RASH_MOUSE
ID RASH_MOUSE Reviewed; 189 AA.
AC Q61411; F7BIB2; Q6P716; Q80WD2; Q811B9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=GTPase HRas;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01112};
DE AltName: Full=H-Ras-1;
DE AltName: Full=Transforming protein p21;
DE AltName: Full=c-H-ras;
DE AltName: Full=p21ras;
DE Contains:
DE RecName: Full=GTPase HRas, N-terminally processed;
DE Flags: Precursor;
GN Name=Hras; Synonyms=Hras1;
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].
RC STRAIN=C57BL/6 X C3H; TISSUE=Liver;
RX PubMed=8922043;
RA Przybojewska B., Plucienniczak G.;
RT "Nucleotide sequence of c-H-ras-1 gene from B6C3F1 mice.";
RL Acta Biochim. Pol. 43:575-578(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Keratinocyte;
RA Lin L., Fu D.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Olfactory epithelium;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 59-75, AND MUTAGENESIS OF GLN-61.
RX PubMed=7526162; DOI=10.1016/0027-5107(94)90067-1;
RA Moulds B.A., Goodman J.I.;
RT "Spontaneous mutation at codon 61 of the Ha-ras gene in the nascent liver
RT of B6C3F1, C3H/He and C57BL/6 mice.";
RL Mutat. Res. 311:1-7(1994).
RN [7]
RP PROTEIN SEQUENCE OF 136-147, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 151-189 (ISOFORM 2), AND ALTERNATIVE
RP SPLICING.
RC STRAIN=NIH/3T3;
RX PubMed=14500341;
RA Guil S., de La Iglesia N., Fernandez-Larrea J., Cifuentes D., Ferrer J.C.,
RA Guinovart J.J., Bach-Elias M.;
RT "Alternative splicing of the human proto-oncogene c-H-ras renders a new Ras
RT family protein that trafficks to cytoplasm and nucleus.";
RL Cancer Res. 63:5178-5187(2003).
RN [9]
RP INTERACTION WITH HSPD1.
RX PubMed=1347942; DOI=10.1073/pnas.89.6.2012;
RA Ikawa S., Weinberg R.A.;
RT "An interaction between p21ras and heat shock protein hsp60, a
RT chaperonin.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2012-2016(1992).
RN [10]
RP INTERACTION WITH RGL3.
RX PubMed=10869344; DOI=10.1074/jbc.m002241200;
RA Shao H., Andres D.A.;
RT "A novel RalGEF-like protein, RGL3, as a candidate effector for rit and
RT Ras.";
RL J. Biol. Chem. 275:26914-26924(2000).
RN [11]
RP INTERACTION WITH OOG1.
RX PubMed=16580637; DOI=10.1016/j.bbrc.2006.03.063;
RA Tsukamoto S., Ihara R., Aizawa A., Kishida S., Kikuchi A., Imai H.,
RA Minami N.;
RT "Oog1, an oocyte-specific protein, interacts with Ras and Ras-signaling
RT proteins during early embryogenesis.";
RL Biochem. Biophys. Res. Commun. 343:1105-1112(2006).
RN [12]
RP INTERACTION WITH PIK3CG.
RX PubMed=19906996; DOI=10.1073/pnas.0905506106;
RA Kurig B., Shymanets A., Bohnacker T., Prajwal X., Brock C., Ahmadian M.R.,
RA Schaefer M., Gohla A., Harteneck C., Wymann M.P., Jeanclos E., Nurnberg B.;
RT "Ras is an indispensable coregulator of the class IB phosphoinositide 3-
RT kinase p87/p110gamma.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:20312-20317(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Liver, 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.
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:P01112};
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: Forms a signaling complex with RASGRP1 and DGKZ (By
CC similarity). In its GTP-bound form interacts with PLCE1 (By
CC similarity). Interacts with TBC1D10C and RASSF5 (By similarity).
CC Interacts with PDE6D (By similarity). Interacts with IKZF3 (By
CC similarity). Found in a complex with at least BRAF, HRAS, MAP2K1, MAPK3
CC and RGS14 (By similarity). Interacts (active GTP-bound form) with RGS14
CC (via RBD 1 domain) (By similarity). Interacts with RACK1 (By
CC similarity). Interacts with RAPGEF2 (By similarity). Interacts with
CC RGL3 (PubMed:10869344). Interacts with HSPD1 (PubMed:1347942).
CC Interacts with PIK3CG; the interaction is required for membrane
CC recruitment and beta-gamma G protein dimer-dependent activation of the
CC PI3K gamma complex PIK3CG:PIK3R6 (PubMed:19906996). Interacts (in GTP-
CC bound form) with Oog1 (PubMed:16580637). {ECO:0000250|UniProtKB:P01112,
CC ECO:0000250|UniProtKB:P20171, ECO:0000269|PubMed:10869344,
CC ECO:0000269|PubMed:1347942, ECO:0000269|PubMed:16580637,
CC ECO:0000269|PubMed:19906996}.
CC -!- INTERACTION:
CC Q61411; Q5EBH1: Rassf5; NbExp=2; IntAct=EBI-400273, EBI-960530;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Golgi apparatus {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Shuttles between the
CC plasma membrane and the Golgi apparatus. The active GTP-bound form is
CC localized most strongly to membranes than the inactive GDP-bound form
CC (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=p21, H-Ras4A;
CC IsoId=Q61411-1; Sequence=Displayed;
CC Name=2; Synonyms=p19, H-RasIDX;
CC IsoId=Q61411-2; Sequence=VSP_041598;
CC -!- PTM: Palmitoylated by the ZDHHC9-GOLGA7 complex. A continuous cycle of
CC de- and re-palmitoylation regulates rapid exchange between plasma
CC membrane and Golgi. {ECO:0000250|UniProtKB:P01112}.
CC -!- PTM: S-nitrosylated; critical for redox regulation. Important for
CC stimulating guanine nucleotide exchange. No structural perturbation on
CC nitrosylation. {ECO:0000250|UniProtKB:P01112}.
CC -!- PTM: The covalent modification of cysteine by 15-deoxy-Delta12,14-
CC prostaglandin-J2 is autocatalytic and reversible. It may occur as an
CC alternative to other cysteine modifications, such as S-nitrosylation
CC and S-palmitoylation. {ECO:0000250|UniProtKB:P01112}.
CC -!- PTM: Acetylation at Lys-104 prevents interaction with guanine
CC nucleotide exchange factors (GEFs). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH61885.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z50013; CAA90306.1; -; Genomic_DNA.
DR EMBL; AY373386; AAQ81319.1; -; mRNA.
DR EMBL; AC108908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466531; EDL18008.1; -; Genomic_DNA.
DR EMBL; CH466531; EDL18009.1; -; Genomic_DNA.
DR EMBL; BC061885; AAH61885.1; ALT_INIT; mRNA.
DR EMBL; S74119; AAP21090.1; -; Genomic_DNA.
DR EMBL; AJ437023; CAD24593.1; -; mRNA.
DR CCDS; CCDS22003.1; -. [Q61411-1]
DR CCDS; CCDS52439.1; -. [Q61411-2]
DR PIR; S57718; S57718.
DR RefSeq; NP_001123915.1; NM_001130443.1. [Q61411-1]
DR RefSeq; NP_001123916.1; NM_001130444.1. [Q61411-2]
DR RefSeq; NP_032310.2; NM_008284.2. [Q61411-1]
DR RefSeq; XP_006536222.2; XM_006536159.2. [Q61411-1]
DR PDB; 6KYH; X-ray; 3.30 A; E/F/G/H=1-167.
DR PDBsum; 6KYH; -.
DR AlphaFoldDB; Q61411; -.
DR SMR; Q61411; -.
DR BioGRID; 200416; 18.
DR ComplexPortal; CPX-413; GTPase Hras - Son of sevenless homolog 1 complex.
DR DIP; DIP-29361N; -.
DR IntAct; Q61411; 8.
DR MINT; Q61411; -.
DR STRING; 10090.ENSMUSP00000026572; -.
DR iPTMnet; Q61411; -.
DR PhosphoSitePlus; Q61411; -.
DR SwissPalm; Q61411; -.
DR EPD; Q61411; -.
DR jPOST; Q61411; -.
DR MaxQB; Q61411; -.
DR PaxDb; Q61411; -.
DR PeptideAtlas; Q61411; -.
DR PRIDE; Q61411; -.
DR ProteomicsDB; 255107; -. [Q61411-1]
DR ProteomicsDB; 255108; -. [Q61411-2]
DR ABCD; Q61411; 1 sequenced antibody.
DR Antibodypedia; 22506; 816 antibodies from 38 providers.
DR DNASU; 15461; -.
DR Ensembl; ENSMUST00000026572; ENSMUSP00000026572; ENSMUSG00000025499. [Q61411-1]
DR Ensembl; ENSMUST00000097957; ENSMUSP00000095570; ENSMUSG00000025499. [Q61411-1]
DR Ensembl; ENSMUST00000124314; ENSMUSP00000147731; ENSMUSG00000025499. [Q61411-2]
DR Ensembl; ENSMUST00000168550; ENSMUSP00000132110; ENSMUSG00000025499. [Q61411-2]
DR GeneID; 15461; -.
DR KEGG; mmu:15461; -.
DR UCSC; uc009kju.2; mouse. [Q61411-1]
DR UCSC; uc009kjv.2; mouse. [Q61411-2]
DR CTD; 3265; -.
DR MGI; MGI:96224; Hras.
DR VEuPathDB; HostDB:ENSMUSG00000025499; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000155653; -.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; Q61411; -.
DR OMA; HYREQIR; -.
DR OrthoDB; 1259506at2759; -.
DR PhylomeDB; Q61411; -.
DR TreeFam; TF312796; -.
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-3928662; EPHB-mediated forward signaling.
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-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 BioGRID-ORCS; 15461; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Hras; mouse.
DR PRO; PR:Q61411; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q61411; protein.
DR Bgee; ENSMUSG00000025499; Expressed in dentate gyrus of hippocampal formation granule cell and 271 other tissues.
DR ExpressionAtlas; Q61411; baseline and differential.
DR Genevisible; Q61411; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1905360; C:GTPase complex; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; IDA:MGI.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0060612; P:adipose tissue development; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0071480; P:cellular response to gamma radiation; ISO:MGI.
DR GO; GO:0090398; P:cellular senescence; IDA:MGI.
DR GO; GO:0042832; P:defense response to protozoan; IMP:MGI.
DR GO; GO:0006897; P:endocytosis; IDA:MGI.
DR GO; GO:0048144; P:fibroblast proliferation; IDA:MGI.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IDA:MGI.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IPI:MGI.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR GO; GO:2000630; P:positive regulation of miRNA metabolic process; ISO:MGI.
DR GO; GO:0010863; P:positive regulation of phospholipase C activity; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISO:MGI.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; ISO:MGI.
DR GO; GO:1900029; P:positive regulation of ruffle assembly; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0090303; P:positive regulation of wound healing; ISO:MGI.
DR GO; GO:0007265; P:Ras protein signal transduction; IGI:ParkinsonsUK-UCL.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:MGI.
DR GO; GO:0043405; P:regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0098696; P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:MGI.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IMP:MGI.
DR GO; GO:0042088; P:T-helper 1 type immune response; 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 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Golgi apparatus; GTP-binding; Hydrolase;
KW Isopeptide bond; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Palmitate; Prenylation; Proto-oncogene; Reference proteome;
KW S-nitrosylation; Ubl conjugation.
FT CHAIN 1..186
FT /note="GTPase HRas"
FT /id="PRO_0000326478"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT CHAIN 2..186
FT /note="GTPase HRas, N-terminally processed"
FT /id="PRO_0000042998"
FT PROPEP 187..189
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000042999"
FT REGION 166..185
FT /note="Hypervariable region"
FT MOTIF 32..40
FT /note="Effector region"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 116..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT MOD_RES 2
FT /note="N-acetylthreonine; in GTPase HRas, N-terminally
FT processed"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT MOD_RES 118
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT MOD_RES 186
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT LIPID 181
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT LIPID 184
FT /note="S-(15-deoxy-Delta12,14-prostaglandin J2-9-
FT yl)cysteine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT LIPID 184
FT /note="S-palmitoyl cysteine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT LIPID 186
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT CROSSLNK 170
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT VAR_SEQ 152..189
FT /note="VEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS -> SRSGSSSGTL
FT WDPPSPGTHVTQRPSSWRGGCLLYTSP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14500341"
FT /id="VSP_041598"
FT MUTAGEN 61
FT /note="Q->R: Found in chemically induced liver tumors."
FT /evidence="ECO:0000269|PubMed:7526162"
FT CONFLICT 55
FT /note="I -> Y (in Ref. 1; CAA90306)"
FT /evidence="ECO:0000305"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:6KYH"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:6KYH"
FT STRAND 36..46
FT /evidence="ECO:0007829|PDB:6KYH"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:6KYH"
FT HELIX 62..67
FT /evidence="ECO:0007829|PDB:6KYH"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:6KYH"
FT STRAND 76..85
FT /evidence="ECO:0007829|PDB:6KYH"
FT HELIX 87..104
FT /evidence="ECO:0007829|PDB:6KYH"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:6KYH"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:6KYH"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:6KYH"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:6KYH"
FT HELIX 152..166
FT /evidence="ECO:0007829|PDB:6KYH"
FT CONFLICT Q61411-2:163
FT /note="D -> G (in Ref. 8; CAD24593)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 189 AA; 21298 MW; EE6DC2D933E2856A CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHQYREQI KRVKDSDDVP MVLVGNKCDL
AARTVESRQA QDLARSYGIP YIETSAKTRQ GVEDAFYTLV REIRQHKLRK LNPPDESGPG
CMSCKCVLS
