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 27-MAR-2024, entry version 260. 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 RT Calu-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 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). RN [55] RP VARIANTS ALA-12; ASP-12; CYS-12; VAL-12; ASN-117 AND THR-146. RX PubMed=34820593; DOI=10.1200/po.21.00223; RA van 't Erve I., Wesdorp N.J., Medina J.E., Ferreira L., Leal A., RA Huiskens J., Bolhuis K., van Waesberghe J.T.M., Swijnenburg R.J., RA van den Broek D., Velculescu V.E., Kazemier G., Punt C.J.A., Meijer G.A., RA Fijneman R.J.A.; RT "KRAS A146 mutations are associated with distinct clinical behavior in RT patients with colorectal liver metastases."; RL JCO Precis. Oncol. 5:0-0(2021). 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; O00270: GPR31; NbExp=4; IntAct=EBI-367427, EBI-34583813; 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; 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="https://atlasgeneticsoncology.org/gene/91/KRAS"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 7KYZ; NMR; -; A=1-189. 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; 7MQU; NMR; -; A=1-169. DR PDB; 7NY8; X-ray; 1.80 A; A/B=1-167. DR PDB; 7O70; X-ray; 1.18 A; A/D=1-169. DR PDB; 7OK3; X-ray; 1.60 A; A=1-169. DR PDB; 7OK4; X-ray; 1.70 A; A=1-169. DR PDB; 7OO7; X-ray; 1.48 A; A/D=1-164. DR PDB; 7Q9U; X-ray; 2.24 A; AAA/BBB=1-176. DR PDB; 7R0M; X-ray; 1.61 A; A/B=1-169. DR PDB; 7R0N; X-ray; 1.20 A; A=1-169. DR PDB; 7R0Q; X-ray; 1.95 A; A/B=1-169. 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; 7SCW; X-ray; 1.98 A; A=1-189. DR PDB; 7SCX; X-ray; 1.96 A; A=1-189. DR PDB; 7STF; EM; 3.14 A; C=7-16. DR PDB; 7T1F; X-ray; 2.20 A; A/B/C=1-169. DR PDB; 7T47; X-ray; 1.27 A; A=1-164. DR PDB; 7TLE; X-ray; 1.99 A; A=1-164. DR PDB; 7TLG; X-ray; 1.80 A; A/B=1-164. DR PDB; 7TLK; X-ray; 1.71 A; A/B=1-164. DR PDB; 7U8H; X-ray; 1.70 A; A/B/C/D=1-169. DR PDB; 7VVB; X-ray; 1.70 A; A=1-189. DR PDB; 7W5R; X-ray; 3.87 A; A/E/I/M/Q/U=1-167. DR PDB; 7YCC; X-ray; 1.79 A; A/B/C=1-169. DR PDB; 7YCE; X-ray; 1.80 A; A=1-169. DR PDB; 7YUZ; X-ray; 1.88 A; A=2-174. DR PDB; 7YV1; X-ray; 1.45 A; A=2-174. DR PDB; 8AFB; X-ray; 1.12 A; A=1-164. DR PDB; 8AFC; X-ray; 2.41 A; A/B=1-164. DR PDB; 8AFD; X-ray; 1.63 A; A/B/C/D=1-164. DR PDB; 8AQ5; X-ray; 1.80 A; A=1-169. DR PDB; 8AQ7; X-ray; 1.65 A; A/B=1-169. DR PDB; 8AZR; X-ray; 1.60 A; A=1-164. DR PDB; 8AZV; X-ray; 1.05 A; A=1-164. DR PDB; 8AZX; X-ray; 1.04 A; A=1-164. DR PDB; 8AZY; X-ray; 1.09 A; A=1-169. DR PDB; 8AZZ; X-ray; 1.02 A; A=1-164. DR PDB; 8B00; X-ray; 1.04 A; A=1-164. DR PDB; 8B6I; X-ray; 1.70 A; A/B=1-169. DR PDB; 8B78; X-ray; 1.11 A; A=1-164. DR PDB; 8CX5; X-ray; 1.72 A; A/B=1-169. DR PDB; 8DNI; X-ray; 1.50 A; A=1-169. DR PDB; 8DNJ; X-ray; 1.81 A; A/B/C=1-169. DR PDB; 8DNK; X-ray; 2.23 A; A=1-169. DR PDB; 8DVG; X-ray; 2.59 A; C=7-16. DR PDB; 8EBZ; X-ray; 1.20 A; A=1-169. DR PDB; 8ECR; X-ray; 1.42 A; A/B=1-186. DR PDB; 8EDY; X-ray; 1.18 A; A=1-186. DR PDB; 8EER; X-ray; 1.18 A; A=1-186. DR PDB; 8EIE; X-ray; 1.41 A; A=1-186. DR PDB; 8EPW; X-ray; 2.00 A; A=1-169. DR PDB; 8EZG; X-ray; 2.52 A; A=1-167. DR PDB; 8F0M; X-ray; 2.44 A; A/C=1-169. DR PDB; 8FMJ; X-ray; 1.33 A; A=1-169. DR PDB; 8FMK; X-ray; 1.48 A; A=1-169. DR PDB; 8G42; EM; 3.02 A; B=1-169. DR PDB; 8G47; EM; 3.19 A; B=1-169. DR PDB; 8G4F; EM; 2.91 A; B=1-166. DR PDB; 8G4H; EM; 2.87 A; B=1-169. DR PDB; 8G9P; X-ray; 1.50 A; A/B=1-169. DR PDB; 8G9Q; X-ray; 1.40 A; A=1-169. DR PDB; 8I5E; X-ray; 2.20 A; P=8-16. DR PDB; 8JJS; X-ray; 1.53 A; A=2-174. DR PDB; 8ONV; X-ray; 1.01 A; A=1-164. DR PDB; 8QU8; EM; 3.50 A; F=1-164. DR PDB; 8QUG; X-ray; 1.56 A; A=1-164. DR PDB; 8QVU; X-ray; 2.24 A; A/E=1-189. DR PDB; 8QW6; X-ray; 2.20 A; A/E=1-169. DR PDB; 8QW7; X-ray; 2.36 A; A/E=1-169. DR PDB; 8STM; X-ray; 2.00 A; A/B/C/D=1-169. DR PDB; 8STN; X-ray; 2.03 A; A/B=1-169. DR PDB; 8TXE; X-ray; 1.35 A; A/B=1-169. DR PDB; 8TXG; X-ray; 1.50 A; A=1-169. DR PDB; 8TXH; X-ray; 1.20 A; A/B=1-169. 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; 7KYZ; -. DR PDBsum; 7LC1; -. DR PDBsum; 7LC2; -. DR PDBsum; 7LGI; -. DR PDBsum; 7LZ5; -. DR PDBsum; 7MDP; -. DR PDBsum; 7MQU; -. DR PDBsum; 7NY8; -. DR PDBsum; 7O70; -. DR PDBsum; 7OK3; -. DR PDBsum; 7OK4; -. DR PDBsum; 7OO7; -. DR PDBsum; 7Q9U; -. DR PDBsum; 7R0M; -. DR PDBsum; 7R0N; -. DR PDBsum; 7R0Q; -. 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; 7SCW; -. DR PDBsum; 7SCX; -. DR PDBsum; 7STF; -. DR PDBsum; 7T1F; -. DR PDBsum; 7T47; -. DR PDBsum; 7TLE; -. DR PDBsum; 7TLG; -. DR PDBsum; 7TLK; -. DR PDBsum; 7U8H; -. DR PDBsum; 7VVB; -. DR PDBsum; 7W5R; -. DR PDBsum; 7YCC; -. DR PDBsum; 7YCE; -. DR PDBsum; 7YUZ; -. DR PDBsum; 7YV1; -. DR PDBsum; 8AFB; -. DR PDBsum; 8AFC; -. DR PDBsum; 8AFD; -. DR PDBsum; 8AQ5; -. DR PDBsum; 8AQ7; -. DR PDBsum; 8AZR; -. DR PDBsum; 8AZV; -. DR PDBsum; 8AZX; -. DR PDBsum; 8AZY; -. DR PDBsum; 8AZZ; -. DR PDBsum; 8B00; -. DR PDBsum; 8B6I; -. DR PDBsum; 8B78; -. DR PDBsum; 8CX5; -. DR PDBsum; 8DNI; -. DR PDBsum; 8DNJ; -. DR PDBsum; 8DNK; -. DR PDBsum; 8DVG; -. DR PDBsum; 8EBZ; -. DR PDBsum; 8ECR; -. DR PDBsum; 8EDY; -. DR PDBsum; 8EER; -. DR PDBsum; 8EIE; -. DR PDBsum; 8EPW; -. DR PDBsum; 8EZG; -. DR PDBsum; 8F0M; -. DR PDBsum; 8FMJ; -. DR PDBsum; 8FMK; -. DR PDBsum; 8G42; -. DR PDBsum; 8G47; -. DR PDBsum; 8G4F; -. DR PDBsum; 8G4H; -. DR PDBsum; 8G9P; -. DR PDBsum; 8G9Q; -. DR PDBsum; 8I5E; -. DR PDBsum; 8JJS; -. DR PDBsum; 8ONV; -. DR PDBsum; 8QU8; -. DR PDBsum; 8QUG; -. DR PDBsum; 8QVU; -. DR PDBsum; 8QW6; -. DR PDBsum; 8QW7; -. DR PDBsum; 8STM; -. DR PDBsum; 8STN; -. DR PDBsum; 8TXE; -. DR PDBsum; 8TXG; -. DR PDBsum; 8TXH; -. DR AlphaFoldDB; P01116; -. DR BMRB; P01116; -. DR EMDB; EMD-22857; -. DR EMDB; EMD-29713; -. DR EMDB; EMD-29715; -. DR EMDB; EMD-29719; -. DR EMDB; EMD-29720; -. DR SASBDB; P01116; -. DR SMR; P01116; -. DR BioGRID; 110043; 2897. DR CORUM; P01116; -. DR DIP; DIP-33951N; -. DR IntAct; P01116; 522. 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 GlyCosmos; P01116; 1 site, No reported glycans. 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; 9606-ENSP00000256078; -. DR PeptideAtlas; P01116; -. DR ProteomicsDB; 51323; -. [P01116-1] DR ProteomicsDB; 51324; -. [P01116-2] DR Pumba; P01116; -. DR TopDownProteomics; P01116-2; -. [P01116-2] DR ABCD; P01116; 11 sequenced antibodies. DR Antibodypedia; 24248; 1031 antibodies from 39 providers. DR CPTC; P01116; 6 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 AGR; HGNC:6407; -. 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; 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; CCGGCVI; -. DR OrthoDB; 8685at2759; -. 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-9680350; Signaling by CSF1 (M-CSF) in myeloid cells. 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; 259 hits in 1133 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 218 other cell types or tissues. DR ExpressionAtlas; P01116; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. 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; IMP:DisProt. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0044877; F:protein-containing complex binding; IDA:MGI. DR GO; GO:0043495; F:protein-membrane adaptor activity; IEA:Ensembl. DR GO; GO:0030036; P:actin cytoskeleton organization; 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:0010467; P:gene expression; 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: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: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 CDD; cd04138; H_N_K_Ras_like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR24070:SF388; GTPASE KRAS; 1. DR PANTHER; PTHR24070; RAS, DI-RAS, AND RHEB FAMILY MEMBERS OF SMALL GTPASE SUPERFAMILY; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR SMART; SM00176; RAN; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51421; RAS; 1. DR Genevisible; P01116; HS. 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 colorectal cancer samples; somatic FT mutation; dbSNP:rs121913529)" FT /evidence="ECO:0000269|PubMed:16959974, FT ECO:0000269|PubMed:34820593" FT /id="VAR_036305" FT VARIANT 12 FT /note="G -> C (in lung carcinoma; somatic mutation; also FT found in metastatic colorectal cancer; dbSNP:rs121913530)" FT /evidence="ECO:0000269|PubMed:16533793, FT ECO:0000269|PubMed:34820593, 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; also FT found in metastatic colorectal cancer; 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:34820593, FT ECO:0000269|PubMed:7773929, 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; also found in FT metastatic colorectal cancer; somatic mutation; it is FT 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:34820593, FT ECO:0000269|PubMed:6092920, 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 FT GTPase-activating protein sensitivity and a strongly FT reduced 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 colorectal cancer samples; somatic FT mutation; dbSNP:rs770248150)" FT /evidence="ECO:0000269|PubMed:16959974, FT ECO:0000269|PubMed:34820593" FT /id="VAR_036307" FT VARIANT 146 FT /note="A -> T (in OES; somatic mutation; also found in FT colorectal cancer samples; dbSNP:rs121913527)" FT /evidence="ECO:0000269|PubMed:16959974, FT ECO:0000269|PubMed:26970110, ECO:0000269|PubMed:30891959, FT ECO:0000269|PubMed:34820593" 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 FT lysine-palmitoylation." FT /evidence="ECO:0000269|PubMed:29239724" FT STRAND 3..9 FT /evidence="ECO:0007829|PDB:8ONV" FT STRAND 12..14 FT /evidence="ECO:0007829|PDB:6EPO" FT HELIX 16..25 FT /evidence="ECO:0007829|PDB:8ONV" 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:8ONV" FT STRAND 49..57 FT /evidence="ECO:0007829|PDB:8ONV" FT HELIX 60..62 FT /evidence="ECO:0007829|PDB:4Q01" FT HELIX 66..73 FT /evidence="ECO:0007829|PDB:8ONV" FT STRAND 76..83 FT /evidence="ECO:0007829|PDB:8ONV" FT HELIX 87..91 FT /evidence="ECO:0007829|PDB:8ONV" FT HELIX 93..104 FT /evidence="ECO:0007829|PDB:8ONV" FT STRAND 105..107 FT /evidence="ECO:0007829|PDB:5VBM" FT STRAND 111..116 FT /evidence="ECO:0007829|PDB:8ONV" FT STRAND 120..122 FT /evidence="ECO:0007829|PDB:4OBE" FT HELIX 127..137 FT /evidence="ECO:0007829|PDB:8ONV" FT STRAND 141..143 FT /evidence="ECO:0007829|PDB:8ONV" FT TURN 146..148 FT /evidence="ECO:0007829|PDB:8ONV" FT HELIX 152..164 FT /evidence="ECO:0007829|PDB:8ONV" 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 FT protein-stimulated GTP hydrolysis but functional in FT interaction 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 //