RASK_HUMAN
ID RASK_HUMAN Reviewed; 189 AA.
AC P01116; A8K8Z5; B0LPF9; P01118; Q96D10;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 251.
DE RecName: Full=GTPase KRas;
DE EC=3.6.5.2 {ECO:0000269|PubMed:20949621};
DE AltName: Full=K-Ras 2;
DE AltName: Full=Ki-Ras;
DE AltName: Full=c-K-ras;
DE AltName: Full=c-Ki-ras;
DE Contains:
DE RecName: Full=GTPase KRas, N-terminally processed;
DE Flags: Precursor;
GN Name=KRAS; Synonyms=KRAS2, RASK2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2A AND 2B).
RX PubMed=6308466; DOI=10.1038/304501a0;
RA McGrath J.P., Capon D.J., Smith D.H., Chen E.Y., Seeburg P.H.,
RA Goeddel D.V., Levinson A.D.;
RT "Structure and organization of the human Ki-ras proto-oncogene and a
RT related processed pseudogene.";
RL Nature 304:501-506(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2A AND 2B).
RC TISSUE=Lung carcinoma;
RX PubMed=6308465; DOI=10.1038/304497a0;
RA Shimizu K., Birnbaum D., Ruley M.A., Fasano O., Suard Y., Edlund L.,
RA Taparowsky E., Goldfarb M., Wigler M.;
RT "Structure of the Ki-ras gene of the human lung carcinoma cell line Calu-
RT 1.";
RL Nature 304:497-500(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2A AND 2B).
RC TISSUE=Colon carcinoma, and Lung;
RX PubMed=6308467; DOI=10.1038/304507a0;
RA Capon D.J., Seeburg P.H., McGrath J.P., Hayflick J.S., Edman U.,
RA Levinson A.D., Goeddel D.V.;
RT "Activation of Ki-ras2 gene in human colon and lung carcinomas by two
RT different point mutations.";
RL Nature 304:507-513(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2A AND 2B), AND VARIANT COLON
RP CANCER VAL-12.
RC TISSUE=Colon carcinoma;
RX PubMed=6092920; DOI=10.1128/mcb.4.8.1577-1582.1984;
RA McCoy M.S., Bargmann C.I., Weinberg R.A.;
RT "Human colon carcinoma Ki-ras2 oncogene and its corresponding proto-
RT oncogene.";
RL Mol. Cell. Biol. 4:1577-1582(1984).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2B).
RX PubMed=3310850;
RA Kahn S., Yamamoto F., Almoguera C., Winter E., Forrester K., Jordano J.,
RA Perucho M.;
RT "The c-K-ras gene and human cancer (review).";
RL Anticancer Res. 7:639-652(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2B).
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2B), AND VARIANT LUNG
RP CARCINOMA HIS-61.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2B).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2B), AND VARIANT LUNG
RP CARCINOMA HIS-61.
RC TISSUE=Lung carcinoma;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37, AND VARIANT LUNG CARCINOMA
RP CYS-12.
RC TISSUE=Lung carcinoma;
RX PubMed=6320174; DOI=10.1073/pnas.81.1.71;
RA Nakano H., Yamamoto F., Neville C., Evans D., Mizuno T., Perucho M.;
RT "Isolation of transforming sequences of two human lung carcinomas:
RT structural and functional analysis of the activated c-K-ras oncogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:71-75(1984).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96.
RC TISSUE=Pancreatic carcinoma;
RX PubMed=3855240; DOI=10.1016/s0006-291x(85)80140-6;
RA Hirai H., Okabe T., Anraku Y., Fujisawa M., Urabe A., Takaku F.;
RT "Activation of the c-K-ras oncogene in a human pancreas carcinoma.";
RL Biochem. Biophys. Res. Commun. 127:168-174(1985).
RN [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37, AND VARIANT GASC VAL-12.
RX PubMed=3034404;
RA Deng G., Lu Y., Chen S., Miao J., Lu G., Li H., Cai H., Xu X., Zheng E.,
RA Liu P.;
RT "Activated c-Ha-ras oncogene with a guanine to thymine transversion at the
RT twelfth codon in a human stomach cancer cell line.";
RL Cancer Res. 47:3195-3198(1987).
RN [15]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36, AND VARIANT BLADDER/LUNG CANCER
RP ARG-12.
RC TISSUE=Lung carcinoma;
RX PubMed=6695174; DOI=10.1126/science.6695174;
RA Santos E., Martin-Zanca D., Reddy P.E., Pierotti M.A., Porta G.,
RA Barbacid M.;
RT "Malignant activation of a K-ras oncogene in lung carcinoma but not in
RT normal tissue of the same patient.";
RL Science 223:661-664(1984).
RN [16]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
RX PubMed=3932274;
RA Sekiya T., Tokunaga A., Fushimi M.;
RT "Essential region for transforming activity of human c-Ha-ras-1.";
RL Jpn. J. Cancer Res. 76:787-791(1985).
RN [17]
RP PROTEIN SEQUENCE OF 1-41; 43-147 AND 150-161, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT MET-1 AND THR-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Calvo F., Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
RN [18]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-96.
RC TISSUE=Lung carcinoma;
RX PubMed=6096811; DOI=10.1093/nar/12.23.8873;
RA Yamamoto F., Perucho M.;
RT "Activation of a human c-K-ras oncogene.";
RL Nucleic Acids Res. 12:8873-8885(1984).
RN [19]
RP GLYCOSYLATION AT THR-35 (MICROBIAL INFECTION).
RX PubMed=19744486; DOI=10.1016/j.febslet.2009.09.006;
RA Huelsenbeck S.C., Klose I., Reichenbach M., Huelsenbeck J., Genth H.;
RT "Distinct kinetics of (H/K/N)Ras glucosylation and Rac1 glucosylation
RT catalysed by Clostridium sordellii lethal toxin.";
RL FEBS Lett. 583:3133-3139(2009).
RN [20]
RP INTERACTION WITH RAP1GDS1.
RX PubMed=20709748; DOI=10.1074/jbc.m110.129916;
RA Berg T.J., Gastonguay A.J., Lorimer E.L., Kuhnmuench J.R., Li R.,
RA Fields A.P., Williams C.L.;
RT "Splice variants of SmgGDS control small GTPase prenylation and membrane
RT localization.";
RL J. Biol. Chem. 285:35255-35266(2010).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP ACETYLATION AT LYS-104, VARIANT VAL-12, FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=22711838; DOI=10.1073/pnas.1201487109;
RA Yang M.H., Nickerson S., Kim E.T., Liot C., Laurent G., Spang R.,
RA Philips M.R., Shan Y., Shaw D.E., Bar-Sagi D., Haigis M.C., Haigis K.M.;
RT "Regulation of RAS oncogenicity by acetylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:10843-10848(2012).
RN [23]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PDE6D.
RX PubMed=23698361; DOI=10.1038/nature12205;
RA Zimmermann G., Papke B., Ismail S., Vartak N., Chandra A., Hoffmann M.,
RA Hahn S.A., Triola G., Wittinghofer A., Bastiaens P.I., Waldmann H.;
RT "Small molecule inhibition of the KRAS-PDE? interaction impairs oncogenic
RT KRAS signalling.";
RL Nature 497:638-642(2013).
RN [24]
RP FUNCTION, AND CHARACTERIZATION OF VARIANT COLON CANCER VAL-12.
RX PubMed=24623306; DOI=10.7554/elife.02313;
RA Serra R.W., Fang M., Park S.M., Hutchinson L., Green M.R.;
RT "A KRAS-directed transcriptional silencing pathway that mediates the CpG
RT island methylator phenotype.";
RL Elife 3:E02313-E02313(2014).
RN [25]
RP INTERACTION WITH RAP1GDS1, AND ISOPRENYLATION AT CYS-186.
RX PubMed=24415755; DOI=10.1074/jbc.m113.527192;
RA Schuld N.J., Vervacke J.S., Lorimer E.L., Simon N.C., Hauser A.D.,
RA Barbieri J.T., Distefano M.D., Williams C.L.;
RT "The chaperone protein SmgGDS interacts with small GTPases entering the
RT prenylation pathway by recognizing the last amino acid in the CAAX motif.";
RL J. Biol. Chem. 289:6862-6876(2014).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [27]
RP PALMITOYLATION AT CYS-180; LYS-182; LYS-184 AND LYS-185, DEPALMITOYLATION
RP BY SIRT2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-180 AND
RP 182-LYS--LYS-185.
RX PubMed=29239724; DOI=10.7554/elife.32436;
RA Jing H., Zhang X., Wisner S.A., Chen X., Spiegelman N.A., Linder M.E.,
RA Lin H.;
RT "SIRT2 and lysine fatty acylation regulate the transforming activity of K-
RT Ras4a.";
RL Elife 6:0-0(2017).
RN [28]
RP INTERACTION WITH GPR31.
RX PubMed=28619714; DOI=10.1083/jcb.201609096;
RA Fehrenbacher N., Tojal da Silva I., Ramirez C., Zhou Y., Cho K.J.,
RA Kuchay S., Shi J., Thomas S., Pagano M., Hancock J.F., Bar-Sagi D.,
RA Philips M.R.;
RT "The G protein-coupled receptor GPR31 promotes membrane association of
RT KRAS.";
RL J. Cell Biol. 216:2329-2338(2017).
RN [29]
RP UBIQUITINATION AT LYS-170.
RX PubMed=30442762; DOI=10.1126/science.aap7607;
RA Steklov M., Pandolfi S., Baietti M.F., Batiuk A., Carai P., Najm P.,
RA Zhang M., Jang H., Renzi F., Cai Y., Abbasi Asbagh L., Pastor T.,
RA De Troyer M., Simicek M., Radaelli E., Brems H., Legius E., Tavernier J.,
RA Gevaert K., Impens F., Messiaen L., Nussinov R., Heymans S., Eyckerman S.,
RA Sablina A.A.;
RT "Mutations in LZTR1 drive human disease by dysregulating RAS
RT ubiquitination.";
RL Science 362:1177-1182(2018).
RN [30]
RP UBIQUITINATION.
RX PubMed=30442766; DOI=10.1126/science.aap8210;
RA Bigenzahn J.W., Collu G.M., Kartnig F., Pieraks M., Vladimer G.I.,
RA Heinz L.X., Sedlyarov V., Schischlik F., Fauster A., Rebsamen M.,
RA Parapatics K., Blomen V.A., Mueller A.C., Winter G.E., Kralovics R.,
RA Brummelkamp T.R., Mlodzik M., Superti-Furga G.;
RT "LZTR1 is a regulator of RAS ubiquitination and signaling.";
RL Science 362:1171-1177(2018).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 1-164 IN COMPLEX WITH THE GTP
RP ANALOG GUANOSINE-5'-DIPHOSPHATE, AND ACTIVITY REGULATION.
RX PubMed=22566140; DOI=10.1002/anie.201201358;
RA Sun Q., Burke J.P., Phan J., Burns M.C., Olejniczak E.T., Waterson A.G.,
RA Lee T., Rossanese O.W., Fesik S.W.;
RT "Discovery of small molecules that bind to K-Ras and inhibit Sos-mediated
RT activation.";
RL Angew. Chem. Int. Ed. Engl. 51:6140-6143(2012).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-164 IN COMPLEX WITH GTP ANALOGS
RP AND MAGNESIUM, FUNCTION, ACTIVITY REGULATION, INTERACTION WITH SOS1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=22431598; DOI=10.1073/pnas.1116510109;
RA Maurer T., Garrenton L.S., Oh A., Pitts K., Anderson D.J., Skelton N.J.,
RA Fauber B.P., Pan B., Malek S., Stokoe D., Ludlam M.J., Bowman K.K., Wu J.,
RA Giannetti A.M., Starovasnik M.A., Mellman I., Jackson P.K., Rudolph J.,
RA Wang W., Fang G.;
RT "Small-molecule ligands bind to a distinct pocket in Ras and inhibit SOS-
RT mediated nucleotide exchange activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5299-5304(2012).
RN [33] {ECO:0007744|PDB:5TAR, ECO:0007744|PDB:5TB5}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-164, ISOPRENYLATION AT CYS-186,
RP AND METHYLATION AT CYS-186.
RX PubMed=27791178; DOI=10.1073/pnas.1615316113;
RA Dharmaiah S., Bindu L., Tran T.H., Gillette W.K., Frank P.H., Ghirlando R.,
RA Nissley D.V., Esposito D., McCormick F., Stephen A.G., Simanshu D.K.;
RT "Structural basis of recognition of farnesylated and methylated KRAS4b by
RT PDEdelta.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E6766-E6775(2016).
RN [34]
RP VARIANT BREAST CANCER ASP-13.
RX PubMed=3627975; DOI=10.1093/nar/15.15.5963;
RA Kozma S.C., Bogaard M.E., Buser K., Saurer S.M., Bos J.L., Groner B.,
RA Hynes N.E.;
RT "The human c-Kirsten ras gene is activated by a novel mutation in codon 13
RT in the breast carcinoma cell line MDA-MB231.";
RL Nucleic Acids Res. 15:5963-5971(1987).
RN [35]
RP VARIANT BLADDER CANCER THR-59.
RX PubMed=1553789; DOI=10.1007/bf00296523;
RA Grimmond S.M., Raghavan D., Russell P.J.;
RT "Detection of a rare point mutation in Ki-ras of a human bladder cancer
RT xenograft by polymerase chain reaction and direct sequencing.";
RL Urol. Res. 20:121-126(1992).
RN [36]
RP VARIANTS PANCREATIC CARCINOMA ASP-12 AND VAL-12.
RX PubMed=8439212; DOI=10.1097/00000658-199302000-00007;
RA Motojima K., Urano T., Nagata Y., Shiku H., Tsurifune T., Kanematsu T.;
RT "Detection of point mutations in the Kirsten-ras oncogene provides evidence
RT for the multicentricity of pancreatic carcinoma.";
RL Ann. Surg. 217:138-143(1993).
RN [37]
RP VARIANTS GASC SER-12 AND ASP-12.
RX PubMed=7773929;
RX DOI=10.1002/1097-0142(19950615)75:12<2794::aid-cncr2820751203>3.0.co;2-f;
RA Lee K.H., Lee J.S., Suh C., Kim S.W., Kim S.B., Lee J.H., Lee M.S.,
RA Park M.Y., Sun H.S., Kim S.H.;
RT "Clinicopathologic significance of the K-ras gene codon 12 point mutation
RT in stomach cancer. An analysis of 140 cases.";
RL Cancer 75:2794-2801(1995).
RN [38]
RP INVOLVEMENT IN AML, VARIANT GLY-10 INS, AND CHARACTERIZATION OF VARIANT
RP GLY-10 INS.
RX PubMed=8955068; DOI=10.1074/jbc.271.51.32491;
RA Bollag G., Adler F., elMasry N., McCabe P.C., Conner E. Jr., Thompson P.,
RA McCormick F., Shannon K.;
RT "Biochemical characterization of a novel KRAS insertion mutation from a
RT human leukemia.";
RL J. Biol. Chem. 271:32491-32494(1996).
RN [39]
RP VARIANTS GASC ASN-5; VAL-12; ASP-13 AND THR-59.
RX PubMed=14534542; DOI=10.1038/sj.onc.1206749;
RA Lee S.H., Lee J.W., Soung Y.H., Kim H.S., Park W.S., Kim S.Y., Lee J.H.,
RA Park J.Y., Cho Y.G., Kim C.J., Nam S.W., Kim S.H., Lee J.Y., Yoo N.J.;
RT "BRAF and KRAS mutations in stomach cancer.";
RL Oncogene 22:6942-6945(2003).
RN [40]
RP VARIANT PYLOCYTIC ASTROCYTOMA ARG-13.
RX PubMed=16247081; DOI=10.1212/01.wnl.0000180409.78098.d7;
RA Sharma M.K., Zehnbauer B.A., Watson M.A., Gutmann D.H.;
RT "RAS pathway activation and an oncogenic RAS mutation in sporadic pilocytic
RT astrocytoma.";
RL Neurology 65:1335-1336(2005).
RN [41]
RP VARIANTS NS3 GLY-152 (ISOSORM 2) AND VAL-153 (ISOFORM 2).
RX PubMed=16773572; DOI=10.1086/504394;
RA Carta C., Pantaleoni F., Bocchinfuso G., Stella L., Vasta I., Sarkozy A.,
RA Digilio C., Palleschi A., Pizzuti A., Grammatico P., Zampino G.,
RA Dallapiccola B., Gelb B.D., Tartaglia M.;
RT "Germline missense mutations affecting KRAS Isoform B are associated with a
RT severe Noonan syndrome phenotype.";
RL Am. J. Hum. Genet. 79:129-135(2006).
RN [42]
RP VARIANTS LUNG CARCINOMA CYS-12; ASP-12; SER-12; VAL-12 AND HIS-61.
RX PubMed=16533793; DOI=10.1158/1078-0432.ccr-05-1981;
RA Tam I.Y.S., Chung L.P., Suen W.S., Wang E., Wong M.C.M., Ho K.K., Lam W.K.,
RA Chiu S.W., Girard L., Minna J.D., Gazdar A.F., Wong M.P.;
RT "Distinct epidermal growth factor receptor and KRAS mutation patterns in
RT non-small cell lung cancer patients with different tobacco exposure and
RT clinicopathologic features.";
RL Clin. Cancer Res. 12:1647-1653(2006).
RN [43]
RP VARIANT CFC2 ARG-60.
RX PubMed=16474404; DOI=10.1038/ng1749;
RA Niihori T., Aoki Y., Narumi Y., Neri G., Cave H., Verloes A., Okamoto N.,
RA Hennekam R.C.M., Gillessen-Kaesbach G., Wieczorek D., Kavamura M.I.,
RA Kurosawa K., Ohashi H., Wilson L., Heron D., Bonneau D., Corona G.,
RA Kaname T., Naritomi K., Baumann C., Matsumoto N., Kato K., Kure S.,
RA Matsubara Y.;
RT "Germline KRAS and BRAF mutations in cardio-facio-cutaneous syndrome.";
RL Nat. Genet. 38:294-296(2006).
RN [44]
RP VARIANTS NS3 ILE-14 AND ILE-58, VARIANT CFC2 ARG-34, AND CHARACTERIZATION
RP OF VARIANTS NS3 ILE-14 AND ILE-58.
RX PubMed=16474405; DOI=10.1038/ng1748;
RA Schubbert S., Zenker M., Rowe S.L., Boell S., Klein C., Bollag G.,
RA van der Burgt I., Musante L., Kalscheuer V., Wehner L.-E., Nguyen H.,
RA West B., Zhang K.Y.J., Sistermans E., Rauch A., Niemeyer C.M., Shannon K.,
RA Kratz C.P.;
RT "Germline KRAS mutations cause Noonan syndrome.";
RL Nat. Genet. 38:331-336(2006).
RN [45]
RP VARIANTS [LARGE SCALE ANALYSIS] ALA-12; ASP-12; SER-12; VAL-12; ASP-13;
RP ARG-61; ASN-117 AND THR-146.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [46]
RP VARIANTS JMML ASP-12; SER-12 AND ASP-13.
RX PubMed=17332249; DOI=10.1182/blood-2006-09-046649;
RA Matsuda K., Shimada A., Yoshida N., Ogawa A., Watanabe A., Yajima S.,
RA Iizuka S., Koike K., Yanai F., Kawasaki K., Yanagimachi M., Kikuchi A.,
RA Ohtsuka Y., Hidaka E., Yamauchi K., Tanaka M., Yanagisawa R., Nakazawa Y.,
RA Shiohara M., Manabe A., Kojima S., Koike K.;
RT "Spontaneous improvement of hematologic abnormalities in patients having
RT juvenile myelomonocytic leukemia with specific RAS mutations.";
RL Blood 109:5477-5480(2007).
RN [47]
RP VARIANT NS3 GLU-5.
RX PubMed=17468812; DOI=10.1007/s10038-007-0146-1;
RA Bertola D.R., Pereira A.C., Brasil A.S., Albano L.M., Kim C.A.,
RA Krieger J.E.;
RT "Further evidence of genetic heterogeneity in Costello syndrome:
RT involvement of the KRAS gene.";
RL J. Hum. Genet. 52:521-526(2007).
RN [48]
RP VARIANTS NS3 ILE-14; ARG-22; LEU-34; GLN-34; MET-36 AND VAL-153 (ISOFORM
RP 2), VARIANT CFC2 GLU-22, VARIANT NS3/CFC2 ILE-156 (ISOFORM 2), AND VARIANTS
RP ASN-5 AND LEU-156 (ISOFORM 2).
RX PubMed=17056636; DOI=10.1136/jmg.2006.046300;
RA Zenker M., Lehmann K., Schulz A.L., Barth H., Hansmann D., Koenig R.,
RA Korinthenberg R., Kreiss-Nachtsheim M., Meinecke P., Morlot S., Mundlos S.,
RA Quante A.S., Raskin S., Schnabel D., Wehner L.E., Kratz C.P., Horn D.,
RA Kutsche K.;
RT "Expansion of the genotypic and phenotypic spectrum in patients with KRAS
RT germline mutations.";
RL J. Med. Genet. 44:131-135(2007).
RN [49]
RP VARIANTS NS3 ILE-58 AND SER-60.
RX PubMed=19396835; DOI=10.1002/ajmg.a.32786;
RA Kratz C.P., Zampino G., Kriek M., Kant S.G., Leoni C., Pantaleoni F.,
RA Oudesluys-Murphy A.M., Di Rocco C., Kloska S.P., Tartaglia M., Zenker M.;
RT "Craniosynostosis in patients with Noonan syndrome caused by germline KRAS
RT mutations.";
RL Am. J. Med. Genet. A 149:1036-1040(2009).
RN [50]
RP CHARACTERIZATION OF VARIANTS NS3 ILE-14; ARG-22; LEU-34; ILE-58 AND VAL-153
RP (ISOFORM 2), CHARACTERIZATION OF VARIANTS CFC2 GLU-22; ARG-34 AND ARG-60,
RP CHARACTERIZATION OF VARIANTS ASN-5 AND LEU-156 (ISOFORM 2), FUNCTION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=20949621; DOI=10.1002/humu.21377;
RA Gremer L., Merbitz-Zahradnik T., Dvorsky R., Cirstea I.C., Kratz C.P.,
RA Zenker M., Wittinghofer A., Ahmadian M.R.;
RT "Germline KRAS mutations cause aberrant biochemical and physical properties
RT leading to developmental disorders.";
RL Hum. Mutat. 32:33-43(2011).
RN [51]
RP VARIANTS CFC2 HIS-71 AND GLU-147.
RX PubMed=21797849; DOI=10.1111/j.1399-0004.2011.01754.x;
RA Stark Z., Gillessen-Kaesbach G., Ryan M.M., Cirstea I.C., Gremer L.,
RA Ahmadian M.R., Savarirayan R., Zenker M.;
RT "Two novel germline KRAS mutations: expanding the molecular and clinical
RT phenotype.";
RL Clin. Genet. 81:590-594(2012).
RN [52]
RP VARIANTS OES ASP-13 AND PHE-19, AND INVOLVEMENT IN OES.
RX PubMed=25808193; DOI=10.1002/ajmg.a.37048;
RA Peacock J.D., Dykema K.J., Toriello H.V., Mooney M.R., Scholten D.J. II,
RA Winn M.E., Borgman A., Duesbery N.S., Hiemenga J.A., Liu C., Campbell S.,
RA Nickoloff B.P., Williams B.O., Steensma M.;
RT "Oculoectodermal syndrome is a mosaic RASopathy associated with KRAS
RT alterations.";
RL Am. J. Med. Genet. A 167:1429-1435(2015).
RN [53]
RP VARIANTS OES THR-146 AND VAL-146, AND INVOLVEMENT IN OES.
RX PubMed=26970110; DOI=10.1111/cge.12775;
RA Boppudi S., Boegershausen N., Hove H.B., Percin E.F., Aslan D., Dvorsky R.,
RA Kayhan G., Li Y., Cursiefen C., Tantcheva-Poor I., Toft P.B., Bartsch O.,
RA Lissewski C., Wieland I., Jakubiczka S., Wollnik B., Ahmadian M.R.,
RA Heindl L.M., Zenker M.;
RT "Specific mosaic KRAS mutations affecting codon 146 cause oculoectodermal
RT syndrome and encephalocraniocutaneous lipomatosis.";
RL Clin. Genet. 90:334-342(2016).
RN [54]
RP VARIANT SFM ASP-12, VARIANTS OES THR-146 AND VAL-146, INVOLVEMENT IN SFM,
RP AND INVOLVEMENT IN OES.
RX PubMed=30891959; DOI=10.1002/mgg3.625;
RA Chacon-Camacho O.F., Lopez-Moreno D., Morales-Sanchez M.A., Hofmann E.,
RA Pacheco-Quito M., Wieland I., Cortes-Gonzalez V., Villanueva-Mendoza C.,
RA Zenker M., Zenteno J.C.;
RT "Expansion of the phenotypic spectrum and description of molecular findings
RT in a cohort of patients with oculocutaneous mosaic RASopathies.";
RL Mol. Genet. Genomic Med. 7:E625-E625(2019).
CC -!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
CC activity (PubMed:20949621). Plays an important role in the regulation
CC of cell proliferation (PubMed:23698361, PubMed:22711838). Plays a role
CC in promoting oncogenic events by inducing transcriptional silencing of
CC tumor suppressor genes (TSGs) in colorectal cancer (CRC) cells in a
CC ZNF304-dependent manner (PubMed:24623306).
CC {ECO:0000269|PubMed:20949621, ECO:0000269|PubMed:22711838,
CC ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:24623306, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000269|PubMed:20949621};
CC -!- ACTIVITY REGULATION: Alternates between an inactive form bound to GDP
CC and an active form bound to GTP. Activated by a guanine nucleotide-
CC exchange factor (GEF) and inactivated by a GTPase-activating protein
CC (GAP). Interaction with SOS1 promotes exchange of bound GDP by GTP.
CC {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:22566140,
CC ECO:0000269|PubMed:22711838}.
CC -!- SUBUNIT: Interacts with PHLPP. Interacts (active GTP-bound form
CC preferentially) with RGS14 (By similarity). Interacts (when
CC farnesylated) with PDE6D; this promotes dissociation from the cell
CC membrane (PubMed:23698361). Interacts with SOS1 (PubMed:22431598).
CC Interacts (when farnesylated) with GPR31 (PubMed:28619714). Interacts
CC with RAP1GDS1 (PubMed:20709748, PubMed:24415755).
CC {ECO:0000250|UniProtKB:P08644, ECO:0000269|PubMed:20709748,
CC ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23698361,
CC ECO:0000269|PubMed:24415755, ECO:0000269|PubMed:28619714}.
CC -!- SUBUNIT: [Isoform 2B]: Interacts with GPR31; in a farnelysation-
CC dependent manner. {ECO:0000269|PubMed:28619714}.
CC -!- INTERACTION:
CC P01116; Q96II5: ARAF; NbExp=3; IntAct=EBI-367415, EBI-9383168;
CC P01116; Q99755: PIP5K1A; NbExp=9; IntAct=EBI-367415, EBI-726414;
CC P01116; P04049: RAF1; NbExp=6; IntAct=EBI-367415, EBI-365996;
CC P01116; P50749: RASSF2; NbExp=2; IntAct=EBI-367415, EBI-960081;
CC P01116-2; P05067: APP; NbExp=3; IntAct=EBI-367427, EBI-77613;
CC P01116-2; P01116-2: KRAS; NbExp=6; IntAct=EBI-367427, EBI-367427;
CC P01116-2; P04049: RAF1; NbExp=3; IntAct=EBI-367427, EBI-365996;
CC P01116-2; Q04631: Fnta; Xeno; NbExp=3; IntAct=EBI-367427, EBI-602447;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22431598,
CC ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor
CC {ECO:0000269|PubMed:29239724, ECO:0000305|PubMed:23698361}; Cytoplasmic
CC side {ECO:0000305|PubMed:23698361}. Endomembrane system
CC {ECO:0000269|PubMed:29239724}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:23698361}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2B]: Cell membrane
CC {ECO:0000269|PubMed:28619714}; Lipid-anchor
CC {ECO:0000305|PubMed:28619714}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Isoforms differ in the C-terminal region which is encoded by
CC two alternative exons (IVA and IVB).;
CC Name=2A; Synonyms=K-Ras4A {ECO:0000303|PubMed:29239724};
CC IsoId=P01116-1; Sequence=Displayed;
CC Name=2B; Synonyms=K-Ras4B;
CC IsoId=P01116-2, P01118-1;
CC Sequence=VSP_011140, VSP_011141;
CC -!- PTM: Acetylation at Lys-104 prevents interaction with guanine
CC nucleotide exchange factors (GEFs). {ECO:0000269|PubMed:22711838,
CC ECO:0000269|Ref.17}.
CC -!- PTM: Palmitoylated at Lys-182, Lys-184 and Lys-185 (PubMed:29239724).
CC Palmitoylation on lysine residues is promoted by palmitoylation at Cys-
CC 180 (PubMed:29239724). Lysine-depalmitoylation by SIRT2 promotes its
CC localization to endomembranes in endocytic pathways (PubMed:29239724).
CC {ECO:0000269|PubMed:29239724}.
CC -!- PTM: Ubiquitinated by the BCR(LZTR1) E3 ubiquitin ligase complex at
CC Lys-170 in a non-degradative manner, leading to inhibit Ras signaling
CC by decreasing Ras association with membranes.
CC {ECO:0000305|PubMed:30442762, ECO:0000305|PubMed:30442766}.
CC -!- PTM: (Microbial infection) Glucosylated at Thr-35 by P.sordellii toxin
CC TcsL. {ECO:0000269|PubMed:19744486}.
CC -!- DISEASE: Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of
CC acute leukemia, a cancer of the white blood cells. AML is a malignant
CC disease of bone marrow characterized by maturational arrest of
CC hematopoietic precursors at an early stage of development. Clonal
CC expansion of myeloid blasts occurs in bone marrow, blood, and other
CC tissue. Myelogenous leukemias develop from changes in cells that
CC normally produce neutrophils, basophils, eosinophils and monocytes.
CC {ECO:0000269|PubMed:8955068}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An
CC aggressive pediatric myelodysplastic syndrome/myeloproliferative
CC disorder characterized by malignant transformation in the hematopoietic
CC stem cell compartment with proliferation of differentiated progeny.
CC Patients have splenomegaly, enlarged lymph nodes, rashes, and
CC hemorrhages. {ECO:0000269|PubMed:17332249}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- DISEASE: Noonan syndrome 3 (NS3) [MIM:609942]: A form of Noonan
CC syndrome, a disease characterized by short stature, facial dysmorphic
CC features such as hypertelorism, a downward eyeslant and low-set
CC posteriorly rotated ears, and a high incidence of congenital heart
CC defects and hypertrophic cardiomyopathy. Other features can include a
CC short neck with webbing or redundancy of skin, deafness, motor delay,
CC variable intellectual deficits, multiple skeletal defects,
CC cryptorchidism, and bleeding diathesis. Individuals with Noonan
CC syndrome are at risk of juvenile myelomonocytic leukemia, a
CC myeloproliferative disorder characterized by excessive production of
CC myelomonocytic cells. {ECO:0000269|PubMed:16474405,
CC ECO:0000269|PubMed:16773572, ECO:0000269|PubMed:17056636,
CC ECO:0000269|PubMed:17468812, ECO:0000269|PubMed:19396835,
CC ECO:0000269|PubMed:20949621}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Gastric cancer (GASC) [MIM:613659]: A malignant disease which
CC starts in the stomach, can spread to the esophagus or the small
CC intestine, and can extend through the stomach wall to nearby lymph
CC nodes and organs. It also can metastasize to other parts of the body.
CC The term gastric cancer or gastric carcinoma refers to adenocarcinoma
CC of the stomach that accounts for most of all gastric malignant tumors.
CC Two main histologic types are recognized, diffuse type and intestinal
CC type carcinomas. Diffuse tumors are poorly differentiated infiltrating
CC lesions, resulting in thickening of the stomach. In contrast,
CC intestinal tumors are usually exophytic, often ulcerating, and
CC associated with intestinal metaplasia of the stomach, most often
CC observed in sporadic disease. {ECO:0000269|PubMed:14534542,
CC ECO:0000269|PubMed:3034404, ECO:0000269|PubMed:7773929}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Note=Defects in KRAS are a cause of pylocytic astrocytoma
CC (PA). Pylocytic astrocytomas are neoplasms of the brain and spinal cord
CC derived from glial cells which vary from histologically benign forms to
CC highly anaplastic and malignant tumors. {ECO:0000269|PubMed:16247081}.
CC -!- DISEASE: Cardiofaciocutaneous syndrome 2 (CFC2) [MIM:615278]: A form of
CC cardiofaciocutaneous syndrome, a multiple congenital anomaly disorder
CC characterized by a distinctive facial appearance, heart defects and
CC intellectual disability. Heart defects include pulmonic stenosis,
CC atrial septal defects and hypertrophic cardiomyopathy. Some affected
CC individuals present with ectodermal abnormalities such as sparse,
CC friable hair, hyperkeratotic skin lesions and a generalized ichthyosis-
CC like condition. Typical facial features are similar to Noonan syndrome.
CC They include high forehead with bitemporal constriction, hypoplastic
CC supraorbital ridges, downslanting palpebral fissures, a depressed nasal
CC bridge, and posteriorly angulated ears with prominent helices. CFC2
CC patients often do not have the skin abnormalities, such as ichthyosis,
CC hyperkeratosis, and hemangioma observed in CFC1.
CC {ECO:0000269|PubMed:16474404, ECO:0000269|PubMed:16474405,
CC ECO:0000269|PubMed:17056636, ECO:0000269|PubMed:20949621,
CC ECO:0000269|PubMed:21797849}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=KRAS mutations are involved in cancer development.
CC {ECO:0000269|PubMed:14534542, ECO:0000269|PubMed:1553789,
CC ECO:0000269|PubMed:16533793, ECO:0000269|PubMed:24623306,
CC ECO:0000269|PubMed:3034404, ECO:0000269|PubMed:3627975,
CC ECO:0000269|PubMed:6092920, ECO:0000269|PubMed:6695174,
CC ECO:0000269|PubMed:7773929}.
CC -!- DISEASE: Oculoectodermal syndrome (OES) [MIM:600268]: A syndrome
CC characterized by the association of epibulbar dermoids and aplasia
CC cutis congenita. Affected individuals show multiple, asymmetric,
CC atrophic, non-scarring and hairless regions that may be associated with
CC hamartomas. Ectodermal changes include linear hyperpigmentation that
CC may follow the lines of Blaschko and rarely epidermal nevus-like
CC lesions. Epibulbar dermoids may be uni-or bilateral. Additional ocular
CC anomalies such as skin tags of the upper eyelid, rarely optic nerve or
CC retinal changes, and microphthalmia can be present. The phenotypic
CC expression is highly variable, and various other abnormalities have
CC occasionally been reported including growth failure, lymphedema,
CC cardiovascular defects, as well as neurodevelopmental symptoms like
CC developmental delay, epilepsy, learning difficulties, and behavioral
CC abnormalities. Benign tumor-like lesions such as nonossifying fibromas
CC of the long bones and giant cell granulomas of the jaws have repeatedly
CC been observed and appear to be age-dependent, becoming a common
CC manifestation in individuals aged 5 years or older.
CC {ECO:0000269|PubMed:25808193, ECO:0000269|PubMed:26970110,
CC ECO:0000269|PubMed:30891959}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Schimmelpenning-Feuerstein-Mims syndrome (SFM) [MIM:163200]: A
CC disease characterized by sebaceous nevi, often on the face, associated
CC with variable ipsilateral abnormalities of the central nervous system,
CC ocular anomalies, and skeletal defects. Many oral manifestations have
CC been reported, not only including hypoplastic and malformed teeth, and
CC mucosal papillomatosis, but also ankyloglossia, hemihyperplastic
CC tongue, intraoral nevus, giant cell granuloma, ameloblastoma, bone
CC cysts, follicular cysts, oligodontia, and odontodysplasia. Sebaceous
CC nevi follow the lines of Blaschko and these can continue as linear
CC intraoral lesions, as in mucosal papillomatosis.
CC {ECO:0000269|PubMed:30891959}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/KRASID91.html";
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DR EMBL; L00049; AAB59444.1; -; Genomic_DNA.
DR EMBL; L00045; AAB59444.1; JOINED; Genomic_DNA.
DR EMBL; L00046; AAB59444.1; JOINED; Genomic_DNA.
DR EMBL; L00047; AAB59444.1; JOINED; Genomic_DNA.
DR EMBL; L00048; AAB59445.1; -; Genomic_DNA.
DR EMBL; L00045; AAB59445.1; JOINED; Genomic_DNA.
DR EMBL; L00046; AAB59445.1; JOINED; Genomic_DNA.
DR EMBL; L00047; AAB59445.1; JOINED; Genomic_DNA.
DR EMBL; M54968; AAB41942.1; -; mRNA.
DR EMBL; AF493917; AAM12631.1; -; mRNA.
DR EMBL; BT007153; AAP35817.1; -; mRNA.
DR EMBL; AK292510; BAF85199.1; -; mRNA.
DR EMBL; CH471094; EAW96511.1; -; Genomic_DNA.
DR EMBL; CH471094; EAW96512.1; -; Genomic_DNA.
DR EMBL; EU332849; ABY87538.1; -; Genomic_DNA.
DR EMBL; BC013572; AAH13572.1; -; mRNA.
DR EMBL; K01519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; K01520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M25876; AAA35683.1; -; Genomic_DNA.
DR EMBL; M34904; AAA36149.1; -; Genomic_DNA.
DR EMBL; M30539; AAA36557.1; -; Genomic_DNA.
DR EMBL; X01669; CAA25828.1; -; Genomic_DNA.
DR EMBL; X02825; CAA26593.1; -; Genomic_DNA.
DR EMBL; K03210; AAA36554.1; -; Genomic_DNA.
DR EMBL; K03209; AAA36554.1; JOINED; Genomic_DNA.
DR CCDS; CCDS8702.1; -. [P01116-2]
DR CCDS; CCDS8703.1; -. [P01116-1]
DR PIR; A93311; TVHUK.
DR PIR; B93311; TVHU2K.
DR RefSeq; NP_004976.2; NM_004985.4. [P01116-2]
DR RefSeq; NP_203524.1; NM_033360.3. [P01116-1]
DR RefSeq; XP_006719132.1; XM_006719069.3.
DR RefSeq; XP_011518955.1; XM_011520653.2.
DR PDB; 1D8D; X-ray; 2.00 A; P=178-188.
DR PDB; 1D8E; X-ray; 3.00 A; P=178-188.
DR PDB; 1KZO; X-ray; 2.20 A; C=169-173.
DR PDB; 1KZP; X-ray; 2.10 A; C=169-173.
DR PDB; 1N4P; X-ray; 2.65 A; M/N=185-189.
DR PDB; 1N4Q; X-ray; 2.40 A; M/N/O/P/Q/R=185-189.
DR PDB; 1N4R; X-ray; 2.80 A; M/N/O/P/Q/R=185-189.
DR PDB; 1N4S; X-ray; 2.60 A; M/N/O/P/Q/R=185-189.
DR PDB; 3GFT; X-ray; 2.27 A; A/B/C/D/E/F=1-164.
DR PDB; 4DSN; X-ray; 2.03 A; A=2-164.
DR PDB; 4DSO; X-ray; 1.85 A; A=2-164.
DR PDB; 4EPR; X-ray; 2.00 A; A=1-164.
DR PDB; 4EPT; X-ray; 2.00 A; A=1-164.
DR PDB; 4EPV; X-ray; 1.35 A; A=1-164.
DR PDB; 4EPW; X-ray; 1.70 A; A=1-164.
DR PDB; 4EPX; X-ray; 1.76 A; A=1-164.
DR PDB; 4EPY; X-ray; 1.80 A; A=1-164.
DR PDB; 4L8G; X-ray; 1.52 A; A=1-169.
DR PDB; 4LDJ; X-ray; 1.15 A; A=1-164.
DR PDB; 4LPK; X-ray; 1.50 A; A/B=1-169.
DR PDB; 4LRW; X-ray; 2.15 A; A/B=1-169.
DR PDB; 4LUC; X-ray; 1.29 A; A/B=1-169.
DR PDB; 4LV6; X-ray; 1.50 A; A/B=1-169.
DR PDB; 4LYF; X-ray; 1.57 A; A/B/C=1-169.
DR PDB; 4LYH; X-ray; 1.37 A; A/B/C=1-169.
DR PDB; 4LYJ; X-ray; 1.93 A; A=1-169.
DR PDB; 4M1O; X-ray; 1.57 A; A/B/C=1-169.
DR PDB; 4M1S; X-ray; 1.55 A; A/B/C=1-169.
DR PDB; 4M1T; X-ray; 1.70 A; A/B/C=1-169.
DR PDB; 4M1W; X-ray; 1.58 A; A/B/C=1-169.
DR PDB; 4M1Y; X-ray; 1.49 A; A/B/C=1-169.
DR PDB; 4M21; X-ray; 1.94 A; A/B/C=1-169.
DR PDB; 4M22; X-ray; 2.09 A; A/B/C=1-169.
DR PDB; 4NMM; X-ray; 1.89 A; A=1-164.
DR PDB; 4OBE; X-ray; 1.24 A; A/B=1-164.
DR PDB; 4PZY; X-ray; 1.88 A; A/B=1-164.
DR PDB; 4PZZ; X-ray; 1.40 A; A=1-164.
DR PDB; 4Q01; X-ray; 1.29 A; A/B=1-164.
DR PDB; 4Q02; X-ray; 1.70 A; A=1-164.
DR PDB; 4Q03; X-ray; 1.20 A; A=1-164.
DR PDB; 4QL3; X-ray; 1.04 A; A=1-11, A=13-164.
DR PDB; 4TQ9; X-ray; 1.49 A; A/B=1-164.
DR PDB; 4TQA; X-ray; 1.13 A; A/B=1-164.
DR PDB; 4WA7; X-ray; 1.99 A; A=1-164.
DR PDB; 5F2E; X-ray; 1.40 A; A=1-169.
DR PDB; 5KYK; X-ray; 2.70 A; A/B/C=1-167.
DR PDB; 5MLA; X-ray; 2.19 A; A=1-166.
DR PDB; 5MLB; X-ray; 3.22 A; A/C/E/G=1-166.
DR PDB; 5O2S; X-ray; 3.22 A; A/C/E/G=1-166.
DR PDB; 5O2T; X-ray; 2.19 A; A=1-166.
DR PDB; 5OCG; X-ray; 1.48 A; A=2-189.
DR PDB; 5OCO; X-ray; 1.66 A; A/B/C/D/E/F=1-169.
DR PDB; 5OCT; X-ray; 2.07 A; A/B/C/D/E/F=1-169.
DR PDB; 5TAR; X-ray; 1.90 A; A=2-164.
DR PDB; 5TB5; X-ray; 2.00 A; A/C=2-164.
DR PDB; 5UFE; X-ray; 2.30 A; A=1-166.
DR PDB; 5UFQ; X-ray; 2.20 A; A/B=1-166.
DR PDB; 5UK9; X-ray; 1.89 A; A/B=1-166.
DR PDB; 5UQW; X-ray; 1.50 A; A/B=1-164.
DR PDB; 5US4; X-ray; 1.83 A; A/B=1-164.
DR PDB; 5USJ; X-ray; 1.94 A; A/B/C/D/E/F=1-164.
DR PDB; 5V6S; X-ray; 1.70 A; A=1-169.
DR PDB; 5V6V; X-ray; 1.72 A; A/B=1-169.
DR PDB; 5V71; X-ray; 2.23 A; A/B/C/D/E/F=1-167.
DR PDB; 5V9L; X-ray; 1.98 A; A/B/C=1-167.
DR PDB; 5V9O; X-ray; 1.56 A; A=1-167.
DR PDB; 5V9U; X-ray; 1.38 A; A/B=1-169.
DR PDB; 5VBM; X-ray; 1.49 A; A=1-169.
DR PDB; 5VP7; X-ray; 1.70 A; A/F=1-169.
DR PDB; 5VPI; X-ray; 1.62 A; A/B=1-169.
DR PDB; 5VPY; X-ray; 2.00 A; A/B=1-169.
DR PDB; 5VPZ; X-ray; 1.85 A; A/B=1-169.
DR PDB; 5VQ0; X-ray; 2.30 A; A/B=1-169.
DR PDB; 5VQ1; X-ray; 1.78 A; A/B=1-169.
DR PDB; 5VQ2; X-ray; 1.96 A; A/B=1-169.
DR PDB; 5VQ6; X-ray; 1.99 A; A/B=1-169.
DR PDB; 5VQ8; X-ray; 2.30 A; A/B=1-169.
DR PDB; 5W22; X-ray; 1.76 A; A/B=1-169.
DR PDB; 5WHA; X-ray; 2.04 A; A/D/G/J=1-166.
DR PDB; 5WHB; X-ray; 2.18 A; A/D/G/J=1-166.
DR PDB; 5WHD; X-ray; 1.64 A; A/B/C/D=1-166.
DR PDB; 5WHE; X-ray; 1.91 A; A/D/G/J=1-166.
DR PDB; 5WLB; X-ray; 1.72 A; A/D=1-166.
DR PDB; 5WPM; X-ray; 1.72 A; A=1-166.
DR PDB; 5XCO; X-ray; 1.25 A; A=1-169.
DR PDB; 5YXZ; X-ray; 1.70 A; A=1-169.
DR PDB; 5YY1; X-ray; 1.69 A; A=1-169.
DR PDB; 6ARK; X-ray; 1.75 A; A=1-169.
DR PDB; 6ASA; X-ray; 2.54 A; A=1-167.
DR PDB; 6ASE; X-ray; 1.55 A; A=1-169.
DR PDB; 6B0V; X-ray; 1.29 A; A/B=1-169.
DR PDB; 6B0Y; X-ray; 1.43 A; A/B=1-169.
DR PDB; 6BOF; X-ray; 1.40 A; A/B=2-169.
DR PDB; 6BP1; X-ray; 2.00 A; A=1-169.
DR PDB; 6CC9; NMR; -; B=1-186.
DR PDB; 6CCH; NMR; -; B=1-186.
DR PDB; 6CCX; NMR; -; B=1-186.
DR PDB; 6CU6; X-ray; 1.50 A; A/B/C=1-169.
DR PDB; 6E6F; X-ray; 3.40 A; A/B=1-166.
DR PDB; 6E6G; X-ray; 1.93 A; A=1-166.
DR PDB; 6EPL; X-ray; 2.55 A; R=1-169.
DR PDB; 6EPM; X-ray; 2.50 A; R=1-169.
DR PDB; 6EPN; X-ray; 2.50 A; R=1-169.
DR PDB; 6EPO; X-ray; 2.40 A; R=1-169.
DR PDB; 6EPP; X-ray; 2.40 A; R=1-169.
DR PDB; 6F76; X-ray; 2.20 A; A/B/C/D/E/F=1-169.
DR PDB; 6FA1; X-ray; 1.97 A; A/C/D/F=1-167, B/E=1-169.
DR PDB; 6FA2; X-ray; 2.60 A; A/B/C/D/E/F=1-167.
DR PDB; 6FA3; X-ray; 1.82 A; A/B/C/D/E/F=1-167.
DR PDB; 6FA4; X-ray; 2.02 A; A/B/C/D/E/F=1-169.
DR PDB; 6GJ5; X-ray; 1.50 A; A/B=1-169.
DR PDB; 6GJ6; X-ray; 1.76 A; A=1-169.
DR PDB; 6GJ7; X-ray; 1.67 A; A=1-169.
DR PDB; 6GJ8; X-ray; 1.65 A; A=1-167.
DR PDB; 6GOD; X-ray; 1.71 A; A=2-173.
DR PDB; 6GOE; X-ray; 1.60 A; A=2-169.
DR PDB; 6GOF; X-ray; 1.98 A; A=2-173.
DR PDB; 6GOG; X-ray; 2.05 A; A/B/C/D/E/F=1-169.
DR PDB; 6GOM; X-ray; 1.63 A; A/B/C/D/E/F=1-167.
DR PDB; 6GQT; X-ray; 1.69 A; A/B/C/D/E/F=1-167.
DR PDB; 6GQW; X-ray; 2.80 A; A/B/C/D/E/F=1-167.
DR PDB; 6GQX; X-ray; 2.20 A; A/B/C/D/E/F=1-167.
DR PDB; 6GQY; X-ray; 2.75 A; A/B/C/D/E/F=1-167.
DR PDB; 6H46; X-ray; 2.22 A; A=1-166.
DR PDB; 6H47; X-ray; 1.70 A; A=1-166.
DR PDB; 6JTN; X-ray; 1.90 A; C=10-19.
DR PDB; 6JTO; X-ray; 1.70 A; C=10-19.
DR PDB; 6JTP; X-ray; 1.90 A; C=10-18.
DR PDB; 6M9W; X-ray; 1.50 A; A=2-169.
DR PDB; 6MBQ; X-ray; 1.35 A; A=2-166.
DR PDB; 6MBT; X-ray; 1.45 A; A/B=1-169.
DR PDB; 6MBU; X-ray; 1.45 A; A/B=1-169.
DR PDB; 6MNX; X-ray; 2.20 A; A/B/C/D/E/F=1-169.
DR PDB; 6MQG; X-ray; 1.50 A; A=3-169.
DR PDB; 6MQN; X-ray; 1.60 A; A/B/C=1-169.
DR PDB; 6MS9; X-ray; 1.49 A; A/B/C=1-169.
DR PDB; 6MTA; X-ray; 2.15 A; A/B/C=1-169.
DR PDB; 6N2J; X-ray; 1.80 A; A=1-169.
DR PDB; 6N2K; X-ray; 1.72 A; A=1-169.
DR PDB; 6O36; X-ray; 2.00 A; A/B/C=1-167.
DR PDB; 6O46; X-ray; 1.90 A; A/B/C=1-167.
DR PDB; 6O4Y; X-ray; 1.58 A; C=7-14.
DR PDB; 6O4Z; X-ray; 1.50 A; C=5-12.
DR PDB; 6O51; X-ray; 1.55 A; C=6-14.
DR PDB; 6O53; X-ray; 1.40 A; C=5-14.
DR PDB; 6OB2; X-ray; 2.85 A; A/C=1-169.
DR PDB; 6OB3; X-ray; 2.10 A; A/C=1-169.
DR PDB; 6OIM; X-ray; 1.65 A; A=1-169.
DR PDB; 6P0Z; X-ray; 1.01 A; A/B=2-169.
DR PDB; 6P8W; X-ray; 2.10 A; A/B=1-169.
DR PDB; 6P8X; X-ray; 2.11 A; A/B/C/D=1-169.
DR PDB; 6P8Y; X-ray; 2.31 A; A/B=1-169.
DR PDB; 6P8Z; X-ray; 1.65 A; A/B=1-169.
DR PDB; 6PGO; X-ray; 1.60 A; A/B=1-169.
DR PDB; 6PGP; X-ray; 1.50 A; A/B=1-169.
DR PDB; 6PQ3; X-ray; 1.75 A; A=1-169.
DR PDB; 6PTS; NMR; -; B=1-186.
DR PDB; 6PTW; NMR; -; B=1-186.
DR PDB; 6QUU; X-ray; 1.48 A; A/B=1-169.
DR PDB; 6QUV; X-ray; 1.48 A; A/B=1-169.
DR PDB; 6QUW; X-ray; 1.24 A; A/B=1-169.
DR PDB; 6QUX; X-ray; 1.62 A; A/B=1-169.
DR PDB; 6T5B; X-ray; 1.37 A; A=1-169.
DR PDB; 6T5U; X-ray; 1.72 A; B=1-166.
DR PDB; 6T5V; X-ray; 1.31 A; A=1-169.
DR PDB; 6TAM; X-ray; 1.64 A; A=1-169.
DR PDB; 6TAN; X-ray; 1.16 A; A=1-169.
DR PDB; 6USX; X-ray; 2.27 A; A/B=1-169.
DR PDB; 6USZ; X-ray; 2.03 A; A=1-169.
DR PDB; 6UT0; X-ray; 1.94 A; A/B/C/D=1-169.
DR PDB; 6V5L; NMR; -; A=1-169.
DR PDB; 6V65; X-ray; 2.76 A; C=1-169.
DR PDB; 6V6F; X-ray; 2.54 A; C=1-169.
DR PDB; 6VC8; X-ray; 2.50 A; A/B/C=1-169.
DR PDB; 6VJJ; X-ray; 1.40 A; A=1-169.
DR PDB; 6W4E; NMR; -; B/C=2-186.
DR PDB; 6W4F; NMR; -; B/C=2-186.
DR PDB; 6WGN; X-ray; 1.60 A; A/B/C=1-169.
DR PDB; 6WS2; X-ray; 1.59 A; A/B/C/D=1-169.
DR PDB; 6WS4; X-ray; 1.84 A; A/B/C/D=1-169.
DR PDB; 6XGU; X-ray; 2.70 A; A=1-169.
DR PDB; 6XGV; X-ray; 2.11 A; A=1-169.
DR PDB; 6XHA; X-ray; 2.87 A; A=1-169.
DR PDB; 6XHB; X-ray; 2.50 A; A=1-169.
DR PDB; 6YR8; X-ray; 1.90 A; A=1-166.
DR PDB; 6YXW; X-ray; 2.06 A; A/C=1-167.
DR PDB; 6ZL5; X-ray; 1.65 A; A=1-169.
DR PDB; 6ZLI; X-ray; 1.73 A; A/B=1-169.
DR PDB; 7A1W; X-ray; 1.76 A; A=1-169.
DR PDB; 7A1X; X-ray; 1.32 A; A=1-164.
DR PDB; 7A1Y; X-ray; 2.00 A; A=1-164.
DR PDB; 7A47; X-ray; 2.16 A; A/C/E=1-169.
DR PDB; 7ACA; X-ray; 1.57 A; A/B/C/D=1-169.
DR PDB; 7ACF; X-ray; 1.91 A; A/B/C/D=1-169.
DR PDB; 7ACH; X-ray; 1.90 A; A/B=1-169.
DR PDB; 7ACQ; X-ray; 1.86 A; A/B/C=1-169.
DR PDB; 7C40; X-ray; 2.52 A; A=1-167.
DR PDB; 7C41; X-ray; 2.28 A; A/G/J/M=1-167.
DR PDB; 7EW9; X-ray; 2.13 A; A/B/C=1-169.
DR PDB; 7EWA; X-ray; 2.25 A; A/B/C=1-169.
DR PDB; 7EWB; X-ray; 1.99 A; A/B/C=1-169.
DR PDB; 7EYX; X-ray; 1.82 A; A=2-169.
DR PDB; 7F0W; X-ray; 1.39 A; A=2-169.
DR PDB; 7KFZ; EM; 3.47 A; A/C=1-169.
DR PDB; 7KMR; X-ray; 1.51 A; A=1-186.
DR PDB; 7LC1; X-ray; 2.35 A; A/C=1-169.
DR PDB; 7LC2; X-ray; 2.70 A; A/B=1-169.
DR PDB; 7LGI; NMR; -; A=1-169.
DR PDB; 7LZ5; X-ray; 1.50 A; A=1-164.
DR PDB; 7MDP; X-ray; 1.96 A; A=1-169.
DR PDB; 7NY8; X-ray; 1.80 A; A/B=1-167.
DR PDB; 7Q9U; X-ray; 2.24 A; AAA/BBB=1-176.
DR PDB; 7ROV; X-ray; 1.32 A; A/B=1-189.
DR PDB; 7RP2; X-ray; 2.20 A; A=1-169.
DR PDB; 7RP3; X-ray; 2.00 A; A=2-169.
DR PDB; 7RP4; X-ray; 2.15 A; A/B=2-169.
DR PDB; 7RPZ; X-ray; 1.30 A; A=1-169.
DR PDB; 7RSC; NMR; -; A/B=2-186.
DR PDB; 7RSE; NMR; -; A/B=2-186.
DR PDB; 7RT1; X-ray; 1.27 A; A=1-169.
DR PDB; 7RT2; X-ray; 1.59 A; A=1-169.
DR PDB; 7RT3; X-ray; 1.56 A; A=1-169.
DR PDB; 7RT4; X-ray; 2.10 A; A=1-169.
DR PDB; 7RT5; X-ray; 1.29 A; A=1-169.
DR PDB; 7T47; X-ray; 1.27 A; A=1-164.
DR PDBsum; 1D8D; -.
DR PDBsum; 1D8E; -.
DR PDBsum; 1KZO; -.
DR PDBsum; 1KZP; -.
DR PDBsum; 1N4P; -.
DR PDBsum; 1N4Q; -.
DR PDBsum; 1N4R; -.
DR PDBsum; 1N4S; -.
DR PDBsum; 3GFT; -.
DR PDBsum; 4DSN; -.
DR PDBsum; 4DSO; -.
DR PDBsum; 4EPR; -.
DR PDBsum; 4EPT; -.
DR PDBsum; 4EPV; -.
DR PDBsum; 4EPW; -.
DR PDBsum; 4EPX; -.
DR PDBsum; 4EPY; -.
DR PDBsum; 4L8G; -.
DR PDBsum; 4LDJ; -.
DR PDBsum; 4LPK; -.
DR PDBsum; 4LRW; -.
DR PDBsum; 4LUC; -.
DR PDBsum; 4LV6; -.
DR PDBsum; 4LYF; -.
DR PDBsum; 4LYH; -.
DR PDBsum; 4LYJ; -.
DR PDBsum; 4M1O; -.
DR PDBsum; 4M1S; -.
DR PDBsum; 4M1T; -.
DR PDBsum; 4M1W; -.
DR PDBsum; 4M1Y; -.
DR PDBsum; 4M21; -.
DR PDBsum; 4M22; -.
DR PDBsum; 4NMM; -.
DR PDBsum; 4OBE; -.
DR PDBsum; 4PZY; -.
DR PDBsum; 4PZZ; -.
DR PDBsum; 4Q01; -.
DR PDBsum; 4Q02; -.
DR PDBsum; 4Q03; -.
DR PDBsum; 4QL3; -.
DR PDBsum; 4TQ9; -.
DR PDBsum; 4TQA; -.
DR PDBsum; 4WA7; -.
DR PDBsum; 5F2E; -.
DR PDBsum; 5KYK; -.
DR PDBsum; 5MLA; -.
DR PDBsum; 5MLB; -.
DR PDBsum; 5O2S; -.
DR PDBsum; 5O2T; -.
DR PDBsum; 5OCG; -.
DR PDBsum; 5OCO; -.
DR PDBsum; 5OCT; -.
DR PDBsum; 5TAR; -.
DR PDBsum; 5TB5; -.
DR PDBsum; 5UFE; -.
DR PDBsum; 5UFQ; -.
DR PDBsum; 5UK9; -.
DR PDBsum; 5UQW; -.
DR PDBsum; 5US4; -.
DR PDBsum; 5USJ; -.
DR PDBsum; 5V6S; -.
DR PDBsum; 5V6V; -.
DR PDBsum; 5V71; -.
DR PDBsum; 5V9L; -.
DR PDBsum; 5V9O; -.
DR PDBsum; 5V9U; -.
DR PDBsum; 5VBM; -.
DR PDBsum; 5VP7; -.
DR PDBsum; 5VPI; -.
DR PDBsum; 5VPY; -.
DR PDBsum; 5VPZ; -.
DR PDBsum; 5VQ0; -.
DR PDBsum; 5VQ1; -.
DR PDBsum; 5VQ2; -.
DR PDBsum; 5VQ6; -.
DR PDBsum; 5VQ8; -.
DR PDBsum; 5W22; -.
DR PDBsum; 5WHA; -.
DR PDBsum; 5WHB; -.
DR PDBsum; 5WHD; -.
DR PDBsum; 5WHE; -.
DR PDBsum; 5WLB; -.
DR PDBsum; 5WPM; -.
DR PDBsum; 5XCO; -.
DR PDBsum; 5YXZ; -.
DR PDBsum; 5YY1; -.
DR PDBsum; 6ARK; -.
DR PDBsum; 6ASA; -.
DR PDBsum; 6ASE; -.
DR PDBsum; 6B0V; -.
DR PDBsum; 6B0Y; -.
DR PDBsum; 6BOF; -.
DR PDBsum; 6BP1; -.
DR PDBsum; 6CC9; -.
DR PDBsum; 6CCH; -.
DR PDBsum; 6CCX; -.
DR PDBsum; 6CU6; -.
DR PDBsum; 6E6F; -.
DR PDBsum; 6E6G; -.
DR PDBsum; 6EPL; -.
DR PDBsum; 6EPM; -.
DR PDBsum; 6EPN; -.
DR PDBsum; 6EPO; -.
DR PDBsum; 6EPP; -.
DR PDBsum; 6F76; -.
DR PDBsum; 6FA1; -.
DR PDBsum; 6FA2; -.
DR PDBsum; 6FA3; -.
DR PDBsum; 6FA4; -.
DR PDBsum; 6GJ5; -.
DR PDBsum; 6GJ6; -.
DR PDBsum; 6GJ7; -.
DR PDBsum; 6GJ8; -.
DR PDBsum; 6GOD; -.
DR PDBsum; 6GOE; -.
DR PDBsum; 6GOF; -.
DR PDBsum; 6GOG; -.
DR PDBsum; 6GOM; -.
DR PDBsum; 6GQT; -.
DR PDBsum; 6GQW; -.
DR PDBsum; 6GQX; -.
DR PDBsum; 6GQY; -.
DR PDBsum; 6H46; -.
DR PDBsum; 6H47; -.
DR PDBsum; 6JTN; -.
DR PDBsum; 6JTO; -.
DR PDBsum; 6JTP; -.
DR PDBsum; 6M9W; -.
DR PDBsum; 6MBQ; -.
DR PDBsum; 6MBT; -.
DR PDBsum; 6MBU; -.
DR PDBsum; 6MNX; -.
DR PDBsum; 6MQG; -.
DR PDBsum; 6MQN; -.
DR PDBsum; 6MS9; -.
DR PDBsum; 6MTA; -.
DR PDBsum; 6N2J; -.
DR PDBsum; 6N2K; -.
DR PDBsum; 6O36; -.
DR PDBsum; 6O46; -.
DR PDBsum; 6O4Y; -.
DR PDBsum; 6O4Z; -.
DR PDBsum; 6O51; -.
DR PDBsum; 6O53; -.
DR PDBsum; 6OB2; -.
DR PDBsum; 6OB3; -.
DR PDBsum; 6OIM; -.
DR PDBsum; 6P0Z; -.
DR PDBsum; 6P8W; -.
DR PDBsum; 6P8X; -.
DR PDBsum; 6P8Y; -.
DR PDBsum; 6P8Z; -.
DR PDBsum; 6PGO; -.
DR PDBsum; 6PGP; -.
DR PDBsum; 6PQ3; -.
DR PDBsum; 6PTS; -.
DR PDBsum; 6PTW; -.
DR PDBsum; 6QUU; -.
DR PDBsum; 6QUV; -.
DR PDBsum; 6QUW; -.
DR PDBsum; 6QUX; -.
DR PDBsum; 6T5B; -.
DR PDBsum; 6T5U; -.
DR PDBsum; 6T5V; -.
DR PDBsum; 6TAM; -.
DR PDBsum; 6TAN; -.
DR PDBsum; 6USX; -.
DR PDBsum; 6USZ; -.
DR PDBsum; 6UT0; -.
DR PDBsum; 6V5L; -.
DR PDBsum; 6V65; -.
DR PDBsum; 6V6F; -.
DR PDBsum; 6VC8; -.
DR PDBsum; 6VJJ; -.
DR PDBsum; 6W4E; -.
DR PDBsum; 6W4F; -.
DR PDBsum; 6WGN; -.
DR PDBsum; 6WS2; -.
DR PDBsum; 6WS4; -.
DR PDBsum; 6XGU; -.
DR PDBsum; 6XGV; -.
DR PDBsum; 6XHA; -.
DR PDBsum; 6XHB; -.
DR PDBsum; 6YR8; -.
DR PDBsum; 6YXW; -.
DR PDBsum; 6ZL5; -.
DR PDBsum; 6ZLI; -.
DR PDBsum; 7A1W; -.
DR PDBsum; 7A1X; -.
DR PDBsum; 7A1Y; -.
DR PDBsum; 7A47; -.
DR PDBsum; 7ACA; -.
DR PDBsum; 7ACF; -.
DR PDBsum; 7ACH; -.
DR PDBsum; 7ACQ; -.
DR PDBsum; 7C40; -.
DR PDBsum; 7C41; -.
DR PDBsum; 7EW9; -.
DR PDBsum; 7EWA; -.
DR PDBsum; 7EWB; -.
DR PDBsum; 7EYX; -.
DR PDBsum; 7F0W; -.
DR PDBsum; 7KFZ; -.
DR PDBsum; 7KMR; -.
DR PDBsum; 7LC1; -.
DR PDBsum; 7LC2; -.
DR PDBsum; 7LGI; -.
DR PDBsum; 7LZ5; -.
DR PDBsum; 7MDP; -.
DR PDBsum; 7NY8; -.
DR PDBsum; 7Q9U; -.
DR PDBsum; 7ROV; -.
DR PDBsum; 7RP2; -.
DR PDBsum; 7RP3; -.
DR PDBsum; 7RP4; -.
DR PDBsum; 7RPZ; -.
DR PDBsum; 7RSC; -.
DR PDBsum; 7RSE; -.
DR PDBsum; 7RT1; -.
DR PDBsum; 7RT2; -.
DR PDBsum; 7RT3; -.
DR PDBsum; 7RT4; -.
DR PDBsum; 7RT5; -.
DR PDBsum; 7T47; -.
DR AlphaFoldDB; P01116; -.
DR BMRB; P01116; -.
DR SASBDB; P01116; -.
DR SMR; P01116; -.
DR BioGRID; 110043; 1824.
DR CORUM; P01116; -.
DR DIP; DIP-33951N; -.
DR IntAct; P01116; 517.
DR MINT; P01116; -.
DR STRING; 9606.ENSP00000256078; -.
DR BindingDB; P01116; -.
DR ChEMBL; CHEMBL2189121; -.
DR DrugBank; DB07771; [(3,7,11-TRIMETHYL-DODECA-2,6,10-TRIENYLOXYCARBAMOYL)-METHYL]-PHOSPHONIC ACID.
DR DrugBank; DB15568; Adagrasib.
DR DrugBank; DB07780; Farnesyl diphosphate.
DR DrugBank; DB15569; Sotorasib.
DR GuidetoPHARMACOLOGY; 2824; -.
DR iPTMnet; P01116; -.
DR PhosphoSitePlus; P01116; -.
DR SwissPalm; P01116; -.
DR BioMuta; KRAS; -.
DR DMDM; 131875; -.
DR CPTAC; CPTAC-1550; -.
DR EPD; P01116; -.
DR jPOST; P01116; -.
DR MassIVE; P01116; -.
DR MaxQB; P01116; -.
DR PaxDb; P01116; -.
DR PeptideAtlas; P01116; -.
DR PRIDE; P01116; -.
DR ProteomicsDB; 51323; -. [P01116-1]
DR ProteomicsDB; 51324; -. [P01116-2]
DR TopDownProteomics; P01116-2; -. [P01116-2]
DR ABCD; P01116; 11 sequenced antibodies.
DR Antibodypedia; 24248; 927 antibodies from 39 providers.
DR CPTC; P01116; 5 antibodies.
DR DNASU; 3845; -.
DR Ensembl; ENST00000256078.10; ENSP00000256078.5; ENSG00000133703.14. [P01116-1]
DR Ensembl; ENST00000311936.8; ENSP00000308495.3; ENSG00000133703.14. [P01116-2]
DR Ensembl; ENST00000685328.1; ENSP00000508921.1; ENSG00000133703.14. [P01116-2]
DR Ensembl; ENST00000688940.1; ENSP00000509238.1; ENSG00000133703.14. [P01116-2]
DR GeneID; 3845; -.
DR KEGG; hsa:3845; -.
DR MANE-Select; ENST00000311936.8; ENSP00000308495.3; NM_004985.5; NP_004976.2. [P01116-2]
DR UCSC; uc001rgp.3; human. [P01116-1]
DR CTD; 3845; -.
DR DisGeNET; 3845; -.
DR GeneCards; KRAS; -.
DR GeneReviews; KRAS; -.
DR HGNC; HGNC:6407; KRAS.
DR HPA; ENSG00000133703; Low tissue specificity.
DR MalaCards; KRAS; -.
DR MIM; 163200; phenotype.
DR MIM; 190070; gene.
DR MIM; 600268; phenotype.
DR MIM; 601626; phenotype.
DR MIM; 607785; phenotype.
DR MIM; 609942; phenotype.
DR MIM; 613659; phenotype.
DR MIM; 615278; phenotype.
DR neXtProt; NX_P01116; -.
DR OpenTargets; ENSG00000133703; -.
DR Orphanet; 1340; Cardiofaciocutaneous syndrome.
DR Orphanet; 146; Differentiated thyroid carcinoma.
DR Orphanet; 2396; Encephalocraniocutaneous lipomatosis.
DR Orphanet; 1333; Familial pancreatic carcinoma.
DR Orphanet; 86834; Juvenile myelomonocytic leukemia.
DR Orphanet; 2612; Linear nevus sebaceus syndrome.
DR Orphanet; 144; Lynch syndrome.
DR Orphanet; 648; Noonan syndrome.
DR Orphanet; 251615; Pilomyxoid astrocytoma.
DR Orphanet; 268114; RAS-associated autoimmune leukoproliferative disease.
DR Orphanet; 357194; Selection of therapeutic option in colorectal cancer.
DR Orphanet; 357191; Selection of therapeutic option in non-small cell lung carcinoma.
DR Orphanet; 3339; Toriello-Lacassie-Droste syndrome.
DR PharmGKB; PA30196; -.
DR VEuPathDB; HostDB:ENSG00000133703; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000155871; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; P01116; -.
DR OMA; CCSGCVV; -.
DR PhylomeDB; P01116; -.
DR TreeFam; TF312796; -.
DR BRENDA; 3.6.5.2; 2681.
DR PathwayCommons; P01116; -.
DR Reactome; R-HSA-112412; SOS-mediated signalling.
DR Reactome; R-HSA-1169092; Activation of RAS in B cells.
DR Reactome; R-HSA-1236382; Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
DR Reactome; R-HSA-1250196; SHC1 events in ERBB2 signaling.
DR Reactome; R-HSA-1250347; SHC1 events in ERBB4 signaling.
DR Reactome; R-HSA-1433557; Signaling by SCF-KIT.
DR Reactome; R-HSA-167044; Signalling to RAS.
DR Reactome; R-HSA-171007; p38MAPK events.
DR Reactome; R-HSA-179812; GRB2 events in EGFR signaling.
DR Reactome; R-HSA-180336; SHC1 events in EGFR signaling.
DR Reactome; R-HSA-186763; Downstream signal transduction.
DR Reactome; R-HSA-1963640; GRB2 events in ERBB2 signaling.
DR Reactome; R-HSA-210993; Tie2 Signaling.
DR Reactome; R-HSA-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-HSA-2424491; DAP12 signaling.
DR Reactome; R-HSA-2428933; SHC-related events triggered by IGF1R.
DR Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
DR Reactome; R-HSA-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-HSA-4086398; Ca2+ pathway. [P01116-2]
DR Reactome; R-HSA-442982; Ras activation upon Ca2+ influx through NMDA receptor.
DR Reactome; R-HSA-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-HSA-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-HSA-5637810; Constitutive Signaling by EGFRvIII.
DR Reactome; R-HSA-5654688; SHC-mediated cascade:FGFR1.
DR Reactome; R-HSA-5654693; FRS-mediated FGFR1 signaling.
DR Reactome; R-HSA-5654699; SHC-mediated cascade:FGFR2.
DR Reactome; R-HSA-5654700; FRS-mediated FGFR2 signaling.
DR Reactome; R-HSA-5654704; SHC-mediated cascade:FGFR3.
DR Reactome; R-HSA-5654706; FRS-mediated FGFR3 signaling.
DR Reactome; R-HSA-5654712; FRS-mediated FGFR4 signaling.
DR Reactome; R-HSA-5654719; SHC-mediated cascade:FGFR4.
DR Reactome; R-HSA-5655253; Signaling by FGFR2 in disease.
DR Reactome; R-HSA-5655291; Signaling by FGFR4 in disease.
DR Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
DR Reactome; R-HSA-5655332; Signaling by FGFR3 in disease.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR Reactome; R-HSA-5673000; RAF activation.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-5674135; MAP2K and MAPK activation.
DR Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
DR Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions.
DR Reactome; R-HSA-6802953; RAS signaling downstream of NF1 loss-of-function variants.
DR Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
DR Reactome; R-HSA-74751; Insulin receptor signalling cascade.
DR Reactome; R-HSA-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-HSA-8851805; MET activates RAS signaling.
DR Reactome; R-HSA-8951936; RUNX3 regulates p14-ARF.
DR Reactome; R-HSA-9026519; Activated NTRK2 signals through RAS.
DR Reactome; R-HSA-9027284; Erythropoietin activates RAS.
DR Reactome; R-HSA-9028731; Activated NTRK2 signals through FRS2 and FRS3.
DR Reactome; R-HSA-9034864; Activated NTRK3 signals through RAS.
DR Reactome; R-HSA-9607240; FLT3 Signaling.
DR Reactome; R-HSA-9634285; Constitutive Signaling by Overexpressed ERBB2.
DR Reactome; R-HSA-9634635; Estrogen-stimulated signaling through PRKCZ.
DR Reactome; R-HSA-9648002; RAS processing.
DR Reactome; R-HSA-9649948; Signaling downstream of RAS mutants.
DR Reactome; R-HSA-9656223; Signaling by RAF1 mutants.
DR Reactome; R-HSA-9664565; Signaling by ERBB2 KD Mutants.
DR Reactome; R-HSA-9665348; Signaling by ERBB2 ECD mutants.
DR Reactome; R-HSA-9665686; Signaling by ERBB2 TMD/JMD mutants.
DR Reactome; R-HSA-9670439; Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants.
DR Reactome; R-HSA-9673767; Signaling by PDGFRA transmembrane, juxtamembrane and kinase domain mutants.
DR Reactome; R-HSA-9673770; Signaling by PDGFRA extracellular domain mutants.
DR Reactome; R-HSA-9674555; Signaling by CSF3 (G-CSF).
DR Reactome; R-HSA-9703465; Signaling by FLT3 fusion proteins.
DR Reactome; R-HSA-9703648; Signaling by FLT3 ITD and TKD mutants.
DR Reactome; R-HSA-9753510; Signaling by RAS GAP mutants.
DR Reactome; R-HSA-9753512; Signaling by RAS GTPase mutants.
DR SignaLink; P01116; -.
DR SIGNOR; P01116; -.
DR BioGRID-ORCS; 3845; 255 hits in 1047 CRISPR screens.
DR ChiTaRS; KRAS; human.
DR EvolutionaryTrace; P01116; -.
DR GeneWiki; KRAS; -.
DR GenomeRNAi; 3845; -.
DR Pharos; P01116; Tclin.
DR PRO; PR:P01116; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P01116; protein.
DR Bgee; ENSG00000133703; Expressed in trigeminal ganglion and 216 other tissues.
DR ExpressionAtlas; P01116; baseline and differential.
DR Genevisible; P01116; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0038002; P:endocrine signaling; IEA:Ensembl.
DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl.
DR GO; GO:0021897; P:forebrain astrocyte development; IEA:Ensembl.
DR GO; GO:0014009; P:glial cell proliferation; IEA:Ensembl.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
DR GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR GO; GO:0030857; P:negative regulation of epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:BHF-UCL.
DR GO; GO:0035022; P:positive regulation of Rac protein signal transduction; IEA:Ensembl.
DR GO; GO:0016601; P:Rac protein signal transduction; IEA:Ensembl.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
DR GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IEA:Ensembl.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0060509; P:type I pneumocyte differentiation; IEA:Ensembl.
DR GO; GO:0008542; P:visual learning; IEA:Ensembl.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR020849; Small_GTPase_Ras-type.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51421; RAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cardiomyopathy;
KW Cell membrane; Cytoplasm; Deafness; Direct protein sequencing;
KW Disease variant; Ectodermal dysplasia; Glycoprotein; GTP-binding;
KW Hydrolase; Intellectual disability; Isopeptide bond; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Palmitate; Prenylation; Proto-oncogene;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..186
FT /note="GTPase KRas"
FT /id="PRO_0000082641"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|Ref.17"
FT CHAIN 2..186
FT /note="GTPase KRas, N-terminally processed"
FT /id="PRO_0000326480"
FT PROPEP 187..189
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:27791178"
FT /id="PRO_0000281291"
FT REGION 166..185
FT /note="Hypervariable region"
FT MOTIF 32..40
FT /note="Effector region"
FT BINDING 10..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:22431598,
FT ECO:0000269|PubMed:22566140"
FT BINDING 29..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:22431598,
FT ECO:0000269|PubMed:22566140"
FT BINDING 59..60
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:22431598,
FT ECO:0000269|PubMed:22566140"
FT BINDING 116..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:22431598,
FT ECO:0000269|PubMed:22566140"
FT MOD_RES 1
FT /note="N-acetylmethionine; in GTPase KRas; alternate"
FT /evidence="ECO:0000269|Ref.17"
FT MOD_RES 2
FT /note="N-acetylthreonine; in GTPase KRas, N-terminally
FT processed"
FT /evidence="ECO:0000269|Ref.17"
FT MOD_RES 104
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:22711838"
FT MOD_RES 186
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000269|PubMed:27791178,
FT ECO:0007744|PDB:5TAR, ECO:0007744|PDB:5TB5"
FT LIPID 180
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:29239724"
FT LIPID 182
FT /note="N6-palmitoyl lysine"
FT /evidence="ECO:0000269|PubMed:29239724"
FT LIPID 184
FT /note="N6-palmitoyl lysine"
FT /evidence="ECO:0000305|PubMed:29239724"
FT LIPID 185
FT /note="N6-palmitoyl lysine"
FT /evidence="ECO:0000305|PubMed:29239724"
FT LIPID 186
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:27791178,
FT ECO:0000305|PubMed:24415755, ECO:0007744|PDB:5TAR,
FT ECO:0007744|PDB:5TB5"
FT CARBOHYD 35
FT /note="(Microbial infection) O-linked (Glc) threonine; by
FT P.sordellii toxin TcsL"
FT /evidence="ECO:0000269|PubMed:19744486"
FT CROSSLNK 170
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000305|PubMed:30442762"
FT VAR_SEQ 151..153
FT /note="RVE -> GVD (in isoform 2B)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:3310850,
FT ECO:0000303|Ref.6, ECO:0000303|Ref.7"
FT /id="VSP_011140"
FT VAR_SEQ 165..189
FT /note="QYRLKKISKEEKTPGCVKIKKCIIM -> KHKEKMSKDGKKKKKKSKTKCVI
FT M (in isoform 2B)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:3310850,
FT ECO:0000303|Ref.6, ECO:0000303|Ref.7"
FT /id="VSP_011141"
FT VARIANT 5
FT /note="K -> E (in NS3; dbSNP:rs193929331)"
FT /evidence="ECO:0000269|PubMed:17468812"
FT /id="VAR_065144"
FT VARIANT 5
FT /note="K -> N (in GASC; found also in a patient with
FT Costello syndrome; exhibits only minor alterations in its
FT in vitro biochemical behavior compared to wild-type
FT protein; dbSNP:rs104894361)"
FT /evidence="ECO:0000269|PubMed:14534542"
FT /id="VAR_064849"
FT VARIANT 10
FT /note="G -> GG (in AML; expression in 3T3 cell causes
FT cellular transformation; expression in COS cells activates
FT the Ras-MAPK signaling pathway; lower GTPase activity;
FT faster GDP dissociation rate)"
FT /evidence="ECO:0000269|PubMed:8955068"
FT /id="VAR_034601"
FT VARIANT 12
FT /note="G -> A (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs121913529)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036305"
FT VARIANT 12
FT /note="G -> C (in lung carcinoma; somatic mutation;
FT dbSNP:rs121913530)"
FT /evidence="ECO:0000269|PubMed:16533793,
FT ECO:0000269|PubMed:6320174"
FT /id="VAR_006839"
FT VARIANT 12
FT /note="G -> D (in GASC, JMML and SFM; somatic mutation;
FT also found in pancreatic carcinoma and lung carcinoma;
FT dbSNP:rs121913529)"
FT /evidence="ECO:0000269|PubMed:16533793,
FT ECO:0000269|PubMed:16959974, ECO:0000269|PubMed:17332249,
FT ECO:0000269|PubMed:30891959, ECO:0000269|PubMed:7773929,
FT ECO:0000269|PubMed:8439212"
FT /id="VAR_016026"
FT VARIANT 12
FT /note="G -> R (in lung cancer and bladder cancer; somatic
FT mutation; dbSNP:rs121913530)"
FT /evidence="ECO:0000269|PubMed:6695174"
FT /id="VAR_016027"
FT VARIANT 12
FT /note="G -> S (in GASC and JMML; also found in lung
FT carcinoma; somatic mutation; dbSNP:rs121913530)"
FT /evidence="ECO:0000269|PubMed:16533793,
FT ECO:0000269|PubMed:16959974, ECO:0000269|PubMed:17332249,
FT ECO:0000269|PubMed:7773929"
FT /id="VAR_016028"
FT VARIANT 12
FT /note="G -> V (in GASC; also found in lung carcinoma,
FT pancreatic carcinoma and colon cancer; somatic mutation; it
FT is constitutively activated and stimulates transcription
FT activation of tumor suppressor genes in non-transformed
FT fibroblasts; dbSNP:rs121913529)"
FT /evidence="ECO:0000269|PubMed:14534542,
FT ECO:0000269|PubMed:16533793, ECO:0000269|PubMed:16959974,
FT ECO:0000269|PubMed:22711838, ECO:0000269|PubMed:24623306,
FT ECO:0000269|PubMed:3034404, ECO:0000269|PubMed:6092920,
FT ECO:0000269|PubMed:8439212"
FT /id="VAR_006840"
FT VARIANT 13
FT /note="G -> D (in GASC, JMML and OES; also found in a
FT breast carcinoma cell line; somatic mutation;
FT dbSNP:rs112445441)"
FT /evidence="ECO:0000269|PubMed:14534542,
FT ECO:0000269|PubMed:16959974, ECO:0000269|PubMed:17332249,
FT ECO:0000269|PubMed:25808193, ECO:0000269|PubMed:3627975"
FT /id="VAR_016029"
FT VARIANT 13
FT /note="G -> R (in pylocytic astrocytoma; somatic mutation;
FT increase activation of the Ras pathway; dbSNP:rs121913535)"
FT /evidence="ECO:0000269|PubMed:16247081"
FT /id="VAR_065145"
FT VARIANT 14
FT /note="V -> I (in NS3; affects activity and impairs
FT responsiveness to GTPase activating proteins; characterized
FT by a strong increase of both intrinsic and guanine
FT nucleotide exchanged factor-catalyzed nucleotide exchange
FT leading to an increased level of the activated state;
FT dbSNP:rs104894365)"
FT /evidence="ECO:0000269|PubMed:16474405"
FT /id="VAR_026109"
FT VARIANT 19
FT /note="L -> F (in OES; somatic mutation;
FT dbSNP:rs121913538)"
FT /evidence="ECO:0000269|PubMed:25808193"
FT /id="VAR_083261"
FT VARIANT 22
FT /note="Q -> E (in CFC2; exhibits an increase in intrinsic
FT and guanine nucleotide exchange factor catalyzed nucleotide
FT exchange in combination with an impaired GTPase-activating
FT protein-stimulated GTP hydrolysis but functional in
FT interaction with effectors; dbSNP:rs121913236)"
FT /evidence="ECO:0000269|PubMed:17056636,
FT ECO:0000269|PubMed:20949621"
FT /id="VAR_064850"
FT VARIANT 22
FT /note="Q -> R (in NS3; impairs GTPase-activating protein
FT stimulated GTP hydrolysis with unaffected intrinsic
FT functions and a virtually functional effector interaction;
FT dbSNP:rs727503110)"
FT /id="VAR_064851"
FT VARIANT 34
FT /note="P -> L (in NS3; characterized by a defective GTPase-
FT activating protein sensitivity and a strongly reduced
FT interaction with effectors; dbSNP:rs104894366)"
FT /id="VAR_064852"
FT VARIANT 34
FT /note="P -> Q (in NS3)"
FT /id="VAR_064853"
FT VARIANT 34
FT /note="P -> R (in CFC2; characterized by a defective
FT GTPase-activating protein sensitivity and a strongly
FT reduced interaction with effectors; dbSNP:rs104894366)"
FT /evidence="ECO:0000269|PubMed:16474405,
FT ECO:0000269|PubMed:20949621"
FT /id="VAR_026110"
FT VARIANT 36
FT /note="I -> M (in NS3; dbSNP:rs727503109)"
FT /id="VAR_064854"
FT VARIANT 58
FT /note="T -> I (in NS3; affects activity and impairs
FT responsiveness to GTPase activating proteins; exhibits only
FT minor alterations in its in vitro biochemical behavior
FT compared to wild-type protein; dbSNP:rs104894364)"
FT /evidence="ECO:0000269|PubMed:16474405,
FT ECO:0000269|PubMed:19396835"
FT /id="VAR_026111"
FT VARIANT 59
FT /note="A -> T (in GASC; also found in bladder cancer;
FT somatic mutation; dbSNP:rs121913528)"
FT /evidence="ECO:0000269|PubMed:14534542,
FT ECO:0000269|PubMed:1553789"
FT /id="VAR_016030"
FT VARIANT 60
FT /note="G -> R (in CFC2; characterized by a defective
FT GTPase-activating protein sensitivity and a strongly
FT reduced interaction with effectors; dbSNP:rs104894359)"
FT /evidence="ECO:0000269|PubMed:16474404,
FT ECO:0000269|PubMed:20949621"
FT /id="VAR_026112"
FT VARIANT 60
FT /note="G -> S (in NS3; dbSNP:rs104894359)"
FT /evidence="ECO:0000269|PubMed:19396835"
FT /id="VAR_065146"
FT VARIANT 61
FT /note="Q -> H (in lung carcinoma; dbSNP:rs17851045)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16533793, ECO:0000269|Ref.7"
FT /id="VAR_006841"
FT VARIANT 61
FT /note="Q -> R (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs121913240)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036306"
FT VARIANT 71
FT /note="Y -> H (in CFC2; dbSNP:rs387907205)"
FT /evidence="ECO:0000269|PubMed:21797849"
FT /id="VAR_069784"
FT VARIANT 117
FT /note="K -> N (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs770248150)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036307"
FT VARIANT 146
FT /note="A -> T (in OES; somatic mutation; also found in a
FT colorectal cancer sample; dbSNP:rs121913527)"
FT /evidence="ECO:0000269|PubMed:16959974,
FT ECO:0000269|PubMed:26970110, ECO:0000269|PubMed:30891959"
FT /id="VAR_036308"
FT VARIANT 146
FT /note="A -> V (in OES; somatic mutation;
FT dbSNP:rs1057519725)"
FT /evidence="ECO:0000269|PubMed:26970110,
FT ECO:0000269|PubMed:30891959"
FT /id="VAR_083262"
FT VARIANT 147
FT /note="K -> E (in CFC2; dbSNP:rs387907206)"
FT /evidence="ECO:0000269|PubMed:21797849"
FT /id="VAR_069785"
FT MUTAGEN 180
FT /note="C->S: Abolished palmitoylation on Cys; reduced
FT palmitoylation on Lys residues."
FT /evidence="ECO:0000269|PubMed:29239724"
FT MUTAGEN 182..185
FT /note="KIKK->RIRR: In K-Ras-3KR; abolished lysine-
FT palmitoylation."
FT /evidence="ECO:0000269|PubMed:29239724"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:6P0Z"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:6EPO"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:6P0Z"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:7F0W"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:6H46"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:6P0Z"
FT STRAND 49..57
FT /evidence="ECO:0007829|PDB:6P0Z"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:4Q01"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:6P0Z"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:6P0Z"
FT HELIX 87..104
FT /evidence="ECO:0007829|PDB:6P0Z"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:5VBM"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:6P0Z"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:4OBE"
FT HELIX 127..136
FT /evidence="ECO:0007829|PDB:6P0Z"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:6P0Z"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:6P0Z"
FT HELIX 152..167
FT /evidence="ECO:0007829|PDB:6P0Z"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:5OCG"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:4DSN"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:5TB5"
FT VARIANT P01116-2:152
FT /note="V -> G (in NS3; dbSNP:rs104894367)"
FT /evidence="ECO:0000305"
FT /id="VAR_082908"
FT VARIANT P01116-2:153
FT /note="D -> V (in CFC2 and NS3, exhibits only minor
FT alterations in its in vitro biochemical behavior compared
FT to wild-type protein; dbSNP:rs104894360)"
FT /evidence="ECO:0000305"
FT /id="VAR_082909"
FT VARIANT P01116-2:156
FT /note="F -> I (in NS3/CFC2; dbSNP:rs397517042)"
FT /evidence="ECO:0000305"
FT /id="VAR_082910"
FT VARIANT P01116-2:156
FT /note="F -> L (found in a patient with Costello syndrome,
FT exhibits an increase in intrinsic and guanine nucleotide
FT exchange factor catalyzed nucleotide exchange in
FT combination with an impaired GTPase-activating protein-
FT stimulated GTP hydrolysis but functional in interaction
FT with effectors; dbSNP:rs104894362)"
FT /evidence="ECO:0000305"
FT /id="VAR_082911"
FT MUTAGEN P01116-2:185
FT /note="C->S: Abolished interaction with GPR131."
FT /evidence="ECO:0000269|PubMed:28619714"
SQ SEQUENCE 189 AA; 21656 MW; 973547B2E11C2C81 CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHHYREQI KRVKDSEDVP MVLVGNKCDL
PSRTVDTKQA QDLARSYGIP FIETSAKTRQ RVEDAFYTLV REIRQYRLKK ISKEEKTPGC
VKIKKCIIM
