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GTPase HRas (H-Ras-1) (Transforming protein p21) (c-H-ras) (p21ras) [Cleaved into: GTPase HRas, N-terminally processed]

 RASH_MOUSE              Reviewed;         189 AA.
Q61411; F7BIB2; Q6P716; Q80WD2; Q811B9;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
05-DEC-2018, entry version 176.
RecName: Full=GTPase HRas;
AltName: Full=H-Ras-1;
AltName: Full=Transforming protein p21;
AltName: Full=c-H-ras;
AltName: Full=p21ras;
Contains:
RecName: Full=GTPase HRas, N-terminally processed;
Flags: Precursor;
Name=Hras; Synonyms=Hras1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=C57BL/6 X C3H; TISSUE=Liver;
PubMed=8922043;
Przybojewska B., Plucienniczak G.;
"Nucleotide sequence of c-H-ras-1 gene from B6C3F1 mice.";
Acta Biochim. Pol. 43:575-578(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=BALB/cJ; TISSUE=Keratinocyte;
Lin L., Fu D.;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Olfactory epithelium;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 59-75, AND MUTAGENESIS OF GLN-61.
PubMed=7526162; DOI=10.1016/0027-5107(94)90067-1;
Moulds B.A., Goodman J.I.;
"Spontaneous mutation at codon 61 of the Ha-ras gene in the nascent
liver of B6C3F1, C3H/He and C57BL/6 mice.";
Mutat. Res. 311:1-7(1994).
[7]
PROTEIN SEQUENCE OF 136-147, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 151-189 (ISOFORM 2), AND ALTERNATIVE
SPLICING.
STRAIN=NIH/3T3;
PubMed=14500341;
Guil S., de La Iglesia N., Fernandez-Larrea J., Cifuentes D.,
Ferrer J.C., Guinovart J.J., Bach-Elias M.;
"Alternative splicing of the human proto-oncogene c-H-ras renders a
new Ras family protein that trafficks to cytoplasm and nucleus.";
Cancer Res. 63:5178-5187(2003).
[9]
INTERACTION WITH HSPD1.
PubMed=1347942; DOI=10.1073/pnas.89.6.2012;
Ikawa S., Weinberg R.A.;
"An interaction between p21ras and heat shock protein hsp60, a
chaperonin.";
Proc. Natl. Acad. Sci. U.S.A. 89:2012-2016(1992).
[10]
INTERACTION WITH RGL3.
PubMed=10869344; DOI=10.1074/jbc.M002241200;
Shao H., Andres D.A.;
"A novel RalGEF-like protein, RGL3, as a candidate effector for rit
and Ras.";
J. Biol. Chem. 275:26914-26924(2000).
[11]
INTERACTION WITH OOG1.
PubMed=16580637; DOI=10.1016/j.bbrc.2006.03.063;
Tsukamoto S., Ihara R., Aizawa A., Kishida S., Kikuchi A., Imai H.,
Minami N.;
"Oog1, an oocyte-specific protein, interacts with Ras and Ras-
signaling proteins during early embryogenesis.";
Biochem. Biophys. Res. Commun. 343:1105-1112(2006).
[12]
INTERACTION WITH PIK3CG.
PubMed=19906996; DOI=10.1073/pnas.0905506106;
Kurig B., Shymanets A., Bohnacker T., Prajwal X., Brock C.,
Ahmadian M.R., Schaefer M., Gohla A., Harteneck C., Wymann M.P.,
Jeanclos E., Nurnberg B.;
"Ras is an indispensable coregulator of the class IB phosphoinositide
3-kinase p87/p110gamma.";
Proc. Natl. Acad. Sci. U.S.A. 106:20312-20317(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Liver, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
activity.
-!- ACTIVITY REGULATION: Alternates between an inactive form bound to
GDP and an active form bound to GTP. Activated by a guanine
nucleotide-exchange factor (GEF) and inactivated by a GTPase-
activating protein (GAP).
-!- SUBUNIT: Forms a signaling complex with RASGRP1 and DGKZ (By
similarity). In its GTP-bound form interacts with PLCE1 (By
similarity). Interacts with TBC1D10C and RASSF5 (By similarity).
Interacts with PDE6D (By similarity). Interacts with IKZF3 (By
similarity). Found in a complex with at least BRAF, HRAS, MAP2K1,
MAPK3 and RGS14 (By similarity). Interacts (active GTP-bound form)
with RGS14 (via RBD 1 domain) (By similarity). Interacts with
RACK1 (By similarity). Interacts with RAPGEF2 (By similarity).
Interacts with RGL3 (PubMed:10869344). Interacts with HSPD1
(PubMed:1347942). Interacts with PIK3CG; the interaction is
required for membrane recruitment and beta-gamma G protein dimer-
dependent activation of the PI3K gamma complex PIK3CG:PIK3R6
(PubMed:19906996). Interacts (in GTP-bound form) with Oog1
(PubMed:16580637). {ECO:0000250|UniProtKB:P01112,
ECO:0000250|UniProtKB:P20171, ECO:0000269|PubMed:10869344,
ECO:0000269|PubMed:1347942, ECO:0000269|PubMed:16580637,
ECO:0000269|PubMed:19906996}.
-!- INTERACTION:
Q5EBH1:Rassf5; NbExp=2; IntAct=EBI-400273, EBI-960530;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Cell membrane
{ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side
{ECO:0000250}. Golgi apparatus {ECO:0000250}. Golgi apparatus
membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Shuttles
between the plasma membrane and the Golgi apparatus. The active
GTP-bound form is localized most strongly to membranes than the
inactive GDP-bound form (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=p21, H-Ras4A;
IsoId=Q61411-1; Sequence=Displayed;
Name=2; Synonyms=p19, H-RasIDX;
IsoId=Q61411-2; Sequence=VSP_041598;
Note=Ref.8 (CAD24593) sequence is in conflict in position:
163:D->G. {ECO:0000305};
-!- PTM: Palmitoylated by the ZDHHC9-GOLGA7 complex. A continuous
cycle of de- and re-palmitoylation regulates rapid exchange
between plasma membrane and Golgi. {ECO:0000250|UniProtKB:P01112}.
-!- PTM: S-nitrosylated; critical for redox regulation. Important for
stimulating guanine nucleotide exchange. No structural
perturbation on nitrosylation. {ECO:0000250|UniProtKB:P01112}.
-!- PTM: The covalent modification of cysteine by 15-deoxy-Delta12,14-
prostaglandin-J2 is autocatalytic and reversible. It may occur as
an alternative to other cysteine modifications, such as S-
nitrosylation and S-palmitoylation.
{ECO:0000250|UniProtKB:P01112}.
-!- PTM: Acetylation at Lys-104 prevents interaction with guanine
nucleotide exchange factors (GEFs). {ECO:0000250}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH61885.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; Z50013; CAA90306.1; -; Genomic_DNA.
EMBL; AY373386; AAQ81319.1; -; mRNA.
EMBL; AC108908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466531; EDL18008.1; -; Genomic_DNA.
EMBL; CH466531; EDL18009.1; -; Genomic_DNA.
EMBL; BC061885; AAH61885.1; ALT_INIT; mRNA.
EMBL; S74119; AAP21090.1; -; Genomic_DNA.
EMBL; AJ437023; CAD24593.1; -; mRNA.
CCDS; CCDS22003.1; -. [Q61411-1]
CCDS; CCDS52439.1; -. [Q61411-2]
PIR; S57718; S57718.
RefSeq; NP_001123915.1; NM_001130443.1. [Q61411-1]
RefSeq; NP_001123916.1; NM_001130444.1. [Q61411-2]
RefSeq; NP_032310.2; NM_008284.2. [Q61411-1]
RefSeq; XP_006536222.2; XM_006536159.2. [Q61411-1]
UniGene; Mm.334313; -.
ProteinModelPortal; Q61411; -.
SMR; Q61411; -.
BioGrid; 200416; 18.
ComplexPortal; CPX-413; GTPase Hras - Son of sevenless homolog 1 complex.
DIP; DIP-29361N; -.
IntAct; Q61411; 11.
MINT; Q61411; -.
STRING; 10090.ENSMUSP00000026572; -.
iPTMnet; Q61411; -.
PhosphoSitePlus; Q61411; -.
SwissPalm; Q61411; -.
EPD; Q61411; -.
PaxDb; Q61411; -.
PeptideAtlas; Q61411; -.
PRIDE; Q61411; -.
Ensembl; ENSMUST00000026572; ENSMUSP00000026572; ENSMUSG00000025499. [Q61411-1]
Ensembl; ENSMUST00000097957; ENSMUSP00000095570; ENSMUSG00000025499. [Q61411-1]
Ensembl; ENSMUST00000124314; ENSMUSP00000147731; ENSMUSG00000025499. [Q61411-2]
Ensembl; ENSMUST00000168550; ENSMUSP00000132110; ENSMUSG00000025499. [Q61411-2]
GeneID; 15461; -.
KEGG; mmu:15461; -.
UCSC; uc009kju.2; mouse. [Q61411-1]
UCSC; uc009kjv.2; mouse. [Q61411-2]
CTD; 3265; -.
MGI; MGI:96224; Hras.
eggNOG; KOG0395; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00940000155653; -.
HOGENOM; HOG000233973; -.
HOVERGEN; HBG009351; -.
InParanoid; Q61411; -.
KO; K02833; -.
OMA; QHIPICL; -.
OrthoDB; EOG091G0UAU; -.
TreeFam; TF312796; -.
Reactome; R-MMU-1169092; Activation of RAS in B cells.
Reactome; R-MMU-1250347; SHC1 events in ERBB4 signaling.
Reactome; R-MMU-1433557; Signaling by SCF-KIT.
Reactome; R-MMU-171007; p38MAPK events.
Reactome; R-MMU-179812; GRB2 events in EGFR signaling.
Reactome; R-MMU-180336; SHC1 events in EGFR signaling.
Reactome; R-MMU-186763; Downstream signal transduction.
Reactome; R-MMU-1963640; GRB2 events in ERBB2 signaling.
Reactome; R-MMU-210993; Tie2 Signaling.
Reactome; R-MMU-2179392; EGFR Transactivation by Gastrin.
Reactome; R-MMU-2424491; DAP12 signaling.
Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
Reactome; R-MMU-375165; NCAM signaling for neurite out-growth.
Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
Reactome; R-MMU-442982; Ras activation upon Ca2+ influx through NMDA receptor.
Reactome; R-MMU-5218921; VEGFR2 mediated cell proliferation.
Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-MMU-5654688; SHC-mediated cascade:FGFR1.
Reactome; R-MMU-5654693; FRS-mediated FGFR1 signaling.
Reactome; R-MMU-5654699; SHC-mediated cascade:FGFR2.
Reactome; R-MMU-5654700; FRS-mediated FGFR2 signaling.
Reactome; R-MMU-5654704; SHC-mediated cascade:FGFR3.
Reactome; R-MMU-5654706; FRS-mediated FGFR3 signaling.
Reactome; R-MMU-5654712; FRS-mediated FGFR4 signaling.
Reactome; R-MMU-5654719; SHC-mediated cascade:FGFR4.
Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
Reactome; R-MMU-5673000; RAF activation.
Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
Reactome; R-MMU-5674135; MAP2K and MAPK activation.
Reactome; R-MMU-5675221; Negative regulation of MAPK pathway.
Reactome; R-MMU-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
Reactome; R-MMU-8851805; MET activates RAS signaling.
PRO; PR:Q61411; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000025499; Expressed in 295 organ(s), highest expression level in striatum.
CleanEx; MM_HRAS1; -.
ExpressionAtlas; Q61411; baseline and differential.
Genevisible; Q61411; MM.
GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0019003; F:GDP binding; ISO:MGI.
GO; GO:0005525; F:GTP binding; IDA:MGI.
GO; GO:0003924; F:GTPase activity; ISO:MGI.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0006915; P:apoptotic process; ISO:MGI.
GO; GO:0007569; P:cell aging; IDA:MGI.
GO; GO:0007050; P:cell cycle arrest; ISO:MGI.
GO; GO:0008283; P:cell proliferation; IPI:MGI.
GO; GO:0071480; P:cellular response to gamma radiation; ISO:MGI.
GO; GO:0090398; P:cellular senescence; ISO:MGI.
GO; GO:0042832; P:defense response to protozoan; IMP:MGI.
GO; GO:0006897; P:endocytosis; IDA:MGI.
GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IMP:MGI.
GO; GO:0007093; P:mitotic cell cycle checkpoint; ISO:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; ISO:MGI.
GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
GO; GO:0034260; P:negative regulation of GTPase activity; ISO:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:MGI.
GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; ISO:MGI.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:MGI.
GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:MGI.
GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
GO; GO:2000630; P:positive regulation of miRNA metabolic process; ISO:MGI.
GO; GO:0010863; P:positive regulation of phospholipase C activity; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISO:MGI.
GO; GO:0046579; P:positive regulation of Ras protein signal transduction; ISO:MGI.
GO; GO:1900029; P:positive regulation of ruffle assembly; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0090303; P:positive regulation of wound healing; ISO:MGI.
GO; GO:0051291; P:protein heterooligomerization; ISO:MGI.
GO; GO:0007265; P:Ras protein signal transduction; IGI:ParkinsonsUK-UCL.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:MGI.
GO; GO:0098696; P:regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; ISO:MGI.
GO; GO:0035900; P:response to isolation stress; IEA:Ensembl.
GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:MGI.
GO; GO:0050852; P:T cell receptor signaling pathway; IMP:MGI.
GO; GO:0042088; P:T-helper 1 type immune response; IMP:MGI.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR020849; Small_GTPase_Ras-type.
PANTHER; PTHR24070; PTHR24070; 1.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51421; RAS; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell membrane; Complete proteome;
Direct protein sequencing; Golgi apparatus; GTP-binding; Lipoprotein;
Membrane; Methylation; Nucleotide-binding; Palmitate; Prenylation;
Proto-oncogene; Reference proteome; S-nitrosylation.
CHAIN 1 186 GTPase HRas.
/FTId=PRO_0000326478.
INIT_MET 1 1 Removed; alternate.
{ECO:0000250|UniProtKB:P01112}.
CHAIN 2 186 GTPase HRas, N-terminally processed.
/FTId=PRO_0000042998.
PROPEP 187 189 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000042999.
NP_BIND 10 17 GTP. {ECO:0000250}.
NP_BIND 57 61 GTP. {ECO:0000250}.
NP_BIND 116 119 GTP. {ECO:0000250}.
REGION 166 185 Hypervariable region.
MOTIF 32 40 Effector region.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P01112}.
MOD_RES 2 2 N-acetylthreonine; in GTPase HRas, N-
terminally processed.
{ECO:0000250|UniProtKB:P01112}.
MOD_RES 118 118 S-nitrosocysteine.
{ECO:0000250|UniProtKB:P01112}.
MOD_RES 186 186 Cysteine methyl ester.
{ECO:0000250|UniProtKB:P01112}.
LIPID 181 181 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P01112}.
LIPID 184 184 S-(15-deoxy-Delta12,14-prostaglandin J2-
9-yl)cysteine; alternate.
{ECO:0000250|UniProtKB:P01112}.
LIPID 184 184 S-palmitoyl cysteine; alternate.
{ECO:0000250|UniProtKB:P01112}.
LIPID 186 186 S-farnesyl cysteine.
{ECO:0000250|UniProtKB:P01112}.
VAR_SEQ 152 189 VEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS ->
SRSGSSSGTLWDPPSPGTHVTQRPSSWRGGCLLYTSP (in
isoform 2).
{ECO:0000303|PubMed:14500341}.
/FTId=VSP_041598.
MUTAGEN 61 61 Q->R: Found in chemically induced liver
tumors. {ECO:0000269|PubMed:7526162}.
CONFLICT 55 55 I -> Y (in Ref. 1; CAA90306).
{ECO:0000305}.
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


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gen16650 RASH_CHICK GTPase HRas ELISA tesk kit 1


 

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