HRAS
entrez
3265
canonical
uniprot
P01112
canonical
ensembl
ENSG00000174775
resolver
ensembl
ENSG00000276536
resolver
ensp
ENSP00000309845
resolver
ensp
ENSP00000388246
resolver
ensp
ENSP00000407586
resolver
genesymbol
HRAS
resolver
genesymbol_syn
HRAS1
resolver
hgnc
HGNC:5173
resolver
uniprot
B5BUA0
resolver
uniprot
Q14080
resolver
uniprot
Q6FHV9
resolver
uniprot
Q9BR65
resolver
uniprot
Q9UCE2
resolver
uniprot
X5D945
resolver
uniprot_entry
RASH_HUMAN
resolver
uniprot_entry
X5D945_HUMAN
resolver
uniprot_sec
B5BUA0
resolver
uniprot_sec
Q14080
resolver
uniprot_sec
Q6FHV9
resolver
uniprot_sec
Q9BR65
resolver
uniprot_sec
Q9UCE2
resolver
activity_regulation
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).
uniprot
proteins
amino_acid_sequence
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS
uniprot
proteins
disease_involvement
DISEASE: Costello syndrome (CSTLO) [MIM:218040]: A rare condition characterized by prenatally increased growth, postnatal growth deficiency, intellectual disability, distinctive facial appearance, cardiovascular abnormalities (typically pulmonic stenosis, hypertrophic cardiomyopathy and/or atrial tachycardia), tumor predisposition, skin and musculoskeletal abnormalities. {ECO:0000269|PubMed:16170316, ECO:0000269|PubMed:16329078, ECO:0000269|PubMed:16443854, ECO:0000269|PubMed:17054105, ECO:0000269|PubMed:18039947, ECO:0000269|PubMed:18247425, ECO:0000269|PubMed:19995790}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Congenital myopathy with excess of muscle spindles (CMEMS) [MIM:218040]: Variant of Costello syndrome. {ECO:0000269|PubMed:17412879}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Thyroid cancer, non-medullary, 2 (NMTC2) [MIM:188470]: A form of non-medullary thyroid cancer (NMTC), a cancer characterized by tumors originating from the thyroid follicular cells. NMTCs represent approximately 95% of all cases of thyroid cancer and are classified into papillary, follicular, Hurthle cell, and anaplastic neoplasms. {ECO:0000269|PubMed:12727991}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Note=Mutations which change positions 12, 13 or 61 activate the potential of HRAS to transform cultured cells and are implicated in a variety of human tumors. {ECO:0000269|PubMed:3670300}.; DISEASE: Bladder cancer (BLC) [MIM:109800]: A malignancy originating in tissues of the urinary bladder. It often presents with multiple tumors appearing at different times and at different sites in the bladder. Most bladder cancers are transitional cell carcinomas that begin in cells that normally make up the inner lining of the bladder. Other types of bladder cancer include squamous cell carcinoma (cancer that begins in thin, flat cells) and adenocarcinoma (cancer that begins in cells that make and release mucus and other fluids). Bladder cancer is a complex disorder with both genetic and environmental influences. {ECO:0000269|PubMed:6298635, ECO:0000269|PubMed:6844927}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Schimmelpenning-Feuerstein-Mims syndrome (SFM) [MIM:163200]: A disease characterized by sebaceous nevi, often on the face, associated with variable ipsilateral abnormalities of the central nervous system, ocular anomalies, and skeletal defects. Many oral manifestations have been reported, not only including hypoplastic and malformed teeth, and mucosal papillomatosis, but also ankyloglossia, hemihyperplastic tongue, intraoral nevus, giant cell granuloma, ameloblastoma, bone cysts, follicular cysts, oligodontia, and odontodysplasia. Sebaceous nevi follow the lines of Blaschko and these can continue as linear intraoral lesions, as in mucosal papillomatosis. {ECO:0000269|PubMed:22683711}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.6.5.2
uniprot
proteins
function
FUNCTION: Signal transducer in the Ras-MAPK signaling pathway that regulates cell proliferation and survival (PubMed:22821884). Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (PubMed:12740440, PubMed:14500341, PubMed:9020151). Recognized by LZTR1 that mediates its ubiquitination by a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex (PubMed:40934300). {ECO:0000269|PubMed:12740440, ECO:0000269|PubMed:14500341, ECO:0000269|PubMed:22821884, ECO:0000269|PubMed:40934300, ECO:0000269|PubMed:9020151}.
uniprot
proteins
mass_dalton
21298
uniprot
proteins
mutagenesis
MUTAGEN 17; /note="S->N: Dominant negative. Prevents PLCE1 EGF-induced recruitment to plasma membrane. No effect on subcellular location of isoform 2."; /evidence="ECO:0000269|PubMed:11022048, ECO:0000269|PubMed:14500341"; MUTAGEN 26; /note="N->G: Loss of interaction with PLCE1; when associated with V-12."; /evidence="ECO:0000269|PubMed:11022048"; MUTAGEN 29; /note="V->A: No effect on interaction with PLCE1; when associated with V-12."; /evidence="ECO:0000269|PubMed:11022048"; MUTAGEN 32; /note="Y->F: Loss of interaction and recruitment to plasma membrane of PLCE1; when associated with V-12."; /evidence="ECO:0000269|PubMed:11022048"; MUTAGEN 34; /note="P->G: No effect on interaction with PLCE1; when associated with V-12."; /evidence="ECO:0000269|PubMed:11022048"; MUTAGEN 35; /note="T->S: Loss of interaction with PLCE1; when associated with V-12."; /evidence="ECO:0000269|PubMed:11022048"; MUTAGEN 37; /note="E->G: No effect on interaction with PLCE1; when associated with V-12."; /evidence="ECO:0000269|PubMed:11022048"; MUTAGEN 38; /note="D->N: No effect on interaction with PLCE1; when associated with V-12."; /evidence="ECO:0000269|PubMed:11022048"; MUTAGEN 39; /note="S->C: No effect on interaction with PLCE1; when associated with V-12."; /evidence="ECO:0000269|PubMed:11022048"; MUTAGEN 59; /note="A->T: Loss of GTPase activity and creation of an autophosphorylation site."; MUTAGEN 61; /note="Q->I: Moderately increased transformation of cultured cell lines."; /evidence="ECO:0000269|PubMed:18073111"; MUTAGEN 61; /note="Q->R: Promotes interaction with SHOC2 and PP1C."; /evidence="ECO:0000269|PubMed:35831509"; MUTAGEN 61; /note="Q->V: Strongly increased transformation of cultured cell lines."; /evidence="ECO:0000269|PubMed:18073111"; MUTAGEN 83; /note="A->T: GTP-binding activity reduced by factor of 30."; /evidence="ECO:0000269|PubMed:3088563"; MUTAGEN 118; /note="C->S: Abolishes S-nitrosylation. No stimulation of guanine nucleotide exchange."; /evidence="ECO:0000269|PubMed:12740440, ECO:0000269|PubMed:9020151"; MUTAGEN 119; /note="D->N: Loss of GTP-binding activity."; /evidence="ECO:0000269|PubMed:3088563"; MUTAGEN 144; /note="T->I: GTP-binding activity reduced by factor of 25."; /evidence="ECO:0000269|PubMed:3088563"; MUTAGEN 164..165; /note="RQ->AV: Loss of GTP-binding activity."; /evidence="ECO:0000269|PubMed:3011420"; MUTAGEN 167..185; /note="KLRKLNPPDESGPGCMSCK->RLRRLNPPDESGPGCMSCR: In H-Ras-3KR mutant; decreased fatty-acylation."; /evidence="ECO:0000269|PubMed:29239724"; MUTAGEN 170; /note="K->R: Increased Ras signaling due to impaired ubiquitination."; /evidence="ECO:0000269|PubMed:30442762"; MUTAGEN 181; /note="C->S: Exclusively localized in Golgi. Non-specifically localized on all endomembranes; when associated with S-184."; /evidence="ECO:0000269|PubMed:15705808, ECO:0000269|PubMed:8626715"; MUTAGEN 184; /note="C->S: Loss of S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine stimulation of Ras-GTPase activity. Mainly localized in Golgi. Non-specifically localized on all endomembranes; when associated with S-181."; /evidence="ECO:0000269|PubMed:12684535, ECO:0000269|PubMed:15705808, ECO:0000269|PubMed:8626715
uniprot
proteins
post_translational_modification
PTM: Palmitoylated by the ZDHHC9-GOLGA7 complex. A continuous cycle of de- and re-palmitoylation regulates rapid exchange between plasma membrane and Golgi.; PTM: S-nitrosylated; critical for redox regulation. Important for stimulating guanine nucleotide exchange. No structural perturbation on nitrosylation.; 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.; PTM: Acetylation at Lys-104 prevents interaction with guanine nucleotide exchange factors (GEFs). {ECO:0000250}.; PTM: Fatty-acylated at Lys-170. {ECO:0000269|PubMed:29239724}.; PTM: Ubiquitinated by the BCR(LZTR1) E3 ubiquitin ligase complex at Lys-170 in a non-degradative manner, leading to inhibit Ras signaling by decreasing Ras association with membranes. {ECO:0000269|PubMed:30442762}.; PTM: (Microbial infection) Glucosylated at Thr-35 by P.sordellii toxin TcsL (PubMed:19744486, PubMed:8626575, PubMed:8626586, PubMed:9632667). Monoglucosylation completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form, leading to inhibit Ras signaling (PubMed:8626575, PubMed:8626586, PubMed:9632667). {ECO:0000269|PubMed:19744486, ECO:0000269|PubMed:8626575, ECO:0000269|PubMed:8626586, ECO:0000269|PubMed:9632667}.
uniprot
proteins
protein_family
Ras family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
10369681
uniprot
proteins
pubmed
10574788
uniprot
proteins
pubmed
10608844
uniprot
proteins
pubmed
11022048
uniprot
proteins
pubmed
11257115
uniprot
proteins
pubmed
11598133
uniprot
proteins
pubmed
11980706
uniprot
proteins
pubmed
12213964
uniprot
proteins
pubmed
12684535
uniprot
proteins
pubmed
12727991
uniprot
proteins
pubmed
12740440
uniprot
proteins
pubmed
14500341
uniprot
proteins
pubmed
1459726
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15546861
uniprot
proteins
pubmed
15705808
uniprot
proteins
pubmed
16000296
uniprot
proteins
pubmed
16170316
uniprot
proteins
pubmed
16329078
uniprot
proteins
pubmed
16443854
uniprot
proteins
pubmed
16698776
uniprot
proteins
pubmed
17054105
uniprot
proteins
pubmed
17230191
uniprot
proteins
pubmed
17412879
uniprot
proteins
pubmed
18039947
uniprot
proteins
pubmed
18073111
uniprot
proteins
pubmed
18247425
uniprot
proteins
pubmed
18596699
uniprot
proteins
pubmed
1899707
uniprot
proteins
pubmed
19054851
uniprot
proteins
pubmed
19744486
uniprot
proteins
pubmed
19995790
uniprot
proteins
pubmed
2196171
uniprot
proteins
pubmed
22683711
uniprot
proteins
pubmed
22821884
uniprot
proteins
pubmed
2448879
uniprot
proteins
pubmed
2476675
uniprot
proteins
pubmed
2661017
uniprot
proteins
pubmed
29239724
uniprot
proteins
pubmed
3011420
uniprot
proteins
pubmed
30442762
uniprot
proteins
pubmed
3088563
uniprot
proteins
pubmed
35522713
uniprot
proteins
pubmed
35768504
uniprot
proteins
pubmed
35831509
uniprot
proteins
pubmed
36175670
uniprot
proteins
pubmed
3670300
uniprot
proteins
pubmed
40934300
uniprot
proteins
pubmed
6087347
uniprot
proteins
pubmed
6290897
uniprot
proteins
pubmed
6298635
uniprot
proteins
pubmed
6844927
uniprot
proteins
pubmed
8142349
uniprot
proteins
pubmed
8393791
uniprot
proteins
pubmed
8626575
uniprot
proteins
pubmed
8626586
uniprot
proteins
pubmed
8626715
uniprot
proteins
pubmed
9020151
uniprot
proteins
pubmed
9219684
uniprot
proteins
pubmed
9632667
uniprot
proteins
sequence_length
189
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20171}; Lipid-anchor; Cytoplasmic side. Golgi apparatus. Golgi apparatus membrane; Lipid-anchor. Note=The active GTP-bound form is localized most strongly to membranes than the inactive GDP-bound form (By similarity). Shuttles between the plasma membrane and the Golgi apparatus. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Note=Colocalizes with RACK1 to the perinuclear region.
uniprot
proteins