RASN_MOUSE
ID RASN_MOUSE Reviewed; 189 AA.
AC P08556;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=GTPase NRas;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01116};
DE AltName: Full=Transforming protein N-Ras;
DE Flags: Precursor;
GN Name=Nras;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3865197; DOI=10.1073/pnas.82.23.7810;
RA Guerrero I., Villasante A., Corces V., Pellicer A.;
RT "Loss of the normal N-ras allele in a mouse thymic lymphoma induced by a
RT chemical carcinogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:7810-7814(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=2835730;
RA Chang H.Y., Guerrero I., Lake R., Pellicer A., D'Eustachio P.;
RT "Mouse N-ras genes: organization of the functional locus and of a truncated
RT cDNA-like pseudogene.";
RL Oncogene Res. 1:129-136(1987).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
CC activity. {ECO:0000250|UniProtKB:P01111}.
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:0000250|UniProtKB:P01116};
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).
CC -!- SUBUNIT: Interacts (active GTP-bound form preferentially) with RGS14.
CC Interacts (active GTP-bound form) with RASSF7 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P01111};
CC Lipid-anchor {ECO:0000250|UniProtKB:P01111}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P01111}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P01111}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P01111}. Note=Shuttles between the plasma
CC membrane and the Golgi apparatus. {ECO:0000250|UniProtKB:P01111}.
CC -!- PTM: Palmitoylated by the ZDHHC9-GOLGA7 complex. Depalmitoylated by
CC ABHD17A, ABHD17B and ABHD17C. A continuous cycle of de- and re-
CC palmitoylation regulates rapid exchange between plasma membrane and
CC Golgi. {ECO:0000250|UniProtKB:P01111}.
CC -!- PTM: Acetylation at Lys-104 prevents interaction with guanine
CC nucleotide exchange factors (GEFs). {ECO:0000250|UniProtKB:P01116}.
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:0000250|UniProtKB:P01112}.
CC -!- PTM: Phosphorylation at Ser-89 by STK19 enhances NRAS-association with
CC its downstream effectors. {ECO:0000250|UniProtKB:P01111}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; M12124; AAA39839.1; -; Genomic_DNA.
DR EMBL; M12121; AAA39839.1; JOINED; Genomic_DNA.
DR EMBL; M12122; AAA39839.1; JOINED; Genomic_DNA.
DR EMBL; M12123; AAA39839.1; JOINED; Genomic_DNA.
DR EMBL; X13664; CAA31958.1; -; mRNA.
DR EMBL; X06909; CAA30010.1; -; Genomic_DNA.
DR PIR; A23560; TVMSNS.
DR AlphaFoldDB; P08556; -.
DR SMR; P08556; -.
DR IntAct; P08556; 1.
DR STRING; 10090.ENSMUSP00000029445; -.
DR iPTMnet; P08556; -.
DR PhosphoSitePlus; P08556; -.
DR SwissPalm; P08556; -.
DR EPD; P08556; -.
DR jPOST; P08556; -.
DR MaxQB; P08556; -.
DR PaxDb; P08556; -.
DR PeptideAtlas; P08556; -.
DR PRIDE; P08556; -.
DR ProteomicsDB; 254991; -.
DR MGI; MGI:97376; Nras.
DR eggNOG; KOG0395; Eukaryota.
DR InParanoid; P08556; -.
DR Reactome; R-MMU-1169092; Activation of RAS in B cells.
DR Reactome; R-MMU-1250347; SHC1 events in ERBB4 signaling.
DR Reactome; R-MMU-1433557; Signaling by SCF-KIT.
DR Reactome; R-MMU-171007; p38MAPK events.
DR Reactome; R-MMU-179812; GRB2 events in EGFR signaling.
DR Reactome; R-MMU-180336; SHC1 events in EGFR signaling.
DR Reactome; R-MMU-186763; Downstream signal transduction.
DR Reactome; R-MMU-1963640; GRB2 events in ERBB2 signaling.
DR Reactome; R-MMU-210993; Tie2 Signaling.
DR Reactome; R-MMU-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-MMU-2424491; DAP12 signaling.
DR Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
DR Reactome; R-MMU-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-MMU-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-MMU-5654688; SHC-mediated cascade:FGFR1.
DR Reactome; R-MMU-5654693; FRS-mediated FGFR1 signaling.
DR Reactome; R-MMU-5654699; SHC-mediated cascade:FGFR2.
DR Reactome; R-MMU-5654700; FRS-mediated FGFR2 signaling.
DR Reactome; R-MMU-5654704; SHC-mediated cascade:FGFR3.
DR Reactome; R-MMU-5654706; FRS-mediated FGFR3 signaling.
DR Reactome; R-MMU-5654712; FRS-mediated FGFR4 signaling.
DR Reactome; R-MMU-5654719; SHC-mediated cascade:FGFR4.
DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR Reactome; R-MMU-5673000; RAF activation.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-5674135; MAP2K and MAPK activation.
DR Reactome; R-MMU-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-MMU-8851805; MET activates RAS signaling.
DR Reactome; R-MMU-9607240; FLT3 Signaling.
DR Reactome; R-MMU-9634635; Estrogen-stimulated signaling through PRKCZ.
DR Reactome; R-MMU-9648002; RAS processing.
DR ChiTaRS; Nras; mouse.
DR PRO; PR:P08556; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P08556; protein.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0042832; P:defense response to protozoan; IMP:MGI.
DR GO; GO:0048642; P:negative regulation of skeletal muscle tissue development; IDA:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:MGI.
DR GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; TAS:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IMP:MGI.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IMP:MGI.
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 Acetylation; Cell membrane; Golgi apparatus; GTP-binding; Hydrolase;
KW Isopeptide bond; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Palmitate; Phosphoprotein; Prenylation; Proto-oncogene; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..186
FT /note="GTPase NRas"
FT /id="PRO_0000043010"
FT PROPEP 187..189
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000043011"
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:0000250|UniProtKB:P01111"
FT BINDING 29..30
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01111"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 116..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P01111"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01111"
FT LIPID 181
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P01111"
FT LIPID 186
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P01111"
FT CROSSLNK 170
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P01111"
FT CONFLICT 189
FT /note="M -> MCKTL (in Ref. 2; CAA31958)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 189 AA; 21199 MW; 688D33F6814855B7 CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLC VFAINNSKSF ADINLYREQI KRVKDSDDVP MVLVGNKCDL
PTRTVDTKQA HELAKSYGIP FIETSAKTRQ GVEDAFYTLV REIRQYRLKK LNSSDDGTQG
CMGSPCVLM
