; 1.90 A; A/B=1-166.
PDB; 2CE2; X-ray; 1.00 A; X=1-166.
PDB; 2CL0; X-ray; 1.80 A; X=1-166.
PDB; 2CL6; X-ray; 1.24 A; X=1-166.
PDB; 2CL7; X-ray; 1.25 A; X=1-166.
PDB; 2CLC; X-ray; 1.30 A; X=1-166.
PDB; 2CLD; X-ray; 1.22 A; X=1-166.
PDB; 2EVW; X-ray; 1.05 A; X=1-166.
PDB; 2GDP; Model; -; A=1-171.
PDB; 2LCF; NMR; -; A=1-166.
PDB; 2LWI; NMR; -; A=1-166.
PDB; 2N42; NMR; -; A=1-166.
PDB; 2N46; NMR; -; A=1-166.
PDB; 2Q21; X-ray; 2.20 A; A=1-171.
PDB; 2QUZ; X-ray; 1.49 A; A=1-166.
PDB; 2RGA; X-ray; 1.90 A; A=1-166.
PDB; 2RGB; X-ray; 1.35 A; A=1-166.
PDB; 2RGC; X-ray; 1.60 A; A=1-166.
PDB; 2RGD; X-ray; 2.00 A; A=1-166.
PDB; 2RGE; X-ray; 1.40 A; A=1-166.
PDB; 2RGG; X-ray; 1.45 A; A=1-166.
PDB; 2UZI; X-ray; 2.00 A; R=1-166.
PDB; 2VH5; X-ray; 2.70 A; R=1-166.
PDB; 2X1V; X-ray; 1.70 A; A=1-166.
PDB; 3DDC; X-ray; 1.80 A; A=1-166.
PDB; 3I3S; X-ray; 1.36 A; R=1-166.
PDB; 3K8Y; X-ray; 1.30 A; A=1-166.
PDB; 3K9L; X-ray; 1.80 A; A/B/C=1-166.
PDB; 3K9N; X-ray; 2.00 A; A=1-166.
PDB; 3KKM; X-ray; 1.70 A; A=1-166.
PDB; 3KKN; X-ray; 2.09 A; A=1-166.
PDB; 3KUD; X-ray; 2.15 A; A=1-166.
PDB; 3L8Y; X-ray; 2.02 A; A=1-166.
PDB; 3L8Z; X-ray; 1.44 A; A=1-166.
PDB; 3LBH; X-ray; 1.85 A; A=1-166.
PDB; 3LBI; X-ray; 2.09 A; A=1-166.
PDB; 3LBN; X-ray; 1.86 A; A=1-166.
PDB; 3LO5; X-ray; 2.57 A; A/C/E=1-166.
PDB; 3OIU; X-ray; 1.32 A; A=1-166.
PDB; 3OIV; X-ray; 1.84 A; A=1-166.
PDB; 3OIW; X-ray; 1.30 A; A=1-166.
PDB; 3RRY; X-ray; 1.60 A; A=1-166.
PDB; 3RRZ; X-ray; 1.60 A; A=1-166.
PDB; 3RS0; X-ray; 1.40 A; A=1-166.
PDB; 3RS2; X-ray; 1.84 A; A=1-166.
PDB; 3RS3; X-ray; 1.52 A; A=1-166.
PDB; 3RS4; X-ray; 1.70 A; A=1-166.
PDB; 3RS5; X-ray; 1.68 A; A=1-166.
PDB; 3RS7; X-ray; 1.70 A; A=1-166.
PDB; 3RSL; X-ray; 1.70 A; A=1-166.
PDB; 3RSO; X-ray; 1.60 A; A=1-166.
PDB; 3TGP; X-ray; 1.31 A; A=1-166.
PDB; 421P; X-ray; 2.20 A; A=1-166.
PDB; 4DLR; X-ray; 1.32 A; A=1-166.
PDB; 4DLS; X-ray; 1.82 A; A=1-166.
PDB; 4DLT; X-ray; 1.70 A; A=1-166.
PDB; 4DLU; X-ray; 1.60 A; A=1-166.
PDB; 4DLV; X-ray; 1.57 A; A=1-166.
PDB; 4DLW; X-ray; 1.72 A; A=1-166.
PDB; 4DLX; X-ray; 1.73 A; A=1-166.
PDB; 4DLY; X-ray; 1.57 A; A=1-166.
PDB; 4DLZ; X-ray; 1.66 A; A=1-166.
PDB; 4DST; X-ray; 2.30 A; A=2-167.
PDB; 4DSU; X-ray; 1.70 A; A=2-167.
PDB; 4EFL; X-ray; 1.90 A; A=1-166.
PDB; 4EFM; X-ray; 1.90 A; A=1-166.
PDB; 4EFN; X-ray; 2.30 A; A=1-166.
PDB; 4G0N; X-ray; 2.45 A; A=1-166.
PDB; 4G3X; X-ray; 3.25 A; A=1-166.
PDB; 4K81; X-ray; 2.40 A; B/D/F/H=1-166.
PDB; 4L9S; X-ray; 1.61 A; A=1-166.
PDB; 4L9W; X-ray; 1.95 A; A=1-166.
PDB; 4NYI; X-ray; 2.96 A; Q/R=1-166.
PDB; 4NYJ; X-ray; 2.85 A; Q/R=1-166.
PDB; 4NYM; X-ray; 3.55 A; Q/R=1-166.
PDB; 4Q21; X-ray; 2.00 A; A=1-189.
PDB; 4RSG; Neutron; 1.91 A; A=1-166.
PDB; 4URU; X-ray; 2.83 A; R=1-166.
PDB; 4URV; X-ray; 2.58 A; R=1-166.
PDB; 4URW; X-ray; 2.76 A; R=1-166.
PDB; 4URX; X-ray; 2.49 A; R=1-166.
PDB; 4URY; X-ray; 2.47 A; R=1-166.
PDB; 4URZ; X-ray; 2.24 A; R=1-166.
PDB; 4US0; X-ray; 2.17 A; R=1-166.
PDB; 4US1; X-ray; 2.65 A; R=1-166.
PDB; 4US2; X-ray; 2.48 A; R=1-166.
PDB; 4XVQ; X-ray; 1.89 A; A=1-166.
PDB; 4XVR; X-ray; 2.03 A; A=1-166.
PDB; 521P; X-ray; 2.60 A; A=1-166.
PDB; 5B2Z; X-ray; 1.56 A; A=1-166.
PDB; 5B30; X-ray; 1.60 A; A=1-166.
PDB; 5E95; X-ray; 1.40 A; A=1-166.
PDB; 5P21; X-ray; 1.35 A; A=1-166.
PDB; 621P; X-ray; 2.40 A; A=1-166.
PDB; 6Q21; X-ray; 1.95 A; A/B/C/D=1-171.
PDB; 721P; X-ray; 2.00 A; A=1-166.
PDB; 821P; X-ray; 1.50 A; A=1-166.
PDBsum; 121P; -.
PDBsum; 1AA9; -.
PDBsum; 1AGP; -.
PDBsum; 1BKD; -.
PDBsum; 1CLU; -.
PDBsum; 1CRP; -.
PDBsum; 1CRQ; -.
PDBsum; 1CRR; -.
PDBsum; 1CTQ; -.
PDBsum; 1GNP; -.
PDBsum; 1GNQ; -.
PDBsum; 1GNR; -.
PDBsum; 1HE8; -.
PDBsum; 1IAQ; -.
PDBsum; 1IOZ; -.
PDBsum; 1JAH; -.
PDBsum; 1JAI; -.
PDBsum; 1K8R; -.
PDBsum; 1LF0; -.
PDBsum; 1LF5; -.
PDBsum; 1LFD; -.
PDBsum; 1NVU; -.
PDBsum; 1NVV; -.
PDBsum; 1NVW; -.
PDBsum; 1NVX; -.
PDBsum; 1P2S; -.
PDBsum; 1P2T; -.
PDBsum; 1P2U; -.
PDBsum; 1P2V; -.
PDBsum; 1PLJ; -.
PDBsum; 1PLK; -.
PDBsum; 1PLL; -.
PDBsum; 1Q21; -.
PDBsum; 1QRA; -.
PDBsum; 1RVD; -.
PDBsum; 1WQ1; -.
PDBsum; 1XCM; -.
PDBsum; 1XD2; -.
PDBsum; 1XJ0; -.
PDBsum; 1ZVQ; -.
PDBsum; 1ZW6; -.
PDBsum; 221P; -.
PDBsum; 2C5L; -.
PDBsum; 2CE2; -.
PDBsum; 2CL0; -.
PDBsum; 2CL6; -.
PDBsum; 2CL7; -.
PDBsum; 2CLC; -.
PDBsum; 2CLD; -.
PDBsum; 2EVW; -.
PDBsum; 2GDP; -.
PDBsum; 2LCF; -.
PDBsum; 2LWI; -.
PDBsum; 2N42; -.
PDBsum; 2N46; -.
PDBsum; 2Q21; -.
PDBsum; 2QUZ; -.
PDBsum; 2RGA; -.
PDBsum; 2RGB; -.
PDBsum; 2RGC; -.
PDBsum; 2RGD; -.
PDBsum; 2RGE; -.
PDBsum; 2RGG; -.
PDBsum; 2UZI; -.
PDBsum; 2VH5; -.
PDBsum; 2X1V; -.
PDBsum; 3DDC; -.
PDBsum; 3I3S; -.
PDBsum; 3K8Y; -.
PDBsum; 3K9L; -.
PDBsum; 3K9N; -.
PDBsum; 3KKM; -.
PDBsum; 3KKN; -.
PDBsum; 3KUD; -.
PDBsum; 3L8Y; -.
PDBsum; 3L8Z; -.
PDBsum; 3LBH; -.
PDBsum; 3LBI; -.
PDBsum; 3LBN; -.
PDBsum; 3LO5; -.
PDBsum; 3OIU; -.
PDBsum; 3OIV; -.
PDBsum; 3OIW; -.
PDBsum; 3RRY; -.
PDBsum; 3RRZ; -.
PDBsum; 3RS0; -.
PDBsum; 3RS2; -.
PDBsum; 3RS3; -.
PDBsum; 3RS4; -.
PDBsum; 3RS5; -.
PDBsum; 3RS7; -.
PDBsum; 3RSL; -.
PDBsum; 3RSO; -.
PDBsum; 3TGP; -.
PDBsum; 421P; -.
PDBsum; 4DLR; -.
PDBsum; 4DLS; -.
PDBsum; 4DLT; -.
PDBsum; 4DLU; -.
PDBsum; 4DLV; -.
PDBsum; 4DLW; -.
PDBsum; 4DLX; -.
PDBsum; 4DLY; -.
PDBsum; 4DLZ; -.
PDBsum; 4DST; -.
PDBsum; 4DSU; -.
PDBsum; 4EFL; -.
PDBsum; 4EFM; -.
PDBsum; 4EFN; -.
PDBsum; 4G0N; -.
PDBsum; 4G3X; -.
PDBsum; 4K81; -.
PDBsum; 4L9S; -.
PDBsum; 4L9W; -.
PDBsum; 4NYI; -.
PDBsum; 4NYJ; -.
PDBsum; 4NYM; -.
PDBsum; 4Q21; -.
PDBsum; 4RSG; -.
PDBsum; 4URU; -.
PDBsum; 4URV; -.
PDBsum; 4URW; -.
PDBsum; 4URX; -.
PDBsum; 4URY; -.
PDBsum; 4URZ; -.
PDBsum; 4US0; -.
PDBsum; 4US1; -.
PDBsum; 4US2; -.
PDBsum; 4XVQ; -.
PDBsum; 4XVR; -.
PDBsum; 521P; -.
PDBsum; 5B2Z; -.
PDBsum; 5B30; -.
PDBsum; 5E95; -.
PDBsum; 5P21; -.
PDBsum; 621P; -.
PDBsum; 6Q21; -.
PDBsum; 721P; -.
PDBsum; 821P; -.
DisProt; DP00153; -.
ProteinModelPortal; P01112; -.
SMR; P01112; -.
BioGrid; 109501; 99.
DIP; DIP-1050N; -.
ELM; P01112; -.
IntAct; P01112; 51.
MINT; MINT-5002362; -.
STRING; 9606.ENSP00000309845; -.
BindingDB; P01112; -.
ChEMBL; CHEMBL2167; -.
DrugBank; DB04315; Guanosine-5'-Diphosphate.
DrugBank; DB04137; Guanosine-5'-Triphosphate.
DrugBank; DB03226; Trifluoroethanol.
GuidetoPHARMACOLOGY; 2822; -.
iPTMnet; P01112; -.
PhosphoSitePlus; P01112; -.
SwissPalm; P01112; -.
BioMuta; HRAS; -.
DMDM; 131869; -.
EPD; P01112; -.
PaxDb; P01112; -.
PeptideAtlas; P01112; -.
PRIDE; P01112; -.
DNASU; 3265; -.
Ensembl; ENST00000311189; ENSP00000309845; ENSG00000174775. [P01112-1]
Ensembl; ENST00000397594; ENSP00000380722; ENSG00000174775. [P01112-2]
Ensembl; ENST00000397596; ENSP00000380723; ENSG00000174775. [P01112-1]
Ensembl; ENST00000417302; ENSP00000388246; ENSG00000174775. [P01112-2]
Ensembl; ENST00000451590; ENSP00000407586; ENSG00000174775. [P01112-1]
Ensembl; ENST00000493230; ENSP00000434023; ENSG00000174775. [P01112-2]
Ensembl; ENST00000610977; ENSP00000480686; ENSG00000276536. [P01112-1]
Ensembl; ENST00000615062; ENSP00000482366; ENSG00000276536. [P01112-1]
Ensembl; ENST00000616241; ENSP00000480317; ENSG00000276536. [P01112-2]
Ensembl; ENST00000631404; ENSP00000488757; ENSG00000276536. [P01112-1]
Ensembl; ENST00000631967; ENSP00000488225; ENSG00000276536. [P01112-2]
Ensembl; ENST00000634098; ENSP00000488296; ENSG00000276536. [P01112-2]
GeneID; 3265; -.
KEGG; hsa:3265; -.
UCSC; uc010qvw.3; human. [P01112-1]
CTD; 3265; -.
DisGeNET; 3265; -.
GeneCards; HRAS; -.
GeneReviews; HRAS; -.
HGNC; HGNC:5173; HRAS.
HPA; CAB002015; -.
HPA; HPA049830; -.
MalaCards; HRAS; -.
MIM; 109800; phenotype.
MIM; 163200; phenotype.
MIM; 188470; phenotype.
MIM; 190020; gene.
MIM; 218040; phenotype.
neXtProt; NX_P01112; -.
OpenTargets; ENSG00000174775; -.
Orphanet; 3071; Costello syndrome.
Orphanet; 2612; Linear nevus sebaceus syndrome.
Orphanet; 2874; Phakomatosis pigmentokeratotica.
PharmGKB; PA29444; -.
eggNOG; KOG0395; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00860000133672; -.
HOGENOM; HOG000233973; -.
HOVERGEN; HBG009351; -.
InParanoid; P01112; -.
KO; K02833; -.
OMA; DCMNCKC; -.
OrthoDB; EOG091G0UAU; -.
PhylomeDB; P01112; -.
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-3928662; EPHB-mediated forward signaling.
Reactome; R-HSA-442982; Ras activation uopn Ca2+ infux 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-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.
SignaLink; P01112; -.
SIGNOR; P01112; -.
EvolutionaryTrace; P01112; -.
GeneWiki; HRAS; -.
GenomeRNAi; 3265; -.
PRO; PR:P01112; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000174775; -.
CleanEx; HS_HRAS; -.
ExpressionAtlas; P01112; baseline and differential.
Genevisible; P01112; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0019003; F:GDP binding; IMP:CAFA.
GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; IDA:WormBase.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0007050; P:cell cycle arrest; IDA:BHF-UCL.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0071480; P:cellular response to gamma radiation; IDA:CAFA.
GO; GO:0090398; P:cellular senescence; IDA:BHF-UCL.
GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
GO; GO:0042832; P:defense response to protozoan; IEA:Ensembl.
GO; GO:0006897; P:endocytosis; IEA:Ensembl.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0007093; P:mitotic cell cycle checkpoint; IDA:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL.
GO; GO:0034260; P:negative regulation of GTPase activity; IDA:BHF-UCL.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IDA:BHF-UCL.
GO; GO:0030335; P:positive regulation of cell migration; IDA:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:0045740; P:positive regulation of DNA replication; IDA:BHF-UCL.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:BHF-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
GO; GO:0043547; P:positive regulation of GTPase activity; IDA:BHF-UCL.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl.
GO; GO:0046330; P:positive regulation of JNK cascade; IDA:BHF-UCL.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:BHF-UCL.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:BHF-UCL.
GO; GO:2000630; P:positive regulation of miRNA metabolic process; IDA:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL.
GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IEA:Ensembl.
GO; GO:1900029; P:positive regulation of ruffle assembly; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0090303; P:positive regulation of wound healing; IDA:BHF-UCL.
GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
GO; GO:0007265; P:Ras protein signal transduction; IDA:BHF-UCL.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
GO; GO:0035900; P:response to isolation stress; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; NAS:ProtInc.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
GO; GO:0042088; P:T-helper 1 type immune response; IEA:Ensembl.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR020849; Small_GTPase_Ras.
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; Alternative splicing; Cell membrane;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disease mutation; Golgi apparatus; GTP-binding; Lipoprotein; Membrane;
Methylation; Nucleotide-binding; Nucleus; Palmitate; Prenylation;
Proto-oncogene; Reference proteome; S-nitrosylation.
CHAIN 1 186 GTPase HRas.
/FTId=PRO_0000042996.
INIT_MET 1 1 Removed; alternate. {ECO:0000269|Ref.12}.
CHAIN 2 186 GTPase HRas, N-terminally processed.
/FTId=PRO_0000326476.
PROPEP 187 189 Removed in mature form.
/FTId=PRO_0000042997.
NP_BIND 10 17 GTP.
NP_BIND 57 61 GTP.
NP_BIND 116 119 GTP.
REGION 166 185 Hypervariable region.
MOTIF 32 40 Effector region.
MOD_RES 1 1 N-acetylmethionine; in GTPase HRas;
alternate. {ECO:0000269|Ref.12}.
MOD_RES 2 2 N-acetylthreonine; in GTPase HRas, N-
terminally processed.
{ECO:0000269|Ref.12}.
MOD_RES 104 104 N6-acetyllysine.
{ECO:0000250|UniProtKB:P01116}.
MOD_RES 118 118 S-nitrosocysteine.
{ECO:0000269|PubMed:9020151}.
MOD_RES 186 186 Cysteine methyl ester.
{ECO:0000269|PubMed:8626715}.
LIPID 181 181 S-palmitoyl cysteine.
{ECO:0000269|PubMed:15705808,
ECO:0000269|PubMed:16000296,
ECO:0000269|PubMed:2661017,
ECO:0000269|PubMed:8626715}.
LIPID 184 184 S-(15-deoxy-Delta12,14-prostaglandin J2-
9-yl)cysteine; alternate.
{ECO:0000269|PubMed:12684535}.
LIPID 184 184 S-palmitoyl cysteine; alternate.
{ECO:0000269|PubMed:15705808,
ECO:0000269|PubMed:16000296,
ECO:0000269|PubMed:2661017,
ECO:0000269|PubMed:8626715}.
LIPID 186 186 S-farnesyl cysteine.
{ECO:0000269|PubMed:8626715}.
VAR_SEQ 152 189 VEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS ->
SRSGSSSSSGTLWDPPGPM (in isoform 2).
{ECO:0000303|PubMed:14500341,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_041597.
VARIANT 12 12 G -> A (in CSTLO; dbSNP:rs104894230).
{ECO:0000269|PubMed:16170316,
ECO:0000269|PubMed:16329078,
ECO:0000269|PubMed:16443854}.
/FTId=VAR_026106.
VARIANT 12 12 G -> C (in CSTLO; dbSNP:rs104894229).
{ECO:0000269|PubMed:16443854,
ECO:0000269|PubMed:18039947}.
/FTId=VAR_045975.
VARIANT 12 12 G -> D (in CSTLO; severe mutation;
dbSNP:rs104894230).
{ECO:0000269|PubMed:18039947}.
/FTId=VAR_068816.
VARIANT 12 12 G -> E (in CSTLO).
{ECO:0000269|PubMed:16443854}.
/FTId=VAR_045976.
VARIANT 12 12 G -> S (in CSTLO and CMEMS; also found in
patients with oral squamous cell
carcinoma; dbSNP:rs104894229).
{ECO:0000269|PubMed:1459726,
ECO:0000269|PubMed:16170316,
ECO:0000269|PubMed:16329078,
ECO:0000269|PubMed:16443854,
ECO:0000269|PubMed:17054105,
ECO:0000269|PubMed:17412879}.
/FTId=VAR_006837.
VARIANT 12 12 G -> V (in CSTLO, bladder carcinoma and
CMEMS; constitutively activated;
interacts and recruits PLCE1 to plasma
membrane; dbSNP:rs104894230).
{ECO:0000269|PubMed:11022048,
ECO:0000269|PubMed:15546861,
ECO:0000269|PubMed:16170316,
ECO:0000269|PubMed:17412879}.
/FTId=VAR_006836.
VARIANT 13 13 G -> C (in CSTLO; dbSNP:rs104894228).
{ECO:0000269|PubMed:16329078}.
/FTId=VAR_026107.
VARIANT 13 13 G -> D (in CSTLO; dbSNP:rs104894226).
{ECO:0000269|PubMed:16170316}.
/FTId=VAR_026108.
VARIANT 13 13 G -> R (in SFM; somatic mutation; shows
constitutive activation of the MAPK and
PI3K-AKT signaling pathways;
dbSNP:rs104894228).
{ECO:0000269|PubMed:22683711}.
/FTId=VAR_068817.
VARIANT 22 22 Q -> K (in CMEMS; dbSNP:rs121917757).
{ECO:0000269|PubMed:17412879}.
/FTId=VAR_045977.
VARIANT 37 37 E -> EE (in CSTLO).
{ECO:0000269|PubMed:19995790}.
/FTId=VAR_068818.
VARIANT 58 58 T -> I (in CSTLO; dbSNP:rs121917758).
{ECO:0000269|PubMed:18247425}.
/FTId=VAR_045978.
VARIANT 61 61 Q -> K (in NMTC2; somatic mutation;
increases transformation of cultured cell
lines; dbSNP:rs28933406).
{ECO:0000269|PubMed:12727991,
ECO:0000269|PubMed:18073111}.
/FTId=VAR_045979.
VARIANT 61 61 Q -> L (in melanoma; strongly reduced GTP
hydrolysis in the presence of RAF1;
increases transformation of cultured cell
lines; dbSNP:rs121913233).
{ECO:0000269|PubMed:18073111}.
/FTId=VAR_006838.
VARIANT 63 63 E -> K (in CMEMS; dbSNP:rs121917756).
{ECO:0000269|PubMed:17412879}.
/FTId=VAR_045980.
VARIANT 89 89 S -> C (found in a patient with severe
fetal hydrops and pleural effusion;
unknown pathological significance;
decreased activation of Ras protein
signal transduction; dbSNP:rs755322824).
{ECO:0000269|PubMed:22821884}.
/FTId=VAR_078259.
VARIANT 117 117 K -> R (in CSTLO; dbSNP:rs104894227).
{ECO:0000269|PubMed:16443854}.
/FTId=VAR_045981.
VARIANT 146 146 A -> T (in CSTLO; dbSNP:rs104894231).
{ECO:0000269|PubMed:17054105}.
/FTId=VAR_045982.
VARIANT 146 146 A -> V (in CSTLO; dbSNP:rs121917759).
{ECO:0000269|PubMed:18247425}.
/FTId=VAR_045983.
MUTAGEN 17 17 S->N: Dominant negative. Prevents PLCE1
EGF-induced recruitment to plasma
membrane. No effect on subcellular
location of isoform 2.
{ECO:0000269|PubMed:11022048,
ECO:0000269|PubMed:14500341}.
MUTAGEN 26 26 N->G: Loss of interaction with PLCE1;
when associated with V-12.
{ECO:0000269|PubMed:11022048}.
MUTAGEN 29 29 V->A: No effect on interaction with
PLCE1; when associated with V-12.
{ECO:0000269|PubMed:11022048}.
MUTAGEN 32 32 Y->F: Loss of interaction and recruitment
to plasma membrane of PLCE1; when
associated with V-12.
{ECO:0000269|PubMed:11022048}.
MUTAGEN 34 34 P->G: No effect on interaction with
PLCE1; when associated with V-12.
{ECO:0000269|PubMed:11022048}.
MUTAGEN 35 35 T->S: Loss of interaction with PLCE1;
when associated with V-12.
{ECO:0000269|PubMed:11022048}.
MUTAGEN 37 37 E->G: No effect on interaction with
PLCE1; when associated with V-12.
{ECO:0000269|PubMed:11022048}.
MUTAGEN 38 38 D->N: No effect on interaction with
PLCE1; when associated with V-12.
{ECO:0000269|PubMed:11022048}.
MUTAGEN 39 39 S->C: No effect on interaction with
PLCE1; when associated with V-12.
{ECO:0000269|PubMed:11022048}.
MUTAGEN 59 59 A->T: Loss of GTPase activity and
creation of an autophosphorylation site.
MUTAGEN 61 61 Q->I: Moderately increased transformation
of cultured cell lines.
{ECO:0000269|PubMed:18073111}.
MUTAGEN 61 61 Q->V: Strongly increased transformation
of cultured cell lines.
{ECO:0000269|PubMed:18073111}.
MUTAGEN 83 83 A->T: GTP-binding activity reduced by
factor of 30.
{ECO:0000269|PubMed:3088563}.
MUTAGEN 118 118 C->S: Abolishes S-nitrosylation. No
stimulation of guanine nucleotide
exchange. {ECO:0000269|PubMed:12740440,
ECO:0000269|PubMed:9020151}.
MUTAGEN 119 119 D->N: Loss of GTP-binding activity.
{ECO:0000269|PubMed:3088563}.
MUTAGEN 144 144 T->I: GTP-binding activity reduced by
factor of 25.
{ECO:0000269|PubMed:3088563}.
MUTAGEN 164 165 RQ->AV: Loss of GTP-binding activity.
{ECO:0000269|PubMed:3011420}.
MUTAGEN 181 181 C->S: Exclusively localized in Golgi.
Non-specifically localized on all
endomembranes; when associated with S-
184. {ECO:0000269|PubMed:15705808,
ECO:0000269|PubMed:8626715}.
MUTAGEN 184 184 C->S: Loss of S-(15-deoxy-Delta12,14-
prostaglandin J2-9-yl)cysteine
stimulation of Ras-GTPase activity.
Mainly localized in Golgi. Non-
specifically localized on all
endomembranes; when associated with S-
181. {ECO:0000269|PubMed:12684535,
ECO:0000269|PubMed:15705808,
ECO:0000269|PubMed:8626715}.
STRAND 3 11 {ECO:0000244|PDB:2CE2}.
STRAND 12 14 {ECO:0000244|PDB:4US0}.
HELIX 16 25 {ECO:0000244|PDB:2CE2}.
STRAND 27 31 {ECO:0000244|PDB:1XCM}.
STRAND 34 37 {ECO:0000244|PDB:1XD2}.
STRAND 38 46 {ECO:0000244|PDB:2CE2}.
STRAND 49 57 {ECO:0000244|PDB:2CE2}.
STRAND 60 63 {ECO:0000244|PDB:2CLD}.
HELIX 66 74 {ECO:0000244|PDB:2CE2}.
STRAND 76 83 {ECO:0000244|PDB:2CE2}.
TURN 84 86 {ECO:0000244|PDB:1CRP}.
HELIX 87 104 {ECO:0000244|PDB:2CE2}.
STRAND 105 107 {ECO:0000244|PDB:6Q21}.
STRAND 111 116 {ECO:0000244|PDB:2CE2}.
STRAND 120 122 {ECO:0000244|PDB:2CLD}.
HELIX 127 136 {ECO:0000244|PDB:2CE2}.
STRAND 141 144 {ECO:0000244|PDB:2CE2}.
TURN 146 148 {ECO:0000244|PDB:2CE2}.
HELIX 152 164 {ECO:0000244|PDB:2CE2}.
SEQUENCE 189 AA; 21298 MW; EE6DC2D933E2856A CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHQYREQI KRVKDSDDVP MVLVGNKCDL
AARTVESRQA QDLARSYGIP YIETSAKTRQ GVEDAFYTLV REIRQHKLRK LNPPDESGPG
CMSCKCVLS


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E1294r ELISA kit c-H-ras,GTPase HRas,Hras,Hras1,H-Ras-1,p21ras,Rat,Rattus norvegicus,Transforming protein p21 96T
E1294m ELISA kit c-H-ras,GTPase HRas,Hras,Hras1,H-Ras-1,Mouse,Mus musculus,p21ras,Transforming protein p21 96T
U1294h CLIA c-H-ras,GTPase HRas,Ha-Ras,Homo sapiens,HRAS,HRAS1,H-Ras-1,Human,p21ras,Transforming protein p21 96T
E1294h ELISA c-H-ras,GTPase HRas,Ha-Ras,Homo sapiens,HRAS,HRAS1,H-Ras-1,Human,p21ras,Transforming protein p21 96T
E1294h ELISA kit c-H-ras,GTPase HRas,Ha-Ras,Homo sapiens,HRAS,HRAS1,H-Ras-1,Human,p21ras,Transforming protein p21 96T
15-288-21015 GTPase HRas - Transforming protein p21; p21ras; H-Ras-1; c-H-ras Polyclonal 0.05 mg
15-288-21015 GTPase HRas - Transforming protein p21; p21ras; H-Ras-1; c-H-ras Polyclonal 0.1 mg
E1294c ELISA Chicken,c-H-ras,Gallus gallus,GTPase HRas,HRAS1,H-Ras-1,p21ras,Transforming protein p21 96T
U1294c CLIA Chicken,c-H-ras,Gallus gallus,GTPase HRas,HRAS1,H-Ras-1,p21ras,Transforming protein p21 96T
E1294c ELISA kit Chicken,c-H-ras,Gallus gallus,GTPase HRas,HRAS1,H-Ras-1,p21ras,Transforming protein p21 96T
SPC-173C RAS Antibody, GTPase Hras, GTPase Kras, GTPase Nras, Ha Ras, K Ras, K ras p21, KRAS, NRAS, p21ras, RASH1, Polyclonal, Host Rabbit , Species reactivity Human, Mouse, Rat, Bovine 25ug
SPC-173D RAS Antibody, GTPase Hras, GTPase Kras, GTPase Nras, Ha Ras, K Ras, K ras p21, KRAS, NRAS, p21ras, RASH2, Polyclonal, Host Rabbit , Species reactivity Human, Mouse, Rat, Bovine 100ug
12059-H08B HRAS _ GTPase Hras Protein (His Tag) 100
CSB-EL010726DO Dog GTPase HRas (HRAS) ELISA kit 96T
CSB-RP155374r Recombinant rat GTPase HRas protein 500ug
CSB-RP155374r Recombinant rat GTPase HRas protein Source: E.coli 1mg
EH1468 GTPase HRas Elisa Kit 96T
YF-PA12448 anti-GTPase Hras 50 ul
P-RAS Rabbit GTPase HRAS Antibody Blocking Peptide 100
PC-RAS Rabbit GTPase HRAS Antibody Positive Control 100
gen16650 RASH_CHICK GTPase HRas ELISA tesk kit 1


 

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