CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001876
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 GTPase NRas 
Protein Synonyms/Alias
 Transforming protein N-Ras 
Gene Name
 NRAS 
Gene Synonyms/Alias
 HRAS1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
88VFAINNSKSFADINLmethylation[1]
117PMVLVGNKCDLPTRTubiquitination[2, 3]
128PTRTVDTKQAHELAKubiquitination[2, 3, 4, 5, 6, 7, 8, 9]
147PFIETSAKTRQGVEDubiquitination[3, 5, 7, 8]
Reference
 [1] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510]
 [2] 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]
 [3] 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]
 [4] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [5] 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]
 [6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [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]
 [8] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [9] 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
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 186 186 Cysteine methyl ester (By similarity).
 LIPID 181 181 S-palmitoyl cysteine.
 LIPID 186 186 S-farnesyl cysteine.  
Keyword
 3D-structure; Acetylation; Cell membrane; Complete proteome; Disease mutation; Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding; Palmitate; 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 VFAINNSKSF ADINLYREQI KRVKDSDDVP MVLVGNKCDL 120
PTRTVDTKQA HELAKSYGIP FIETSAKTRQ GVEDAFYTLV REIRQYRMKK LNSSDDGTQG 180
CMGLPCVVM 189 
Gene Ontology
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IEA:InterPro.
 GO:0030036; P:actin cytoskeleton organization; IEA:Compara.
 GO:0000186; P:activation of MAPKK activity; TAS:Reactome.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0007596; P:blood coagulation; TAS:Reactome.
 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:0043524; P:negative regulation of neuron apoptotic process; IEA:Compara.
 GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
 GO:0008284; P:positive regulation of cell proliferation; IEA:Compara.
 GO:0035022; P:positive regulation of Rac protein signal transduction; IEA:Compara.
 GO:0007265; P:Ras protein signal transduction; TAS:Reactome.
 GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Compara.
 GO:0032228; P:regulation of synaptic transmission, GABAergic; IEA:Compara.
 GO:0051146; P:striated muscle cell differentiation; IEA:Compara.
 GO:0008542; P:visual learning; 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.