CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001877
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 GTPase KRas 
Protein Synonyms/Alias
 K-Ras 2; Ki-Ras; c-K-ras; c-Ki-ras; GTPase KRas, N-terminally processed 
Gene Name
 KRAS 
Gene Synonyms/Alias
 KRAS2; RASK2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
117PMVLVGNKCDLPSRTubiquitination[1, 2]
128PSRTVDTKQAQDLARubiquitination[1, 2, 3, 4, 5, 6]
147PFIETSAKTRQRVEDubiquitination[4, 7]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [7] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965
Functional Description
 Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. 
Sequence Annotation
 NP_BIND 10 17 GTP.
 NP_BIND 57 61 GTP.
 NP_BIND 116 119 GTP.
 REGION 166 185 Hypervariable region.
 MOTIF 32 40 Effector region.
 MOD_RES 1 1 N-acetylmethionine; in GTPase KRas;
 MOD_RES 2 2 N-acetylthreonine; in GTPase KRas, N-
 MOD_RES 104 104 N6-acetyllysine.
 MOD_RES 186 186 Cysteine methyl ester.
 LIPID 180 180 S-palmitoyl cysteine.
 LIPID 186 186 S-farnesyl cysteine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Cardiomyopathy; Cell membrane; Complete proteome; Deafness; Direct protein sequencing; Disease mutation; GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding; Palmitate; Polymorphism; Prenylation; Proto-oncogene; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 189 AA 
Protein Sequence
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG 60
QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHHYREQI KRVKDSEDVP MVLVGNKCDL 120
PSRTVDTKQA QDLARSYGIP FIETSAKTRQ RVEDAFYTLV REIRQYRLKK ISKEEKTPGC 180
VKIKKCIIM 189 
Gene Ontology
 GO:0045121; C:membrane raft; IEA:Compara.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0019003; F:GDP binding; IEA:Compara.
 GO:0019002; F:GMP binding; IEA:Compara.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0000186; P:activation of MAPKK activity; TAS:Reactome.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0007596; P:blood coagulation; TAS:Reactome.
 GO:0019221; P:cytokine-mediated signaling pathway; IEA:Compara.
 GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
 GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
 GO:0050900; P:leukocyte migration; TAS:Reactome.
 GO:0000165; P:MAPK cascade; TAS:Reactome.
 GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
 GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
 GO:0043406; P:positive regulation of MAP kinase activity; IEA:Compara.
 GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Compara.
 GO:0051000; P:positive regulation of nitric-oxide synthase activity; IEA:Compara.
 GO:0007265; P:Ras protein signal transduction; TAS:Reactome.
 GO:0051384; P:response to glucocorticoid stimulus; IEA:Compara.
 GO:0051385; P:response to mineralocorticoid stimulus; IEA:Compara.
 GO:0035176; P:social behavior; IEA:Compara. 
Interpro
 IPR027417; P-loop_NTPase.
 IPR005225; Small_GTP-bd_dom.
 IPR001806; Small_GTPase.
 IPR020849; Small_GTPase_Ras. 
Pfam
 PF00071; Ras 
SMART
 SM00173; RAS 
PROSITE
 PS51421; RAS 
PRINTS
 PR00449; RASTRNSFRMNG.