RASH_MESAU
ID RASH_MESAU Reviewed; 96 AA.
AC Q60529;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 111.
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: Fragment;
GN Name=HRAS; Synonyms=HRAS1;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Kidney;
RA Chakravarti D., Cavalieri E.L., Rogan E.G.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
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. In its GTP-
CC bound form interacts with PLCE1. Interacts with TBC1D10C. Interacts
CC with RGL3 and RASSF5. Interacts with HSPD1. Interacts with PDE6D.
CC Interacts with IKZF3. Found in a complex with at least BRAF, HRAS,
CC MAP2K1, MAPK3 and RGS14. Interacts (active GTP-bound form) with RGS14
CC (via RBD 1 domain). Interacts with RACK1. Interacts with PIK3CG; the
CC interaction is required for membrane recruitment and beta-gamma G
CC protein dimer-dependent activation of the PI3K gamma complex
CC PIK3CG:PIK3R6. Interacts with RAPGEF2. Interacts (in GTP-bound form)
CC with Oog1. {ECO:0000250|UniProtKB:P20171,
CC ECO:0000250|UniProtKB:Q61411}.
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 -!- 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}.
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DR EMBL; U38462; AAB60504.1; -; Genomic_DNA.
DR AlphaFoldDB; Q60529; -.
DR SMR; Q60529; -.
DR STRING; 10036.XP_005064275.1; -.
DR eggNOG; KOG0395; Eukaryota.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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 3: Inferred from homology;
KW Acetylation; Cell membrane; Golgi apparatus; GTP-binding; Hydrolase;
KW Lipoprotein; Membrane; Nucleotide-binding; Palmitate; Proto-oncogene;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..96
FT /note="GTPase HRas"
FT /id="PRO_0000326477"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01112"
FT CHAIN 2..96
FT /note="GTPase HRas, N-terminally processed"
FT /id="PRO_0000082640"
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 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 NON_TER 96
SQ SEQUENCE 96 AA; 10848 MW; BAF79C4CD28ECF75 CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHQY
