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UniProtKB/Swiss-Prot entry P01112


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RASH_HUMAN
Primary accession number P01112
Secondary accession numbers Q14080 Q6FHV9
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 120)
Name and origin of the protein
Protein name GTPase HRas [Precursor]
Synonyms Transforming protein p21
p21ras
H-Ras-1
c-H-ras
Ha-Ras
Gene name
Name: HRAS
Synonyms: HRAS1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1038/302033a0; PubMed=6298635 [NCBI, ExPASy, EBI, Israel, Japan]
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].
PubMed=6844927 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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 [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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
DOI=10.1038/300143a0; PubMed=6290897 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
PubMed=3670300 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
PROTEIN SEQUENCE OF 1-41; 43-117; 129-161 AND 170-185, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND THR-2, AND MASS SPECTROMETRY.
TISSUE=Cervix carcinoma;
Bienvenut W.V., Calvo F., Kolch W.;
Submitted (FEB-2008) to UniProtKB.
[11]
MUTAGENESIS OF ALA-83; ASP-119 AND THR-144.
PubMed=3088563 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
MUTAGENESIS OF 164-ARG-GLN-165.
PubMed=3011420 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[13]
PALMITOYLATION AT CYS-181 AND CYS-184.
DOI=10.1016/0092-8674(89)90054-8; PubMed=2661017 [NCBI, ExPASy, EBI, Israel, Japan]
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]
PALMITOYLATION AT CYS-181 AND CYS-184, ISOPRENYLATION AT CYS-186, METHYLATION AT CYS-186, AND MUTAGENESIS OF CYS-181 AND CYS-184.
DOI=10.1074/jbc.271.19.11541; PubMed=8626715 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[15]
S-NITROSYLATION AT CYS-118, FUNCTION, MASS SPECTROMETRY, AND MUTAGENESIS OF CYS-118.
DOI=10.1074/jbc.272.7.4323; PubMed=9020151 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[16]
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.
DOI=10.1074/jbc.M008324200; PubMed=11022048 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[17]
IDENTIFICATION IN A COMPLEX WITH RASGRP1 AND DGKZ.
DOI=10.1083/jcb.152.6.1135; PubMed=11257115 [NCBI, ExPASy, EBI, Israel, Japan]
Topham M.K., Prescott S.M.;
"Diacylglycerol kinase zeta regulates Ras activation by a novel mechanism.";
J. Cell Biol. 152:1135-1143(2001).
[18]
PALMITOYLATION AT CYS-181 AND CYS-184.
DOI=10.1074/jbc.M504113200; PubMed=16000296 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[19]
PALMITOYLATION AT CYS-181 AND CYS-184, MUTAGENESIS OF CYS-181 AND CYS-184, AND SUBCELLULAR LOCATION.
DOI=10.1126/science.1105654; PubMed=15705808 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[20]
INTERACTION WITH TBC1D10C.
DOI=10.1038/nature05476; PubMed=17230191 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[21]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed=2448879 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[22]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
DOI=10.1038/341209a0; PubMed=2476675 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[23]
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
PubMed=2196171 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[24]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
DOI=10.1016/0022-2836(91)90753-S; PubMed=1899707 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[25]
STRUCTURE BY NMR OF 1-166.
DOI=10.1021/bi00178a008; PubMed=8142349 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[26]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-166 IN COMPLEX WITH RASGAP.
DOI=10.1126/science.277.5324.333; PubMed=9219684 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[27]
X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS).
DOI=10.1016/S0969-2126(00)80021-0; PubMed=10574788 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[28]
STRUCTURE BY NMR OF 1-166, MASS SPECTROMETRY, S-NITROSYLATION, FUNCTION, AND MUTAGENESIS OF CYS-118.
DOI=10.1073/pnas.1037299100; PubMed=12740440 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[29]
VARIANT OSCC SER-12.
PubMed=1459726 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[30]
VARIANT LYS-61, AND INVOLVEMENT IN SUSCEPTIBILITY TO HURTHLE CELL THYROID CARCINOMA.
DOI=10.1210/jc.2002-021907; PubMed=12727991 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[31]
VARIANTS COSTELLO SYNDROME ALA-12; SER-12; VAL-12 AND ASP-13.
DOI=10.1038/ng1641; PubMed=16170316 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[32]
VARIANTS COSTELLO SYNDROME ALA-12; SER-12 AND CYS-13.
DOI=10.1002/ajmg.a.31047; PubMed=16329078 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[33]
VARIANTS COSTELLO SYNDROME SER-12; CYS-12; GLU-12; ALA-12 AND ARG-117.
DOI=10.1136/jmg.2005.040352; PubMed=16443854 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[34]
VARIANTS COSTELLO SYNDROME SER-12 AND THR-146.
DOI=10.1002/humu.20431; PubMed=17054105 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[35]
VARIANTS CMEMS VAL-12; SER-12; LYS-22 AND LYS-63.
DOI=10.1136/jmg.2007.049270; PubMed=17412879 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[36]
VARIANTS COSTELLO SYNDROME ILE-58 AND VAL-146.
DOI=10.1002/ajmg.a.32227; PubMed=18247425 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J00277; AAB02605.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF493916; AAM12630.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT019421; AAV38228.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR536579; CAG38816.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR542271; CAG47067.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC095471; AAH95471.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M17232; AAA35685.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A93299; TVHUH.
RefSeq NP_001123914.1; -.
NP_005334.1; -.
UniGene Hs.37003
3D structure databases
PDB
121P; X-ray; 1.54 A; A=1-166.[ExPASy / RCSB / EBI]
1AA9; NMR; -; A=1-171.[ExPASy / RCSB / EBI]
1AGP; X-ray; 2.30 A; A=1-166.[ExPASy / RCSB / EBI]
1BKD; X-ray; 2.80 A; R=1-166.[ExPASy / RCSB / EBI]
1CLU; X-ray; 1.70 A; A=1-166.[ExPASy / RCSB / EBI]
1CRP; NMR; -; A=1-166.[ExPASy / RCSB / EBI]
1CRQ; NMR; -; A=1-166.[ExPASy / RCSB / EBI]
1CRR; NMR; -; A=1-166.[ExPASy / RCSB / EBI]
1CTQ; X-ray; 1.26 A; A=1-166.[ExPASy / RCSB / EBI]
1GNP; X-ray; 2.70 A; A=1-166.[ExPASy / RCSB / EBI]
1GNQ; X-ray; 2.50 A; A=1-166.[ExPASy / RCSB / EBI]
1GNR; X-ray; 1.85 A; A=1-166.[ExPASy / RCSB / EBI]
1HE8; X-ray; 3.00 A; B=1-166.[ExPASy / RCSB / EBI]
1IAQ; X-ray; 2.90 A; A/B/C=1-166.[ExPASy / RCSB / EBI]
1IOZ; X-ray; 2.00 A; A=1-171.[ExPASy / RCSB / EBI]
1JAH; X-ray; 1.80 A; A=1-166.[ExPASy / RCSB / EBI]
1JAI; X-ray; 1.80 A; A=1-166.[ExPASy / RCSB / EBI]
1K8R; X-ray; 3.00 A; A=1-166.[ExPASy / RCSB / EBI]
1LF0; X-ray; 1.70 A; A=1-166.[ExPASy / RCSB / EBI]
1LF5; X-ray; 1.70 A; A=1-166.[ExPASy / RCSB / EBI]
1LFD; X-ray; 2.10 A; B/D=1-167.[ExPASy / RCSB / EBI]
1NVU; X-ray; 2.20 A; Q/R=1-166.[ExPASy / RCSB / EBI]
1NVV; X-ray; 2.18 A; Q/R=1-166.[ExPASy / RCSB / EBI]
1NVW; X-ray; 2.70 A; Q/R=1-166.[ExPASy / RCSB / EBI]
1NVX; X-ray; 3.20 A; Q/R=1-166.[ExPASy / RCSB / EBI]
1P2S; X-ray; 2.45 A; A=1-166.[ExPASy / RCSB / EBI]
1P2T; X-ray; 2.00 A; A=1-166.[ExPASy / RCSB / EBI]
1P2U; X-ray; 2.00 A; A=1-166.[ExPASy / RCSB / EBI]
1P2V; X-ray; 2.30 A; A=1-166.[ExPASy / RCSB / EBI]
1PLJ; X-ray; 2.80 A; A=1-166.[ExPASy / RCSB / EBI]
1PLK; X-ray; 2.80 A; A=1-166.[ExPASy / RCSB / EBI]
1PLL; X-ray; 2.80 A; A=1-166.[ExPASy / RCSB / EBI]
1Q21; X-ray; 2.20 A; A=1-171.[ExPASy / RCSB / EBI]
1QRA; X-ray; 1.60 A; A=1-166.[ExPASy / RCSB / EBI]
1RVD; X-ray; 1.90 A; A=1-166.[ExPASy / RCSB / EBI]
1WQ1; X-ray; 2.50 A; R=1-166.[ExPASy / RCSB / EBI]
1XCM; X-ray; 1.84 A; A=1-167.[ExPASy / RCSB / EBI]
1XD2; X-ray; 2.70 A; A/B=1-166.[ExPASy / RCSB / EBI]
1XJ0; X-ray; 1.70 A; A=1-166.[ExPASy / RCSB / EBI]
1ZVQ; X-ray; 2.00 A; A=1-166.[ExPASy / RCSB / EBI]
1ZW6; X-ray; 1.50 A; A=1-166.[ExPASy / RCSB / EBI]
221P; X-ray; 2.30 A; A=1-166.[ExPASy / RCSB / EBI]
2C5L; X-ray; 1.90 A; A/B=1-166.[ExPASy / RCSB / EBI]
2CE2; X-ray; 1.00 A; X=1-166.[ExPASy / RCSB / EBI]
2CL0; X-ray; 1.80 A; X=1-166.[ExPASy / RCSB / EBI]
2CL6; X-ray; 1.24 A; X=1-166.[ExPASy / RCSB / EBI]
2CL7; X-ray; 1.25 A; X=1-166.[ExPASy / RCSB / EBI]
2CLC; X-ray; 1.30 A; X=1-166.[ExPASy / RCSB / EBI]
2CLD; X-ray; 1.22 A; X=1-166.[ExPASy / RCSB / EBI]
2EVW; X-ray; 1.05 A; X=1-166.[ExPASy / RCSB / EBI]
2GDP; Model; -; A=1-171.[ExPASy / RCSB / EBI]
2Q21; X-ray; 2.20 A; A=1-171.[ExPASy / RCSB / EBI]
2QUZ; X-ray; 1.49 A; A=1-166.[ExPASy / RCSB / EBI]
2RGA; X-ray; 1.90 A; A=1-166.[ExPASy / RCSB / EBI]
2RGB; X-ray; 1.35 A; A=1-166.[ExPASy / RCSB / EBI]
2RGC; X-ray; 1.60 A; A=1-166.[ExPASy / RCSB / EBI]
2RGD; X-ray; 2.00 A; A=1-166.[ExPASy / RCSB / EBI]
2RGE; X-ray; 1.40 A; A=1-166.[ExPASy / RCSB / EBI]
2RGG; X-ray; 1.45 A; A=1-166.[ExPASy / RCSB / EBI]
2UZI; X-ray; 2.00 A; R=1-166.[ExPASy / RCSB / EBI]
2VH5; X-ray; 2.70 A; R=1-166.[ExPASy / RCSB / EBI]
3DDC; X-ray; 1.80 A; A=1-166.[ExPASy / RCSB / EBI]
421P; X-ray; 2.20 A; A=1-166.[ExPASy / RCSB / EBI]
4Q21; X-ray; 2.00 A; A=1-189.[ExPASy / RCSB / EBI]
521P; X-ray; 2.60 A; A=1-166.[ExPASy / RCSB / EBI]
5P21; X-ray; 1.35 A; A=1-166.[ExPASy / RCSB / EBI]
621P; X-ray; 2.40 A; A=1-166.[ExPASy / RCSB / EBI]
6Q21; X-ray; 1.95 A; A/B/C/D=1-171.[ExPASy / RCSB / EBI]
721P; X-ray; 2.00 A; A=1-166.[ExPASy / RCSB / EBI]
821P; X-ray; 1.50 A; A=1-166.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 121P; -.
1AA9; -.
1AGP; -.
1BKD; -.
1CLU; -.
1CRP; -.
1CRQ; -.
1CRR; -.
1CTQ; -.
1GNP; -.
1GNQ; -.
1GNR; -.
1HE8; -.
1IAQ; -.
1IOZ; -.
1JAH; -.
1JAI; -.
1K8R; -.
1LF0; -.
1LF5; -.
1LFD; -.
1NVU; -.
1NVV; -.
1NVW; -.
1NVX; -.
1P2S; -.
1P2T; -.
1P2U; -.
1P2V; -.
1PLJ; -.
1PLK; -.
1PLL; -.
1Q21; -.
1QRA; -.
1RVD; -.
1WQ1; -.
1XCM; -.
1XD2; -.
1XJ0; -.
1ZVQ; -.
1ZW6; -.
221P; -.
2C5L; -.
2CE2; -.
2CL0; -.
2CL6; -.
2CL7; -.
2CLC; -.
2CLD; -.
2EVW; -.
2GDP; -.
2Q21; -.
2QUZ; -.
2RGA; -.
2RGB; -.
2RGC; -.
2RGD; -.
2RGE; -.
2RGG; -.
2UZI; -.
2VH5; -.
3DDC; -.
421P; -.
4Q21; -.
521P; -.
5P21; -.
621P; -.
6Q21; -.
721P; -.
821P; -.
DisProt DP00153; -.
ModBase P01112.
Protein-protein interaction databases
DIP DIP:1050N; -.
IntAct P01112; -.
PTM databases
PhosphoSite P01112; -.
Enzyme and pathway databases
Reactome REACT_498; Signaling by insulin receptor.
Organism-specific databases
H-InvDB HIX0009354; -.
HGNC HGNC:5173; HRAS.
GenAtlas HRAS.
HPA CAB002015; -.
MIM 109800; phenotype. [NCBI / EBI]
190020; gene. [NCBI / EBI]
218040; phenotype. [NCBI / EBI]
607464; phenotype. [NCBI / EBI]
Orphanet 3071; Costello syndrome.
PharmGKB PA29444; -.
GeneCards P01112.
Gene expression databases
ArrayExpress P01112; -.
CleanEx HS_HRAS; -.
GermOnline ENSG00000174775; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (traceable author statement from ProtInc).
GO:0005886; Cellular component: plasma membrane (traceable author statement from ProtInc).
GO:0008022; Molecular function: protein C-terminus binding (inferred from physical interaction from UniProtKB).
GO:0007166; Biological process: cell surface receptor linked signal transduction (traceable author statement from ProtInc).
GO:0006935; Biological process: chemotaxis (traceable author statement from ProtInc).
GO:0009887; Biological process: organ morphogenesis (traceable author statement from ProtInc).
GO:0007265; Biological process: Ras protein signal transduction (inferred from experiment from Reactome).
QuickGo view.
Family and domain databases
InterPro IPR003577; GTPase_Ras.
IPR013753; Ras.
IPR015592; Ras_Ras_related.
IPR001806; Ras_trnsfrmng.
IPR005225; Small_GTP_bd.
Graphical view of domain structure.
PANTHER PTHR11708:SF125; Ras_Ras_related; 1.
Pfam PF00071; Ras; 1.
Pfam graphical view of domain structure.
PRINTS PR00449; RASTRNSFRMNG.
SMART SM00173; RAS; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR00231; small_GTP; 1.
BLOCKS P01112.
ProtoNet P01112.
Other
SWISS-3DIMAGE P01112.
Genome annotation databases
Ensembl ENSG00000174775; Homo sapiens. [Contig view]
GeneID 3265; -.
KEGG hsa:3265; -.
Phylogenomic databases
HOVERGEN P01112; -.
Other
DrugBank DB00605; Sulindac.
LinkHub P01112; -.
NextBio 12961; -.
SOURCE HRAS; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Cell membrane; Direct protein sequencing; Disease mutation; Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding; Palmitate; Prenylation; Proto-oncogene; S-nitrosylation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   186  186     GTPase HRas. PRO_0000042996
INIT_MET   1     1        Removed; alternate. 
CHAIN   2   186  185     GTPase HRas. PRO_0000326476
PROPEP   187   189  3     Removed in mature form. PRO_0000042997
NP_BIND   10    17  8     GTP. 
NP_BIND   57    61  5     GTP. 
NP_BIND   116   119  4     GTP. 
REGION   166   185  20     Hypervariable region. 
MOTIF   32    40  9     Effector region. 
MOD_RES   1     1        N-acetylmethionine; alternate. 
MOD_RES