HRAS

GTPase HRas also known as transforming protein p21 is an enzyme that in humans is encoded by the HRAS gene.

HARVEY RAT SARCOMA VIRUS ONCOGENE

Involved in the activation of Ras protein signal transduction (PubMed:22821884).

Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (PubMed:12740440, PubMed:14500341, PubMed:9020151).

Animal organ morphogenesis Source: ProtInc
Cell surface receptor signaling pathway Source: ProtInc
Cellular response to gamma radiation Source: CAFA
Cellular senescence Source: BHF-UCL
Chemotaxis Source: ProtInc
Defense response to protozoan Source: Ensembl
Endocytosis Source: Ensembl
Intrinsic apoptotic signaling pathway Source: Ensembl
MAPK cascade Source: Reactome
Negative regulation of cell population proliferation Source: BHF-UCL
Negative regulation of gene expression Source: BHF-UCL
Negative regulation of GTPase activity Source: BHF-UCL
Negative regulation of neuron apoptotic process Source: Ensembl
Positive regulation of actin cytoskeleton reorganization Source: BHF-UCL
Positive regulation of cell migration Source: BHF-UCL
Positive regulation of cell population proliferation Source: BHF-UCL
Positive regulation of epithelial cell proliferation Source: BHF-UCL
Positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
Positive regulation of GTPase activity Source: BHF-UCL
Positive regulation of interferon-gamma production Source: Ensembl
Positive regulation of JNK cascade Source: BHF-UCL
Positive regulation of MAPK cascade Source: BHF-UCL
Positive regulation of MAP kinase activity Source: BHF-UCL
Positive regulation of miRNA metabolic process Source: BHF-UCL
Positive regulation of phospholipase C activity Source: UniProtKB
Positive regulation of protein phosphorylation Source: BHF-UCL
Positive regulation of protein targeting to membrane Source: UniProtKB
Positive regulation of ruffle assembly Source: BHF-UCL
Positive regulation of transcription by RNA polymerase II Source: BHF-UCL
Positive regulation of wound healing Source: BHF-UCL
Ras protein signal transduction Source: BHF-UCL
Regulation of cell cycle Source: BHF-UCL
Regulation of cell population proliferation Source: ComplexPortal
Regulation of long-term neuronal synaptic plasticity Source: Ensembl
Regulation of MAP kinase activity Source: ComplexPortal
Regulation of neurotransmitter receptor localization to postsynaptic specialization membrane Source: SynGO
Regulation of transcription by RNA polymerase II Source: ComplexPortal
Signal transduction Source: ProtInc
T cell receptor signaling pathway Source: Ensembl
T-helper 1 type immune response Source: Ensembl

Cell membrane; Golgi apparatus; Golgi apparatus membrane. 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.
Isoform 2: Cytoplasm; Nucleus; Perinuclear region. Colocalizes with RACK1 to the perinuclear region.

Costello syndrome (CSTLO):
A rare condition characterized by prenatally increased growth, postnatal growth deficiency, mental retardation, distinctive facial appearance, cardiovascular abnormalities (typically pulmonic stenosis, hypertrophic cardiomyopathy and/or atrial tachycardia), tumor predisposition, skin and musculoskeletal abnormalities.
Congenital myopathy with excess of muscle spindles (CMEMS):
Variant of Costello syndrome.
Thyroid cancer, non-medullary, 2 (NMTC2):
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. 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.
Bladder cancer (BLC):
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.
Schimmelpenning-Feuerstein-Mims syndrome (SFM):
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.

Palmitoylated by the ZDHHC9-GOLGA7 complex. A continuous cycle of de- and re-palmitoylation regulates rapid exchange between plasma membrane and Golgi.
S-nitrosylated; critical for redox regulation. Important for stimulating guanine nucleotide exchange. No structural perturbation on nitrosylation.
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.
Acetylation at Lys-104 prevents interaction with guanine nucleotide exchange factors (GEFs).By similarity
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.(Microbial infection) Glucosylated at Thr-35 by P.sordellii toxin TcsL (PubMed:8626586, PubMed:8626575, PubMed:9632667, PubMed:19744486). Monoglucosylation completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form, leading to inhibit Ras signaling (PubMed:8626586, PubMed:8626575, PubMed:9632667).