##gff-version 3 ##sequence-region P01112 1 189 P01112 UniProtKB Chain 1 186 . . . ID=PRO_0000042996;Note=GTPase HRas P01112 UniProtKB Initiator methionine 1 1 . . . Note=Removed%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.12 P01112 UniProtKB Chain 2 186 . . . ID=PRO_0000326476;Note=GTPase HRas%2C N-terminally processed P01112 UniProtKB Propeptide 187 189 . . . ID=PRO_0000042997;Note=Removed in mature form P01112 UniProtKB Region 166 185 . . . Note=Hypervariable region P01112 UniProtKB Motif 32 40 . . . Note=Effector region P01112 UniProtKB Binding site 13 18 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16698776;Dbxref=PMID:16698776 P01112 UniProtKB Binding site 29 35 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16698776;Dbxref=PMID:16698776 P01112 UniProtKB Binding site 59 60 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16698776;Dbxref=PMID:16698776 P01112 UniProtKB Binding site 116 119 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16698776;Dbxref=PMID:16698776 P01112 UniProtKB Binding site 145 147 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16698776;Dbxref=PMID:16698776 P01112 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine%3B in GTPase HRas%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.12 P01112 UniProtKB Modified residue 2 2 . . . Note=N-acetylthreonine%3B in GTPase HRas%2C N-terminally processed;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.12 P01112 UniProtKB Modified residue 118 118 . . . Note=S-nitrosocysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9020151;Dbxref=PMID:9020151 P01112 UniProtKB Modified residue 186 186 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8626715;Dbxref=PMID:8626715 P01112 UniProtKB Lipidation 181 181 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15705808,ECO:0000269|PubMed:16000296,ECO:0000269|PubMed:2661017,ECO:0000269|PubMed:8626715;Dbxref=PMID:15705808,PMID:16000296,PMID:2661017,PMID:8626715 P01112 UniProtKB Lipidation 184 184 . . . Note=S-(15-deoxy-Delta12%2C14-prostaglandin J2-9-yl)cysteine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12684535;Dbxref=PMID:12684535 P01112 UniProtKB Lipidation 184 184 . . . Note=S-palmitoyl cysteine%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15705808,ECO:0000269|PubMed:16000296,ECO:0000269|PubMed:2661017,ECO:0000269|PubMed:8626715;Dbxref=PMID:15705808,PMID:16000296,PMID:2661017,PMID:8626715 P01112 UniProtKB Lipidation 186 186 . . . Note=S-farnesyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8626715;Dbxref=PMID:8626715 P01112 UniProtKB Glycosylation 35 35 . . . Note=(Microbial infection) O-linked (Glc) threonine%3B by P.sordellii toxin TcsL;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19744486,ECO:0000269|PubMed:8626575,ECO:0000269|PubMed:8626586,ECO:0000269|PubMed:9632667;Dbxref=PMID:19744486,PMID:8626575,PMID:8626586,PMID:9632667 P01112 UniProtKB Cross-link 170 170 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30442762;Dbxref=PMID:30442762 P01112 UniProtKB Alternative sequence 152 189 . . . ID=VSP_041597;Note=In isoform 2. VEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS->SRSGSSSSSGTLWDPPGPM;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:14500341,ECO:0000303|PubMed:15489334;Dbxref=PMID:14500341,PMID:15489334 P01112 UniProtKB Natural variant 12 12 . . . ID=VAR_026106;Note=In CSTLO. G->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16170316,ECO:0000269|PubMed:16329078,ECO:0000269|PubMed:16443854;Dbxref=dbSNP:rs104894230,PMID:16170316,PMID:16329078,PMID:16443854 P01112 UniProtKB Natural variant 12 12 . . . ID=VAR_045975;Note=In CSTLO. G->C;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16443854,ECO:0000269|PubMed:18039947;Dbxref=dbSNP:rs104894229,PMID:16443854,PMID:18039947 P01112 UniProtKB Natural variant 12 12 . . . ID=VAR_068816;Note=In CSTLO%3B severe mutation. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18039947;Dbxref=dbSNP:rs104894230,PMID:18039947 P01112 UniProtKB Natural variant 12 12 . . . ID=VAR_045976;Note=In CSTLO. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16443854;Dbxref=PMID:16443854 P01112 UniProtKB Natural variant 12 12 . . . ID=VAR_006837;Note=In CSTLO and CMEMS%3B also found in patients with oral squamous cell carcinoma. G->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1459726,ECO:0000269|PubMed:16170316,ECO:0000269|PubMed:16329078,ECO:0000269|PubMed:16443854,ECO:0000269|PubMed:17054105,ECO:0000269|PubMed:17412879;Dbxref=dbSNP:rs104894229,PMID:1459726,PMID:16170316,PMID:16329078,PMID:16443854,PMID:17054105,PMID:17412879 P01112 UniProtKB Natural variant 12 12 . . . ID=VAR_006836;Note=In CSTLO%2C bladder carcinoma and CMEMS%3B constitutively activated%3B interacts and recruits PLCE1 to plasma membrane. G->V;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11022048,ECO:0000269|PubMed:15546861,ECO:0000269|PubMed:16170316,ECO:0000269|PubMed:17412879;Dbxref=dbSNP:rs104894230,PMID:11022048,PMID:15546861,PMID:16170316,PMID:17412879 P01112 UniProtKB Natural variant 13 13 . . . ID=VAR_026107;Note=In CSTLO. G->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16329078;Dbxref=dbSNP:rs104894228,PMID:16329078 P01112 UniProtKB Natural variant 13 13 . . . ID=VAR_026108;Note=In CSTLO. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16170316;Dbxref=dbSNP:rs104894226,PMID:16170316 P01112 UniProtKB Natural variant 13 13 . . . ID=VAR_068817;Note=In SFM%3B somatic mutation%3B shows constitutive activation of the MAPK and PI3K-AKT signaling pathways. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22683711;Dbxref=dbSNP:rs104894228,PMID:22683711 P01112 UniProtKB Natural variant 22 22 . . . ID=VAR_045977;Note=In CMEMS. Q->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17412879;Dbxref=dbSNP:rs121917757,PMID:17412879 P01112 UniProtKB Natural variant 37 37 . . . ID=VAR_068818;Note=In CSTLO. E->EE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19995790;Dbxref=PMID:19995790 P01112 UniProtKB Natural variant 58 58 . . . ID=VAR_045978;Note=In CSTLO. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18247425;Dbxref=dbSNP:rs121917758,PMID:18247425 P01112 UniProtKB Natural variant 61 61 . . . ID=VAR_045979;Note=In NMTC2%3B somatic mutation%3B increases transformation of cultured cell lines. Q->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12727991,ECO:0000269|PubMed:18073111;Dbxref=dbSNP:rs28933406,PMID:12727991,PMID:18073111 P01112 UniProtKB Natural variant 61 61 . . . ID=VAR_006838;Note=In melanoma%3B strongly reduced GTP hydrolysis in the presence of RAF1%3B increases transformation of cultured cell lines. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18073111;Dbxref=dbSNP:rs121913233,PMID:18073111 P01112 UniProtKB Natural variant 63 63 . . . ID=VAR_045980;Note=In CMEMS. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17412879;Dbxref=dbSNP:rs121917756,PMID:17412879 P01112 UniProtKB Natural variant 89 89 . . . ID=VAR_078259;Note=Found in a patient with severe fetal hydrops and pleural effusion%3B unknown pathological significance%3B decreased activation of Ras protein signal transduction. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22821884;Dbxref=dbSNP:rs755322824,PMID:22821884 P01112 UniProtKB Natural variant 117 117 . . . ID=VAR_045981;Note=In CSTLO. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16443854;Dbxref=dbSNP:rs104894227,PMID:16443854 P01112 UniProtKB Natural variant 146 146 . . . ID=VAR_045982;Note=In CSTLO. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17054105;Dbxref=dbSNP:rs104894231,PMID:17054105 P01112 UniProtKB Natural variant 146 146 . . . ID=VAR_045983;Note=In CSTLO. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18247425;Dbxref=dbSNP:rs121917759,PMID:18247425 P01112 UniProtKB Mutagenesis 17 17 . . . Note=Dominant negative. Prevents PLCE1 EGF-induced recruitment to plasma membrane. No effect on subcellular location of isoform 2. S->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11022048,ECO:0000269|PubMed:14500341;Dbxref=PMID:11022048,PMID:14500341 P01112 UniProtKB Mutagenesis 26 26 . . . Note=Loss of interaction with PLCE1%3B when associated with V-12. N->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11022048;Dbxref=PMID:11022048 P01112 UniProtKB Mutagenesis 29 29 . . . Note=No effect on interaction with PLCE1%3B when associated with V-12. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11022048;Dbxref=PMID:11022048 P01112 UniProtKB Mutagenesis 32 32 . . . Note=Loss of interaction and recruitment to plasma membrane of PLCE1%3B when associated with V-12. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11022048;Dbxref=PMID:11022048 P01112 UniProtKB Mutagenesis 34 34 . . . Note=No effect on interaction with PLCE1%3B when associated with V-12. P->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11022048;Dbxref=PMID:11022048 P01112 UniProtKB Mutagenesis 35 35 . . . Note=Loss of interaction with PLCE1%3B when associated with V-12. T->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11022048;Dbxref=PMID:11022048 P01112 UniProtKB Mutagenesis 37 37 . . . Note=No effect on interaction with PLCE1%3B when associated with V-12. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11022048;Dbxref=PMID:11022048 P01112 UniProtKB Mutagenesis 38 38 . . . Note=No effect on interaction with PLCE1%3B when associated with V-12. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11022048;Dbxref=PMID:11022048 P01112 UniProtKB Mutagenesis 39 39 . . . Note=No effect on interaction with PLCE1%3B when associated with V-12. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11022048;Dbxref=PMID:11022048 P01112 UniProtKB Mutagenesis 59 59 . . . Note=Loss of GTPase activity and creation of an autophosphorylation site. A->T P01112 UniProtKB Mutagenesis 61 61 . . . Note=Moderately increased transformation of cultured cell lines. Q->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18073111;Dbxref=PMID:18073111 P01112 UniProtKB Mutagenesis 61 61 . . . Note=Strongly increased transformation of cultured cell lines. Q->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18073111;Dbxref=PMID:18073111 P01112 UniProtKB Mutagenesis 83 83 . . . Note=GTP-binding activity reduced by factor of 30. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3088563;Dbxref=PMID:3088563 P01112 UniProtKB Mutagenesis 118 118 . . . Note=Abolishes S-nitrosylation. No stimulation of guanine nucleotide exchange. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12740440,ECO:0000269|PubMed:9020151;Dbxref=PMID:12740440,PMID:9020151 P01112 UniProtKB Mutagenesis 119 119 . . . Note=Loss of GTP-binding activity. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3088563;Dbxref=PMID:3088563 P01112 UniProtKB Mutagenesis 144 144 . . . Note=GTP-binding activity reduced by factor of 25. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3088563;Dbxref=PMID:3088563 P01112 UniProtKB Mutagenesis 164 165 . . . Note=Loss of GTP-binding activity. RQ->AV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3011420;Dbxref=PMID:3011420 P01112 UniProtKB Mutagenesis 167 185 . . . Note=In H-Ras-3KR mutant%3B decreased fatty-acylation. KLRKLNPPDESGPGCMSCK->RLRRLNPPDESGPGCMSCR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29239724;Dbxref=PMID:29239724 P01112 UniProtKB Mutagenesis 170 170 . . . Note=Increased Ras signaling due to impaired ubiquitination. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30442762;Dbxref=PMID:30442762 P01112 UniProtKB Mutagenesis 181 181 . . . Note=Exclusively localized in Golgi. Non-specifically localized on all endomembranes%3B when associated with S-184. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15705808,ECO:0000269|PubMed:8626715;Dbxref=PMID:15705808,PMID:8626715 P01112 UniProtKB Mutagenesis 184 184 . . . Note=Loss of S-(15-deoxy-Delta12%2C14-prostaglandin J2-9-yl)cysteine stimulation of Ras-GTPase activity. Mainly localized in Golgi. Non-specifically localized on all endomembranes%3B when associated with S-181. C->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12684535,ECO:0000269|PubMed:15705808,ECO:0000269|PubMed:8626715;Dbxref=PMID:12684535,PMID:15705808,PMID:8626715 P01112 UniProtKB Beta strand 3 11 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CE2 P01112 UniProtKB Beta strand 12 15 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6V9M P01112 UniProtKB Helix 16 25 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CE2 P01112 UniProtKB Beta strand 27 31 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1XCM P01112 UniProtKB Beta strand 34 37 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1XD2 P01112 UniProtKB Beta strand 38 46 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CE2 P01112 UniProtKB Beta strand 49 57 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CE2 P01112 UniProtKB Beta strand 60 63 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CLD P01112 UniProtKB Helix 66 74 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CE2 P01112 UniProtKB Beta strand 76 83 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CE2 P01112 UniProtKB Turn 84 86 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CRP P01112 UniProtKB Helix 87 104 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CE2 P01112 UniProtKB Beta strand 105 107 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6Q21 P01112 UniProtKB Beta strand 111 116 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CE2 P01112 UniProtKB Beta strand 120 122 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CLD P01112 UniProtKB Helix 127 136 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CE2 P01112 UniProtKB Beta strand 141 144 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CE2 P01112 UniProtKB Turn 146 148 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CE2 P01112 UniProtKB Helix 152 164 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CE2